,Unnamed: 0.2,Unnamed: 0.1,Unnamed: 0,entry,protein2,uniprot_description,rank,protein1,protein_name,function,GPT_description,all_description
0,0,0,39,O53666-F294A,MSHYRSNVRDQVFNLFEVLGVDKALGHGEFSDVDVDTARDMLAEVSRLAEGPVAESFVEGDRNPPVFDPKTHSVMLPESFKKSVNAMLEAGWDKVGIDEALGGMPMPKAVVWALHEHILGANPAVWMYAGGAGFAQILYHLGTEEQKKWAVLAAERGWGSTMVLTEPDAGSDVGAARTKAVQQADGSWHIDGVKRFITSGDSGDLFENIFHLVLARPEGAGPGTKGLSLYFVPKFLFDVETGEPGERNGVFVTNVEHKMGLKVSATCELAFGQHGVPAKGWLVGEVHNGIAQMAEVIEQARMMVGTKAIATLSTGYLNALQYAKSRVQGADLTQMTDKTAPRVTITHHPDVRRSLMTQKAYAEGLRALYLYTATFQDAAVAEVVHGVDAKLAVKVNDLMLPVVKGVGSEQAYAKLTESLQTLGGSGFLQDYPIEQYIRDAKIDSLYEGTTAIQAQDFFFRKIVRDKGVALAHVSGQIQEFVDSGAGNGRLKTERALLAKALTDVQGMAAALTGYLMAAQQDVTSLYKVGLGSVRFLMSVGDLIIGWLLQRQAAVAVAALDAGATGDERSFYEGKVAVASFFAKNFLPLLTSTREVIETLDNDIMELDEAAF,Increases affinity for eicosanoyl-CoA; when associated with A-447.,,MSHYRSNVRDQVFNLFEVLGVDKALGHGEFSDVDVDTARDMLAEVSRLAEGPVAESFVEGDRNPPVFDPKTHSVMLPESFKKSVNAMLEAGWDKVGIDEALGGMPMPKAVVWALHEHILGANPAVWMYAGGAGFAQILYHLGTEEQKKWAVLAAERGWGSTMVLTEPDAGSDVGAARTKAVQQADGSWHIDGVKRFITSGDSGDLFENIFHLVLARPEGAGPGTKGLSLYFVPKFLFDVETGEPGERNGVFVTNVEHKMGLKVSATCELAFGQHGVPAKGWLVGEVHNGIAQMFEVIEQARMMVGTKAIATLSTGYLNALQYAKSRVQGADLTQMTDKTAPRVTITHHPDVRRSLMTQKAYAEGLRALYLYTATFQDAAVAEVVHGVDAKLAVKVNDLMLPVVKGVGSEQAYAKLTESLQTLGGSGFLQDYPIEQYIRDAKIDSLYEGTTAIQAQDFFFRKIVRDKGVALAHVSGQIQEFVDSGAGNGRLKTERALLAKALTDVQGMAAALTGYLMAAQQDVTSLYKVGLGSVRFLMSVGDLIIGWLLQRQAAVAVAALDAGATGDERSFYEGKVAVASFFAKNFLPLLTSTREVIETLDNDIMELDEAAF,Broad-specificity linear acyl-CoA dehydrogenase FadE5,"Acyl-CoA dehydrogenase that exhibits broad specificity for linear acyl-CoA substrates, with a preference for long-chain substrates.",The mutation in FadE5 from Mycobacterium tuberculosis (MtbFadE5) has been reported to play a role in drug resistance.,Increases affinity for eicosanoyl-CoA; when associated with A-447. The mutation in FadE5 from Mycobacterium tuberculosis (MtbFadE5) has been reported to play a role in drug resistance.
1,1,1,178,Q14680-C286A,MKDYDELLKYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHLQTCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQMLQVDPKKRISMKNLLNHPWIMQDYNYPVEWQSKNPFIHLDDDAVTELSVHHRNNRQTMEDLISLWQYDHLTATYLLLLAKKARGKPVRLRLSSFSCGQASATPFTDIKSNNWSLEDVTASDKNYVAGLIDYDWCEDDLSTGAATPRTSQFTKYWTESNGVESKSLTPALCRTPANKLKNKENVYTPKSAVKNEEYFMFPEPKTPVNKNQHKREILTTPNRYTTPSKARNQCLKETPIKIPVNSTGTDKLMTGVISPERRCRSVELDLNQAHMEETPKRKGAKVFGSLERGLDKVITVLTRSKRKGSARDGPRRLKLHYNVTTTRLVNPDQLLNEIMSILPKKHVDFVQKGYTLKCQTQSDFGKVTMQFELEVCQLQKPDVVGIRRQRLKGDAWVYKRLVEDILSSCKV,Abolishes dependence to reducing agents; when associated with V-29; V-70; A-89; A-154; A-168; A-169; A-204; and A-339.,,MKDYDELLKYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHLQTCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQMLQVDPKKRISMKNLLNHPWIMQDYNYPVEWQSKNPFIHLDDDCVTELSVHHRNNRQTMEDLISLWQYDHLTATYLLLLAKKARGKPVRLRLSSFSCGQASATPFTDIKSNNWSLEDVTASDKNYVAGLIDYDWCEDDLSTGAATPRTSQFTKYWTESNGVESKSLTPALCRTPANKLKNKENVYTPKSAVKNEEYFMFPEPKTPVNKNQHKREILTTPNRYTTPSKARNQCLKETPIKIPVNSTGTDKLMTGVISPERRCRSVELDLNQAHMEETPKRKGAKVFGSLERGLDKVITVLTRSKRKGSARDGPRRLKLHYNVTTTRLVNPDQLLNEIMSILPKKHVDFVQKGYTLKCQTQSDFGKVTMQFELEVCQLQKPDVVGIRRQRLKGDAWVYKRLVEDILSSCKV,Maternal embryonic leucine zipper kinase,"Serine/threonine-protein kinase involved in various processes such as cell cycle regulation, self-renewal of stem cells, apoptosis and splicing regulation. Has a broad substrate specificity; phosphorylates BCL2L14, CDC25B, MAP3K5/ASK1 and ZNF622. Acts as an activator of apoptosis by phosphorylating and activating MAP3K5/ASK1. Acts as a regulator of cell cycle, notably by mediating phosphorylation of CDC25B, promoting localization of CDC25B to the centrosome and the spindle poles during mitosis. Plays a key role in cell proliferation and carcinogenesis. Required for proliferation of embryonic and postnatal multipotent neural progenitors. Phosphorylates and inhibits BCL2L14, possibly leading to affect mammary carcinogenesis by mediating inhibition of the pro-apoptotic function of BCL2L14. Also involved in the inhibition of spliceosome assembly during mitosis by phosphorylating ZNF622, thereby contributing to its redirection to the nucleus. May also play a role in primitive hematopoiesis.",,Abolishes dependence to reducing agents; when associated with V-29; V-70; A-89; A-154; A-168; A-169; A-204; and A-339.
2,2,2,199,P56633-K64A,MKLTCVVIVVVLFLTACQLITADDSRRTQKHRALRSTTKLSLSTRCRIPNQKCFQHLDDCCSRACNRFNKCV,1.2-fold decrease of toxicity.,,MKLTCVVIVVVLFLTACQLITADDSRRTQKHRALRSTTKLSLSTRCRIPNQKCFQHLDDCCSRKCNRFNKCV,Kappa-conotoxin PVIIA,"Kappa-conotoxins bind and inhibit voltage-gated potassium channels (Kv). This toxin inhibits the drosophila Shaker channel (IC(50)=57-80 nM). In vivo, when tested in fish, this toxin induces hyperactivity, followed by continuous contraction and extension of major fins, without immobilization or death. Injection of this peptide together with the delta-conotoxin PVIA causes the sudden tetanus of prey (STOP) syndrome, which is a single, lethal 'fin-pop' in envenomed fish. When tested in mice, induces hyperactivity.",The mutation in kappa-Conotoxin PVIIA has been shown to cause functional changes in the peptide.,1.2-fold decrease of toxicity. The mutation in kappa-Conotoxin PVIIA has been shown to cause functional changes in the peptide.
3,3,3,240,Q9Y3C6-Y78C,MAAIPPDSWQPPNVYLETSMGIIVLELYWKHAPKTCKNFAELARRGYYNGTKFHRIIKDFMIQGGDPTGTGRGGASICGKQFEDELHPDLKFTGAGILAMANAGPDTNGSQFFVTLAPTQWLDGKHTIFGRVCQGIGMVNRVGMVETNSQDRPVDDVKIIKAYPSG,In PCH14; unknown pathological significance; strongly reduced protein levels compared to wild-type after transfection in HEK293T cell line.,,MAAIPPDSWQPPNVYLETSMGIIVLELYWKHAPKTCKNFAELARRGYYNGTKFHRIIKDFMIQGGDPTGTGRGGASIYGKQFEDELHPDLKFTGAGILAMANAGPDTNGSQFFVTLAPTQWLDGKHTIFGRVCQGIGMVNRVGMVETNSQDRPVDDVKIIKAYPSG,Peptidyl-prolyl cis-trans isomerase-like 1,Involved in pre-mRNA splicing as component of the spliceosome. PPIases accelerate the folding of proteins. Catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Catalyzes prolyl peptide bond isomerization in CDC40/PRP17. Plays an important role in embryonic brain development; this function is independent of its isomerase activity.,,In PCH14; unknown pathological significance; strongly reduced protein levels compared to wild-type after transfection in HEK293T cell line.
4,4,4,270,Q9CXG9-N75S,METQALEPGTLEAFGATSPNKGGLSKTKKNFKDLMSKVTEGQFVLCRWTDGLYYLGKIKRVSSPKQSCLVTFEDSSKYWVLWKDIQHAGVPGEEPKCDVCMGKTSGPMNEILICGKCGLGYHQQCHIPIAVDANWPLLTHWFCRRCIFALAVRKGGALKKGAIAKTLQAVKMVLSYQPEELDWDSPHRTNQQQCYCYCGGPGEWYLRMLQCYRCRQWFHEACTQCLSEPMVFGDRFYLFFCSVCNQGPEYIERLPLRWVDIVHLALYNLGVQSKKRYFDFEEILAFVNHHWELLQLGKLTSTPMTERGPHLLNALNSYKSRFLCGKEIKKKKCIFRLRIRVPPAPPGKLLPDRALMPSDKGTSELLRKKGKSKPGLLPQEPQQQKRRVYRRKRSKFLLEDAIPSSDFTSAWSTDHHLASIFDFTLDEIQSLKSGSSGQTFFSDVDSTDAASTSGSASTSLSYDSRWTVGSRKRKLTAKVHRPLRAKQRAAELEGRCASDSNAEGAVGPEQPDEGIDSHTLESISGDDSSLSHLKSSITNYFGAAGRLACGEKYRVLARRVTPEGKVQYLLEWEGTTPY,Does not affect ability to promote H3K27me3 methylation; when associated with S-78.,,METQALEPGTLEAFGATSPNKGGLSKTKKNFKDLMSKVTEGQFVLCRWTDGLYYLGKIKRVSSPKQSCLVTFEDNSKYWVLWKDIQHAGVPGEEPKCDVCMGKTSGPMNEILICGKCGLGYHQQCHIPIAVDANWPLLTHWFCRRCIFALAVRKGGALKKGAIAKTLQAVKMVLSYQPEELDWDSPHRTNQQQCYCYCGGPGEWYLRMLQCYRCRQWFHEACTQCLSEPMVFGDRFYLFFCSVCNQGPEYIERLPLRWVDIVHLALYNLGVQSKKRYFDFEEILAFVNHHWELLQLGKLTSTPMTERGPHLLNALNSYKSRFLCGKEIKKKKCIFRLRIRVPPAPPGKLLPDRALMPSDKGTSELLRKKGKSKPGLLPQEPQQQKRRVYRRKRSKFLLEDAIPSSDFTSAWSTDHHLASIFDFTLDEIQSLKSGSSGQTFFSDVDSTDAASTSGSASTSLSYDSRWTVGSRKRKLTAKVHRPLRAKQRAAELEGRCASDSNAEGAVGPEQPDEGIDSHTLESISGDDSSLSHLKSSITNYFGAAGRLACGEKYRVLARRVTPEGKVQYLLEWEGTTPY,PHD finger protein 19,"Polycomb group (PcG) protein that specifically binds histone H3 trimethylated at 'Lys-36' (H3K36me3) and recruits the PRC2 complex, thus enhancing PRC2 H3K27me3 methylation activity. Probably involved in the transition from an active state to a repressed state in embryonic stem cells: acts by binding to H3K36me3, a mark for transcriptional activation, and recruiting H3K36me3 histone demethylases RIOX1 or KDM2B, leading to demethylation of H3K36 and recruitment of the PRC2 complex that mediates H3K27me3 methylation, followed by de novo silencing. Recruits the PRC2 complex to CpG islands and contributes to embryonic stem cell self-renewal. Also binds histone H3 dimethylated at 'Lys-36' (H3K36me2).",,Does not affect ability to promote H3K27me3 methylation; when associated with S-78.
5,5,5,446,O65282-G181A,MAATQLTASPVTMSARSLASLDGLRASSVKFSSLKPGTLRQSQFRRLVVKAASVVAPKYTSIKPLGDRVLVKIKEAEEKTLGGILLPSTAQSKPQGGEVVAVGEGRTIGKNKIDITVPTGAQIIYSKYAGTEVEFNDVKHLILKEDDIVGILETEDIKDLKPLNDRVFIKVAEAEEKTAGALLLTETTKEKPSIGTVIAVGPGSLDEEGKITPLPVSTGSTVLYSKYAGNDFKGKDGSNYIALRASDVMAILS,Reduces co-chaperone activity more than 3-fold.,,MAATQLTASPVTMSARSLASLDGLRASSVKFSSLKPGTLRQSQFRRLVVKAASVVAPKYTSIKPLGDRVLVKIKEAEEKTLGGILLPSTAQSKPQGGEVVAVGEGRTIGKNKIDITVPTGAQIIYSKYAGTEVEFNDVKHLILKEDDIVGILETEDIKDLKPLNDRVFIKVAEAEEKTAGGLLLTETTKEKPSIGTVIAVGPGSLDEEGKITPLPVSTGSTVLYSKYAGNDFKGKDGSNYIALRASDVMAILS,"20 kDa chaperonin, chloroplastic","Seems to function only as a co-chaperone, along with CPN60, and in certain cases is essential for the discharge of biologically active proteins from CPN60. Required to activate the iron superoxide dismutases (FeSOD).Involved in abscisic acid (ABA) signaling, independently of its co-chaperone role. Acts as negative regulator of the CHLH-WRKY40 coupled ABA signaling pathway, downstream of CHLH and upstream of WRKY40.",,Reduces co-chaperone activity more than 3-fold.
6,6,6,468,Q8NBJ5-G377R,MAAAPRAGRRRGQPLLALLLLLLAPLPPGAPPGADAYFPEERWSPESPLQAPRVLIALLARNAAHALPTTLGALERLRHPRERTALWVATDHNMDNTSTVLREWLVAVKSLYHSVEWRPAEEPRSYPDEEGPKHWSDSRYEHVMKLRQAALKSARDMWADYILFVDADNLILNPDTLSLLIAENKTVVAPMLDSRAAYSNFWCGMTSQGYYKRTPAYIPIRKRDRRGCFAVPMVHSTFLIDLRKAASRNLAFYPPHPDYTWSFDDIIVFAFSCKQAEVQMYVCNKEEYGFLPVPLRAHSTLQDEAESFMHVQLEVMVKHPPAEPSRFISAPTKTPDKMGFDEVFMINLRRRQDRRERMLRALQAQEIECRLVEAVDRKAMNTSQVEALGIQMLPGYRDPYHGRPLTKGELGCFLSHYNIWKEVVDRGLQKSLVFEDDLRFEIFFKRRLMNLMRDVEREGLDWDLIYVGRKRMQVEHPEKAVPRVRNLVEADYSYWTLAYVISLQGARKLLAAEPLSKMLPVDEFLPVMFDKHPVSEYKAHFSLRNLHAFSVEPLLIYPTHYTGDDGYVSDTETSVVWNNEHVKTDWDRAKSQKMREQQALSREAKNSDVLQSPLDSAARDEL,In BSVD3.,,MAAAPRAGRRRGQPLLALLLLLLAPLPPGAPPGADAYFPEERWSPESPLQAPRVLIALLARNAAHALPTTLGALERLRHPRERTALWVATDHNMDNTSTVLREWLVAVKSLYHSVEWRPAEEPRSYPDEEGPKHWSDSRYEHVMKLRQAALKSARDMWADYILFVDADNLILNPDTLSLLIAENKTVVAPMLDSRAAYSNFWCGMTSQGYYKRTPAYIPIRKRDRRGCFAVPMVHSTFLIDLRKAASRNLAFYPPHPDYTWSFDDIIVFAFSCKQAEVQMYVCNKEEYGFLPVPLRAHSTLQDEAESFMHVQLEVMVKHPPAEPSRFISAPTKTPDKMGFDEVFMINLRRRQDRRERMLRALQAQEIECRLVEAVDGKAMNTSQVEALGIQMLPGYRDPYHGRPLTKGELGCFLSHYNIWKEVVDRGLQKSLVFEDDLRFEIFFKRRLMNLMRDVEREGLDWDLIYVGRKRMQVEHPEKAVPRVRNLVEADYSYWTLAYVISLQGARKLLAAEPLSKMLPVDEFLPVMFDKHPVSEYKAHFSLRNLHAFSVEPLLIYPTHYTGDDGYVSDTETSVVWNNEHVKTDWDRAKSQKMREQQALSREAKNSDVLQSPLDSAARDEL,Procollagen galactosyltransferase 1,"Beta-galactosyltransferase that transfers beta-galactose to hydroxylysine residues of type I collagen. By acting on collagen glycosylation, facilitates the formation of collagen triple helix. Also involved in the biosynthesis of collagen type IV.","The mutation in COL4A1 impairs the secretion of collagen to the extracellular matrix, resulting in vessel fragility.","In BSVD3. The mutation in COL4A1 impairs the secretion of collagen to the extracellular matrix, resulting in vessel fragility."
7,7,7,624,P29590-K487A,MEPAPARSPRPQQDPARPQEPTMPPPETPSEGRQPSPSPSPTERAPASEEEFQFLRCQQCQAEAKCPKLLPCLHTLCSGCLEASGMQCPICQAPWPLGADTPALDNVFFESLQRRLSVYRQIVDAQAVCTRCKESADFWCFECEQLLCAKCFEAHQWFLKHEARPLAELRNQSVREFLDGTRKTNNIFCSNPNHRTPTLTSIYCRGCSKPLCCSCALLDSSHSELKCDISAEIQQRQEELDAMTQALQEQDSAFGAVHAQMHAAVGQLGRARAETEELIRERVRQVVAHVRAQERELLEAVDARYQRDYEEMASRLGRLDAVLQRIRTGSALVQRMKCYASDQEVLDMHGFLRQALCRLRQEEPQSLQAAVRTDGFDEFKVRLQDLSSCITQGKDAAVSKKASPEAASTPRDPIDVDLPEEAERVKAQVQALGLAEAQPMAVVQSVPGAHPVPVYAFSIKGPSYGEDVSNTTTAQKRKCSQTQCPRAVIKMESEEGKEARLARSSPEQPRPSTSKAVSPPHLDGPPSPRSPVIGSEVFLPNSNHVASGAGEAEERVVVISSSEDSDAENSSSRELDDSSSESSDLQLEGPSTLRVLDENLADPQAEDRPLVFFDLKIDNETQKISQLAAVNRESKFRVVIQPEAFFSIYSKAVSLEVGLQHFLSFLSSMRRPILACYKLWGPGLPNFFRALEDINRLWEFQEAISGFLAALPLIRERVPGASSFKLKNLAQTYLARNMSERSAMAAVLAMRDLCRLLEVSPGPQLAQHVYPFSSLQCFASLQPLVQAAVLPRAEARLLALHNVSFMELLSAHRRDRQGGLKKYSRYLSLQTTTLPPAQPAFNLQALGTYFEGLLEGPALARAEGVSTPLAGRGLAERASQQS,Loss of nuclear localization; when associated with A-490.,,MEPAPARSPRPQQDPARPQEPTMPPPETPSEGRQPSPSPSPTERAPASEEEFQFLRCQQCQAEAKCPKLLPCLHTLCSGCLEASGMQCPICQAPWPLGADTPALDNVFFESLQRRLSVYRQIVDAQAVCTRCKESADFWCFECEQLLCAKCFEAHQWFLKHEARPLAELRNQSVREFLDGTRKTNNIFCSNPNHRTPTLTSIYCRGCSKPLCCSCALLDSSHSELKCDISAEIQQRQEELDAMTQALQEQDSAFGAVHAQMHAAVGQLGRARAETEELIRERVRQVVAHVRAQERELLEAVDARYQRDYEEMASRLGRLDAVLQRIRTGSALVQRMKCYASDQEVLDMHGFLRQALCRLRQEEPQSLQAAVRTDGFDEFKVRLQDLSSCITQGKDAAVSKKASPEAASTPRDPIDVDLPEEAERVKAQVQALGLAEAQPMAVVQSVPGAHPVPVYAFSIKGPSYGEDVSNTTTAQKRKCSQTQCPRKVIKMESEEGKEARLARSSPEQPRPSTSKAVSPPHLDGPPSPRSPVIGSEVFLPNSNHVASGAGEAEERVVVISSSEDSDAENSSSRELDDSSSESSDLQLEGPSTLRVLDENLADPQAEDRPLVFFDLKIDNETQKISQLAAVNRESKFRVVIQPEAFFSIYSKAVSLEVGLQHFLSFLSSMRRPILACYKLWGPGLPNFFRALEDINRLWEFQEAISGFLAALPLIRERVPGASSFKLKNLAQTYLARNMSERSAMAAVLAMRDLCRLLEVSPGPQLAQHVYPFSSLQCFASLQPLVQAAVLPRAEARLLALHNVSFMELLSAHRRDRQGGLKKYSRYLSLQTTTLPPAQPAFNLQALGTYFEGLLEGPALARAEGVSTPLAGRGLAERASQQS,Protein PML,"Functions via its association with PML-nuclear bodies (PML-NBs) in a wide range of important cellular processes, including tumor suppression, transcriptional regulation, apoptosis, senescence, DNA damage response, and viral defense mechanisms. Acts as the scaffold of PML-NBs allowing other proteins to shuttle in and out, a process which is regulated by SUMO-mediated modifications and interactions. Isoform PML-4 has a multifaceted role in the regulation of apoptosis and growth suppression: activates RB1 and inhibits AKT1 via interactions with PP1 and PP2A phosphatases respectively, negatively affects the PI3K pathway by inhibiting MTOR and activating PTEN, and positively regulates p53/TP53 by acting at different levels (by promoting its acetylation and phosphorylation and by inhibiting its MDM2-dependent degradation). Isoform PML-4 also: acts as a transcriptional repressor of TBX2 during cellular senescence and the repression is dependent on a functional RBL2/E2F4 repressor complex, regulates double-strand break repair in gamma-irradiation-induced DNA damage responses via its interaction with WRN, acts as a negative regulator of telomerase by interacting with TERT, and regulates PER2 nuclear localization and circadian function. Isoform PML-6 inhibits specifically the activity of the tetrameric form of PKM. The nuclear isoforms (isoform PML-1, isoform PML-2, isoform PML-3, isoform PML-4 and isoform PML-5) in concert with SATB1 are involved in local chromatin-loop remodeling and gene expression regulation at the MHC-I locus. Isoform PML-2 is required for efficient IFN-gamma induced MHC II gene transcription via regulation of CIITA. Cytoplasmic PML is involved in the regulation of the TGF-beta signaling pathway. PML also regulates transcription activity of ELF4 and can act as an important mediator for TNF-alpha- and IFN-alpha-mediated inhibition of endothelial cell network formation and migration.Exhibits antiviral activity against both DNA and RNA viruses. The antiviral activity can involve one or several isoform(s) and can be enhanced by the permanent PML-NB-associated protein DAXX or by the recruitment of p53/TP53 within these structures. Isoform PML-4 restricts varicella zoster virus (VZV) via sequestration of virion capsids in PML-NBs thereby preventing their nuclear egress and inhibiting formation of infectious virus particles. The sumoylated isoform PML-4 restricts rabies virus by inhibiting viral mRNA and protein synthesis. The cytoplasmic isoform PML-14 can restrict herpes simplex virus-1 (HHV-1) replication by sequestering the viral E3 ubiquitin-protein ligase ICP0 in the cytoplasm. Isoform PML-6 shows restriction activity towards human cytomegalovirus (HHV-5) and influenza A virus strains PR8(H1N1) and ST364(H3N2). Sumoylated isoform PML-4 and isoform PML-12 show antiviral activity against encephalomyocarditis virus (EMCV) by promoting nuclear sequestration of viral polymerase (P3D-POL) within PML NBs. Isoform PML-3 exhibits antiviral activity against poliovirus by inducing apoptosis in infected cells through the recruitment and the activation of p53/TP53 in the PML-NBs. Isoform PML-3 represses human foamy virus (HFV) transcription by complexing the HFV transactivator, bel1/tas, preventing its binding to viral DNA. PML may positively regulate infectious hepatitis C viral (HCV) production and isoform PML-2 may enhance adenovirus transcription. Functions as an E3 SUMO-protein ligase that sumoylates (HHV-5) immediate early protein IE1, thereby participating in the antiviral response. Isoforms PML-3 and PML-6 display the highest levels of sumoylation activity.","Over-expression of PML-2KA mutant in the cytoplasm, which was generated by mutagenesis of the nuclear localization signals of PML, in MCF-7 breast cancer cells suppressed PKM2 activity and the accumulation of lactate. PKM2 exists in either an active tetrameric form which has high affinity for its substrate phosphoenolpyruvate (PEP) or a less active dimeric form which has low affinity for its substrate. Over-expression of PML-2KA suppressed the activity of the tetrameric form of PKM2, but not the dimeric form. PML with a mutation shows an inability to mediate apoptosis.","Loss of nuclear localization; when associated with A-490. Over-expression of PML-2KA mutant in the cytoplasm, which was generated by mutagenesis of the nuclear localization signals of PML, in MCF-7 breast cancer cells suppressed PKM2 activity and the accumulation of lactate. PKM2 exists in either an active tetrameric form which has high affinity for its substrate phosphoenolpyruvate (PEP) or a less active dimeric form which has low affinity for its substrate. Over-expression of PML-2KA suppressed the activity of the tetrameric form of PKM2, but not the dimeric form. PML with a mutation shows an inability to mediate apoptosis."
8,8,8,642,E3PJ86-V676A,MFWRDITLSVWRKKTTGLKTKKRLLPLVLAAALCSSPVWAEEATFTANFKDTDLKSFIETVGANLNKTIIMGPGVQGKVSIRTMTPLNERQYYQLFLNLLEAQGYAVVPMENDVLKVVKSSAAKVEPLPLVGEGSDNYAGDEMVTKVVPVRNVSVRELAPILRQMIDSAGSGNVVNYDPSNVIMLTGRASVVERLTEVIQRVDHAGNRTEEVIPLDNASASEIARVLESLTKNSGENQPATLKSQIVADERTNSVIVSGDPATRDKMRRLIRRLDSEMERSGNSQVFYLKYSKAEDLVDVLKQVSGTLTAAKEEAEGTVGSGREIVSIAASKHSNALIVTAPQDIMQSLQSVIEQLDIRRAQVHVEALIVEVAEGSNINFGVQWASKDAGLMQFANGTQIPIGTLGAAISQAKPQKGSTVISENGATTINPDTNGDLSTLAQLLSGFSGTAVGVVKGDWMALVQAVKNDSSSNVLSTPSITTLDNQEAFFMVGQDVPVLTGSTVGSNNSNPFNTVERKKVGIMLKVTPQINEGNAVQMVIEQEVSKVEGQTSLDVVFGERKLKTTVLANDGELIVLGGLMDDQAGESVAKVPLLGDIPLIGNLFKSTADKKEKRNLMVFIRPTILRDGMAADGVSQRKYNYMRAEQIYRDEQGLSLMPHTAQPVLPAQNQALPPEARAFLNAGRTR,Binds AspS2 normally.,,MFWRDITLSVWRKKTTGLKTKKRLLPLVLAAALCSSPVWAEEATFTANFKDTDLKSFIETVGANLNKTIIMGPGVQGKVSIRTMTPLNERQYYQLFLNLLEAQGYAVVPMENDVLKVVKSSAAKVEPLPLVGEGSDNYAGDEMVTKVVPVRNVSVRELAPILRQMIDSAGSGNVVNYDPSNVIMLTGRASVVERLTEVIQRVDHAGNRTEEVIPLDNASASEIARVLESLTKNSGENQPATLKSQIVADERTNSVIVSGDPATRDKMRRLIRRLDSEMERSGNSQVFYLKYSKAEDLVDVLKQVSGTLTAAKEEAEGTVGSGREIVSIAASKHSNALIVTAPQDIMQSLQSVIEQLDIRRAQVHVEALIVEVAEGSNINFGVQWASKDAGLMQFANGTQIPIGTLGAAISQAKPQKGSTVISENGATTINPDTNGDLSTLAQLLSGFSGTAVGVVKGDWMALVQAVKNDSSSNVLSTPSITTLDNQEAFFMVGQDVPVLTGSTVGSNNSNPFNTVERKKVGIMLKVTPQINEGNAVQMVIEQEVSKVEGQTSLDVVFGERKLKTTVLANDGELIVLGGLMDDQAGESVAKVPLLGDIPLIGNLFKSTADKKEKRNLMVFIRPTILRDGMAADGVSQRKYNYMRAEQIYRDEQGLSLMPHTAQPVLPAQNQALPPEVRAFLNAGRTR,Secretin GspD 2,"Part of a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of folded proteins across the outer membrane (Probable). This subunit forms the outer membrane channel (Probable).",,Binds AspS2 normally.
9,9,9,750,P35658-P387S,MGDEMDAMIPEREMKDFQFRALKKVRIFDSPEELPKERSSLLAVSNKYGLVFAGGASGLQIFPTKNLLIQNKPGDDPNKIVDKVQGLLVPMKFPIHHLALSCDNLTLSACMMSSEYGSIIAFFDVRTFSNEAKQQKRPFAYHKLLKDAGGMVIDMKWNPTVPSMVAVCLADGSIAVLQVTETVKVCATLPSTVAVTSVCWSPKGKQLAVGKQNGTVVQYLPTLQEKKVIPCPPFYESDHPVRVLDVLWIGTYVFAIVYAAADGTLETSPDVVMALLPKKEEKHPEIFVNFMEPCYGSCTERQHHYYLSYIEEWDLVLAASAASTEVSILARQSDQINWESWLLEDSSRAELPVTDKSDDSLPMGVVVDYTNQVEITISDEKTLPPASVLMLLSTDGVLCPFYMINQNPGVKSLIKTPERLSLEGERQPKSPGSTPTTPTSSQAPQKLDASAAAAPASLPPSSPAAPIATFSLLPAGGAPTVFSFGSSSLKSSATVTGEPPSYSSGSDSSKAAPGPGPSTFSFVPPSKASLAPTPAASPVAPSAASFSFGSSGFKPTLESTPVPSVSAPNIAMKPSFPPSTSAVKVNLSEKFTAAATSTPVSSSQSAPPMSPFSSASKPAASGPLSHPTPLSAPPSSVPLKSSVLPSPSGRSAQGSSSPVPSMVQKSPRITPPAAKPGSPQAKSLQPAVAEKQGHQWKDSDPVMAGIGEEIAHFQKELEELKARTSKACFQVGTSEEMKMLRTESDDLHTFLLEIKETTESLHGDISSLKTTLLEGFAGVEEAREQNERNRDSGYLHLLYKRPLDPKSEAQLQEIRRLHQYVKFAVQDVNDVLDLEWDQHLEQKKKQRHLLVPERETLFNTLANNREIINQQRKRLNHLVDSLQQLRLYKQTSLWSLSSAVPSQSSIHSFDSDLESLCNALLKTTIESHTKSLPKVPAKLSPMKQAQLRNFLAKRKTPPVRSTAPASLSRSAFLSQRYYEDLDEVSSTSSVSQSLESEDARTSCKDDEAVVQAPRHAPVVRTPSI,In IIAE9.,,MGDEMDAMIPEREMKDFQFRALKKVRIFDSPEELPKERSSLLAVSNKYGLVFAGGASGLQIFPTKNLLIQNKPGDDPNKIVDKVQGLLVPMKFPIHHLALSCDNLTLSACMMSSEYGSIIAFFDVRTFSNEAKQQKRPFAYHKLLKDAGGMVIDMKWNPTVPSMVAVCLADGSIAVLQVTETVKVCATLPSTVAVTSVCWSPKGKQLAVGKQNGTVVQYLPTLQEKKVIPCPPFYESDHPVRVLDVLWIGTYVFAIVYAAADGTLETSPDVVMALLPKKEEKHPEIFVNFMEPCYGSCTERQHHYYLSYIEEWDLVLAASAASTEVSILARQSDQINWESWLLEDSSRAELPVTDKSDDSLPMGVVVDYTNQVEITISDEKTLPPAPVLMLLSTDGVLCPFYMINQNPGVKSLIKTPERLSLEGERQPKSPGSTPTTPTSSQAPQKLDASAAAAPASLPPSSPAAPIATFSLLPAGGAPTVFSFGSSSLKSSATVTGEPPSYSSGSDSSKAAPGPGPSTFSFVPPSKASLAPTPAASPVAPSAASFSFGSSGFKPTLESTPVPSVSAPNIAMKPSFPPSTSAVKVNLSEKFTAAATSTPVSSSQSAPPMSPFSSASKPAASGPLSHPTPLSAPPSSVPLKSSVLPSPSGRSAQGSSSPVPSMVQKSPRITPPAAKPGSPQAKSLQPAVAEKQGHQWKDSDPVMAGIGEEIAHFQKELEELKARTSKACFQVGTSEEMKMLRTESDDLHTFLLEIKETTESLHGDISSLKTTLLEGFAGVEEAREQNERNRDSGYLHLLYKRPLDPKSEAQLQEIRRLHQYVKFAVQDVNDVLDLEWDQHLEQKKKQRHLLVPERETLFNTLANNREIINQQRKRLNHLVDSLQQLRLYKQTSLWSLSSAVPSQSSIHSFDSDLESLCNALLKTTIESHTKSLPKVPAKLSPMKQAQLRNFLAKRKTPPVRSTAPASLSRSAFLSQRYYEDLDEVSSTSSVSQSLESEDARTSCKDDEAVVQAPRHAPVVRTPSI,Nuclear pore complex protein Nup214,Part of the nuclear pore complex. Has a critical role in nucleocytoplasmic transport. May serve as a docking site in the receptor-mediated import of substrates across the nuclear pore complex.(Microbial infection) Required for capsid disassembly of the human adenovirus 5 (HadV-5) leading to release of the viral genome to the nucleus (in vitro).,Biallelic missense variant in the NUP214 gene causing acute febrile encephalopathy. Reduced NUP214 protein levels in primary skin fibroblasts derived from affected individuals. Defects in the classical protein import and mRNA export pathways in affected cells. Delay in stress response and surge in apoptotic cell death in fibroblasts from affected individuals.,In IIAE9. Biallelic missense variant in the NUP214 gene causing acute febrile encephalopathy. Reduced NUP214 protein levels in primary skin fibroblasts derived from affected individuals. Defects in the classical protein import and mRNA export pathways in affected cells. Delay in stress response and surge in apoptotic cell death in fibroblasts from affected individuals.
10,10,10,754,P17302-Y17S,MGDWSALGKLLDKVQASSTAGGKVWLSVLFIFRILLLGTAVESAWGDEQSAFRCNTQQPGCENVCYDKSFPISHVRFWVLQIIFVSVPTLLYLAHVFYVMRKEEKLNKKEEELKVAQTDGVNVDMHLKQIEIKKFKYGIEEHGKVKMRGGLLRTYIISILFKSIFEVAFLLIQWYIYGFSLSAVYTCKRDPCPHQVDCFLSRPTEKTIFIIFMLVVSLVSLALNIIELFYVFFKGVKDRVKGKSDPYHATSGALSPAKDCGSQKYAYFNGCSSPTAPLSPMSPPGYKLVTGDRNNSSCRNYNKQASEQNWANYSAEQNRMGQAGSTISNSHAQPFDFPDDNQNSKKLAAGHELQPLAIVDQRPSSRASSRASSRPRPDDLEI,In ODDD.,,MGDWSALGKLLDKVQAYSTAGGKVWLSVLFIFRILLLGTAVESAWGDEQSAFRCNTQQPGCENVCYDKSFPISHVRFWVLQIIFVSVPTLLYLAHVFYVMRKEEKLNKKEEELKVAQTDGVNVDMHLKQIEIKKFKYGIEEHGKVKMRGGLLRTYIISILFKSIFEVAFLLIQWYIYGFSLSAVYTCKRDPCPHQVDCFLSRPTEKTIFIIFMLVVSLVSLALNIIELFYVFFKGVKDRVKGKSDPYHATSGALSPAKDCGSQKYAYFNGCSSPTAPLSPMSPPGYKLVTGDRNNSSCRNYNKQASEQNWANYSAEQNRMGQAGSTISNSHAQPFDFPDDNQNSKKLAAGHELQPLAIVDQRPSSRASSRASSRPRPDDLEI,Gap junction alpha-1 protein,"Gap junction protein that acts as a regulator of bladder capacity. A gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. May play a critical role in the physiology of hearing by participating in the recycling of potassium to the cochlear endolymph. Negative regulator of bladder functional capacity: acts by enhancing intercellular electrical and chemical transmission, thus sensitizing bladder muscles to cholinergic neural stimuli and causing them to contract. May play a role in cell growth inhibition through the regulation of NOV expression and localization. Plays an essential role in gap junction communication in the ventricles.",These mutations may cause misassembly of channels or alter channel conduction properties.,In ODDD. These mutations may cause misassembly of channels or alter channel conduction properties.
11,11,11,760,Q494U1-G2A,MANSHCVPQAPRRLRASFSRKPSLKGNREDSARMSAGLPGPEAARSGDAAANKLFHYIPGTDILDLENQRENLEQPFLSVFKKGRRRVPVRNLGKVVHYAKVQLRFQHSQDVSDCYLELFPAHLYFQAHGSEGLTFQGLLPLTELSVCPLEGSREHAFQITGPLPAPLLVLCPSRAELDRWLYHLEKQTALLGGPRRCHSAPPQRRLTRLRTASGHEPGGSAVCASRVKLQHLPAQEQWDRLLVLYPTSLAIFSEELDGLCFKGELPLRAVHINLEEKEKQIRSFLIEGPLINTIRVVCASYEDYGHWLLCLRAVTHREGAPPLPGAESFPGSQVMGSGRGSLSSGGQTSWDSGCLAPPSTRTSHSLPESSVPSTVGCSSQHTPDQANSDRASIGRRRTELRRSGSSRSPGSKARAEGRGPVTPLHLDLTQLHRLSLESSPDAPDHTSETSHSPLYADPYTPPATSHRRVTDVRGLEEFLSAMQSARGPTPSSPLPSVPVSVPASDPRSCSSGPAGPYLLSKKGALQSRAAQRHRGSAKDGGPQPPDAPQLVSSAREGSPEPWLPLTDGRSPRRSRDPGYDHLWDETLSSSHQKCPQLGGPEASGGLVQWI,"Loss of myristoylation, reduced protein stability, morphological alterations in mitochondria but no effect on its mitochondrial localization. Loss of cell membrane localization leading to localization to intracellular organelles.",,MGNSHCVPQAPRRLRASFSRKPSLKGNREDSARMSAGLPGPEAARSGDAAANKLFHYIPGTDILDLENQRENLEQPFLSVFKKGRRRVPVRNLGKVVHYAKVQLRFQHSQDVSDCYLELFPAHLYFQAHGSEGLTFQGLLPLTELSVCPLEGSREHAFQITGPLPAPLLVLCPSRAELDRWLYHLEKQTALLGGPRRCHSAPPQRRLTRLRTASGHEPGGSAVCASRVKLQHLPAQEQWDRLLVLYPTSLAIFSEELDGLCFKGELPLRAVHINLEEKEKQIRSFLIEGPLINTIRVVCASYEDYGHWLLCLRAVTHREGAPPLPGAESFPGSQVMGSGRGSLSSGGQTSWDSGCLAPPSTRTSHSLPESSVPSTVGCSSQHTPDQANSDRASIGRRRTELRRSGSSRSPGSKARAEGRGPVTPLHLDLTQLHRLSLESSPDAPDHTSETSHSPLYADPYTPPATSHRRVTDVRGLEEFLSAMQSARGPTPSSPLPSVPVSVPASDPRSCSSGPAGPYLLSKKGALQSRAAQRHRGSAKDGGPQPPDAPQLVSSAREGSPEPWLPLTDGRSPRRSRDPGYDHLWDETLSSSHQKCPQLGGPEASGGLVQWI,Pleckstrin homology domain-containing family N member 1,"Controls the stability of the leptin mRNA harboring an AU-rich element (ARE) in its 3' UTR, in cooperation with the RNA stabilizer ELAVL1. Decreases the stability of the leptin mRNA by antagonizing the function of ELAVL1 by inducing its atypical recruitment from the nucleus to the cytosol. Binds to cardiolipin (CL), phosphatidic acid (PA), phosphatidylinositol 4-phosphate (PtdIns(4)P) and phosphatidylserine (PS). Promotes apoptosis by enhancing BAX-BAK hetero-oligomerization via interaction with BID in colon cancer cells.",The expression of the G/A mutant of CLPABP induced morphological alterations in mitochondria. N-myristoylation of CLPABP was predicted to affect its stability onto the mitochondrial membrane rather than its subcellular localization.,"Loss of myristoylation, reduced protein stability, morphological alterations in mitochondria but no effect on its mitochondrial localization. Loss of cell membrane localization leading to localization to intracellular organelles. The expression of the G/A mutant of CLPABP induced morphological alterations in mitochondria. N-myristoylation of CLPABP was predicted to affect its stability onto the mitochondrial membrane rather than its subcellular localization."
12,12,12,767,P00966-G117D,MSSKGSVVLAYSGGLDTSCILVWLKEQGYDVIAYLANIGQKEDFEEARKKALKLGAKKVFIEDVSREFVEEFIWPAIQSSALYEDRYLLGTSLARPCIARKQVEIAQREGAKYVSHDATGKGNDQVRFELSCYSLAPQIKVIAPWRMPEFYNRFKGRNDLMEYAKQHGIPIPVTPKNPWSMDENLMHISYEAGILENPKNQAPPGLYTKTQDPAKAPNTPDILEIEFKKGVPVKVTNVKDGTTHQTSLELFMYLNEVAGKHGVGRIDIVENRFIGMKSRGIYETPAGTILYHAHLDIEAFTMDREVRKIKQGLGLKFAELVYTGFWHSPECEFVRHCIAKSQERVEGKVQVSVLKGQVYILGRESPLSLYNEELVSMNVQGDYEPTDATGFININSLRLKEYHRLQSKVTAK,In CTLN1.,,MSSKGSVVLAYSGGLDTSCILVWLKEQGYDVIAYLANIGQKEDFEEARKKALKLGAKKVFIEDVSREFVEEFIWPAIQSSALYEDRYLLGTSLARPCIARKQVEIAQREGAKYVSHGATGKGNDQVRFELSCYSLAPQIKVIAPWRMPEFYNRFKGRNDLMEYAKQHGIPIPVTPKNPWSMDENLMHISYEAGILENPKNQAPPGLYTKTQDPAKAPNTPDILEIEFKKGVPVKVTNVKDGTTHQTSLELFMYLNEVAGKHGVGRIDIVENRFIGMKSRGIYETPAGTILYHAHLDIEAFTMDREVRKIKQGLGLKFAELVYTGFWHSPECEFVRHCIAKSQERVEGKVQVSVLKGQVYILGRESPLSLYNEELVSMNVQGDYEPTDATGFININSLRLKEYHRLQSKVTAK,Argininosuccinate synthase,"One of the enzymes of the urea cycle, the metabolic pathway transforming neurotoxic amonia produced by protein catabolism into inocuous urea in the liver of ureotelic animals. Catalyzes the formation of arginosuccinate from aspartate, citrulline and ATP and together with ASL it is responsible for the biosynthesis of arginine in most body tissues.",The subacute form is compound heterozygous for / (new mutation).,In CTLN1. The subacute form is compound heterozygous for / (new mutation).
13,13,13,785,Q564A5-Q28E,MGKELLTFSDLTWLDSSPDTVRSAFTREYGTTPDGIALNSEGYFGYHSPPITEQYGRPCYKQTGETKITLQDLAPPTDAILGNSIARNRGDSPITLTVSVEGKWSDSTSWSTSTETGVKMSSEFGVEGAFKMGGEFSLTVSVGKSGSSSVEKTSTSSVQVTVPPRSKVVVSMVGIMKKEKVFFEVPVTVDGSFGANFPSTVQGHYFWFMDARSCLNKTSGVIKGTIDHANVFDVSVEVGPSEPL,No effect; when associated with L-140.,,MGKELLTFSDLTWLDSSPDTVRSAFTRQYGTTPDGIALNSEGYFGYHSPPITEQYGRPCYKQTGETKITLQDLAPPTDAILGNSIARNRGDSPITLTVSVEGKWSDSTSWSTSTETGVKMSSEFGVEGAFKMGGEFSLTVSVGKSGSSSVEKTSTSSVQVTVPPRSKVVVSMVGIMKKEKVFFEVPVTVDGSFGANFPSTVQGHYFWFMDARSCLNKTSGVIKGTIDHANVFDVSVEVGPSEPL,Hydralysin-2,"Induces an immediate fast muscle contraction followed by flaccid paralysis when injected into blowfly larvae. Has strong cytolytic activity against insect Sf9 cells and human HeLa cells, weak activity against human JAR cells, and no activity against human HEK293 cells. Binds to erythrocyte membranes and has hemolytic activity, probably mediated by oligomerization and pore formation.",,No effect; when associated with L-140.
14,14,14,851,Q16568-S66T,MESSRVRLLPLLGAALLLMLPLLGTRAQEDAELQPRALDIYSAVDDASHEKELIEALQEVLKKLKTKRVPIYEKKYGQVPMCDAGEQCAVRKGARIGKLCDCPRGTSCNSFLLKCL,,,MESSRVRLLPLLGAALLLMLPLLGTRAQEDAELQPRALDIYSAVDDASHEKELIEALQEVLKKLKSKRVPIYEKKYGQVPMCDAGEQCAVRKGARIGKLCDCPRGTSCNSFLLKCL,Cocaine- and amphetamine-regulated transcript protein [Cleaved into: CART,Satiety factor closely associated with the actions of leptin and neuropeptide Y; this anorectic peptide inhibits both normal and starvation-induced feeding and completely blocks the feeding response induced by neuropeptide Y and regulated by leptin in the hypothalamus. It promotes neuronal development and survival in vitro.,"A novel amino acid change, , was found in 2 probands and in 0 of 100 control subjects but did not cosegregate with obesity in family studies.","A novel amino acid change, , was found in 2 probands and in 0 of 100 control subjects but did not cosegregate with obesity in family studies."
15,15,15,855,Q8BHY3-D784A,MRVPEKYSTLPAEDRSVHIVNICAIEDLGYLPSEGTLLNSLSVDPDAECKYGLYFRDGKRKVDYILVYHHKRASGSRTLARRGLQNDMVLGTRSVRQDQPLPGKGSPVDAGSPEVPMDYHEDDKRFRREEYEGNLLEAGLELENDEDTKIHGVGFVKIHAPWHVLCREAEFLKLKMPTKKVYHISETRGLLKTINSVLQKITDPIQPKVAEHRPQTTKRLSYPFSREKQHLFDLTDRDSFFDSKTRSTIVYEILKRTTCTKAKYSMGITSLLANGVYSAAYPLHDGDYEGDNVEFNDRKLLYEEWASYGVFYKYQPIDLVRKYFGEKVGLYFAWLGAYTQMLIPASIVGVIVFLYGCATVDENIPSMEMCDQRYNITMCPLCDKTCSYWKMSSACATARASHLFDNPATVFFSVFMALWAATFMEHWKRKQMRLNYRWDLTGFEEEEEAVKDHPRAEYEARVLEKSLRKESRNKETDKVKLTWRDRFPAYFTNLVSIIFMIAVTFAIVLGVIIYRISTAAALAMNSSPSVRSNIRVTVTATAVIINLVVIILLDEVYGCIARWLTKIEVPKTEKSFEERLTFKAFLLKFVNSYTPIFYVAFFKGRFVGRPGDYVYIFRSFRMEECAPGGCLMELCIQLSIIMLGKQLIQNNLFEIGIPKMKKFIRYLKLRRQSPSDREEYVKRKQRYEVDFNLEPFAGLTPEYMEMIIQFGFVTLFVASFPLAPLFALLNNIIEIRLDAKKFVTELRRPVAIRAKDIGIWYNILRGVGKLAVIINAFVISFTSAFIPRLVYLYMYSQNGTMHGFVNHTLSSFNVSDFQNGTAPNDPLDLGYEVQICRYKDYREPPWSEHKYDISKDFWAVLAARLAFVIVFQNLVMFMSDFVDWVIPDIPKDISQQIHKEKVLMVELFMREEQGKQQLLDTWMEKEKPRDVPCNNHSPTTHPEAGDGSPVPSYEYHGDAL,Increased permeability to chloride ions.,,MRVPEKYSTLPAEDRSVHIVNICAIEDLGYLPSEGTLLNSLSVDPDAECKYGLYFRDGKRKVDYILVYHHKRASGSRTLARRGLQNDMVLGTRSVRQDQPLPGKGSPVDAGSPEVPMDYHEDDKRFRREEYEGNLLEAGLELENDEDTKIHGVGFVKIHAPWHVLCREAEFLKLKMPTKKVYHISETRGLLKTINSVLQKITDPIQPKVAEHRPQTTKRLSYPFSREKQHLFDLTDRDSFFDSKTRSTIVYEILKRTTCTKAKYSMGITSLLANGVYSAAYPLHDGDYEGDNVEFNDRKLLYEEWASYGVFYKYQPIDLVRKYFGEKVGLYFAWLGAYTQMLIPASIVGVIVFLYGCATVDENIPSMEMCDQRYNITMCPLCDKTCSYWKMSSACATARASHLFDNPATVFFSVFMALWAATFMEHWKRKQMRLNYRWDLTGFEEEEEAVKDHPRAEYEARVLEKSLRKESRNKETDKVKLTWRDRFPAYFTNLVSIIFMIAVTFAIVLGVIIYRISTAAALAMNSSPSVRSNIRVTVTATAVIINLVVIILLDEVYGCIARWLTKIEVPKTEKSFEERLTFKAFLLKFVNSYTPIFYVAFFKGRFVGRPGDYVYIFRSFRMEECAPGGCLMELCIQLSIIMLGKQLIQNNLFEIGIPKMKKFIRYLKLRRQSPSDREEYVKRKQRYEVDFNLEPFAGLTPEYMEMIIQFGFVTLFVASFPLAPLFALLNNIIEIRLDAKKFVTELRRPVAIRAKDIGIWYNILRGVGKLAVIINAFVISFTSDFIPRLVYLYMYSQNGTMHGFVNHTLSSFNVSDFQNGTAPNDPLDLGYEVQICRYKDYREPPWSEHKYDISKDFWAVLAARLAFVIVFQNLVMFMSDFVDWVIPDIPKDISQQIHKEKVLMVELFMREEQGKQQLLDTWMEKEKPRDVPCNNHSPTTHPEAGDGSPVPSYEYHGDAL,Anoctamin-1,"Calcium-activated chloride channel (CaCC). Plays a role in transepithelial anion transport and smooth muscle contraction. Required for the normal functioning of the interstitial cells of Cajal (ICCs) which generate electrical pacemaker activity in gastrointestinal smooth muscles. Acts as a major contributor to basal and stimulated chloride conductance in airway epithelial cells and plays an important role in tracheal cartilage development. Required for CFTR activation by enhancing endoplasmic reticulum Ca(2+) store release and is also required for CFTR membrane expression. Required for basal and ATP-dependent mucus secretion in airways and intestine, probably by controlling exocytosis of mucus-filled granules by providing Ca(2+) to an apical signaling compartment. Contributes to airway mucus expression induced by interleukins IL3 and IL8 and by the asthma-associated protein CLCA1 and is required for expression of mucin MUC5AC. However, was shown in another study not to be required for MUC5AC expression. Plays a role in the propagation of Ca(2+) waves in Kolliker's organ in the cochlea and contributes to the refinement of auditory brainstem circuitries prior to hearing onset. In vomeronasal sensory neurons, modulates spontaneous firing patterns in the absence of stimuli as well as the firing pattern of pheromone-evoked activity. Responsible for calcium-activated chloride channel activity in type I taste cells of the vallate papillae. Acts as a heat sensor in nociceptive neurons. In dorsal root ganglion neurons, plays a role in mediating non-histaminergic Mas-related G-protein coupled receptor (MRGPR)-dependent itching, acting as a downstream effector of MRGPRs. In the developing brain, required for the Ca(2+)-dependent process extension of radial glial cells.",,Increased permeability to chloride ions.
16,16,16,1003,Q96H96-M78V,MLGSRAAGFARGLRAVALAWLPGWRGRSFALARAAGAPHGGDLQPPACPEPRGRQLSLSAAAVVDSAPRPLQPYLRLVRLDKPIGTWLLYLPCTWSIGLAAEPGCFPDWYMLSLFGTGAILMRGAGCTINDMWDQDYDKKVTRTANRPIAAGDISTFQSFVFLGGQLTLALGVLLCLNYYSIALGAGSLLLVITYPLMKRISYWPQLALGLTFNWGALLGWSAIKGSCDPSVCLPLYFSGVMWTLIYDTIYAHQDKRDDVLIGLKSTALRFGENTKPWLSGFSVAMLGALSLVGVNSGQTAPYYAALGAVGAHLTHQIYTLDIHRPEDCWNKFISNRTLGLIVFLGIVLGNLWKEKKTDKTKKGIENKIEN,In MSA1; associated with disease susceptibility; decreased ubiquinone biosynthesis.,,MLGSRAAGFARGLRAVALAWLPGWRGRSFALARAAGAPHGGDLQPPACPEPRGRQLSLSAAAVVDSAPRPLQPYLRLMRLDKPIGTWLLYLPCTWSIGLAAEPGCFPDWYMLSLFGTGAILMRGAGCTINDMWDQDYDKKVTRTANRPIAAGDISTFQSFVFLGGQLTLALGVLLCLNYYSIALGAGSLLLVITYPLMKRISYWPQLALGLTFNWGALLGWSAIKGSCDPSVCLPLYFSGVMWTLIYDTIYAHQDKRDDVLIGLKSTALRFGENTKPWLSGFSVAMLGALSLVGVNSGQTAPYYAALGAVGAHLTHQIYTLDIHRPEDCWNKFISNRTLGLIVFLGIVLGNLWKEKKTDKTKKGIENKIEN,"4-hydroxybenzoate polyprenyltransferase, mitochondrial","Mediates the second step in the final reaction sequence of coenzyme Q (CoQ) biosynthesis. Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl donor (such as all-trans-decaprenyl diphosphate). The length of the polyprenyl side chain varies depending on the species, in humans, the side chain is comprised of 10 isoprenyls (decaprenyl) producing CoQ10 (also known as ubiquinone), whereas rodents predominantly generate CoQ9. However, this specificity is not complete, human tissues have low amounts of CoQ9 and rodent organs contain some CoQ10. Plays a central role in the biosynthesis of CoQ10. CoQ10 is a vital molecule that transports electrons from mitochondrial respiratory chain complexes. CoQs also function as cofactors for uncoupling protein and play a role as regulators of the extracellularly-induced ceramide-dependent apoptotic pathway. Regulates mitochondrial permeability transition pore (mPTP) opening and ROS production (pivotal events in cell death) in a tissue specific manner.",,In MSA1; associated with disease susceptibility; decreased ubiquinone biosynthesis.
17,17,17,1013,Q9NZ08-R725Q,MVFLPLKWSLATMSFLLSSLLALLTVSTPSWCQSTEASPKRSDGTPFPWNKIRLPEYVIPVHYDLLIHANLTTLTFWGTTKVEITASQPTSTIILHSHHLQISRATLRKGAGERLSEEPLQVLEHPRQEQIALLAPEPLLVGLPYTVVIHYAGNLSETFHGFYKSTYRTKEGELRILASTQFEPTAARMAFPCFDEPAFKASFSIKIRREPRHLAISNMPLVKSVTVAEGLIEDHFDVTVKMSTYLVAFIISDFESVSKITKSGVKVSVYAVPDKINQADYALDAAVTLLEFYEDYFSIPYPLPKQDLAAIPDFQSGAMENWGLTTYRESALLFDAEKSSASSKLGITMTVAHELAHQWFGNLVTMEWWNDLWLNEGFAKFMEFVSVSVTHPELKVGDYFFGKCFDAMEVDALNSSHPVSTPVENPAQIREMFDDVSYDKGACILNMLREYLSADAFKSGIVQYLQKHSYKNTKNEDLWDSMASICPTDGVKGMDGFCSRSQHSSSSSHWHQEGVDVKTMMNTWTLQKGFPLITITVRGRNVHMKQEHYMKGSDGAPDTGYLWHVPLTFITSKSDMVHRFLLKTKTDVLILPEEVEWIKFNVGMNGYYIVHYEDDGWDSLTGLLKGTHTAVSSNDRASLINNAFQLVSIGKLSIEKALDLSLYLKHETEIMPVFQGLNELIPMYKLMEKRDMNEVETQFKAFLIRLLRDLIDKQTWTDEGSVSEQMLRSQLLLLACVHNYQPCVQRAEGYFRKWKESNGNLSLPVDVTLAVFAVGAQSTEGWDFLYSKYQFSLSSTEKSQIEFALCRTQNKEKLQWLLDESFKGDKIKTQEFPQILTLIGRNPVGYPLAWQFLRKNWNKLVQKFELGSSSIAHMVMGTTNQFSTRTRLEEVKGFFSSLKENGSQLRCVQQTIETIEENIGWMDKNFDKIRVWLQSEKLERM,,,MVFLPLKWSLATMSFLLSSLLALLTVSTPSWCQSTEASPKRSDGTPFPWNKIRLPEYVIPVHYDLLIHANLTTLTFWGTTKVEITASQPTSTIILHSHHLQISRATLRKGAGERLSEEPLQVLEHPRQEQIALLAPEPLLVGLPYTVVIHYAGNLSETFHGFYKSTYRTKEGELRILASTQFEPTAARMAFPCFDEPAFKASFSIKIRREPRHLAISNMPLVKSVTVAEGLIEDHFDVTVKMSTYLVAFIISDFESVSKITKSGVKVSVYAVPDKINQADYALDAAVTLLEFYEDYFSIPYPLPKQDLAAIPDFQSGAMENWGLTTYRESALLFDAEKSSASSKLGITMTVAHELAHQWFGNLVTMEWWNDLWLNEGFAKFMEFVSVSVTHPELKVGDYFFGKCFDAMEVDALNSSHPVSTPVENPAQIREMFDDVSYDKGACILNMLREYLSADAFKSGIVQYLQKHSYKNTKNEDLWDSMASICPTDGVKGMDGFCSRSQHSSSSSHWHQEGVDVKTMMNTWTLQKGFPLITITVRGRNVHMKQEHYMKGSDGAPDTGYLWHVPLTFITSKSDMVHRFLLKTKTDVLILPEEVEWIKFNVGMNGYYIVHYEDDGWDSLTGLLKGTHTAVSSNDRASLINNAFQLVSIGKLSIEKALDLSLYLKHETEIMPVFQGLNELIPMYKLMEKRDMNEVETQFKAFLIRLLRDLIDKQTWTDEGSVSERMLRSQLLLLACVHNYQPCVQRAEGYFRKWKESNGNLSLPVDVTLAVFAVGAQSTEGWDFLYSKYQFSLSSTEKSQIEFALCRTQNKEKLQWLLDESFKGDKIKTQEFPQILTLIGRNPVGYPLAWQFLRKNWNKLVQKFELGSSSIAHMVMGTTNQFSTRTRLEEVKGFFSSLKENGSQLRCVQQTIETIEENIGWMDKNFDKIRVWLQSEKLERM,Endoplasmic reticulum aminopeptidase 1,"Aminopeptidase that plays a central role in peptide trimming, a step required for the generation of most HLA class I-binding peptides. Peptide trimming is essential to customize longer precursor peptides to fit them to the correct length required for presentation on MHC class I molecules. Strongly prefers substrates 9-16 residues long. Rapidly degrades 13-mer to a 9-mer and then stops. Preferentially hydrolyzes the residue Leu and peptides with a hydrophobic C-terminus, while it has weak activity toward peptides with charged C-terminus. May play a role in the inactivation of peptide hormones. May be involved in the regulation of blood pressure through the inactivation of angiotensin II and/or the generation of bradykinin in the kidney.",This mutation may result in altered enzymatic activity or protein function.,This mutation may result in altered enzymatic activity or protein function.
18,18,18,1068,Q99496-K93A,MSQAVQTNGTQPLSKTWELSLYELQRTPQEAITDGLEIVVSPRSLHSELMCPICLDMLKNTMTTKECLHRFCADCIITALRSGNKECPTCRKALVSKRSLRPDPNFDALISKIYPSRDEYEAHQERVLARINKHNNQQALSHSIEEGLKIQAMNRLQRGKKQQIENGSGAEDNGDSSHCSNASTHSNQEAGPSNKRTKTSDDSGLELDNNNAAMAIDPVMDGASEIELVFRPHPTLMEKDDSAQTRYIKTSGNATVDHLSKYLAVRLALEELRSKGESNQMNLDTASEKQYTIYIATASGQFTVLNGSFSLELVSEKYWKVNKPMELYYAPTKEHK,Mildly decreases ubiquitin ligase activity on histone H2A.,,MSQAVQTNGTQPLSKTWELSLYELQRTPQEAITDGLEIVVSPRSLHSELMCPICLDMLKNTMTTKECLHRFCADCIITALRSGNKECPTCRKKLVSKRSLRPDPNFDALISKIYPSRDEYEAHQERVLARINKHNNQQALSHSIEEGLKIQAMNRLQRGKKQQIENGSGAEDNGDSSHCSNASTHSNQEAGPSNKRTKTSDDSGLELDNNNAAMAIDPVMDGASEIELVFRPHPTLMEKDDSAQTRYIKTSGNATVDHLSKYLAVRLALEELRSKGESNQMNLDTASEKQYTIYIATASGQFTVLNGSFSLELVSEKYWKVNKPMELYYAPTKEHK,E3 ubiquitin-protein ligase RING2,"E3 ubiquitin-protein ligase that mediates monoubiquitination of 'Lys-119' of histone H2A (H2AK119Ub), thereby playing a central role in histone code and gene regulation. H2AK119Ub gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. May be involved in the initiation of both imprinted and random X inactivation. Essential component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones, rendering chromatin heritably changed in its expressibility. E3 ubiquitin-protein ligase activity is enhanced by BMI1/PCGF4. Acts as the main E3 ubiquitin ligase on histone H2A of the PRC1 complex, while RING1 may rather act as a modulator of RNF2/RING2 activity (Probable). Association with the chromosomal DNA is cell-cycle dependent. In resting B- and T-lymphocytes, interaction with AURKB leads to block its activity, thereby maintaining transcription in resting lymphocytes. Also acts as a negative regulator of autophagy by mediating ubiquitination of AMBRA1, leading to its subsequent degradation.",,Mildly decreases ubiquitin ligase activity on histone H2A.
19,19,19,1102,P68871-V24G,MVHLTPEEKSAVTALWGKVNVDEGGGEALGRLLVVYPWTQRFFESFGDLSTPDAVMGNPKVKAHGKKVLGAFSDGLAHLDNLKGTFATLSELHCDKLHVDPENFRLLGNVLVCVLAHHFGKEFTPPVQAAYQKVVAGVANALAHKYH,In Miyashiro; O(2) affinity up; unstable.,,MVHLTPEEKSAVTALWGKVNVDEVGGEALGRLLVVYPWTQRFFESFGDLSTPDAVMGNPKVKAHGKKVLGAFSDGLAHLDNLKGTFATLSELHCDKLHVDPENFRLLGNVLVCVLAHHFGKEFTPPVQAAYQKVVAGVANALAHKYH,Hemoglobin subunit beta,"Functions as an endogenous inhibitor of enkephalin-degrading enzymes such as DPP3, and as a selective antagonist of the P2RX3 receptor which is involved in pain signaling, these properties implicate it as a regulator of pain and inflammation.",This results in a slightly unstable hemoglobin that cannot be separated from Hb A by electrophoresis. Carriers of this variant show an increased whole blood oxygen affinity.,In Miyashiro; O(2) affinity up; unstable. This results in a slightly unstable hemoglobin that cannot be separated from Hb A by electrophoresis. Carriers of this variant show an increased whole blood oxygen affinity.
28,28,28,1611,P9WI55-D54N,MQFDVTIEIPKGQRNKYEVDHETGRVRLDRYLYTPMAYPTDYGFIEDTLGDDGNPLDALVLLPQPVFPGVLVAARPVGMFRMVDEHGGDDKVLCVPAGDPRWDHVQDIGDVPAFELDAIKHFFVHYKDLEPGKFVKAADWVDRAEAEAEVQRSVERFKAGTH,"3-fold decrease in catalytic activity, and 2-fold decrease in substrate affinity.",,MQFDVTIEIPKGQRNKYEVDHETGRVRLDRYLYTPMAYPTDYGFIEDTLGDDGDPLDALVLLPQPVFPGVLVAARPVGMFRMVDEHGGDDKVLCVPAGDPRWDHVQDIGDVPAFELDAIKHFFVHYKDLEPGKFVKAADWVDRAEAEAEVQRSVERFKAGTH,Inorganic pyrophosphatase,"Antigen that activates dendritic cells (DCs), increasing their expression of cell surface molecules and augmenting their production of TNF-alpha, IL-1beta, IL-6, IL-23 and IL-12p70. Rv3628 mediates these effects by binding to TLR2 and activating downstream MyD88-, MAPK- and NF-kappaB-dependent signaling pathways. Rv3628-stimulated DCs induce the expansion of OVA-specific CD4+ and CD8+ T cells which secrete IFN-gamma and IL-2, and the generation of effector/memory T cells. Thus, Rv3628 polarizes DCs toward a Th1 immune response and promotes protective immunity against M.tuberculosis infection. Is not able to bind to TLR4 molecules on the cell surface.",,"3-fold decrease in catalytic activity, and 2-fold decrease in substrate affinity."
32,32,32,1906,P49768-T116N,MTELPAPLSYFQNAQMSEDNHLSNTVRSQNDNRERQEHNDRRSLGHPEPLSNGRPQGNSRQVVEQDEEEDEELTLKYGAKHVIMLFVPVTLCMVVVVATIKSVSFYTRKDGQLIYNPFTEDTETVGQRALHSILNAAIMISVIVVMTILLVVLYKYRCYKVIHAWLIISSLLLLFFFSFIYLGEVFKTYNVAVDYITVALLIWNFGVVGMISIHWKGPLRLQQAYLIMISALMALVFIKYLPEWTAWLILAVISVYDLVAVLCPKGPLRMLVETAQERNETLFPALIYSSTMVWLVNMAEGDPEAQRRVSKNSKYNAESTERESQDTVAENDDGGFSEEWEAQRDSHLGPHRSTPESRAAVQELSSSILAGEDPEERGVKLGLGDFIFYSVLVGKASATASGDWNTTIACFVAILIGLCLTLLLLAIFKKALPALPISITFGLVFYFATDYLVQPFMDQLAFHQFYI,In AD3; unusual amyloid cotton wool plaques detected in one patient's brain; severe decrease of protease activity with APP; results in increased amyloid-beta 42/amyloid-beta 40 ratio.,,MTELPAPLSYFQNAQMSEDNHLSNTVRSQNDNRERQEHNDRRSLGHPEPLSNGRPQGNSRQVVEQDEEEDEELTLKYGAKHVIMLFVPVTLCMVVVVATIKSVSFYTRKDGQLIYTPFTEDTETVGQRALHSILNAAIMISVIVVMTILLVVLYKYRCYKVIHAWLIISSLLLLFFFSFIYLGEVFKTYNVAVDYITVALLIWNFGVVGMISIHWKGPLRLQQAYLIMISALMALVFIKYLPEWTAWLILAVISVYDLVAVLCPKGPLRMLVETAQERNETLFPALIYSSTMVWLVNMAEGDPEAQRRVSKNSKYNAESTERESQDTVAENDDGGFSEEWEAQRDSHLGPHRSTPESRAAVQELSSSILAGEDPEERGVKLGLGDFIFYSVLVGKASATASGDWNTTIACFVAILIGLCLTLLLLAIFKKALPALPISITFGLVFYFATDYLVQPFMDQLAFHQFYI,Presenilin-1,"Catalytic subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (amyloid-beta precursor protein). Requires the presence of the other members of the gamma-secretase complex for protease activity. Plays a role in Notch and Wnt signaling cascades and regulation of downstream processes via its role in processing key regulatory proteins, and by regulating cytosolic CTNNB1 levels. Stimulates cell-cell adhesion via its interaction with CDH1; this stabilizes the complexes between CDH1 (E-cadherin) and its interaction partners CTNNB1 (beta-catenin), CTNND1 and JUP (gamma-catenin). Under conditions of apoptosis or calcium influx, cleaves CDH1. This promotes the disassembly of the complexes between CDH1 and CTNND1, JUP and CTNNB1, increases the pool of cytoplasmic CTNNB1, and thereby negatively regulates Wnt signaling. Required for normal embryonic brain and skeleton development, and for normal angiogenesis. Mediates the proteolytic cleavage of EphB2/CTF1 into EphB2/CTF2. The holoprotein functions as a calcium-leak channel that allows the passive movement of calcium from endoplasmic reticulum to cytosol and is therefore involved in calcium homeostasis. Involved in the regulation of neurite outgrowth. Is a regulator of presynaptic facilitation, spike transmission and synaptic vesicles replenishment in a process that depends on gamma-secretase activity. It acts through the control of SYT7 presynaptic expression.","This substitution occurs in an evolutionary highly conserved region of the presenilin-1 protein and is associated with onset of early-onset Alzheimer's disease between age 35 and 41 years and 4-8 years' duration of the disease. The family described in the document has a missense mutation in the PSEN1 gene. This mutation is associated with early onset familial Alzheimer disease (FAD). The clinical symptoms include progressive memory impairment, amnestic aphasia, and gait disturbances. Neuropathological assessment revealed widespread β-amyloid and tau pathology, Cotton wool plaques were observed mainly in the occipital cortex. Cerebral amyloid angiopathy was present throughout the brain. The pattern of sarkosyl-insoluble tau was similar to sporadic AD. No α-synuclein or TDP-43 pathology was found.","In AD3; unusual amyloid cotton wool plaques detected in one patient's brain; severe decrease of protease activity with APP; results in increased amyloid-beta 42/amyloid-beta 40 ratio. This substitution occurs in an evolutionary highly conserved region of the presenilin-1 protein and is associated with onset of early-onset Alzheimer's disease between age 35 and 41 years and 4-8 years' duration of the disease. The family described in the document has a missense mutation in the PSEN1 gene. This mutation is associated with early onset familial Alzheimer disease (FAD). The clinical symptoms include progressive memory impairment, amnestic aphasia, and gait disturbances. Neuropathological assessment revealed widespread β-amyloid and tau pathology, Cotton wool plaques were observed mainly in the occipital cortex. Cerebral amyloid angiopathy was present throughout the brain. The pattern of sarkosyl-insoluble tau was similar to sporadic AD. No α-synuclein or TDP-43 pathology was found."
41,41,41,2778,O75531-K41E,MTTSQKHRDFVAEPMGEKPVGSLAGIGEVLGKKLEERGFDEAYVVLGQFLVLKKDEDLFREWLKDTCGANAKQSRDCFGCLREWCDAFL,Reduces histone H1/H3 binding.,,MTTSQKHRDFVAEPMGEKPVGSLAGIGEVLGKKLEERGFDKAYVVLGQFLVLKKDEDLFREWLKDTCGANAKQSRDCFGCLREWCDAFL,Barrier-to-autointegration factor,"Non-specific DNA-binding protein that plays key roles in mitotic nuclear reassembly, chromatin organization, DNA damage response, gene expression and intrinsic immunity against foreign DNA. Contains two non-specific double-stranded DNA (dsDNA)-binding sites which promote DNA cross-bridging. Plays a key role in nuclear membrane reformation at the end of mitosis by driving formation of a single nucleus in a spindle-independent manner. Transiently cross-bridges anaphase chromosomes via its ability to bridge distant DNA sites, leading to the formation of a dense chromatin network at the chromosome ensemble surface that limits membranes to the surface. Also acts as a negative regulator of innate immune activation by restricting CGAS activity toward self-DNA upon acute loss of nuclear membrane integrity. Outcompetes CGAS for DNA-binding, thereby preventing CGAS activation and subsequent damaging autoinflammatory responses. Also involved in DNA damage response: interacts with PARP1 in response to oxidative stress, thereby inhibiting the ADP-ribosyltransferase activity of PARP1. Involved in the recognition of exogenous dsDNA in the cytosol: associates with exogenous dsDNA immediately after its appearance in the cytosol at endosome breakdown and is required to avoid autophagy. In case of poxvirus infection, has an antiviral activity by blocking viral DNA replication.(Microbial infection) Exploited by retroviruses for inhibiting self-destructing autointegration of retroviral DNA, thereby promoting integration of viral DNA into the host chromosome. EMD and BAF are cooperative cofactors of HIV-1 infection. Association of EMD with the viral DNA requires the presence of BAF and viral integrase. The association of viral DNA with chromatin requires the presence of BAF and EMD.","The mutation in MAN1 has been shown to inhibit the binding of MAN1 to selected partners of emerin, such as GCL, Btf, and barrier-to-autointegration factor (BAF).","Reduces histone H1/H3 binding. The mutation in MAN1 has been shown to inhibit the binding of MAN1 to selected partners of emerin, such as GCL, Btf, and barrier-to-autointegration factor (BAF)."
42,42,42,2856,P43508-N301A,MKYLILAALVAVTAGLVIPLVPKTQEAITEYVNSKQSLWKAEIPKDITIEQVKKRLMRTEFVAPHTPDVEVVKHDINEDTIPATFDARTQWPNCMSINNIRDQSDCGSCWAFAAAEAASDRFCIASNGAVNTLLSAEDVLSCCSNCGYGCEGGYPINAWKYLVKSGFCTGGSYEAQFGCKPYSLAPCGETVGNVTWPSCPDDGYDTPACVNKCTNKNYNVAYTADKHFGSTAYAVGKKVSQIQAEIIAHGPVEAAFTVYEDFYQYKTGVYVHTTGQELGGHAIRILGWGTDNGTPYWLVAASWNVNWGENGYFRIIRGTNECGIEHAVVGGVPKV,No effect on protease or RIBE activity.,,MKYLILAALVAVTAGLVIPLVPKTQEAITEYVNSKQSLWKAEIPKDITIEQVKKRLMRTEFVAPHTPDVEVVKHDINEDTIPATFDARTQWPNCMSINNIRDQSDCGSCWAFAAAEAASDRFCIASNGAVNTLLSAEDVLSCCSNCGYGCEGGYPINAWKYLVKSGFCTGGSYEAQFGCKPYSLAPCGETVGNVTWPSCPDDGYDTPACVNKCTNKNYNVAYTADKHFGSTAYAVGKKVSQIQAEIIAHGPVEAAFTVYEDFYQYKTGVYVHTTGQELGGHAIRILGWGTDNGTPYWLVANSWNVNWGENGYFRIIRGTNECGIEHAVVGGVPKV,Cathepsin B-like cysteine proteinase 4,Thiol protease which shows activity against the fluorogenic substrate z-Arg-Arg-AMC.,,No effect on protease or RIBE activity.
46,46,46,2953,P06396-D214Y,MAPHRPAPALLCALSLALCALSLPVRAATASRGASQAGAPQGRVPEARPNSMVVEHPEFLKAGKEPGLQIWRVEKFDLVPVPTNLYGDFFTGDAYVILKTVQLRNGNLQYDLHYWLGNECSQDESGAAAIFTVQLDDYLNGRAVQHREVQGFESATFLGYFKSGLKYKKGGVASGFKHVVPNEVVVQRLFQVKGRRVVRATEVPVSWESFNNGYCFILDLGNNIHQWCGSNSNRYERLKATQVSKGIRDNERSGRARVHVSEEGTEPEAMLQVLGPKPALPAGTEDTAKEDAANRKLAKLYKVSNGAGTMSVSLVADENPFAQGALKSEDCFILDHGKDGKIFVWKGKQANTEERKAALKTASDFITKMDYPKQTQVSVLPEGGETPLFKQFFKNWRDPDQTDGLGLSYLSSHIANVERVPFDAATLHTSTAMAAQHGMDDDGTGQKQIWRIEGSNKVPVDPATYGQFYGGDSYIILYNYRHGGRQGQIIYNWQGAQSTQDEVAASAILTAQLDEELGGTPVQSRVVQGKEPAHLMSLFGGKPMIIYKGGTSREGGQTAPASTRLFQVRANSAGATRAVEVLPKAGALNSNDAFVLKTPSAAYLWVGTGASEAEKTGAQELLRVLRAQPVQVAEGSEPDGFWEALGGKAAYRTSPRLKDKKMDAHPPRLFACSNKIGRFVIEEVPGELMQEDLATDDVMLLDTWDQVFVWVGKDSQEEEKTEALTSAKRYIETDPANRDRRTPITVVKQGFEPPSFVGWFLGWDDDYWSVDPLDRAMAELAA,In AMYL5.,,MAPHRPAPALLCALSLALCALSLPVRAATASRGASQAGAPQGRVPEARPNSMVVEHPEFLKAGKEPGLQIWRVEKFDLVPVPTNLYGDFFTGDAYVILKTVQLRNGNLQYDLHYWLGNECSQDESGAAAIFTVQLDDYLNGRAVQHREVQGFESATFLGYFKSGLKYKKGGVASGFKHVVPNEVVVQRLFQVKGRRVVRATEVPVSWESFNNGDCFILDLGNNIHQWCGSNSNRYERLKATQVSKGIRDNERSGRARVHVSEEGTEPEAMLQVLGPKPALPAGTEDTAKEDAANRKLAKLYKVSNGAGTMSVSLVADENPFAQGALKSEDCFILDHGKDGKIFVWKGKQANTEERKAALKTASDFITKMDYPKQTQVSVLPEGGETPLFKQFFKNWRDPDQTDGLGLSYLSSHIANVERVPFDAATLHTSTAMAAQHGMDDDGTGQKQIWRIEGSNKVPVDPATYGQFYGGDSYIILYNYRHGGRQGQIIYNWQGAQSTQDEVAASAILTAQLDEELGGTPVQSRVVQGKEPAHLMSLFGGKPMIIYKGGTSREGGQTAPASTRLFQVRANSAGATRAVEVLPKAGALNSNDAFVLKTPSAAYLWVGTGASEAEKTGAQELLRVLRAQPVQVAEGSEPDGFWEALGGKAAYRTSPRLKDKKMDAHPPRLFACSNKIGRFVIEEVPGELMQEDLATDDVMLLDTWDQVFVWVGKDSQEEEKTEALTSAKRYIETDPANRDRRTPITVVKQGFEPPSFVGWFLGWDDDYWSVDPLDRAMAELAA,Gelsolin,"Calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping). It can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed. Plays a role in ciliogenesis.",Substitution of the acidic D at residue 214 with the uncharged Y creates a conformation that may be preferentially amyloidogenic for gelsolin.,In AMYL5. Substitution of the acidic D at residue 214 with the uncharged Y creates a conformation that may be preferentially amyloidogenic for gelsolin.
53,53,53,3183,P98170-L141A,MTFNSFEGSKTCVPADINKEEEFVEEFNRLKTFANFPSGSPVSASTLARAGFLYTGEGDTVRCFSCHAAVDRWQYGDSAVGRHRKVSPNCRFINGFYLENSATQSTNSGIQNGQYKVENYLGSRDHFALDRPSETHADYLARTGQVVDISDTIYPRNPAMYSEEARLKSFQNWPDYAHLTPRELASAGLYYTGIGDQVQCFCCGGKLKNWEPCDRAWSEHRRHFPNCFFVLGRNLNIRSESDAVSSDRNFPNSTNLPRNPSMADYEARIFTFGTWIYSVNKEQLARAGFYALGEGDKVKCFHCGGGLTDWKPSEDPWEQHAKWYPGCKYLLEQKGQEYINNIHLTHSLEECLVRTTEKTPSLTRRIDDTIFQNPMVQEAIRMGFSFKDIKKIMEEKIQISGSNYKSLEVLVADLVNAQKDSMQDESSQTSLQKEISTEEQLRRLQEEKLCKICMDRNIAIVFVPCGHLVTCKQCAEAVDKCPMCYTVITFKQKIFMS,Reduced inhibition of caspase-3.,,MTFNSFEGSKTCVPADINKEEEFVEEFNRLKTFANFPSGSPVSASTLARAGFLYTGEGDTVRCFSCHAAVDRWQYGDSAVGRHRKVSPNCRFINGFYLENSATQSTNSGIQNGQYKVENYLGSRDHFALDRPSETHADYLLRTGQVVDISDTIYPRNPAMYSEEARLKSFQNWPDYAHLTPRELASAGLYYTGIGDQVQCFCCGGKLKNWEPCDRAWSEHRRHFPNCFFVLGRNLNIRSESDAVSSDRNFPNSTNLPRNPSMADYEARIFTFGTWIYSVNKEQLARAGFYALGEGDKVKCFHCGGGLTDWKPSEDPWEQHAKWYPGCKYLLEQKGQEYINNIHLTHSLEECLVRTTEKTPSLTRRIDDTIFQNPMVQEAIRMGFSFKDIKKIMEEKIQISGSNYKSLEVLVADLVNAQKDSMQDESSQTSLQKEISTEEQLRRLQEEKLCKICMDRNIAIVFVPCGHLVTCKQCAEAVDKCPMCYTVITFKQKIFMS,E3 ubiquitin-protein ligase XIAP,"Multi-functional protein which regulates not only caspases and apoptosis, but also modulates inflammatory signaling and immunity, copper homeostasis, mitogenic kinase signaling, cell proliferation, as well as cell invasion and metastasis. Acts as a direct caspase inhibitor. Directly bind to the active site pocket of CASP3 and CASP7 and obstructs substrate entry. Inactivates CASP9 by keeping it in a monomeric, inactive state. Acts as an E3 ubiquitin-protein ligase regulating NF-kappa-B signaling and the target proteins for its E3 ubiquitin-protein ligase activity include: RIPK1, MAP3K2/MEKK2, DIABLO/SMAC, AIFM1, CCS and BIRC5/survivin. Ubiquitination of CCS leads to enhancement of its chaperone activity toward its physiologic target, SOD1, rather than proteasomal degradation. Ubiquitination of MAP3K2/MEKK2 and AIFM1 does not lead to proteasomal degradation. Plays a role in copper homeostasis by ubiquitinating COMMD1 and promoting its proteasomal degradation. Can also function as E3 ubiquitin-protein ligase of the NEDD8 conjugation pathway, targeting effector caspases for neddylation and inactivation. Ubiquitinates and therefore mediates the proteosomal degradation of BCL2 in response to apoptosis. Regulates the BMP signaling pathway and the SMAD and MAP3K7/TAK1 dependent pathways leading to NF-kappa-B and JNK activation. Acts as an important regulator of innate immune signaling via regulation of Nod-like receptors (NLRs). Protects cells from spontaneous formation of the ripoptosome, a large multi-protein complex that has the capability to kill cancer cells in a caspase-dependent and caspase-independent manner. Suppresses ripoptosome formation by ubiquitinating RIPK1 and CASP8. Acts as a positive regulator of Wnt signaling and ubiquitinates TLE1, TLE2, TLE3, TLE4 and AES. Ubiquitination of TLE3 results in inhibition of its interaction with TCF7L2/TCF4 thereby allowing efficient recruitment and binding of the transcriptional coactivator beta-catenin to TCF7L2/TCF4 that is required to initiate a Wnt-specific transcriptional program.",The absence or presence of these residues may explain the differences in caspase inhibition observed for different truncated and full-length IAPs.,Reduced inhibition of caspase-3. The absence or presence of these residues may explain the differences in caspase inhibition observed for different truncated and full-length IAPs.
71,71,71,5038,A0A0K8P6T7-W159A,MNFPRASRLMQAAVLGGLMAVSAAATAQTNPYARGPNPTAASLEASAGPFTVRSFTVSRPSGYGAGTVYYPTNAGGTVGAIAIVPGYTARQSSIKWWGPRLASHGFVVITIDTNSTLDQPSSRSSQQMAALRQVASLNGTSSSPIYGKVDTARMGVMGASMGGGGSLISAANNPSLKAAAPQAPWDSSTNFSSVTVPTLIFACENDSIAPVNSSALPIYDSMSRNAKQFLEINGGSHSCANSGNSNQALIGKKGVAWMKRFMDNDTRYSTFACENPNSTRVSDFRTANCS,Displays decreased enzymatic activity on PET film and on BHET.,,MNFPRASRLMQAAVLGGLMAVSAAATAQTNPYARGPNPTAASLEASAGPFTVRSFTVSRPSGYGAGTVYYPTNAGGTVGAIAIVPGYTARQSSIKWWGPRLASHGFVVITIDTNSTLDQPSSRSSQQMAALRQVASLNGTSSSPIYGKVDTARMGVMGWSMGGGGSLISAANNPSLKAAAPQAPWDSSTNFSSVTVPTLIFACENDSIAPVNSSALPIYDSMSRNAKQFLEINGGSHSCANSGNSNQALIGKKGVAWMKRFMDNDTRYSTFACENPNSTRVSDFRTANCS,Poly,"Involved in the degradation and assimilation of the plastic poly(ethylene terephthalate) (PET), which allows I.sakaiensis to use PET as its major energy and carbon source for growth. Likely acts synergistically with MHETase to depolymerize PET. Catalyzes the hydrolysis of PET to produce mono(2-hydroxyethyl) terephthalate (MHET) as the major product. Also depolymerizes another semiaromatic polyester, poly(ethylene-2,5-furandicarboxylate) (PEF), which is an emerging, bioderived PET replacement with improved gas barrier properties. In contrast, PETase does not degrade aliphatic polyesters such as polylactic acid (PLA) and polybutylene succinate (PBS). Is also able to hydrolyze bis(hydroxyethyl) terephthalate (BHET) to yield MHET with no further decomposition, but terephthalate (TPA) can also be observed. Shows esterase activity towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters) in vitro.",,Displays decreased enzymatic activity on PET film and on BHET.
75,75,75,5231,Q641K1-R910W,MSKLKVVGEKSLTNSSRVVGLLAQLEKINTDSTESDTARYVTSKILHLAQSQEKTRREMTTKGSTGMEVLLSTLENTKDLQTVLNILSILIELVSSGGGRRASFLVAKGGSQILLQLLMNASKDSPPHEEVMVQTHSILAKIGPKDKKFGVKARVNGALTVTLNLVKQHFQNYRLVLPCLQLLRVYSTNSVNSVSLGKNGVVELMFKIIGPFSKKNSGLMKVALDTLAALLKSKTNARRAVDRGYVQVLLTIYVDWHRHDNRHRNMLIRKGILQSLKSVTNIKLGRKAFIDANGMKILYNTSQECLAVRTLDPLVNTSSLIMRKCFPKNRLPLPTIKSSFHFQLPIIPVTGPVAQLYSLPPEVDDVVDESDDNDDIDLEVENELENEDDLDQSFKNDDIETDINKLRPQQVPGRTIEELKMYEHLFPELVDDFQDYELISKEPKPFVFEGKARGPIVVPTAGEEVPGNSGSVKKGVVMKERASPKGEEAKEDPKGHDRTLPQQLGGQSRVAPSAHSFNNDLVKALDRITLQNVPSQVASGLNAGMRKDFGLPLTVLSCTKACPHVAKCGSTLFEGRTVHLGKLCCTGVETEDDEDTESHSSTEQAPSVEASDGPTLHDPDLYIEIVKNTKSVPEYSEVAYPDYFGHIPPPFKEPILERPYGVQRTKIAQDIERLIHQNDIIDRVVYDLDNPTYTTPEEGDTLKFNSKFESGNLRKVIQIRKSEYDLILNSDINSNHYHQWFYFEVSGMRPGVAYRFNIINCEKSNSQFNYGMQPLMYSVQEALNARPWWIRMGTDICYYKNHFSRSSVAAGGQKGKSYYTITFTVNFPHKDDVCYFAYHYPYTYSTLQMHLQKLESAHNPQQIYFRKDVLCETLSGNICPLVTITAMPESNYYEHICQFRTRPYIFLSAWVHPGETNASWVMKGTLEYLMSNSPTAQSLRESYIFKIVPMLNPDGVINGNHRCSLSGEDLNRQWQSPNPELHPTIYHAKGLLQYLAAVKRLPLVYCDYHGHSRKKNVFMYGCSI,Decreased tubulin deglutamylation.,,MSKLKVVGEKSLTNSSRVVGLLAQLEKINTDSTESDTARYVTSKILHLAQSQEKTRREMTTKGSTGMEVLLSTLENTKDLQTVLNILSILIELVSSGGGRRASFLVAKGGSQILLQLLMNASKDSPPHEEVMVQTHSILAKIGPKDKKFGVKARVNGALTVTLNLVKQHFQNYRLVLPCLQLLRVYSTNSVNSVSLGKNGVVELMFKIIGPFSKKNSGLMKVALDTLAALLKSKTNARRAVDRGYVQVLLTIYVDWHRHDNRHRNMLIRKGILQSLKSVTNIKLGRKAFIDANGMKILYNTSQECLAVRTLDPLVNTSSLIMRKCFPKNRLPLPTIKSSFHFQLPIIPVTGPVAQLYSLPPEVDDVVDESDDNDDIDLEVENELENEDDLDQSFKNDDIETDINKLRPQQVPGRTIEELKMYEHLFPELVDDFQDYELISKEPKPFVFEGKARGPIVVPTAGEEVPGNSGSVKKGVVMKERASPKGEEAKEDPKGHDRTLPQQLGGQSRVAPSAHSFNNDLVKALDRITLQNVPSQVASGLNAGMRKDFGLPLTVLSCTKACPHVAKCGSTLFEGRTVHLGKLCCTGVETEDDEDTESHSSTEQAPSVEASDGPTLHDPDLYIEIVKNTKSVPEYSEVAYPDYFGHIPPPFKEPILERPYGVQRTKIAQDIERLIHQNDIIDRVVYDLDNPTYTTPEEGDTLKFNSKFESGNLRKVIQIRKSEYDLILNSDINSNHYHQWFYFEVSGMRPGVAYRFNIINCEKSNSQFNYGMQPLMYSVQEALNARPWWIRMGTDICYYKNHFSRSSVAAGGQKGKSYYTITFTVNFPHKDDVCYFAYHYPYTYSTLQMHLQKLESAHNPQQIYFRKDVLCETLSGNICPLVTITAMPESNYYEHICQFRTRPYIFLSARVHPGETNASWVMKGTLEYLMSNSPTAQSLRESYIFKIVPMLNPDGVINGNHRCSLSGEDLNRQWQSPNPELHPTIYHAKGLLQYLAAVKRLPLVYCDYHGHSRKKNVFMYGCSI,Cytosolic carboxypeptidase 1,"Metallocarboxypeptidase that mediates protein deglutamylation of tubulin and non-tubulin target proteins. Catalyzes the removal of polyglutamate side chains present on the gamma-carboxyl group of glutamate residues within the C-terminal tail of alpha- and beta-tubulin. Specifically cleaves tubulin long-side-chains, while it is not able to remove the branching point glutamate. Also catalyzes the removal of polyglutamate residues from the carboxy-terminus of alpha-tubulin as well as non-tubulin proteins such as MYLK. Involved in KLF4 deglutamylation which promotes KLF4 proteasome-mediated degradation, thereby negatively regulating cell pluripotency maintenance and embryogenesis.",,Decreased tubulin deglutamylation.
77,77,77,5413,P00492-C23F,MATRSPGVVISDDEPGYDLDLFFIPNHYAEDLERVFIPHGLIMDRTERLARDVMKEMGGHHIVALCVLKGGYKFFADLLDYIKALNRNSDRSIPMTVDFIRLKSYCNDQSTGDIKVIGGDDLSTLTGKNVLIVEDIIDTGKTMQTLLSLVRQYNPKMVKVASLLVKRTPRSVGYKPDFVGFEIPDKFVVGYALDYNEYFRDLNHVCVISETGKAKYKA,In HRH; Reduces enzymatic activity.,,MATRSPGVVISDDEPGYDLDLFCIPNHYAEDLERVFIPHGLIMDRTERLARDVMKEMGGHHIVALCVLKGGYKFFADLLDYIKALNRNSDRSIPMTVDFIRLKSYCNDQSTGDIKVIGGDDLSTLTGKNVLIVEDIIDTGKTMQTLLSLVRQYNPKMVKVASLLVKRTPRSVGYKPDFVGFEIPDKFVVGYALDYNEYFRDLNHVCVISETGKAKYKA,Hypoxanthine-guanine phosphoribosyltransferase,"Converts guanine to guanosine monophosphate, and hypoxanthine to inosine monophosphate. Transfers the 5-phosphoribosyl group from 5-phosphoribosylpyrophosphate onto the purine. Plays a central role in the generation of purine nucleotides through the purine salvage pathway.",,In HRH; Reduces enzymatic activity.
105,105,105,6864,O00391-C70S,MRRCNSGSGPPPSLLLLLLWLLAVPGANAAPRSALYSPSDPLTLLQADTVRGAVLGSRSAWAVEFFASWSGHCIAFAPTWKALAEDVKAWRPALYLAALDCAEETNSAVCRDFNIPGFPTVRFFKAFTKNGSGAVFPVAGADVQTLRERLIDALESHHDTWPPACPPLEPAKLEEIDGFFARNNEEYLALIFEKGGSYLGREVALDLSQHKGVAVRRVLNTEANVVRKFGVTDFPSCYLLFRNGSVSRVPVLMESRSFYTAYLQRLSGLTREAAQTTVAPTTANKIAPTVWKLADRSKIYMADLESALHYILRIEVGRFPVLEGQRLVALKKFVAVLAKYFPGRPLVQNFLHSVNEWLKRQKRNKIPYSFFKTALDDRKEGAVLAKKVNWIGCQGSEPHFRGFPCSLWVLFHFLTVQAARQNVDHSQEAAKAKEVLPAIRGYVHYFFGCRDCASHFEQMAAASMHRVGSPNAAVLWLWSSHNRVNARLAGAPSEDPQFPKVQWPPRELCSACHNERLDVPVWDVEATLNFLKAHFSPSNIILDFPAAGSAARRDVQNVAAAPELAMGALELESRNSTLDPGKPEMMKSPTNTTPHVPAEGPEASRPPKLHPGLRAAPGQEPPEHMAELQRNEQEQPLGQWHLSKRDTGAALLAESRAEKNRLWGPLEVRRVGRSSKQLVDIPEGQLEARAGRGRGQWLQVLGGGFSYLDISLCVGLYSLSFMGLLAMYTYFQAKIRALKGHAGHPAA,Reduces activity by 93%.,,MRRCNSGSGPPPSLLLLLLWLLAVPGANAAPRSALYSPSDPLTLLQADTVRGAVLGSRSAWAVEFFASWCGHCIAFAPTWKALAEDVKAWRPALYLAALDCAEETNSAVCRDFNIPGFPTVRFFKAFTKNGSGAVFPVAGADVQTLRERLIDALESHHDTWPPACPPLEPAKLEEIDGFFARNNEEYLALIFEKGGSYLGREVALDLSQHKGVAVRRVLNTEANVVRKFGVTDFPSCYLLFRNGSVSRVPVLMESRSFYTAYLQRLSGLTREAAQTTVAPTTANKIAPTVWKLADRSKIYMADLESALHYILRIEVGRFPVLEGQRLVALKKFVAVLAKYFPGRPLVQNFLHSVNEWLKRQKRNKIPYSFFKTALDDRKEGAVLAKKVNWIGCQGSEPHFRGFPCSLWVLFHFLTVQAARQNVDHSQEAAKAKEVLPAIRGYVHYFFGCRDCASHFEQMAAASMHRVGSPNAAVLWLWSSHNRVNARLAGAPSEDPQFPKVQWPPRELCSACHNERLDVPVWDVEATLNFLKAHFSPSNIILDFPAAGSAARRDVQNVAAAPELAMGALELESRNSTLDPGKPEMMKSPTNTTPHVPAEGPEASRPPKLHPGLRAAPGQEPPEHMAELQRNEQEQPLGQWHLSKRDTGAALLAESRAEKNRLWGPLEVRRVGRSSKQLVDIPEGQLEARAGRGRGQWLQVLGGGFSYLDISLCVGLYSLSFMGLLAMYTYFQAKIRALKGHAGHPAA,Sulfhydryl oxidase 1,"Catalyzes the oxidation of sulfhydryl groups in peptide and protein thiols to disulfides with the reduction of oxygen to hydrogen peroxide. Plays a role in disulfide bond formation in a variety of extracellular proteins. In fibroblasts, required for normal incorporation of laminin into the extracellular matrix, and thereby for normal cell-cell adhesion and cell migration.","The four other cysteine residues chosen for mutagenesis, C70, C73, C449, and C452, are all crucial for efficient oxidation of reduced RNase.","Reduces activity by 93%. The four other cysteine residues chosen for mutagenesis, C70, C73, C449, and C452, are all crucial for efficient oxidation of reduced RNase."
113,113,113,7518,P11413-G163D,MAEQVALSRTQVCGILREELFQGDAFHQSDTHIFIIMGASGDLAKKKIYPTIWWLFRDGLLPENTFIVGYARSRLTVADIRKQSEPFFKATPEEKLKLEDFFARNSYVAGQYDDAASYQRLNSHMNALHLGSQANRLFYLALPPTVYEAVTKNIHESCMSQIDWNRIIVEKPFGRDLQSSDRLSNHISSLFREDQIYRIDHYLGKEMVQNLMVLRFANRIFGPIWNRDNIACVILTFKEPFGTEGRGGYFDEFGIIRDVMQNHLLQMLCLVAMEKPASTNSDDVRDEKVKVLKCISEVQANNVVLGQYVGNPDGEGEATKGYLDDPTVPRGSTTATFAAVVLYVENERWDGVPFILRCGKALNERKAEVRLQFHDVAGDIFHQQCKRNELVIRVQPNEAVYTKMMTKKPGMFFNPEESELDLTYGNRYKNVKLPDAYERLILDVFCGSQMHFVRSDELREAWRIFTPLLHQIELEKPKPIPYIYGSRGPTEADELMKRVGFQYEGTYKWVNPHKL,In NSHA; Plymouth; class I.,,MAEQVALSRTQVCGILREELFQGDAFHQSDTHIFIIMGASGDLAKKKIYPTIWWLFRDGLLPENTFIVGYARSRLTVADIRKQSEPFFKATPEEKLKLEDFFARNSYVAGQYDDAASYQRLNSHMNALHLGSQANRLFYLALPPTVYEAVTKNIHESCMSQIGWNRIIVEKPFGRDLQSSDRLSNHISSLFREDQIYRIDHYLGKEMVQNLMVLRFANRIFGPIWNRDNIACVILTFKEPFGTEGRGGYFDEFGIIRDVMQNHLLQMLCLVAMEKPASTNSDDVRDEKVKVLKCISEVQANNVVLGQYVGNPDGEGEATKGYLDDPTVPRGSTTATFAAVVLYVENERWDGVPFILRCGKALNERKAEVRLQFHDVAGDIFHQQCKRNELVIRVQPNEAVYTKMMTKKPGMFFNPEESELDLTYGNRYKNVKLPDAYERLILDVFCGSQMHFVRSDELREAWRIFTPLLHQIELEKPKPIPYIYGSRGPTEADELMKRVGFQYEGTYKWVNPHKL,Glucose-6-phosphate 1-dehydrogenase,"Catalyzes the rate-limiting step of the oxidative pentose-phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis. The main function of this enzyme is to provide reducing power (NADPH) and pentose phosphates for fatty acid and nucleic acid synthesis.",The mutation in the glucose-6-phosphate dehydrogenase enzyme has been identified in individuals with chronic nonspherocytic hemolytic anemia. This mutation results in a deficiency of the enzyme.,In NSHA; Plymouth; class I. The mutation in the glucose-6-phosphate dehydrogenase enzyme has been identified in individuals with chronic nonspherocytic hemolytic anemia. This mutation results in a deficiency of the enzyme.
114,114,114,7676,Q8WZK3-R76A,MSTLSYVSPDALKGWLMESPNEISIIDVRDYDYEGERIPGSVRIPSDTFLASVDQHVDDLMKKRSLIVHCTYSQVAGPKAARVLSEILRNRITESKEKLSLSQKEKLFQNLPTVYILHGGFSAWKRRYGGQQGLIEYD,No catalytic activity.,,MSTLSYVSPDALKGWLMESPNEISIIDVRDYDYEGERIPGSVRIPSDTFLASVDQHVDDLMKKRSLIVHCTYSQVRGPKAARVLSEILRNRITESKEKLSLSQKEKLFQNLPTVYILHGGFSAWKRRYGGQQGLIEYD,Dual specificity phosphatase ibp1,May play a role in DNA replication checkpoint via regulation of hsk1 or may act downstream of hsk1 in an S phase regulatory pathway.,,No catalytic activity.
132,132,132,9202,P61978-K422R,METEQPEETFPNTETNGEFGKRPAEDMEEEQAFKRSRNTDEMVELRILLQSKNAGAVIGKGGKNIKALRTDYNASVSVPDSSGPERILSISADIETIGEILKKIIPTLEEGLQLPSPTATSQLPLESDAVECLNYQHYKGSDFDCELRLLIHQSLAGGIIGVKGAKIKELRENTQTTIKLFQECCPHSTDRVVLIGGKPDRVVECIKIILDLISESPIKGRAQPYDPNFYDETYDYGGFTMMFDDRRGRPVGFPMRGRGGFDRMPPGRGGRPMPPSRRDYDDMSPRRGPPPPPPGRGGRGGSRARNLPLPPPPPPRGGDLMAYDRRGRPGDRYDGMVGFSADETWDSAIDTWSPSEWQMAYEPQGGSGYDYSYAGGRGSYGDLGGPIITTQVTIPKDLAGSIIGKGGQRIKQIRHESGASIRIDEPLEGSEDRIITITGTQDQIQNAQYLLQNSVKQYSGKFF,Loss of sumoylation. Loss of TP53 transcriptional stimulation.,,METEQPEETFPNTETNGEFGKRPAEDMEEEQAFKRSRNTDEMVELRILLQSKNAGAVIGKGGKNIKALRTDYNASVSVPDSSGPERILSISADIETIGEILKKIIPTLEEGLQLPSPTATSQLPLESDAVECLNYQHYKGSDFDCELRLLIHQSLAGGIIGVKGAKIKELRENTQTTIKLFQECCPHSTDRVVLIGGKPDRVVECIKIILDLISESPIKGRAQPYDPNFYDETYDYGGFTMMFDDRRGRPVGFPMRGRGGFDRMPPGRGGRPMPPSRRDYDDMSPRRGPPPPPPGRGGRGGSRARNLPLPPPPPPRGGDLMAYDRRGRPGDRYDGMVGFSADETWDSAIDTWSPSEWQMAYEPQGGSGYDYSYAGGRGSYGDLGGPIITTQVTIPKDLAGSIIGKGGQRIKQIRHESGASIKIDEPLEGSEDRIITITGTQDQIQNAQYLLQNSVKQYSGKFF,Heterogeneous nuclear ribonucleoprotein K,"One of the major pre-mRNA-binding proteins. Binds tenaciously to poly(C) sequences. Likely to play a role in the nuclear metabolism of hnRNAs, particularly for pre-mRNAs that contain cytidine-rich sequences. Can also bind poly(C) single-stranded DNA. Plays an important role in p53/TP53 response to DNA damage, acting at the level of both transcription activation and repression. When sumoylated, acts as a transcriptional coactivator of p53/TP53, playing a role in p21/CDKN1A and 14-3-3 sigma/SFN induction. As far as transcription repression is concerned, acts by interacting with long intergenic RNA p21 (lincRNA-p21), a non-coding RNA induced by p53/TP53. This interaction is necessary for the induction of apoptosis, but not cell cycle arrest. As part of a ribonucleoprotein complex composed at least of ZNF827, HNRNPL and the circular RNA circZNF827 that nucleates the complex on chromatin, may negatively regulate the transcription of genes involved in neuronal differentiation.","DNA damage stimulates hnRNP K sumoylation through Pc2 E3 activity, and this modification is required for p53 transcriptional activation.","Loss of sumoylation. Loss of TP53 transcriptional stimulation. DNA damage stimulates hnRNP K sumoylation through Pc2 E3 activity, and this modification is required for p53 transcriptional activation."
140,140,140,9785,Q86YC2-Y28A,MDEPPGKPLSCEEKEKLKEKLAFLKREASKTLARLQRAQRAEKIKHSIKKTVEEQDCLSQQDLSPQLKHSEPKNKICVYDKLHIKTHLDEETGEKTSITLDVGPESFNPGDGPGGLPIQRTDDTQEHFPHRVSDPSGEQKQKLPSRRKKQQKRTFISQERDCVFGTDSLRLSGKRLKEQEEISSKNPARSPVTEIRTHLLSLKSELPDSPEPVTEINEDSVLIPPTAQPEKGVDTFLRRPNFTRATTVPLQTLSDSGSSQHLEHIPPKGSSELTTHDLKNIRFTSPVSLEAQGKKMTVSTDNLLVNKAISKSGQLPTSSNLEANISCSLNELTYNNLPANENQNLKEQNQTEKSLKSPSDTLDGRNENLQESEILSQPKSLSLEATSPLSAEKHSCTVPEGLLFPAEYYVRTTRSMSNCQRKVAVEAVIQSHLDVKKKGFKNKNKDASKNLNLSNEETDQSEIRMSGTCTGQPSSRTSQKLLSLTKVSSPAGPTEDNDLSRKAVAQAPGRRYTGKRKSACTPASDHCEPLLPTSSLSIVNRSKEEVTSHKYQHEKLFIQVKGKKSRHQKEDSLSWSNSAYLSLDDDAFTAPFHRDGMLSLKQLLSFLSITDFQLPDEDFGPLKLEKVKSCSEKPVEPFESKMFGERHLKEGSCIFPEELSPKRMDTEMEDLEEDLIVLPGKSHPKRPNSQSQHTKTGLSSSILLYTPLNTVAPDDNDRPTTDMCSPAFPILGTTPAFGPQGSYEKASTEVAGRTCCTPQLAHLKDSVCLASDTKQFDSSGSPAKPHTTLQVSGRQGQPTCDCDSVPPGTPPPIESFTFKENQLCRNTCQELHKHSVEQTETAELPASDSINPGNLQLVSELKNPSGSCSVDVSAMFWERAGCKEPCIITACEDVVSLWKALDAWQWEKLYTWHFAEVPVLQIVPVPDVYNLVCVALGNLEIREIRALFCSSDDESEKQVLLKSGNIKAVLGLTKRRLVSSSGTLSDQQVEVMTFAEDGGGKENQFLMPPEETILTFAEVQGMQE,Loss of interaction with BRCA1 but no effect on interaction with BRCA2.,,MDEPPGKPLSCEEKEKLKEKLAFLKREYSKTLARLQRAQRAEKIKHSIKKTVEEQDCLSQQDLSPQLKHSEPKNKICVYDKLHIKTHLDEETGEKTSITLDVGPESFNPGDGPGGLPIQRTDDTQEHFPHRVSDPSGEQKQKLPSRRKKQQKRTFISQERDCVFGTDSLRLSGKRLKEQEEISSKNPARSPVTEIRTHLLSLKSELPDSPEPVTEINEDSVLIPPTAQPEKGVDTFLRRPNFTRATTVPLQTLSDSGSSQHLEHIPPKGSSELTTHDLKNIRFTSPVSLEAQGKKMTVSTDNLLVNKAISKSGQLPTSSNLEANISCSLNELTYNNLPANENQNLKEQNQTEKSLKSPSDTLDGRNENLQESEILSQPKSLSLEATSPLSAEKHSCTVPEGLLFPAEYYVRTTRSMSNCQRKVAVEAVIQSHLDVKKKGFKNKNKDASKNLNLSNEETDQSEIRMSGTCTGQPSSRTSQKLLSLTKVSSPAGPTEDNDLSRKAVAQAPGRRYTGKRKSACTPASDHCEPLLPTSSLSIVNRSKEEVTSHKYQHEKLFIQVKGKKSRHQKEDSLSWSNSAYLSLDDDAFTAPFHRDGMLSLKQLLSFLSITDFQLPDEDFGPLKLEKVKSCSEKPVEPFESKMFGERHLKEGSCIFPEELSPKRMDTEMEDLEEDLIVLPGKSHPKRPNSQSQHTKTGLSSSILLYTPLNTVAPDDNDRPTTDMCSPAFPILGTTPAFGPQGSYEKASTEVAGRTCCTPQLAHLKDSVCLASDTKQFDSSGSPAKPHTTLQVSGRQGQPTCDCDSVPPGTPPPIESFTFKENQLCRNTCQELHKHSVEQTETAELPASDSINPGNLQLVSELKNPSGSCSVDVSAMFWERAGCKEPCIITACEDVVSLWKALDAWQWEKLYTWHFAEVPVLQIVPVPDVYNLVCVALGNLEIREIRALFCSSDDESEKQVLLKSGNIKAVLGLTKRRLVSSSGTLSDQQVEVMTFAEDGGGKENQFLMPPEETILTFAEVQGMQE,Partner and localizer of BRCA2,"Plays a critical role in homologous recombination repair (HRR) through its ability to recruit BRCA2 and RAD51 to DNA breaks. Strongly stimulates the DNA strand-invasion activity of RAD51, stabilizes the nucleoprotein filament against a disruptive BRC3-BRC4 polypeptide and helps RAD51 to overcome the suppressive effect of replication protein A (RPA). Functionally cooperates with RAD51AP1 in promoting of D-loop formation by RAD51. Serves as the molecular scaffold in the formation of the BRCA1-PALB2-BRCA2 complex which is essential for homologous recombination. Via its WD repeats is proposed to scaffold a HR complex containing RAD51C and BRCA2 which is thought to play a role in HR-mediated DNA repair. Essential partner of BRCA2 that promotes the localization and stability of BRCA2. Also enables its recombinational repair and checkpoint functions of BRCA2. May act by promoting stable association of BRCA2 with nuclear structures, allowing BRCA2 to escape the effects of proteasome-mediated degradation. Binds DNA with high affinity for D loop, which comprises single-stranded, double-stranded and branched DNA structures. May play a role in the extension step after strand invasion at replication-dependent DNA double-strand breaks; together with BRCA2 is involved in both POLH localization at collapsed replication forks and DNA polymerization activity.",BRCA1 mutations identified in cancer patients disrupted the specific interaction between BRCA1 and PALB2.,Loss of interaction with BRCA1 but no effect on interaction with BRCA2. BRCA1 mutations identified in cancer patients disrupted the specific interaction between BRCA1 and PALB2.
150,150,150,10991,Q9PZT0-P723A,MSKESGKWWESDDKFAKAVYQQFVEFYEKVTGTDLELIQILKDHYNISLDNPLENPSSLFDLVARIKNNLKNSPDLYSHHFQSHGQLSDHPHALSSSSSHAEPRGENAVLSSEDLHKPGQVSVQLPGTNYVGPGNELQAGPPQSAVDSAARIHDFRYSQLAKLGINPYTHWTVADEELLKNIKNETGFQAQVVKDYFTLKGAAAPVAHFQGSLPEVPAYNASEKYPSMTSVNSAEASTGAGGGGSNPVKSMWSEGATFSANSVTCTFSRQFLIPYDPEHHYKVFSPAASSCHNASGKEAKVCTISPIMGYSTPWRYLDFNALNLFFSPLEFQHLIENYGSIAPDALTVTISEIAVKDVTDKTGGGVQVTDSTTGRLSMLVDHEYKYPYVLGQGQDTLAPELPIWVYFPPQYAYLTVGDVNTQGISGDSKKLASEESAFYVLEHSSFQLLGTGGTATMSYKFPPVPPENLEGCSQHFYEMYNPLYGSRLGVPDTLGGDPKFRSLTHEDHAIQPQNFMPGPLVNSVSTKEGDSSNTGAGKALTGLSTGTSQNTRISLRPGPVSQPYHHWDTDKYVPGINAISHGQTTYGNAEDKEYQQGVGRFPNEKEQLKQLQGLNMHTYFPNKGTQQYTDQIERPLMVGSVWNRRALHYESQLWSKIPNLDDSFKTQFAALGGWGLHQPPPQIFLKILPQSGPIGGIKSMGITTLVQYAVGIMTVTMTFKLGARKATGRWNPQPGVYPPHAAGHLPYVLYDPTATDAKQHHRHGYEKPEELWTAKSRVHPL,Host nucleocytoplasmic localization.,,MSKESGKWWESDDKFAKAVYQQFVEFYEKVTGTDLELIQILKDHYNISLDNPLENPSSLFDLVARIKNNLKNSPDLYSHHFQSHGQLSDHPHALSSSSSHAEPRGENAVLSSEDLHKPGQVSVQLPGTNYVGPGNELQAGPPQSAVDSAARIHDFRYSQLAKLGINPYTHWTVADEELLKNIKNETGFQAQVVKDYFTLKGAAAPVAHFQGSLPEVPAYNASEKYPSMTSVNSAEASTGAGGGGSNPVKSMWSEGATFSANSVTCTFSRQFLIPYDPEHHYKVFSPAASSCHNASGKEAKVCTISPIMGYSTPWRYLDFNALNLFFSPLEFQHLIENYGSIAPDALTVTISEIAVKDVTDKTGGGVQVTDSTTGRLSMLVDHEYKYPYVLGQGQDTLAPELPIWVYFPPQYAYLTVGDVNTQGISGDSKKLASEESAFYVLEHSSFQLLGTGGTATMSYKFPPVPPENLEGCSQHFYEMYNPLYGSRLGVPDTLGGDPKFRSLTHEDHAIQPQNFMPGPLVNSVSTKEGDSSNTGAGKALTGLSTGTSQNTRISLRPGPVSQPYHHWDTDKYVPGINAISHGQTTYGNAEDKEYQQGVGRFPNEKEQLKQLQGLNMHTYFPNKGTQQYTDQIERPLMVGSVWNRRALHYESQLWSKIPNLDDSFKTQFAALGGWGLHQPPPQIFLKILPQSGPIGGIKSMGITTLVQYAVGIMTVTMTFKLGPRKATGRWNPQPGVYPPHAAGHLPYVLYDPTATDAKQHHRHGYEKPEELWTAKSRVHPL,Minor capsid protein VP1,"Capsid protein self-assembles to form an icosahedral capsid with a T=1 symmetry, about 20 nm in diameter, and consisting of 60 copies of two size variants of the capsid proteins, VP1 and VP2, which differ by the presence of an N-terminal extension in the minor protein VP1. The capsid encapsulates the genomic ssDNA (Probable). Binds to erythroid progenitor cells expressing high levels of P antigen and uses host ITGA5-ITGB1 and XRCC5/Ku80 autoantigen as coreceptors on the cell surface to provide virion attachment to target cell. This attachment induces virion internalization predominantly through clathrin-dependent endocytosis. Binding to the host receptors also induces capsid rearrangements leading to surface exposure of VP1 N-terminus, specifically its phospholipase A2-like region. The additional N-terminal region of isoform Minor capsid protein VP1, called VP1u, may serve as a lipolytic enzyme to breach the endosomal membrane during entry into host cell and might contribute to virus transport to the nucleus.",The mutation in the VP2 protein has been identified and shown to be necessary for the nuclear localization of VP2. This mutation affects the transport of the protein into the nucleus.,Host nucleocytoplasmic localization. The mutation in the VP2 protein has been identified and shown to be necessary for the nuclear localization of VP2. This mutation affects the transport of the protein into the nucleus.
152,152,152,11052,P04925-P104L,MANLGYWLLALFVTMWTDVGLCKKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGTWGQPHGGGWGQPHGGSWGQPHGGSWGQPHGGGWGQGGGTHNQWNKPSKLKTNLKHVAGAAAAGAVVGGLGGYMLGSAMSRPMIHFGNDWEDRYYRENMYRYPNQVYYRPVDQYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCVTQYQKESQAYYDGRRSSSTVLFSSPPVILLISFLIFLIVG,No effect on interaction with GRB2.,,MANLGYWLLALFVTMWTDVGLCKKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGTWGQPHGGGWGQPHGGSWGQPHGGSWGQPHGGGWGQGGGTHNQWNKPSKPKTNLKHVAGAAAAGAVVGGLGGYMLGSAMSRPMIHFGNDWEDRYYRENMYRYPNQVYYRPVDQYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCVTQYQKESQAYYDGRRSSSTVLFSSPPVILLISFLIFLIVG,Major prion protein,Its primary physiological function is unclear. May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May promote myelin homeostasis through acting as an agonist for ADGRG6 receptor. May play a role in iron uptake and iron homeostasis. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro). Association with GPC1 (via its heparan sulfate chains) targets PRNP to lipid rafts. Also provides Cu(2+) or Zn(2+) for the ascorbate-mediated GPC1 deaminase degradation of its heparan sulfate side chains.,,No effect on interaction with GRB2.
160,160,160,11643,O70469-Y276F,MVRMEEPAVKQGFLHLQQQQTFGKKWRRFAAVLYGESGCALARLELQDVPEKTRRGEATRKVVRLSDCLRVAEVGSEASSPRDTSAFILETKERLYLLAAPSAERSDWIQAICLLAFPGQRKGSPGLEEKSGSPCMEENELYSSSTTGLCKEYMVTIRPTEASERCRLRGSYTLRTGVSALELWGGPEPGTQLYDWPYRFLRRFGRDKATFSFEAGRRCLSGEGNFEFETRHGNEIFQALEKVIAVQKNATPSGPPSLPATGPMMPTVLPRPESPFSRPHDSLPSPSPGTLVPGMRPGAPEGEYAVPFDTVAHSLRKSFRGLLTGPPPHLPDPLYDSIQEDPGAPLPDHIYDEPEGVAALSLYDRTQRPSGETWREQATADGGPSSLQQDSSVPDWPQATEYDNVILKKGPK,No loss of binding to SH2 domain of RASGAP or NCK. Complete loss of binding to SH2 domain of RASGAP; when associated with F-304.,,MVRMEEPAVKQGFLHLQQQQTFGKKWRRFAAVLYGESGCALARLELQDVPEKTRRGEATRKVVRLSDCLRVAEVGSEASSPRDTSAFILETKERLYLLAAPSAERSDWIQAICLLAFPGQRKGSPGLEEKSGSPCMEENELYSSSTTGLCKEYMVTIRPTEASERCRLRGSYTLRTGVSALELWGGPEPGTQLYDWPYRFLRRFGRDKATFSFEAGRRCLSGEGNFEFETRHGNEIFQALEKVIAVQKNATPSGPPSLPATGPMMPTVLPRPESPYSRPHDSLPSPSPGTLVPGMRPGAPEGEYAVPFDTVAHSLRKSFRGLLTGPPPHLPDPLYDSIQEDPGAPLPDHIYDEPEGVAALSLYDRTQRPSGETWREQATADGGPSSLQQDSSVPDWPQATEYDNVILKKGPK,Docking protein 2,"DOK proteins are enzymatically inert adaptor or scaffolding proteins. They provide a docking platform for the assembly of multimolecular signaling complexes. DOK2 may modulate the cellular proliferation induced by IL-4, as well as IL-2 and IL-3. May be involved in modulating Bcr-Abl signaling. Attenuates EGF-stimulated MAP kinase activation.",phosphorylated Y276 and Y304 are proposed to dock the tandem Src homology 2 (SH2) domains of the p21(Ras) GTPase-activating protein rasGAP.,No loss of binding to SH2 domain of RASGAP or NCK. Complete loss of binding to SH2 domain of RASGAP; when associated with F-304. phosphorylated Y276 and Y304 are proposed to dock the tandem Src homology 2 (SH2) domains of the p21(Ras) GTPase-activating protein rasGAP.
188,188,188,13978,P31271-I368F,MTASVLLHPRWIEPTVMFLYDNGGGLVADELNKNMEGAAAAAAAAAAAAAAGAGGGGFPHPAAAAAGGNFSVAAAAAAAAAAAANQCRNLMAHPAPLAPGAASAYSSAPGEAPPSAAAAAAAAAAAAAAAAAASSSGGPGPAGPAGAEAAKQCSPCSAAAQSSSGPAALPYGYFGSGYYPCARMGPHPNAIKSCAQPASAAAAAAFADKYMDTAGPAAEEFSSRAKEFAFYHQGYAAGPYHHHQPMPGYLDMPVVPGLGGPGESRHEPLGLPMESYQPWALPNGWNGQMYCPKEQAQPPHLWKSTLPDVVSHPSDASSYRRGRKKRVPYTKVQLKELEREYATNKFITKDKRRRISATTNLSERQVTFWFQNRRVKEKKVINKLKTTS,In HFG; severe phenotype overlapping with Guttmacher syndrome.,,MTASVLLHPRWIEPTVMFLYDNGGGLVADELNKNMEGAAAAAAAAAAAAAAGAGGGGFPHPAAAAAGGNFSVAAAAAAAAAAAANQCRNLMAHPAPLAPGAASAYSSAPGEAPPSAAAAAAAAAAAAAAAAAASSSGGPGPAGPAGAEAAKQCSPCSAAAQSSSGPAALPYGYFGSGYYPCARMGPHPNAIKSCAQPASAAAAAAFADKYMDTAGPAAEEFSSRAKEFAFYHQGYAAGPYHHHQPMPGYLDMPVVPGLGGPGESRHEPLGLPMESYQPWALPNGWNGQMYCPKEQAQPPHLWKSTLPDVVSHPSDASSYRRGRKKRVPYTKVQLKELEREYATNKFITKDKRRRISATTNLSERQVTIWFQNRRVKEKKVINKLKTTS,Homeobox protein Hox-A13,"Sequence-specific, AT-rich binding transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.","Heterozygous HOXA13 mutations have been previously reported in hand-foot-genital syndrome and Guttmacher syndrome, which are variably associated with small nails, short distal and middle phalanges, short thumbs and halluces, but not absent nails. Considering the molecular data, the phenotype in the present patient was defined as the severe end of hand-foot-genital and Guttmacher syndrome spectrum. Our observation expands the clinical spectrum caused by heterozygous HOXA13 mutations and reinforces the difficulty of differential diagnosis on clinical grounds for the disorders with short distal phalanges, short thumbs, and short halluces.","In HFG; severe phenotype overlapping with Guttmacher syndrome. Heterozygous HOXA13 mutations have been previously reported in hand-foot-genital syndrome and Guttmacher syndrome, which are variably associated with small nails, short distal and middle phalanges, short thumbs and halluces, but not absent nails. Considering the molecular data, the phenotype in the present patient was defined as the severe end of hand-foot-genital and Guttmacher syndrome spectrum. Our observation expands the clinical spectrum caused by heterozygous HOXA13 mutations and reinforces the difficulty of differential diagnosis on clinical grounds for the disorders with short distal phalanges, short thumbs, and short halluces."
200,200,200,14893,Q96P20-D82R,MKMASTRCKLARYLEDLEDVDLKKFKMHLEDYPPQKGCIPLPRGQTEKADHVDLATLMIDFNGEEKAWAMAVWIFAAINRRRLYEKAKRDEPKWGSDNARVSNPTVICQEDSIEEEWMGLLEYLSRISICKMKKDYRKKYRKYVRSRFQCIEDRNARLGESVSLNKRYTRLRLIKEHRSQQEREQELLAIGKTKTCESPVSPIKMELLFDPDDEHSEPVHTVVFQGAAGIGKTILARKMMLDWASGTLYQDRFDYLFYIHCREVSLVTQRSLGDLIMSCCPDPNPPIHKIVRKPSRILFLMDGFDELQGAFDEHIGPLCTDWQKAERGDILLSSLIRKKLLPEASLLITTRPVALEKLQHLLDHPRHVEILGFSEAKRKEYFFKYFSDEAQARAAFSLIQENEVLFTMCFIPLVCWIVCTGLKQQMESGKSLAQTSKTTTAVYVFFLSSLLQPRGGSQEHGLCAHLWGLCSLAADGIWNQKILFEESDLRNHGLQKADVSAFLRMNLFQKEVDCEKFYSFIHMTFQEFFAAMYYLLEEEKEGRTNVPGSRLKLPSRDVTVLLENYGKFEKGYLIFVVRFLFGLVNQERTSYLEKKLSCKISQQIRLELLKWIEVKAKAKKLQIQPSQLELFYCLYEMQEEDFVQRAMDYFPKIEINLSTRMDHMVSSFCIENCHRVESLSLGFLHNMPKEEEEEEKEGRHLDMVQCVLPSSSHAACSHGLVNSHLTSSFCRGLFSVLSTSQSLTELDLSDNSLGDPGMRVLCETLQHPGCNIRRLWLGRCGLSHECCFDISLVLSSNQKLVELDLSDNALGDFGIRLLCVGLKHLLCNLKKLWLVSCCLTSACCQDLASVLSTSHSLTRLYVGENALGDSGVAILCEKAKNPQCNLQKLGLVNSGLTSVCCSALSSVLSTNQNLTHLYLRGNTLGDKGIKLLCEGLLHPDCKLQVLELDNCNLTSHCCWDLSTLLTSSQSLRKLSLGNNDLGDLGVMMFCEVLKQQSCLLQNLGLSEMYFNYETKSALETLQEE,Complete loss of PYCARD/ASC filament nucleation.,,MKMASTRCKLARYLEDLEDVDLKKFKMHLEDYPPQKGCIPLPRGQTEKADHVDLATLMIDFNGEEKAWAMAVWIFAAINRRDLYEKAKRDEPKWGSDNARVSNPTVICQEDSIEEEWMGLLEYLSRISICKMKKDYRKKYRKYVRSRFQCIEDRNARLGESVSLNKRYTRLRLIKEHRSQQEREQELLAIGKTKTCESPVSPIKMELLFDPDDEHSEPVHTVVFQGAAGIGKTILARKMMLDWASGTLYQDRFDYLFYIHCREVSLVTQRSLGDLIMSCCPDPNPPIHKIVRKPSRILFLMDGFDELQGAFDEHIGPLCTDWQKAERGDILLSSLIRKKLLPEASLLITTRPVALEKLQHLLDHPRHVEILGFSEAKRKEYFFKYFSDEAQARAAFSLIQENEVLFTMCFIPLVCWIVCTGLKQQMESGKSLAQTSKTTTAVYVFFLSSLLQPRGGSQEHGLCAHLWGLCSLAADGIWNQKILFEESDLRNHGLQKADVSAFLRMNLFQKEVDCEKFYSFIHMTFQEFFAAMYYLLEEEKEGRTNVPGSRLKLPSRDVTVLLENYGKFEKGYLIFVVRFLFGLVNQERTSYLEKKLSCKISQQIRLELLKWIEVKAKAKKLQIQPSQLELFYCLYEMQEEDFVQRAMDYFPKIEINLSTRMDHMVSSFCIENCHRVESLSLGFLHNMPKEEEEEEKEGRHLDMVQCVLPSSSHAACSHGLVNSHLTSSFCRGLFSVLSTSQSLTELDLSDNSLGDPGMRVLCETLQHPGCNIRRLWLGRCGLSHECCFDISLVLSSNQKLVELDLSDNALGDFGIRLLCVGLKHLLCNLKKLWLVSCCLTSACCQDLASVLSTSHSLTRLYVGENALGDSGVAILCEKAKNPQCNLQKLGLVNSGLTSVCCSALSSVLSTNQNLTHLYLRGNTLGDKGIKLLCEGLLHPDCKLQVLELDNCNLTSHCCWDLSTLLTSSQSLRKLSLGNNDLGDLGVMMFCEVLKQQSCLLQNLGLSEMYFNYETKSALETLQEE,"NACHT, LRR and PYD domains-containing protein 3","Sensor component of the NLRP3 inflammasome, which mediates inflammasome activation in response to defects in membrane integrity, leading to secretion of inflammatory cytokines IL1B and IL18 and pyroptosis. In response to pathogens and other damage-associated signals that affect the integrity of membranes, initiates the formation of the inflammasome polymeric complex composed of NLRP3, CASP1 and PYCARD/ASC. Recruitment of pro-caspase-1 (proCASP1) to the NLRP3 inflammasome promotes caspase-1 (CASP1) activation, which subsequently cleaves and activates inflammatory cytokines IL1B and IL18 and gasdermin-D (GSDMD), promoting cytokine secretion and pyroptosis. Activation of NLRP3 inflammasome is also required for HMGB1 secretion; stimulating inflammatory responses. Under resting conditions, ADP-bound NLRP3 is autoinhibited. NLRP3 activation stimuli include extracellular ATP, nigericin, reactive oxygen species, crystals of monosodium urate or cholesterol, amyloid-beta fibers, environmental or industrial particles and nanoparticles, such as asbestos, silica, aluminum salts, cytosolic dsRNA, etc. Almost all stimuli trigger intracellular K(+) efflux. These stimuli lead to membrane perturbation and activation of NLRP3. Upon activation, NLRP3 is transported to microtubule organizing center (MTOC), where it is unlocked by NEK7, leading to its relocalization to dispersed trans-Golgi network (dTGN) vesicle membranes and formation of an active inflammasome complex. Associates with dTGN vesicle membranes by binding to phosphatidylinositol 4-phosphate (PtdIns4P). Shows ATPase activity.Independently of inflammasome activation, regulates the differentiation of T helper 2 (Th2) cells and has a role in Th2 cell-dependent asthma and tumor growth. During Th2 differentiation, required for optimal IRF4 binding to IL4 promoter and for IRF4-dependent IL4 transcription. Binds to the consensus DNA sequence 5'-GRRGGNRGAG-3'. May also participate in the transcription of IL5, IL13, GATA3, CCR3, CCR4 and MAF.",The mutation in ASC leads to functional changes in the protein.,Complete loss of PYCARD/ASC filament nucleation. The mutation in ASC leads to functional changes in the protein.
204,204,204,15108,O95716-T86A,MASAGDTQAGPRDAADQNFDYMFKLLLIGNSSVGKTSFLFRYADDSFTPAFVSTVGIDFKVKTVYRHDKRIKLQIWDTAGQERYRAITTAYYRGAMGFLLMYDIANQESFAAVQDWATQIKTYSWDNAQVILVGNKCDLEDERVVPAEDGRRLADDLGFEFFEASAKENINVKQVFERLVDVICEKMNESLEPSSSSGSNGKGPAVGDAPAPQPSSCSC,Loss of phosphorylation. Reduced binding of CHM and CHML binding.,,MASAGDTQAGPRDAADQNFDYMFKLLLIGNSSVGKTSFLFRYADDSFTPAFVSTVGIDFKVKTVYRHDKRIKLQIWDTAGQERYRTITTAYYRGAMGFLLMYDIANQESFAAVQDWATQIKTYSWDNAQVILVGNKCDLEDERVVPAEDGRRLADDLGFEFFEASAKENINVKQVFERLVDVICEKMNESLEPSSSSGSNGKGPAVGDAPAPQPSSCSC,Ras-related protein Rab-3D,Protein transport. Probably involved in regulated exocytosis.,,Loss of phosphorylation. Reduced binding of CHM and CHML binding.
206,206,206,15195,P32004-T38M,MVVALRYVWPLLLCSPCLLIQIPEEYEGHHVMEPPVIMEQSPRRLVVFPTDDISLKCEASGKPEVQFRWTRDGVHFKPKEELGVTVYQSPHSGSFTITGNNSNFAQRFQGIYRCFASNKLGTAMSHEIRLMAEGAPKWPKETVKPVEVEEGESVVLPCNPPPSAEPLRIYWMNSKILHIKQDERVTMGQNGNLYFANVLTSDNHSDYICHAHFPGTRTIIQKEPIDLRVKATNSMIDRKPRLLFPTNSSSHLVALQGQPLVLECIAEGFPTPTIKWLRPSGPMPADRVTYQNHNKTLQLLKVGEEDDGEYRCLAENSLGSARHAYYVTVEAAPYWLHKPQSHLYGPGETARLDCQVQGRPQPEVTWRINGIPVEELAKDQKYRIQRGALILSNVQPSDTMVTQCEARNRHGLLLANAYIYVVQLPAKILTADNQTYMAVQGSTAYLLCKAFGAPVPSVQWLDEDGTTVLQDERFFPYANGTLGIRDLQANDTGRYFCLAANDQNNVTIMANLKVKDATQITQGPRSTIEKKGSRVTFTCQASFDPSLQPSITWRGDGRDLQELGDSDKYFIEDGRLVIHSLDYSDQGNYSCVASTELDVVESRAQLLVVGSPGPVPRLVLSDLHLLTQSQVRVSWSPAEDHNAPIEKYDIEFEDKEMAPEKWYSLGKVPGNQTSTTLKLSPYVHYTFRVTAINKYGPGEPSPVSETVVTPEAAPEKNPVDVKGEGNETTNMVITWKPLRWMDWNAPQVQYRVQWRPQGTRGPWQEQIVSDPFLVVSNTSTFVPYEIKVQAVNSQGKGPEPQVTIGYSGEDYPQAIPELEGIEILNSSAVLVKWRPVDLAQVKGHLRGYNVTYWREGSQRKHSKRHIHKDHVVVPANTTSVILSGLRPYSSYHLEVQAFNGRGSGPASEFTFSTPEGVPGHPEALHLECQSNTSLLLRWQPPLSHNGVLTGYVLSYHPLDEGGKGQLSFNLRDPELRTHNLTDLSPHLRYRFQLQATTKEGPGEAIVREGGTMALSGISDFGNIS,No effect on localization at the cell surface.,,MVVALRYVWPLLLCSPCLLIQIPEEYEGHHVMEPPVITEQSPRRLVVFPTDDISLKCEASGKPEVQFRWTRDGVHFKPKEELGVTVYQSPHSGSFTITGNNSNFAQRFQGIYRCFASNKLGTAMSHEIRLMAEGAPKWPKETVKPVEVEEGESVVLPCNPPPSAEPLRIYWMNSKILHIKQDERVTMGQNGNLYFANVLTSDNHSDYICHAHFPGTRTIIQKEPIDLRVKATNSMIDRKPRLLFPTNSSSHLVALQGQPLVLECIAEGFPTPTIKWLRPSGPMPADRVTYQNHNKTLQLLKVGEEDDGEYRCLAENSLGSARHAYYVTVEAAPYWLHKPQSHLYGPGETARLDCQVQGRPQPEVTWRINGIPVEELAKDQKYRIQRGALILSNVQPSDTMVTQCEARNRHGLLLANAYIYVVQLPAKILTADNQTYMAVQGSTAYLLCKAFGAPVPSVQWLDEDGTTVLQDERFFPYANGTLGIRDLQANDTGRYFCLAANDQNNVTIMANLKVKDATQITQGPRSTIEKKGSRVTFTCQASFDPSLQPSITWRGDGRDLQELGDSDKYFIEDGRLVIHSLDYSDQGNYSCVASTELDVVESRAQLLVVGSPGPVPRLVLSDLHLLTQSQVRVSWSPAEDHNAPIEKYDIEFEDKEMAPEKWYSLGKVPGNQTSTTLKLSPYVHYTFRVTAINKYGPGEPSPVSETVVTPEAAPEKNPVDVKGEGNETTNMVITWKPLRWMDWNAPQVQYRVQWRPQGTRGPWQEQIVSDPFLVVSNTSTFVPYEIKVQAVNSQGKGPEPQVTIGYSGEDYPQAIPELEGIEILNSSAVLVKWRPVDLAQVKGHLRGYNVTYWREGSQRKHSKRHIHKDHVVVPANTTSVILSGLRPYSSYHLEVQAFNGRGSGPASEFTFSTPEGVPGHPEALHLECQSNTSLLLRWQPPLSHNGVLTGYVLSYHPLDEGGKGQLSFNLRDPELRTHNLTDLSPHLRYRFQLQATTKEGPGEAIVREGGTMALSGISDFGNIS,Neural cell adhesion molecule L1,"Neural cell adhesion molecule involved in the dynamics of cell adhesion and in the generation of transmembrane signals at tyrosine kinase receptors. During brain development, critical in multiple processes, including neuronal migration, axonal growth and fasciculation, and synaptogenesis. In the mature brain, plays a role in the dynamics of neuronal structure and function, including synaptic plasticity.",The variant p. preserves L1CAM-mediated cell-cell aggregation.,No effect on localization at the cell surface. The variant p. preserves L1CAM-mediated cell-cell aggregation.
217,217,217,15867,P33487-L60V,MIVLSVGSASSSPIVVVFSVALLLFYFSETSLGAPCPINGLPIVRNISDLPQDNYGRPGVSHMTVAGSVLHGMKEVEIWLQTFAPGSETPIHRHSCEEVFVVLKGSGTLYLAETHGNFPGKPIEFPIFANSTIHIPINDAHQVKNTGHEDLQVLVIISRPPIKIFIYEDWFMPHTAARLKFPYYWDEQCIQESQKDEL,Slight reduction of activation by auxin. Slight reduction of activation by auxin; when associated with K-57.,,MIVLSVGSASSSPIVVVFSVALLLFYFSETSLGAPCPINGLPIVRNISDLPQDNYGRPGLSHMTVAGSVLHGMKEVEIWLQTFAPGSETPIHRHSCEEVFVVLKGSGTLYLAETHGNFPGKPIEFPIFANSTIHIPINDAHQVKNTGHEDLQVLVIISRPPIKIFIYEDWFMPHTAARLKFPYYWDEQCIQESQKDEL,Auxin-binding protein 1,"Auxin receptor that controls cell elongation and cell division. Involved in embryonic morphogenesis. Acts on the cell cycle, endocycle, cell plate formation, and cell expansion and contributes to the control of auxin-related gene expression. Controls root meristem size and mediates auxin responsiveness. Involved in activation of ROP GTPases in response to auxin and regulation of clathrin-mediated endocytosis in roots. Acts as a positive factor in clathrin recruitment to the plasma membrane, thereby promoting endocytosis. Upon auxin binding, restricts the internalization of PIN proteins by inhibiting clathrin-mediated endocytosis. Involved in the regulation of polar auxin transport. Behaves as a negative regulator of the SCF(TIR1/AFB) signaling pathway, protecting AUX/IAA repressors from degradation. Regulates the expression of cell wall remodeling genes via an SCF(TIR1/AFB)-dependent pathway. Involved in the modulation of hemicellulose xyloglucan structure. Required for rapid auxin-mediated re-orientation of microtubules to regulate cell elongation in roots and dark-grown hypocotyls as well as asymmetric growth during gravitropic responses. Involved in the shade avoidance response. Forms with TMK1 a cell surface auxin perception complex that activates ROP signaling pathways. ABP1 sensing of auxin is important for the ABP1-TMK1 complex formation. Interacts functionally with phytochrome to regulate growth.",,Slight reduction of activation by auxin. Slight reduction of activation by auxin; when associated with K-57.
249,249,249,17740,Q8NBS3-R739Q,MAAATRRVFHLQPCENSPTMSQNGYFEDSSYYKCDTDDTFEAREEILGDEAFDTANSSIVSGESIRFFVNVNLEMQATNTENEATSGGCVLLHTSRKYLKLKNFKEEIRAHRDLDGFLAQASIVLNETATSLDNVLRTMLRRFARDPDNNEPNCNLDLLMAMLFTDAGAPMRGKVHLLSDTIQGVTATVTGVRYQQSWLCIICTMKALQKRHVCISRLVRPQNWGENSCEVRFVILVLAPPKMKSTKTAMEVARTFATMFSDIAFRQKLLETRTEEEFKEALVHQRQLLTMVSHGPVAPRTKERSTVSLPAHRHPEPPKCKDFVPFGKGIREDIARRFPLYPLDFTDGIIGKNKAVGKYITTTLFLYFACLLPTIAFGSLNDENTDGAIDVQKTIAGQSIGGLLYALFSGQPLVILLTTAPLALYIQVIRVICDDYDLDFNSFYAWTGLWNSFFLALYAFFNLSLVMSLFKRSTEEIIALFISITFVLDAVKGTVKIFWKYYYGHYLDDYHTKRTSSLVSLSGLGASLNASLHTALNASFLASPTELPSATHSGQATAVLSLLIMLGTLWLGYTLYQFKKSPYLHPCVREILSDCALPIAVLAFSLISSHGFREIEMSKFRYNPSESPFAMAQIQSLSLRAVSGAMGLGFLLSMLFFIEQNLVAALVNAPENRLVKGTAYHWDLLLLAIINTGLSLFGLPWIHAAYPHSPLHVRALALVEERVENGHIYDTIVNVKETQLTSLGASVLVGLSLLLLPVPLQWIPKPVLYGLFLYIALTSLDGNQLVQRVALLLKEQTAYPPTHYIRRVPQRKIHYFTGLQVLQLLLLCAFGMSSLPYMKMIFPLIMIAMIPIRYILLPRIIEAKYLDVMDAEHRP,In CHED; affects protein processing and transport to the cell surface; the mutant protein is retained intracellularly; coexpression with wild-type protein partially rescues the cell surface trafficking of CHED mutant.,,MAAATRRVFHLQPCENSPTMSQNGYFEDSSYYKCDTDDTFEAREEILGDEAFDTANSSIVSGESIRFFVNVNLEMQATNTENEATSGGCVLLHTSRKYLKLKNFKEEIRAHRDLDGFLAQASIVLNETATSLDNVLRTMLRRFARDPDNNEPNCNLDLLMAMLFTDAGAPMRGKVHLLSDTIQGVTATVTGVRYQQSWLCIICTMKALQKRHVCISRLVRPQNWGENSCEVRFVILVLAPPKMKSTKTAMEVARTFATMFSDIAFRQKLLETRTEEEFKEALVHQRQLLTMVSHGPVAPRTKERSTVSLPAHRHPEPPKCKDFVPFGKGIREDIARRFPLYPLDFTDGIIGKNKAVGKYITTTLFLYFACLLPTIAFGSLNDENTDGAIDVQKTIAGQSIGGLLYALFSGQPLVILLTTAPLALYIQVIRVICDDYDLDFNSFYAWTGLWNSFFLALYAFFNLSLVMSLFKRSTEEIIALFISITFVLDAVKGTVKIFWKYYYGHYLDDYHTKRTSSLVSLSGLGASLNASLHTALNASFLASPTELPSATHSGQATAVLSLLIMLGTLWLGYTLYQFKKSPYLHPCVREILSDCALPIAVLAFSLISSHGFREIEMSKFRYNPSESPFAMAQIQSLSLRAVSGAMGLGFLLSMLFFIEQNLVAALVNAPENRLVKGTAYHWDLLLLAIINTGLSLFGLPWIHAAYPHSPLHVRALALVEERVENGHIYDTIVNVKETRLTSLGASVLVGLSLLLLPVPLQWIPKPVLYGLFLYIALTSLDGNQLVQRVALLLKEQTAYPPTHYIRRVPQRKIHYFTGLQVLQLLLLCAFGMSSLPYMKMIFPLIMIAMIPIRYILLPRIIEAKYLDVMDAEHRP,Solute carrier family 4 member 11,"Multifunctional transporter with an impact in cell morphology and differentiation. In the presence of borate B(OH)4(-), acts as a voltage-dependent electrogenic Na(+)-coupled B(OH)4(-) cotransporter controlling boron homeostasis. At early stages of stem cell differentiation, participates in synergy with ITGA5-ITGB1 and ITGAV-ITGB3 integrins and BMPR1A to promote cell adhesion and contractility that drives differentiation toward osteogenic commitment while inhibiting adipogenesis. In the absence of B(OH)4(-), acts as a Na(+)-coupled OH(-) or H(+) permeable channel with implications in cellular redox balance. Regulates the oxidative stress response in corneal endothelium by enhancing antioxidant defenses and protecting cells from reactive oxygen species. In response to hypo-osmotic challenge, also acts as water permeable channel at the basolateral cell membrane of corneal endothelial cells and facilitates transendothelial fluid reabsorption in the aqueous humor. In the presence of ammonia, acts as an electrogenic NH3/H(+) cotransporter and may play a role in ammonia transport and reabsorption in renal Henle's loop epithelium.",The mutation in the SLC4A11 gene causes functional changes in the sodium bicarbonate transporter-like solute carrier family 4 member 11 protein. The functional changes caused by the mutation in the SLC4A11 protein are not mentioned in the document.,In CHED; affects protein processing and transport to the cell surface; the mutant protein is retained intracellularly; coexpression with wild-type protein partially rescues the cell surface trafficking of CHED mutant. The mutation in the SLC4A11 gene causes functional changes in the sodium bicarbonate transporter-like solute carrier family 4 member 11 protein. The functional changes caused by the mutation in the SLC4A11 protein are not mentioned in the document.
271,271,271,19771,Q9LRB7-W165A,MVRGVEQGGPAMDESSSSSSPSPVSAPAGQAAMTAGGIATVAAVLIVFAALTLAFVLLQCYCDERRRAVTTTSTSGRGRRPRPRRRSGSGGDGGTGGGVDPEVLRSLPVTVYSRSTAAAAAKEEEEEDDDGVECAVCLAELEDGEEARFLPRCGHGFHAECVDMALGSHSTCPLCRLTVVVPPPPLPPVPPEPPASYTVSLPASVLLGLSDHGAGAVTMTAEGRSTLVIEIPESAASTTPRDAAARSSPSLARLRSLRRLWSFGRQGAAGSTSSCSCATGGDNDDGDVEHGVSVTVAIRAVEAATPARPPEAEAGARTAAAHVRN,Loss of E3 ubiquitin ligase activity. Rootless phenotype.,,MVRGVEQGGPAMDESSSSSSPSPVSAPAGQAAMTAGGIATVAAVLIVFAALTLAFVLLQCYCDERRRAVTTTSTSGRGRRPRPRRRSGSGGDGGTGGGVDPEVLRSLPVTVYSRSTAAAAAKEEEEEDDDGVECAVCLAELEDGEEARFLPRCGHGFHAECVDMWLGSHSTCPLCRLTVVVPPPPLPPVPPEPPASYTVSLPASVLLGLSDHGAGAVTMTAEGRSTLVIEIPESAASTTPRDAAARSSPSLARLRSLRRLWSFGRQGAAGSTSSCSCATGGDNDDGDVEHGVSVTVAIRAVEAATPARPPEAEAGARTAAAHVRN,E3 ubiquitin-protein ligase EL5,"Functions as a E3 ubiquitin-protein ligase in cooperation with the E2 ubiquitin conjugating enzymes UBC5A and UBC5B. Involved in root development. Required for the maintenance of cell viability after the initiation of root primordial formation. May mediate the degradation of cytotoxic proteins produced in root cells after the actions of auxin, cytokinin and jasmonic acid. Mediates 'Lys-48'-linked polyubiquitination of MBP in vitro.","The E3 activity of EL5 is shown to be dependent on a W located at the center of the groove. Plants expressing EL5W165A, which encode an inactive E3, showed a rootless phenotype accompanied by cell death in root primordia.","Loss of E3 ubiquitin ligase activity. Rootless phenotype. The E3 activity of EL5 is shown to be dependent on a W located at the center of the groove. Plants expressing EL5W165A, which encode an inactive E3, showed a rootless phenotype accompanied by cell death in root primordia."
289,289,289,20633,B5A7L9-Y211A,MRVYITNINGQSIQSTAQLCQNTVTDVAVSLGYRELGIYCYQIHTDSESELSKRLDGIVAGLRHGDVVIFQTPTWNTTEFDEKLMNKLKLYDIKIVLFIHDVVPLMFSGNFYLMDRTIAYYNKADVVVAPSQKMIDKLRDFGMNVSKTVVQGMWDHPTQAPMFPAGLKREIHFPGNPERFSFVKEWKYDIPLKVYTWQNVELPQNVHKINARPDEQLLMEMSQGGFGLVWMDDKDKEYQSLYCSYKLGSFLAAGIPVIVQEGIANQELIENNGLGWIVKDVEEAIMKVKNVNEDEYIELVKNVRSFNPILRKGFFTRRLLTESVFQAICD,"25% glycosyltransferase activity, partially restores Fap1 glycosylation in vivo.",,MRVYITNINGQSIQSTAQLCQNTVTDVAVSLGYRELGIYCYQIHTDSESELSKRLDGIVAGLRHGDVVIFQTPTWNTTEFDEKLMNKLKLYDIKIVLFIHDVVPLMFSGNFYLMDRTIAYYNKADVVVAPSQKMIDKLRDFGMNVSKTVVQGMWDHPTQAPMFPAGLKREIHFPGNPERFSFVKEWKYDIPLKVYTWQNVELPQNVHKINYRPDEQLLMEMSQGGFGLVWMDDKDKEYQSLYCSYKLGSFLAAGIPVIVQEGIANQELIENNGLGWIVKDVEEAIMKVKNVNEDEYIELVKNVRSFNPILRKGFFTRRLLTESVFQAICD,Glucosyltransferase 3,Required for polymorphic O-glycosylation of the serine-rich repeat protein Fap1. Catalyzes the second step in glycosylation of the serine-rich repeat protein in this bacteria. Transfers glucose from UDP-glucose to the terminal GlcNAc moiety of 3-O-(N-acetyl-alpha-D-glucosaminyl)-L-seryl-[protein] which results from the first glycosylation step of Fap1; does not use other sugar nucleotides as substrates.,,"25% glycosyltransferase activity, partially restores Fap1 glycosylation in vivo."
298,298,298,21364,Q8ZND6-R252H,MSRIIMLIPTGTSVGLTSVSLGVIRAMERKGVRLSVFKPIAQPRAGGDAPDQTTTIVRANSTLPAAEPLKMSHVESLLSSNQKDVLMEEIIANYHANTKDAEVVLVEGLVPTRKHQFAQSLNYEIAKTLNAEIVFVMSQGTDTPEQLNERIELTRSSFGGAKNTNITGVIINKLNAPVDEQGRTRPDLSEIFDDSSKAQVIKIDPAKLQESSPLPVLGAVPWSFDLIATRAIDMARHLNATIINEGDIKTRHVKSVTFCARSIPHMLEHFRAGSLLVTSADRPDVLVAACLAAMNGVEIGALLLTGGYEMDARISKLCERAFATGLPVFMVNTNTWQTSLSLQSFNLEVPVDDHERIEKVQEYVANYVNAEWIESLTATSERSRRLSPPAFRYQLTELARKAGKRVVLPEGDEPRTVKAAAICAERGIATCVLLGNPDEINRVAASQGVELGAGIEIVDPEVVRESYVARLVELRKSKGMTEPVAREQLEDNVVLGTLMLEQDEVDGLVSGAVHTTANTIRPPLQLIKTAPGSSLVSSVFFMLLPEQVYVYGDCAINPDPTAEQLAEIAIQSADSAIAFGIEPRVAMLSYSTGTSGAGSDVEKVREATRLAQEKRPDLMIDGPLQYDAAVMADVAKSKAPNSPVAGRATVFIFPDLNTGNTTYKAVQRSADLISIGPMLQGMRKPVNDLSRGALVDDIVYTIALTAIQASQQQQ,Increases speed of forward and back reactions by 2-3 fold. Not inhibited by NADH.,,MSRIIMLIPTGTSVGLTSVSLGVIRAMERKGVRLSVFKPIAQPRAGGDAPDQTTTIVRANSTLPAAEPLKMSHVESLLSSNQKDVLMEEIIANYHANTKDAEVVLVEGLVPTRKHQFAQSLNYEIAKTLNAEIVFVMSQGTDTPEQLNERIELTRSSFGGAKNTNITGVIINKLNAPVDEQGRTRPDLSEIFDDSSKAQVIKIDPAKLQESSPLPVLGAVPWSFDLIATRAIDMARHLNATIINEGDIKTRRVKSVTFCARSIPHMLEHFRAGSLLVTSADRPDVLVAACLAAMNGVEIGALLLTGGYEMDARISKLCERAFATGLPVFMVNTNTWQTSLSLQSFNLEVPVDDHERIEKVQEYVANYVNAEWIESLTATSERSRRLSPPAFRYQLTELARKAGKRVVLPEGDEPRTVKAAAICAERGIATCVLLGNPDEINRVAASQGVELGAGIEIVDPEVVRESYVARLVELRKSKGMTEPVAREQLEDNVVLGTLMLEQDEVDGLVSGAVHTTANTIRPPLQLIKTAPGSSLVSSVFFMLLPEQVYVYGDCAINPDPTAEQLAEIAIQSADSAIAFGIEPRVAMLSYSTGTSGAGSDVEKVREATRLAQEKRPDLMIDGPLQYDAAVMADVAKSKAPNSPVAGRATVFIFPDLNTGNTTYKAVQRSADLISIGPMLQGMRKPVNDLSRGALVDDIVYTIALTAIQASQQQQ,Phosphate acetyltransferase,"Involved in acetate metabolism. Catalyzes the reversible interconversion of acetyl-CoA and acetyl phosphate. The direction of the overall reaction changes depending on growth conditions. Required for acetate recapture but not for acetate excretion when this organism is grown on ethanolamine (EA); is unable to complement an eutD deletion during growth on EA. Works with proprionate kinase PduW to capture exogenous propionate and regenerate propionyl-CoA during degradation of propionate and 1,2-propanediol (1,2-PD).","NADH did not inhibit variant protein Pta(). Pyruvate stimulated Pta(WT) activity, and its effect was potentiated in the variants, being most pronounced on Pta().","Increases speed of forward and back reactions by 2-3 fold. Not inhibited by NADH. NADH did not inhibit variant protein Pta(). Pyruvate stimulated Pta(WT) activity, and its effect was potentiated in the variants, being most pronounced on Pta()."
304,304,304,21921,O75695-R32A,MGCFFSKRRKADKESRPENEEERPKQYSWDQAEKVDPKDYMFSGLKDETVGRLPGTVAGQQFLIQDCENCNIYIFDHSATVTIDDCTNCIIFLGPVKGSVFFRNCRDCKCTLACQQFRVRDCRKLEVFLCCATQPIIESSSNIKFGCFQWYYPELAFQFKDAGLSIFNNTWSNIHDFTPVSGELNWSLLPEDAVVQDYVPIPTTEELKAVRVSTEANRSIVPISRGQRQKSSDESCLVVLFAGDYTIANARKLIDEMVGKGFFLVQTKEVSMKAEDAQRVFREKAPDFLPLLNKGPVIALEFNGDGAVEVCQLIVNEIFNGTKMFVSESKETASGDVDSFYNFADIQMGI,Does not reduce affinity for mouse ARL3; when associated with A-31.,,MGCFFSKRRKADKESRPENEEERPKQYSWDQREKVDPKDYMFSGLKDETVGRLPGTVAGQQFLIQDCENCNIYIFDHSATVTIDDCTNCIIFLGPVKGSVFFRNCRDCKCTLACQQFRVRDCRKLEVFLCCATQPIIESSSNIKFGCFQWYYPELAFQFKDAGLSIFNNTWSNIHDFTPVSGELNWSLLPEDAVVQDYVPIPTTEELKAVRVSTEANRSIVPISRGQRQKSSDESCLVVLFAGDYTIANARKLIDEMVGKGFFLVQTKEVSMKAEDAQRVFREKAPDFLPLLNKGPVIALEFNGDGAVEVCQLIVNEIFNGTKMFVSESKETASGDVDSFYNFADIQMGI,Protein XRP2,"Acts as a GTPase-activating protein (GAP) involved in trafficking between the Golgi and the ciliary membrane. Involved in localization of proteins, such as NPHP3, to the cilium membrane by inducing hydrolysis of GTP ARL3, leading to the release of UNC119 (or UNC119B). Acts as a GTPase-activating protein (GAP) for tubulin in concert with tubulin-specific chaperone C, but does not enhance tubulin heterodimerization. Acts as guanine nucleotide dissociation inhibitor towards ADP-ribosylation factor-like proteins.",The mutation in the Arl3 gene has been shown to have an effect on the Arl3-GppNHp-RP2 complex structure.,Does not reduce affinity for mouse ARL3; when associated with A-31. The mutation in the Arl3 gene has been shown to have an effect on the Arl3-GppNHp-RP2 complex structure.
305,305,305,22034,Q96BN8-D54A,MSRGTMPQPEAWPGASCAETPAREAAATARDGGKAAASGQPRPEMQCPAEHEEAMYRAADEIEKEKELLIHERGASEPRLSVAPEMDIMDYCKKEWRGNTQKATCMKMGYEEVSQKFTSIRRVRGDNYCALRATLFQAMSQAVGLPPWLQDPELMLLPEKLISKYNWIKQWKLGLKFDGKNEDLVDKIKESLTLLRKKWAGLAEMRTAEARQIACDELFTNEAEEYSLYEAVKFLMLNRAIELYNDKEKGKEVPFFSVLLFARDTSNDPGQLLRNHLNQVGHTGGLEQVEMFLLAYAVRHTIQVYRLSKYNTEEFITVYPTDPPKDWPVVTLIAEDDRHYNIPVRVCEETSL,Reduced interaction with RNF31.,,MSRGTMPQPEAWPGASCAETPAREAAATARDGGKAAASGQPRPEMQCPAEHEEDMYRAADEIEKEKELLIHERGASEPRLSVAPEMDIMDYCKKEWRGNTQKATCMKMGYEEVSQKFTSIRRVRGDNYCALRATLFQAMSQAVGLPPWLQDPELMLLPEKLISKYNWIKQWKLGLKFDGKNEDLVDKIKESLTLLRKKWAGLAEMRTAEARQIACDELFTNEAEEYSLYEAVKFLMLNRAIELYNDKEKGKEVPFFSVLLFARDTSNDPGQLLRNHLNQVGHTGGLEQVEMFLLAYAVRHTIQVYRLSKYNTEEFITVYPTDPPKDWPVVTLIAEDDRHYNIPVRVCEETSL,Ubiquitin thioesterase otulin,"Deubiquitinase that specifically removes linear ('Met-1'-linked) polyubiquitin chains to substrates and acts as a regulator of angiogenesis and innate immune response. Required during angiogenesis, craniofacial and neuronal development by regulating the canonical Wnt signaling together with the LUBAC complex. Acts as a negative regulator of NF-kappa-B by regulating the activity of the LUBAC complex. OTULIN function is mainly restricted to homeostasis of the LUBAC complex: acts by removing 'Met-1'-linked autoubiquitination of the LUBAC complex, thereby preventing inactivation of the LUBAC complex. Acts as a key negative regulator of inflammation by restricting spontaneous inflammation and maintaining immune homeostasis. In myeloid cell, required to prevent unwarranted secretion of cytokines leading to inflammation and autoimmunity by restricting linear polyubiquitin formation. Plays a role in innate immune response by restricting linear polyubiquitin formation on LUBAC complex in response to NOD2 stimulation, probably to limit NOD2-dependent pro-inflammatory signaling.",,Reduced interaction with RNF31.
313,313,313,22461,P56524-N353A,MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPAITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIH,No effect on interaction with ANKRA2.,,MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIH,Histone deacetylase 4,"Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Involved in muscle maturation via its interaction with the myocyte enhancer factors such as MEF2A, MEF2C and MEF2D. Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer. Deacetylates HSPA1A and HSPA1B at 'Lys-77' leading to their preferential binding to co-chaperone STUB1.",,No effect on interaction with ANKRA2.
315,315,315,22479,Q8IY37-R487H,MGKLRRRYNIKGRQQAGPGPSKGPPEPPPVQLELEDKDTLKGVDASNALVLPGKKKKKTKAPPLSKKEKKPLTKKEKKVLQKILEQKEKKSQRAEMLQKLSEVQASEAEMRLFYTTSKLGTGNRMYHTKEKADEVVAPGQEKISSLSGAHRKRRRWPSAEEEEEEEEESESELEEESELDEDPAAEPAEAGVGTTVAPLPPAPAPSSQPVPAGMTVPPPPAAAPPLPRALAKPAVFIPVNRSPEMQEERLKLPILSEEQVIMEAVAEHPIVIVCGETGSGKTTQVPQFLYEAGFSSEDSIIGVTEPRRVAAVAMSQRVAKEMNLSQRVVSYQIRYEGNVTEETRIKFMTDGVLLKEIQKDFLLLRYKVVIIDEAHERSVYTDILIGLLSRIVTLRAKRNLPLKLLIMSATLRVEDFTQNPRLFAKPPPVIKVESRQFPVTVHFNKRTPLEDYSGECFRKVCKIHRMLPAGGILVFLTGQAEVHALCHRLRKAFPPSRARPQEKDDDQKDSVEEMRKFKKSRARAKKARAEVLPQINLDHYSVLPAGEGDEDREAEVDEEEGALDSDLDLDLGDGGQDGGEQPDASLPLHVLPLYSLLAPEKQAQVFKPPPEGTRLCVVATNVAETSLTIPGIKYVVDCGKVKKRYYDRVTGVSSFRVTWVSQASADQRAGRAGRTEPGHCYRLYSSAVFGDFEQFPPPEITRRPVEDLILQMKALNVEKVINFPFPTPPSVEALLAAEELLIALGALQPPQKAERVKQLQENRLSCPITALGRTMATFPVAPRYAKMLALSRQHGCLPYAITIVASMTVRELFEELDRPAASDEELTRLKSKRARVAQMKRTWAGQGASLKLGDLMVLLGAVGACEYASCTPQFCEANGLRYKAMMEIRRLRGQLTTAVNAVCPEAELFVDPKMQPPTESQVTYLRQIVTAGLGDHLARRVQSEEMLEDKWRNAYKTPLLDDPVFIHPSSVLFKELPEFVVYQEIVETTKMYMKGVSSVEVQWIPALLPSYCQFDKPLEEPAPT,In NEDBAVC; unknown pathological significance.,,MGKLRRRYNIKGRQQAGPGPSKGPPEPPPVQLELEDKDTLKGVDASNALVLPGKKKKKTKAPPLSKKEKKPLTKKEKKVLQKILEQKEKKSQRAEMLQKLSEVQASEAEMRLFYTTSKLGTGNRMYHTKEKADEVVAPGQEKISSLSGAHRKRRRWPSAEEEEEEEEESESELEEESELDEDPAAEPAEAGVGTTVAPLPPAPAPSSQPVPAGMTVPPPPAAAPPLPRALAKPAVFIPVNRSPEMQEERLKLPILSEEQVIMEAVAEHPIVIVCGETGSGKTTQVPQFLYEAGFSSEDSIIGVTEPRRVAAVAMSQRVAKEMNLSQRVVSYQIRYEGNVTEETRIKFMTDGVLLKEIQKDFLLLRYKVVIIDEAHERSVYTDILIGLLSRIVTLRAKRNLPLKLLIMSATLRVEDFTQNPRLFAKPPPVIKVESRQFPVTVHFNKRTPLEDYSGECFRKVCKIHRMLPAGGILVFLTGQAEVHALCRRLRKAFPPSRARPQEKDDDQKDSVEEMRKFKKSRARAKKARAEVLPQINLDHYSVLPAGEGDEDREAEVDEEEGALDSDLDLDLGDGGQDGGEQPDASLPLHVLPLYSLLAPEKQAQVFKPPPEGTRLCVVATNVAETSLTIPGIKYVVDCGKVKKRYYDRVTGVSSFRVTWVSQASADQRAGRAGRTEPGHCYRLYSSAVFGDFEQFPPPEITRRPVEDLILQMKALNVEKVINFPFPTPPSVEALLAAEELLIALGALQPPQKAERVKQLQENRLSCPITALGRTMATFPVAPRYAKMLALSRQHGCLPYAITIVASMTVRELFEELDRPAASDEELTRLKSKRARVAQMKRTWAGQGASLKLGDLMVLLGAVGACEYASCTPQFCEANGLRYKAMMEIRRLRGQLTTAVNAVCPEAELFVDPKMQPPTESQVTYLRQIVTAGLGDHLARRVQSEEMLEDKWRNAYKTPLLDDPVFIHPSSVLFKELPEFVVYQEIVETTKMYMKGVSSVEVQWIPALLPSYCQFDKPLEEPAPT,Probable ATP-dependent RNA helicase DHX37,"ATP-binding RNA helicase that plays a role in maturation of the small ribosomal subunit in ribosome biogenesis. Required for the release of the U3 snoRNP from pre-ribosomal particles. Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome. Plays a role in early testis development. Probably also plays a role in brain development.",,In NEDBAVC; unknown pathological significance.
324,324,324,22816,Q9GYI0-S437A,MDGNDINIQKNEFSRDQSALLMMDQHSDHKNHESAIGEPGMSYTASQPALSSTEHQTPLVSEASVAAPQNHLNGNSHESVSEMDRNSVDFAIESVLMKARAYNKMGAPKDPRRKQHNPKSEPKIEPHVTDSSDNQAAMSNKMEAEAPKMESNQNYVSNGSEPPFRFVSISNFDEMKTKKKEVQEELKLEVDSDSEEDDVPEQKTPKESDRCGGCGKFTHEDDLIALEEEKKKEKEKPLMSKKKSHHHKKNDFQWIGCDSCQTWYHFLCSGLEQFEYYLYEKFFCPKCVPHTGHSIRYKVVAPHRYRWYSPNEKHLGIEVGSKTWIEDFITRENTVPSPTDDEVCIVEDGYEFRREFEKLGGADNWGKVFMVKDMDGLNMTMPKPGFDLEDVVKIMGSDYEVDTIDVYNQSTYSMKLDTFRKLFRDTKNRPLLYNFLALEFSDNNEMKEIAKPPRFVQEISMVNRLWPDVSGAEYIKLLQREEYLPEDQRPKVEQFCLAGMAGSYTDFHVDFGGSSVYYHILKGEKIFYIAAPTEQNFAAYQAHETSPDTTTWFGDIANGAVKRVVIKEGQTLLIPAGWIHAVLTPVDSLVFGGNFLHLGNLEMQMRVYHLENAIRKEIRSEEKFYFPNFELLHWMYMRNVLLEKITEANQEGSDMREQEKNIWTASQIMKAEMERWMDRELRLGPEKNAILPTDDKNKIMISVRKQIEIQTKIQNAKNKPMGLKQKRKSRESAERDDEDYCPSSSTAYKKKYTKKAKKDNDDAPKVKKAKKEEVPEEKVPVPEAAGPSEVTAPLTIKIGMGPTEDQKGVVQIFNNQCTSSGRKVKLNQNVADYCGSHLEARVEEIPEKATKSFRELDNELERCEAVHSGEKIKKVKEPKPPKQPKEKKEKPPPKKKEMSSRDRLMKKLKM,Abolishes histone methyltransferase activity.,,MDGNDINIQKNEFSRDQSALLMMDQHSDHKNHESAIGEPGMSYTASQPALSSTEHQTPLVSEASVAAPQNHLNGNSHESVSEMDRNSVDFAIESVLMKARAYNKMGAPKDPRRKQHNPKSEPKIEPHVTDSSDNQAAMSNKMEAEAPKMESNQNYVSNGSEPPFRFVSISNFDEMKTKKKEVQEELKLEVDSDSEEDDVPEQKTPKESDRCGGCGKFTHEDDLIALEEEKKKEKEKPLMSKKKSHHHKKNDFQWIGCDSCQTWYHFLCSGLEQFEYYLYEKFFCPKCVPHTGHSIRYKVVAPHRYRWYSPNEKHLGIEVGSKTWIEDFITRENTVPSPTDDEVCIVEDGYEFRREFEKLGGADNWGKVFMVKDMDGLNMTMPKPGFDLEDVVKIMGSDYEVDTIDVYNQSTYSMKLDTFRKLFRDTKNRPLLYNFLSLEFSDNNEMKEIAKPPRFVQEISMVNRLWPDVSGAEYIKLLQREEYLPEDQRPKVEQFCLAGMAGSYTDFHVDFGGSSVYYHILKGEKIFYIAAPTEQNFAAYQAHETSPDTTTWFGDIANGAVKRVVIKEGQTLLIPAGWIHAVLTPVDSLVFGGNFLHLGNLEMQMRVYHLENAIRKEIRSEEKFYFPNFELLHWMYMRNVLLEKITEANQEGSDMREQEKNIWTASQIMKAEMERWMDRELRLGPEKNAILPTDDKNKIMISVRKQIEIQTKIQNAKNKPMGLKQKRKSRESAERDDEDYCPSSSTAYKKKYTKKAKKDNDDAPKVKKAKKEEVPEEKVPVPEAAGPSEVTAPLTIKIGMGPTEDQKGVVQIFNNQCTSSGRKVKLNQNVADYCGSHLEARVEEIPEKATKSFRELDNELERCEAVHSGEKIKKVKEPKPPKQPKEKKEKPPPKKKEMSSRDRLMKKLKM,Lysine-specific demethylase 7 homolog,"Histone demethylase required for nervous system development. Specifically demethylates dimethylated 'Lys-9', 'Lys-23' and 'Lys-27' (H3K9me2, H3K23me2 and H3K27me2, respectively) of histone H3, thereby playing a central role in histone code. Promotes mitochondrial stress-induced longevity.",,Abolishes histone methyltransferase activity.
339,339,339,23682,P35498-F945L,MEQTVLVPPGPDSFNFFTRESLAAIERRIAEEKAKNPKPDKKDDDENGPKPNSDLEAGKNLPFIYGDIPPEMVSEPLEDLDPYYINKKTFIVLNKGKAIFRFSATSALYILTPFNPLRKIAIKILVHSLFSMLIMCTILTNCVFMTMSNPPDWTKNVEYTFTGIYTFESLIKIIARGFCLEDFTFLRDPWNWLDFTVITFAYVTEFVDLGNVSALRTFRVLRALKTISVIPGLKTIVGALIQSVKKLSDVMILTVFCLSVFALIGLQLFMGNLRNKCIQWPPTNASLEEHSIEKNITVNYNGTLINETVFEFDWKSYIQDSRYHYFLEGFLDALLCGNSSDAGQCPEGYMCVKAGRNPNYGYTSFDTFSWAFLSLFRLMTQDFWENLYQLTLRAAGKTYMIFFVLVIFLGSFYLINLILAVVAMAYEEQNQATLEEAEQKEAEFQQMIEQLKKQQEAAQQAATATASEHSREPSAAGRLSDSSSEASKLSSKSAKERRNRRKKRKQKEQSGGEEKDEDEFQKSESEDSIRRKGFRFSIEGNRLTYEKRYSSPHQSLLSIRGSLFSPRRNSRTSLFSFRGRAKDVGSENDFADDEHSTFEDNESRRDSLFVPRRHGERRNSNLSQTSRSSRMLAVFPANGKMHSTVDCNGVVSLVGGPSVPTSPVGQLLPEVIIDKPATDDNGTTTETEMRKRRSSSFHVSMDFLEDPSQRQRAMSIASILTNTVEELEESRQKCPPCWYKFSNIFLIWDCSPYWLKVKHVVNLVVMDPFVDLAITICIVLNTLFMAMEHYPMTDHFNNVLTVGNLVFTGIFTAEMFLKIIAMDPYYYFQEGWNIFDGFIVTLSLVELGLANVEGLSVLRSFRLLRVFKLAKSWPTLNMLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKSYKDCVCKIASDCQLPRWHMNDFFHSFLIVLRVLCGEWIETMWDCMEVAGQAMCLTVFMMVMVIGNLVVLNLFLALLLSSFSADNLAATDDDNEMNNLQIAVDRMHKGVA,In DRVT.,,MEQTVLVPPGPDSFNFFTRESLAAIERRIAEEKAKNPKPDKKDDDENGPKPNSDLEAGKNLPFIYGDIPPEMVSEPLEDLDPYYINKKTFIVLNKGKAIFRFSATSALYILTPFNPLRKIAIKILVHSLFSMLIMCTILTNCVFMTMSNPPDWTKNVEYTFTGIYTFESLIKIIARGFCLEDFTFLRDPWNWLDFTVITFAYVTEFVDLGNVSALRTFRVLRALKTISVIPGLKTIVGALIQSVKKLSDVMILTVFCLSVFALIGLQLFMGNLRNKCIQWPPTNASLEEHSIEKNITVNYNGTLINETVFEFDWKSYIQDSRYHYFLEGFLDALLCGNSSDAGQCPEGYMCVKAGRNPNYGYTSFDTFSWAFLSLFRLMTQDFWENLYQLTLRAAGKTYMIFFVLVIFLGSFYLINLILAVVAMAYEEQNQATLEEAEQKEAEFQQMIEQLKKQQEAAQQAATATASEHSREPSAAGRLSDSSSEASKLSSKSAKERRNRRKKRKQKEQSGGEEKDEDEFQKSESEDSIRRKGFRFSIEGNRLTYEKRYSSPHQSLLSIRGSLFSPRRNSRTSLFSFRGRAKDVGSENDFADDEHSTFEDNESRRDSLFVPRRHGERRNSNLSQTSRSSRMLAVFPANGKMHSTVDCNGVVSLVGGPSVPTSPVGQLLPEVIIDKPATDDNGTTTETEMRKRRSSSFHVSMDFLEDPSQRQRAMSIASILTNTVEELEESRQKCPPCWYKFSNIFLIWDCSPYWLKVKHVVNLVVMDPFVDLAITICIVLNTLFMAMEHYPMTDHFNNVLTVGNLVFTGIFTAEMFLKIIAMDPYYYFQEGWNIFDGFIVTLSLVELGLANVEGLSVLRSFRLLRVFKLAKSWPTLNMLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKSYKDCVCKIASDCQLPRWHMNDFFHSFLIVFRVLCGEWIETMWDCMEVAGQAMCLTVFMMVMVIGNLVVLNLFLALLLSSFSADNLAATDDDNEMNNLQIAVDRMHKGVA,Sodium channel protein type 1 subunit alpha,"Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient. Plays a key role in brain, probably by regulating the moment when neurotransmitters are released in neurons. Involved in sensory perception of mechanical pain: activation in somatosensory neurons induces pain without neurogenic inflammation and produces hypersensitivity to mechanical, but not thermal stimuli.","The mutation in the SCN1A gene has been found in cases of Dravet syndrome. This mutation alters the function of the voltage gated sodium channel subunit, resulting in severe infantile epileptic encephalopathy.","In DRVT. The mutation in the SCN1A gene has been found in cases of Dravet syndrome. This mutation alters the function of the voltage gated sodium channel subunit, resulting in severe infantile epileptic encephalopathy."
352,352,352,24738,Q05320-N563D,MGVTGILQLPRDRFKRTSFFLWVIILFQRTFSIPLGVIHNSTLQVSDVDKLVCRDKLSSTNQLRSVGLNLEGNGVATDVPSATKRWGFRSGVPPKVVNYEAGEWAENCYNLEIKKPDGSECLPAAPDGIRGFPRCRYVHKVSGTGPCAGDFAFHKEGAFFLYDRLASTVIYRGTTFAEGVVAFLILPQAKKDFFSSHPLREPVNATEDPSSGYYSTTIRYQATGFGTNETEYLFEVDNLTYVQLESRFTPQFLLQLNETIYTSGKRSNTTGKLIWKVNPEIDTTIGEWAFWETKKNLTRKIRSEELSFTVVSNGAKNISGQSPARTSSDPGTNTTTEDHKIMASENSSAMVQVHSQGREAAVSHLTTLATISTSPQSLTTKPGPDNSTHNTPVYKLDISEATQVEQHHRRTDNDSTASDTPSATTAAGPPKAENTNTSKSTDFLDPATTTSPQNHSETAGNNNTHHQDTGEESASSGKLGLITNTIAGVAGLITGGRRTRREAIVNAQPKCNPNLHYWTTQDEGAAIGLAWIPYFGPAAEGIYIEGLMHNQDGLICGLRQLADETTQALQLFLRATTELRTFSILNRKAIDFLLQRWGGTCHILGPDCCIEPHDWTKNITDKIDQIIHDFVDKTLPDQGDNDNWWTGWRQWIPAGIGVTGVIIAVIALFCICKFVF,"Reduced levels of expression of GP, GP1 and GP2. 20% loss of virus capability to enter into host cell.",,MGVTGILQLPRDRFKRTSFFLWVIILFQRTFSIPLGVIHNSTLQVSDVDKLVCRDKLSSTNQLRSVGLNLEGNGVATDVPSATKRWGFRSGVPPKVVNYEAGEWAENCYNLEIKKPDGSECLPAAPDGIRGFPRCRYVHKVSGTGPCAGDFAFHKEGAFFLYDRLASTVIYRGTTFAEGVVAFLILPQAKKDFFSSHPLREPVNATEDPSSGYYSTTIRYQATGFGTNETEYLFEVDNLTYVQLESRFTPQFLLQLNETIYTSGKRSNTTGKLIWKVNPEIDTTIGEWAFWETKKNLTRKIRSEELSFTVVSNGAKNISGQSPARTSSDPGTNTTTEDHKIMASENSSAMVQVHSQGREAAVSHLTTLATISTSPQSLTTKPGPDNSTHNTPVYKLDISEATQVEQHHRRTDNDSTASDTPSATTAAGPPKAENTNTSKSTDFLDPATTTSPQNHSETAGNNNTHHQDTGEESASSGKLGLITNTIAGVAGLITGGRRTRREAIVNAQPKCNPNLHYWTTQDEGAAIGLAWIPYFGPAAEGIYIEGLMHNQDGLICGLRQLANETTQALQLFLRATTELRTFSILNRKAIDFLLQRWGGTCHILGPDCCIEPHDWTKNITDKIDQIIHDFVDKTLPDQGDNDNWWTGWRQWIPAGIGVTGVIIAVIALFCICKFVF,Envelope glycoprotein,"Trimeric GP1,2 complexes form the virion surface spikes and mediate the viral entry processes, with GP1 acting as the receptor-binding subunit and GP2 as the membrane fusion subunit. At later times of infection, down-regulates the expression of various host cell surface molecules that are essential for immune surveillance and cell adhesion. Down-modulates several integrins including ITGA1, ITGA2, ITGA3, ITGA4, ITGA5, ITGA6, ITGAV and ITGB1. This decrease in cell adhesion molecules may lead to cell detachment, contributing to the disruption of blood vessel integrity and hemorrhages developed during infection (cytotoxicity) (Probable). Interacts with host TLR4 and thereby stimulates the differentiation and activation of monocytes leading to bystander death of T-lymphocytes. Down-regulates as well the function of host natural killer cells. Counteracts the antiviral effect of host BST2/tetherin that restricts release of progeny virions from infected cells. However, cooperates with VP40 and host BST2 to activate canonical NF-kappa-B pathway in a manner dependent on neddylation.Functions as a decoy for anti-GP1,2 antibodies thereby contributing to viral immune evasion. Interacts and activates host macrophages and dendritic cells inducing up-regulation of cytokine transcription. This effect is mediated throught activation of host TLR4.Responsible for binding to the receptor(s) on target cells. Interacts with CD209/DC-SIGN and CLEC4M/DC-SIGNR which act as cofactors for virus entry into dendritic cells (DCs) and endothelial cells. Binding to the macrophage specific lectin CLEC10A also seems to enhance virus infectivity. Interaction with FOLR1/folate receptor alpha may be a cofactor for virus entry in some cell types, although results are contradictory. Members of the Tyro3 receptor tyrosine kinase family also seem to be cell entry factors in filovirus infection. Once attached, the virions are internalized through clathrin-dependent endocytosis and/or macropinocytosis. After internalization of the virus into the endosomes of the host cell, proteolysis of GP1 by two cysteine proteases, CTSB/cathepsin B and CTSL/cathepsin L removes the glycan cap and allows GP1 binding to the host entry receptor NPC1. NPC1-binding, Ca(2+) and acidic pH induce a conformational change of GP2, which unmasks its fusion peptide and permit membranes fusion.Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in GP2, releasing the fusion hydrophobic peptide.",,"Reduced levels of expression of GP, GP1 and GP2. 20% loss of virus capability to enter into host cell."
357,357,357,25376,Q8TD31-S776C,MFPPSGSTGLIPPSHFQARPLSTLPRMAPTWLSDIPLVQPPGHQDVSERRLDTQRPQVTMWERDVSSDRQEPGRRGRSWGLEGSQALSQQAEVIVRQLQELRRLEEEVRLLRETSLQQKMRLEAQAMELEALARAEKAGRAEAEGLRAALAGAEVVRKNLEEGSQRELEEVQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLSSLETRRAGEAKELAEAQREAELLRKQLSKTQEDLEAQVTLVENLRKYVGEQVPSEVHSQTWELERQKLLETMQHLQEDRDSLHATAELLQVRVQSLTHILALQEEELTRKVQPSDSLEPEFTRKCQSLLNRWREKVFALMVQLKAQELEHSDSVKQLKGQVASLQEKVTSQSQEQAILQRSLQDKAAEVEVERMGAKGLQLELSRAQEARRRWQQQTASAEEQLRLVVNAVSSSQIWLETTMAKVEGAAAQLPSLNNRLSYAVRKVHTIRGLIARKLALAQLRQESCPLPPPVTDVSLELQQLREERNRLDAELQLSARLIQQEVGRAREQGEAERQQLSKVAQQLEQELQQTQESLASLGLQLEVARQGQQESTEEAASLRQELTQQQELYGQALQEKVAEVETRLREQLSDTERRLNEARREHAKAVVSLRQIQRRAAQEKERSQELRRLQEEARKEEGQRLARRLQELERDKNLMLATLQQEGLLSRYKQQRLLTVLPSLLDKKKSVVSSPRPPECSASAPVAAAVPTRESIKGSLSVLLDDLQDLSEAISKEEAVCQGDNLDRCSSCNPQMSS,In allele HCR*WWCC; associated with psoriasis.,,MFPPSGSTGLIPPSHFQARPLSTLPRMAPTWLSDIPLVQPPGHQDVSERRLDTQRPQVTMWERDVSSDRQEPGRRGRSWGLEGSQALSQQAEVIVRQLQELRRLEEEVRLLRETSLQQKMRLEAQAMELEALARAEKAGRAEAEGLRAALAGAEVVRKNLEEGSQRELEEVQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLSSLETRRAGEAKELAEAQREAELLRKQLSKTQEDLEAQVTLVENLRKYVGEQVPSEVHSQTWELERQKLLETMQHLQEDRDSLHATAELLQVRVQSLTHILALQEEELTRKVQPSDSLEPEFTRKCQSLLNRWREKVFALMVQLKAQELEHSDSVKQLKGQVASLQEKVTSQSQEQAILQRSLQDKAAEVEVERMGAKGLQLELSRAQEARRRWQQQTASAEEQLRLVVNAVSSSQIWLETTMAKVEGAAAQLPSLNNRLSYAVRKVHTIRGLIARKLALAQLRQESCPLPPPVTDVSLELQQLREERNRLDAELQLSARLIQQEVGRAREQGEAERQQLSKVAQQLEQELQQTQESLASLGLQLEVARQGQQESTEEAASLRQELTQQQELYGQALQEKVAEVETRLREQLSDTERRLNEARREHAKAVVSLRQIQRRAAQEKERSQELRRLQEEARKEEGQRLARRLQELERDKNLMLATLQQEGLLSRYKQQRLLTVLPSLLDKKKSVVSSPRPPECSASAPVAAAVPTRESIKGSLSVLLDDLQDLSEAISKEEAVCQGDNLDRCSSSNPQMSS,Coiled-coil alpha-helical rod protein 1,May be a regulator of keratinocyte proliferation or differentiation.,,In allele HCR*WWCC; associated with psoriasis.
377,377,377,26317,A0A0P0FGV9-W226Y,MNSSYYQNQINRLEKDIADLQKKIADENKKEIDKNKQIDSVHRTINKNTSISTLNSKQRQIDGYQKDILNCRTKIASYQKSIATKSAELGKKRQELLKAQQSEQKKLQDDQLKFQKKLQSEIEIQKRHLETLIAQNYSTQNNKLVSTEDIPEPTKQYDFFISHASEDKDDIVRDLAEALRNNGFEVWYDEFELKIGDSLRKKIDYGLSNANYGIVIISPSFVKKNYTEYELNGMVAREMNGHKVILPIWHKITKDEVLRFSPSLADKLALNTSIHTIDDIVENLKNL,"60% 2-cADPR produced, very little ADPR made.",,MNSSYYQNQINRLEKDIADLQKKIADENKKEIDKNKQIDSVHRTINKNTSISTLNSKQRQIDGYQKDILNCRTKIASYQKSIATKSAELGKKRQELLKAQQSEQKKLQDDQLKFQKKLQSEIEIQKRHLETLIAQNYSTQNNKLVSTEDIPEPTKQYDFFISHASEDKDDIVRDLAEALRNNGFEVWYDEFELKIGDSLRKKIDYGLSNANYGIVIISPSFVKKNWTEYELNGMVAREMNGHKVILPIWHKITKDEVLRFSPSLADKLALNTSIHTIDDIVENLKNL,2' cyclic ADP-D-ribose synthase BtTIR,NAD(+) hydrolase (NADase) that cleaves NAD(+) into nicotinamide and 2' cyclic ADP-D-ribose (2'cADPR).,unknown,"60% 2-cADPR produced, very little ADPR made. unknown"
380,380,380,26467,Q06413-S387A,MGRKKIQITRIMDERNRQVTFTKRKFGLMKKAYELSVLCDCEIALIIFNSTNKLFQYASTDMDKVLLKYTEYNEPHESRTNSDIVETLRKKGLNGCDSPDPDADDSVGHSPESEDKYRKINEDIDLMISRQRLCAVPPPNFEMPVSIPVSSHNSLVYSNPVSSLGNPNLLPLAHPSLQRNSMSPGVTHRPPSAGNTGGLMGGDLTSGAGTSAGNGYGNPRNSPGLLVSPGNLNKNMQAKSPPPMNLGMNNRKPDLRVLIPPGSKNTMPSVSEDVDLLLNQRINNSQSAQSLATPVVSVATPTLPGQGMGGYPSAISTTYGTEYSLSSADLSSLSGFNTASALHLGSVTGWQQQHLHNMPPSALSQLGACTSTHLSQSSNLSLPSTQALNIKSEPVSPPRDRTTTPSRYPQHTRHEAGRSPVDSLSSCSSSYDGSDREDHRNEFHSPIGLTRPSPDERESPSVKRMRLSEGWAT,No change in transactivational activation for isoforms with or without the beta domain.,,MGRKKIQITRIMDERNRQVTFTKRKFGLMKKAYELSVLCDCEIALIIFNSTNKLFQYASTDMDKVLLKYTEYNEPHESRTNSDIVETLRKKGLNGCDSPDPDADDSVGHSPESEDKYRKINEDIDLMISRQRLCAVPPPNFEMPVSIPVSSHNSLVYSNPVSSLGNPNLLPLAHPSLQRNSMSPGVTHRPPSAGNTGGLMGGDLTSGAGTSAGNGYGNPRNSPGLLVSPGNLNKNMQAKSPPPMNLGMNNRKPDLRVLIPPGSKNTMPSVSEDVDLLLNQRINNSQSAQSLATPVVSVATPTLPGQGMGGYPSAISTTYGTEYSLSSADLSSLSGFNTASALHLGSVTGWQQQHLHNMPPSALSQLGACTSTHLSQSSNLSLPSTQSLNIKSEPVSPPRDRTTTPSRYPQHTRHEAGRSPVDSLSSCSSSYDGSDREDHRNEFHSPIGLTRPSPDERESPSVKRMRLSEGWAT,Myocyte-specific enhancer factor 2C,"Transcription activator which binds specifically to the MEF2 element present in the regulatory regions of many muscle-specific genes. Controls cardiac morphogenesis and myogenesis, and is also involved in vascular development. Enhances transcriptional activation mediated by SOX18. Plays an essential role in hippocampal-dependent learning and memory by suppressing the number of excitatory synapses and thus regulating basal and evoked synaptic transmission. Crucial for normal neuronal development, distribution, and electrical activity in the neocortex. Necessary for proper development of megakaryocytes and platelets and for bone marrow B-lymphopoiesis. Required for B-cell survival and proliferation in response to BCR stimulation, efficient IgG1 antibody responses to T-cell-dependent antigens and for normal induction of germinal center B-cells. May also be involved in neurogenesis and in the development of cortical architecture. Isoforms that lack the repressor domain are more active than isoform 1.",,No change in transactivational activation for isoforms with or without the beta domain.
397,397,397,27151,I6X8R5-Y60A,MKTGTATTRRRLLAVLIALALPGAAVALLAEPSATGASDPCAASEVARTVGSVAKSMGDALDSHPETNQVMTAVLQQQVGPGSVASLKAHFEANPKVASDLHALSQPLTDLSTRCSLPISGLQAIGLMQAVQGARR,Does not bind heme.,,MKTGTATTRRRLLAVLIALALPGAAVALLAEPSATGASDPCAASEVARTVGSVAKSMGDYLDSHPETNQVMTAVLQQQVGPGSVASLKAHFEANPKVASDLHALSQPLTDLSTRCSLPISGLQAIGLMQAVQGARR,Heme-binding protein Rv0203,Part of a heme-iron acquisition system. Acts by binding heme and delivering it to the membrane proteins MmpL3 and MmpL11. Can use free heme or heme from host hemoglobin.,Mutagenesis experiments determined that residue Y59 is required for Rv0203-notag to efficiently bind heme.,Does not bind heme. Mutagenesis experiments determined that residue Y59 is required for Rv0203-notag to efficiently bind heme.
399,399,399,27252,P97434-L857P,MSAAKENPCRKFQANIFNKSKCQNCFKPRESHLLNDEDLTQAKPIYGGWLLLAPDGTDFDNPVHRSRKWQRRFFILYEHGLLRYALDEMPTTLPQGTINMNQCTDVVDGEARTGQKFSLCILTPDKEHFIRAETKEIISGWLEMLMVYPRTNKQNQKKKRKVEPPTPQEPGPAKMAVTSSSGGSSGSSSSIPSAEKVPTTKSTLWQEEMRAKDQPDGTSLSPAQSPSQSQPPAACTPREPGLESKEDESTISGDRVDGGRKVRVESGYFSLEKAKQDLRAEEQLPPLLSPPSPSTPHSRRSQVIEKFEALDIEKAEHMETNMLILTTPSSDTRQGRSERRAIPRKRDFASEAPTAPLSDACPLSPHRRAKSLDRRSTESSMTPDLLNFKKGWLTKQYEDGQWKKHWFVLADQSLRYYRDSVAEEAADLDGEINLSTCYDVTEYPVQRNYGFQIHTKEGEFTLSAMTSGIRRNWIQTIMKHVLPASAPDVTSSLPEGKNKSTSFETCSRSTEKQEAEPGEPDPEQKKSRARERRREGRSKTFDWAEFRPIQQALAQERASAVGSSDSGDPGCLEAEPGELERERARRREERRKRFGMLDTIDGPGMEDTALRMDIDRSPGLLGTPDLKTQNVHVEIEQRWHQVETTPLREEKQVPIAPLHLSLEDRSERLSTHELTSLLEKELEQSQKEASDLLEQNRLLQDQLRVALGREQSAREGYVLQATCERGFAAMEETHQKKIEDLQRQHQRELEKLREEKDRLLAEETAATISAIEAMKNAHREEMERELEKSQRSQISSINSDIEALRRQYLEELQSVQRELEVLSEQYSQKCLENAHLAQALEAERQALRQCQRENQEPNAHNQELNNRLAAEITRLRTLLTGDGGGESTGLPLTQGKDAYELEVLLRVKESEIQYLKQEISSLKDELQTALRDKKYASDKYKDIYTELSIAKAKADCDISRLKEQLKAATEALGEKSPEGTTVSGYDIMKSKSNPDFLKKDRSCVTRQLRNIRSKSVIEQVSWDN,Loss of interaction with PPP1R12C and PPP1R12A.,,MSAAKENPCRKFQANIFNKSKCQNCFKPRESHLLNDEDLTQAKPIYGGWLLLAPDGTDFDNPVHRSRKWQRRFFILYEHGLLRYALDEMPTTLPQGTINMNQCTDVVDGEARTGQKFSLCILTPDKEHFIRAETKEIISGWLEMLMVYPRTNKQNQKKKRKVEPPTPQEPGPAKMAVTSSSGGSSGSSSSIPSAEKVPTTKSTLWQEEMRAKDQPDGTSLSPAQSPSQSQPPAACTPREPGLESKEDESTISGDRVDGGRKVRVESGYFSLEKAKQDLRAEEQLPPLLSPPSPSTPHSRRSQVIEKFEALDIEKAEHMETNMLILTTPSSDTRQGRSERRAIPRKRDFASEAPTAPLSDACPLSPHRRAKSLDRRSTESSMTPDLLNFKKGWLTKQYEDGQWKKHWFVLADQSLRYYRDSVAEEAADLDGEINLSTCYDVTEYPVQRNYGFQIHTKEGEFTLSAMTSGIRRNWIQTIMKHVLPASAPDVTSSLPEGKNKSTSFETCSRSTEKQEAEPGEPDPEQKKSRARERRREGRSKTFDWAEFRPIQQALAQERASAVGSSDSGDPGCLEAEPGELERERARRREERRKRFGMLDTIDGPGMEDTALRMDIDRSPGLLGTPDLKTQNVHVEIEQRWHQVETTPLREEKQVPIAPLHLSLEDRSERLSTHELTSLLEKELEQSQKEASDLLEQNRLLQDQLRVALGREQSAREGYVLQATCERGFAAMEETHQKKIEDLQRQHQRELEKLREEKDRLLAEETAATISAIEAMKNAHREEMERELEKSQRSQISSINSDIEALRRQYLEELQSVQRELEVLSEQYSQKCLENAHLAQALEAERQALRQCQRENQELNAHNQELNNRLAAEITRLRTLLTGDGGGESTGLPLTQGKDAYELEVLLRVKESEIQYLKQEISSLKDELQTALRDKKYASDKYKDIYTELSIAKAKADCDISRLKEQLKAATEALGEKSPEGTTVSGYDIMKSKSNPDFLKKDRSCVTRQLRNIRSKSVIEQVSWDN,Myosin phosphatase Rho-interacting protein,Targets myosin phosphatase to the actin cytoskeleton. Required for the regulation of the actin cytoskeleton by RhoA and ROCK1. Depletion leads to an increased number of stress fibers in smooth muscle cells through stabilization of actin fibers by phosphorylated myosin. Overexpression of MRIP as well as its F-actin-binding region leads to disassembly of stress fibers in neuronal cells.,,Loss of interaction with PPP1R12C and PPP1R12A.
434,434,434,29040,B2B3C0-E300A,MKGLFAFGLGLLSLVNALPQAQGGGAAASAKVSGTRFVIDGKTGYFAGTNSYWIGFLTNNRDVDTTLDHIASSGLKILRVWGFNDVNNQPSGNTVWFQRLASSGSQINTGPNGLQRLDYLVRSAETRGIKLIIALVNYWDDFGGMKAYVNAFGGTKESWYTNARAQEQYKRYIQAVVSRYVNSPAIFAWELANEPRCKGCNTNVIFNWATQISDYIRSLDKDHLITLGDEGFGLPGQTTYPYQYGEGTDFVKNLQIKNLDFGTFHMYPGHWGVPTSFGPGWIKDHAAACRAAGKPCLLEAYGYESDRCNVQKGWQQASRELSRDGMSGDLFWQWGDQLSTGQTHNDGFTIYYGSSLATCLVTDHVRAINALPA,Abolishes catalytic activity.,,MKGLFAFGLGLLSLVNALPQAQGGGAAASAKVSGTRFVIDGKTGYFAGTNSYWIGFLTNNRDVDTTLDHIASSGLKILRVWGFNDVNNQPSGNTVWFQRLASSGSQINTGPNGLQRLDYLVRSAETRGIKLIIALVNYWDDFGGMKAYVNAFGGTKESWYTNARAQEQYKRYIQAVVSRYVNSPAIFAWELANEPRCKGCNTNVIFNWATQISDYIRSLDKDHLITLGDEGFGLPGQTTYPYQYGEGTDFVKNLQIKNLDFGTFHMYPGHWGVPTSFGPGWIKDHAAACRAAGKPCLLEEYGYESDRCNVQKGWQQASRELSRDGMSGDLFWQWGDQLSTGQTHNDGFTIYYGSSLATCLVTDHVRAINALPA,"Mannan endo-1,4-beta-mannosidase A","Endo-1,4-mannanase that catalyzes the random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans and heteromannans. It is a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans. Hydrolyzes structurally different mannan polysaccharides, such as galactomannans, glucomannans, and beta-1,4-mannans from different sources, yielding principally mannobiose. Also has transglycosylation activity.",,Abolishes catalytic activity.
450,450,450,29995,P04042-G284V,MSKIRVLSVDDSALMRQIMTEIINSHSDMEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRPMPVVMVSSLTGKGSEVTLRALELGAIDFVTKPQLGIREGMLAYSEMIAEKVRTAARARIAAHKPMAAPTTLKAGPLLSSEKLIAIGASTGGTEAIRHVLQPLPLSSPAVIITQHMPPGFTRSFAERLNKLCQISVKEAEDGERVLPGHAYIAPGDKHMELARSGANYQIKIHDGPPVNRHRPSVDVLFHSVAKHAGRNAVGVILTGMVNDGAAGMLAMYQAGAWTIAQNEASCVVFGMPREAINMGGVSEVVDLSQVSQQMLAKISAGQAIRI,Loss of methylesterase activity.,,MSKIRVLSVDDSALMRQIMTEIINSHSDMEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRPMPVVMVSSLTGKGSEVTLRALELGAIDFVTKPQLGIREGMLAYSEMIAEKVRTAARARIAAHKPMAAPTTLKAGPLLSSEKLIAIGASTGGTEAIRHVLQPLPLSSPAVIITQHMPPGFTRSFAERLNKLCQISVKEAEDGERVLPGHAYIAPGDKHMELARSGANYQIKIHDGPPVNRHRPSVDVLFHSVAKHAGRNAVGVILTGMGNDGAAGMLAMYQAGAWTIAQNEASCVVFGMPREAINMGGVSEVVDLSQVSQQMLAKISAGQAIRI,Protein-glutamate methylesterase/protein-glutamine glutaminase,Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid.,Mutation of the second glycine in this region (G284) to a valine also caused a complete loss of esterase activity.,Loss of methylesterase activity. Mutation of the second glycine in this region (G284) to a valine also caused a complete loss of esterase activity.
454,454,454,30405,Q8N6T7-S45A,MSVNYAAGLSPYADKGKCGLPEIFDPPEELERKVWELARLVWQSASVVFHTGAGISTASGIPDFRGPHGVWTMEERGLAPKFDTTFESARPTQTHMALVQLERVGLLRFLVSQNVDGLHVRSGFPRDKLAELHGNMFVEECAKCKTQYVRDTVVGTMGLKATGRLCTVAKARGLRACRGELRDTILDWEDSLPDRDLALADEASRNADLSITLGTSLQIRPSGNLPLATKRRGGRLVIVNLQPTKHDRHADLRIHGYVDEVMTRLMKHLGLEIPAWDGPRVLERALPPLPRPPTPKLEPKEESPTRINGSIPAGPKQEPCAQHNGSEPASPKRERPTSPAPHRPPKRVKAKAVPS,In AAA mutant; strongly decreased nucleosome-binding; when associated with 206-A--A-208.,,MSVNYAAGLSPYADKGKCGLPEIFDPPEELERKVWELARLVWQSSSVVFHTGAGISTASGIPDFRGPHGVWTMEERGLAPKFDTTFESARPTQTHMALVQLERVGLLRFLVSQNVDGLHVRSGFPRDKLAELHGNMFVEECAKCKTQYVRDTVVGTMGLKATGRLCTVAKARGLRACRGELRDTILDWEDSLPDRDLALADEASRNADLSITLGTSLQIRPSGNLPLATKRRGGRLVIVNLQPTKHDRHADLRIHGYVDEVMTRLMKHLGLEIPAWDGPRVLERALPPLPRPPTPKLEPKEESPTRINGSIPAGPKQEPCAQHNGSEPASPKRERPTSPAPHRPPKRVKAKAVPS,NAD-dependent protein deacylase sirtuin-6,"NAD-dependent protein deacetylase, deacylase and mono-ADP-ribosyltransferase that plays an essential role in DNA damage repair, telomere maintenance, metabolic homeostasis, inflammation, tumorigenesis and aging. Displays protein-lysine deacetylase or defatty-acylase (demyristoylase and depalmitoylase) activity, depending on the context. Acts as a key histone deacetylase by catalyzing deacetylation of histone H3 at 'Lys-9', 'Lys-18' and 'Lys-56' (H3K9ac, H3K18ac and H3K56ac, respectively), suppressing target gene expression of several transcription factors, including NF-kappa-B. Acts as an inhibitor of transcription elongation by mediating deacetylation of H3K9ac and H3K56ac, preventing release of NELFE from chromatin and causing transcriptional pausing. Involved in DNA repair by promoting double-strand break (DSB) repair: acts as a DSB sensor by recognizing and binding DSB sites, leading to (1) recruitment of DNA repair proteins, such as SMARCA5/SNF2H, and (2) deacetylation of histone H3K9ac and H3K56ac. SIRT6 participation to DSB repair is probably involved in extension of life span. Also promotes DNA repair by deacetylating non-histone proteins, such as DDB2 and p53/TP53. Specifically deacetylates H3K18ac at pericentric heterochromatin, thereby maintaining pericentric heterochromatin silencing at centromeres and protecting against genomic instability and cellular senescence. Involved in telomere maintenance by catalyzing deacetylation of histone H3 in telomeric chromatin, regulating telomere position effect and telomere movement in response to DNA damage. Required for embryonic stem cell differentiation by mediating histone deacetylation of H3K9ac. Plays a major role in metabolism by regulating processes such as glycolysis, gluconeogenesis, insulin secretion and lipid metabolism. Inhibits glycolysis via histone deacetylase activity and by acting as a corepressor of the transcription factor HIF1A, thereby controlling the expression of multiple glycolytic genes. Has tumor suppressor activity by repressing glycolysis, thereby inhibiting the Warburg effect. Also regulates glycolysis and tumorigenesis by mediating deacetylation and nuclear export of non-histone proteins, such as isoform M2 of PKM (PKM2). Acts as a negative regulator of gluconeogenesis by mediating deacetylation of non-histone proteins, such as FOXO1 and KAT2A/GCN5. Promotes beta-oxidation of fatty acids during fasting by catalyzing deacetylation of NCOA2, inducing coactivation of PPARA. Acts as a regulator of lipid catabolism in brown adipocytes, both by catalyzing deacetylation of histones and non-histone proteins, such as FOXO1. Also acts as a regulator of circadian rhythms, both by regulating expression of clock-controlled genes involved in lipid and carbohydrate metabolism, and by catalyzing deacetylation of PER2. The defatty-acylase activity is specifically involved in regulation of protein secretion. Has high activity toward long-chain fatty acyl groups and mediates protein-lysine demyristoylation and depalmitoylation of target proteins, such as RRAS2 and TNF, thereby regulating their secretion. Also acts as a mono-ADP-ribosyltransferase by mediating mono-ADP-ribosylation of PARP1, TRIM28/KAP1 or SMARCC2/BAF170. Mono-ADP-ribosyltransferase activity is involved in DNA repair, cellular senescence, repression of LINE-1 retrotransposon elements and regulation of transcription.","The mutation in the SIRT6 protein leads to a loss of function in deacetylating histone H3 and repressing transcription. This mutation disrupts the tight interaction between SIRT6 and nucleosome core particles, resulting in reduced efficiency in deacetylating histones on endogenous chromatin.","In AAA mutant; strongly decreased nucleosome-binding; when associated with 206-A--A-208. The mutation in the SIRT6 protein leads to a loss of function in deacetylating histone H3 and repressing transcription. This mutation disrupts the tight interaction between SIRT6 and nucleosome core particles, resulting in reduced efficiency in deacetylating histones on endogenous chromatin."
475,475,475,31744,Q9HD67-L893Q,MDNFFTEGTRVWLRENGQHFPSTVNSCAEGIVVFRTDYGQVFTYKQSTITHQKVTAMHPTNEEGVDDMASLTELHGGSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAGLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILISGESGAGKTESTKLILKFLSVISQQSLELSLKEKTSCVERAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNQSGCVEDKTISDQESFREVITAMDVMQFSKEEVREVSRLLAGILHLGNIEFITAGGAQVSFKTALGRSAELLGLDPTQLTDALTQRSMFLRGEEILTPLNVQQAVDSRDSLAMALYACCFEWVIKKINSRIKGNEDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLEQLEYSREGLVWEDIDWIDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQHANNHFYVKPRVAVNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNNQDTLKCGSKHRRPTVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNLALPEDVRGKCTSLLQLYDASNSEWQLGKTKVFLRESLEQKLEKRREEEVSHAAMVIRAHVLGFLARKQYRKVLYCVVIIQKNYRAFLLRRRFLHLKKAAIVFQKQLRGQIARRVYRQLLAEKREQEEKKKQEEEEKKKREEEERERERERREAELRAQQEEETRKQQELEALQKSQKEAELTRELEKQKENKQVEEILRQEKEIEDLQRMKEQQELSLTEASLQKLQERRDQELRRLEEEACRAAQEFLESLNFDEIDECVRNIERSLSVGSEFSSELAESACEEKPNFNFSQPYPEEEVDEGFEADDDAFKDSPNPSEHGHSDQRTSGIR,Abolishes dimerization.,,MDNFFTEGTRVWLRENGQHFPSTVNSCAEGIVVFRTDYGQVFTYKQSTITHQKVTAMHPTNEEGVDDMASLTELHGGSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAGLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILISGESGAGKTESTKLILKFLSVISQQSLELSLKEKTSCVERAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNQSGCVEDKTISDQESFREVITAMDVMQFSKEEVREVSRLLAGILHLGNIEFITAGGAQVSFKTALGRSAELLGLDPTQLTDALTQRSMFLRGEEILTPLNVQQAVDSRDSLAMALYACCFEWVIKKINSRIKGNEDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLEQLEYSREGLVWEDIDWIDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQHANNHFYVKPRVAVNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNNQDTLKCGSKHRRPTVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNLALPEDVRGKCTSLLQLYDASNSEWQLGKTKVFLRESLEQKLEKRREEEVSHAAMVIRAHVLGFLARKQYRKVLYCVVIIQKNYRAFLLRRRFLHLKKAAIVFQKQLRGQIARRVYRQLLAEKREQEEKKKQEEEEKKKREEEERERERERREAELRAQQEEETRKQQELEALQKSQKEAELTRELEKQKENKQVEEILRLEKEIEDLQRMKEQQELSLTEASLQKLQERRDQELRRLEEEACRAAQEFLESLNFDEIDECVRNIERSLSVGSEFSSELAESACEEKPNFNFSQPYPEEEVDEGFEADDDAFKDSPNPSEHGHSDQRTSGIR,Unconventional myosin-X,"Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. MYO10 binds to actin filaments and actin bundles and functions as a plus end-directed motor. Moves with higher velocity and takes larger steps on actin bundles than on single actin filaments. The tail domain binds to membranous compartments containing phosphatidylinositol 3,4,5-trisphosphate or integrins, and mediates cargo transport along actin filaments. Regulates cell shape, cell spreading and cell adhesion. Stimulates the formation and elongation of filopodia. In hippocampal neurons it induces the formation of dendritic filopodia by trafficking the actin-remodeling protein VASP to the tips of filopodia, where it promotes actin elongation. Plays a role in formation of the podosome belt in osteoclasts.Functions as a dominant-negative regulator of isoform 1, suppressing its filopodia-inducing and axon outgrowth-promoting activities. In hippocampal neurons, it increases VASP retention in spine heads to induce spine formation and spine head expansion.",Disruption of the anti-CC either by single-point mutations or by replacement of the anti-CC with a parallel coiled coil with a similar length compromised the filopodial induction activity of myosin X.,Abolishes dimerization. Disruption of the anti-CC either by single-point mutations or by replacement of the anti-CC with a parallel coiled coil with a similar length compromised the filopodial induction activity of myosin X.
485,485,485,32375,P15056-G596R,MAALSGGGGGGAEPGQALFNGDMEPEAGAGAGAAASSAADPAIPEEVWNIKQMIKLTQEHIEALLDKFGGEHNPPSIYLEAYEEYTSKLDALQQREQQLLESLGNGTDFSVSSSASMDTVTSSSSSSLSVLPSSLSVFQNPTDVARSNPKSPQKPIVRVFLPNKQRTVVPARCGVTVRDSLKKALMMRGLIPECCAVYRIQDGEKKPIGWDTDISWLTGEELHVEVLENVPLTTHNFVRKTFFTLAFCDFCRKLLFQGFRCQTCGYKFHQRCSTEVPLMCVNYDQLDLLFVSKFFEHHPIPQEEASLAETALTSGSSPSAPASDSIGPQILTSPSPSKSIPIPQPFRPADEDHRNQFGQRDRSSSAPNVHINTIEPVNIDDLIRDQGFRGDGGSTTGLSATPPASLPGSLTNVKALQKSPGPQRERKSSSSSEDRNRMKTLGRRDSSDDWEIPDGQITVGQRIGSGSFGTVYKGKWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLAIVTQWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFRLATVKSRWSGSHQFEQLSGSILWMAPEVIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSPDLSKVRSNCPKAMKRLMAECLKKKRDERPLFPQILASIELLARSLPKIHRSASEPSLNRAGFQTEDFSLYACASPKTPIQAGGYGAFPVH,In a colorectal adenocarcinoma sample; somatic mutation.,,MAALSGGGGGGAEPGQALFNGDMEPEAGAGAGAAASSAADPAIPEEVWNIKQMIKLTQEHIEALLDKFGGEHNPPSIYLEAYEEYTSKLDALQQREQQLLESLGNGTDFSVSSSASMDTVTSSSSSSLSVLPSSLSVFQNPTDVARSNPKSPQKPIVRVFLPNKQRTVVPARCGVTVRDSLKKALMMRGLIPECCAVYRIQDGEKKPIGWDTDISWLTGEELHVEVLENVPLTTHNFVRKTFFTLAFCDFCRKLLFQGFRCQTCGYKFHQRCSTEVPLMCVNYDQLDLLFVSKFFEHHPIPQEEASLAETALTSGSSPSAPASDSIGPQILTSPSPSKSIPIPQPFRPADEDHRNQFGQRDRSSSAPNVHINTIEPVNIDDLIRDQGFRGDGGSTTGLSATPPASLPGSLTNVKALQKSPGPQRERKSSSSSEDRNRMKTLGRRDSSDDWEIPDGQITVGQRIGSGSFGTVYKGKWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLAIVTQWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQFEQLSGSILWMAPEVIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSPDLSKVRSNCPKAMKRLMAECLKKKRDERPLFPQILASIELLARSLPKIHRSASEPSLNRAGFQTEDFSLYACASPKTPIQAGGYGAFPVH,Serine/threonine-protein kinase B-raf,"Protein kinase involved in the transduction of mitogenic signals from the cell membrane to the nucleus (Probable). Phosphorylates MAP2K1, and thereby activates the MAP kinase signal transduction pathway. May play a role in the postsynaptic responses of hippocampal neurons.",,In a colorectal adenocarcinoma sample; somatic mutation.
521,521,521,35637,O95859-A237P,MAREDSVKCLRCLLYALNLLFWLMSISVLAVSAWMRDYLNNVLTLTAETRVEEAVILTYFPVVHPVMIAVCCFLIIVGMLGYCGTVKRNLLLLAWYFGSLLVIFCVELACGVWTYEQELMVPVQWSDMVTLKARMTNYGLPRYRWLTHAWNFFQREFKCCGVVYFTDWLEMTEMDWPPDSCCVREFPGCSKQAHQEDLSDLYQEGCGKKMYSFLRGTKQLQVLRFLGISIGVTQILPMILTITLLWALYYDRREPGTDQMMSLKNDNSQHLSCPSVELLKPSLSRIFEHTSMANSFNTHFEMEEL,In EVR5.,,MAREDSVKCLRCLLYALNLLFWLMSISVLAVSAWMRDYLNNVLTLTAETRVEEAVILTYFPVVHPVMIAVCCFLIIVGMLGYCGTVKRNLLLLAWYFGSLLVIFCVELACGVWTYEQELMVPVQWSDMVTLKARMTNYGLPRYRWLTHAWNFFQREFKCCGVVYFTDWLEMTEMDWPPDSCCVREFPGCSKQAHQEDLSDLYQEGCGKKMYSFLRGTKQLQVLRFLGISIGVTQILAMILTITLLWALYYDRREPGTDQMMSLKNDNSQHLSCPSVELLKPSLSRIFEHTSMANSFNTHFEMEEL,Tetraspanin-12,"Regulator of cell surface receptor signal transduction. Plays a central role in retinal vascularization by regulating norrin (NDP) signal transduction. Acts in concert with norrin (NDP) to promote FZD4 multimerization and subsequent activation of FZD4, leading to promote accumulation of beta-catenin (CTNNB1) and stimulate LEF/TCF-mediated transcriptional programs. Suprisingly, it only activates the norrin (NDP)-dependent activation of FZD4, while it does not activate the Wnt-dependent activation of FZD4, suggesting the existence of a Wnt-independent signaling that also promote accumulation the beta-catenin (CTNNB1). Acts as a regulator of membrane proteinases such as ADAM10 and MMP14/MT1-MMP. Activates ADAM10-dependent cleavage activity of amyloid precursor protein (APP). Activates MMP14/MT1-MMP-dependent cleavage activity.","The variant in the TSPAN12 protein has been identified as a causative genetic defect in familial exudative vitreoretinopathy (FEVR). This protein, along with other proteins encoded by FZD4, LRP5, and NDP, is involved in regulating the development of retinal vasculature.","In EVR5. The variant in the TSPAN12 protein has been identified as a causative genetic defect in familial exudative vitreoretinopathy (FEVR). This protein, along with other proteins encoded by FZD4, LRP5, and NDP, is involved in regulating the development of retinal vasculature."
552,552,552,37742,D0PV95-T434I,MESNQSNNGGSGNAALNRGGRYVPPHLRGGDGGAAAAASAGGDDRRGGAGGGGYRRGGGNSGGGGGGGYDRGYNDNRDDRDNRGGSGGYGRDRNYEDRGYNGGGGGGGNRGYNNNRGGGGGGYNRQDRGDGGSSNFSRGGYNNRDEGSDNRGSGRSYNNDRRDNGGDGQNTRWNNLDAPPSRGTSKWENRGARDERIEQELFSGQLSGINFDKYEEIPVEATGDDVPQPISLFSDLSLHEWIEENIKTAGYDRPTPVQKYSIPALQGGRDLMSCAQTGSGKTAAFLVPLVNAILQDGPDAVHRSVTSSGGRKKQYPSALVLSPTRELSLQIFNESRKFAYRTPITSALLYGGRENYKDQIHKLRLGCHILIATPGRLIDVMDQGLIGMEGCRYLVLDEADRMLDMGFEPQIRQIVECNRMPSKEERITAMFSAIFPKEIQLLAQDFLKENYVFLAVGRVGSTSENIMQKIVWVEEDEKRSYLMDLLDATGDSSLTLVFVETKRGASDLAYYLNRQNYEVVTIHGDLKQFEREKHLDLFRTGTAPILVATAVAARGLDIPNVKHVINYDLPSDVDEYVHRIGRTGRVGNVGLATSFFNDKNRNIARELMDLIVEANQELPDWLEGMSGDMRSGGGYRGRGGRGNGQRFGGRDHRYQGGSGNGGGGNGGGGGFGGGGQRSGGGGGFQSGGGGGRQQQQQQRAQPQQDWWS,In q267; embryonic lethal.,,MESNQSNNGGSGNAALNRGGRYVPPHLRGGDGGAAAAASAGGDDRRGGAGGGGYRRGGGNSGGGGGGGYDRGYNDNRDDRDNRGGSGGYGRDRNYEDRGYNGGGGGGGNRGYNNNRGGGGGGYNRQDRGDGGSSNFSRGGYNNRDEGSDNRGSGRSYNNDRRDNGGDGQNTRWNNLDAPPSRGTSKWENRGARDERIEQELFSGQLSGINFDKYEEIPVEATGDDVPQPISLFSDLSLHEWIEENIKTAGYDRPTPVQKYSIPALQGGRDLMSCAQTGSGKTAAFLVPLVNAILQDGPDAVHRSVTSSGGRKKQYPSALVLSPTRELSLQIFNESRKFAYRTPITSALLYGGRENYKDQIHKLRLGCHILIATPGRLIDVMDQGLIGMEGCRYLVLDEADRMLDMGFEPQIRQIVECNRMPSKEERITAMFSATFPKEIQLLAQDFLKENYVFLAVGRVGSTSENIMQKIVWVEEDEKRSYLMDLLDATGDSSLTLVFVETKRGASDLAYYLNRQNYEVVTIHGDLKQFEREKHLDLFRTGTAPILVATAVAARGLDIPNVKHVINYDLPSDVDEYVHRIGRTGRVGNVGLATSFFNDKNRNIARELMDLIVEANQELPDWLEGMSGDMRSGGGYRGRGGRGNGQRFGGRDHRYQGGSGNGGGGNGGGGGFGGGGQRSGGGGGFQSGGGGGRQQQQQQRAQPQQDWWS,ATP-dependent RNA helicase laf-1,"Multifunctional ATP-dependent RNA helicase. Plays a role in RNA remodeling, but is not required for RNA unwinding. Binds to RNA in a concentration-dependent manner to stimulate annealing between two complementary strands of RNA. This process is also dependent upon ATP; ATP reduces binding to RNA and subsequently diminishes RNA annealing. Involved in many cellular processes, which do not necessarily require its ATPase/helicase catalytic activities. Involved in the regulation of transcription and translation initiation. Involved in innate immunity. Involved in both stress and inflammatory responses. Promotes liquid-liquid phase separation of P granules, which is a process important for intracellular organization and stress granule assembly. Required for embryonic development. Plays a role in sexual cell fate determination by negatively regulating the translation of the sex determining protein tra-2. May play a protective role in the response to heat and oxidative stress. May negatively regulate extrinsic apoptotic signaling pathway via death domain receptors. May be involved in mitotic chromosome segregation.",The mutation affects a small region of the laf-1 protein in or near helicase motif III. The phenotypes resulting from laf-1 mutations are due to loss or reduction of laf-1 function. Laf-1 functions to negatively regulate expression of the sex determination protein TRA-2.,In q267; embryonic lethal. The mutation affects a small region of the laf-1 protein in or near helicase motif III. The phenotypes resulting from laf-1 mutations are due to loss or reduction of laf-1 function. Laf-1 functions to negatively regulate expression of the sex determination protein TRA-2.
554,554,554,37931,P08411-C135A,MAAKVHVDIEADSPFIKSLQKAFPSFEVESLQVTPNDHANARAFSHLATKLIEQETDKDTLILDIGSAPSRRMMSTHKYHCVCPMRSAEDPERLVCYAKKLAAASGKVLDREIAGKITDLQTVMATPDAESPTFALHTDVTCRTAAEVAVYQDVYAVHAPTSLYHQAMKGVRTAYWIGFDTTPFMFDALAGAYPTYATNWADEQVLQARNIGLCAASLTEGRLGKLSILRKKQLKPCDTVMFSVGSTLYTESRKLLRSWHLPSVFHLKGKQSFTCRCDTIVSCEGYVVKKITMCPGLYGKTVGYAVTYHAEGFLVCKTTDTVKGERVSFPVCTYVPSTICDQMTGILATDVTPEDAQKLLVGLNQRIVVNGRTQRNTNTMKNYLLPIVAVAFSKWAREYKADLDDEKPLGVRERSLTCCCLWAFKTRKMHTMYKKPDTQTIVKVPSEFNSFVIPSLWSTGLAIPVRSRIKMLLAKKTKRELIPVLDASSARDAEQEEKERLEAELTREALPPLVPIAPAETGVVDVDVEELEYHAGAGVVETPRSALKVTAQPNDVLLGNYVVLSPQTVLKSSKLAPVHPLAEQVKIITHNGRAGRYQVDGYDGRVLLPCGSAIPVPEFQALSESATMVYNEREFVNRKLYHIAVHGPSLNTDEENYEKVRAERTDAEYVFDVDKKCCVKREEASGLVLVGELTNPPFHEFAYEGLKIRPSAPYKTTVVGVFGVPGSGKSAIIKSLVTKHDLVTSGKKENCQEIVNDVKKHRGLDIQAKTVDSILLNGCRRAVDILYVDEAFACHSGTLLALIALVKPRSKVVLCGDPKQCGFFNMMQLKVNFNHNICTEVCHKSISRRCTRPVTAIVSTLHYGGKMRTTNPCNKPIIIDTTGQTKPKPGDIVLTCFRGWVKQLQLDYRGHEVMTAAASQGLTRKGVYAVRQKVNENPLYAPASEHVNVLLTRTEDRLVWKTLAGDPWIKVLSNIPQGNFTATLEEWQEEHDKIMKVIEGPAAPVDAFQNKANVCWAKSLVPVL,90% loss of guanine-7-methyl transferase activity and complete loss of guanylyltransferase activity in vitro.,,MAAKVHVDIEADSPFIKSLQKAFPSFEVESLQVTPNDHANARAFSHLATKLIEQETDKDTLILDIGSAPSRRMMSTHKYHCVCPMRSAEDPERLVCYAKKLAAASGKVLDREIAGKITDLQTVMATPDAESPTFCLHTDVTCRTAAEVAVYQDVYAVHAPTSLYHQAMKGVRTAYWIGFDTTPFMFDALAGAYPTYATNWADEQVLQARNIGLCAASLTEGRLGKLSILRKKQLKPCDTVMFSVGSTLYTESRKLLRSWHLPSVFHLKGKQSFTCRCDTIVSCEGYVVKKITMCPGLYGKTVGYAVTYHAEGFLVCKTTDTVKGERVSFPVCTYVPSTICDQMTGILATDVTPEDAQKLLVGLNQRIVVNGRTQRNTNTMKNYLLPIVAVAFSKWAREYKADLDDEKPLGVRERSLTCCCLWAFKTRKMHTMYKKPDTQTIVKVPSEFNSFVIPSLWSTGLAIPVRSRIKMLLAKKTKRELIPVLDASSARDAEQEEKERLEAELTREALPPLVPIAPAETGVVDVDVEELEYHAGAGVVETPRSALKVTAQPNDVLLGNYVVLSPQTVLKSSKLAPVHPLAEQVKIITHNGRAGRYQVDGYDGRVLLPCGSAIPVPEFQALSESATMVYNEREFVNRKLYHIAVHGPSLNTDEENYEKVRAERTDAEYVFDVDKKCCVKREEASGLVLVGELTNPPFHEFAYEGLKIRPSAPYKTTVVGVFGVPGSGKSAIIKSLVTKHDLVTSGKKENCQEIVNDVKKHRGLDIQAKTVDSILLNGCRRAVDILYVDEAFACHSGTLLALIALVKPRSKVVLCGDPKQCGFFNMMQLKVNFNHNICTEVCHKSISRRCTRPVTAIVSTLHYGGKMRTTNPCNKPIIIDTTGQTKPKPGDIVLTCFRGWVKQLQLDYRGHEVMTAAASQGLTRKGVYAVRQKVNENPLYAPASEHVNVLLTRTEDRLVWKTLAGDPWIKVLSNIPQGNFTATLEEWQEEHDKIMKVIEGPAAPVDAFQNKANVCWAKSLVPVL,Polyprotein P1234,"Inactive precursor of the viral replicase, which is activated by cleavages carried out by the viral protease nsP2.The early replication complex formed by the polyprotein P123 and nsP4 synthesizes minus-strand RNAs. As soon P123 is cleaved into mature proteins, the plus-strand RNAs synthesis begins.The early replication complex formed by the polyprotein P123' and nsP4 synthesizes minus-strand RNAs (Probable). Polyprotein P123' is a short-lived polyprotein that accumulates during early stage of infection (Probable). As soon P123' is cleaved into mature proteins, the plus-strand RNAs synthesis begins (Probable).Cytoplasmic capping enzyme that catalyzes two virus-specific reactions: methyltransferase and nsP1 guanylyltransferase. mRNA-capping is necessary since all viral RNAs are synthesized in the cytoplasm, and host capping enzymes are restricted to the nucleus (Probable). The enzymatic reaction involves a covalent link between 7-methyl-GMP and nsP1, whereas eukaryotic capping enzymes form a covalent complex only with GMP (Probable). nsP1 capping consists in the following reactions: GTP is first methylated into 7-methyl-GMP and then is covalently linked to nsP1 to form the m7GMp-nsP1 complex from which 7-methyl-GMP complex is transferred to the mRNA to create the cap structure (Probable). NsP1 is also needed for the initiation of the minus-strand RNAs synthesis. Probably serves as a membrane anchor for the replication complex composed of nsP1-nsP4 (Probable). Palmitoylated nsP1 is remodeling host cell cytoskeleton, and induces filopodium-like structure formation at the surface of the host cell.Multifunctional protein whose N-terminus is part of the RNA polymerase complex and displays NTPase, RNA triphosphatase and helicase activities. NTPase and RNA triphosphatase are involved in viral RNA capping and helicase keeps a check on the dsRNA replication intermediates (Probable). The C-terminus harbors a protease that specifically cleaves and releases the mature proteins. Required for the shutoff of minus-strand RNAs synthesis. Specifically inhibits the host IFN response by promoting the nuclear export of host STAT1. Also inhibits host transcription by inducing rapid proteasome-dependent degradation of POLR2A, a catalytic subunit of the RNAPII complex. The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response (Probable).Seems to be essential for minus-strand RNAs and subgenomic 26S mRNAs synthesis. Displays mono-ADP-ribosylhydrolase activity (Probable). ADP-ribosylation is a post-translational modification that controls various processes of the host cell and the virus probably needs to revert it for optimal viral replication (Probable). Binds proteins of FXR family and sequesters them into the viral RNA replication complexes thereby inhibiting the formation of host stress granules on viral mRNAs (Probable). The nsp3'-FXR complexes bind viral RNAs and probably orchestrate the assembly of viral replication complexes, thanks to the ability of FXR family members to self-assemble and bind DNA (Probable).Seems to be essential for minus-strand RNAs and subgenomic 26S mRNAs synthesis. Displays mono-ADP-ribosylhydrolase activity. ADP-ribosylation is a post-translational modification that controls various processes of the host cell and the virus probably needs to revert it for optimal viral replication. Binds proteins of G3BP family and sequesters them into the viral RNA replication complexes thereby inhibiting the formation of host stress granules on viral mRNAs. The nsp3-G3BP complexes bind viral RNAs and probably orchestrate the assembly of viral replication complexes, thanks to the ability of G3BP family members to self-assemble and bind DNA.RNA dependent RNA polymerase. Replicates genomic and antigenomic RNA by recognizing replications specific signals. The early replication complex formed by the polyprotein P123 and nsP4 synthesizes minus-strand RNAs. The late replication complex composed of fully processed nsP1-nsP4 is responsible for the production of genomic and subgenomic plus-strand RNAs.","Mutation of C135 to alanine destroyed or greatly reduced the MT activity of nsP1. All MT-negative mutants lost also the GT activity, confirming that methylation of GTP is an essential prerequisite for the synthesis of the covalent guanylate complex.","90% loss of guanine-7-methyl transferase activity and complete loss of guanylyltransferase activity in vitro. Mutation of C135 to alanine destroyed or greatly reduced the MT activity of nsP1. All MT-negative mutants lost also the GT activity, confirming that methylation of GTP is an essential prerequisite for the synthesis of the covalent guanylate complex."
575,575,575,39779,Q9P267-A857T,MNGGKECDGGDKEGGLPAIQVPVGWQRRVDQNGVLYVSPSGSLLSCLEQVKTYLLTDGTCKCGLECPLILPKVFNFDPGAAVKQRTAEDVKADEDVTKLCIHKRKIIAVATLHKSMEAPHPSLVLTSPGGGTNATPVVPSRAATPRSVRNKSHEGITNSVMPECKNPFKLMIGSSNAMGRLYVQELPGSQQQELHPVYPRQRLGSSEHGQKSPFRGSHGGLPSPASSGSQIYGDGSISPRTDPLGSPDVFTRSNPGFHGAPNSSPIHLNRTPLSPPSVMLHGSPVQSSCAMAGRTNIPLSPTLTTKSPVMKKPMCNFSTNMEIPRAMFHHKPPQGPPPPPPPSCALQKKPLTSEKDPLGILDPIPSKPVNQNPVIINPTSFHSNVHSQVPMMNVSMPPAVVPLPSNLPLPTVKPGHMNHGSHVQRVQHSASTSLSPSPVTSPVHMMGTGIGRIEASPQRSRSSSTSSDHGNFMMPPVGPQATSSGIKVPPRSPRSTIGSPRPSMPSSPSTKSDGHHQYKDIPNPLIAGISNVLNTPSSAAFPTASAGSSSVKSQPGLLGMPLNQILNQHNAASFPASSLLSAAAKAQLANQNKLAGNNSSSSSNSGAVAGSGNTEGHSTLNTMFPPTANMLLPTGEGQSGRAALRDKLMSQQKDALRKRKQPPTTVLSLLRQSQMDSSAVPKPGPDLLRKQGQGSFPISSMSQLLQSMSCQSSHLSSNSTPGCGASNTALPCSANQLHFTDPSMNSSVLQNIPLRGEAVHCHNANTNFVHSNSPVPNHHLAGLINQIQASGNCGMLSQSGMALGNSLHPNPPQSRISTSSTPVIPNSIVSSYNQTSSEAGGSGPSSSIAIAGTNHPTITKTTSVLQDGVIVTTAAGNPLQSQLPIGSDFPFVGQEHALHFPSNSTSNNHLPHPLNPSLLSSLPISLPVNQQHLLNQNLLNILQPSAGEGDMSSINNTLSNHQLTHLQSLLNNNQMFPPNQQQQQLLQGYQNLQAFQGQSTIPCPANNNPMACLFQNFQVRMQED,In MRD1; unknown pathological significance.,,MNGGKECDGGDKEGGLPAIQVPVGWQRRVDQNGVLYVSPSGSLLSCLEQVKTYLLTDGTCKCGLECPLILPKVFNFDPGAAVKQRTAEDVKADEDVTKLCIHKRKIIAVATLHKSMEAPHPSLVLTSPGGGTNATPVVPSRAATPRSVRNKSHEGITNSVMPECKNPFKLMIGSSNAMGRLYVQELPGSQQQELHPVYPRQRLGSSEHGQKSPFRGSHGGLPSPASSGSQIYGDGSISPRTDPLGSPDVFTRSNPGFHGAPNSSPIHLNRTPLSPPSVMLHGSPVQSSCAMAGRTNIPLSPTLTTKSPVMKKPMCNFSTNMEIPRAMFHHKPPQGPPPPPPPSCALQKKPLTSEKDPLGILDPIPSKPVNQNPVIINPTSFHSNVHSQVPMMNVSMPPAVVPLPSNLPLPTVKPGHMNHGSHVQRVQHSASTSLSPSPVTSPVHMMGTGIGRIEASPQRSRSSSTSSDHGNFMMPPVGPQATSSGIKVPPRSPRSTIGSPRPSMPSSPSTKSDGHHQYKDIPNPLIAGISNVLNTPSSAAFPTASAGSSSVKSQPGLLGMPLNQILNQHNAASFPASSLLSAAAKAQLANQNKLAGNNSSSSSNSGAVAGSGNTEGHSTLNTMFPPTANMLLPTGEGQSGRAALRDKLMSQQKDALRKRKQPPTTVLSLLRQSQMDSSAVPKPGPDLLRKQGQGSFPISSMSQLLQSMSCQSSHLSSNSTPGCGASNTALPCSANQLHFTDPSMNSSVLQNIPLRGEAVHCHNANTNFVHSNSPVPNHHLAGLINQIQASGNCGMLSQSGMALGNSLHPNPPQSRISTSSTPVIPNSIVSSYNQTSSEAGGSGPSSSIAIAGTNHPAITKTTSVLQDGVIVTTAAGNPLQSQLPIGSDFPFVGQEHALHFPSNSTSNNHLPHPLNPSLLSSLPISLPVNQQHLLNQNLLNILQPSAGEGDMSSINNTLSNHQLTHLQSLLNNNQMFPPNQQQQQLLQGYQNLQAFQGQSTIPCPANNNPMACLFQNFQVRMQED,Methyl-CpG-binding domain protein 5,Binds to heterochromatin. Does not interact with either methylated or unmethylated DNA (in vitro).,The document does not mention any functional changes caused by the mutation.,In MRD1; unknown pathological significance. The document does not mention any functional changes caused by the mutation.
589,589,589,41131,Q13286-N310Q,MGGCAGSRRRFSDSEGEETVPEPRLPLLDHQGAHWKNAVGFWLLGLCNNFSYVVMLSAAHDILSHKRTSGNQSHVDPGPTPIPHNSSSRFDCNSVSTAAVLLADILPTLVIKLLAPLGLHLLPYSPRVLVSGICAAGSFVLVAFSHSVGTSLCGVVFASISSGLGEVTFLSLTAFYPRAVISWWSSGTGGAGLLGALSYLGLTQAGLSPQQTLLSMLGIPALLLASYFLLLTSPEAQDPGGEEEAESAARQPLIRTEAPESKPGSSSSLSLRERWTVFKGLLWYIVPLVVVYFAEYFINQGLFELLFFWQTSLSHAQQYRWYQMLYQAGVFASRSSLRCCRIRFTWALALLQCLNLVFLLADVWFGFLPSIYLVFLIILYEGLLGGAAYVNTFHNIALETSDEHREFAMAATCISDTLGISLSGLLALPLHDFLCQLS,Does not affect glycosylation.,,MGGCAGSRRRFSDSEGEETVPEPRLPLLDHQGAHWKNAVGFWLLGLCNNFSYVVMLSAAHDILSHKRTSGNQSHVDPGPTPIPHNSSSRFDCNSVSTAAVLLADILPTLVIKLLAPLGLHLLPYSPRVLVSGICAAGSFVLVAFSHSVGTSLCGVVFASISSGLGEVTFLSLTAFYPRAVISWWSSGTGGAGLLGALSYLGLTQAGLSPQQTLLSMLGIPALLLASYFLLLTSPEAQDPGGEEEAESAARQPLIRTEAPESKPGSSSSLSLRERWTVFKGLLWYIVPLVVVYFAEYFINQGLFELLFFWNTSLSHAQQYRWYQMLYQAGVFASRSSLRCCRIRFTWALALLQCLNLVFLLADVWFGFLPSIYLVFLIILYEGLLGGAAYVNTFHNIALETSDEHREFAMAATCISDTLGISLSGLLALPLHDFLCQLS,Battenin,"Mediates microtubule-dependent, anterograde transport connecting the Golgi network, endosomes, autophagosomes, lysosomes and plasma membrane, and participates in several cellular processes such as regulation of lysosomal pH, lysosome protein degradation, receptor-mediated endocytosis, autophagy, transport of proteins and lipids from the TGN, apoptosis and synaptic transmission. Facilitates the proteins transport from trans-Golgi network (TGN)-to other membrane compartments such as transport of microdomain-associated proteins to the plasma membrane, IGF2R transport to the lysosome where it regulates the CTSD release leading to regulation of CTSD maturation and thereby APP intracellular processing. Moreover regulates CTSD activity in response to osmotic stress. Also binds galactosylceramide and transports it from the trans Golgi to the rafts, which may have immediate and downstream effects on cell survival by modulating ceramide synthesis. At the plasma membrane, regulates actin-dependent events including filopodia formation, cell migration, and pinocytosis through ARF1-CDC42 pathway and also the cytoskeleton organization through interaction with MYH10 and fodrin leading to the regulation of the plasma membrane association of Na+, K+ ATPase complex. Regulates synaptic transmission in the amygdala, hippocampus, and cerebellum through regulation of synaptic vesicles density and their proximity to active zones leading to modulation of short-term plasticity and age-dependent anxious behavior, learning and memory. Regulates autophagic vacuoles (AVs) maturation by modulating the trafficking between endocytic and autophagolysosomal/lysosomal compartments, which involves vesicle fusion leading to regulation of degradation process. Participates also in cellular homeostasis of compounds such as, water, ions, amino acids, proteins and lipids in several tissue namely in brain and kidney through regulation of their transport and synthesis.",The functional changes caused by the mutation in the CLN3 gene are not mentioned in the document.,Does not affect glycosylation. The functional changes caused by the mutation in the CLN3 gene are not mentioned in the document.
597,597,597,41863,Q9Z1W9-T243Q,MAEPSGSPVHVQLSQQAAPVTAAAATAPAAATSAPAPAPAPAPAASAAPAPAPAAAPAPAPAAQAVGWPICRDAYELQEVIGSGATAVVQAALCKPRQERVAIKRINLEKCQTSMDELLKEIQAMSQCSHPNVVTYYTSFVVKDELWLVMKLLSGGSMLDIIKYIVNRGEHKNGVLEEAIIATILKEVLEGLDYLHRNGQIHRDLKAGNILLGEDGSVQIADFGVSAFLATGGDVTRNKVRKQFVGTPCWMAPEVMEQVRGYDFKADMWSFGITAIELATGAAPYHKYPPMKVLMLTLQNDPPTLETGVEDKEMMKKYGKSFRKLLSLCLQKDPSKRPTAAELLKCKFFQKAKNREYLIEKLLTRTPDIAQRAKKVRRVPGSSGHLHKTEDGDWEWSDDEMDEKSEEGKAAASQEKSRRVKEENSEISVNAGGIPEQIQSLSVHDSQAQPNANEDYREGPCAVNLVLRLRNSRKELNDIRFEFTPGRDTADGVSQELFSAGLVDGHDVVIVAANLQKIVDDPKALKTLTFKLASGCDGSEIPDEVKLIGFAQLSVS,Increased kinase activity and autophosphorylation.,,MAEPSGSPVHVQLSQQAAPVTAAAATAPAAATSAPAPAPAPAPAASAAPAPAPAAAPAPAPAAQAVGWPICRDAYELQEVIGSGATAVVQAALCKPRQERVAIKRINLEKCQTSMDELLKEIQAMSQCSHPNVVTYYTSFVVKDELWLVMKLLSGGSMLDIIKYIVNRGEHKNGVLEEAIIATILKEVLEGLDYLHRNGQIHRDLKAGNILLGEDGSVQIADFGVSAFLATGGDVTRNKVRKTFVGTPCWMAPEVMEQVRGYDFKADMWSFGITAIELATGAAPYHKYPPMKVLMLTLQNDPPTLETGVEDKEMMKKYGKSFRKLLSLCLQKDPSKRPTAAELLKCKFFQKAKNREYLIEKLLTRTPDIAQRAKKVRRVPGSSGHLHKTEDGDWEWSDDEMDEKSEEGKAAASQEKSRRVKEENSEISVNAGGIPEQIQSLSVHDSQAQPNANEDYREGPCAVNLVLRLRNSRKELNDIRFEFTPGRDTADGVSQELFSAGLVDGHDVVIVAANLQKIVDDPKALKTLTFKLASGCDGSEIPDEVKLIGFAQLSVS,STE20/SPS1-related proline-alanine-rich protein kinase,"May act as a mediator of stress-activated signals. Mediates the inhibition of SLC4A4, SLC26A6 as well as CFTR activities by the WNK scaffolds, probably through phosphorylation. Phosphorylates RELT.",,Increased kinase activity and autophosphorylation.
604,604,604,42346,P23064-V330A,MGKFLATLILFFQFCPLILGDYSPSCCTLTIGVSSYHSKPCNPAQPVCSWTLDLLALSADQALQPPCPNLVSYSSYHATYSLYLFPHWIKKPNRNGGGYYSASYSDPCSLKCPYLGCQSWTCPYTGAVSSPYWKFQQDVNFTQEVSRLNINLHFSKCGFPFSLLVDAPGYDPIWFLNTEPSQLPPTAPPLLPHSNLDHILEPSIPWKSKLLTLVQLTLQSTNYTCIVCIDRASLSTWHVLYSPNVSVPSSSSTPLLYPSLALPAPHLTLPFNWTHCFDPQIQAIVSSPCHNSLILPPFSLSPVPTLGSRSRRAVPVAVWLVSALAMGAGAAGGITGSMSLASGKSLLHEVDKDISQLTQAIVKNHKNLLKIAQYAAQNRRGLDLLFWEQGGLCKALQEQCCFLNITNSHVSILQERPPLENRVLTGWGLNWDLGLSQWAREALQTGITLVALLLLVILAGPCILRQLRHLPSRVRYPHYSLINPESSL,30% loss of transmembrane protein cell-cell fusion activity.,,MGKFLATLILFFQFCPLILGDYSPSCCTLTIGVSSYHSKPCNPAQPVCSWTLDLLALSADQALQPPCPNLVSYSSYHATYSLYLFPHWIKKPNRNGGGYYSASYSDPCSLKCPYLGCQSWTCPYTGAVSSPYWKFQQDVNFTQEVSRLNINLHFSKCGFPFSLLVDAPGYDPIWFLNTEPSQLPPTAPPLLPHSNLDHILEPSIPWKSKLLTLVQLTLQSTNYTCIVCIDRASLSTWHVLYSPNVSVPSSSSTPLLYPSLALPAPHLTLPFNWTHCFDPQIQAIVSSPCHNSLILPPFSLSPVPTLGSRSRRAVPVAVWLVSALAMGAGVAGGITGSMSLASGKSLLHEVDKDISQLTQAIVKNHKNLLKIAQYAAQNRRGLDLLFWEQGGLCKALQEQCCFLNITNSHVSILQERPPLENRVLTGWGLNWDLGLSQWAREALQTGITLVALLLLVILAGPCILRQLRHLPSRVRYPHYSLINPESSL,Envelope glycoprotein gp62,"The surface protein (SU) attaches the virus to the host cell by binding to its receptor. This interaction triggers the refolding of the transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide. Fusion occurs at the host cell plasma membrane.The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm.","A substitutions at other positions had smaller effects (G-329, V-330, and G-332) or no effect on fusion function.","30% loss of transmembrane protein cell-cell fusion activity. A substitutions at other positions had smaller effects (G-329, V-330, and G-332) or no effect on fusion function."
605,605,605,42356,Q03103-C150A,MRLRTAIATLCLTAFTSATSNNSYIATDQTQNAFNDTHFCKVDRNDHVSPSCNVTFNELNAINENIRDDLSALLKSDFFKYFRLDLYKQCSFWDANDGLCLNRACSVDVVEDWDTLPEYWQPEILGSFNNDTMKEADDSDDECKFLDQLAQTSKKPVDIEDTINYCDVNDFNGKNAVLIDLTANPERFTGYGGKQAGQIWSTIYQDNCFTIGETGESLAKDAFYRLVSGFHASIGTHLSKEYLNTKTGKWEPNLDLFMARIGNFPDRVTNMYFNYAVVAKALWKIQPYLPEFSFCDLVNKEIKNKMDNVISQLDTKIFNEDLVFANDLSLTLKDEFRSRFKNVTKIMDCVQCDRCRLWGKIQTTGYATALKILFEINDADEFTKQHIVGKLTKYELIALLQTFGRLSESIESVNMFEKMYGKRLNGSENRLSSFFQNNFFNILKEAGKSIRYTIENINSTKEGKKKTNNSQSHVFDDLKMPKAEIVPRPSNGTVNKWKKAWNTEVNNVLEAFRFIYRSYLDLPRNIWELSLMKVYKFWNKFIGVADYVSEETREPISYKLDIQ,Loss of regulatory disulfide bond and strongly increased activity towards PDI; when associated with A-295.,,MRLRTAIATLCLTAFTSATSNNSYIATDQTQNAFNDTHFCKVDRNDHVSPSCNVTFNELNAINENIRDDLSALLKSDFFKYFRLDLYKQCSFWDANDGLCLNRACSVDVVEDWDTLPEYWQPEILGSFNNDTMKEADDSDDECKFLDQLCQTSKKPVDIEDTINYCDVNDFNGKNAVLIDLTANPERFTGYGGKQAGQIWSTIYQDNCFTIGETGESLAKDAFYRLVSGFHASIGTHLSKEYLNTKTGKWEPNLDLFMARIGNFPDRVTNMYFNYAVVAKALWKIQPYLPEFSFCDLVNKEIKNKMDNVISQLDTKIFNEDLVFANDLSLTLKDEFRSRFKNVTKIMDCVQCDRCRLWGKIQTTGYATALKILFEINDADEFTKQHIVGKLTKYELIALLQTFGRLSESIESVNMFEKMYGKRLNGSENRLSSFFQNNFFNILKEAGKSIRYTIENINSTKEGKKKTNNSQSHVFDDLKMPKAEIVPRPSNGTVNKWKKAWNTEVNNVLEAFRFIYRSYLDLPRNIWELSLMKVYKFWNKFIGVADYVSEETREPISYKLDIQ,Endoplasmic oxidoreductin-1,"Essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. Acts by oxidizing directly PDI1 isomerase through a direct disulfide exchange. Does not act as a direct oxidant of folding substrate, but relies on PDI1 to transfer oxidizing equivalent. Also able to oxidize directly the PDI related protein MPD2. Does not oxidize all PDI related proteins, suggesting that it can discriminate between PDI1 and related proteins. Reoxidation of ERO1 probably involves electron transfer to molecular oxygen via FAD. Acts independently of glutathione. May be responsible for a significant proportion of reactive oxygen species (ROS) in the cell, thereby being a source of oxidative stress.","Attenuation of Ero1p activity through noncatalytic cysteine pairs prevents hyperoxidation of the ER, leading to increased enzyme activity, decreased lag phase in kinetic assays, and growth defects in vivo.","Loss of regulatory disulfide bond and strongly increased activity towards PDI; when associated with A-295. Attenuation of Ero1p activity through noncatalytic cysteine pairs prevents hyperoxidation of the ER, leading to increased enzyme activity, decreased lag phase in kinetic assays, and growth defects in vivo."
608,608,608,42529,Q92854-F244N,MRMCTPIRGLLMALAVMFGTAMAFAPIPRITWEHREVHLVQFHEPDIYNYSALLLSEDKDTLYIGAREAVFAVNALNISEKQHEVYWKVSEDKKAKCAEKGKSKQTECLNYIRVLQPLSATSLYVCGTNAFQPACDHLNLTSFKFLGKNEDGKGRCPFDPAHSYTSVMVDGELYSGTSYNFLGSEPIISRNSSHSPLRTEYAIPWLNEPSFVFADVIRKSPDSPDGEDDRVYFFFTEVSVEYENVFRVLIPRIARVCKGDQGGLRTLQKKWTSFLKARLICSRPDSGLVFNVLRDVFVLRSPGLKVPVFYALFTPQLNNVGLSAVCAYNLSTAEEVFSHGKYMQSTTVEQSHTKWVRYNGPVPKPRPGACIDSEARAANYTSSLNLPDKTLQFVKDHPLMDDSVTPIDNRPRLIKKDVNYTQIVVDRTQALDGTVYDVMFVSTDRGALHKAISLEHAVHIIEETQLFQDFEPVQTLLLSSKKGNRFVYAGSNSGVVQAPLAFCGKHGTCEDCVLARDPYCAWSPPTATCVALHQTESPSRGLIQEMSGDASVCPDKSKGSYRQHFFKHGGTAELKCSQKSNLARVFWKFQNGVLKAESPKYGLMGRKNLLIFNLSEGDSGVYQCLSEERVKNKTVFQVVAKHVLEVKVVPKPVVAPTLSVVQTEGSRIATKVLVASTQGSSPPTPAVQATSSGAITLPPKPAPTGTSCEPKIVINTVPQLHSEKTMYLKSSDNRLLMSLFLFFFVLFLCLFFYNCYKGYLPRQCLKFRSALLIGKKKPKSDFCDREQSLKETLVEPGSFSQQNGEHPKPALDTGYETEQDTITSKVPTDREDSQRIDDLSARDKPFDVKCELKFADSDADGD,"Abolishes homodimerization, abolishes collapse of growth cones and reduces PLXNB1 binding; when associated with S-246.",,MRMCTPIRGLLMALAVMFGTAMAFAPIPRITWEHREVHLVQFHEPDIYNYSALLLSEDKDTLYIGAREAVFAVNALNISEKQHEVYWKVSEDKKAKCAEKGKSKQTECLNYIRVLQPLSATSLYVCGTNAFQPACDHLNLTSFKFLGKNEDGKGRCPFDPAHSYTSVMVDGELYSGTSYNFLGSEPIISRNSSHSPLRTEYAIPWLNEPSFVFADVIRKSPDSPDGEDDRVYFFFTEVSVEYEFVFRVLIPRIARVCKGDQGGLRTLQKKWTSFLKARLICSRPDSGLVFNVLRDVFVLRSPGLKVPVFYALFTPQLNNVGLSAVCAYNLSTAEEVFSHGKYMQSTTVEQSHTKWVRYNGPVPKPRPGACIDSEARAANYTSSLNLPDKTLQFVKDHPLMDDSVTPIDNRPRLIKKDVNYTQIVVDRTQALDGTVYDVMFVSTDRGALHKAISLEHAVHIIEETQLFQDFEPVQTLLLSSKKGNRFVYAGSNSGVVQAPLAFCGKHGTCEDCVLARDPYCAWSPPTATCVALHQTESPSRGLIQEMSGDASVCPDKSKGSYRQHFFKHGGTAELKCSQKSNLARVFWKFQNGVLKAESPKYGLMGRKNLLIFNLSEGDSGVYQCLSEERVKNKTVFQVVAKHVLEVKVVPKPVVAPTLSVVQTEGSRIATKVLVASTQGSSPPTPAVQATSSGAITLPPKPAPTGTSCEPKIVINTVPQLHSEKTMYLKSSDNRLLMSLFLFFFVLFLCLFFYNCYKGYLPRQCLKFRSALLIGKKKPKSDFCDREQSLKETLVEPGSFSQQNGEHPKPALDTGYETEQDTITSKVPTDREDSQRIDDLSARDKPFDVKCELKFADSDADGD,Semaphorin-4D,"Cell surface receptor for PLXNB1 and PLXNB2 that plays an important role in cell-cell signaling. Regulates GABAergic synapse development. Promotes the development of inhibitory synapses in a PLXNB1-dependent manner. Modulates the complexity and arborization of developing neurites in hippocampal neurons by activating PLXNB1 and interaction with PLXNB1 mediates activation of RHOA. Promotes the migration of cerebellar granule cells. Plays a role in the immune system; induces B-cells to aggregate and improves their viability (in vitro). Induces endothelial cell migration through the activation of PTK2B/PYK2, SRC, and the phosphatidylinositol 3-kinase-AKT pathway.",,"Abolishes homodimerization, abolishes collapse of growth cones and reduces PLXNB1 binding; when associated with S-246."
629,629,629,43579,Q9N2K0-V81L,MIFAGKAPSNTSTLMKFYSLLLYSLLFSFPFLCHPLPLPSYLHHTINLTHSLLAASNPSLVNNCWLCISLSSSAYTAVPALQTDWATSPISLHLRTSFNSPHLYPPEELIYFLDRSSKTSPDISHQQAAALLRTYLKNLSPYINSTPPIFGPLTTQTTIPVAAPLCISWQRPTGIPLGNLSPSRCSFTLHLRSPTTNINETIGAFQLHITDKPSINTDKLKNISSNYCLGRHLPCISLHPWLSSPCSSDSPPRPSSCLLIPSPENNSERLLVDTRRFLIHHENRTFPSTQLPHQSPLQPLTAAALAGSLGVWVQDTPFSTPSHLFTLHLQFCLAQGLFFLCGSSTYMCLPANWTGTCTLVFLTPKIQFANGTEELPVPLMTPTQQKRVIPLIPLMVGLGLSASTVALGTGIAGISTSVMTFRSLSNDFSASITDISQTLSVLQAQVDSLAAVVLQNRRGLDLLTAEKGGLCIFLNEECCFYLNQSGLVYDNIKKLKDRAQKLANQASNYAEPPWALSNWMSWVLPIVSPLIPIFLLLLFGPCIFRLVSQFIQNRIQAITNHSIRQMFLLTSPQYHPLPQDLPSA,In allele HERV-H19.,,MIFAGKAPSNTSTLMKFYSLLLYSLLFSFPFLCHPLPLPSYLHHTINLTHSLLAASNPSLVNNCWLCISLSSSAYTAVPAVQTDWATSPISLHLRTSFNSPHLYPPEELIYFLDRSSKTSPDISHQQAAALLRTYLKNLSPYINSTPPIFGPLTTQTTIPVAAPLCISWQRPTGIPLGNLSPSRCSFTLHLRSPTTNINETIGAFQLHITDKPSINTDKLKNISSNYCLGRHLPCISLHPWLSSPCSSDSPPRPSSCLLIPSPENNSERLLVDTRRFLIHHENRTFPSTQLPHQSPLQPLTAAALAGSLGVWVQDTPFSTPSHLFTLHLQFCLAQGLFFLCGSSTYMCLPANWTGTCTLVFLTPKIQFANGTEELPVPLMTPTQQKRVIPLIPLMVGLGLSASTVALGTGIAGISTSVMTFRSLSNDFSASITDISQTLSVLQAQVDSLAAVVLQNRRGLDLLTAEKGGLCIFLNEECCFYLNQSGLVYDNIKKLKDRAQKLANQASNYAEPPWALSNWMSWVLPIVSPLIPIFLLLLFGPCIFRLVSQFIQNRIQAITNHSIRQMFLLTSPQYHPLPQDLPSA,HERV-H_2q24.3 provirus ancestral Env polyprotein,"Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. Endogenous envelope proteins may have kept, lost or modified their original function during evolution. This endogenous envelope protein has lost its original fusogenic properties but has immunosuppressive properties in vivo.SU mediates receptor recognition.TM anchors the envelope heterodimer to the viral membrane through one transmembrane domain. The other hydrophobic domain, called fusion peptide, mediates fusion of the viral membrane with the target cell membrane.","The sequencing of the largest envelope gene, HERV-H/env62, This mutation may have functional implications, such as altering the protein's structure or function.","In allele HERV-H19. The sequencing of the largest envelope gene, HERV-H/env62, This mutation may have functional implications, such as altering the protein's structure or function."
635,635,635,43827,P38812-D47N,MNISGTLNTLRLLYNPSLCKPSLVVPTFNDLPIPIHDSIKAVVLDKNNCIAFPHDDKIWPDYLQHWETLRSKYSNKALLIVSNTAGSNSDKDYSQAKLLEDKTGIPVLRHSTKKPGCHNEILDYFYRNKTITNPKEVAVVGDRLFTDILMANLMGSYGVWIRDGVKVSANPLSKFEKKLYNFLGF,Abolishes phosphatase activity and impairs cardiolipin biosynthesis.,,MNISGTLNTLRLLYNPSLCKPSLVVPTFNDLPIPIHDSIKAVVLDKDNCIAFPHDDKIWPDYLQHWETLRSKYSNKALLIVSNTAGSNSDKDYSQAKLLEDKTGIPVLRHSTKKPGCHNEILDYFYRNKTITNPKEVAVVGDRLFTDILMANLMGSYGVWIRDGVKVSANPLSKFEKKLYNFLGF,"Phosphatidylglycerophosphatase GEP4, mitochondrial","Phosphatidylglycerophosphatase involved in the biosynthesis of cardiolipin (CL), a unique dimeric phosphoglycerolipid predominantly present in mitochondrial membranes and which has important functions for cellular energy metabolism, mitochondrial dynamics and the initiation of apoptotic pathways. Required for the stability of respiratory chain supercomplexes and for growth at elevated temperature, in presence of ethidium bromide or in absence of prohibitins.",,Abolishes phosphatase activity and impairs cardiolipin biosynthesis.
642,642,642,44370,Q09573-G602D,MSNARRRFSTVTQINTEGLQAMGKGGGRMETVGEDGIPADYKGNRKFTTSLGHLALYKEDEGIGTQASFISGYTTPGPKERATSEHVKANLGVMLGVYLPTIQHILGVTMFIRLFWVVGMSGVAWTMALLAICCLSTLLTSISLSAVATNGVVESGGAYFIISRNLGAEFGSAVGILFYLANTVAASMYIVGGVEVILMYLWPEMAIGGADALHDTEMFGSLYNNLRLYGTVFLLIQALIVAMGVKFVQLLAPVSLMCVILAIAACIGGGIEKQITMEGMKVCAIDNHLLQSSIVTHPIHKNQTSWFNETVDFCNLCDKSLYLESVFCANVNNDEASAEDDVFCTHYTSKKMTCQLAFPGFNMKTLNDNMWPEYMEKSEVVPGVRGKETAEVVQDESSTFFMLMAIYFPAVTGIFTGTNMSGDLRDPQRSIPVGTIAATLTTSAIYYILAILFGGSITRSVLRDKFGRSIGNTMVVAALSWPHPAVVTVGAFLSTFGAALQCLCSAPRLLQSIAKDDVIPILAPFARVTKNNEPFLGLVLTVIIAECGILLGAVDKIAEVLDFFFLMCYAFVNLIAVLHSVLKSPNWRPRFKYFHWTLSLLDAALCFFIMFASSVPLACIACTATAVIYKYVEWKGAKKEWGDGMRGLALTTAQYSLLKVEDKDPHPKNWRPQVLILLTSQWSKEMIDRRAVSMLNLGAQLKAGRGLAIACAFLKGSVDSQKDKNRARDVKTTLVKDMSSVRLRGFAKTMFYNNHQINGTISGLYQSIGIGGLRPNTILLNWPNEKNPDELVLFAEEIIHGAANDNCLIVTKGITDFPEYSERLTGFIDIWWIVQDGGILMLIAYLLRQHKVWKGCTLRIFAVSEQDSTKSEDMKAGLQKYIYMLRIDAELFIVDLLDMEVSDEVVEKAAEVERKQKEREEMRRSKSGYLNDGFMEDNGKPRQVMMRHSDSARSFSPQPGAHTSINLDETETSFTESLFDDFYRSGTPNEDLEGAMKLNIHKMNTSVRLNRVIRENSPDSQLIL,In nj94; defects in thermotaxis.,,MSNARRRFSTVTQINTEGLQAMGKGGGRMETVGEDGIPADYKGNRKFTTSLGHLALYKEDEGIGTQASFISGYTTPGPKERATSEHVKANLGVMLGVYLPTIQHILGVTMFIRLFWVVGMSGVAWTMALLAICCLSTLLTSISLSAVATNGVVESGGAYFIISRNLGAEFGSAVGILFYLANTVAASMYIVGGVEVILMYLWPEMAIGGADALHDTEMFGSLYNNLRLYGTVFLLIQALIVAMGVKFVQLLAPVSLMCVILAIAACIGGGIEKQITMEGMKVCAIDNHLLQSSIVTHPIHKNQTSWFNETVDFCNLCDKSLYLESVFCANVNNDEASAEDDVFCTHYTSKKMTCQLAFPGFNMKTLNDNMWPEYMEKSEVVPGVRGKETAEVVQDESSTFFMLMAIYFPAVTGIFTGTNMSGDLRDPQRSIPVGTIAATLTTSAIYYILAILFGGSITRSVLRDKFGRSIGNTMVVAALSWPHPAVVTVGAFLSTFGAALQCLCSAPRLLQSIAKDDVIPILAPFARVTKNNEPFLGLVLTVIIAECGILLGAVDKIAEVLDFFFLMCYAFVNLIAVLHSVLKSPNWRPRFKYFHWTLSLLGAALCFFIMFASSVPLACIACTATAVIYKYVEWKGAKKEWGDGMRGLALTTAQYSLLKVEDKDPHPKNWRPQVLILLTSQWSKEMIDRRAVSMLNLGAQLKAGRGLAIACAFLKGSVDSQKDKNRARDVKTTLVKDMSSVRLRGFAKTMFYNNHQINGTISGLYQSIGIGGLRPNTILLNWPNEKNPDELVLFAEEIIHGAANDNCLIVTKGITDFPEYSERLTGFIDIWWIVQDGGILMLIAYLLRQHKVWKGCTLRIFAVSEQDSTKSEDMKAGLQKYIYMLRIDAELFIVDLLDMEVSDEVVEKAAEVERKQKEREEMRRSKSGYLNDGFMEDNGKPRQVMMRHSDSARSFSPQPGAHTSINLDETETSFTESLFDDFYRSGTPNEDLEGAMKLNIHKMNTSVRLNRVIRENSPDSQLIL,Potassium/chloride cotransporter 3,"Probable potassium/chloride cotransporter that functions in the amphid sheath glial cells to regulate thermotaxis behavior. By maintaining chloride homeostasis, negatively regulates guanylate cyclase gcy-8 in the thermosensory AFD neurons and thereby controls the microvilli receptive ending morphology of the AFD neurons and thermotaxis. Modulates the temperature-evoked neuronal activity of the AFD neurons such as calcium responses to temperature gradients. Might also play a role in the chemotaxis behavior mediated by the sensory neurons AWA and AWC.","The mutation in the kcc-3 gene was isolated from a genetic screen for mutants defective in thermotaxis. KCC-3 is expressed and functions in the amphid sheath glia that ensheathes the AFD neuron, a major thermosensory neuron known to be required for thermotaxis. The regulation of the thermosensory behavior by KCC-3 is mediated through AFD, and KCC-3 in the amphid sheath glia regulates the dynamics of the AFD activity.","In nj94; defects in thermotaxis. The mutation in the kcc-3 gene was isolated from a genetic screen for mutants defective in thermotaxis. KCC-3 is expressed and functions in the amphid sheath glia that ensheathes the AFD neuron, a major thermosensory neuron known to be required for thermotaxis. The regulation of the thermosensory behavior by KCC-3 is mediated through AFD, and KCC-3 in the amphid sheath glia regulates the dynamics of the AFD activity."
656,656,656,45169,P31414-E229Q,MVAPALLPELWTEILVPICAVIGIAFSLFQWYVVSRVKLTSDLGASSSGGANNGKNGYGDYLIEEEEGVNDQSVVAKCAEIQTAISEGATSFLFTEYKYVGVFMIFFAAVIFVFLGSVEGFSTDNKPCTYDTTRTCKPALATAAFSTIAFVLGAVTSVLSGFLGMKIATYANARTTLEARKGVGKAFIVAFRSGAVMGFLLAASGLLVLYITINVFKIYYGDDWEGLFQAITGYGLGGSSMALFGRVGGGIYTKAADVGADLVGKIERNIPEDDPRNPAVIADNVGDNVGDIAGMGSDLFGSYAEASCAALVVASISSFGINHDFTAMCYPLLISSMGILVCLITTLFATDFFEIKLVKEIEPALKNQLIISTVIMTVGIAIVSWVGLPTSFTIFNFGTQKVVKNWQLFLCVCVGLWAGLIIGFVTEYYTSNAYSPVQDVADSCRTGAATNVIFGLALGYKSVIIPIFAIAISIFVSFSFAAMYGVAVAALGMLSTIATGLAIDAYGPISDNAGGIAEMAGMSHRIRERTDALDAAGNTTAAIGKGFAIGSAALVSLALFGAFVSRAGIHTVDVLTPKVIIGLLVGAMLPYWFSAMTMKSVGSAALKMVEEVRRQFNTIPGLMEGTAKPDYATCVKISTDASIKEMIPPGCLVMLTPLIVGFFFGVETLSGVLAGSLVSGVQIAISASNTGGAWDNAKKYIEAGVSEHAKSLGPKGSEPHKAAVIGDTIGDPLKDTSGPSLNILIKLMAVESLVFAPFFATHGGILFKYF,Slight reduction of PPi hydrolysis and H(+) translocation.,,MVAPALLPELWTEILVPICAVIGIAFSLFQWYVVSRVKLTSDLGASSSGGANNGKNGYGDYLIEEEEGVNDQSVVAKCAEIQTAISEGATSFLFTEYKYVGVFMIFFAAVIFVFLGSVEGFSTDNKPCTYDTTRTCKPALATAAFSTIAFVLGAVTSVLSGFLGMKIATYANARTTLEARKGVGKAFIVAFRSGAVMGFLLAASGLLVLYITINVFKIYYGDDWEGLFEAITGYGLGGSSMALFGRVGGGIYTKAADVGADLVGKIERNIPEDDPRNPAVIADNVGDNVGDIAGMGSDLFGSYAEASCAALVVASISSFGINHDFTAMCYPLLISSMGILVCLITTLFATDFFEIKLVKEIEPALKNQLIISTVIMTVGIAIVSWVGLPTSFTIFNFGTQKVVKNWQLFLCVCVGLWAGLIIGFVTEYYTSNAYSPVQDVADSCRTGAATNVIFGLALGYKSVIIPIFAIAISIFVSFSFAAMYGVAVAALGMLSTIATGLAIDAYGPISDNAGGIAEMAGMSHRIRERTDALDAAGNTTAAIGKGFAIGSAALVSLALFGAFVSRAGIHTVDVLTPKVIIGLLVGAMLPYWFSAMTMKSVGSAALKMVEEVRRQFNTIPGLMEGTAKPDYATCVKISTDASIKEMIPPGCLVMLTPLIVGFFFGVETLSGVLAGSLVSGVQIAISASNTGGAWDNAKKYIEAGVSEHAKSLGPKGSEPHKAAVIGDTIGDPLKDTSGPSLNILIKLMAVESLVFAPFFATHGGILFKYF,Pyrophosphate-energized vacuolar membrane proton pump 1,"Contributes to the transtonoplast (from cytosol to vacuole lumen) H(+)-electrochemical potential difference. It establishes a proton gradient of similar and often greater magnitude than the H(+)-ATPase on the same membrane. In addition, facilitates auxin transport by modulating apoplastic pH and regulates auxin-mediated developmental processes. Confers tolerance to NaCl and to drought by increasing ion retention.",The proportionate diminution of PPi hydrolytic and H+ translocation activity and conservation of wild type DCCD sensitivity in mutants refute the notion that E229 is the residue whose covalent modification by DCCD is responsible for the abolition of PPi-dependent H+ translocation.,Slight reduction of PPi hydrolysis and H(+) translocation. The proportionate diminution of PPi hydrolytic and H+ translocation activity and conservation of wild type DCCD sensitivity in mutants refute the notion that E229 is the residue whose covalent modification by DCCD is responsible for the abolition of PPi-dependent H+ translocation.
661,661,661,45570,Q5H8A4-R669C,MRLGSGTFATCCVAIEVLGIAVFLRGFFPAPVRSSARAEHGAEPPAPEPSAGASSNWTTLPPPLFSKVVIVLIDALRDDFVFGSKGVKFMPYTTYLVEKGASHSFVAEAKPPTVTMPRIKALMTGSLPGFVDVIRNLNSPALLEDSVIRQAKAAGKRIVFYGDETWVKLFPKHFVEYDGTTSFFVSDYTEVDNNVTRHLDKVLKRGDWDILILHYLGLDHIGHISGPNSPLIGQKLSEMDSVLMKIHTSLQSKERETPLPNLLVLCGDHGMSETGSHGASSTEEVNTPLILISSAFERKPGDIRHPKHVQQTDVAATLAIALGLPIPKDSVGSLLFPVVEGRPMREQLRFLHLNTVQLSKLLQENVPSYEKDPGFEQFKMSERLHGNWIRLYLEEKHSEVLFNLGSKVLRQYLDALKTLSLSLSAQVAQYDIYSMMVGTVVVLEVLTLLLLSVPQALRRKAELEVPLSSPGFSLLFYLVILVLSAVHVIVCTSAESSCYFCGLSWLAAGGVMVLASALLCVIVSVLTNVLVGGNTPRKNPMHPSSRWSELDLLILLGTAGHVLSLGASSFVEEEHQTWYFLVNTLCLALSQETYRNYFLGDDGEPPCGLCVEQGHDGATAAWQDGPGCDVLERDKGHGSPSTSEVLRGREKWMVLASPWLILACCRLLCSLNQTGVQWAHRPDLGHWLTSSDHKAELSVLAALSLLVVFVLVQRGCSPVSKAALALGLLGVYCYRAAIGSVRFPWRPDSKDISKGIIEARFVYVFVLGILFTGTKDLLKSQVIAADFKLKTVGLWEIYSGLVLLAALLFRPHNLPVLAFSLLIQTLMTKFIWKPLRHDAAEITVMHYWFGQAFFYFQGNSNNIATVDISAGFVGLDTYVEIPAVLLTAFGTYAGPVLWASHLVHFLSSETRSGSALSHACFCYALICSIPVFTYIVLVTSLRYHLFIWSVFSPKLLYEGMHLLITAAVCVFFTAMDQTRLTQS,In NEDHSCA; almost complete loss of ethanolamine phosphate transferase activity as evidenced by abnormal accumulation of the GPI precursors H7 and H7' and absence of mature GPI precursor H8 in patient lymphoblasts; does not affect protein expression levels in transfected HEK293 cells.,,MRLGSGTFATCCVAIEVLGIAVFLRGFFPAPVRSSARAEHGAEPPAPEPSAGASSNWTTLPPPLFSKVVIVLIDALRDDFVFGSKGVKFMPYTTYLVEKGASHSFVAEAKPPTVTMPRIKALMTGSLPGFVDVIRNLNSPALLEDSVIRQAKAAGKRIVFYGDETWVKLFPKHFVEYDGTTSFFVSDYTEVDNNVTRHLDKVLKRGDWDILILHYLGLDHIGHISGPNSPLIGQKLSEMDSVLMKIHTSLQSKERETPLPNLLVLCGDHGMSETGSHGASSTEEVNTPLILISSAFERKPGDIRHPKHVQQTDVAATLAIALGLPIPKDSVGSLLFPVVEGRPMREQLRFLHLNTVQLSKLLQENVPSYEKDPGFEQFKMSERLHGNWIRLYLEEKHSEVLFNLGSKVLRQYLDALKTLSLSLSAQVAQYDIYSMMVGTVVVLEVLTLLLLSVPQALRRKAELEVPLSSPGFSLLFYLVILVLSAVHVIVCTSAESSCYFCGLSWLAAGGVMVLASALLCVIVSVLTNVLVGGNTPRKNPMHPSSRWSELDLLILLGTAGHVLSLGASSFVEEEHQTWYFLVNTLCLALSQETYRNYFLGDDGEPPCGLCVEQGHDGATAAWQDGPGCDVLERDKGHGSPSTSEVLRGREKWMVLASPWLILACCRLLRSLNQTGVQWAHRPDLGHWLTSSDHKAELSVLAALSLLVVFVLVQRGCSPVSKAALALGLLGVYCYRAAIGSVRFPWRPDSKDISKGIIEARFVYVFVLGILFTGTKDLLKSQVIAADFKLKTVGLWEIYSGLVLLAALLFRPHNLPVLAFSLLIQTLMTKFIWKPLRHDAAEITVMHYWFGQAFFYFQGNSNNIATVDISAGFVGLDTYVEIPAVLLTAFGTYAGPVLWASHLVHFLSSETRSGSALSHACFCYALICSIPVFTYIVLVTSLRYHLFIWSVFSPKLLYEGMHLLITAAVCVFFTAMDQTRLTQS,GPI ethanolamine phosphate transferase 2,Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the GPI second mannose.,The Japanese individual was compound heterozygous for c. 2005C>T (p. ),In NEDHSCA; almost complete loss of ethanolamine phosphate transferase activity as evidenced by abnormal accumulation of the GPI precursors H7 and H7' and absence of mature GPI precursor H8 in patient lymphoblasts; does not affect protein expression levels in transfected HEK293 cells. The Japanese individual was compound heterozygous for c. 2005C>T (p. )
666,666,666,45812,Q68DH5-Q326E,MSGAALGLEIVFVFFLALFLLHRYGDFKKQHRLVIIGTLLAWYLCFLIVFILPLDVSTTIYNRCKHAAANSSPPENSNITGLYATANPVPSQHPCFKPWSYIPDGIMPIFWRVVYWTSQFLTWILLPFMQSYARSGGFSITGKIKTALIENAIYYGTYLLIFGAFLIYVAVNPHLHLEWNQLQTIGIAAANTWGLFLLVLLLGYGLVEIPRSYWNGAKRGYLLMKTYFKAAKLMTEKADAEENLEDAMEEVRKVNESIKYNHPLRKCVDTILKKCPTEYQEKMGRNMDDYEDFDEKHSIYPSEKSLVKLHKQVIYSVQRHRRTQVEWQILLEQAFYLEDVAKNETSATHQFVHTFQSPEPENRFIQYFYNPTFEWYWECLLRPWFYKILAVVLSIFSVIVVWSECTFFSTTPVLSLFAVFIQLAEKTYNYIYIEIACFLSIFFLSICVYSTVFRIRVFNYYYLASHHQTDAYSLLFSGMLFCRLTPPLCLNFLGLTHMDSSISHKNTQPTAYTSIMGSMKVLSFIADGFYIYYPMLVVILCIATYFSLGTRCLNLLGFQQFMGDDDMTSDLVNEGKELIRKEKRKRQRQEEGENRRREWKERYGHNREDSTRNRNIHTDPKESNFSDVNTNRSAFKYTRANNRTERDRIELLQDAEPLDFNAETFTDDPLESESGRYQPGGRYLSMSRSDIFNDV,In DENBA; unknown pathological significance.,,MSGAALGLEIVFVFFLALFLLHRYGDFKKQHRLVIIGTLLAWYLCFLIVFILPLDVSTTIYNRCKHAAANSSPPENSNITGLYATANPVPSQHPCFKPWSYIPDGIMPIFWRVVYWTSQFLTWILLPFMQSYARSGGFSITGKIKTALIENAIYYGTYLLIFGAFLIYVAVNPHLHLEWNQLQTIGIAAANTWGLFLLVLLLGYGLVEIPRSYWNGAKRGYLLMKTYFKAAKLMTEKADAEENLEDAMEEVRKVNESIKYNHPLRKCVDTILKKCPTEYQEKMGRNMDDYEDFDEKHSIYPSEKSLVKLHKQVIYSVQRHRRTQVQWQILLEQAFYLEDVAKNETSATHQFVHTFQSPEPENRFIQYFYNPTFEWYWECLLRPWFYKILAVVLSIFSVIVVWSECTFFSTTPVLSLFAVFIQLAEKTYNYIYIEIACFLSIFFLSICVYSTVFRIRVFNYYYLASHHQTDAYSLLFSGMLFCRLTPPLCLNFLGLTHMDSSISHKNTQPTAYTSIMGSMKVLSFIADGFYIYYPMLVVILCIATYFSLGTRCLNLLGFQQFMGDDDMTSDLVNEGKELIRKEKRKRQRQEEGENRRREWKERYGHNREDSTRNRNIHTDPKESNFSDVNTNRSAFKYTRANNRTERDRIELLQDAEPLDFNAETFTDDPLESESGRYQPGGRYLSMSRSDIFNDV,G-protein coupled receptor-associated protein LMBRD2,"Recruited to ligand-activated beta-2 adrenergic receptor/ADRB2, it negatively regulates the adrenergic receptor signaling pathway. May also regulate other G-protein coupled receptors including type-1 angiotensin II receptor/AGTR1 (Probable).",,In DENBA; unknown pathological significance.
677,677,677,46463,Q9BV79-R258W,MWVCSTLWRVRTPARQWRGLLPASGCHGPAASSYSASAEPARVRALVYGHHGDPAKVVELKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIPANAGLGTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRDRPDIQKLSDRLKSLGAEHVITEEELRRPEMKNFFKDMPQPWLALNCVGGKSSTELLRQLARGGTMVTYGGMAKQPVVASVSLLIFKDLKLRGFWLSQWKKDHSPDQFKELILTLCDLIRRGQLTAPACSQVPLQDYQSALEASMKPFISSKQILTM,In DYTOABG.,,MWVCSTLWRVRTPARQWRGLLPASGCHGPAASSYSASAEPARVRALVYGHHGDPAKVVELKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIPANAGLGTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRDRPDIQKLSDRLKSLGAEHVITEEELRRPEMKNFFKDMPQPRLALNCVGGKSSTELLRQLARGGTMVTYGGMAKQPVVASVSLLIFKDLKLRGFWLSQWKKDHSPDQFKELILTLCDLIRRGQLTAPACSQVPLQDYQSALEASMKPFISSKQILTM,"Enoyl-[acyl-carrier-protein] reductase, mitochondrial","Catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis (fatty acid synthesis type II). Fatty acid chain elongation in mitochondria uses acyl carrier protein (ACP) as an acyl group carrier, but the enzyme accepts both ACP and CoA thioesters as substrates in vitro. Displays a preference for medium-chain over short- and long-chain substrates. May provide the octanoyl chain used for lipoic acid biosynthesis, regulating protein lipoylation and mitochondrial respiratory activity particularly in Purkinje cells.",The missense mutation in MECR involves a conserved amino acid residue and is located within the cofactor binding domain. It is predicted to have a destabilizing effect.,In DYTOABG. The missense mutation in MECR involves a conserved amino acid residue and is located within the cofactor binding domain. It is predicted to have a destabilizing effect.
686,686,686,47536,Q06102-W70A,MSLIHPDTAKYPFKFEPFLRQEYSFSLDPDRPICEFYNSREGPKSCPRGPLCPKKHVLPIFQNKIVCRHALRGLCKKNDQCEYLHEYNLRKMPECVFFSKNGYCTQSPDCQYLHIDPASKIPKCENYEMGFCPLGSSCPRRHIKKVFCQRYMTGFCPLGKDECDMEHPQFIIPDEGSKLRIKRDDEINTRKMDEEKERRLNAIINGEV,Temperature- and formamide-sensitive; abolishes cleavage and polyadenylation activity.,,MSLIHPDTAKYPFKFEPFLRQEYSFSLDPDRPICEFYNSREGPKSCPRGPLCPKKHVLPIFQNKIVCRHWLRGLCKKNDQCEYLHEYNLRKMPECVFFSKNGYCTQSPDCQYLHIDPASKIPKCENYEMGFCPLGSSCPRRHIKKVFCQRYMTGFCPLGKDECDMEHPQFIIPDEGSKLRIKRDDEINTRKMDEEKERRLNAIINGEV,mRNA 3'-end-processing protein YTH1,"RNA-binding component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB.",,Temperature- and formamide-sensitive; abolishes cleavage and polyadenylation activity.
690,690,690,47938,O60391-L472P,MEFVRALWLGLALALGPGSAGGHPQPCGVLARLGGSVRLGALLPRAPLARARARAALARAALAPRLPHNLSLELVVAAPPARDPASLTRGLCQALVPPGVAALLAFPEARPELLQLHFLAAATETPVLSLLRREARAPLGAPNPFHLQLHWASPLETLLDVLVAVLQAHAWEDVGLALCRTQDPGGLVALWTSRAGRPPQLVLDLSRRDTGDAGLRARLAPMAAPVGGEAPVPAAVLLGCDIARARRVLEAVPPGPHWLLGTPLPPKALPTAGLPPGLLALGEVARPPLEAAIHDIVQLVARALGSAAQVQPKRALLPAPVNCGDLQPAGPESPGRFLARFLANTSFQGRTGPVWVTGSSQVHMSRHFKVWSLRRDPRGAPAWATVGSWRDGQLDLEPGGASARPPPPQGAQVWPKLRVVTLLEHPFVFARDPDEDGQCPAGQLCLDPGTNDSATLDALFAALANGSAPRAPRKCCYGYCIDLLERLAEDTPFDFELYLVGDGKYGALRDGRWTGLVGDLLAGRAHMAVTSFSINSARSQVVDFTSPFFSTSLGIMVRARDTASPIGAFMWPLHWSTWLGVFAALHLTALFLTVYEWRSPYGLTPRGRNRSTVFSYSSALNLCYAILFRRTVSSKTPKCPTGRLLMNLWAIFCLLVLSSYTANLAAVMVGDKTFEELSGIHDPKLHHPAQGFRFGTVWESSAEAYIKKSFPDMHAHMRRHSAPTTPRGVAMLTSDPPKLNAFIMDKSLLDYEVSIDADCKLLTVGKPFAIEGYGIGLPQNSPLTSNLSEFISRYKSSGFIDLLHDKWYKMVPCGKRVFAVTETLQMSIYHFAGLFVLLCLGLGSALLSSLGEHAFFRLALPRIRKGSRLQYWLHTSQKIHRALNTEPPEGSKEETAEAEPSGPEVEQQQQQQDQPTAPEGWKRARRAVDKERRVRFLLEPAVVVAPEADAEAEAAPREGPVWLCSYGRPPAARPTGAPQPGELQELERRIEVARERLRQALVRRGQLLAQLGDSARHRPRRLLQ,Found in a patient with autism spectrum disorder; unknown pathological significance.,,MEFVRALWLGLALALGPGSAGGHPQPCGVLARLGGSVRLGALLPRAPLARARARAALARAALAPRLPHNLSLELVVAAPPARDPASLTRGLCQALVPPGVAALLAFPEARPELLQLHFLAAATETPVLSLLRREARAPLGAPNPFHLQLHWASPLETLLDVLVAVLQAHAWEDVGLALCRTQDPGGLVALWTSRAGRPPQLVLDLSRRDTGDAGLRARLAPMAAPVGGEAPVPAAVLLGCDIARARRVLEAVPPGPHWLLGTPLPPKALPTAGLPPGLLALGEVARPPLEAAIHDIVQLVARALGSAAQVQPKRALLPAPVNCGDLQPAGPESPGRFLARFLANTSFQGRTGPVWVTGSSQVHMSRHFKVWSLRRDPRGAPAWATVGSWRDGQLDLEPGGASARPPPPQGAQVWPKLRVVTLLEHPFVFARDPDEDGQCPAGQLCLDPGTNDSATLDALFAALANGSAPRALRKCCYGYCIDLLERLAEDTPFDFELYLVGDGKYGALRDGRWTGLVGDLLAGRAHMAVTSFSINSARSQVVDFTSPFFSTSLGIMVRARDTASPIGAFMWPLHWSTWLGVFAALHLTALFLTVYEWRSPYGLTPRGRNRSTVFSYSSALNLCYAILFRRTVSSKTPKCPTGRLLMNLWAIFCLLVLSSYTANLAAVMVGDKTFEELSGIHDPKLHHPAQGFRFGTVWESSAEAYIKKSFPDMHAHMRRHSAPTTPRGVAMLTSDPPKLNAFIMDKSLLDYEVSIDADCKLLTVGKPFAIEGYGIGLPQNSPLTSNLSEFISRYKSSGFIDLLHDKWYKMVPCGKRVFAVTETLQMSIYHFAGLFVLLCLGLGSALLSSLGEHAFFRLALPRIRKGSRLQYWLHTSQKIHRALNTEPPEGSKEETAEAEPSGPEVEQQQQQQDQPTAPEGWKRARRAVDKERRVRFLLEPAVVVAPEADAEAEAAPREGPVWLCSYGRPPAARPTGAPQPGELQELERRIEVARERLRQALVRRGQLLAQLGDSARHRPRRLLQ,"Glutamate receptor ionotropic, NMDA 3B","NMDA receptor subtype of glutamate-gated ion channels with reduced single-channel conductance, low calcium permeability and low voltage-dependent sensitivity to magnesium. Mediated by glycine.",,Found in a patient with autism spectrum disorder; unknown pathological significance.
698,698,698,48216,Q92838-P118L,MGYPEVERRELLPAAAPRERGSQGCGCGGAPARAGEGNSCLLFLGFFGLSLALHLLTLCCYLELRSELRRERGAESRLGGSGTPGTSGTLSSLGGLDPDSPITSHLGQPSPKQQPLELGEAALHSDSQDGHQMALLNFFFPDEKPYSEEESRRVRRNKRSKSNEGADGPVKNKKKGKKAGPPGPNGPPGPPGPPGPQGPPGIPGIPGIPGTTVMGPPGPPGPPGPQGPPGLQGPSGAADKAGTRENQPAVVHLQGQGSAIQVKNDLSGGVLNDWSRITMNPKVFKLHPRSGELEVLVDGTYFIYSQVEVYYINFTDFASYEVVVDEKPFLQCTRSIETGKTNYNTCYTAGVCLLKARQKIAVKMVHADISINMSKHTTFFGAIRLGEAPAS,In a colorectal cancer sample; somatic mutation.,,MGYPEVERRELLPAAAPRERGSQGCGCGGAPARAGEGNSCLLFLGFFGLSLALHLLTLCCYLELRSELRRERGAESRLGGSGTPGTSGTLSSLGGLDPDSPITSHLGQPSPKQQPLEPGEAALHSDSQDGHQMALLNFFFPDEKPYSEEESRRVRRNKRSKSNEGADGPVKNKKKGKKAGPPGPNGPPGPPGPPGPQGPPGIPGIPGIPGTTVMGPPGPPGPPGPQGPPGLQGPSGAADKAGTRENQPAVVHLQGQGSAIQVKNDLSGGVLNDWSRITMNPKVFKLHPRSGELEVLVDGTYFIYSQVEVYYINFTDFASYEVVVDEKPFLQCTRSIETGKTNYNTCYTAGVCLLKARQKIAVKMVHADISINMSKHTTFFGAIRLGEAPAS,Ectodysplasin-A,"Cytokine which is involved in epithelial-mesenchymal signaling during morphogenesis of ectodermal organs. Functions as a ligand activating the DEATH-domain containing receptors EDAR and EDA2R. May also play a role in cell adhesion.Binds only to the receptor EDAR, while isoform 3 binds exclusively to the receptor EDA2R.Binds only to the receptor EDA2R.",,In a colorectal cancer sample; somatic mutation.
702,702,702,48468,P29965-M36R,MIETYNQTSPRSAATGLPISMKIFMYLLTVFLITQRIGSALFAVYLHRRLDKIEDERNLHEDFVFMKTIQRCNTGERSLSLLNCEEIKSQFEGFVKDIMLNKEETKKENSFEMQKGDQNPQIAAHVISEASSKTTSVLQWAEKGYYTMSNNLVTLENGKQLTVKRQGLYYIYAQVTFCSNREASSQAPFIASLCLKSPGRFERILLRAANTHSSAKPCGQQSIHLGGVFELQPGASVFVNVTDPSQVSHGTGFTSFGLLKL,In HIGM1.,,MIETYNQTSPRSAATGLPISMKIFMYLLTVFLITQMIGSALFAVYLHRRLDKIEDERNLHEDFVFMKTIQRCNTGERSLSLLNCEEIKSQFEGFVKDIMLNKEETKKENSFEMQKGDQNPQIAAHVISEASSKTTSVLQWAEKGYYTMSNNLVTLENGKQLTVKRQGLYYIYAQVTFCSNREASSQAPFIASLCLKSPGRFERILLRAANTHSSAKPCGQQSIHLGGVFELQPGASVFVNVTDPSQVSHGTGFTSFGLLKL,CD40 ligand,"Cytokine that acts as a ligand to CD40/TNFRSF5. Costimulates T-cell proliferation and cytokine production. Its cross-linking on T-cells generates a costimulatory signal which enhances the production of IL4 and IL10 in conjunction with the TCR/CD3 ligation and CD28 costimulation. Induces the activation of NF-kappa-B. Induces the activation of kinases MAPK8 and PAK2 in T-cells. Induces tyrosine phosphorylation of isoform 3 of CD28. Mediates B-cell proliferation in the absence of co-stimulus as well as IgE production in the presence of IL4. Involved in immunoglobulin class switching.Acts as a ligand for integrins, specifically ITGA5:ITGB1 and ITGAV:ITGB3; both integrins and the CD40 receptor are required for activation of CD40-CD40LG signaling, which have cell-type dependent effects, such as B-cell activation, NF-kappa-B signaling and anti-apoptotic signaling.",The mutation affects the CD40 ligand protein.,In HIGM1. The mutation affects the CD40 ligand protein.
706,706,706,48856,P32485-W320R,MTTNEEFIRTQIFGTVFEITNRYNDLNPVGMGAFGLVCSATDTLTSQPVAIKKIMKPFSTAVLAKRTYRELKLLKHLRHENLICLQDIFLSPLEDIYFVTELQGTDLHRLLQTRPLEKQFVQYFLYQILRGLKYVHSAGVIHRDLKPSNILINENCDLKICDFGLARIQDPQMTGYVSTRYYRAPEIMLTWQKYDVEVDIWSAGCIFAEMIEGKPLFPGKDHVHQFSIITDLLGSPPKDVINTICSENTLKFVTSLPHRDPIPFSERFKTVEPDAVDLLEKMLVFDPKKRITAADALAHPYSAPYHDPTDEPVADAKFDRHFNDADLPVDTWRVMMYSEILDFHKIGGSDGQIDISATFDDQVAAATAAAAQAQAQAQAQVQLNMAAHSHNGAGTTGNDHSDIAGGNKVSDHVAANDTITDYGNQAIQYANEFQQ,"Activates HOG1 in a constitutive manner, without the need of a stimulating stress.",,MTTNEEFIRTQIFGTVFEITNRYNDLNPVGMGAFGLVCSATDTLTSQPVAIKKIMKPFSTAVLAKRTYRELKLLKHLRHENLICLQDIFLSPLEDIYFVTELQGTDLHRLLQTRPLEKQFVQYFLYQILRGLKYVHSAGVIHRDLKPSNILINENCDLKICDFGLARIQDPQMTGYVSTRYYRAPEIMLTWQKYDVEVDIWSAGCIFAEMIEGKPLFPGKDHVHQFSIITDLLGSPPKDVINTICSENTLKFVTSLPHRDPIPFSERFKTVEPDAVDLLEKMLVFDPKKRITAADALAHPYSAPYHDPTDEPVADAKFDWHFNDADLPVDTWRVMMYSEILDFHKIGGSDGQIDISATFDDQVAAATAAAAQAQAQAQAQVQLNMAAHSHNGAGTTGNDHSDIAGGNKVSDHVAANDTITDYGNQAIQYANEFQQ,Mitogen-activated protein kinase HOG1,"Mitogen-activated protein kinase involved in a signal transduction pathway that is activated by changes in the osmolarity of the extracellular environment. Controls osmotic regulation of transcription via the stress response element (STRE) in promoters of target genes. Upon osmotic shock, associates with the SKO1-SSN6-TUP1 complex, phosphorylates SKO1, and converts it into an activator that subsequently recruits Swi/Snf and SAGA complexes. Activates the SMP1 transcription factor and the RCK2 kinase, both also involved in the regulation of the expression of a subset of osmotic stress-related genes. Phosphorylation of HSL1 by HOG1 leads to a G2 arrest essential for cell survival at high osmolarity. Mediates also cell-cycle arrest in G1 phase by the dual targeting of SIC1. Regulates MFA2 ARE-mediated translation in response to carbon source. Targets RPD3 histone deacetylase to osmoresponsive promoters to induce gene expression on stress. Required for the Golgi apparatus localization of MNN1. Plays an essential role in maintaining water homeostasis, arsenite detoxification, copper-resistance, cold-resistance, hydrogen peroxide response, adaptation to citric acid stress, and repression of the mating pathway activity. Functions as an arsenic sensor and effector via direct binding to arsenic and subsequent phosphorylation of the ARR1 transcription factor.",The mutation in the conserved L16 domain of the Hog1 protein results in a hyperactive and MAPKK-independent variant of the MAPK Hog1.,"Activates HOG1 in a constitutive manner, without the need of a stimulating stress. The mutation in the conserved L16 domain of the Hog1 protein results in a hyperactive and MAPKK-independent variant of the MAPK Hog1."
735,735,735,50877,Q68CP4-P311L,MTGARASAAEQRRAGRSGQARAAERAAGMSGAGRALAALLLAASVLSAALLAPGGSSGRDAQAAPPRDLDKKRHAELKMDQALLLIHNELLWTNLTVYWKSECCYHCLFQVLVNVPQSPKAGKPSAAAASVSTQHGSILQLNDTLEEKEVCRLEYRFGEFGNYSLLVKNIHNGVSEIACDLAVNEDPVDSNLPVSIAFLIGLAVIIVISFLRLLLSLDDFNNWISKAISSRETDRLINSELGSPSRTDPLDGDVQPATWRLSALPPRLRSVDTFRGIALILMVFVNYGGGKYWYFKHASWNGLTVADLVFLWFVFIMGSSIFLSMTSILQRGCSKFRLLGKIAWRSFLLICIGIIIVNPNYCLGPLSWDKVRIPGVLQRLGVTYFVVAVLELLFAKPVPEHCASERSCLSLRDITSSWPQWLLILVLEGLWLGLTFLLPVPGCPTGYLGPGGIGDFGKYPNCTGGAAGYIDRLLLGDDHLYQHPSSAVLYHTEVAYDPEGILGTINSIVMAFLGVQAGKILLYYKARTKDILIRFTAWCCILGLISVALTKVSENEGFIPVNKNLWSLSYVTTLSSFAFFILLVLYPVVDVKGLWTGTPFFYPGMNSILVYVGHEVFENYFPFQWKLKDNQSHKEHLTQNIVATALWVLIAYILYRKKIFWKI,In MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum.,,MTGARASAAEQRRAGRSGQARAAERAAGMSGAGRALAALLLAASVLSAALLAPGGSSGRDAQAAPPRDLDKKRHAELKMDQALLLIHNELLWTNLTVYWKSECCYHCLFQVLVNVPQSPKAGKPSAAAASVSTQHGSILQLNDTLEEKEVCRLEYRFGEFGNYSLLVKNIHNGVSEIACDLAVNEDPVDSNLPVSIAFLIGLAVIIVISFLRLLLSLDDFNNWISKAISSRETDRLINSELGSPSRTDPLDGDVQPATWRLSALPPRLRSVDTFRGIALILMVFVNYGGGKYWYFKHASWNGLTVADLVFPWFVFIMGSSIFLSMTSILQRGCSKFRLLGKIAWRSFLLICIGIIIVNPNYCLGPLSWDKVRIPGVLQRLGVTYFVVAVLELLFAKPVPEHCASERSCLSLRDITSSWPQWLLILVLEGLWLGLTFLLPVPGCPTGYLGPGGIGDFGKYPNCTGGAAGYIDRLLLGDDHLYQHPSSAVLYHTEVAYDPEGILGTINSIVMAFLGVQAGKILLYYKARTKDILIRFTAWCCILGLISVALTKVSENEGFIPVNKNLWSLSYVTTLSSFAFFILLVLYPVVDVKGLWTGTPFFYPGMNSILVYVGHEVFENYFPFQWKLKDNQSHKEHLTQNIVATALWVLIAYILYRKKIFWKI,Heparan-alpha-glucosaminide N-acetyltransferase,"Lysosomal acetyltransferase that acetylates the non-reducing terminal alpha-glucosamine residue of intralysosomal heparin or heparan sulfate, converting it into a substrate for luminal alpha-N-acetyl glucosaminidase.",The mutation in the HGSNAT gene affects the structure and function of the enzyme.,In MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum. The mutation in the HGSNAT gene affects the structure and function of the enzyme.
751,751,751,52377,O95786-K154R,MTTEQRRSLQAFQDYIRKTLDPTYILSYMAPWFREEEVQYIQAEKNNKGPMEAATLFLKFLLELQEEGWFRGFLDALDHAGYSGLYEAIESWDFKKIEKLEEYRLLLKRLQPEFKTRIIPTDIISDLSECLINQECEEILQICSTKGMMAGAERLVECLLRSDKENWPKTLKLALEKERNKFSELWIVEKGIKDVETEDLEDKMETSDIQIFYQEDPECQNLSENSCPPSEVSDTNLYSPFKPRNYQLELALPAMKGKNTIICAPTGCGKTFVSLLICEHHLKKFPQGQKGKVVFFANQIPVYEQQKSVFSKYFERHGYRVTGISGATAENVPVEQIVENNDIIILTPQILVNNLKKGTIPSLSIFTLMIFDECHNTSKQHPYNMIMFNYLDQKLGGSSGPLPQVIGLTASVGVGDAKNTDEALDYICKLCASLDASVIATVKHNLEELEQVVYKPQKFFRKVESRISDKFKYIIAQLMRDTESLAKRICKDLENLSQIQNREFGTQKYEQWIVTVQKACMVFQMPDKDEESRICKALFLYTSHLRKYNDALIISEHARMKDALDYLKDFFSNVRAAGFDEIEQDLTQRFEEKLQELESVSRDPSNENPKLEDLCFILQEEYHLNPETITILFVKTRALVDALKNWIEGNPKLSFLKPGILTGRGKTNQNTGMTLPAQKCILDAFKASGDHNILIATSVADEGIDIAQCNLVILYEYVGNVIKMIQTRGRGRARGSKCFLLTSNAGVIEKEQINMYKEKMMNDSILRLQTWDEAVFREKILHIQTHEKFIRDSQEKPKPVPDKENKKLLCRKCKALACYTADVRVIEECHYTVLGDAFKECFVSRPHPKPKQFSSFEKRAKIFCARQNCSHDWGIHVKYKTFEIPVIKIESFVVEDIATGVQTLYSKWKDFHFEKIPFDPAEMSK,Reduction of ubiquitination. Reduction of INFB induction.,,MTTEQRRSLQAFQDYIRKTLDPTYILSYMAPWFREEEVQYIQAEKNNKGPMEAATLFLKFLLELQEEGWFRGFLDALDHAGYSGLYEAIESWDFKKIEKLEEYRLLLKRLQPEFKTRIIPTDIISDLSECLINQECEEILQICSTKGMMAGAEKLVECLLRSDKENWPKTLKLALEKERNKFSELWIVEKGIKDVETEDLEDKMETSDIQIFYQEDPECQNLSENSCPPSEVSDTNLYSPFKPRNYQLELALPAMKGKNTIICAPTGCGKTFVSLLICEHHLKKFPQGQKGKVVFFANQIPVYEQQKSVFSKYFERHGYRVTGISGATAENVPVEQIVENNDIIILTPQILVNNLKKGTIPSLSIFTLMIFDECHNTSKQHPYNMIMFNYLDQKLGGSSGPLPQVIGLTASVGVGDAKNTDEALDYICKLCASLDASVIATVKHNLEELEQVVYKPQKFFRKVESRISDKFKYIIAQLMRDTESLAKRICKDLENLSQIQNREFGTQKYEQWIVTVQKACMVFQMPDKDEESRICKALFLYTSHLRKYNDALIISEHARMKDALDYLKDFFSNVRAAGFDEIEQDLTQRFEEKLQELESVSRDPSNENPKLEDLCFILQEEYHLNPETITILFVKTRALVDALKNWIEGNPKLSFLKPGILTGRGKTNQNTGMTLPAQKCILDAFKASGDHNILIATSVADEGIDIAQCNLVILYEYVGNVIKMIQTRGRGRARGSKCFLLTSNAGVIEKEQINMYKEKMMNDSILRLQTWDEAVFREKILHIQTHEKFIRDSQEKPKPVPDKENKKLLCRKCKALACYTADVRVIEECHYTVLGDAFKECFVSRPHPKPKQFSSFEKRAKIFCARQNCSHDWGIHVKYKTFEIPVIKIESFVVEDIATGVQTLYSKWKDFHFEKIPFDPAEMSK,Antiviral innate immune response receptor RIG-I,"Innate immune receptor that senses cytoplasmic viral nucleic acids and activates a downstream signaling cascade leading to the production of type I interferons and pro-inflammatory cytokines. Forms a ribonucleoprotein complex with viral RNAs on which it homooligomerizes to form filaments. The homooligomerization allows the recruitment of RNF135 an E3 ubiquitin-protein ligase that activates and amplifies the RIG-I-mediated antiviral signaling in an RNA length-dependent manner through ubiquitination-dependent and -independent mechanisms. Upon activation, associates with mitochondria antiviral signaling protein (MAVS/IPS1) that activates the IKK-related kinases TBK1 and IKBKE which in turn phosphorylate the interferon regulatory factors IRF3 and IRF7, activating transcription of antiviral immunological genes including the IFN-alpha and IFN-beta interferons. Ligands include 5'-triphosphorylated ssRNAs and dsRNAs but also short dsRNAs (<1 kb in length). In addition to the 5'-triphosphate moiety, blunt-end base pairing at the 5'-end of the RNA is very essential. Overhangs at the non-triphosphorylated end of the dsRNA RNA have no major impact on its activity. A 3'overhang at the 5'triphosphate end decreases and any 5'overhang at the 5' triphosphate end abolishes its activity. Detects both positive and negative strand RNA viruses including members of the families Paramyxoviridae: Human respiratory syncytial virus and measles virus (MeV), Rhabdoviridae: vesicular stomatitis virus (VSV), Orthomyxoviridae: influenza A and B virus, Flaviviridae: Japanese encephalitis virus (JEV), hepatitis C virus (HCV), dengue virus (DENV) and west Nile virus (WNV). It also detects rotaviruses and reoviruses. Detects and binds to SARS-CoV-2 RNAs which is inhibited by m6A RNA modifications (Ref.67). Also involved in antiviral signaling in response to viruses containing a dsDNA genome such as Epstein-Barr virus (EBV). Detects dsRNA produced from non-self dsDNA by RNA polymerase III, such as Epstein-Barr virus-encoded RNAs (EBERs). May play important roles in granulocyte production and differentiation, bacterial phagocytosis and in the regulation of cell migration.",The K154 residue of the RIG-I CARD domain is critical for efficient REUL-mediated ubiquitination and the ability of RIG-I to induce activation of IFN-beta promoter.,Reduction of ubiquitination. Reduction of INFB induction. The K154 residue of the RIG-I CARD domain is critical for efficient REUL-mediated ubiquitination and the ability of RIG-I to induce activation of IFN-beta promoter.
752,752,752,52427,O15479-E61K,MPRGQKSKLRAREKRRKARDETRGLNVPQVTEAEEEEAPCCSSSVSGGAASSSPAAGIPQKPQRAPTTAAAAAAGVSSTKSKKGAKSHQGEKNASSSQASTSTKSPSEDPLTRKSGSLVQFLLYKYKIKKSVTKGEMLKIVGKRFREHFPEILKKASEGLSVVFGLELNKVNPNGHTYTFIDKVDLTDEESLLSSWDFPRRKLLMPLLGVIFLNGNSATEEEIWEFLNMLGVYDGEEHSVFGEPWKLITKDLVQEKYLEYKQVPSSDPPRFQFLWGPRAYAETSKMKVLEFLAKVNGTTPCAFPTHYEEALKDEEKAGV,,,MPRGQKSKLRAREKRRKARDETRGLNVPQVTEAEEEEAPCCSSSVSGGAASSSPAAGIPQEPQRAPTTAAAAAAGVSSTKSKKGAKSHQGEKNASSSQASTSTKSPSEDPLTRKSGSLVQFLLYKYKIKKSVTKGEMLKIVGKRFREHFPEILKKASEGLSVVFGLELNKVNPNGHTYTFIDKVDLTDEESLLSSWDFPRRKLLMPLLGVIFLNGNSATEEEIWEFLNMLGVYDGEEHSVFGEPWKLITKDLVQEKYLEYKQVPSSDPPRFQFLWGPRAYAETSKMKVLEFLAKVNGTTPCAFPTHYEEALKDEEKAGV,Melanoma-associated antigen B2,May enhance ubiquitin ligase activity of RING-type zinc finger-containing E3 ubiquitin-protein ligases. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex.,"This mutation may have functional implications in tumor recognition, cancer therapy, and autoimmune diseases.","This mutation may have functional implications in tumor recognition, cancer therapy, and autoimmune diseases."
778,778,778,54261,Q9ZJ12-Y118A,MSETATWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLFPFETRFVGPGHSQGINLYLMTSPEYHMKRLLAAGCGPVFQLCRSFRNEEMGRHHNPEFTMLEWARPHYDMYRLMNEVDDLLQQVLDCQPAESLSYQQAFQRHLEIDPLSADKTQLREAAAKLDLSNIADTEEDRDTLLQLLFTMGVEPHIGKEKPTFIYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQQPIDQNLLDALAAGLPDCSGVALGVDRLVMLALGAESLADVIAFTVDRA,No effect on activity.,,MSETATWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLFPFETRFVGPGHSQGINLYLMTSPEYHMKRLLAAGCGPVFQLCRSFRNEEMGRHHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCQPAESLSYQQAFQRHLEIDPLSADKTQLREAAAKLDLSNIADTEEDRDTLLQLLFTMGVEPHIGKEKPTFIYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQQPIDQNLLDALAAGLPDCSGVALGVDRLVMLALGAESLADVIAFTVDRA,Elongation factor P--,"With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34' (Probable). Can also use L-alpha-lysine as a substrate, but probably with lower efficiency. Cannot aminoacylate tRNA(Lys) with lysine.","The mutation in the poxA gene leads to attenuated virulence in mice, increased ability to respire under nutrient-limiting conditions, hypersusceptibility to diverse growth inhibitors, and altered expression of multiple proteins.","No effect on activity. The mutation in the poxA gene leads to attenuated virulence in mice, increased ability to respire under nutrient-limiting conditions, hypersusceptibility to diverse growth inhibitors, and altered expression of multiple proteins."
797,797,797,55554,Q13496-K255A,MASASTSKYNSHSLENESIKRTSRDGVNRDLTEAVPRLPGETLITDKEVIYICPFNGPIKGRVYITNYRLYLRSLETDSSLILDVPLGVISRIEKMGGATSRGENSYGLDITCKDMRNLRFALKQEGHSRRDMFEILTRYAFPLAHSLPLFAFLNEEKFNVDGWTVYNPVEEYRRQGLPNHHWRITFINKCYELCDTYPALLVVPYRASDDDLRRVATFRSRNRIPVLSWIHPENKTVIVRCSQPLVGMSGKRNADDEKYLDVIRETNKQISKLTIYDARPSVNAVANKATGGGYESDDAYHNAELFFLDIHNIHVMRESLKKVKDIVYPNVEESHWLSSLESTHWLEHIKLVLTGAIQVADKVSSGKSSVLVHCSDGWDRTAQLTSLAMLMLDSFYRSIEGFEILVQKEWISFGHKFASRIGHGDKNHTDADRSPIFLQFIDCVWQMSKQFPTAFEFNEQFLIIILDHLYSCRFGTFLFNCESARERQKVTERTVSLWSLINSNKEKFKNPFYTKEINRVLYPVASMRHLELWVNYYIRWNPRIKQQQPNPVEQRYMELLALRDEYIKRLEELQLANSAKLSDPPTSPSSPSQMMPHVQTHF,Disrupts interaction with DES.,,MASASTSKYNSHSLENESIKRTSRDGVNRDLTEAVPRLPGETLITDKEVIYICPFNGPIKGRVYITNYRLYLRSLETDSSLILDVPLGVISRIEKMGGATSRGENSYGLDITCKDMRNLRFALKQEGHSRRDMFEILTRYAFPLAHSLPLFAFLNEEKFNVDGWTVYNPVEEYRRQGLPNHHWRITFINKCYELCDTYPALLVVPYRASDDDLRRVATFRSRNRIPVLSWIHPENKTVIVRCSQPLVGMSGKRNKDDEKYLDVIRETNKQISKLTIYDARPSVNAVANKATGGGYESDDAYHNAELFFLDIHNIHVMRESLKKVKDIVYPNVEESHWLSSLESTHWLEHIKLVLTGAIQVADKVSSGKSSVLVHCSDGWDRTAQLTSLAMLMLDSFYRSIEGFEILVQKEWISFGHKFASRIGHGDKNHTDADRSPIFLQFIDCVWQMSKQFPTAFEFNEQFLIIILDHLYSCRFGTFLFNCESARERQKVTERTVSLWSLINSNKEKFKNPFYTKEINRVLYPVASMRHLELWVNYYIRWNPRIKQQQPNPVEQRYMELLALRDEYIKRLEELQLANSAKLSDPPTSPSSPSQMMPHVQTHF,Myotubularin,"Lipid phosphatase which dephosphorylates phosphatidylinositol 3-monophosphate (PI3P) and phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2). Has also been shown to dephosphorylate phosphotyrosine- and phosphoserine-containing peptides. Negatively regulates EGFR degradation through regulation of EGFR trafficking from the late endosome to the lysosome. Plays a role in vacuolar formation and morphology. Regulates desmin intermediate filament assembly and architecture. Plays a role in mitochondrial morphology and positioning. Required for skeletal muscle maintenance but not for myogenesis. In skeletal muscles, stabilizes MTMR12 protein levels.",,Disrupts interaction with DES.
800,800,800,55867,Q39232-H65R,MGAYETEKPTKDAAALETQSPEDFDQPSPLRKIISVASIAAGVQFGWALQLSLLTPYVQLLGIPRKWSSLIWLCGPVSGMIVQPIVGFHSDRCRSKFGRRRPFIATGAALVAVAVFLIGYAADFGYKMGDKLEEKVKVRAIGIFALGFWILDVANNTLQGPCRAFLADLAAGDAKRTRVANAFFSFFMAVGNVLGYAAGSYTNLHKMFPFTMTKACDIYCANLKTCFFLSITLLLIVTVTSLWYVNDKQWSPPPRNADDDEKTSSVPLFGEIFGAFKVMKRPMWMLLIVTALNWIAWFPFLLFDTDWMGREVFGGDSDGNERSKKLYSLGVQSGAMGLMFNSIVLGFMSLGVEWIGRKLGGAKRLWGIVNFILAAGLAMTVLVTKFAEDHRKTAGDLAGPSASVKAGALSLFAVLGIPLAITFSTPFALASIFSSCSGAGQGLSLGVLNLAIVIPQMIVSLGGGPFDALFGGGNLPAFIVAAIAAAISGVLALTVLPSPPPDAPKATTMGGFH,"Enhanced sucrose transport activity, reduced sensitivity to DEPC.",,MGAYETEKPTKDAAALETQSPEDFDQPSPLRKIISVASIAAGVQFGWALQLSLLTPYVQLLGIPHKWSSLIWLCGPVSGMIVQPIVGFHSDRCRSKFGRRRPFIATGAALVAVAVFLIGYAADFGYKMGDKLEEKVKVRAIGIFALGFWILDVANNTLQGPCRAFLADLAAGDAKRTRVANAFFSFFMAVGNVLGYAAGSYTNLHKMFPFTMTKACDIYCANLKTCFFLSITLLLIVTVTSLWYVNDKQWSPPPRNADDDEKTSSVPLFGEIFGAFKVMKRPMWMLLIVTALNWIAWFPFLLFDTDWMGREVFGGDSDGNERSKKLYSLGVQSGAMGLMFNSIVLGFMSLGVEWIGRKLGGAKRLWGIVNFILAAGLAMTVLVTKFAEDHRKTAGDLAGPSASVKAGALSLFAVLGIPLAITFSTPFALASIFSSCSGAGQGLSLGVLNLAIVIPQMIVSLGGGPFDALFGGGNLPAFIVAAIAAAISGVLALTVLPSPPPDAPKATTMGGFH,Sucrose transport protein SUC1,"Responsible for the transport of sucrose into the cell, with the concomitant uptake of protons (symport system). This transport is both voltage- and energy-dependent. Can also transport other glucosides such as maltose, alpha-phenylglucoside and beta-phenylglucoside. May also transport biotin. Required for normal pollen germination and anthocyanin accumulation induced by sucrose.",The mutant transports sucrose at significantly higher rates than the wild-type symporter.,"Enhanced sucrose transport activity, reduced sensitivity to DEPC. The mutant transports sucrose at significantly higher rates than the wild-type symporter."
805,805,805,56418,P25724-S336L,MFRSNLEGSGAAAVGVANPPSLAQSGKIFQLQDNFSAFHARGGLNILGLQDMYLDTSGANSSATLSPPITPVTPDPSTSAQSTHFPFLADSAATANSLLMQRQYHYHLLLQQQQQLAMAQHQLALAASAAAASASHQQTDEIARSLKIFAQVTTGAAENAAGSMQDVMQEFATNGYASDDLGRMSYGSAPPQVQMPPQQQHQQQQGLHLPLGRNPAQLQTNGGNLMPIPLATHWLNNYREHLNNVWRNMSYIPAAPNTMGLQAQTAATVSTNLGVGMGLGLPVQGEQLRGASNSSNNNNNNNKVYKRYNSKAKEISRHCVFCENNNEPEAVINSHLVRDNFNRVLCPKLRTYVCPICGASGDSAHTIKYCPKKPIITMEDAIKAESFRLAKSSYYKQQMKV,Strong defects in abdomen and oogenesis.,,MFRSNLEGSGAAAVGVANPPSLAQSGKIFQLQDNFSAFHARGGLNILGLQDMYLDTSGANSSATLSPPITPVTPDPSTSAQSTHFPFLADSAATANSLLMQRQYHYHLLLQQQQQLAMAQHQLALAASAAAASASHQQTDEIARSLKIFAQVTTGAAENAAGSMQDVMQEFATNGYASDDLGRMSYGSAPPQVQMPPQQQHQQQQGLHLPLGRNPAQLQTNGGNLMPIPLATHWLNNYREHLNNVWRNMSYIPAAPNTMGLQAQTAATVSTNLGVGMGLGLPVQGEQLRGASNSSNNNNNNNKVYKRYNSKAKEISRHCVFCENNNEPEAVINSHSVRDNFNRVLCPKLRTYVCPICGASGDSAHTIKYCPKKPIITMEDAIKAESFRLAKSSYYKQQMKV,Protein nanos,"Maternal RNA-binding protein that is required for germ cells proliferation and self-renewal. Acts by forming a complex with pum and brat that regulates translation and mRNA stability. The complex binds to the Nanos Response Element (NRE), a 16 bp sequence in the hb mRNA 3'-UTR and prevents its translation. Controls posterior development. Rescuing factor for the abdominal defect of posterior group mutants. The other posterior group genes are not required for nanos function but rather play a role in localization or distribution of nanos protein.",,Strong defects in abdomen and oogenesis.
833,833,833,57977,Q9BXA5-R252A,MLGIMAWNATCKNWLAAEAALEKYYLSIFYGIEFVVGVLGNTIVVYGYIFSLKNWNSSNIYLFNLSVSDLAFLCTLPMLIRSYANGNWIYGDVLCISNRYVLHANLYTSILFLTFISIDRYLIIKYPFREHLLQKKEFAILISLAIWVLVTLELLPILPLINPVITDNGTTCNDFASSGDPNYNLIYSMCLTLLGFLIPLFVMCFFYYKIALFLKQRNRQVATALPLEKPLNLVIMAVVIFSVLFTPYHVMANVRIASRLGSWKQYQCTQVVINSFYIVTRPLAFLNSVINPVFYFLLGDHFRDMLMNQLRHNFKSLTSFSRWAHELLLSFREK,Abolishes activation by succinate.,,MLGIMAWNATCKNWLAAEAALEKYYLSIFYGIEFVVGVLGNTIVVYGYIFSLKNWNSSNIYLFNLSVSDLAFLCTLPMLIRSYANGNWIYGDVLCISNRYVLHANLYTSILFLTFISIDRYLIIKYPFREHLLQKKEFAILISLAIWVLVTLELLPILPLINPVITDNGTTCNDFASSGDPNYNLIYSMCLTLLGFLIPLFVMCFFYYKIALFLKQRNRQVATALPLEKPLNLVIMAVVIFSVLFTPYHVMRNVRIASRLGSWKQYQCTQVVINSFYIVTRPLAFLNSVINPVFYFLLGDHFRDMLMNQLRHNFKSLTSFSRWAHELLLSFREK,Succinate receptor 1,Receptor for succinate.,,Abolishes activation by succinate.
835,835,835,58158,P56962-G264L,MSEDEEKVKLRRLEPAIQKFIKIVIPTDLERLRKHQINIEKYQRCRIWDKLHEEHINAGRTVQQLRSNIREIEKLCLKVRKDDLVLLKRMIDPVKEEASAATAEFLQLHLESVEELKKQFNDEETLLQPPLTRSMTVGGAFHTTEAEASSQSLTQIYALPEIPQDQNAAESWETLEADLIELSQLVTDFSLLVNSQQEKIDSIADHVNSAAVNVEEGTKNLGKAAKYKLAALPVAGALIGGMVGGPIGLLAGFKVAGIAAALGLGVLGFTGGKLIQRKKQKMMEKLTSSCPDLPSQTDKKCS,Alters localization to the autophagosome; when associated with Leu-268.,,MSEDEEKVKLRRLEPAIQKFIKIVIPTDLERLRKHQINIEKYQRCRIWDKLHEEHINAGRTVQQLRSNIREIEKLCLKVRKDDLVLLKRMIDPVKEEASAATAEFLQLHLESVEELKKQFNDEETLLQPPLTRSMTVGGAFHTTEAEASSQSLTQIYALPEIPQDQNAAESWETLEADLIELSQLVTDFSLLVNSQQEKIDSIADHVNSAAVNVEEGTKNLGKAAKYKLAALPVAGALIGGMVGGPIGLLAGFKVAGIAAALGGGVLGFTGGKLIQRKKQKMMEKLTSSCPDLPSQTDKKCS,Syntaxin-17,"SNAREs, soluble N-ethylmaleimide-sensitive factor-attachment protein receptors, are essential proteins for fusion of cellular membranes. SNAREs localized on opposing membranes assemble to form a trans-SNARE complex, an extended, parallel four alpha-helical bundle that drives membrane fusion. STX17 is a SNARE of the autophagosome involved in autophagy through the direct control of autophagosome membrane fusion with the lysosome membrane. May also play a role in the early secretory pathway where it may maintain the architecture of the endoplasmic reticulum-Golgi intermediate compartment/ERGIC and Golgi and/or regulate transport between the endoplasmic reticulum, the ERGIC and the Golgi.","The mutation in syntaxin 17 causes a disruption in its association with the autophagosomal membrane, leading to accumulation of autophagosomes without degradation.","Alters localization to the autophagosome; when associated with Leu-268. The mutation in syntaxin 17 causes a disruption in its association with the autophagosomal membrane, leading to accumulation of autophagosomes without degradation."
864,864,864,60517,K7LSB9-G49A,MVKCFDFFLSLNFGKMTKLLVWRTDKPQDDMPQTPNSQVTIVSRDHPRAGNY,No effect on alkalinization activity.,,MVKCFDFFLSLNFGKMTKLLVWRTDKPQDDMPQTPNSQVTIVSRDHPRGGNY,Protein PROPEP914,"Produces a rapid alkalinization of the cellular media and the induction of defense-related genes, including chitinase 1b, chalcone synthase and CYP93A1. Not active in tobacco or Arabidopsis. The receptor for GmPep914 is probably different from the receptor for GmSubPep.","The peptide GmPep914, which contains the mutation , is capable of alkalinizing the media of soybean suspension cells, a response that is generally associated with defense peptides.","No effect on alkalinization activity. The peptide GmPep914, which contains the mutation , is capable of alkalinizing the media of soybean suspension cells, a response that is generally associated with defense peptides."
867,867,867,60730,Q8NB78-R151A,MATPRGRTKKKASFDHSPDSLPLRSSGRQAKKKATETTDEDEDGGSEKKYRKCEKAGCTATCPVCFASASERCAKNGYTSRWYHLSCGEHFCNECFDHYYRSHKDGYDKYTTWKKIWTSNGKTEPSPKAFMADQQLPYWVQCTKPECRKWAQLTKEIQLTPQIAKTYRCGMKPNTAIKPETSDHCSLPEDLRVLEVSNHWWYSMLILPPLLKDSVAAPLLSAYYPDCVGMSPSCTSTNRAAATGNASPGKLEHSKAALSVHVPGMNRYFQPFYQPNECGKALCVRPDVMELDELYEFPEYSRDPTMYLALRNLILALWYTNCKEALTPQKCIPHIIVRGLVRIRCVQEVERILYFMTRKGLINTGVLSVGADQYLLPKDYHNKSVIIIGAGPAGLAAARQLHNFGIKVTVLEAKDRIGGRVWDDKSFKGVTVGRGAQIVNGCINNPVALMCEQLGISMHKFGERCDLIQEGGRITDPTIDKRMDFHFNALLDVVSEWRKDKTQLQDVPLGEKIEEIYKAFIKESGIQFSELEGQVLQFHLSNLEYACGSNLHQVSARSWDHNEFFAQFAGDHTLLTPGYSVIIEKLAEGLDIQLKSPVQCIDYSGDEVQVTTTDGTGYSAQKVLVTVPLALLQKGAIQFNPPLSEKKMKAINSLGAGIIEKIALQFPYRFWDSKVQGADFFGHVPPSASKRGLFAVFYDMDPQKKHSVLMSVIAGEAVASVRTLDDKQVLQQCMATLRELFKEQEVPDPTKYFVTRWSTDPWIQMAYSFVKTGGSGEAYDIIAEDIQGTVFFAGEATNRHFPQTVTGAYLSGVREASKIAAF,Loss of demethylase activity.,,MATPRGRTKKKASFDHSPDSLPLRSSGRQAKKKATETTDEDEDGGSEKKYRKCEKAGCTATCPVCFASASERCAKNGYTSRWYHLSCGEHFCNECFDHYYRSHKDGYDKYTTWKKIWTSNGKTEPSPKAFMADQQLPYWVQCTKPECRKWRQLTKEIQLTPQIAKTYRCGMKPNTAIKPETSDHCSLPEDLRVLEVSNHWWYSMLILPPLLKDSVAAPLLSAYYPDCVGMSPSCTSTNRAAATGNASPGKLEHSKAALSVHVPGMNRYFQPFYQPNECGKALCVRPDVMELDELYEFPEYSRDPTMYLALRNLILALWYTNCKEALTPQKCIPHIIVRGLVRIRCVQEVERILYFMTRKGLINTGVLSVGADQYLLPKDYHNKSVIIIGAGPAGLAAARQLHNFGIKVTVLEAKDRIGGRVWDDKSFKGVTVGRGAQIVNGCINNPVALMCEQLGISMHKFGERCDLIQEGGRITDPTIDKRMDFHFNALLDVVSEWRKDKTQLQDVPLGEKIEEIYKAFIKESGIQFSELEGQVLQFHLSNLEYACGSNLHQVSARSWDHNEFFAQFAGDHTLLTPGYSVIIEKLAEGLDIQLKSPVQCIDYSGDEVQVTTTDGTGYSAQKVLVTVPLALLQKGAIQFNPPLSEKKMKAINSLGAGIIEKIALQFPYRFWDSKVQGADFFGHVPPSASKRGLFAVFYDMDPQKKHSVLMSVIAGEAVASVRTLDDKQVLQQCMATLRELFKEQEVPDPTKYFVTRWSTDPWIQMAYSFVKTGGSGEAYDIIAEDIQGTVFFAGEATNRHFPQTVTGAYLSGVREASKIAAF,Lysine-specific histone demethylase 2,"Histone demethylase that demethylates 'Lys-4' of histone H3, a specific tag for epigenetic transcriptional activation, thereby acting as a corepressor. Required for de novo DNA methylation of a subset of imprinted genes during oogenesis. Acts by oxidizing the substrate by FAD to generate the corresponding imine that is subsequently hydrolyzed. Demethylates both mono- and di-methylated 'Lys-4' of histone H3. Has no effect on tri-methylated 'Lys-4', mono-, di- or tri-methylated 'Lys-9', mono-, di- or tri-methylated 'Lys-27', mono-, di- or tri-methylated 'Lys-36' of histone H3, or on mono-, di- or tri-methylated 'Lys-20' of histone H4. Alone, it is unable to demethylate H3K4me on nucleosomes and requires the presence of GLYR1 to achieve such activity, they form a multifunctional enzyme complex that modifies transcribed chromatin and facilitates Pol II transcription through nucleosomes.","The N-terminal zinc-finger domain, composed of a novel C4H2C2-type zinc finger and a specific CW-type zinc finger, is required for demethylase activity and, surprisingly, the binding of cofactor flavin adenine dinucleotide (FAD). In fact, a relay of extensive interactions through the zinc finger-SWIRM-oxidase domains is required for LSD2 demethylase activity and the binding of FAD.","Loss of demethylase activity. The N-terminal zinc-finger domain, composed of a novel C4H2C2-type zinc finger and a specific CW-type zinc finger, is required for demethylase activity and, surprisingly, the binding of cofactor flavin adenine dinucleotide (FAD). In fact, a relay of extensive interactions through the zinc finger-SWIRM-oxidase domains is required for LSD2 demethylase activity and the binding of FAD."
874,874,874,61721,Q7TQQ0-C179S,MGALNQTRVTEFIFLGLTDNWVLEILFFVPFTVTYMLTLLGNFLIVVTIVFTPRLHNPMYFFLSNLSFIDICHSSVTVPKMLEGLLLERKTISFDNCIAQLFFLHLFACSEIFLLTIMAYDRYVAICIPLHYSNVMNMKVCVQLVFALWLGGTIHSLVQTFLTIRLPYCGPNIIDSYFSDVPPVIKLACTDTYLTGILIVSNSGTISLVCFLALVTSYTVILFSLRKQSAEGRRKALSTCSAHFMVVALFFGPCIFLYTRPDSSFSIDKVVSVFYTVVTPLLNPLIYTLRNEEVKTAMKHLRQRRICS,"No receptor activity in response to MTMT binding, even in the presence of copper. Little to no expression detected on plasma membrane.",,MGALNQTRVTEFIFLGLTDNWVLEILFFVPFTVTYMLTLLGNFLIVVTIVFTPRLHNPMYFFLSNLSFIDICHSSVTVPKMLEGLLLERKTISFDNCIAQLFFLHLFACSEIFLLTIMAYDRYVAICIPLHYSNVMNMKVCVQLVFALWLGGTIHSLVQTFLTIRLPYCGPNIIDSYFCDVPPVIKLACTDTYLTGILIVSNSGTISLVCFLALVTSYTVILFSLRKQSAEGRRKALSTCSAHFMVVALFFGPCIFLYTRPDSSFSIDKVVSVFYTVVTPLLNPLIYTLRNEEVKTAMKHLRQRRICS,Olfactory receptor 4E2,Olfactory receptor that is activated by the binding of organosulfur odorants with thioether groups such as (methylthio)methanethiol (MTMT) and bis(methylthiomethyl) disulfide. Also binds odorants cis-cyclooctene and tert-butyl mercaptan. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase (Potential).,The mutation in the MOR244-3 receptor affects its activation towards MTMT and other sulfur compounds.,"No receptor activity in response to MTMT binding, even in the presence of copper. Little to no expression detected on plasma membrane. The mutation in the MOR244-3 receptor affects its activation towards MTMT and other sulfur compounds."
879,879,879,62133,P07902-V44M,MSRSGTDPQQRQQASEADAAAATFRANDHQHIRYNPLQDEWVLMSAHRMKRPWQGQVEPQLLKTVPRHDPLNPLCPGAIRANGEVNPQYDSTFLFDNDFPALQPDAPSPGPSDHPLFQAKSARGVCKVMCFHPWSDVTLPLMSVPEIRAVVDAWASVTEELGAQYPWVQIFENKGAMMGCSNPHPHCQVWASSFLPDIAQREERSQQAYKSQHGEPLLMEYSRQELLRKERLVLTSEHWLVLVPFWATWPYQTLLLPRRHVRRLPELTPAERDDLASIMKKLLTKYDNLFETSFPYSMGWHGAPTGSEAGANWNHWQLHAHYYPPLLRSATVRKFMVGYEMLAQAQRDLTPEQAAERLRALPEVHYHLGQKDRETATIA,In GALAC1; reduced enzyme activity.,,MSRSGTDPQQRQQASEADAAAATFRANDHQHIRYNPLQDEWVLVSAHRMKRPWQGQVEPQLLKTVPRHDPLNPLCPGAIRANGEVNPQYDSTFLFDNDFPALQPDAPSPGPSDHPLFQAKSARGVCKVMCFHPWSDVTLPLMSVPEIRAVVDAWASVTEELGAQYPWVQIFENKGAMMGCSNPHPHCQVWASSFLPDIAQREERSQQAYKSQHGEPLLMEYSRQELLRKERLVLTSEHWLVLVPFWATWPYQTLLLPRRHVRRLPELTPAERDDLASIMKKLLTKYDNLFETSFPYSMGWHGAPTGSEAGANWNHWQLHAHYYPPLLRSATVRKFMVGYEMLAQAQRDLTPEQAAERLRALPEVHYHLGQKDRETATIA,Galactose-1-phosphate uridylyltransferase,Plays an important role in galactose metabolism.,The mutation leads to a drastic reduction in GALT activity when individual mutant cDNAs were overexpressed in a mammalian cell system.,In GALAC1; reduced enzyme activity. The mutation leads to a drastic reduction in GALT activity when individual mutant cDNAs were overexpressed in a mammalian cell system.
882,882,882,62231,Q96DC9-N226A,MSETSFNLISEKCDILSILRDHPENRIYRRKIEELSKRFTAIRKTKGDGNCFYRALGYSYLESLLGKSREIFKFKERVLQTPNDLLAAGFEEHKFRNFFNAFYSVVELVEKDGSVSSLLKVFNDQSASDHIVQFLRLLTSAFIRNRADFFRHFIDEEMDIKDFCTHEVEPMATECDHIQITALSQALSIALQVEYVDEMDTALNHHVFPEAATPSVYLLYKTSHYAILYAADKH,Abolishes deubiquitinase activity.,,MSETSFNLISEKCDILSILRDHPENRIYRRKIEELSKRFTAIRKTKGDGNCFYRALGYSYLESLLGKSREIFKFKERVLQTPNDLLAAGFEEHKFRNFFNAFYSVVELVEKDGSVSSLLKVFNDQSASDHIVQFLRLLTSAFIRNRADFFRHFIDEEMDIKDFCTHEVEPMATECDHIQITALSQALSIALQVEYVDEMDTALNHHVFPEAATPSVYLLYKTSHYNILYAADKH,Ubiquitin thioesterase OTUB2,"Hydrolase that can remove conjugated ubiquitin from proteins in vitro and may therefore play an important regulatory role at the level of protein turnover by preventing degradation. Mediates deubiquitination of 'Lys-11'-,'Lys-48'- and 'Lys-63'-linked polyubiquitin chains, with a preference for 'Lys-63'-linked polyubiquitin chains.",,Abolishes deubiquitinase activity.
892,892,892,62934,Q86YS6-T82E,MAGPGPGPGDPDEQYDFLFKLVLVGDASVGKTCVVQRFKTGAFSERQGSTIGVDFTMKTLEIQGKRVKLQIWDTAGQERFREITQSYYRSANGAILAYDITKRSSFLSVPHWIEDVRKYAGSNIVQLLIGNKSDLSELREVSLAEAQSLAEHYDILCAIETSAKDSSNVEEAFLRVATELIMRHGGPLFSEKSPDHIQLNSKDIGEGWGCGC,"Phosphomimetic mutant. Loss of binding to GDI1, GDI2, CHM and CHML.",,MAGPGPGPGDPDEQYDFLFKLVLVGDASVGKTCVVQRFKTGAFSERQGSTIGVDFTMKTLEIQGKRVKLQIWDTAGQERFRTITQSYYRSANGAILAYDITKRSSFLSVPHWIEDVRKYAGSNIVQLLIGNKSDLSELREVSLAEAQSLAEHYDILCAIETSAKDSSNVEEAFLRVATELIMRHGGPLFSEKSPDHIQLNSKDIGEGWGCGC,Ras-related protein Rab-43,"The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. The low intrinsic GTPase activity of RAB43 is activated by USP6NL. Involved in retrograde transport from the endocytic pathway to the Golgi apparatus. Involved in the transport of Shiga toxin from early and recycling endosomes to the trans-Golgi network. Required for the structural integrity of the Golgi complex. Plays a role in the maturation of phagosomes that engulf pathogens, such as S.aureus and M.tuberculosis.",,"Phosphomimetic mutant. Loss of binding to GDI1, GDI2, CHM and CHML."
893,893,893,63000,P07332-V743M,MGFSSELCSPQGHGVLQQMQEAELRLLEGMRKWMAQRVKSDREYAGLLHHMSLQDSGGQSRAISPDSPISQSWAEITSQTEGLSRLLRQHAEDLNSGPLSKLSLLIRERQQLRKTYSEQWQQLQQELTKTHSQDIEKLKSQYRALARDSAQAKRKYQEASKDKDRDKAKDKYVRSLWKLFAHHNRYVLGVRAAQLHHQHHHQLLLPGLLRSLQDLHEEMACILKEILQEYLEISSLVQDEVVAIHREMAAAAARIQPEAEYQGFLRQYGSAPDVPPCVTFDESLLEEGEPLEPGELQLNELTVESVQHTLTSVTDELAVATEMVFRRQEMVTQLQQELRNEEENTHPRERVQLLGKRQVLQEALQGLQVALCSQAKLQAQQELLQTKLEHLGPGEPPPVLLLQDDRHSTSSSEQEREGGRTPTLEILKSHISGIFRPKFSLPPPLQLIPEVQKPLHEQLWYHGAIPRAEVAELLVHSGDFLVRESQGKQEYVLSVLWDGLPRHFIIQSLDNLYRLEGEGFPSIPLLIDHLLSTQQPLTKKSGVVLHRAVPKDKWVLNHEDLVLGEQIGRGNFGEVFSGRLRADNTLVAVKSCRETLPPDLKAKFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVMELVQGGDFLTFLRTEGARLRVKTLLQMVGDAAAGMEYLESKCCIHRDLAARNCLVTEKNVLKISDFGMSREEADGVYAASGGLRQVPVKWTAPEALNYGRYSSESDMWSFGILLWETFSLGASPYPNLSNQQTREFVEKGGRLPCPELCPDAVFRLMEQCWAYEPGQRPSFSTIYQELQSIRKRHR,Strongly reduced autophosphorylation and kinase activity.,,MGFSSELCSPQGHGVLQQMQEAELRLLEGMRKWMAQRVKSDREYAGLLHHMSLQDSGGQSRAISPDSPISQSWAEITSQTEGLSRLLRQHAEDLNSGPLSKLSLLIRERQQLRKTYSEQWQQLQQELTKTHSQDIEKLKSQYRALARDSAQAKRKYQEASKDKDRDKAKDKYVRSLWKLFAHHNRYVLGVRAAQLHHQHHHQLLLPGLLRSLQDLHEEMACILKEILQEYLEISSLVQDEVVAIHREMAAAAARIQPEAEYQGFLRQYGSAPDVPPCVTFDESLLEEGEPLEPGELQLNELTVESVQHTLTSVTDELAVATEMVFRRQEMVTQLQQELRNEEENTHPRERVQLLGKRQVLQEALQGLQVALCSQAKLQAQQELLQTKLEHLGPGEPPPVLLLQDDRHSTSSSEQEREGGRTPTLEILKSHISGIFRPKFSLPPPLQLIPEVQKPLHEQLWYHGAIPRAEVAELLVHSGDFLVRESQGKQEYVLSVLWDGLPRHFIIQSLDNLYRLEGEGFPSIPLLIDHLLSTQQPLTKKSGVVLHRAVPKDKWVLNHEDLVLGEQIGRGNFGEVFSGRLRADNTLVAVKSCRETLPPDLKAKFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVMELVQGGDFLTFLRTEGARLRVKTLLQMVGDAAAGMEYLESKCCIHRDLAARNCLVTEKNVLKISDFGMSREEADGVYAASGGLRQVPVKWTAPEALNYGRYSSESDVWSFGILLWETFSLGASPYPNLSNQQTREFVEKGGRLPCPELCPDAVFRLMEQCWAYEPGQRPSFSTIYQELQSIRKRHR,Tyrosine-protein kinase Fes/Fps,"Tyrosine-protein kinase that acts downstream of cell surface receptors and plays a role in the regulation of the actin cytoskeleton, microtubule assembly, cell attachment and cell spreading. Plays a role in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Acts down-stream of the activated FCER1 receptor and the mast/stem cell growth factor receptor KIT. Plays a role in the regulation of mast cell degranulation. Plays a role in the regulation of cell differentiation and promotes neurite outgrowth in response to NGF signaling. Plays a role in cell scattering and cell migration in response to HGF-induced activation of EZR. Phosphorylates BCR and down-regulates BCR kinase activity. Phosphorylates HCLS1/HS1, PECAM1, STAT3 and TRIM28.",The mutation in the Fps/Fes protein kinase domain results in inactivation of Fps/Fes. The mutation substantially reduced Fes autophosphorylation and STAT3 Y-705 phosphorylation compared with wild-type Fes.,Strongly reduced autophosphorylation and kinase activity. The mutation in the Fps/Fes protein kinase domain results in inactivation of Fps/Fes. The mutation substantially reduced Fes autophosphorylation and STAT3 Y-705 phosphorylation compared with wild-type Fes.
900,900,900,63787,P77718-K321R,MKFIIKLFPEITIKSQSVRLRFIKILTGNIRNVLKHYDETLAVVRHWDNIEVRAKDENQRLAIRDALTRIPGIHHILEVEDVPFTDMHDIFEKALVQYRDQLEGKTFCVRVKRRGKHDFSSIDVERYVGGGLNQHIESARVKLTNPDVTVHLEVEDDRLLLIKGRYEGIGGFPIGTQEDVLSLISGGFDSGVSSYMLMRRGCRVHYCFFNLGGAAHEIGVRQVAHYLWNRFGSSHRVRFVAINFEPVVGEILEKIDDGQMGVILKRMMVRAASKVAERYGVQALVTGEALGQVSSQTLTNLRLIDNVSDTLILRPLISYDREHIINLARQIGTEDFARTMPEYCGVISKSPTVKAVKSKIEAEEEKFDFSILDKVVEEANNVDIREIAQQTEQEVVEVETVNGFGPNDVILDIRSIDEQEDKPLKVEGIDVVSLPFYKLSTKFGDLDQNKTWLLWCERGVMSRLQALYLREQGFNNVKVYRP,Approximately half of wild-type activity.,,MKFIIKLFPEITIKSQSVRLRFIKILTGNIRNVLKHYDETLAVVRHWDNIEVRAKDENQRLAIRDALTRIPGIHHILEVEDVPFTDMHDIFEKALVQYRDQLEGKTFCVRVKRRGKHDFSSIDVERYVGGGLNQHIESARVKLTNPDVTVHLEVEDDRLLLIKGRYEGIGGFPIGTQEDVLSLISGGFDSGVSSYMLMRRGCRVHYCFFNLGGAAHEIGVRQVAHYLWNRFGSSHRVRFVAINFEPVVGEILEKIDDGQMGVILKRMMVRAASKVAERYGVQALVTGEALGQVSSQTLTNLRLIDNVSDTLILRPLISYDKEHIINLARQIGTEDFARTMPEYCGVISKSPTVKAVKSKIEAEEEKFDFSILDKVVEEANNVDIREIAQQTEQEVVEVETVNGFGPNDVILDIRSIDEQEDKPLKVEGIDVVSLPFYKLSTKFGDLDQNKTWLLWCERGVMSRLQALYLREQGFNNVKVYRP,tRNA sulfurtransferase,"Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS.","Further scrutiny of sequence data and the crystal structures of two members of the PPi synthetase family implicated K321 in the proposed adenylation function of ThiI, and the critical nature of K321 has been demonstrated by site-directed mutagenesis and genetic screening.","Approximately half of wild-type activity. Further scrutiny of sequence data and the crystal structures of two members of the PPi synthetase family implicated K321 in the proposed adenylation function of ThiI, and the critical nature of K321 has been demonstrated by site-directed mutagenesis and genetic screening."
910,910,910,64804,P18054-Q261R,MGRYRIRVATGAWLFSGSYNRVQLWLVGTRGEAELELQLRPARGEEEEFDHDVAEDLGLLQFVRLRKHHWLVDDAWFCDRITVQGPGACAEVAFPCYRWVQGEDILSLPEGTARLPGDNALDMFQKHREKELKDRQQIYCWATWKEGLPLTIAADRKDDLPPNMRFHEEKRLDFEWTLKAGALEMALKRVYTLLSSWNCLEDFDQIFWGQKSALAEKVRQCWQDDELFSYQFLNGANPMLLRRSTSLPSRLVLPSGMEELRAQLEKELQNGSLFEADFILLDGIPANVIRGEKQYLAAPLVMLKMEPNGKLQPMVIQIQPPNPSSPTPTLFLPSDPPLAWLLAKSWVRNSDFQLHEIQYHLLNTHLVAEVIAVATMRCLPGLHPIFKFLIPHIRYTMEINTRARTQLISDGGIFDKAVSTGGGGHVQLLRRAAAQLTYCSLCPPDDLADRGLLGLPGALYAHDALRLWEIIARYVEGIVHLFYQRDDIVKGDPELQAWCREITEVGLCQAQDRGFPVSFQSQSQLCHFLTMCVFTCTAQHAAINQGQLDWYAWVPNAPCTMRMPPPTTKEDVTMATVMGSLPDVRQACLQMAISWHLSRRQPDMVPLGHHKEKYFSGPKPKAVLNQFRTDLEKLEKEITARNEQLDWPYEYLKPSCIENSVTI,Does not affect lipoxygenase activity.,,MGRYRIRVATGAWLFSGSYNRVQLWLVGTRGEAELELQLRPARGEEEEFDHDVAEDLGLLQFVRLRKHHWLVDDAWFCDRITVQGPGACAEVAFPCYRWVQGEDILSLPEGTARLPGDNALDMFQKHREKELKDRQQIYCWATWKEGLPLTIAADRKDDLPPNMRFHEEKRLDFEWTLKAGALEMALKRVYTLLSSWNCLEDFDQIFWGQKSALAEKVRQCWQDDELFSYQFLNGANPMLLRRSTSLPSRLVLPSGMEELQAQLEKELQNGSLFEADFILLDGIPANVIRGEKQYLAAPLVMLKMEPNGKLQPMVIQIQPPNPSSPTPTLFLPSDPPLAWLLAKSWVRNSDFQLHEIQYHLLNTHLVAEVIAVATMRCLPGLHPIFKFLIPHIRYTMEINTRARTQLISDGGIFDKAVSTGGGGHVQLLRRAAAQLTYCSLCPPDDLADRGLLGLPGALYAHDALRLWEIIARYVEGIVHLFYQRDDIVKGDPELQAWCREITEVGLCQAQDRGFPVSFQSQSQLCHFLTMCVFTCTAQHAAINQGQLDWYAWVPNAPCTMRMPPPTTKEDVTMATVMGSLPDVRQACLQMAISWHLSRRQPDMVPLGHHKEKYFSGPKPKAVLNQFRTDLEKLEKEITARNEQLDWPYEYLKPSCIENSVTI,Polyunsaturated fatty acid lipoxygenase ALOX12,"Catalyzes the regio and stereo-specific incorporation of molecular oxygen into free and esterified polyunsaturated fatty acids generating lipid hydroperoxides that can be further reduced to the corresponding hydroxy species. Mainly converts arachidonate ((5Z,8Z,11Z,14Z)-eicosatetraenoate) to the specific bioactive lipid (12S)-hydroperoxyeicosatetraenoate/(12S)-HPETE. Through the production of bioactive lipids like (12S)-HPETE it regulates different biological processes including platelet activation. It can also catalyze the epoxidation of double bonds of polyunsaturated fatty acids such as (14S)-hydroperoxy-docosahexaenoate/(14S)-HPDHA resulting in the formation of (13S,14S)-epoxy-DHA. Furthermore, it may participate in the sequential oxidations of DHA ((4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate) to generate specialized pro-resolving mediators (SPMs) like resolvin D5 ((7S,17S)-diHPDHA) and (7S,14S)-diHPDHA, that actively down-regulate the immune response and have anti-aggregation properties with platelets. An additional function involves a multistep process by which it transforms leukotriene A4/LTA4 into the bioactive lipids lipoxin A4/LXA4 and lipoxin B4/LXB4, both are vasoactive and LXA4 may regulate neutrophil function via occupancy of specific recognition sites. Can also peroxidize linoleate ((9Z,12Z)-octadecadienoate) to (13S)-hydroperoxyoctadecadienoate/ (13S-HPODE). Due to its role in regulating both the expression of the vascular endothelial growth factor (VEGF, an angiogenic factor involved in the survival and metastasis of solid tumors) and the expression of integrin beta-1 (known to affect tumor cell migration and proliferation), it can be regarded as protumorigenic. Important for cell survival, as it may play a role not only in proliferation but also in the prevention of apoptosis in vascular smooth muscle cells.","The mutation in ALOX12 is associated with colon cancer risk in Caucasians. The increased risk of CRC was also associated with the 12-LOX 261Q/Q genotype compared with the R/R genotype (adjusted OR = 1. 38, 95% CI = 1. 09-1. 74). The deduced sequence from the clone plT3 showed 65% identity with human reticulocyte 15-lipoxygenase and 42% identity with human leukocyte 5-lipoxygenase.","Does not affect lipoxygenase activity. The mutation in ALOX12 is associated with colon cancer risk in Caucasians. The increased risk of CRC was also associated with the 12-LOX 261Q/Q genotype compared with the R/R genotype (adjusted OR = 1. 38, 95% CI = 1. 09-1. 74). The deduced sequence from the clone plT3 showed 65% identity with human reticulocyte 15-lipoxygenase and 42% identity with human leukocyte 5-lipoxygenase."
920,920,920,65199,P08123-G109D,MLSFVDTRTLLLLAVTLCLATCQSLQEETVRKGPAGDRGPRGERGPPGPPGRDGEDGPTGPPGPPGPPGPPGLGGNFAAQYDGKGVGLGPGPMGLMGPRGPPGAAGAPDPQGFQGPAGEPGEPGQTGPAGARGPAGPPGKAGEDGHPGKPGRPGERGVVGPQGARGFPGTPGLPGFKGIRGHNGLDGLKGQPGAPGVKGEPGAPGENGTPGQTGARGLPGERGRVGAPGPAGARGSDGSVGPVGPAGPIGSAGPPGFPGAPGPKGEIGAVGNAGPAGPAGPRGEVGLPGLSGPVGPPGNPGANGLTGAKGAAGLPGVAGAPGLPGPRGIPGPVGAAGATGARGLVGEPGPAGSKGESGNKGEPGSAGPQGPPGPSGEEGKRGPNGEAGSAGPPGPPGLRGSPGSRGLPGADGRAGVMGPPGSRGASGPAGVRGPNGDAGRPGEPGLMGPRGLPGSPGNIGPAGKEGPVGLPGIDGRPGPIGPAGARGEPGNIGFPGPKGPTGDPGKNGDKGHAGLAGARGAPGPDGNNGAQGPPGPQGVQGGKGEQGPPGPPGFQGLPGPSGPAGEVGKPGERGLHGEFGLPGPAGPRGERGPPGESGAAGPTGPIGSRGPSGPPGPDGNKGEPGVVGAVGTAGPSGPSGLPGERGAAGIPGGKGEKGEPGLRGEIGNPGRDGARGAPGAVGAPGPAGATGDRGEAGAAGPAGPAGPRGSPGERGEVGPAGPNGFAGPAGAAGQPGAKGERGAKGPKGENGVVGPTGPVGAAGPAGPNGPPGPAGSRGDGGPPGMTGFPGAAGRTGPPGPSGISGPPGPPGPAGKEGLRGPRGDQGPVGRTGEVGAVGPPGFAGEKGPSGEAGTAGPPGTPGPQGLLGAPGILGLPGSRGERGLPGVAGAVGEPGPLGIAGPPGARGPPGAVGSPGVNGAPGEAGRDGNPGNDGPPGRDGQPGHKGERGYPGNIGPVGAAGAPGPHGPVGPAGKHGNRGETGPSGPVGPAGAVGPRGPSGPQGIRGDKGEPGEKGPRGLPGLKG,In OIEDS2; decreased N-terminal propeptide processing.,,MLSFVDTRTLLLLAVTLCLATCQSLQEETVRKGPAGDRGPRGERGPPGPPGRDGEDGPTGPPGPPGPPGPPGLGGNFAAQYDGKGVGLGPGPMGLMGPRGPPGAAGAPGPQGFQGPAGEPGEPGQTGPAGARGPAGPPGKAGEDGHPGKPGRPGERGVVGPQGARGFPGTPGLPGFKGIRGHNGLDGLKGQPGAPGVKGEPGAPGENGTPGQTGARGLPGERGRVGAPGPAGARGSDGSVGPVGPAGPIGSAGPPGFPGAPGPKGEIGAVGNAGPAGPAGPRGEVGLPGLSGPVGPPGNPGANGLTGAKGAAGLPGVAGAPGLPGPRGIPGPVGAAGATGARGLVGEPGPAGSKGESGNKGEPGSAGPQGPPGPSGEEGKRGPNGEAGSAGPPGPPGLRGSPGSRGLPGADGRAGVMGPPGSRGASGPAGVRGPNGDAGRPGEPGLMGPRGLPGSPGNIGPAGKEGPVGLPGIDGRPGPIGPAGARGEPGNIGFPGPKGPTGDPGKNGDKGHAGLAGARGAPGPDGNNGAQGPPGPQGVQGGKGEQGPPGPPGFQGLPGPSGPAGEVGKPGERGLHGEFGLPGPAGPRGERGPPGESGAAGPTGPIGSRGPSGPPGPDGNKGEPGVVGAVGTAGPSGPSGLPGERGAAGIPGGKGEKGEPGLRGEIGNPGRDGARGAPGAVGAPGPAGATGDRGEAGAAGPAGPAGPRGSPGERGEVGPAGPNGFAGPAGAAGQPGAKGERGAKGPKGENGVVGPTGPVGAAGPAGPNGPPGPAGSRGDGGPPGMTGFPGAAGRTGPPGPSGISGPPGPPGPAGKEGLRGPRGDQGPVGRTGEVGAVGPPGFAGEKGPSGEAGTAGPPGTPGPQGLLGAPGILGLPGSRGERGLPGVAGAVGEPGPLGIAGPPGARGPPGAVGSPGVNGAPGEAGRDGNPGNDGPPGRDGQPGHKGERGYPGNIGPVGAAGAPGPHGPVGPAGKHGNRGETGPSGPVGPAGAVGPRGPSGPQGIRGDKGEPGEKGPRGLPGLKG,Collagen alpha-2,Type I collagen is a member of group I collagen (fibrillar forming collagen).,,In OIEDS2; decreased N-terminal propeptide processing.
925,925,925,65560,Q8HWS3-V506G,MAKVPELEDTFLQAQPAPQLSPGIQEDCCVQLLGKGLLVYPEETVYLAAEGQPGGEQGGGEKGEDPELPGAVKSEMHLNNGNFSSEEEDADNHDSKTKAADQYLSQKKTITQIVKDKKKQTQLTLQWLEENYIVCEGVCLPRCILYAHYLDFCRKEKLEPACAATFGKTIRQKFPLLTTRRLGTRGHSKYHYYGIGIKESSAYYHSVYSGKGLTRFSGSKLKNEGGFTRKYSLSSKTGTLLPEFPSAQHLVYQGCISKDKVDTLIMMYKTHCQCILDNAINGNFEEIQHFLLHFWQGMPDHLLPLLENPVIIDIFCVCDSILYKVLTDVLIPATMQEMPESLLADIRNFAKNWEQWVVSSLENLPEALTDKKIPIVRRFVSSLKRQTSFLHLAQIARPALFDQHVVNSMVSDIERVDLNSIGSQALLTISGSTDTESGIYTEHDSITVFQELKDLLKKNATVEAFIEWLDTVVEQRVIKTSKQNGRSLKKRAQDFLLKWSFFGARGMHNLTLNNASSFGSFHLIRMLLDEYILLAMETQFNNDKEQELQNLLDKYMKNSDASKAAFTASPSSCFLANRNKGSMVSSDAVKNESHVETTYLPLPSSQPGGLGPALHQFPAGNTDNMPLTGQMELSQIAGHLMTPPISPAMASRGSVINQGPMAGRPPSVGPVLSAPSHCSTYPEPIYPTLPQANHDFYSTSSNYQTVFRAQPHSTSGLYPHHTEHGRCMAWTEQQLSRDFFSGSCAGSPYNSRPPSSYGPSLQAQDSHNMQFLNTGSFNFLSNTGAASCQGATLPPNSPNGYYGSNINYPESHRLGSMVNQHVSVISSIRSLPPYSDIHDPLNILDDSGRKQTSSFYTDTSSPVACRTPVLASSLQTPIPSSSSQCMYGTSNQYPAQETLDSHGTSSREMVSSLPPINTVFMGTAAGGT,In MTCHRS; inhibits the transactivation of the insulin and beta-cell L-type calcium channel genes.,,MAKVPELEDTFLQAQPAPQLSPGIQEDCCVQLLGKGLLVYPEETVYLAAEGQPGGEQGGGEKGEDPELPGAVKSEMHLNNGNFSSEEEDADNHDSKTKAADQYLSQKKTITQIVKDKKKQTQLTLQWLEENYIVCEGVCLPRCILYAHYLDFCRKEKLEPACAATFGKTIRQKFPLLTTRRLGTRGHSKYHYYGIGIKESSAYYHSVYSGKGLTRFSGSKLKNEGGFTRKYSLSSKTGTLLPEFPSAQHLVYQGCISKDKVDTLIMMYKTHCQCILDNAINGNFEEIQHFLLHFWQGMPDHLLPLLENPVIIDIFCVCDSILYKVLTDVLIPATMQEMPESLLADIRNFAKNWEQWVVSSLENLPEALTDKKIPIVRRFVSSLKRQTSFLHLAQIARPALFDQHVVNSMVSDIERVDLNSIGSQALLTISGSTDTESGIYTEHDSITVFQELKDLLKKNATVEAFIEWLDTVVEQRVIKTSKQNGRSLKKRAQDFLLKWSFFGARVMHNLTLNNASSFGSFHLIRMLLDEYILLAMETQFNNDKEQELQNLLDKYMKNSDASKAAFTASPSSCFLANRNKGSMVSSDAVKNESHVETTYLPLPSSQPGGLGPALHQFPAGNTDNMPLTGQMELSQIAGHLMTPPISPAMASRGSVINQGPMAGRPPSVGPVLSAPSHCSTYPEPIYPTLPQANHDFYSTSSNYQTVFRAQPHSTSGLYPHHTEHGRCMAWTEQQLSRDFFSGSCAGSPYNSRPPSSYGPSLQAQDSHNMQFLNTGSFNFLSNTGAASCQGATLPPNSPNGYYGSNINYPESHRLGSMVNQHVSVISSIRSLPPYSDIHDPLNILDDSGRKQTSSFYTDTSSPVACRTPVLASSLQTPIPSSSSQCMYGTSNQYPAQETLDSHGTSSREMVSSLPPINTVFMGTAAGGT,DNA-binding protein RFX6,"Transcription factor required to direct islet cell differentiation during endocrine pancreas development. Specifically required for the differentiation of 4 of the 5 islet cell types and for the production of insulin. Not required for pancreatic PP (polypeptide-producing) cells differentiation. Acts downstream of NEUROG3 and regulates the transcription factors involved in beta-cell maturation and function, thereby restricting the expression of the beta-cell differentiation and specification genes, and thus the beta-cell fate choice. Activates transcription by forming a heterodimer with RFX3 and binding to the X-box in the promoter of target genes. Involved in glucose-stimulated insulin secretion by promoting insulin and L-type calcium channel gene transcription.",The homozygous missense RFX6 mutation (p. ) is associated with neonatal diabetes. This mutation lacks the capacity to activate the insulin promoter and to increase Ca(2+)-channel expression.,In MTCHRS; inhibits the transactivation of the insulin and beta-cell L-type calcium channel genes. The homozygous missense RFX6 mutation (p. ) is associated with neonatal diabetes. This mutation lacks the capacity to activate the insulin promoter and to increase Ca(2+)-channel expression.
932,932,932,65818,P40028-R486E,MGVSQIWEFLKPYLQDSRIPLRKFVIDFNKSQKRAPRIAIDAYGWLFECGFIQNIDISARSRSRSRSPTRSPRDSDIDSSQEYYGSRSYTTTGKAVINFISRLKELLSLNVEFLLVFDGVMKPSFKRKFNHEQNATTCDDEKEYYSSWEQHVKNHEVYGNCKGLLAPSDPEFISLVRKLLDLMNISYVIACGEGEAQCVWLQVSGAVDFILSNDSDTLVFGGEKILKNYSKFYDDFGPSSITSHSPSRHHDSKESFVTVIDLPKINKVAGKKFDRLSLLFFSVLLGADYNRGVKGLGKNKSLQLAQCEDPNFSMEFYDIFKDFNLEDLTSESLRKSRYRLFQKRLYLYCKDHSVELFGRNYPVLLNQGSFEGWPSTVAIMHYFHPIVQPYFDEEVLSDKYINMAGNGHYRNLNFNELKYFLQSLNLPQISSFDKWFHDSMHEMFLLREFLSIDESDNIGKGNMRITEEKIMNIDGGKFQIPCFKIEYTTFLPNIPISSQSPLKRSNSPSRSKSPTRRQMDIMEHPNSLWLPKYLIPQSHPLVIQYYETQQLIQKEKEKKGKKSNKSRLPQKNNLDEFLRKHTSPIKSIGKVGESRKEILEPVRKRLFVDTDEDTSLEEIPAPTRLTTVDEHSDNDDDSLIFVDEITNSQSVLDSSPGKRIRDLTQDEQVDVWKDVIEISPIKKSRTTNAEKNPPESGLKSRSSITINARLQGTKMLPPNLTAPRLEREHSSVLDQLVTDAQDTVDRFVACDSDSSSTIE,Mutants show a strong growth defect after treatment with DNA-damaging agent MMS.,,MGVSQIWEFLKPYLQDSRIPLRKFVIDFNKSQKRAPRIAIDAYGWLFECGFIQNIDISARSRSRSRSPTRSPRDSDIDSSQEYYGSRSYTTTGKAVINFISRLKELLSLNVEFLLVFDGVMKPSFKRKFNHEQNATTCDDEKEYYSSWEQHVKNHEVYGNCKGLLAPSDPEFISLVRKLLDLMNISYVIACGEGEAQCVWLQVSGAVDFILSNDSDTLVFGGEKILKNYSKFYDDFGPSSITSHSPSRHHDSKESFVTVIDLPKINKVAGKKFDRLSLLFFSVLLGADYNRGVKGLGKNKSLQLAQCEDPNFSMEFYDIFKDFNLEDLTSESLRKSRYRLFQKRLYLYCKDHSVELFGRNYPVLLNQGSFEGWPSTVAIMHYFHPIVQPYFDEEVLSDKYINMAGNGHYRNLNFNELKYFLQSLNLPQISSFDKWFHDSMHEMFLLREFLSIDESDNIGKGNMRITEEKIMNIDGGKFQIPCFKIRYTTFLPNIPISSQSPLKRSNSPSRSKSPTRRQMDIMEHPNSLWLPKYLIPQSHPLVIQYYETQQLIQKEKEKKGKKSNKSRLPQKNNLDEFLRKHTSPIKSIGKVGESRKEILEPVRKRLFVDTDEDTSLEEIPAPTRLTTVDEHSDNDDDSLIFVDEITNSQSVLDSSPGKRIRDLTQDEQVDVWKDVIEISPIKKSRTTNAEKNPPESGLKSRSSITINARLQGTKMLPPNLTAPRLEREHSSVLDQLVTDAQDTVDRFVACDSDSSSTIE,Holliday junction resolvase YEN1,"Endonuclease which resolves Holliday junctions by the introduction of symmetrically related cuts across the junction point, to produce nicked duplex products in which the nicks can be readily ligated. Four-way DNA intermediates, also known as Holliday junctions, are formed during homologous recombination and DNA repair, and their resolution is necessary for proper chromosome segregation. Involved in DNA-damage repair in vegetative cells.",,Mutants show a strong growth defect after treatment with DNA-damaging agent MMS.
934,934,934,65980,A5JTM5-G114A,MYEAIGHRVEDGVAEITIKLPRHRNALSVKAMQEVTDALNRAEEDDSVGAVMITGAEDAFCAGFYLREIPLDKGVAGVRDHFRIGALWWHQMIHKIIRVKRPVLAAINGVAAGAGLGISLASDMAICADSAKFVCAWHTIGIGNDTATSYSLARIVGMRRAMELMLTNRTLYPEEAKDWGLVSRVYPKDDFREVAWKVARELAAAPTHLQVMAKERFHAGWMQPVEECTEFEIQNVIASVTHPHFMPCLTEFLDGHRADRPQVELPAGV,Strongly reduced catalytic activity and substrate benzoyl group binding.,,MYEAIGHRVEDGVAEITIKLPRHRNALSVKAMQEVTDALNRAEEDDSVGAVMITGAEDAFCAGFYLREIPLDKGVAGVRDHFRIGALWWHQMIHKIIRVKRPVLAAINGVAAGGGLGISLASDMAICADSAKFVCAWHTIGIGNDTATSYSLARIVGMRRAMELMLTNRTLYPEEAKDWGLVSRVYPKDDFREVAWKVARELAAAPTHLQVMAKERFHAGWMQPVEECTEFEIQNVIASVTHPHFMPCLTEFLDGHRADRPQVELPAGV,4-chlorobenzoyl coenzyme A dehalogenase,"Dehalogenates 4-chlorobenzoyl-CoA, 4-iodobenzoyl-CoA and 4-bromobenzoyl-CoA, but not 4-fluorobenzoyl-CoA. Inactive towards crotonyl-CoA, alpha-methylcrotonyl-CoA and beta-methylcrotonyl-CoA.","The H-bond interactions between the G114 and F64 backbone amide NHs and the substrate benzoyl C=O group contribute an additional 3. 1 kcal/mol of stabilization at the rate-limiting transition state. The mutant was shown to be strongly inhibited in both substrate binding and activation, indicating that H-bonding and/or interaction with the dipole of the 114-121 alpha-helix may be crucial.","Strongly reduced catalytic activity and substrate benzoyl group binding. The H-bond interactions between the G114 and F64 backbone amide NHs and the substrate benzoyl C=O group contribute an additional 3. 1 kcal/mol of stabilization at the rate-limiting transition state. The mutant was shown to be strongly inhibited in both substrate binding and activation, indicating that H-bonding and/or interaction with the dipole of the 114-121 alpha-helix may be crucial."
946,946,946,67077,Q17339-S39A,MPSCTTPTYGVSTQLESQSSESPSRSSVMTPTSLDGDNAPRKRFPIIDNVPADRWPSTRRDGWSSVRAPPPARLTLSTNNRHIMSPISSAYSQTPNSLLSPAMFNPKSRSIFSPTLPATPMSYGKSSMDKSLFSPTATEPIEVEATVEYLADLVKEKKHLTLFPHMFSNVERLLDDEIGRVRVALFQTEFPRVELPEPAGDMISITEKIYVPKNEYPDYNFVGRILGPRGMTAKQLEQDTGCKIMVRGKGSMRDKSKESAHRGKANWEHLEDDLHVLVQCEDTENRVHIKLQAALEQVKKLLIPAPEGTDELKRKQLMELAIINGTYRPMKSPNPARVMTAVPLLSPTPLRSSGPVLMSPTPGSGLPSTTFGGSILSPTLTASNLLGSNVFDYSLLSPSMFDSFSSLQLASDLTFPKYPTTTSFVNSFPGLFTSASSFANQTNTNVSPSGASPSASSVNNTSF,May abolish phosphorylation by cdk-2. Increased expression in the gonad mitotic zone and reduction in the size of the mitotic region; when associated with A-22 and A-348.,,MPSCTTPTYGVSTQLESQSSESPSRSSVMTPTSLDGDNSPRKRFPIIDNVPADRWPSTRRDGWSSVRAPPPARLTLSTNNRHIMSPISSAYSQTPNSLLSPAMFNPKSRSIFSPTLPATPMSYGKSSMDKSLFSPTATEPIEVEATVEYLADLVKEKKHLTLFPHMFSNVERLLDDEIGRVRVALFQTEFPRVELPEPAGDMISITEKIYVPKNEYPDYNFVGRILGPRGMTAKQLEQDTGCKIMVRGKGSMRDKSKESAHRGKANWEHLEDDLHVLVQCEDTENRVHIKLQAALEQVKKLLIPAPEGTDELKRKQLMELAIINGTYRPMKSPNPARVMTAVPLLSPTPLRSSGPVLMSPTPGSGLPSTTFGGSILSPTLTASNLLGSNVFDYSLLSPSMFDSFSSLQLASDLTFPKYPTTTSFVNSFPGLFTSASSFANQTNTNVSPSGASPSASSVNNTSF,Female germline-specific tumor suppressor gld-1,"RNA-binding protein which recognizes the 5'-UACUCAU-3' RNA consensus sequence. Binds sequences in both the 5'coding and the 3'-UTR region of rme-2 mRNA. Binds sequences in the 3'-UTR region of cye-1 mRNA. Binds to cyb-2.1, cyb-2.2 and cyb-3 mRNA. Binds sequences in the 3'-UTR region of tra-2 mRNA. Germ line-specific tumor suppressor essential for oogenesis. Controls the spatial pattern of translation of multiple oogenesis specific mRNAs (e.g. yolk receptor rme-2) by repression of translation during early meiotic prophase (leptotene to pachytene) and then derepression of translation during diplotene/ diakinesis, following its degradation. Also functions to promote the male sexual fate in the hermaphrodite germline but not the male germline. Represses translation of the vacuolar ATPase component vha-13 in the distal gonad. Functions redundantly with gld-2 to promote the initiation of meiotic development and/or inhibit stem cell proliferation. By regulating cye-1 expression, prevents entry into mitosis in meiotic germline cells.",,May abolish phosphorylation by cdk-2. Increased expression in the gonad mitotic zone and reduction in the size of the mitotic region; when associated with A-22 and A-348.
949,949,949,67597,Q8HWB0-G86R,MMLLLPLLAVFLVKRSHTRTHSLRYFRLAVSDPGPVVPEFISVGYVDSHPITTYDSVTRQKEPKAPWMAENLAPDHWERYTQLLRRWQQTFKAELRHLQRHYNHSGLHTYQRMIGCELLEDGSTTGFLQYAYDGQDFIIFNKDTLSWLAMDYVAHITKQAWEANLHELQYQKNWLEEECIAWLKRFLEYGRDTLERTEHPVVRTTRKETFPGITTFFCRAHGFYPPEISMTWMKNGEEIAQEVDYGGVLPSGDGTYQTWLSVNLDPQSNDVYSCHVEHCGRQMVLEAPRESGDILRVSTISGTTILIIALAGVGVLIWRRSQELKEVMYQPTQVNEGSSPS,Loss of MAIT cell activation.,,MMLLLPLLAVFLVKRSHTRTHSLRYFRLAVSDPGPVVPEFISVGYVDSHPITTYDSVTRQKEPKAPWMAENLAPDHWERYTQLLRGWQQTFKAELRHLQRHYNHSGLHTYQRMIGCELLEDGSTTGFLQYAYDGQDFIIFNKDTLSWLAMDYVAHITKQAWEANLHELQYQKNWLEEECIAWLKRFLEYGRDTLERTEHPVVRTTRKETFPGITTFFCRAHGFYPPEISMTWMKNGEEIAQEVDYGGVLPSGDGTYQTWLSVNLDPQSNDVYSCHVEHCGRQMVLEAPRESGDILRVSTISGTTILIIALAGVGVLIWRRSQELKEVMYQPTQVNEGSSPS,Major histocompatibility complex class I-related gene protein,"Antigen-presenting molecule specialized in displaying microbial pyrimidine-based metabolites to alpha-beta T cell receptors (TCR) on innate-type mucosal-associated invariant T (MAIT) cells. In complex with B2M preferentially presents riboflavin-derived metabolites to semi-invariant TRAV1 TCRs on MAIT cells, guiding immune surveillance of the microbial metabolome at mucosal epithelial barriers. Signature pyrimidine-based microbial antigens are generated via non-enzymatic condensation of metabolite intermediates of the riboflavin pathway with by-products arising from other metabolic pathways such as glycolysis. Typical potent antigenic metabolites are 5-(2-oxoethylideneamino)-6-D-ribitylaminouracil (5-OE-RU) and 5-(2-oxopropylideneamino)-6-D-ribitylaminouracil (5-OP-RU), products of condensation of 5-amino-6-D-ribityaminouracil (5-A-RU) with glyoxal or methylglyoxal by-products, respectively. May present microbial antigens to various TRAV1-negative MAIT cell subsets, providing for unique recognition of diverse microbes, including pathogens that do not synthesize riboflavin. Upon antigen recognition, elicits rapid innate-type MAIT cell activation to eliminate pathogenic microbes by directly killing infected cells. During T cell development, drives thymic selection and post-thymic terminal differentiation of MAIT cells in a process dependent on commensal microflora. Acts as an immune sensor of cancer cell metabolome. May present a tumor-specific or -associated metabolite essential for cancer cell survival to a pan-cancer TCR on a non-MAIT CD8-positive T cell clone, triggering T cell-mediated killing of a wide range of cancer cell types.",The mutation in MR1 severely reduces surface expression of folded molecules.,Loss of MAIT cell activation. The mutation in MR1 severely reduces surface expression of folded molecules.
951,951,951,67687,Q3UMW7-T203A,MDGETAGEKGSLVPPPGALGGSALGGAPAPGVRREPKKYAVTDDYQLSKQVLGLGVNGKVLECYHRRSGQKCALKLLYDSPKARQEVDHHWQASGGPHIVRILDVYENMHHGKRCLLIVMECMEGGELFSRIQERGDQAFTEREAAEIMRDIGTAIQFLHSRNIAHRDVKPENLLYTSKEKDAVLKLTDFGFAKETTQNALQAPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFYSNTGQAISPGMKRRIRLGQYSFPNPEWLDVSEDAKQLIRLLLKTDPTERLTIMQFMNHPWINQSMVVPQTPLYTARVLQEDKDHWDDVKEEMTSALATMRVDYDQVKIKDLKTSNNRLLNKRRKKQAGSSSASQGCNNQ,Prevents degradation of isoform 3.,,MDGETAGEKGSLVPPPGALGGSALGGAPAPGVRREPKKYAVTDDYQLSKQVLGLGVNGKVLECYHRRSGQKCALKLLYDSPKARQEVDHHWQASGGPHIVRILDVYENMHHGKRCLLIVMECMEGGELFSRIQERGDQAFTEREAAEIMRDIGTAIQFLHSRNIAHRDVKPENLLYTSKEKDAVLKLTDFGFAKETTQNALQTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFYSNTGQAISPGMKRRIRLGQYSFPNPEWLDVSEDAKQLIRLLLKTDPTERLTIMQFMNHPWINQSMVVPQTPLYTARVLQEDKDHWDDVKEEMTSALATMRVDYDQVKIKDLKTSNNRLLNKRRKKQAGSSSASQGCNNQ,MAP kinase-activated protein kinase 3,"Stress-activated serine/threonine-protein kinase involved in cytokines production, endocytosis, cell migration, chromatin remodeling and transcriptional regulation. Following stress, it is phosphorylated and activated by MAP kinase p38-alpha/MAPK14, leading to phosphorylation of substrates. Phosphorylates serine in the peptide sequence, Hyd-X-R-X(2)-S, where Hyd is a large hydrophobic residue. MAPKAPK2 and MAPKAPK3, share the same function and substrate specificity, but MAPKAPK3 kinase activity and level in protein expression are lower compared to MAPKAPK2. Phosphorylates HSP27/HSPB1, KRT18, KRT20, RCSD1, RPS6KA3, TAB3 and TTP/ZFP36. Mediates phosphorylation of HSP27/HSPB1 in response to stress, leading to dissociate HSP27/HSPB1 from large small heat-shock protein (sHsps) oligomers and impair their chaperone activities and ability to protect against oxidative stress effectively. Involved in inflammatory response by regulating tumor necrosis factor (TNF) and IL6 production post-transcriptionally: acts by phosphorylating AU-rich elements (AREs)-binding proteins, such as TTP/ZFP36, leading to regulate the stability and translation of TNF and IL6 mRNAs. Phosphorylation of TTP/ZFP36, a major post-transcriptional regulator of TNF, promotes its binding to 14-3-3 proteins and reduces its ARE mRNA affinity leading to inhibition of dependent degradation of ARE-containing transcript. Involved in toll-like receptor signaling pathway (TLR) in dendritic cells: required for acute TLR-induced macropinocytosis by phosphorylating and activating RPS6KA3. Also acts as a modulator of Polycomb-mediated repression.",Replacing T-203 with alanine prevented the loss of MK3. 2 following osmotic stress,Prevents degradation of isoform 3. Replacing T-203 with alanine prevented the loss of MK3. 2 following osmotic stress
957,957,957,68123,P04412-N342A,MLLRRRNGPCPFPLLLLLLAHCICIWPASAARDRYARQNNRQRHQDIDRDRDRDRFLYRSSSAQNRQRGGANFALGLGANGVTIPTSLEDKNKNEFVKGKICIGTKSRLSVPSNKEHHYRNLRDRYTNCTYVDGNLKLTWLPNENLDLSFLDNIREVTGYILISHVDVKKVVFPKLQIIRGRTLFSLSVEEEKYALFVTYSKMYTLEIPDLRDVLNGQVGFHNNYNLCHMRTIQWSEIVSNGTDAYYNYDFTAPERECPKCHESCTHGCWGEGPKNCQKFSKLTCSPQCAGGRCYGPKPRECCHLFCAGGCTGPTQKDCIACKNFFDEAVSKEECPPMRKYAPTTYVLETNPEGKYAYGATCVKECPGHLLRDNGACVRSCPQDKMDKGGECVPCNGPCPKTCPGVTVLHAGNIDSFRNCTVIDGNIRILDQTFSGFQDVYANYTMGPRYIPLDPERREVFSTVKEITGYLNIEGTHPQFRNLSYFRNLETIHGRQLMESMFAALAIVKSSLYSLEMRNLKQISSGSVVIQHNRDLCYVSNIRWPAIQKEPEQKVWVNENLRADLCEKNGTICSDQCNEDGCWGAGTDQCLTCKNFNFNGTCIADCGYISNAYKFDNRTCKICHPECRTCNGAGADHCQECVHVRDGQHCVSECPKNKYNDRGVCRECHATCDGCTGPKDTIGIGACTTCNLAIINNDATVKRCLLKDDKCPDGYFWEYVHPQEQGSLKPLAGRAVCRKCHPLCELCTNYGYHEQVCSKCTHYKRREQCETECPADHYTDEEQRECFQRHPECNGCTGPGADDCKSCRNFKLFDANETGPYVNSTMFNCTSKCPLEMRHVNYQYTAIGPYCAASPPRSSKITANLDVNMIFIITGAVLVPTICILCVVTYICRQKQKAKKETVKMTMALSGCEDSEPLRPSNIGANLCKLRIVKDAELRKGGVLGMGAFGRVYKGVWVPEGENVKIPVAIKELLKSTGAESSEEFLREAYIMASEEHVNLLKLLAVCMSSQMMLITQLMPLGCL,In dim-arm; Does not form dimers even in the presence of spitz; when associated with E-341; D-344; E-346; A-347 and D-348.,,MLLRRRNGPCPFPLLLLLLAHCICIWPASAARDRYARQNNRQRHQDIDRDRDRDRFLYRSSSAQNRQRGGANFALGLGANGVTIPTSLEDKNKNEFVKGKICIGTKSRLSVPSNKEHHYRNLRDRYTNCTYVDGNLKLTWLPNENLDLSFLDNIREVTGYILISHVDVKKVVFPKLQIIRGRTLFSLSVEEEKYALFVTYSKMYTLEIPDLRDVLNGQVGFHNNYNLCHMRTIQWSEIVSNGTDAYYNYDFTAPERECPKCHESCTHGCWGEGPKNCQKFSKLTCSPQCAGGRCYGPKPRECCHLFCAGGCTGPTQKDCIACKNFFDEAVSKEECPPMRKYNPTTYVLETNPEGKYAYGATCVKECPGHLLRDNGACVRSCPQDKMDKGGECVPCNGPCPKTCPGVTVLHAGNIDSFRNCTVIDGNIRILDQTFSGFQDVYANYTMGPRYIPLDPERREVFSTVKEITGYLNIEGTHPQFRNLSYFRNLETIHGRQLMESMFAALAIVKSSLYSLEMRNLKQISSGSVVIQHNRDLCYVSNIRWPAIQKEPEQKVWVNENLRADLCEKNGTICSDQCNEDGCWGAGTDQCLTCKNFNFNGTCIADCGYISNAYKFDNRTCKICHPECRTCNGAGADHCQECVHVRDGQHCVSECPKNKYNDRGVCRECHATCDGCTGPKDTIGIGACTTCNLAIINNDATVKRCLLKDDKCPDGYFWEYVHPQEQGSLKPLAGRAVCRKCHPLCELCTNYGYHEQVCSKCTHYKRREQCETECPADHYTDEEQRECFQRHPECNGCTGPGADDCKSCRNFKLFDANETGPYVNSTMFNCTSKCPLEMRHVNYQYTAIGPYCAASPPRSSKITANLDVNMIFIITGAVLVPTICILCVVTYICRQKQKAKKETVKMTMALSGCEDSEPLRPSNIGANLCKLRIVKDAELRKGGVLGMGAFGRVYKGVWVPEGENVKIPVAIKELLKSTGAESSEEFLREAYIMASEEHVNLLKLLAVCMSSQMMLITQLMPLGCL,Epidermal growth factor receptor,"Receptor tyrosine kinase, binding ligands of the EGF family and activating several signaling cascades to convert extracellular cues into appropriate cellular responses. Known ligands include spitz, gurken, vein and giant-lens. Transduces the signal through the ras-raf-MAPK pathway. Critical for the proliferation of imaginal tissues, and for the determination of both the antero-posterior and dorso-ventral polarities of the oocyte. In the embryo, plays a role in the establishment of ventral cell fates, maintenance of amnioserosa and ventral neuroectodermal cells, germ band retraction, cell fate specification in the central nervous system, and production and repair of the cuticle. During dorsal closure (DC) functions with the dpp- and ACK-signaling pathways to regulate expression of the myosin zip in the embryonic epidermis and amnioserosa (AS), and thus coordinate the progression of epidermal cell shape changes required for correct DC. In the embryonic epidermis, functions by negatively regulating dpp and consequently the dpp-dependent expression of the myosin zip. In the AS, negatively regulates the production/ and or secretion of a diffusible signal which, is produced by the ACK-signaling pathway, and acts in the AS and epidermal cells to promote zip expression. Also required in the AS to inhibit or delay apoptosis, and consequently slow the rate of DC. Therefore functions at multiple levels to negatively regulate morphogenesis during DC, suggesting that it acts as a general brake mechanism for adjusting the rate of dorsal closure to ensure that closure proceeds smoothly and without loss of epidermal integrity. During oogenesis, one of two tyrosine kinase chemoattractant receptors (Egfr and Pvr), that function in the border cells (BC) to detect guidance cues from the oocyte and transduce this information to the guidance pathway that regulate the collective migration of the BC cluster through the nurse cells to the oocyte.",,In dim-arm; Does not form dimers even in the presence of spitz; when associated with E-341; D-344; E-346; A-347 and D-348.
958,958,958,68206,Q6QNK2-C454Y,MEKLLRLCCWYSWLLLFYYNFQVRGVYSRSQDHPGFQVLASASHYWPLENVDGIHELQDTTGDIVEGKVNKGIYLKEEKGVTLLYYGRYNSSCISKPEQCGPEGVTFSFFWKTQGEQSRPIPSAYGGQVISNGFKVCSSGGRGSVELYTRDNSMTWEASFSPPGPYWTHVLFTWKSKEGLKVYVNGTLSTSDPSGKVSRDYGESNVNLVIGSEQDQAKCYENGAFDEFIIWERALTPDEIAMYFTAAIGKHALLSSTLPSLFMTSTASPVMPTDAYHPIITNLTEERKTFQSPGVILSYLQNVSLSLPSKSLSEQTALNLTKTFLKAVGEILLLPGWIALSEDSAVVLSLIDTIDTVMGHVSSNLHGSTPQVTVEGSSAMAEFSVAKILPKTVNSSHYRFPAHGQSFIQIPHEAFHRHAWSTVVGLLYHSMHYYLNNIWPAHTKIAEAMHHQDYLLFATSHLISLEVSPPPTLSQNLSGSPLITVHLKHRLTRKQHSEATNSSNRVFVYCAFLDFSSGEGVWSNHGCALTRGNLTYSVCRCTHLTNFAILMQVVPLELARGHQVALSSISYVGCSLSVLCLVATLVTFAVLSSVSTIRNQRYHIHANLSFAVLVAQVLLLISFRLEPGTTPCQVMAVLLHYFFLSAFAWMLVEGLHLYSMVIKVFGSEDSKHRYYYGMGWGFPLLICIISLSFAMDSYGTSNNCWLSLASGAIWAFVAPALFVIVVNIGILIAVTRVISQISADNYKIHGDPSAFKLTAKAVAVLLPILGTSWVFGVLAVNGCAVVFQYMFATLNSLQGLFIFLFHCLLNSEVRAAFKHKTKVWSLTSSSARTSNAKPFHSDLMNGTRPGMASTKLSPWDKSSHSAHRVDLSAV,Does not affect subcellular location; does not change G-protein coupled receptor activity.,,MEKLLRLCCWYSWLLLFYYNFQVRGVYSRSQDHPGFQVLASASHYWPLENVDGIHELQDTTGDIVEGKVNKGIYLKEEKGVTLLYYGRYNSSCISKPEQCGPEGVTFSFFWKTQGEQSRPIPSAYGGQVISNGFKVCSSGGRGSVELYTRDNSMTWEASFSPPGPYWTHVLFTWKSKEGLKVYVNGTLSTSDPSGKVSRDYGESNVNLVIGSEQDQAKCYENGAFDEFIIWERALTPDEIAMYFTAAIGKHALLSSTLPSLFMTSTASPVMPTDAYHPIITNLTEERKTFQSPGVILSYLQNVSLSLPSKSLSEQTALNLTKTFLKAVGEILLLPGWIALSEDSAVVLSLIDTIDTVMGHVSSNLHGSTPQVTVEGSSAMAEFSVAKILPKTVNSSHYRFPAHGQSFIQIPHEAFHRHAWSTVVGLLYHSMHYYLNNIWPAHTKIAEAMHHQDCLLFATSHLISLEVSPPPTLSQNLSGSPLITVHLKHRLTRKQHSEATNSSNRVFVYCAFLDFSSGEGVWSNHGCALTRGNLTYSVCRCTHLTNFAILMQVVPLELARGHQVALSSISYVGCSLSVLCLVATLVTFAVLSSVSTIRNQRYHIHANLSFAVLVAQVLLLISFRLEPGTTPCQVMAVLLHYFFLSAFAWMLVEGLHLYSMVIKVFGSEDSKHRYYYGMGWGFPLLICIISLSFAMDSYGTSNNCWLSLASGAIWAFVAPALFVIVVNIGILIAVTRVISQISADNYKIHGDPSAFKLTAKAVAVLLPILGTSWVFGVLAVNGCAVVFQYMFATLNSLQGLFIFLFHCLLNSEVRAAFKHKTKVWSLTSSSARTSNAKPFHSDLMNGTRPGMASTKLSPWDKSSHSAHRVDLSAV,Adhesion G-protein coupled receptor D1,Orphan receptor. Signals via G(s)-alpha family of G-proteins. Has protumorigenic function especially in glioblastoma.,,Does not affect subcellular location; does not change G-protein coupled receptor activity.
969,969,969,70014,P25737-E438A,MVSETKTTEAPGLRRELKARHLTMIAIGGSIGTGLFVASGATISQAGPGGALLSYMLIGLMVYFLMTSLGELAAYMPVSGSFATYGQNYVEEGFGFALGWNYWYNWAVTIAVDLVAAQLVMSWWFPDTPGWIWSALFLGVIFLLNYISVRGFGEAEYWFSLIKVTTVIVFIIVGVLMIIGIFKGAQPAGWSNWTIGEAPFAGGFAAMIGVAMIVGFSFQGTELIGIAAGESEDPAKNIPRAVRQVFWRILLFYVFAILIISLIIPYTDPSLLRNDVKDISVSPFTLVFQHAGLLSAAAVMNAVILTAVLSAGNSGMYASTRMLYTLACDGKAPRIFAKLSRGGVPRNALYATTVIAGLCFLTSMFGNQTVYLWLLNTSGMTGFIAWLGIAISHYRFRRGYVLQGHDINDLPYRSGFFPLGPIFAFILCLIITLGQNYAAFLKDTIDWGGVAATYIGIPLFLIIWFGYKLIKGTHFVRYSEMKFPQNDKK,Retains 14% of wild-type lysine uptake activity. Is unable to inhibit CadC.,,MVSETKTTEAPGLRRELKARHLTMIAIGGSIGTGLFVASGATISQAGPGGALLSYMLIGLMVYFLMTSLGELAAYMPVSGSFATYGQNYVEEGFGFALGWNYWYNWAVTIAVDLVAAQLVMSWWFPDTPGWIWSALFLGVIFLLNYISVRGFGEAEYWFSLIKVTTVIVFIIVGVLMIIGIFKGAQPAGWSNWTIGEAPFAGGFAAMIGVAMIVGFSFQGTELIGIAAGESEDPAKNIPRAVRQVFWRILLFYVFAILIISLIIPYTDPSLLRNDVKDISVSPFTLVFQHAGLLSAAAVMNAVILTAVLSAGNSGMYASTRMLYTLACDGKAPRIFAKLSRGGVPRNALYATTVIAGLCFLTSMFGNQTVYLWLLNTSGMTGFIAWLGIAISHYRFRRGYVLQGHDINDLPYRSGFFPLGPIFAFILCLIITLGQNYEAFLKDTIDWGGVAATYIGIPLFLIIWFGYKLIKGTHFVRYSEMKFPQNDKK,Lysine-specific permease LysP,"Permease involved in lysine uptake. In addition, functions as a lysine sensor that mediates the lysine-dependent regulation of the transcriptional activator CadC. In the absence of lysine, or at low lysine concentrations, LysP inhibits CadC by an interaction with the transmembrane domain of CadC. In the presence of lysine, LysP loses its ability to interact with and inhibit CadC, and acts as a lysine permease.",,Retains 14% of wild-type lysine uptake activity. Is unable to inhibit CadC.
971,971,971,70089,O85673-D217N,MTARNLAEWQNFVQGCIDFRPNDGVYRIARDMFTEPELFELEMELIFEKVWIYACHESEIPNNNDFVTVQIGRQPMIVSRDGKGELHAMVNACEHRGATLTRVAKGNQSVFTCPFHAWCYKSDGRLVKVKAPGEYCEDFDKSSRGLKQGRIASYRGFVFVSLDTQATDSLEDFLGDAKVFLDLMVDQSPTGELEVLQGKSAYTFAGNWKLQNENGLNGYHVSTVHYNYVSTVQHRQQVNAAKGDELDTLDYSKLGAGDSETDDGWFSFKNGHSVLFSDMPNPTVRPGYNTVMPYLVEKFGEKRAEWAMHRLRNLNLYPSLFFMDQISSQLRIIRPVAWNKTEVISQCIGVKGESSEARRNRIRQFEDFFNVSGLGTPDDLVEFREQQKGFQGRIERWSDISRGYHQWTYGPTQNSQDLGIEPVITGREFTHEGLYVNQHGQWQRLILDGLNKKALKMHDVTFDNQSVMDEV,Loss of dioxygenase activity.,,MTARNLAEWQNFVQGCIDFRPNDGVYRIARDMFTEPELFELEMELIFEKVWIYACHESEIPNNNDFVTVQIGRQPMIVSRDGKGELHAMVNACEHRGATLTRVAKGNQSVFTCPFHAWCYKSDGRLVKVKAPGEYCEDFDKSSRGLKQGRIASYRGFVFVSLDTQATDSLEDFLGDAKVFLDLMVDQSPTGELEVLQGKSAYTFAGNWKLQNENGLDGYHVSTVHYNYVSTVQHRQQVNAAKGDELDTLDYSKLGAGDSETDDGWFSFKNGHSVLFSDMPNPTVRPGYNTVMPYLVEKFGEKRAEWAMHRLRNLNLYPSLFFMDQISSQLRIIRPVAWNKTEVISQCIGVKGESSEARRNRIRQFEDFFNVSGLGTPDDLVEFREQQKGFQGRIERWSDISRGYHQWTYGPTQNSQDLGIEPVITGREFTHEGLYVNQHGQWQRLILDGLNKKALKMHDVTFDNQSVMDEV,"Anthranilate 1,2-dioxygenase large subunit",Component of anthranilate dioxygenase multicomponent enzyme system which catalyzes the incorporation of both atoms of molecular oxygen into anthranilate to form catechol.,"The Rieske center reduction potential of this variant was measured to be approximately 100 mV more negative than that for the wild-type enzyme at neutral pH. The wild-type AntAB became completely inactive at pH 9 and exhibited an altered Rieske center absorption spectrum which resembled that of the D217 variants at neutral pH. These results support a role for this aspartate in maintaining the protonated state and reduction potential of the Rieske center. Both the wild-type and variant AntABs exhibited substrate-dependent rapid phases of Rieske center oxidations in stopped-flow time courses. However, since the single turnovers resulted in anthranilate dihydroxylation by the wild-type enzyme but not by the variant, this aspartate must also play a crucial role in substrate dihydroxylation at or near the mononuclear iron site.","Loss of dioxygenase activity. The Rieske center reduction potential of this variant was measured to be approximately 100 mV more negative than that for the wild-type enzyme at neutral pH. The wild-type AntAB became completely inactive at pH 9 and exhibited an altered Rieske center absorption spectrum which resembled that of the D217 variants at neutral pH. These results support a role for this aspartate in maintaining the protonated state and reduction potential of the Rieske center. Both the wild-type and variant AntABs exhibited substrate-dependent rapid phases of Rieske center oxidations in stopped-flow time courses. However, since the single turnovers resulted in anthranilate dihydroxylation by the wild-type enzyme but not by the variant, this aspartate must also play a crucial role in substrate dihydroxylation at or near the mononuclear iron site."
994,994,994,71757,Q8R173-Y18F,MMLIPTHHFRDIERKPEFLQPEKCAPPPFPGPAGAMWFIRDGCGIACAIVTWFLVLYAEFVVLFVMLVPSRDYAYSIINGIVFNLLAFLALASHCRAMLTDPGAVPKGNATKEFIESLQLKPGQVVYKCPKCCSIKPDRAHHCSVCKRCIRKMDHHCPWVNNCVGENNQKYFVLFTMYIALISLHALIMVGFHFLHCFEEDWTKCSSFSPPTTVILLILLCFEALLFLIFTSVMFGTQVHSICTDETGIEQLKKEERRWAKKTKWMNMKAVFGHPFSLGWASPFATPDQGKADPYQYVV,Decreased phosphorylation by FGFR1.,,MMLIPTHHFRDIERKPEYLQPEKCAPPPFPGPAGAMWFIRDGCGIACAIVTWFLVLYAEFVVLFVMLVPSRDYAYSIINGIVFNLLAFLALASHCRAMLTDPGAVPKGNATKEFIESLQLKPGQVVYKCPKCCSIKPDRAHHCSVCKRCIRKMDHHCPWVNNCVGENNQKYFVLFTMYIALISLHALIMVGFHFLHCFEEDWTKCSSFSPPTTVILLILLCFEALLFLIFTSVMFGTQVHSICTDETGIEQLKKEERRWAKKTKWMNMKAVFGHPFSLGWASPFATPDQGKADPYQYVV,Palmitoyltransferase ZDHHC3,"Golgi-localized palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates. Has no stringent fatty acid selectivity and in addition to palmitate can also transfer onto target proteins myristate from tetradecanoyl-CoA and stearate from octadecanoyl-CoA (Probable). Plays an important role in G protein-coupled receptor signaling pathways involving GNAQ and potentially other heterotrimeric G proteins by regulating their dynamic association with the plasma membrane. Palmitoylates ITGA6 and ITGB4, thereby regulating the alpha-6/beta-4 integrin localization, expression and function in cell adhesion to laminin. Plays a role in the TRAIL-activated apoptotic signaling pathway most probably through the palmitoylation and localization to the plasma membrane of TNFRSF10A. In the brain, by palmitoylating the gamma subunit GABRG2 of GABA(A) receptors and regulating their postsynaptic accumulation, plays a role in synaptic GABAergic inhibitory function and GABAergic innervation. Palmitoylates the neuronal protein GAP43 which is also involved in the formation of GABAergic synapses. Palmitoylates NCDN thereby regulating its association with endosome membranes. Probably palmitoylates PRCD and is involved in its proper localization within the photoreceptor. Could mediate the palmitoylation of NCAM1 and regulate neurite outgrowth. Could palmitoylate DNAJC5 and regulate its localization to Golgi membranes. Also constitutively palmitoylates DLG4. May also palmitoylate SNAP25. Could palmitoylate the glutamate receptors GRIA1 and GRIA2 but this has not been confirmed in vivo. Could also palmitoylate the D(2) dopamine receptor DRD2.May also function as a calcium transporter.","mutation specifically abrogates phosphorylation by FGFR1, leading to increased ZDHHC3 autopalmitoylation, enhanced interaction with NCAM, and upregulated NCAM palmitoylation. This mutation promotes neurite outgrowth in cultured hippocampal neurons.","Decreased phosphorylation by FGFR1. mutation specifically abrogates phosphorylation by FGFR1, leading to increased ZDHHC3 autopalmitoylation, enhanced interaction with NCAM, and upregulated NCAM palmitoylation. This mutation promotes neurite outgrowth in cultured hippocampal neurons."
1006,1006,1006,72873,Q9ZAG3-N55D,MTSKIEQPRWASKDSAAGAASTPDEKIVLEFMDALTSNDAAKLIEYFAEDTMYQDMPLPPAYGRDAVEQTLAGLFTVMSIDAVETFHIGSSNGLVYTERVDVLRALPTGKSYNLSILGVFQLTEGKITGWRDYFDLREFEEAVDLPLRG,No activity.,,MTSKIEQPRWASKDSAAGAASTPDEKIVLEFMDALTSNDAAKLIEYFAEDTMYQNMPLPPAYGRDAVEQTLAGLFTVMSIDAVETFHIGSSNGLVYTERVDVLRALPTGKSYNLSILGVFQLTEGKITGWRDYFDLREFEEAVDLPLRG,"Limonene-1,2-epoxide hydrolase","Catalyzes the conversion of limonene-1,2-epoxide to limonene-1,2-diol. Can use both the (-) and (+) isomers of limonene-1,2-epoxide as substrates and also has some activity with 1-methylcyclohexene oxide, cyclohexene oxide and indene oxide as substrates.",Site-directed mutagenesis supports the conclusion that this is the active site.,No activity. Site-directed mutagenesis supports the conclusion that this is the active site.
1011,1011,1011,73533,A0A109QYD3-G15D,MGTPILDAFNVRVEDSGDKYLVFAHGFGTDQSAWQRVLPYFTRSYKVILYDLVCAGSVNPDHFDFRRYTTLDAYVDDLLNILDSLHVTRCAYVGHSISAMTGMLASIRRPELFSKLILIGASPRFLNDGENYHGGFEQGEIEHVFSAMEANYEAWVNGFAPLAVGADVPTAVREFSRTLFNMRPDISLFVSRTVFNSDLRGILGLVNVPCCIMQTARDMSVPASVATYMKEHIGGKSTVQWLDTEGHLPHLSAPSYLAHQLEIALSQ,"In rms3-3; ramosus phenotype, reduced plant height and extensive vegetative branching from both basal and aerial nodes.",,MGTPILDAFNVRVEGSGDKYLVFAHGFGTDQSAWQRVLPYFTRSYKVILYDLVCAGSVNPDHFDFRRYTTLDAYVDDLLNILDSLHVTRCAYVGHSISAMTGMLASIRRPELFSKLILIGASPRFLNDGENYHGGFEQGEIEHVFSAMEANYEAWVNGFAPLAVGADVPTAVREFSRTLFNMRPDISLFVSRTVFNSDLRGILGLVNVPCCIMQTARDMSVPASVATYMKEHIGGKSTVQWLDTEGHLPHLSAPSYLAHQLEIALSQ,Strigolactone esterase RMS3,"Involved in strigolactone signaling pathway. Functions downstream of strigolactone synthesis, as a component of hormone signaling and as an enzyme that participates in the conversion of strigolactones to the bioactive form. Binds and hydrolyzes the synthetic strigolactone analog GR24 and its enantiomers in vitro. Forms a stable covalent complex with the D-ring of strigolactone, which is essential for hormone bioactivity. The D-ring is attached to His-247 of the catalytic triad. The hydrolysis of strigolactone into a covalently linked intermediate molecule is required to trigger strigolactone signaling. This mechanism defines RMS3 as a non-canonical hormone receptor with dual functions to generate and sense the active form of strigolactone. Strigolactones are hormones that inhibit tillering and shoot branching through the MAX-dependent pathway, contribute to the regulation of shoot architectural response to phosphate-limiting conditions and function as rhizosphere signal that stimulates hyphal branching of arbuscular mycorrhizal fungi and trigger seed germination of root parasitic weeds (Probable).",The mutation in the D14 protein causes a functional change in the strigolactone receptor. It is involved in the hydrolysis of the bond between the ABC lactone and the D ring.,"In rms3-3; ramosus phenotype, reduced plant height and extensive vegetative branching from both basal and aerial nodes. The mutation in the D14 protein causes a functional change in the strigolactone receptor. It is involved in the hydrolysis of the bond between the ABC lactone and the D ring."
1015,1015,1015,73776,A0A0A1I6N9-N30K,MEIKYLLTVFLVLLIVSDHCQAFLFSLIPKAISGLLSAFKGRRKRNLDGQIDRFRNFRKRDAELEELLSKLPIY,"Shows important increase in antimicrobial activity against E.coli (MIC=8 uM) and slight increase against S.aureus (MIC=4 uM) and C.albicans (MIC=4 uM), as well as slight increase in hemolytic activity (32 uM for 100% hemolysis). Also shows anti-proliferative effects on four cancer cell lines; when associated with K-26; K-33 and K-37.",,MEIKYLLTVFLVLLIVSDHCQAFLFSLIPNAISGLLSAFKGRRKRNLDGQIDRFRNFRKRDAELEELLSKLPIY,Antimicrobial peptide AcrAP2,Has antimicrobial activity against the Gram-positive bacteria S.aureus (MIC=8 uM) and the yeast C.albicans (MIC=16 uM). Causes hemolysis on horse erythrocytes (64 uM for 100% hemolysis). Minimum bactericidal concentrations have also been tested against S.aureus and is four-fold higher (MBC=32 uM).,,"Shows important increase in antimicrobial activity against E.coli (MIC=8 uM) and slight increase against S.aureus (MIC=4 uM) and C.albicans (MIC=4 uM), as well as slight increase in hemolytic activity (32 uM for 100% hemolysis). Also shows anti-proliferative effects on four cancer cell lines; when associated with K-26; K-33 and K-37."
1023,1023,1023,74550,P04198-E73K,MPSCSTSTMPGMICKNPDLEFDSLQPCFYPDEDDFYFGGPDSTPPGEDIWKKFELLPTPPLSPSRGFAEHSSKPPSWVTEMLLENELWGSPAEEDAFGLGGLGGLTPNPVILQDCMWSGFSAREKLERAVSEKLQHGRGPPTAGSTAQSPGAGAASPAGRGHGGAAGAGRAGAALPAELAHPAAECVDPAVVFPFPVNKREPAPVPAAPASAPAAGPAVASGAGIAAPAGAPGVAPPRPGGRQTSGGDHKALSTSGEDTLSDSDDEDDEEEDEEEEIDVVTVEKRRSSSNTKAVTTFTITVRPKNAALGPGRAQSSELILKRCLPIHQQHNYAAPSPYVESEDAPPQKKIKSEASPRPLKSVIPPKAKSLSPRNSDSEDSERRRNHNILERQRRNDLRSSFLTLRDHVPELVKNEKAAKVVILKKATEYVHSLQAEEHQLLLEKEKLQARQQQLLKKIEHARTC,Reduces binding to AURKA.,,MPSCSTSTMPGMICKNPDLEFDSLQPCFYPDEDDFYFGGPDSTPPGEDIWKKFELLPTPPLSPSRGFAEHSSEPPSWVTEMLLENELWGSPAEEDAFGLGGLGGLTPNPVILQDCMWSGFSAREKLERAVSEKLQHGRGPPTAGSTAQSPGAGAASPAGRGHGGAAGAGRAGAALPAELAHPAAECVDPAVVFPFPVNKREPAPVPAAPASAPAAGPAVASGAGIAAPAGAPGVAPPRPGGRQTSGGDHKALSTSGEDTLSDSDDEDDEEEDEEEEIDVVTVEKRRSSSNTKAVTTFTITVRPKNAALGPGRAQSSELILKRCLPIHQQHNYAAPSPYVESEDAPPQKKIKSEASPRPLKSVIPPKAKSLSPRNSDSEDSERRRNHNILERQRRNDLRSSFLTLRDHVPELVKNEKAAKVVILKKATEYVHSLQAEEHQLLLEKEKLQARQQQLLKKIEHARTC,N-myc proto-oncogene protein,Positively regulates the transcription of MYCNOS in neuroblastoma cells.,,Reduces binding to AURKA.
1038,1038,1038,75303,P20646-W137E,MRAVPLHLVGTASLTLGFLLLLSLRLDPGQAKELKFVTLVFRHGDRGPIETFPNDPIKESSWPQGFGQLTKWGMGQHYELGSYIRRRYGRFLNNSYKHDQVYIRSTDVDRTLMSAMTNLAALFPPEGISIWNPRLLEQPIPVHTVSLSEDRLLYLPFRDCPRFQELKSETLKSEEFLKRLQPYKSFIDTLPSLSGFEDQDLFEIWSRLYDPLYCESVHNFTLPTWATEDAMTKLKELSELSLLSLYGIHKQKEKSRLQGGVLVNEILKNMKLATQPQKARKLIMYSAHDTTVSGLQMALDVYNGLLPPYASCHIMELYQDNGGHFVEMYYRNETQNEPYPLTLPGCTHSCPLEKFAELLDPVIPQDWATECMGTSNHQASL,Abolishes most of enzyme activity and dimer formation. No enzyme activity nor dimer formation; when associated with D-143.,,MRAVPLHLVGTASLTLGFLLLLSLRLDPGQAKELKFVTLVFRHGDRGPIETFPNDPIKESSWPQGFGQLTKWGMGQHYELGSYIRRRYGRFLNNSYKHDQVYIRSTDVDRTLMSAMTNLAALFPPEGISIWNPRLLWQPIPVHTVSLSEDRLLYLPFRDCPRFQELKSETLKSEEFLKRLQPYKSFIDTLPSLSGFEDQDLFEIWSRLYDPLYCESVHNFTLPTWATEDAMTKLKELSELSLLSLYGIHKQKEKSRLQGGVLVNEILKNMKLATQPQKARKLIMYSAHDTTVSGLQMALDVYNGLLPPYASCHIMELYQDNGGHFVEMYYRNETQNEPYPLTLPGCTHSCPLEKFAELLDPVIPQDWATECMGTSNHQASL,Prostatic acid phosphatase,"A non-specific tyrosine phosphatase that dephosphorylates a diverse number of substrates under acidic conditions (pH 4-6) including alkyl, aryl, and acyl orthophosphate monoesters and phosphorylated proteins. Has lipid phosphatase activity and inactivates lysophosphatidic acid in seminal plasma.In addition to its tyrosine phosphatase activity, also has ecto-5'-nucleotidase activity in dorsal root ganglion (DRG) neurons. Generates adenosine from AMP. This extracellular adenosine leads to a decrease in chronic pain by activating A1R in nociceptive neurons.",,Abolishes most of enzyme activity and dimer formation. No enzyme activity nor dimer formation; when associated with D-143.
1053,1053,1053,76384,Q86V24-D219A,MNEPTENRLGCSRTPEPDIRLRKGHQLDGTRRGDNDSHQGDLEPILEASVLSSHHKKSSEEHEYSDEAPQEDEGFMGMSPLLQAHHAMEKMEEFVCKVWEGRWRVIPHDVLPDWLKDNDFLLHGHRPPMPSFRACFKSIFRIHTETGNIWTHLLGCVFFLCLGIFYMFRPNISFVAPLQEKVVFGLFFLGAILCLSFSWLFHTVYCHSEGVSRLFSKLAYSGIALLIMGSFVPWLYYSFYCNPQPCFIYLIVICVLGIAAIIVSQWDMFATPQYRGVRAGVFLGLGLSGIIPTLHYVISEGFLKAATIGQIGWLMLMASLYITGAALYAARIPERFFPGKCDIWFHSHQLFHIFVVAGAFVHFHGVSNLQEFRFMIGGGCSEEDAL,Impairs response to ADIPOQ binding. Abolishes response to ADIPOQ binding; when associated with A-202; A-348 and A-352.,,MNEPTENRLGCSRTPEPDIRLRKGHQLDGTRRGDNDSHQGDLEPILEASVLSSHHKKSSEEHEYSDEAPQEDEGFMGMSPLLQAHHAMEKMEEFVCKVWEGRWRVIPHDVLPDWLKDNDFLLHGHRPPMPSFRACFKSIFRIHTETGNIWTHLLGCVFFLCLGIFYMFRPNISFVAPLQEKVVFGLFFLGAILCLSFSWLFHTVYCHSEGVSRLFSKLDYSGIALLIMGSFVPWLYYSFYCNPQPCFIYLIVICVLGIAAIIVSQWDMFATPQYRGVRAGVFLGLGLSGIIPTLHYVISEGFLKAATIGQIGWLMLMASLYITGAALYAARIPERFFPGKCDIWFHSHQLFHIFVVAGAFVHFHGVSNLQEFRFMIGGGCSEEDAL,Adiponectin receptor protein 2,"Receptor for ADIPOQ, an essential hormone secreted by adipocytes that regulates glucose and lipid metabolism. Required for normal body fat and glucose homeostasis. ADIPOQ-binding activates a signaling cascade that leads to increased PPARA activity, and ultimately to increased fatty acid oxidation and glucose uptake. Has intermediate affinity for globular and full-length adiponectin. Required for normal revascularization after chronic ischemia caused by severing of blood vessels.",,Impairs response to ADIPOQ binding. Abolishes response to ADIPOQ binding; when associated with A-202; A-348 and A-352.
1055,1055,1055,76492,Q8BHY3-P658G,MRVPEKYSTLPAEDRSVHIVNICAIEDLGYLPSEGTLLNSLSVDPDAECKYGLYFRDGKRKVDYILVYHHKRASGSRTLARRGLQNDMVLGTRSVRQDQPLPGKGSPVDAGSPEVPMDYHEDDKRFRREEYEGNLLEAGLELENDEDTKIHGVGFVKIHAPWHVLCREAEFLKLKMPTKKVYHISETRGLLKTINSVLQKITDPIQPKVAEHRPQTTKRLSYPFSREKQHLFDLTDRDSFFDSKTRSTIVYEILKRTTCTKAKYSMGITSLLANGVYSAAYPLHDGDYEGDNVEFNDRKLLYEEWASYGVFYKYQPIDLVRKYFGEKVGLYFAWLGAYTQMLIPASIVGVIVFLYGCATVDENIPSMEMCDQRYNITMCPLCDKTCSYWKMSSACATARASHLFDNPATVFFSVFMALWAATFMEHWKRKQMRLNYRWDLTGFEEEEEAVKDHPRAEYEARVLEKSLRKESRNKETDKVKLTWRDRFPAYFTNLVSIIFMIAVTFAIVLGVIIYRISTAAALAMNSSPSVRSNIRVTVTATAVIINLVVIILLDEVYGCIARWLTKIEVPKTEKSFEERLTFKAFLLKFVNSYTPIFYVAFFKGRFVGRPGDYVYIFRSFRMEECAPGGCLMELCIQLSIIMLGKQLIQNNLFEIGIGKMKKFIRYLKLRRQSPSDREEYVKRKQRYEVDFNLEPFAGLTPEYMEMIIQFGFVTLFVASFPLAPLFALLNNIIEIRLDAKKFVTELRRPVAIRAKDIGIWYNILRGVGKLAVIINAFVISFTSDFIPRLVYLYMYSQNGTMHGFVNHTLSSFNVSDFQNGTAPNDPLDLGYEVQICRYKDYREPPWSEHKYDISKDFWAVLAARLAFVIVFQNLVMFMSDFVDWVIPDIPKDISQQIHKEKVLMVELFMREEQGKQQLLDTWMEKEKPRDVPCNNHSPTTHPEAGDGSPVPSYEYHGDAL,Moderately increased threshold for activation by calcium.,,MRVPEKYSTLPAEDRSVHIVNICAIEDLGYLPSEGTLLNSLSVDPDAECKYGLYFRDGKRKVDYILVYHHKRASGSRTLARRGLQNDMVLGTRSVRQDQPLPGKGSPVDAGSPEVPMDYHEDDKRFRREEYEGNLLEAGLELENDEDTKIHGVGFVKIHAPWHVLCREAEFLKLKMPTKKVYHISETRGLLKTINSVLQKITDPIQPKVAEHRPQTTKRLSYPFSREKQHLFDLTDRDSFFDSKTRSTIVYEILKRTTCTKAKYSMGITSLLANGVYSAAYPLHDGDYEGDNVEFNDRKLLYEEWASYGVFYKYQPIDLVRKYFGEKVGLYFAWLGAYTQMLIPASIVGVIVFLYGCATVDENIPSMEMCDQRYNITMCPLCDKTCSYWKMSSACATARASHLFDNPATVFFSVFMALWAATFMEHWKRKQMRLNYRWDLTGFEEEEEAVKDHPRAEYEARVLEKSLRKESRNKETDKVKLTWRDRFPAYFTNLVSIIFMIAVTFAIVLGVIIYRISTAAALAMNSSPSVRSNIRVTVTATAVIINLVVIILLDEVYGCIARWLTKIEVPKTEKSFEERLTFKAFLLKFVNSYTPIFYVAFFKGRFVGRPGDYVYIFRSFRMEECAPGGCLMELCIQLSIIMLGKQLIQNNLFEIGIPKMKKFIRYLKLRRQSPSDREEYVKRKQRYEVDFNLEPFAGLTPEYMEMIIQFGFVTLFVASFPLAPLFALLNNIIEIRLDAKKFVTELRRPVAIRAKDIGIWYNILRGVGKLAVIINAFVISFTSDFIPRLVYLYMYSQNGTMHGFVNHTLSSFNVSDFQNGTAPNDPLDLGYEVQICRYKDYREPPWSEHKYDISKDFWAVLAARLAFVIVFQNLVMFMSDFVDWVIPDIPKDISQQIHKEKVLMVELFMREEQGKQQLLDTWMEKEKPRDVPCNNHSPTTHPEAGDGSPVPSYEYHGDAL,Anoctamin-1,"Calcium-activated chloride channel (CaCC). Plays a role in transepithelial anion transport and smooth muscle contraction. Required for the normal functioning of the interstitial cells of Cajal (ICCs) which generate electrical pacemaker activity in gastrointestinal smooth muscles. Acts as a major contributor to basal and stimulated chloride conductance in airway epithelial cells and plays an important role in tracheal cartilage development. Required for CFTR activation by enhancing endoplasmic reticulum Ca(2+) store release and is also required for CFTR membrane expression. Required for basal and ATP-dependent mucus secretion in airways and intestine, probably by controlling exocytosis of mucus-filled granules by providing Ca(2+) to an apical signaling compartment. Contributes to airway mucus expression induced by interleukins IL3 and IL8 and by the asthma-associated protein CLCA1 and is required for expression of mucin MUC5AC. However, was shown in another study not to be required for MUC5AC expression. Plays a role in the propagation of Ca(2+) waves in Kolliker's organ in the cochlea and contributes to the refinement of auditory brainstem circuitries prior to hearing onset. In vomeronasal sensory neurons, modulates spontaneous firing patterns in the absence of stimuli as well as the firing pattern of pheromone-evoked activity. Responsible for calcium-activated chloride channel activity in type I taste cells of the vallate papillae. Acts as a heat sensor in nociceptive neurons. In dorsal root ganglion neurons, plays a role in mediating non-histaminergic Mas-related G-protein coupled receptor (MRGPR)-dependent itching, acting as a downstream effector of MRGPRs. In the developing brain, required for the Ca(2+)-dependent process extension of radial glial cells.","The mutation in TMEM16A alters the electrostatic properties of the ion conduction path and triggers a conformational rearrangement of an α-helix that comes into physical contact with the bound ligand, and thereby directly couples ligand binding and pore opening.","Moderately increased threshold for activation by calcium. The mutation in TMEM16A alters the electrostatic properties of the ion conduction path and triggers a conformational rearrangement of an α-helix that comes into physical contact with the bound ligand, and thereby directly couples ligand binding and pore opening."
1058,1058,1058,76719,Q6SSJ6-V257A,MQFHLNGFRPGNPLIAPASPLAPAHTEAVPSQVDVLIVGCGPAGLTLAAQLAAFPDIRTCIVEQKEGPMELGQADGIACRTMEMFEAFEFADSILKEACWINDVTFWKPDPAQPGRIARHGRVQDTEDGLSEFPHVILNQARVHDHYLERMRNSPSRLEPHYARRVLDVKIDHGAADYPVTVTLERCDAAHAGQIETVQARYVVGCDGARSNVRRAIGRQLVGDSANQAWGVMDVLAVTDFPDVRYKVAIQSEQGNALIIPREGGHLVRFYVEMDKLDADERVASRNITVEQLIATAQRVLHPYKLDVKNVPWWSVYEIGQRICAKYDDVADAVATPDSPLPRVFIAGDACHTHSPKAGQGMNFSMQDSFNLGWKLAAVLRKQCAPELLHTYSSERQVVAQQLIDFDREWAKMFSDPAKEGGQGGVDPKEFQKYFEQHGRFTAGVGTHYAPSLLTGQASHQALASGFTVGMRFHSAPVVRVSDAKPLQLGHCGKADGRWRLYAFAGQNDLAQPESGLLALCRFLESDAASPLRRFTPSGQDIDSIFDLRAIFPQAYTEVALETLPALLLPPKGQLGMIDYEKVFSPDLKNAGQDIFELRGIDRQQGALVVVRPDQYVAQVLPLGDHAALSAYFESFMRA,Broadens the substrate range rendering it able to transform phenol to catechol.,,MQFHLNGFRPGNPLIAPASPLAPAHTEAVPSQVDVLIVGCGPAGLTLAAQLAAFPDIRTCIVEQKEGPMELGQADGIACRTMEMFEAFEFADSILKEACWINDVTFWKPDPAQPGRIARHGRVQDTEDGLSEFPHVILNQARVHDHYLERMRNSPSRLEPHYARRVLDVKIDHGAADYPVTVTLERCDAAHAGQIETVQARYVVGCDGARSNVRRAIGRQLVGDSANQAWGVMDVLAVTDFPDVRYKVAIQSEQGNVLIIPREGGHLVRFYVEMDKLDADERVASRNITVEQLIATAQRVLHPYKLDVKNVPWWSVYEIGQRICAKYDDVADAVATPDSPLPRVFIAGDACHTHSPKAGQGMNFSMQDSFNLGWKLAAVLRKQCAPELLHTYSSERQVVAQQLIDFDREWAKMFSDPAKEGGQGGVDPKEFQKYFEQHGRFTAGVGTHYAPSLLTGQASHQALASGFTVGMRFHSAPVVRVSDAKPLQLGHCGKADGRWRLYAFAGQNDLAQPESGLLALCRFLESDAASPLRRFTPSGQDIDSIFDLRAIFPQAYTEVALETLPALLLPPKGQLGMIDYEKVFSPDLKNAGQDIFELRGIDRQQGALVVVRPDQYVAQVLPLGDHAALSAYFESFMRA,3-hydroxybenzoate 4-monooxygenase,"Converts 3-hydroxybenzoate (m-hydroxybenzoate), and to a lesser extent p-hydroxybenzoate, to 3,4-dihydroxybenzoate (protocatechuate). Also acts on a number of analogs of 3-hydroxybenzoate substituted in the 2, 4, 5 and 6 positions.","The mutant MobA with a single substitution was able to transform phenol to catechol, providing the first example of monooxygenase acting on phenolic acids that can also hydroxylate phenol. The mutant MobA also has enhanced ability to transform resorcinol, hydroquinone, p-hydroxybenzoate, 2, 5-dihydroxybenzoate, 3, 4-dihydroxybenzoate, 3-chlorophenol, 4-chlorophenol, 4-chlororesorcinol, and 4-nitrophenol.","Broadens the substrate range rendering it able to transform phenol to catechol. The mutant MobA with a single substitution was able to transform phenol to catechol, providing the first example of monooxygenase acting on phenolic acids that can also hydroxylate phenol. The mutant MobA also has enhanced ability to transform resorcinol, hydroquinone, p-hydroxybenzoate, 2, 5-dihydroxybenzoate, 3, 4-dihydroxybenzoate, 3-chlorophenol, 4-chlorophenol, 4-chlororesorcinol, and 4-nitrophenol."
1067,1067,1067,77230,Q03164-R12A,MAHSCRWRFPAAPGTTGGGGGGGRRGLGGAPRQRVPALLLPPGPPVGGGGPGAPPSPPAVAAAAAAAGSSGAGVPGGAAAASAASSSSASSSSSSSSSASSGPALLRVGPGFDAALQVSAAIGTNLRRFRAVFGESGGGGGSGEDEQFLGFGSDEEVRVRSPTRSPSVKTSPRKPRGRPRSGSDRNSAILSDPSVFSPLNKSETKSGDKIKKKDSKSIEKKRGRPPTFPGVKIKITHGKDISELPKGNKEDSLKKIKRTPSATFQQATKIKKLRAGKLSPLKSKFKTGKLQIGRKGVQIVRRRGRPPSTERIKTPSGLLINSELEKPQKVRKDKEGTPPLTKEDKTVVRQSPRRIKPVRIIPSSKRTDATIAKQLLQRAKKGAQKKIEKEAAQLQGRKVKTQVKNIRQFIMPVVSAISSRIIKTPRRFIEDEDYDPPIKIARLESTPNSRFSAPSCGSSEKSSAASQHSSQMSSDSSRSSSPSVDTSTDSQASEEIQVLPEERSDTPEVHPPLPISQSPENESNDRRSRRYSVSERSFGSRTTKKLSTLQSAPQQQTSSSPPPPLLTPPPPLQPASSISDHTPWLMPPTIPLASPFLPASTAPMQGKRKSILREPTFRWTSLKHSRSEPQYFSSAKYAKEGLIRKPIFDNFRPPPLTPEDVGFASGFSASGTAASARLFSPLHSGTRFDMHKRSPLLRAPRFTPSEAHSRIFESVTLPSNRTSAGTSSSGVSNRKRKRKVFSPIRSEPRSPSHSMRTRSGRLSSSELSPLTPPSSVSSSLSISVSPLATSALNPTFTFPSHSLTQSGESAEKNQRPRKQTSAPAEPFSSSSPTPLFPWFTPGSQTERGRNKDKAPEELSKDRDADKSVEKDKSRERDREREKENKRESRKEKRKKGSEIQSSSALYPVGRVSKEKVVGEDVATSSSAKKATGRKKSSSHDSGTDITSVTLGDTTAVKTKILIKKGRGNLEKTNLDLGPTAPSLEKEKTLCLSTPSSSTVKHSTSSIGSMLAQADKLPMTDKRVA,Reduced interaction with MEN1.,,MAHSCRWRFPARPGTTGGGGGGGRRGLGGAPRQRVPALLLPPGPPVGGGGPGAPPSPPAVAAAAAAAGSSGAGVPGGAAAASAASSSSASSSSSSSSSASSGPALLRVGPGFDAALQVSAAIGTNLRRFRAVFGESGGGGGSGEDEQFLGFGSDEEVRVRSPTRSPSVKTSPRKPRGRPRSGSDRNSAILSDPSVFSPLNKSETKSGDKIKKKDSKSIEKKRGRPPTFPGVKIKITHGKDISELPKGNKEDSLKKIKRTPSATFQQATKIKKLRAGKLSPLKSKFKTGKLQIGRKGVQIVRRRGRPPSTERIKTPSGLLINSELEKPQKVRKDKEGTPPLTKEDKTVVRQSPRRIKPVRIIPSSKRTDATIAKQLLQRAKKGAQKKIEKEAAQLQGRKVKTQVKNIRQFIMPVVSAISSRIIKTPRRFIEDEDYDPPIKIARLESTPNSRFSAPSCGSSEKSSAASQHSSQMSSDSSRSSSPSVDTSTDSQASEEIQVLPEERSDTPEVHPPLPISQSPENESNDRRSRRYSVSERSFGSRTTKKLSTLQSAPQQQTSSSPPPPLLTPPPPLQPASSISDHTPWLMPPTIPLASPFLPASTAPMQGKRKSILREPTFRWTSLKHSRSEPQYFSSAKYAKEGLIRKPIFDNFRPPPLTPEDVGFASGFSASGTAASARLFSPLHSGTRFDMHKRSPLLRAPRFTPSEAHSRIFESVTLPSNRTSAGTSSSGVSNRKRKRKVFSPIRSEPRSPSHSMRTRSGRLSSSELSPLTPPSSVSSSLSISVSPLATSALNPTFTFPSHSLTQSGESAEKNQRPRKQTSAPAEPFSSSSPTPLFPWFTPGSQTERGRNKDKAPEELSKDRDADKSVEKDKSRERDREREKENKRESRKEKRKKGSEIQSSSALYPVGRVSKEKVVGEDVATSSSAKKATGRKKSSSHDSGTDITSVTLGDTTAVKTKILIKKGRGNLEKTNLDLGPTAPSLEKEKTLCLSTPSSSTVKHSTSSIGSMLAQADKLPMTDKRVA,Histone-lysine N-methyltransferase 2A,"Histone methyltransferase that plays an essential role in early development and hematopoiesis. Catalytic subunit of the MLL1/MLL complex, a multiprotein complex that mediates both methylation of 'Lys-4' of histone H3 (H3K4me) complex and acetylation of 'Lys-16' of histone H4 (H4K16ac). Catalyzes methyl group transfer from S-adenosyl-L-methionine to the epsilon-amino group of 'Lys-4' of histone H3 (H3K4) via a non-processive mechanism. Part of chromatin remodeling machinery predominantly forms H3K4me1 and H3K4me2 methylation marks at active chromatin sites where transcription and DNA repair take place. Has weak methyltransferase activity by itself, and requires other component of the MLL1/MLL complex to obtain full methyltransferase activity. Has no activity toward histone H3 phosphorylated on 'Thr-3', less activity toward H3 dimethylated on 'Arg-8' or 'Lys-9', while it has higher activity toward H3 acetylated on 'Lys-9'. Binds to unmethylated CpG elements in the promoter of target genes and helps maintain them in the nonmethylated state. Required for transcriptional activation of HOXA9. Promotes PPP1R15A-induced apoptosis. Plays a critical role in the control of circadian gene expression and is essential for the transcriptional activation mediated by the CLOCK-BMAL1 heterodimer. Establishes a permissive chromatin state for circadian transcription by mediating a rhythmic methylation of 'Lys-4' of histone H3 (H3K4me) and this histone modification directs the circadian acetylation at H3K9 and H3K14 allowing the recruitment of CLOCK-BMAL1 to chromatin. Also has auto-methylation activity on Cys-3882 in absence of histone H3 substrate.",,Reduced interaction with MEN1.
1075,1075,1075,77915,Q86X52-P539R,MAARGRRAWLSVLLGLVLGFVLASRLVLPRASELKRAGPRRRASPEGCRSGQAAASQAGGARGDARGAQLWPPGSDPDGGPRDRNFLFVGVMTAQKYLQTRAVAAYRTWSKTIPGKVQFFSSEGSDTSVPIPVVPLRGVDDSYPPQKKSFMMLKYMHDHYLDKYEWFMRADDDVYIKGDRLENFLRSLNSSEPLFLGQTGLGTTEEMGKLALEPGENFCMGGPGVIMSREVLRRMVPHIGKCLREMYTTHEDVEVGRCVRRFAGVQCVWSYEMQQLFYENYEQNKKGYIRDLHNSKIHQAITLHPNKNPPYQYRLHSYMLSRKISELRHRTIQLHREIVLMSKYSNTEIHKEDLQLGIPPSFMRFQPRQREEILEWEFLTGKYLYSAVDGQPPRRGMDSAQREALDDIVMQVMEMINANAKTRGRIIDFKEIQYGYRRVNPMYGAEYILDLLLLYKKHKGKKMTVPVRRHAYLQQTFSKIQFVEHEELDAQELAKRINQESGSLSFLSNSLKKLVPFQLPGSKSEHKEPKDKKINILIRLSGRFDMFVRFMGNFEKTCLIPNQNVKLVVLLFNSDSNPDKAKQVELMRDYRIKYPKADMQILPVSGEFSRALALEVGSSQFNNESLLFFCDVDLVFTTEFLQRCRANTVLGQQIYFPIIFSQYDPKIVYSGKVPSDNHFAFTQKTGFWRNYGFGITCIYKGDLVRVGGFDVSIQGWGLEDVDLFNKVVQAGLKTFRSQEVGVVHVHHPVFCDPNLDPKQYKMCLGSKASTYGSTQQLAEMWLEKNDPSYSKSSNNNGSVRTA,In TPBS.,,MAARGRRAWLSVLLGLVLGFVLASRLVLPRASELKRAGPRRRASPEGCRSGQAAASQAGGARGDARGAQLWPPGSDPDGGPRDRNFLFVGVMTAQKYLQTRAVAAYRTWSKTIPGKVQFFSSEGSDTSVPIPVVPLRGVDDSYPPQKKSFMMLKYMHDHYLDKYEWFMRADDDVYIKGDRLENFLRSLNSSEPLFLGQTGLGTTEEMGKLALEPGENFCMGGPGVIMSREVLRRMVPHIGKCLREMYTTHEDVEVGRCVRRFAGVQCVWSYEMQQLFYENYEQNKKGYIRDLHNSKIHQAITLHPNKNPPYQYRLHSYMLSRKISELRHRTIQLHREIVLMSKYSNTEIHKEDLQLGIPPSFMRFQPRQREEILEWEFLTGKYLYSAVDGQPPRRGMDSAQREALDDIVMQVMEMINANAKTRGRIIDFKEIQYGYRRVNPMYGAEYILDLLLLYKKHKGKKMTVPVRRHAYLQQTFSKIQFVEHEELDAQELAKRINQESGSLSFLSNSLKKLVPFQLPGSKSEHKEPKDKKINILIPLSGRFDMFVRFMGNFEKTCLIPNQNVKLVVLLFNSDSNPDKAKQVELMRDYRIKYPKADMQILPVSGEFSRALALEVGSSQFNNESLLFFCDVDLVFTTEFLQRCRANTVLGQQIYFPIIFSQYDPKIVYSGKVPSDNHFAFTQKTGFWRNYGFGITCIYKGDLVRVGGFDVSIQGWGLEDVDLFNKVVQAGLKTFRSQEVGVVHVHHPVFCDPNLDPKQYKMCLGSKASTYGSTQQLAEMWLEKNDPSYSKSSNNNGSVRTA,Chondroitin sulfate synthase 1,"Has both beta-1,3-glucuronic acid and beta-1,4-N-acetylgalactosamine transferase activity. Transfers glucuronic acid (GlcUA) from UDP-GlcUA and N-acetylgalactosamine (GalNAc) from UDP-GalNAc to the non-reducing end of the elongating chondroitin polymer. Involved in the negative control of osteogenesis likely through the modulation of NOTCH signaling.","Loss of human CHSY1 function causes autosomal-recessive Temtamy preaxial brachydactyly syndrome (TPBS), mainly characterized by limb malformations, short stature, and hearing loss.","In TPBS. Loss of human CHSY1 function causes autosomal-recessive Temtamy preaxial brachydactyly syndrome (TPBS), mainly characterized by limb malformations, short stature, and hearing loss."
1085,1085,1085,78630,Q9NPJ1-L454P,MSRLEAKKPSLCKSEPLTTERVRTTLSVLKRIVTSCYGPSGRLKQLHNGFGGYVCTTSQSSALLSHLLVTHPILKILTASIQNHVSSFSDCGLFTAILCCNLIENVQRLGLTPTTVIRLNKHLLSLCISYLKSETCGCRIPVDFSSTQILLCLVRSILTSKPACMLTRKETEHVSALILRAFLLTIPENAEGHIILGKSLIVPLKGQRVIDSTVLPGILIEMSEVQLMRLLPIKKSTALKVALFCTTLSGDTSDTGEGTVVVSYGVSLENAVLDQLLNLGRQLISDHVDLVLCQKVIHPSLKQFLNMHRIIAIDRIGVTLMEPLTKMTGTQPIGSLGSICPNSYGSVKDVCTAKFGSKHFFHLIPNEATICSLLLCNRNDTAWDELKLTCQTALHVLQLTLKEPWALLGGGCTETHLAAYIRHKTHNDPESILKDDECTQTELQLIAEAFCSAPESVVGSLEHDGGEILTDMKYGHLWSVQADSPCVANWPDLLSQCGCGLYNSQEELNWSFLRSTRRPFVPQSCLPHEAVGSASNLTLDCLTAKLSGLQVAVETANLILDLSYVIEDKN,No effect on import to the nucleus.,,MSRLEAKKPSLCKSEPLTTERVRTTLSVLKRIVTSCYGPSGRLKQLHNGFGGYVCTTSQSSALLSHLLVTHPILKILTASIQNHVSSFSDCGLFTAILCCNLIENVQRLGLTPTTVIRLNKHLLSLCISYLKSETCGCRIPVDFSSTQILLCLVRSILTSKPACMLTRKETEHVSALILRAFLLTIPENAEGHIILGKSLIVPLKGQRVIDSTVLPGILIEMSEVQLMRLLPIKKSTALKVALFCTTLSGDTSDTGEGTVVVSYGVSLENAVLDQLLNLGRQLISDHVDLVLCQKVIHPSLKQFLNMHRIIAIDRIGVTLMEPLTKMTGTQPIGSLGSICPNSYGSVKDVCTAKFGSKHFFHLIPNEATICSLLLCNRNDTAWDELKLTCQTALHVLQLTLKEPWALLGGGCTETHLAAYIRHKTHNDPESILKDDECTQTELQLIAEAFCSALESVVGSLEHDGGEILTDMKYGHLWSVQADSPCVANWPDLLSQCGCGLYNSQEELNWSFLRSTRRPFVPQSCLPHEAVGSASNLTLDCLTAKLSGLQVAVETANLILDLSYVIEDKN,Molecular chaperone MKKS,"Probable molecular chaperone that assists the folding of proteins upon ATP hydrolysis. Plays a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. May play a role in protein processing in limb, cardiac and reproductive system development. May play a role in cytokinesis.",,No effect on import to the nucleus.
1090,1090,1090,78801,O31608-E85A,MLNSANTTAPSLLSAYGLNSYTSSNSGSVTKAAESTETAVADSASNKHEANQIRSGDFSIDSAIKKAADKYGVDEKLIRAVIKQASGFNAKAVSGAGAMGLMQLMPSTASSLGVSNPLDPQQNVEGGTKYLKQMLDKYDGNVSMALAAYNAGPGNVDRYGGIPPFQETQNYVKKITSVYYA,Lacks both muramidase and transglycosylase activities. Confers a defect in swarming motility.,,MLNSANTTAPSLLSAYGLNSYTSSNSGSVTKAAESTETAVADSASNKHEANQIRSGDFSIDSAIKKAADKYGVDEKLIRAVIKQESGFNAKAVSGAGAMGLMQLMPSTASSLGVSNPLDPQQNVEGGTKYLKQMLDKYDGNVSMALAAYNAGPGNVDRYGGIPPFQETQNYVKKITSVYYA,Bifunctional muramidase/lytic transglycosylase CwlQ,"Exhibits both muramidase and lytic transglycosidase activities. Cleaves the beta-1,4-glycosidic bond between N-acetylmuramic acid and N-acetylglucosamine (MurNAc-GlcNAc) in peptidoglycan, producing both N-acetylmuramic acid and 1,6-anhydro-N-acetylmuramic acid. Is conditionally required for swarming motility and may play a role in flagella function specifically on harder surface environments, but is not required for flagellar assembly.",Glutamic acid 85 (E-85) is an amino acid residue essential to both activities. Cells mutated for the lytic transglycosylase CwlQ exhibit a severe defect in flagellum-dependent swarming motility.,Lacks both muramidase and transglycosylase activities. Confers a defect in swarming motility. Glutamic acid 85 (E-85) is an amino acid residue essential to both activities. Cells mutated for the lytic transglycosylase CwlQ exhibit a severe defect in flagellum-dependent swarming motility.
1097,1097,1097,79121,Q96IZ0-L69I,MATGGYRTSSGLGGSTTDFLEEWKAKREKMRAKQNPPGPAPPGGGSSDAAGKPPAGALGTPAAAAANEINNNLPGGAPAAPAVPGPGGVNCAVGSAMLTRAAPGPRRSEDEPPAASASAAPPPQRDEEEPDGVPEKGKSSGPSARKGKGQIEKRKLREKRRSTGVVNIPAAECLDEYEDDEAGQKERKREDAITQQNTIQNEAVNLLDPGSSYLLQEPPRTVSGRYKSTTSVSEEDVSSRYSRTDRSGFPRYNRDANVSGTLVSSSTLEKKIEDLEKEVVRERQENLRLVRLMQDKEEMIGKLKEEIDLLNRDLDDIEDENEQLKQENKTLLKVVGQLTR,"Only slighlty increased interaction with SPSB2. Only slightly increased interaction with SPSB4. Increased interaction with SPSB1, SPSB2 and SPSB4; when associated with A-68.",,MATGGYRTSSGLGGSTTDFLEEWKAKREKMRAKQNPPGPAPPGGGSSDAAGKPPAGALGTPAAAAANELNNNLPGGAPAAPAVPGPGGVNCAVGSAMLTRAAPGPRRSEDEPPAASASAAPPPQRDEEEPDGVPEKGKSSGPSARKGKGQIEKRKLREKRRSTGVVNIPAAECLDEYEDDEAGQKERKREDAITQQNTIQNEAVNLLDPGSSYLLQEPPRTVSGRYKSTTSVSEEDVSSRYSRTDRSGFPRYNRDANVSGTLVSSSTLEKKIEDLEKEVVRERQENLRLVRLMQDKEEMIGKLKEEIDLLNRDLDDIEDENEQLKQENKTLLKVVGQLTR,PRKC apoptosis WT1 regulator protein,"Pro-apoptotic protein capable of selectively inducing apoptosis in cancer cells, sensitizing the cells to diverse apoptotic stimuli and causing regression of tumors in animal models. Induces apoptosis in certain cancer cells by activation of the Fas prodeath pathway and coparallel inhibition of NF-kappa-B transcriptional activity. Inhibits the transcriptional activation and augments the transcriptional repression mediated by WT1. Down-regulates the anti-apoptotic protein BCL2 via its interaction with WT1. Seems also to be a transcriptional repressor by itself. May be directly involved in regulating the amyloid precursor protein (APP) cleavage activity of BACE1.",Mutation of L69 to I enhanced binding to SPSB proteins.,"Only slighlty increased interaction with SPSB2. Only slightly increased interaction with SPSB4. Increased interaction with SPSB1, SPSB2 and SPSB4; when associated with A-68. Mutation of L69 to I enhanced binding to SPSB proteins."
1100,1100,1100,79713,O14929-E64A,MAGFGAMEKFLVEYKSAVEKKLAEYKCNTNTAIELKLVRFPEDLENDIRTFFPEYTHQLFGDDATAFGYKGLKILLYYIAGSLSTMFRVEYASKVDENFDCVEADDVEGKIRQIIPPGFCTNTNDFLSLLEKEVDFKPFGTLLHTYSVLSPTGGENFTFQIYKADMTCRGFREYHERLQTFLMWFIETASFIDVDDERWHYFLVFEKYNKDGATLFATVGYMTVYNYYVYPDKTRPRVSQMLILTPFQGQGHGAQLLETVHRYYTEFPTVLDITAEDPSKSYVKLRDFVLVKLCQDLPCFSREKLMQGFNEDMVIEAQQKFKINKQHARRVYEILRLLVTDMSDAEQYRSYRLDIKRRLISPYKKKQRDLAKMRKCLRPEELTNQMNQIEISMQHEQLEESFQELVEDYRRVIERLAQE,Strongly reduces HAT activity.,,MAGFGAMEKFLVEYKSAVEKKLAEYKCNTNTAIELKLVRFPEDLENDIRTFFPEYTHQLFGDDETAFGYKGLKILLYYIAGSLSTMFRVEYASKVDENFDCVEADDVEGKIRQIIPPGFCTNTNDFLSLLEKEVDFKPFGTLLHTYSVLSPTGGENFTFQIYKADMTCRGFREYHERLQTFLMWFIETASFIDVDDERWHYFLVFEKYNKDGATLFATVGYMTVYNYYVYPDKTRPRVSQMLILTPFQGQGHGAQLLETVHRYYTEFPTVLDITAEDPSKSYVKLRDFVLVKLCQDLPCFSREKLMQGFNEDMVIEAQQKFKINKQHARRVYEILRLLVTDMSDAEQYRSYRLDIKRRLISPYKKKQRDLAKMRKCLRPEELTNQMNQIEISMQHEQLEESFQELVEDYRRVIERLAQE,Histone acetyltransferase type B catalytic subunit,"Histone acetyltransferase that plays a role in different biological processes including cell cycle progression, glucose metabolism, histone production or DNA damage repair. Coordinates histone production and acetylation via H4 promoter binding. Acetylates histone H4 at 'Lys-5' (H4K5ac) and 'Lys-12' (H4K12ac) and, to a lesser extent, histone H2A at 'Lys-5' (H2AK5ac). Drives H4 production by chromatin binding to support chromatin replication and acetylation. Since transcription of H4 genes is tightly coupled to S-phase, plays an important role in S-phase entry and progression. Promotes homologous recombination in DNA repair by facilitating histone turnover and incorporation of acetylated H3.3 at sites of double-strand breaks. In addition, acetylates other substrates such as chromatin-related proteins. Acetylates also RSAD2 which mediates the interaction of ubiquitin ligase UBE4A with RSAD2 leading to RSAD2 ubiquitination and subsequent degradation.(Microbial infection) Contributes to hepatitis B virus (HBV) replication by acetylating histone H4 at the sites of 'Lys-5' and 'Lys-12' on the covalently closed circular DNA (cccDNA) minichromosome leading to its accumulation within the host cell.","The crystal structure reveals that the side chain of lysine 12 of histone H4 peptide interacts with the enzyme including the invariant residue E64. Therefore, mutation may disrupt this interaction and affect the substrate-binding specificity of histone acetyltransferase 1.","Strongly reduces HAT activity. The crystal structure reveals that the side chain of lysine 12 of histone H4 peptide interacts with the enzyme including the invariant residue E64. Therefore, mutation may disrupt this interaction and affect the substrate-binding specificity of histone acetyltransferase 1."
1117,1117,1117,80990,P35523-V536L,MEQSRSQQRGGEQSWWGSDPQYQYMPFEHCTSYGLPSENGGLQHRLRKDAGPRHNVHPTQIYGHHKEQFSDREQDIGMPKKTGSSSTVDSKDEDHYSKCQDCIHRLGQVVRRKLGEDGIFLVLLGLLMALVSWSMDYVSAKSLQAYKWSYAQMQPSLPLQFLVWVTFPLVLILFSALFCHLISPQAVGSGIPEMKTILRGVVLKEYLTMKAFVAKVVALTAGLGSGIPVGKEGPFVHIASICAAVLSKFMSVFCGVYEQPYYYSDILTVGCAVGVGCCFGTPLGGVLFSIEVTSTYFAVRNYWRGFFAATFSAFVFRVLAVWNKDAVTITALFRTNFRMDFPFDLKELPAFAAIGICCGLLGAVFVYLHRQVMLGVRKHKALSQFLAKHRLLYPGIVTFVIASFTFPPGMGQFMAGELMPREAISTLFDNNTWVKHAGDPESLGQSAVWIHPRVNVVIIIFLFFVMKFWMSIVATTMPIPCGGFMPVFVLGAAFGRLVGEIMAMLFPDGILFDDIIYKILPGGYAVIGAAALTGALSHTVSTAVICFELTGQIAHILPMMVAVILANMVAQSLQPSLYDSIIQVKKLPYLPDLGWNQLSKYTIFVEDIMVRDVKFVSASYTYGELRTLLQTTTVKTLPLVDSKDSMILLGSVERSELQALLQRHLCPERRLRAAQEMARKLSELPYDGKARLAGEGLPGAPPGRPESFAFVDEDEDEDLSGKSELPPSLALHPSTTAPLSPEEPNGPLPGHKQQPEAPEPAGQRPSIFQSLLHCLLGRARPTKKKTTQDSTDLVDNMSPEEIEAWEQEQLSQPVCFDSCCIDQSPFQLVEQTTLHKTHTLFSLLGLHLAYVTSMGKLRGVLALEELQKAIEGHTKSGVQLRPPLASFRNTTSTRKSTGAPPSSAENWNLPEDRPGATGTGDVIAASPETPVPSPSPEPPLSLAPGKVEGELEELELVESPGLEEELADILQGPSLRSTDEEDEDELIL,In MCAR; unknown pathological significance.,,MEQSRSQQRGGEQSWWGSDPQYQYMPFEHCTSYGLPSENGGLQHRLRKDAGPRHNVHPTQIYGHHKEQFSDREQDIGMPKKTGSSSTVDSKDEDHYSKCQDCIHRLGQVVRRKLGEDGIFLVLLGLLMALVSWSMDYVSAKSLQAYKWSYAQMQPSLPLQFLVWVTFPLVLILFSALFCHLISPQAVGSGIPEMKTILRGVVLKEYLTMKAFVAKVVALTAGLGSGIPVGKEGPFVHIASICAAVLSKFMSVFCGVYEQPYYYSDILTVGCAVGVGCCFGTPLGGVLFSIEVTSTYFAVRNYWRGFFAATFSAFVFRVLAVWNKDAVTITALFRTNFRMDFPFDLKELPAFAAIGICCGLLGAVFVYLHRQVMLGVRKHKALSQFLAKHRLLYPGIVTFVIASFTFPPGMGQFMAGELMPREAISTLFDNNTWVKHAGDPESLGQSAVWIHPRVNVVIIIFLFFVMKFWMSIVATTMPIPCGGFMPVFVLGAAFGRLVGEIMAMLFPDGILFDDIIYKILPGGYAVIGAAALTGAVSHTVSTAVICFELTGQIAHILPMMVAVILANMVAQSLQPSLYDSIIQVKKLPYLPDLGWNQLSKYTIFVEDIMVRDVKFVSASYTYGELRTLLQTTTVKTLPLVDSKDSMILLGSVERSELQALLQRHLCPERRLRAAQEMARKLSELPYDGKARLAGEGLPGAPPGRPESFAFVDEDEDEDLSGKSELPPSLALHPSTTAPLSPEEPNGPLPGHKQQPEAPEPAGQRPSIFQSLLHCLLGRARPTKKKTTQDSTDLVDNMSPEEIEAWEQEQLSQPVCFDSCCIDQSPFQLVEQTTLHKTHTLFSLLGLHLAYVTSMGKLRGVLALEELQKAIEGHTKSGVQLRPPLASFRNTTSTRKSTGAPPSSAENWNLPEDRPGATGTGDVIAASPETPVPSPSPEPPLSLAPGKVEGELEELELVESPGLEEELADILQGPSLRSTDEEDEDELIL,Chloride channel protein 1,Voltage-gated chloride channel. Plays an important role in membrane repolarization in skeletal muscle cells after muscle contraction. The CLC channel family contains both chloride channels and proton-coupled anion transporters that exchange chloride or another anion for protons (Probable). The absence of conserved gating glutamate residues is typical for family members that function as channels (Probable).,"The mutation in the CLCN1 gene causes functional changes in the chloride channel, but the specific effects are not mentioned in the document.","In MCAR; unknown pathological significance. The mutation in the CLCN1 gene causes functional changes in the chloride channel, but the specific effects are not mentioned in the document."
1124,1124,1124,81568,Q8NXR5-P39A,MNNLKWVAYFLKSRMNWIFWILFLNLLMLGISLIDYDFAIDSLFYIVSLNLSLTMIFLILTYFKEVKLYKHFDKDKEIEEIKHKDLAETPFQRHTVDYLYRQISAHKEKVVEQQLQLNMHEQTITEFVHDIKTPVTAMKLLIDQEKNQERKQALLYEWSRINSMLDTQLYITRLESQRKDMYFDYVSLKRMVIDEIQLTRHISQVKGIGFDVDFKVDDYVYTDIKWCRMIIRQILSNALKYSENFNIEIGTELNDQHVSLYIKDYGRGISKKDMPRIFERGFTSTANRNETTSSGMGLYLVNSVKDQLGIHLQVTSTVGKGTTVRLIFPLQNEIVERMSEVTNLSF,About 50% decreased resistance to host cationic antimicrobial peptides.,,MNNLKWVAYFLKSRMNWIFWILFLNLLMLGISLIDYDFPIDSLFYIVSLNLSLTMIFLILTYFKEVKLYKHFDKDKEIEEIKHKDLAETPFQRHTVDYLYRQISAHKEKVVEQQLQLNMHEQTITEFVHDIKTPVTAMKLLIDQEKNQERKQALLYEWSRINSMLDTQLYITRLESQRKDMYFDYVSLKRMVIDEIQLTRHISQVKGIGFDVDFKVDDYVYTDIKWCRMIIRQILSNALKYSENFNIEIGTELNDQHVSLYIKDYGRGISKKDMPRIFERGFTSTANRNETTSSGMGLYLVNSVKDQLGIHLQVTSTVGKGTTVRLIFPLQNEIVERMSEVTNLSF,Sensor protein kinase GraS,"Member of the two-component regulatory system GraR/GraS involved in resistance against cationic antimicrobial peptides (CAMPs). Functions as a sensor protein kinase which phosphorylates GraR through the auxiliary protein GraX. In turn, GraR up-regulates many genes such as adhesins, exoproteins, transporters, toxins, and proteins involved in cell wall synthesis. Down-regulates the expression of many genes involved in RNA and amino acid synthesis or glycolysis (By similarity).",The mutation in the GraS protein correlated with a moderate increase in susceptibility to HD-CAPs.,About 50% decreased resistance to host cationic antimicrobial peptides. The mutation in the GraS protein correlated with a moderate increase in susceptibility to HD-CAPs.
1126,1126,1126,81807,P42224-Y701C,MSQWYELQQLDSKFLEQVHQLYDDSFPMEIRQYLAQWLEKQDWEHAANDVSFATIRFHDLLSQLDDQYSRFSLENNFLLQHNIRKSKRNLQDNFQEDPIQMSMIIYSCLKEERKILENAQRFNQAQSGNIQSTVMLDKQKELDSKVRNVKDKVMCIEHEIKSLEDLQDEYDFKCKTLQNREHETNGVAKSDQKQEQLLLKKMYLMLDNKRKEVVHKIIELLNVTELTQNALINDELVEWKRRQQSACIGGPPNACLDQLQNWFTIVAESLQQVRQQLKKLEELEQKYTYEHDPITKNKQVLWDRTFSLFQQLIQSSFVVERQPCMPTHPQRPLVLKTGVQFTVKLRLLVKLQELNYNLKVKVLFDKDVNERNTVKGFRKFNILGTHTKVMNMEESTNGSLAAEFRHLQLKEQKNAGTRTNEGPLIVTEELHSLSFETQLCQPGLVIDLETTSLPVVVISNVSQLPSGWASILWYNMLVAEPRNLSFFLTPPCARWAQLSEVLSWQFSSVTKRGLNVDQLNMLGEKLLGPNASPDGLIPWTRFCKENINDKNFPFWLWIESILELIKKHLLPLWNDGCIMGFISKERERALLKDQQPGTFLLRFSESSREGAITFTWVERSQNGGEPDFHAVEPYTKKELSAVTFPDIIRNYKVMAAENIPENPLKYLYPNIDKDHAFGKYYSRPKEAPEPMELDGPKGTGCIKTELISVSEVHPSRLQTTDNLLPMSPEEFDEVSRIVGSVEFDSMMNTV,In IMD31B; disrupts transactivation activity in response to IFNG.,,MSQWYELQQLDSKFLEQVHQLYDDSFPMEIRQYLAQWLEKQDWEHAANDVSFATIRFHDLLSQLDDQYSRFSLENNFLLQHNIRKSKRNLQDNFQEDPIQMSMIIYSCLKEERKILENAQRFNQAQSGNIQSTVMLDKQKELDSKVRNVKDKVMCIEHEIKSLEDLQDEYDFKCKTLQNREHETNGVAKSDQKQEQLLLKKMYLMLDNKRKEVVHKIIELLNVTELTQNALINDELVEWKRRQQSACIGGPPNACLDQLQNWFTIVAESLQQVRQQLKKLEELEQKYTYEHDPITKNKQVLWDRTFSLFQQLIQSSFVVERQPCMPTHPQRPLVLKTGVQFTVKLRLLVKLQELNYNLKVKVLFDKDVNERNTVKGFRKFNILGTHTKVMNMEESTNGSLAAEFRHLQLKEQKNAGTRTNEGPLIVTEELHSLSFETQLCQPGLVIDLETTSLPVVVISNVSQLPSGWASILWYNMLVAEPRNLSFFLTPPCARWAQLSEVLSWQFSSVTKRGLNVDQLNMLGEKLLGPNASPDGLIPWTRFCKENINDKNFPFWLWIESILELIKKHLLPLWNDGCIMGFISKERERALLKDQQPGTFLLRFSESSREGAITFTWVERSQNGGEPDFHAVEPYTKKELSAVTFPDIIRNYKVMAAENIPENPLKYLYPNIDKDHAFGKYYSRPKEAPEPMELDGPKGTGYIKTELISVSEVHPSRLQTTDNLLPMSPEEFDEVSRIVGSVEFDSMMNTV,Signal transducer and activator of transcription 1-alpha/beta,"Signal transducer and transcription activator that mediates cellular responses to interferons (IFNs), cytokine KITLG/SCF and other cytokines and other growth factors. Following type I IFN (IFN-alpha and IFN-beta) binding to cell surface receptors, signaling via protein kinases leads to activation of Jak kinases (TYK2 and JAK1) and to tyrosine phosphorylation of STAT1 and STAT2. The phosphorylated STATs dimerize and associate with ISGF3G/IRF-9 to form a complex termed ISGF3 transcription factor, that enters the nucleus. ISGF3 binds to the IFN stimulated response element (ISRE) to activate the transcription of IFN-stimulated genes (ISG), which drive the cell in an antiviral state. In response to type II IFN (IFN-gamma), STAT1 is tyrosine- and serine-phosphorylated. It then forms a homodimer termed IFN-gamma-activated factor (GAF), migrates into the nucleus and binds to the IFN gamma activated sequence (GAS) to drive the expression of the target genes, inducing a cellular antiviral state. Becomes activated in response to KITLG/SCF and KIT signaling. May mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4.",,In IMD31B; disrupts transactivation activity in response to IFNG.
1142,1142,1142,83140,O75143-F444A,METDLNSQDRKDLDKFIKFFALKTVQVIVQARLGEKICTRSSSSPTGSDWFNLAIKDIPEVTHEAKKALAGQLPAVGRSMCVEISLKTSEGDSMELEIWCLEMNEKCDKEIKVSYTVYNRLSLLLKSLLAITRVTPAYRLSRKQGHEYVILYRIYFGEVQLSGLGEGFQTVRVGTVGTPVGTITLSCAYRINLAFMSTRQFERTPPIMGIIIDHFVDRPYPSSSPMHPCNYRTAGEDTGVIYPSVEDSQEVCTTSFSTSPPSQLSSSRLSYQPAALGVGSADLAYPVVFAAGLNATHPHQLMVPGKEGGVPLAPNQPVHGTQADQERLATCTPSDRTHCAATPSSSEDTETVSNSSEGRASPHDVLETIFVRKVGAFVNKPINQVTLTSLDIPFAMFAPKNLELEDTDPMVNPPDSPETESPLQGSLHSDGSSGGSSGNTHDDAVMIDFKPAFSKDDILPMDLGTFYREFQNPPQLSSLSIDIGAQSMAEDLDSLPEKLAVHEKNVREFDAFVETLQ,Decreases interaction with MAP1LC3A.,,METDLNSQDRKDLDKFIKFFALKTVQVIVQARLGEKICTRSSSSPTGSDWFNLAIKDIPEVTHEAKKALAGQLPAVGRSMCVEISLKTSEGDSMELEIWCLEMNEKCDKEIKVSYTVYNRLSLLLKSLLAITRVTPAYRLSRKQGHEYVILYRIYFGEVQLSGLGEGFQTVRVGTVGTPVGTITLSCAYRINLAFMSTRQFERTPPIMGIIIDHFVDRPYPSSSPMHPCNYRTAGEDTGVIYPSVEDSQEVCTTSFSTSPPSQLSSSRLSYQPAALGVGSADLAYPVVFAAGLNATHPHQLMVPGKEGGVPLAPNQPVHGTQADQERLATCTPSDRTHCAATPSSSEDTETVSNSSEGRASPHDVLETIFVRKVGAFVNKPINQVTLTSLDIPFAMFAPKNLELEDTDPMVNPPDSPETESPLQGSLHSDGSSGGSSGNTHDDFVMIDFKPAFSKDDILPMDLGTFYREFQNPPQLSSLSIDIGAQSMAEDLDSLPEKLAVHEKNVREFDAFVETLQ,Autophagy-related protein 13,"Autophagy factor required for autophagosome formation and mitophagy. Target of the TOR kinase signaling pathway that regulates autophagy through the control of the phosphorylation status of ATG13 and ULK1, and the regulation of the ATG13-ULK1-RB1CC1 complex. Through its regulation of ULK1 activity, plays a role in the regulation of the kinase activity of mTORC1 and cell proliferation.",,Decreases interaction with MAP1LC3A.
1154,1154,1154,84454,Q9H8V3-R586Q,MAENSVLTSTTGRTSLADSSIFDSKVTEISKENLLIGSTSYVEEEMPQIETRVILVQEAGKQEELIKALKTIKIMEVPVIKIKESCPGKSDEKLIKSVINMDIKVGFVKMESVEEFEGLDSPEFENVFVVTDFQDSVFNDLYKADCRVIGPPVVLNCSQKGEPLPFSCRPLYCTSMMNLVLCFTGFRKKEELVRLVTLVHHMGGVIRKDFNSKVTHLVANCTQGEKFRVAVSLGTPIMKPEWIYKAWERRNEQDFYAAVDDFRNEFKVPPFQDCILSFLGFSDEEKTNMEEMTEMQGGKYLPLGDERCTHLVVEENIVKDLPFEPSKKLYVVKQEWFWGSIQMDARAGETMYLYEKANTPELKKSVSMLSLNTPNSNRKRRRLKETLAQLSRETDVSPFPPRKRPSAEHSLSIGSLLDISNTPESSINYGDTPKSCTKSSKSSTPVPSKQSARWQVAKELYQTESNYVNILATIIQLFQVPLEEEGQRGGPILAPEEIKTIFGSIPDIFDVHTKIKDDLEDLIVNWDESKSIGDIFLKYSKDLVKTYPPFVNFFEMSKETIIKCEKQKPRFHAFLKINQAKPECGQQSLVELLIRPVQRLPSVALLLNDLKKHTADENPDKSTLEKAIGSLKEVMTHINEDKRKTEAQKQIFDVVYEVDGCPANLLSSHRSLVQRVETISLGEHPCDRGEQVTLFLFNDCLEIARKRHKVIGTFRSPHGQTRPPASLKHIHLMPLSQIKKVLDIRETEDCHNAFALLVRPPTEQANVLLSFQMTSDELPKENWLKMLCRHVANTICKADAENLIYTADPESFEVNTKDMDSTLSRASRAIKKTSKKVTRAFSFSKTPKRALRRALMTSHGSVEGRSPSSNDKHVMSRLSSTSSLAGIPSPSLVSLPSFFERRSHTLSRSTTHLI,Complete loss of GEF activity and failure to support cytokinesis.,,MAENSVLTSTTGRTSLADSSIFDSKVTEISKENLLIGSTSYVEEEMPQIETRVILVQEAGKQEELIKALKTIKIMEVPVIKIKESCPGKSDEKLIKSVINMDIKVGFVKMESVEEFEGLDSPEFENVFVVTDFQDSVFNDLYKADCRVIGPPVVLNCSQKGEPLPFSCRPLYCTSMMNLVLCFTGFRKKEELVRLVTLVHHMGGVIRKDFNSKVTHLVANCTQGEKFRVAVSLGTPIMKPEWIYKAWERRNEQDFYAAVDDFRNEFKVPPFQDCILSFLGFSDEEKTNMEEMTEMQGGKYLPLGDERCTHLVVEENIVKDLPFEPSKKLYVVKQEWFWGSIQMDARAGETMYLYEKANTPELKKSVSMLSLNTPNSNRKRRRLKETLAQLSRETDVSPFPPRKRPSAEHSLSIGSLLDISNTPESSINYGDTPKSCTKSSKSSTPVPSKQSARWQVAKELYQTESNYVNILATIIQLFQVPLEEEGQRGGPILAPEEIKTIFGSIPDIFDVHTKIKDDLEDLIVNWDESKSIGDIFLKYSKDLVKTYPPFVNFFEMSKETIIKCEKQKPRFHAFLKINQAKPECGRQSLVELLIRPVQRLPSVALLLNDLKKHTADENPDKSTLEKAIGSLKEVMTHINEDKRKTEAQKQIFDVVYEVDGCPANLLSSHRSLVQRVETISLGEHPCDRGEQVTLFLFNDCLEIARKRHKVIGTFRSPHGQTRPPASLKHIHLMPLSQIKKVLDIRETEDCHNAFALLVRPPTEQANVLLSFQMTSDELPKENWLKMLCRHVANTICKADAENLIYTADPESFEVNTKDMDSTLSRASRAIKKTSKKVTRAFSFSKTPKRALRRALMTSHGSVEGRSPSSNDKHVMSRLSSTSSLAGIPSPSLVSLPSFFERRSHTLSRSTTHLI,Protein ECT2,"Guanine nucleotide exchange factor (GEF) that catalyzes the exchange of GDP for GTP. Promotes guanine nucleotide exchange on the Rho family members of small GTPases, like RHOA, RHOC, RAC1 and CDC42. Required for signal transduction pathways involved in the regulation of cytokinesis. Component of the centralspindlin complex that serves as a microtubule-dependent and Rho-mediated signaling required for the myosin contractile ring formation during the cell cycle cytokinesis. Regulates the translocation of RHOA from the central spindle to the equatorial region. Plays a role in the control of mitotic spindle assembly; regulates the activation of CDC42 in metaphase for the process of spindle fibers attachment to kinetochores before chromosome congression. Involved in the regulation of epithelial cell polarity; participates in the formation of epithelial tight junctions in a polarity complex PARD3-PARD6-protein kinase PRKCQ-dependent manner. Plays a role in the regulation of neurite outgrowth. Inhibits phenobarbital (PB)-induced NR1I3 nuclear translocation. Stimulates the activity of RAC1 through its association with the oncogenic PARD6A-PRKCI complex in cancer cells, thereby acting to coordinately drive tumor cell proliferation and invasion. Also stimulates genotoxic stress-induced RHOB activity in breast cancer cells leading to their cell death.",The mutation in Ect2 dysregulates its function in vitro and in vivo.,Complete loss of GEF activity and failure to support cytokinesis. The mutation in Ect2 dysregulates its function in vitro and in vivo.
1155,1155,1155,84702,Q7RTT9-E206D,MGSVGSQRLEEPSVAGTPDPGVVMSFTFDSHQLEEAAEAAQGQGLRARGVPAFTDTTLDEPVPDDRYHAIYFAMLLAGVGFLLPYNSFITDVDYLHHKYPGTSIVFDMSLTYILVALAAVLLNNVLVERLTLHTRITAGYLLALGPLLFISICDVWLQLFSRDQAYAINLAAVGTVAFGCTVQQSSFYGYTGMLPKRYTQGVMTGDSTAGVMISLSRILTKLLLPDERASTLIFFLVSVALELLCFLLHLLVRRSRFVLFYTTRPRDSHRGRPGLGRGYGYRVHHDVVAGDVHFEHPAPALAPNESPKDSPAHEVTGSGGAYMRFDVPRPRVQRSWPTFRALLLHRYVVARVIWADMLSIAVTYFITLCLFPGLESEIRHCILGEWLPILIMAVFNLSDFVGKILAALPVDWRGTHLLACSCLRVVFIPLFILCVYPSGMPALRHPAWPCIFSLLMGISNGYFGSVPMILAAGKVSPKQRELAGNTMTVSYMSGLTLGSAVAYCTYSLTRDAHGSCLHASTANGSILAGL,"No change in dopamine, serotonin and MPP(+) uptake; no uridine uptake activity.",,MGSVGSQRLEEPSVAGTPDPGVVMSFTFDSHQLEEAAEAAQGQGLRARGVPAFTDTTLDEPVPDDRYHAIYFAMLLAGVGFLLPYNSFITDVDYLHHKYPGTSIVFDMSLTYILVALAAVLLNNVLVERLTLHTRITAGYLLALGPLLFISICDVWLQLFSRDQAYAINLAAVGTVAFGCTVQQSSFYGYTGMLPKRYTQGVMTGESTAGVMISLSRILTKLLLPDERASTLIFFLVSVALELLCFLLHLLVRRSRFVLFYTTRPRDSHRGRPGLGRGYGYRVHHDVVAGDVHFEHPAPALAPNESPKDSPAHEVTGSGGAYMRFDVPRPRVQRSWPTFRALLLHRYVVARVIWADMLSIAVTYFITLCLFPGLESEIRHCILGEWLPILIMAVFNLSDFVGKILAALPVDWRGTHLLACSCLRVVFIPLFILCVYPSGMPALRHPAWPCIFSLLMGISNGYFGSVPMILAAGKVSPKQRELAGNTMTVSYMSGLTLGSAVAYCTYSLTRDAHGSCLHASTANGSILAGL,Equilibrative nucleoside transporter 4,"Electrogenic voltage-dependent transporter that mediates the transport of a variety of endogenous bioactive amines, cationic xenobiotics and drugs. Utilizes the physiologic inside-negative membrane potential as a driving force to facilitate cellular uptake of organic cations. Functions as a Na(+)- and Cl(-)-independent bidirectional transporter. Substrate transport is pH-dependent and enhanced under acidic condition, which is most likely the result of allosteric changes in the transporter structure. Implicated in monoamine neurotransmitters uptake such as serotonin, dopamine, adrenaline/epinephrine, noradrenaline/norepinephrine, histamine and tyramine, thereby supporting a role in homeostatic regulation of aminergic neurotransmission in the central nervous system. Also responsible for the uptake of bioactive amines and drugs through the blood-cerebrospinal fluid (CSF) barrier, from the CSF into choroid plexus epithelial cells, thereby playing a significant role in the clearance of cationic neurotoxins, xenobiotics and metabolic waste in the brain. Involved in bidirectional transport of the purine nucleoside adenosine and plays a role in the regulation of extracellular adenosine concentrations in cardiac tissues, in particular during ischemia. May be involved in organic cation uptake from the tubular lumen into renal tubular cells, thereby contributing to organic cation reabsorption in the kidney. Also transports guanidine.","Eliminating the charge at E(206) () resulted in loss of organic cation transport activity, whereas conserving the negative charge () restored transporter function.","No change in dopamine, serotonin and MPP(+) uptake; no uridine uptake activity. Eliminating the charge at E(206) () resulted in loss of organic cation transport activity, whereas conserving the negative charge () restored transporter function."
1164,1164,1164,85158,H2AM12-C589S,MLLNIVLISNLACLAFALPLKEGTRGSRCFLNGELVKTVNTSKVVSECCVKDDISIIKSNAEHYKSGDRLAAVIKYYRLYQVKDWHSCNPIYDDHGSFMILDIDNTGTLIPKMHTCRVECEIALNKDTGEVILNSYRINHYRISGTMHVSGWFKNKIEIPLENTCESIEVTCGLKTLNFHACFHTHKSCTRYFKGSILPELMIESFCTNLELILLVTFILVGSVMMMILTKTYIVYVFIPIFYPFVKLYAYMYNKYFKLCKNCLLAVHPFTNCPSTCICGMIYTTTESLKLHRMCNNCSGYKALPKTRKLCKSKISNIVLCVITSLIFFSFITPISSQCIDIEKLPDEYITCKRELANIKSLTIDDTYSFIYSCTCIIVLILLKKAAKYILYCNCSFCGMVHERRGLKIMDNFTNKCLSCVCAENKGLTIHRASEKCLFKFESSYNRTGLIIFMLLLVPTIVMTQETSINCKNIQSTQLTIEHLSKCMAFYQNKTSSPVVINEIISDASVDEQELIKSLNLNCNVIDRFISESSVIETQVYYEYIKSQLCPLQVHDIFTINSASNIQWKALARSFTLGVCNTNPHKHISRCLESMQMCTSTKTDHAREMSIYYDGHPDRFEHDMKIILNIMRYIVPGLGRVLLDQIKQTKDYQALRHIQGKLSPKSQSNLQLKGFLEFVDFILGANVTIEKTPQTLTTLSLIKGAHRNLDQKDPGPTPILVCKSPQKVVCYSPRGVTHPGDYISCKSKMYKWPSLGVYKHNRDQQQACSSDTHCLEMFEPAERTITTKICKVSDMTYSESPYSTGIPSCNVKRFGSCNVRGHQWQIAECSNGLFYYVSAKAHSKTNDITLYCLSANCLDLRYAFRSSSCSDIVWDTSYRNKLTPKSINHPDIENYIAALQSDIANDLTMHYFKPLKNLPAIIPQYKTMTLNGDKVSNGIRNSYIESHIPAINGLSAGINIAMPNGESLFSIIIYVRRVINKASYRFLYETGPTIGINAKHEEVCTGKCPSPIPHQDGWVTFSKE,Loss of disulfide bond; when associated with S-580.,,MLLNIVLISNLACLAFALPLKEGTRGSRCFLNGELVKTVNTSKVVSECCVKDDISIIKSNAEHYKSGDRLAAVIKYYRLYQVKDWHSCNPIYDDHGSFMILDIDNTGTLIPKMHTCRVECEIALNKDTGEVILNSYRINHYRISGTMHVSGWFKNKIEIPLENTCESIEVTCGLKTLNFHACFHTHKSCTRYFKGSILPELMIESFCTNLELILLVTFILVGSVMMMILTKTYIVYVFIPIFYPFVKLYAYMYNKYFKLCKNCLLAVHPFTNCPSTCICGMIYTTTESLKLHRMCNNCSGYKALPKTRKLCKSKISNIVLCVITSLIFFSFITPISSQCIDIEKLPDEYITCKRELANIKSLTIDDTYSFIYSCTCIIVLILLKKAAKYILYCNCSFCGMVHERRGLKIMDNFTNKCLSCVCAENKGLTIHRASEKCLFKFESSYNRTGLIIFMLLLVPTIVMTQETSINCKNIQSTQLTIEHLSKCMAFYQNKTSSPVVINEIISDASVDEQELIKSLNLNCNVIDRFISESSVIETQVYYEYIKSQLCPLQVHDIFTINSASNIQWKALARSFTLGVCNTNPHKHICRCLESMQMCTSTKTDHAREMSIYYDGHPDRFEHDMKIILNIMRYIVPGLGRVLLDQIKQTKDYQALRHIQGKLSPKSQSNLQLKGFLEFVDFILGANVTIEKTPQTLTTLSLIKGAHRNLDQKDPGPTPILVCKSPQKVVCYSPRGVTHPGDYISCKSKMYKWPSLGVYKHNRDQQQACSSDTHCLEMFEPAERTITTKICKVSDMTYSESPYSTGIPSCNVKRFGSCNVRGHQWQIAECSNGLFYYVSAKAHSKTNDITLYCLSANCLDLRYAFRSSSCSDIVWDTSYRNKLTPKSINHPDIENYIAALQSDIANDLTMHYFKPLKNLPAIIPQYKTMTLNGDKVSNGIRNSYIESHIPAINGLSAGINIAMPNGESLFSIIIYVRRVINKASYRFLYETGPTIGINAKHEEVCTGKCPSPIPHQDGWVTFSKE,Envelopment polyprotein,Glycoprotein C and glycoprotein N interact with each other and are present at the surface of the virion. Glycoprotein N probably locks the Gn-Gc complex in a prefusion state. Glycoprotein N and glycoprotein C are able to attach the virion to host cell receptors. This attachment induces virion internalization predominantly through clathrin-dependent endocytosis.Glycoprotein C and glycoprotein N interact with each other and are present at the surface of the virion. The spikes at the surface of the virion are formed by an N-terminal extension of glycoprotein C. Glycoprotein N and glycoprotein C are able to attach the virion to host cell receptors. This attachment induces virion internalization predominantly through clathrin-dependent endocytosis. Class II fusion protein that promotes fusion of viral membrane with host endosomal membrane after endocytosis of the virion. Exposure to potassium is necessary for the conformational change leading to fusion.,The mutation in the SBV Gc protein affects the interaction with a subset of Gc-specific monoclonal antibodies.,Loss of disulfide bond; when associated with S-580. The mutation in the SBV Gc protein affects the interaction with a subset of Gc-specific monoclonal antibodies.
1177,1177,1177,86550,Q16630-G86V,MADGVDHIDIYADVGEEFNQEAEYGGHDQIDLYDDVISPSANNGDAPEDRDYMDTLPPTVGDDVGKGAAPNVVYTYTGKRIALYIVNLTWWTTDEDLTEAVHSLGVNDILEIKFFENRANGQSKGFALVGVGSEASSKKLMDLLPKRELHGQNPVVTPCNKQFLSQFEMQSRKTTQSGQMSGEGKAGPPGGSSRAAFPQGGRGRGRFPGAVPGGDRFPGPAGPGGPPPPFPAGQTPPRPPLGPPGPPGPPGPPPPGQVLPPPLAGPPNRGDRPPPPVLFPGQPFGQPPLGPLPPGPPPPVPGYGPPPGPPPPQQGPPPPPGPFPPRPPGPLGPPLTLAPPPHLPGPPPGAPPPAPHVNPAFFPPPTNSGMPTSDSRGPPPTDPYGRPPPYDRGDYGPPGREMDTARTPLSEAEFEEIMNRNRAISSSAISRAVSDASAGDYGSAIETLVTAISLIKQSKVSADDRCKVLISSLQDCLHGIESKSYGSGSRRERSRERDHSRSREKSRRHKSRSRDRHDDYYRERSRERERHRDRDRDRDRERDREREYRHR,Abolishes interaction with NUDT21/CPSF5; when associated with V-87.,,MADGVDHIDIYADVGEEFNQEAEYGGHDQIDLYDDVISPSANNGDAPEDRDYMDTLPPTVGDDVGKGAAPNVVYTYTGKRIALYIGNLTWWTTDEDLTEAVHSLGVNDILEIKFFENRANGQSKGFALVGVGSEASSKKLMDLLPKRELHGQNPVVTPCNKQFLSQFEMQSRKTTQSGQMSGEGKAGPPGGSSRAAFPQGGRGRGRFPGAVPGGDRFPGPAGPGGPPPPFPAGQTPPRPPLGPPGPPGPPGPPPPGQVLPPPLAGPPNRGDRPPPPVLFPGQPFGQPPLGPLPPGPPPPVPGYGPPPGPPPPQQGPPPPPGPFPPRPPGPLGPPLTLAPPPHLPGPPPGAPPPAPHVNPAFFPPPTNSGMPTSDSRGPPPTDPYGRPPPYDRGDYGPPGREMDTARTPLSEAEFEEIMNRNRAISSSAISRAVSDASAGDYGSAIETLVTAISLIKQSKVSADDRCKVLISSLQDCLHGIESKSYGSGSRRERSRERDHSRSREKSRRHKSRSRDRHDDYYRERSRERERHRDRDRDRDRERDREREYRHR,Cleavage and polyadenylation specificity factor subunit 6,"Component of the cleavage factor Im (CFIm) complex that functions as an activator of the pre-mRNA 3'-end cleavage and polyadenylation processing required for the maturation of pre-mRNA into functional mRNAs. CFIm contributes to the recruitment of multiprotein complexes on specific sequences on the pre-mRNA 3'-end, so called cleavage and polyadenylation signals (pA signals). Most pre-mRNAs contain multiple pA signals, resulting in alternative cleavage and polyadenylation (APA) producing mRNAs with variable 3'-end formation. The CFIm complex acts as a key regulator of cleavage and polyadenylation site choice during APA through its binding to 5'-UGUA-3' elements localized in the 3'-untranslated region (UTR) for a huge number of pre-mRNAs. CPSF6 enhances NUDT21/CPSF5 binding to 5'-UGUA-3' elements localized upstream of pA signals and promotes RNA looping, and hence activates directly the mRNA 3'-processing machinery. Plays a role in mRNA export.(Microbial infection) Binds HIV-1 capsid-nucleocapsid (HIV-1 CA-NC) complexes and might thereby promote the integration of the virus in the nucleus of dividing cells (in vitro).",The mutation in CF I(m)68 has been identified to cause a change in the protein's structure and function. potentially affecting the protein's RNA binding capabilities and its ability to interact with other splicing factors. It may also impact the subcellular localization of CF I(m)68 and its involvement in transcriptional control and RNA processing.,Abolishes interaction with NUDT21/CPSF5; when associated with V-87. The mutation in CF I(m)68 has been identified to cause a change in the protein's structure and function. potentially affecting the protein's RNA binding capabilities and its ability to interact with other splicing factors. It may also impact the subcellular localization of CF I(m)68 and its involvement in transcriptional control and RNA processing.
1206,1206,1206,89390,O44342-R41S,MMHILVTLLLVAIHSIPTTWAVTCTGCVDLDELSFEKTVESFPYSVVKFDIAYPYGEKHEAFTAFSKSAHKATKDLLIATVGVKDYGELENKALGDRYKVDDKNFPSIFLFKGNADEYVQLPSHVDVTLDNLKAFVSANTPLYIGRDGCIKEFNEVLKNYANIPDAEQLKLIEKLQAKQEQLTDPEQQQNARAYLIYMRKIHEVGYDFLEEETKRLLRLKAGKVTEAKKEELLRKLNILEVFRVHKVTKTAPEKEEL,Does not affect homodimerization. Abolishes homodimerization and subcellular targeting of pip; when associated with N-31.,,MMHILVTLLLVAIHSIPTTWAVTCTGCVDLDELSFEKTVERFPYSVVKFDIAYPYGEKHEAFTAFSKSAHKATKDLLIATVGVKDYGELENKALGDRYKVDDKNFPSIFLFKGNADEYVQLPSHVDVTLDNLKAFVSANTPLYIGRDGCIKEFNEVLKNYANIPDAEQLKLIEKLQAKQEQLTDPEQQQNARAYLIYMRKIHEVGYDFLEEETKRLLRLKAGKVTEAKKEELLRKLNILEVFRVHKVTKTAPEKEEL,Protein windbeutel,Probable chaperone protein involved in dorsoventral axis patterning in early embryos. Probably acts by folding and targeting pipe (pip) into the Golgi.,"The mutation is mentioned in the document. However, there is no specific functional information provided for this mutation.","Does not affect homodimerization. Abolishes homodimerization and subcellular targeting of pip; when associated with N-31. The mutation is mentioned in the document. However, there is no specific functional information provided for this mutation."
1220,1220,1220,90331,P00451-D561H,MQIELSTCFFLCLLRFCFSATRRYYLGAVELSWDYMQSDLGELPVDARFPPRVPKSFPFNTSVVYKKTLFVEFTDHLFNIAKPRPPWMGLLGPTIQAEVYDTVVITLKNMASHPVSLHAVGVSYWKASEGAEYDDQTSQREKEDDKVFPGGSHTYVWQVLKENGPMASDPLCLTYSYLSHVDLVKDLNSGLIGALLVCREGSLAKEKTQTLHKFILLFAVFDEGKSWHSETKNSLMQDRDAASARAWPKMHTVNGYVNRSLPGLIGCHRKSVYWHVIGMGTTPEVHSIFLEGHTFLVRNHRQASLEISPITFLTAQTLLMDLGQFLLFCHISSHQHDGMEAYVKVDSCPEEPQLRMKNNEEAEDYDDDLTDSEMDVVRFDDDNSPSFIQIRSVAKKHPKTWVHYIAAEEEDWDYAPLVLAPDDRSYKSQYLNNGPQRIGRKYKKVRFMAYTDETFKTREAIQHESGILGPLLYGEVGDTLLIIFKNQASRPYNIYPHGITDVRPLYSRRLPKGVKHLKDFPILPGEIFKYKWTVTVEDGPTKSDPRCLTRYYSSFVNMERHLASGLIGPLLICYKESVDQRGNQIMSDKRNVILFSVFDENRSWYLTENIQRFLPNPAGVQLEDPEFQASNIMHSINGYVFDSLQLSVCLHEVAYWYILSIGAQTDFLSVFFSGYTFKHKMVYEDTLTLFPFSGETVFMSMENPGLWILGCHNSDFRNRGMTALLKVSSCDKNTGDYYEDSYEDISAYLLSKNNAIEPRSFSQNSRHPSTRQKQFNATTIPENDIEKTDPWFAHRTPMPKIQNVSSSDLLMLLRQSPTPHGLSLSDLQEAKYETFSDDPSPGAIDSNNSLSEMTHFRPQLHHSGDMVFTPESGLQLRLNEKLGTTAATELKKLDFKVSSTSNNLISTIPSDNLAAGTDNTSSLGPPSMPVHYDSQLDTTLFGKKSSPLTESGGPLSLSEENNDSKLLESGLMNSQESSWGKNVSSTESGRLFKGKRAHGPALLTKDNALFKVSISLLKTNKTSN,In HEMA.,,MQIELSTCFFLCLLRFCFSATRRYYLGAVELSWDYMQSDLGELPVDARFPPRVPKSFPFNTSVVYKKTLFVEFTDHLFNIAKPRPPWMGLLGPTIQAEVYDTVVITLKNMASHPVSLHAVGVSYWKASEGAEYDDQTSQREKEDDKVFPGGSHTYVWQVLKENGPMASDPLCLTYSYLSHVDLVKDLNSGLIGALLVCREGSLAKEKTQTLHKFILLFAVFDEGKSWHSETKNSLMQDRDAASARAWPKMHTVNGYVNRSLPGLIGCHRKSVYWHVIGMGTTPEVHSIFLEGHTFLVRNHRQASLEISPITFLTAQTLLMDLGQFLLFCHISSHQHDGMEAYVKVDSCPEEPQLRMKNNEEAEDYDDDLTDSEMDVVRFDDDNSPSFIQIRSVAKKHPKTWVHYIAAEEEDWDYAPLVLAPDDRSYKSQYLNNGPQRIGRKYKKVRFMAYTDETFKTREAIQHESGILGPLLYGEVGDTLLIIFKNQASRPYNIYPHGITDVRPLYSRRLPKGVKHLKDFPILPGEIFKYKWTVTVEDGPTKSDPRCLTRYYSSFVNMERDLASGLIGPLLICYKESVDQRGNQIMSDKRNVILFSVFDENRSWYLTENIQRFLPNPAGVQLEDPEFQASNIMHSINGYVFDSLQLSVCLHEVAYWYILSIGAQTDFLSVFFSGYTFKHKMVYEDTLTLFPFSGETVFMSMENPGLWILGCHNSDFRNRGMTALLKVSSCDKNTGDYYEDSYEDISAYLLSKNNAIEPRSFSQNSRHPSTRQKQFNATTIPENDIEKTDPWFAHRTPMPKIQNVSSSDLLMLLRQSPTPHGLSLSDLQEAKYETFSDDPSPGAIDSNNSLSEMTHFRPQLHHSGDMVFTPESGLQLRLNEKLGTTAATELKKLDFKVSSTSNNLISTIPSDNLAAGTDNTSSLGPPSMPVHYDSQLDTTLFGKKSSPLTESGGPLSLSEENNDSKLLESGLMNSQESSWGKNVSSTESGRLFKGKRAHGPALLTKDNALFKVSISLLKTNKTSN,Coagulation factor VIII,"Factor VIII, along with calcium and phospholipid, acts as a cofactor for F9/factor IXa when it converts F10/factor X to the activated form, factor Xa.",resulting in a change from aspartic acid (D) to histidine (H).,In HEMA. resulting in a change from aspartic acid (D) to histidine (H).
1221,1221,1221,90388,P22610-C97G,MPLLDYLASHPLAFVLCTILLGLLVGSFLNVVVHRLPKMMERNWKAEAREALGLEPEPKQATYNLVLPNSACPRCGHEIRPWENIPLVSYLALGGKGSSCKAAIGKRYPLVELATALLSGYVAWHFGFTWQAGAMLLLTWGLLAMSLIDADHQLLPDVLVLPLLWLGLIANHFGLFASLDDALFGAVFGYLSLWSVFWLFKLVTGKEGMGYGDFKLLAMLGAWGGWQILPLTILLSSLVGAILGVIMLRLRNAESGTPIPFGPYLAIAGWIALLWGDQITRTYLQFAGFK,Complete loss of peptidase and methylase activity.,,MPLLDYLASHPLAFVLCTILLGLLVGSFLNVVVHRLPKMMERNWKAEAREALGLEPEPKQATYNLVLPNSACPRCGHEIRPWENIPLVSYLALGGKCSSCKAAIGKRYPLVELATALLSGYVAWHFGFTWQAGAMLLLTWGLLAMSLIDADHQLLPDVLVLPLLWLGLIANHFGLFASLDDALFGAVFGYLSLWSVFWLFKLVTGKEGMGYGDFKLLAMLGAWGGWQILPLTILLSSLVGAILGVIMLRLRNAESGTPIPFGPYLAIAGWIALLWGDQITRTYLQFAGFK,Prepilin leader peptidase/N-methyltransferase,"Plays an essential role in type IV pili and type II pseudopili formation by proteolytically removing the leader sequence from substrate proteins and subsequently monomethylating the alpha-amino group of the newly exposed N-terminal phenylalanine. Substrates include proteins required for pilus biogenesis PilE, PilV, PilW, and PilX as well as some components of the type II general secretory apparatus GspG, GspH, GspI and GspJ.","Mutagenesis in PilD resulted in a specific amino acid substitution,","Complete loss of peptidase and methylase activity. Mutagenesis in PilD resulted in a specific amino acid substitution,"
1224,1224,1224,90426,P0CG51-Q49E,MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKELEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGY,Rate of phosphorylation by an insect Pink1 is slightly decreased.,,MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGY,Polyubiquitin-B [Cleaved into: Ubiquitin],"[Ubiquitin]: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in proteotoxic stress response and cell cycle; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.",,Rate of phosphorylation by an insect Pink1 is slightly decreased.
1235,1235,1235,91429,Q96FW1-Q39L,MAAEEPQQQKQEPLGSDSEGVNCLAYDEAIMAQQDRIQLEIAVQNPLVSERLELSVLYKEYAEDDNIYQQKIKDLHKKYSYIRKTRPDGNCFYRAFGFSHLEALLDDSKELQRFKAVSAKSKEDLVSQGFTEFTIEDFHNTFMDLIEQVEKQTSVADLLASFNDQSTSDYLVVYLRLLTSGYLQRESKFFEHFIEGGRTVKEFCQQEVEPMCKESDHIHIIALAQALSVSIQVEYMDRGEGGTTNPHIFPEGSEPKVYLLYRPGHYDILYK,Does not affect activity in DNA repair and ability to inhibit UBE2N/UBC13.,,MAAEEPQQQKQEPLGSDSEGVNCLAYDEAIMAQQDRIQQEIAVQNPLVSERLELSVLYKEYAEDDNIYQQKIKDLHKKYSYIRKTRPDGNCFYRAFGFSHLEALLDDSKELQRFKAVSAKSKEDLVSQGFTEFTIEDFHNTFMDLIEQVEKQTSVADLLASFNDQSTSDYLVVYLRLLTSGYLQRESKFFEHFIEGGRTVKEFCQQEVEPMCKESDHIHIIALAQALSVSIQVEYMDRGEGGTTNPHIFPEGSEPKVYLLYRPGHYDILYK,Ubiquitin thioesterase OTUB1,"Hydrolase that can specifically remove 'Lys-48'-linked conjugated ubiquitin from proteins and plays an important regulatory role at the level of protein turnover by preventing degradation. Regulator of T-cell anergy, a phenomenon that occurs when T-cells are rendered unresponsive to antigen rechallenge and no longer respond to their cognate antigen. Acts via its interaction with RNF128/GRAIL, a crucial inductor of CD4 T-cell anergy. Isoform 1 destabilizes RNF128, leading to prevent anergy. In contrast, isoform 2 stabilizes RNF128 and promotes anergy. Surprisingly, it regulates RNF128-mediated ubiquitination, but does not deubiquitinate polyubiquitinated RNF128. Deubiquitinates estrogen receptor alpha (ESR1). Mediates deubiquitination of 'Lys-48'-linked polyubiquitin chains, but not 'Lys-63'-linked polyubiquitin chains. Not able to cleave di-ubiquitin. Also capable of removing NEDD8 from NEDD8 conjugates, but with a much lower preference compared to 'Lys-48'-linked ubiquitin.Plays a key non-catalytic role in DNA repair regulation by inhibiting activity of RNF168, an E3 ubiquitin-protein ligase that promotes accumulation of 'Lys-63'-linked histone H2A and H2AX at DNA damage sites. Inhibits RNF168 independently of ubiquitin thioesterase activity by binding and inhibiting UBE2N/UBC13, the E2 partner of RNF168, thereby limiting spreading of 'Lys-63'-linked histone H2A and H2AX marks. Inhibition occurs by binding to free ubiquitin: free ubiquitin acts as an allosteric regulator that increases affinity for UBE2N/UBC13 and disrupts interaction with UBE2V1. The OTUB1-UBE2N/UBC13-free ubiquitin complex adopts a configuration that mimics a cleaved 'Lys48'-linked di-ubiquitin chain.",,Does not affect activity in DNA repair and ability to inhibit UBE2N/UBC13.
1236,1236,1236,91525,U2UMQ6-K780A,MTQFEGFTNLYQVSKTLRFELIPQGKTLKHIQEQGFIEEDKARNDHYKELKPIIDRIYKTYADQCLQLVQLDWENLSAAIDSYRKEKTEETRNALIEEQATYRNAIHDYFIGRTDNLTDAINKRHAEIYKGLFKAELFNGKVLKQLGTVTTTEHENALLRSFDKFTTYFSGFYENRKNVFSAEDISTAIPHRIVQDNFPKFKENCHIFTRLITAVPSLREHFENVKKAIGIFVSTSIEEVFSFPFYNQLLTQTQIDLYNQLLGGISREAGTEKIKGLNEVLNLAIQKNDETAHIIASLPHRFIPLFKQILSDRNTLSFILEEFKSDEEVIQSFCKYKTLLRNENVLETAEALFNELNSIDLTHIFISHKKLETISSALCDHWDTLRNALYERRISELTGKITKSAKEKVQRSLKHEDINLQEIISAAGKELSEAFKQKTSEILSHAHAALDQPLPTTLKKQEEKEILKSQLDSLLGLYHLLDWFAVDESNEVDPEFSARLTGIKLEMEPSLSFYNKARNYATKKPYSVEKFKLNFQMPTLASGWDVNKEKNNGAILFVKNGLYYLGIMPKQKGRYKALSFEPTEKTSEGFDKMYYDYFPDAAKMIPKCSTQLKAVTAHFQTHTTPILLSNNFIEPLEITKEIYDLNNPEKEPKKFQTAYAKKTGDQKGYREALCKWIDFTRDFLSKYTKTTSIDLSSLRPSSQYKDLGEYYAELNPLLYHISFQRIAEKEIMDAVETGKLYLFQIYNKDFAKGHHGKPNLHTLYWTGLFSPENLAKTSIALNGQAELFYRPKSRMKRMAHRLGEKMLNKKLKDQKTPIPDTLYQELYDYVNHRLSHDLSDEARALLPNVITKEVSHEIIKDRRFTSDKFFFHVPITLNYQAANSPSKFNQRVNAYLKEHPETPIIGIDRGERNLIYITVIDSTGKILEQRSLNTIQQFDYQKKLDNREKERVAARQAWSVVGTIKDLKQGYLSQVIHEIVDLMIHYQAVVVLENLNFGFKSKRTGIAEKAVYQQFEKMLIDKLN,Nearly complete loss of guided indel formation.,,MTQFEGFTNLYQVSKTLRFELIPQGKTLKHIQEQGFIEEDKARNDHYKELKPIIDRIYKTYADQCLQLVQLDWENLSAAIDSYRKEKTEETRNALIEEQATYRNAIHDYFIGRTDNLTDAINKRHAEIYKGLFKAELFNGKVLKQLGTVTTTEHENALLRSFDKFTTYFSGFYENRKNVFSAEDISTAIPHRIVQDNFPKFKENCHIFTRLITAVPSLREHFENVKKAIGIFVSTSIEEVFSFPFYNQLLTQTQIDLYNQLLGGISREAGTEKIKGLNEVLNLAIQKNDETAHIIASLPHRFIPLFKQILSDRNTLSFILEEFKSDEEVIQSFCKYKTLLRNENVLETAEALFNELNSIDLTHIFISHKKLETISSALCDHWDTLRNALYERRISELTGKITKSAKEKVQRSLKHEDINLQEIISAAGKELSEAFKQKTSEILSHAHAALDQPLPTTLKKQEEKEILKSQLDSLLGLYHLLDWFAVDESNEVDPEFSARLTGIKLEMEPSLSFYNKARNYATKKPYSVEKFKLNFQMPTLASGWDVNKEKNNGAILFVKNGLYYLGIMPKQKGRYKALSFEPTEKTSEGFDKMYYDYFPDAAKMIPKCSTQLKAVTAHFQTHTTPILLSNNFIEPLEITKEIYDLNNPEKEPKKFQTAYAKKTGDQKGYREALCKWIDFTRDFLSKYTKTTSIDLSSLRPSSQYKDLGEYYAELNPLLYHISFQRIAEKEIMDAVETGKLYLFQIYNKDFAKGHHGKPNLHTLYWTGLFSPENLAKTSIKLNGQAELFYRPKSRMKRMAHRLGEKMLNKKLKDQKTPIPDTLYQELYDYVNHRLSHDLSDEARALLPNVITKEVSHEIIKDRRFTSDKFFFHVPITLNYQAANSPSKFNQRVNAYLKEHPETPIIGIDRGERNLIYITVIDSTGKILEQRSLNTIQQFDYQKKLDNREKERVAARQAWSVVGTIKDLKQGYLSQVIHEIVDLMIHYQAVVVLENLNFGFKSKRTGIAEKAVYQQFEKMLIDKLN,CRISPR-associated endonuclease Cas12a,"CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Recognizes a short motif in the CRISPR repeat sequences (the 5' PAM or protospacer adjacent motif, TTTN in this organism) to help distinguish self versus nonself, as targets within the bacterial CRISPR locus do not have PAMs. Has dsDNA endonuclease activity, results in staggered 4-base 5' overhangs 19 and 22 bases downstream of the PAM on the non-targeted and targeted strand respectively. Non-target strand cleavage by the RuvC domain is probably a prerequisite of target strand cleavage by the Nuc domain. In this CRISPR system correct processing of pre-crRNA requires only this protein and the CRISPR locus.",,Nearly complete loss of guided indel formation.
1256,1256,1256,92747,Q99ML2-K148A,MLPEASSLWLLRLLRDVQLAQFYRPILEELNVTRPEHFDFVRPEDLDNIGMGRPAQRRLNEALKRYRSGVKSKNWVYKILGGFAPEQKEIPPRSDSPLCFHEPEGGLKCLIPEGAVRRGELLGSGCFGVVHRGLWTLPSGQSIPVAVASLRVGPEGPMGTELGDFLREVSVMMKLEHPHVLRLHGLVLGQPLQMVMELAPLGSLHARLTAPAPTPPLPVALLCLFLRQLAGAMAYLGSCGLVHRDLATRNLLLASPRMIKVADFGLVRPLGGARGRYVMGGPRPIPYAWCAPESLRQGAFSSASDVWMFGVTLWEMFSGGEEPWAGVPPYLILQRLEKDRARLPKPPLCSRALYSLALRCWAPHPADRPSFSNLEGLLQEAWLSEGRCVREVTEPGALRMEPGDPITIIEGSLDTATWKGQNGRTLKVGNFPASAVTLADLGGSPVTHPAHRGSPAHGEKCRGGTDGDREKATLQDLPPARSHRTKMPLQRMRGISKSLESVLSLGPRPTGGGSSPPELRRTRAMPQRLPDLPPRPPDLPPRPPIICNSSQPTQPHKARPKRESSHNHRTGAPGASKATVPSGGPLSDPEWQRKVVEVELSVHGVTYQECQVALRTTGGDVASAIRNLKVDQLFHLSNRSRADCRRILEHHQWDLSAASRYILARS,Loss of autophosphorylation.,,MLPEASSLWLLRLLRDVQLAQFYRPILEELNVTRPEHFDFVRPEDLDNIGMGRPAQRRLNEALKRYRSGVKSKNWVYKILGGFAPEQKEIPPRSDSPLCFHEPEGGLKCLIPEGAVRRGELLGSGCFGVVHRGLWTLPSGQSIPVAVKSLRVGPEGPMGTELGDFLREVSVMMKLEHPHVLRLHGLVLGQPLQMVMELAPLGSLHARLTAPAPTPPLPVALLCLFLRQLAGAMAYLGSCGLVHRDLATRNLLLASPRMIKVADFGLVRPLGGARGRYVMGGPRPIPYAWCAPESLRQGAFSSASDVWMFGVTLWEMFSGGEEPWAGVPPYLILQRLEKDRARLPKPPLCSRALYSLALRCWAPHPADRPSFSNLEGLLQEAWLSEGRCVREVTEPGALRMEPGDPITIIEGSLDTATWKGQNGRTLKVGNFPASAVTLADLGGSPVTHPAHRGSPAHGEKCRGGTDGDREKATLQDLPPARSHRTKMPLQRMRGISKSLESVLSLGPRPTGGGSSPPELRRTRAMPQRLPDLPPRPPDLPPRPPIICNSSQPTQPHKARPKRESSHNHRTGAPGASKATVPSGGPLSDPEWQRKVVEVELSVHGVTYQECQVALRTTGGDVASAIRNLKVDQLFHLSNRSRADCRRILEHHQWDLSAASRYILARS,Non-receptor tyrosine-protein kinase TNK1,May function in signaling pathways utilized broadly during fetal development and more selectively in adult tissues and in cells of the lymphohematopoietic system. Could specifically be involved in phospholipid signal transduction. Involved in negative regulation of cell growth. Has tumor suppressor properties. Plays a negative regulatory role in the Ras-MAPK pathway.,"Stable overexpression of Kos1 inhibits growth of NIH 3T3 cells, while the kinase-dead Kos1(CN) promotes cell growth in both liquid culture and soft agar. In addition, forced expression of Kos1 inhibits Ras activity in an indirect mechanism that results in the downregulation of the Ras-Raf1-MAPK growth pathway. Furthermore, overexpression of Kos1 in NCI-H82 lung cancer cells that express oncogenic Ha-Ras() inhibits cell growth under reduced serum (0. 5%) conditions in close association with the upregulation of the Ras inhibitor, Rap1A.","Loss of autophosphorylation. Stable overexpression of Kos1 inhibits growth of NIH 3T3 cells, while the kinase-dead Kos1(CN) promotes cell growth in both liquid culture and soft agar. In addition, forced expression of Kos1 inhibits Ras activity in an indirect mechanism that results in the downregulation of the Ras-Raf1-MAPK growth pathway. Furthermore, overexpression of Kos1 in NCI-H82 lung cancer cells that express oncogenic Ha-Ras() inhibits cell growth under reduced serum (0. 5%) conditions in close association with the upregulation of the Ras inhibitor, Rap1A."
1274,1274,1274,94392,Q9Y679-E388A,MELPSGPGPERLFDSHRLPGDCFLLLVLLLYAPVGFCLLVLRLFLGIHVFLVSCALPDSVLRRFVVRTMCAVLGLVARQEDSGLRDHSVRVLISNHVTPFDHNIVNLLTTCSTPLLNSPPSFVCWSRGFMEMNGRGELVESLKRFCASTRLPPTPLLLFPEEEATNGREGLLRFSSWPFSIQDVVQPLTLQVQRPLVSVTVSDASWVSELLWSLFVPFTVYQVRWLRPVHRQLGEANEEFALRVQQLVAKELGQTGTRLTPADKAEHMKRQRHPRLRPQSAQSSFPPSPGPSPDVQLATLAQRVKEVLPHVPLGVIQRDLAKTGCVDLTITNLLEGAVAFMPEDITKGTQSLPTASASKFPSSGPVTPQPTALTFAKSSWARQESLQARKQALYEYARRRFTERRAQEAD,No effect on interaction with UBE2G2.,,MELPSGPGPERLFDSHRLPGDCFLLLVLLLYAPVGFCLLVLRLFLGIHVFLVSCALPDSVLRRFVVRTMCAVLGLVARQEDSGLRDHSVRVLISNHVTPFDHNIVNLLTTCSTPLLNSPPSFVCWSRGFMEMNGRGELVESLKRFCASTRLPPTPLLLFPEEEATNGREGLLRFSSWPFSIQDVVQPLTLQVQRPLVSVTVSDASWVSELLWSLFVPFTVYQVRWLRPVHRQLGEANEEFALRVQQLVAKELGQTGTRLTPADKAEHMKRQRHPRLRPQSAQSSFPPSPGPSPDVQLATLAQRVKEVLPHVPLGVIQRDLAKTGCVDLTITNLLEGAVAFMPEDITKGTQSLPTASASKFPSSGPVTPQPTALTFAKSSWARQESLQERKQALYEYARRRFTERRAQEAD,Lipid droplet-regulating VLDL assembly factor AUP1,"Plays a role in the translocation of terminally misfolded proteins from the endoplasmic reticulum lumen to the cytoplasm and their degradation by the proteasome. Plays a role in lipid droplet formation. Induces lipid droplet clustering. Recruits ubiquitin-conjugating enzyme UBE2G2 to lipid droplets which facilitates its interaction with ubiquitin ligases AMFR/gp78 and RNF139/TRC8, leading to sterol-induced ubiquitination of HMGCR and its subsequent proteasomal degradation. Also required for the degradation of INSIG1, SREBF1 and SREBF2. Plays a role in regulating assembly and secretion of very low density lipoprotein particles and stability of apolipoprotein APOB.(Microbial infection) Following Dengue virus infection, required for induction of lipophagy which facilitates production of virus progeny particles.",,No effect on interaction with UBE2G2.
1287,1287,1287,95533,Q03103-C105A,MRLRTAIATLCLTAFTSATSNNSYIATDQTQNAFNDTHFCKVDRNDHVSPSCNVTFNELNAINENIRDDLSALLKSDFFKYFRLDLYKQCSFWDANDGLCLNRAASVDVVEDWDTLPEYWQPEILGSFNNDTMKEADDSDDECKFLDQLCQTSKKPVDIEDTINYCDVNDFNGKNAVLIDLTANPERFTGYGGKQAGQIWSTIYQDNCFTIGETGESLAKDAFYRLVSGFHASIGTHLSKEYLNTKTGKWEPNLDLFMARIGNFPDRVTNMYFNYAVVAKALWKIQPYLPEFSFCDLVNKEIKNKMDNVISQLDTKIFNEDLVFANDLSLTLKDEFRSRFKNVTKIMDCVQCDRCRLWGKIQTTGYATALKILFEINDADEFTKQHIVGKLTKYELIALLQTFGRLSESIESVNMFEKMYGKRLNGSENRLSSFFQNNFFNILKEAGKSIRYTIENINSTKEGKKKTNNSQSHVFDDLKMPKAEIVPRPSNGTVNKWKKAWNTEVNNVLEAFRFIYRSYLDLPRNIWELSLMKVYKFWNKFIGVADYVSEETREPISYKLDIQ,Loss of activity.,,MRLRTAIATLCLTAFTSATSNNSYIATDQTQNAFNDTHFCKVDRNDHVSPSCNVTFNELNAINENIRDDLSALLKSDFFKYFRLDLYKQCSFWDANDGLCLNRACSVDVVEDWDTLPEYWQPEILGSFNNDTMKEADDSDDECKFLDQLCQTSKKPVDIEDTINYCDVNDFNGKNAVLIDLTANPERFTGYGGKQAGQIWSTIYQDNCFTIGETGESLAKDAFYRLVSGFHASIGTHLSKEYLNTKTGKWEPNLDLFMARIGNFPDRVTNMYFNYAVVAKALWKIQPYLPEFSFCDLVNKEIKNKMDNVISQLDTKIFNEDLVFANDLSLTLKDEFRSRFKNVTKIMDCVQCDRCRLWGKIQTTGYATALKILFEINDADEFTKQHIVGKLTKYELIALLQTFGRLSESIESVNMFEKMYGKRLNGSENRLSSFFQNNFFNILKEAGKSIRYTIENINSTKEGKKKTNNSQSHVFDDLKMPKAEIVPRPSNGTVNKWKKAWNTEVNNVLEAFRFIYRSYLDLPRNIWELSLMKVYKFWNKFIGVADYVSEETREPISYKLDIQ,Endoplasmic oxidoreductin-1,"Essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. Acts by oxidizing directly PDI1 isomerase through a direct disulfide exchange. Does not act as a direct oxidant of folding substrate, but relies on PDI1 to transfer oxidizing equivalent. Also able to oxidize directly the PDI related protein MPD2. Does not oxidize all PDI related proteins, suggesting that it can discriminate between PDI1 and related proteins. Reoxidation of ERO1 probably involves electron transfer to molecular oxygen via FAD. Acts independently of glutathione. May be responsible for a significant proportion of reactive oxygen species (ROS) in the cell, thereby being a source of oxidative stress.","Attenuation of Ero1p activity through noncatalytic cysteine pairs prevents hyperoxidation of the ER, leading to increased enzyme activity, decreased lag phase in kinetic assays, and growth defects in vivo.","Loss of activity. Attenuation of Ero1p activity through noncatalytic cysteine pairs prevents hyperoxidation of the ER, leading to increased enzyme activity, decreased lag phase in kinetic assays, and growth defects in vivo."
1296,1296,1296,96280,Q9UQ52-S585C,MRLLWKLVILLPLINSSAGDGLLSRPIFTQEPHDVIFPLDLSKSEVILNCAANGYPSPHYRWKQNGTDIDFTMSYHYRLDGGSLAINSPHTDQDIGMYQCLATNLLGTILSRKAKLQFAYIEDFETKTRSTVSVREGQGVVLLCGPPPHFGDLSYAWTFNDNPLYVQEDNRRFVSQETGNLYIAKVEPSDVGNYTCFITNKEAQRSVQGPPTPLVQRTDGVMGEYEPKIEVRFPETIQAAKDSSVKLECFALGNPVPDISWRRLDGSPLPGKVKYSKSQAILEIPNFQQEDEGFYECIASNLRGRNLAKGQLIFYAPPEWEQKIQNTHLSIYDNLLWECKASGKPNPWYTWLKNGERLNPEERIQIENGTLIITMLNVSDSGVYQCAAENKYQIIYANAELRVLASAPDFSKSPVKKKSFVQVGGDIVIGCKPNAFPRAAISWKRGTETLRQSKRIFLLEDGSLKIYNITRSDAGSYTCIATNQFGTAKNTGSLIVKERTVITVPPSKMDVTVGESIVLPCQVSHDPSIEVVFVWFFNGDVIDLKKGVAHFERIGGESVGDLMIRNIQLHHSGKYLCTVQTTLECLSAVADIIVRGPPGPPEDVQVEDISSTTSQLSWRAGPDNNSPIQIFTIQTRTPFSVGWQAVATVPEILNGKTYNATVVGLSPWVEYEFRVVAGNSIGIGEPSEPSELLRTKASVPVVAPVNIHGGGGSRSELVITWESIPEELQNGEGFGYIIMFRPVGSTTWSKEKVSSVESSRFVYRNESIIPLSPFEVKVGVYNNEGEGSLSTVTIVYSGEDEPQLAPRGTSLQSFSASEMEVSWNAIAWNRNTGRVLGYEVLYWTDDSKESMIGKIRVSGNVTTKNITGLKANTIYFASVRAYNTAGTGPSSPPVNVTTKKSPPSQPPANIAWKLTNSKLCLNWEHVKTMENESEVLGYKILYRQNRQSKTHILETNNTSAELLVPFEEDYLIEIRTVSDGGDGSSSEEIRIPKMSSLSSRGIQFLEPSTHFLSIVIVIFHCFAI,In a breast cancer sample; somatic mutation.,,MRLLWKLVILLPLINSSAGDGLLSRPIFTQEPHDVIFPLDLSKSEVILNCAANGYPSPHYRWKQNGTDIDFTMSYHYRLDGGSLAINSPHTDQDIGMYQCLATNLLGTILSRKAKLQFAYIEDFETKTRSTVSVREGQGVVLLCGPPPHFGDLSYAWTFNDNPLYVQEDNRRFVSQETGNLYIAKVEPSDVGNYTCFITNKEAQRSVQGPPTPLVQRTDGVMGEYEPKIEVRFPETIQAAKDSSVKLECFALGNPVPDISWRRLDGSPLPGKVKYSKSQAILEIPNFQQEDEGFYECIASNLRGRNLAKGQLIFYAPPEWEQKIQNTHLSIYDNLLWECKASGKPNPWYTWLKNGERLNPEERIQIENGTLIITMLNVSDSGVYQCAAENKYQIIYANAELRVLASAPDFSKSPVKKKSFVQVGGDIVIGCKPNAFPRAAISWKRGTETLRQSKRIFLLEDGSLKIYNITRSDAGSYTCIATNQFGTAKNTGSLIVKERTVITVPPSKMDVTVGESIVLPCQVSHDPSIEVVFVWFFNGDVIDLKKGVAHFERIGGESVGDLMIRNIQLHHSGKYLCTVQTTLESLSAVADIIVRGPPGPPEDVQVEDISSTTSQLSWRAGPDNNSPIQIFTIQTRTPFSVGWQAVATVPEILNGKTYNATVVGLSPWVEYEFRVVAGNSIGIGEPSEPSELLRTKASVPVVAPVNIHGGGGSRSELVITWESIPEELQNGEGFGYIIMFRPVGSTTWSKEKVSSVESSRFVYRNESIIPLSPFEVKVGVYNNEGEGSLSTVTIVYSGEDEPQLAPRGTSLQSFSASEMEVSWNAIAWNRNTGRVLGYEVLYWTDDSKESMIGKIRVSGNVTTKNITGLKANTIYFASVRAYNTAGTGPSSPPVNVTTKKSPPSQPPANIAWKLTNSKLCLNWEHVKTMENESEVLGYKILYRQNRQSKTHILETNNTSAELLVPFEEDYLIEIRTVSDGGDGSSSEEIRIPKMSSLSSRGIQFLEPSTHFLSIVIVIFHCFAI,Contactin-6,Contactins mediate cell surface interactions during nervous system development. Participates in oligodendrocytes generation by acting as a ligand of NOTCH1. Its association with NOTCH1 promotes NOTCH1 activation through the released notch intracellular domain (NICD) and subsequent translocation to the nucleus. Involved in motor coordination.,,In a breast cancer sample; somatic mutation.
1298,1298,1298,96567,Q08209-Y341F,MSEPKAIDPKLSTTDRVVKAVPFPPSHRLTAKEVFDNDGKPRVDILKAHLMKEGRLEESVALRIITEGASILRQEKNLLDIDAPVTVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDACMDAFDCLPLAALMNQQFLCVHGGLSPEINTLDDIRKLDRFKEPPAYGPMCDILWSDPLEDFGNEKTQEHFTHNTVRGCSYFYSYPAVCEFLQHNNLLSILRAHEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPFWLPNFMDVFTWSLPFVGEKVTEMLVNVLNICSDDELGSEEDGFDGATAAARKEVIRNKIRAIGKMARVFSVLREESESVLTLKGLTPTGMLPSGVLSGGKQTLQSATVEAIEADEAIKGFSPQHKITSFEEAKGLDRINERMPPRRDAMPSDANLNSINKALTSETNGTDSNGSNSSNIQ,"Resistant to cyclosporin A-mediated inhibition. Loss of Ca(2+)-mediated transcription factor NFAT activation; when associated with N-288, A-228 or 328-V--R-332 DEL. Partial loss in Ca(2+)-mediated transcription factor NFAT activation; when associated with F-288.",,MSEPKAIDPKLSTTDRVVKAVPFPPSHRLTAKEVFDNDGKPRVDILKAHLMKEGRLEESVALRIITEGASILRQEKNLLDIDAPVTVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDACMDAFDCLPLAALMNQQFLCVHGGLSPEINTLDDIRKLDRFKEPPAYGPMCDILWSDPLEDFGNEKTQEHFTHNTVRGCSYFYSYPAVCEFLQHNNLLSILRAHEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYWLPNFMDVFTWSLPFVGEKVTEMLVNVLNICSDDELGSEEDGFDGATAAARKEVIRNKIRAIGKMARVFSVLREESESVLTLKGLTPTGMLPSGVLSGGKQTLQSATVEAIEADEAIKGFSPQHKITSFEEAKGLDRINERMPPRRDAMPSDANLNSINKALTSETNGTDSNGSNSSNIQ,Protein phosphatase 3 catalytic subunit alpha,"Calcium-dependent, calmodulin-stimulated protein phosphatase which plays an essential role in the transduction of intracellular Ca(2+)-mediated signals. Many of the substrates contain a PxIxIT motif and/or a LxVP motif. In response to increased Ca(2+) levels, dephosphorylates and activates phosphatase SSH1 which results in cofilin dephosphorylation. In response to increased Ca(2+) levels following mitochondrial depolarization, dephosphorylates DNM1L inducing DNM1L translocation to the mitochondrion. Positively regulates the CACNA1B/CAV2.2-mediated Ca(2+) release probability at hippocampal neuronal soma and synaptic terminals. Dephosphorylates heat shock protein HSPB1. Dephosphorylates and activates transcription factor NFATC1. In response to increased Ca(2+) levels, regulates NFAT-mediated transcription probably by dephosphorylating NFAT and promoting its nuclear translocation. Dephosphorylates and inactivates transcription factor ELK1. Dephosphorylates DARPP32. May dephosphorylate CRTC2 at 'Ser-171' resulting in CRTC2 dissociation from 14-3-3 proteins. Dephosphorylates transcription factor TFEB at 'Ser-211' following Coxsackievirus B3 infection, promoting nuclear translocation. Required for postnatal development of the nephrogenic zone and superficial glomeruli in the kidneys, cell cycle homeostasis in the nephrogenic zone, and ultimately normal kidney function. Plays a role in intracellular AQP2 processing and localization to the apical membrane in the kidney, may thereby be required for efficient kidney filtration. Required for secretion of salivary enzymes amylase, peroxidase, lysozyme and sialic acid via formation of secretory vesicles in the submandibular glands. Required for calcineurin activity and homosynaptic depotentiation in the hippocampus. Required for normal differentiation and survival of keratinocytes and therefore required for epidermis superstructure formation. Positively regulates osteoblastic bone formation, via promotion of osteoblast differentiation. Positively regulates osteoclast differentiation, potentially via NFATC1 signaling. May play a role in skeletal muscle fiber type specification, potentially via NFATC1 signaling. Negatively regulates MAP3K14/NIK signaling via inhibition of nuclear translocation of the transcription factors RELA and RELB. Required for antigen-specific T-cell proliferation response.",,"Resistant to cyclosporin A-mediated inhibition. Loss of Ca(2+)-mediated transcription factor NFAT activation; when associated with N-288, A-228 or 328-V--R-332 DEL. Partial loss in Ca(2+)-mediated transcription factor NFAT activation; when associated with F-288."
1299,1299,1299,96613,P40340-S259A,MARNLRNRRGSDVEDASNAKVGYETQIKDENGIIHTTTRSLRKINYAEIEKVFDFLEDDQVMDKDETPVDVTSDEHHNNNQKGDDEDDDVDLVSPHENARTNEELTNERNLRKRKAHDPEEDDESFHEEDVDDDEEEEEADEFEDEYLDEDSKDNNRRRRAADRKFVVPDPDDDEEYDEDDEEGDRISHSASSKRLKRANSRRTRSSRHPETPPPVRRALRSRTRHSRTSNEENDDENDNSRNEALTLADEIRELQEDAPIREKRFLRERTKPVNYKLPPPLTASNAEEFIDKNNNALSFHNPSPARRGRGGWNASQNSGPTRRLFPTGGPFGGNDVTTIFGKNTNFYNQVPSAFSDNNNNKLILDSDSSDDEILPLGVTPKTKKENTQKKKKKKPEIADLDPLGVDMNVNFDDIGGLDNYIDQLKEMVALPLLYPELYQNFNITPPRGVLFHGPPGTGKTLMARALAASCSSDERKITFFMRKGADILSKWVGEAERQLRLLFEEAKKHQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGMDNRGQVIVIGATNRPDAVDPALRRPGRFDREFYFPLPDVKARFKILQIQTRKWSSPLSTNFIDKLAFLTKGYGGADLRSLCTEAALISIQRSFPQIYRSNDKLLVDPSKIKVKVSDFMLALKKIVPSSARSTGSSPQPLPELIKPLLADQLNNLKNKLDYMLNIKDTTFQRNTSLLQNFIDYEEYSGEEEEHDKYGGNEDTSSFRSYEFFESMAESQICKPRLLINGPKGNGQQYVGAAILNYLEEFNVQNLDLASLVSESSRTIEAAVVQSFMEAKKRQPSVVFIPNLDIWINTIPENVILVLSGLFRSLQSNEKILLLCLAENLDISEVKNGILSDFAFDKNIFQLHKPSKENITRYFSNLIELLKTKPSDIPMKKRRVKPLPELQKVTSNAAPTNFDENGEPLSEKVVLRRKLKSFQHQDMRLKNVLKIKLSGLMDLFKNRYKRFRKPPIDDAFLVHLFEPETSNDPNWQPA,"Severely decreases phosphorylation, causes a G2/M transition delay, and leads to sensitivity to 6-azauracil (impairs transcriptional elongation); when associated with A-11; A-67; A-94; A-212; A-230; A-241; A-285; A-304; A-369; A-370; A-380 and A-445.",,MARNLRNRRGSDVEDASNAKVGYETQIKDENGIIHTTTRSLRKINYAEIEKVFDFLEDDQVMDKDETPVDVTSDEHHNNNQKGDDEDDDVDLVSPHENARTNEELTNERNLRKRKAHDPEEDDESFHEEDVDDDEEEEEADEFEDEYLDEDSKDNNRRRRAADRKFVVPDPDDDEEYDEDDEEGDRISHSASSKRLKRANSRRTRSSRHPETPPPVRRALRSRTRHSRTSNEENDDENDNSRNEALTLADEIRELQEDSPIREKRFLRERTKPVNYKLPPPLTASNAEEFIDKNNNALSFHNPSPARRGRGGWNASQNSGPTRRLFPTGGPFGGNDVTTIFGKNTNFYNQVPSAFSDNNNNKLILDSDSSDDEILPLGVTPKTKKENTQKKKKKKPEIADLDPLGVDMNVNFDDIGGLDNYIDQLKEMVALPLLYPELYQNFNITPPRGVLFHGPPGTGKTLMARALAASCSSDERKITFFMRKGADILSKWVGEAERQLRLLFEEAKKHQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGMDNRGQVIVIGATNRPDAVDPALRRPGRFDREFYFPLPDVKARFKILQIQTRKWSSPLSTNFIDKLAFLTKGYGGADLRSLCTEAALISIQRSFPQIYRSNDKLLVDPSKIKVKVSDFMLALKKIVPSSARSTGSSPQPLPELIKPLLADQLNNLKNKLDYMLNIKDTTFQRNTSLLQNFIDYEEYSGEEEEHDKYGGNEDTSSFRSYEFFESMAESQICKPRLLINGPKGNGQQYVGAAILNYLEEFNVQNLDLASLVSESSRTIEAAVVQSFMEAKKRQPSVVFIPNLDIWINTIPENVILVLSGLFRSLQSNEKILLLCLAENLDISEVKNGILSDFAFDKNIFQLHKPSKENITRYFSNLIELLKTKPSDIPMKKRRVKPLPELQKVTSNAAPTNFDENGEPLSEKVVLRRKLKSFQHQDMRLKNVLKIKLSGLMDLFKNRYKRFRKPPIDDAFLVHLFEPETSNDPNWQPA,ATPase histone chaperone YTA7,"Functions as an ATP-dependent nucleosome disassembly factor that helps evict canonical histone H3 from the 5'-end of genes upon their induction. Also contributes to kinetochore assembly by cooperating with SCM3 to load the histone H3 variant CSE4/CENP-A at centromeres. Provides a chromatin boundary function at the 5'-end of genes that restricts access by RTT106 and thus prevents ectopic spreading of repressive chromatin into coding regions. Also prevents heterochromatin spreading downstream of the silent mating-type locus HMR, this function is independent of the tRNA boundary element. Contributes to appropriate cell cycle regulation of histone gene expression by recruiting RNA polymerase II to histone genes, and subsequent CDK1- and casein kinase II-dependent eviction from chromatin is required to promote transcriptional elongation.",,"Severely decreases phosphorylation, causes a G2/M transition delay, and leads to sensitivity to 6-azauracil (impairs transcriptional elongation); when associated with A-11; A-67; A-94; A-212; A-230; A-241; A-285; A-304; A-369; A-370; A-380 and A-445."
1300,1300,1300,96655,Q56184-C286A,MTIGSLGSTEFALHGKPAIRWGDLPQRVGKPETRRYQKVLLLNPSATLFRHDLPRCTYPLGLGYIAAVLEKYGYEVKILDVFAEGYYNAQPVDGDDQFLRYGLSDDDIVKVMKEFGPDVVGISSIFSNQADNVHHLLKLADLVTPEAVTAIGGAHARYFPKACLDDPNLDAVFLGEGEMTFLLWMEHLNGNVSDDEVHGIAWRDRDGKVQIKPELPLISSMRPEGPETGKSSPMLSMAGELDHIPFPAWHHYNMEKYFEIKAYQSPYTVGSRVGQLYTSRGCTAHATFCTTTHFWGQKLRRRSVQDVVDEVLRLRDEYGIDEFHIQDDNITNDMDHARELFRAFKEVGLPWATPQGTALWRMDEELLDLMAESGAYQVTFAIESGVQRVLKELIKKPLNLERTSHLIKYARSLGMHVHGFFIIGMPPMCGNAGESIEEMQASYDYAEEAGFSSASFFAASPIVGSELLRECIRQGFVDPEESLYRMTYKQGIINVPGLWDGEEIAELAAKFNRDFNARRDRAYTPQKQWNANQY,Lacks the [4Fe-4S] cluster; when associated with A-282 and A-289.,,MTIGSLGSTEFALHGKPAIRWGDLPQRVGKPETRRYQKVLLLNPSATLFRHDLPRCTYPLGLGYIAAVLEKYGYEVKILDVFAEGYYNAQPVDGDDQFLRYGLSDDDIVKVMKEFGPDVVGISSIFSNQADNVHHLLKLADLVTPEAVTAIGGAHARYFPKACLDDPNLDAVFLGEGEMTFLLWMEHLNGNVSDDEVHGIAWRDRDGKVQIKPELPLISSMRPEGPETGKSSPMLSMAGELDHIPFPAWHHYNMEKYFEIKAYQSPYTVGSRVGQLYTSRGCTAHCTFCTTTHFWGQKLRRRSVQDVVDEVLRLRDEYGIDEFHIQDDNITNDMDHARELFRAFKEVGLPWATPQGTALWRMDEELLDLMAESGAYQVTFAIESGVQRVLKELIKKPLNLERTSHLIKYARSLGMHVHGFFIIGMPPMCGNAGESIEEMQASYDYAEEAGFSSASFFAASPIVGSELLRECIRQGFVDPEESLYRMTYKQGIINVPGLWDGEEIAELAAKFNRDFNARRDRAYTPQKQWNANQY,Cytidylyl-2-hydroxyethylphosphonate methyltransferase,Involved in fosfomycin biosynthesis. Catalyzes the C-methylation of cytidylyl-2-hydroxyethylphosphonate (HEP-CMP) to form cytidylyl-2-hydroxypropylphosphonate (HPP-CMP). The C-methylation is not stereoselective and the ratio of (S)- to (R)-HPP-CMP is almost equal in vitro.,Site-directed mutagenesis of the cysteine residues in the radical SAM CxxxCxxC motif indicates that each residue is essential for functional cluster formation.,Lacks the [4Fe-4S] cluster; when associated with A-282 and A-289. Site-directed mutagenesis of the cysteine residues in the radical SAM CxxxCxxC motif indicates that each residue is essential for functional cluster formation.
1322,1322,1322,98594,P10619-Q49R,MIRAAPPPLFLLLLLLLLLVSWASRGEAAPDQDEIQRLPGLAKQPSFRRYSGYLKGSGSKHLHYWFVESQKDPENSPVVLWLNGGPGCSSLDGLLTEHGPFLVQPDGVTLEYNPYSWNLIANVLYLESPAGVGFSYSDDKFYATNDTEVAQSNFEALQDFFRLFPEYKNNKLFLTGESYAGIYIPTLAVLVMQDPSMNLQGLAVGNGLSSYEQNDNSLVYFAYYHGLLGNRLWSSLQTHCCSQNKCNFYDNKDLECVTNLQEVARIVGNSGLNIYNLYAPCAGGVPSHFRYEKDTVVVQDLGNIFTRLPLKRMWHQALLRSGDKVRMDPPCTNTTAASTYLNNPYVRKALNIPEQLPQWDMCNFLVNLQYRRLYRSMNSQYLKLLSSQKYQILLYNGDVDMACNFMGDEWFVDSLNQKMEVQRRPWLVKYGDSGEQIAGFVKEFSHIAFLTIKGAGHMVPTDKPLAAFTMFSRFLNKQPY,In GSL.,,MIRAAPPPLFLLLLLLLLLVSWASRGEAAPDQDEIQRLPGLAKQPSFRQYSGYLKGSGSKHLHYWFVESQKDPENSPVVLWLNGGPGCSSLDGLLTEHGPFLVQPDGVTLEYNPYSWNLIANVLYLESPAGVGFSYSDDKFYATNDTEVAQSNFEALQDFFRLFPEYKNNKLFLTGESYAGIYIPTLAVLVMQDPSMNLQGLAVGNGLSSYEQNDNSLVYFAYYHGLLGNRLWSSLQTHCCSQNKCNFYDNKDLECVTNLQEVARIVGNSGLNIYNLYAPCAGGVPSHFRYEKDTVVVQDLGNIFTRLPLKRMWHQALLRSGDKVRMDPPCTNTTAASTYLNNPYVRKALNIPEQLPQWDMCNFLVNLQYRRLYRSMNSQYLKLLSSQKYQILLYNGDVDMACNFMGDEWFVDSLNQKMEVQRRPWLVKYGDSGEQIAGFVKEFSHIAFLTIKGAGHMVPTDKPLAAFTMFSRFLNKQPY,Lysosomal protective protein,"Protective protein appears to be essential for both the activity of beta-galactosidase and neuraminidase, it associates with these enzymes and exerts a protective function necessary for their stability and activity. This protein is also a carboxypeptidase and can deamidate tachykinins.","The mutant cDNA clone, transiently expressed in a transformed galactosialidosis cell line, did not restore the secondarily deficient beta-galactosidase or alpha-neuraminidase activity.","In GSL. The mutant cDNA clone, transiently expressed in a transformed galactosialidosis cell line, did not restore the secondarily deficient beta-galactosidase or alpha-neuraminidase activity."
1336,1336,1336,99755,P46544-P37L,MMQITEKYLPFGNWQTYCRIVGEATDRAPLLLLHGGLGSSHNYFEVLDQVAEKSGRQVIMYDQLGCGNSSIPDDQAETAYTAQTWVKELENVREQLGLDQIHLLGQSWGGMLALIYLCDYQPEGVKSLILSSTLASAKLWSQELHRLIKYLPKGEQAAIKEAETTGNYDSLAYQAANAHFMDQHAIKLTPDLPEPVLRKKKGGSLAYLTGWGPNEYTPIGNLHGYEYTDRLKDLHLPALITSGTDDLCTPLVAKSMYDNLPNARWELFAGCGHMPFVQENAKYQELLSDWLISQD,Loss of activity.,,MMQITEKYLPFGNWQTYCRIVGEATDRAPLLLLHGGPGSSHNYFEVLDQVAEKSGRQVIMYDQLGCGNSSIPDDQAETAYTAQTWVKELENVREQLGLDQIHLLGQSWGGMLALIYLCDYQPEGVKSLILSSTLASAKLWSQELHRLIKYLPKGEQAAIKEAETTGNYDSLAYQAANAHFMDQHAIKLTPDLPEPVLRKKKGGSLAYLTGWGPNEYTPIGNLHGYEYTDRLKDLHLPALITSGTDDLCTPLVAKSMYDNLPNARWELFAGCGHMPFVQENAKYQELLSDWLISQD,Proline iminopeptidase,"Releases the N-terminal proline from various substrates. Has a high specificity towards di- or tripeptides with proline at the NH(2)-terminal position, but is not able to hydrolyze longer peptides, or peptides with hydroxyproline at the NH(2)-end. Partially hydrolyzes also peptides with alanine, glycine and leucine at the NH(2)-terminal position.",,Loss of activity.
1352,1352,1352,100998,P14222-I224N,MAARLLLLGILLLLLPLPVPAPCHTAARSECKRSHKFVPGAWLAGEGVDVTSLRRSGSFPVDTQRFLRPDGTCTLCENALQEGTLQRLPLALTNWRAQGSGCQRHVTRAKVSSTEAVARDAARSIRNDWKVGLDVTPKPTSNVHVSVAGSHSQAANFAAQKTHQDQYSFSTDTVECRFYSFHVVHTPPLHPDFKRALGDLPHHFNASTQPAYLRLISNYGTHFNRAVELGGRISALTALRTCELALEGLTDNEVEDCLTVEAQVNIGIHGSISAEAKACEEKKKKHKMTASFHQTYRERHSEVVGGHHTSINDLLFGIQAGPEQYSAWVNSLPGSPGLVDYTLEPLHVLLDSQDPRREALRRALSQYLTDRARWRDCSRPCPPGRQKSPRDPCQCVCHGSAVTTQDCCPRQRGLAQLEVTFIQAWGLWGDWFTATDAYVKLFFGGQELRTSTVWDNNNPIWSVRLDFGDVLLATGGPLRLQVWDQDSGRDDDLLGTCDQAPKSGSHEVRCNLNHGHLKFRYHARCLPHLGGGTCLDYVPQMLLGEPPGNRSGAVW,In FHL2.,,MAARLLLLGILLLLLPLPVPAPCHTAARSECKRSHKFVPGAWLAGEGVDVTSLRRSGSFPVDTQRFLRPDGTCTLCENALQEGTLQRLPLALTNWRAQGSGCQRHVTRAKVSSTEAVARDAARSIRNDWKVGLDVTPKPTSNVHVSVAGSHSQAANFAAQKTHQDQYSFSTDTVECRFYSFHVVHTPPLHPDFKRALGDLPHHFNASTQPAYLRLISNYGTHFIRAVELGGRISALTALRTCELALEGLTDNEVEDCLTVEAQVNIGIHGSISAEAKACEEKKKKHKMTASFHQTYRERHSEVVGGHHTSINDLLFGIQAGPEQYSAWVNSLPGSPGLVDYTLEPLHVLLDSQDPRREALRRALSQYLTDRARWRDCSRPCPPGRQKSPRDPCQCVCHGSAVTTQDCCPRQRGLAQLEVTFIQAWGLWGDWFTATDAYVKLFFGGQELRTSTVWDNNNPIWSVRLDFGDVLLATGGPLRLQVWDQDSGRDDDLLGTCDQAPKSGSHEVRCNLNHGHLKFRYHARCLPHLGGGTCLDYVPQMLLGEPPGNRSGAVW,Perforin-1,"Pore-forming protein that plays a key role in granzyme-mediated programmed cell death, and in defense against virus-infected or neoplastic cells. Plays an important role in killing other cells that are recognized as non-self by the immune system, e.g. in transplant rejection or some forms of autoimmune disease. Can insert into the membrane of target cells in its calcium-bound form, oligomerize and form large pores. Promotes cytolysis and apoptosis of target cells by facilitating the uptake of cytotoxic granzymes. Promotes cytolysis and apoptosis of target cells by facilitating the uptake of cytotoxic granzymes. Perforin pores allow the release of mature caspase-7 (CASP7) into the extracellular milieu.",A missense mutation at codon 224 () was identified in one patient.,In FHL2. A missense mutation at codon 224 () was identified in one patient.
1379,1379,1379,102856,Q62651-D204N,MATAMTVSSKLLGLLMQQLRGTRQLYFNVSLRSLSSSAQEASKRIPEEVSDHNYESIQVTSAQKHVLHVQLNRPEKRNAMNRAFWRELVECFQKISKDSDCRAVVVSGAGKMFTSGIDLMDMASDILQPPGDDVARIAWYLRDLISRYQKTFTVIEKCPKPVIAAIHGGCIGGGVDLISACDIRYCTQDAFFQVKEVDVGLAANVGTLQRLPKVIGNRSLVNELTFTARKMMADEALDSGLVSRVFPDKDVMLNAAFALAADISSKSPVAVQGSKINLIYSRDHSVDESLDYMATWNMSMLQTQDIIKSVQAAMEKKDSKSITFSKL,Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.,,MATAMTVSSKLLGLLMQQLRGTRQLYFNVSLRSLSSSAQEASKRIPEEVSDHNYESIQVTSAQKHVLHVQLNRPEKRNAMNRAFWRELVECFQKISKDSDCRAVVVSGAGKMFTSGIDLMDMASDILQPPGDDVARIAWYLRDLISRYQKTFTVIEKCPKPVIAAIHGGCIGGGVDLISACDIRYCTQDAFFQVKEVDVGLAADVGTLQRLPKVIGNRSLVNELTFTARKMMADEALDSGLVSRVFPDKDVMLNAAFALAADISSKSPVAVQGSKINLIYSRDHSVDESLDYMATWNMSMLQTQDIIKSVQAAMEKKDSKSITFSKL,Delta,"Isomerization of 3-trans,5-cis-dienoyl-CoA to 2-trans,4-trans-dienoyl-CoA.","Substitutions of D(204) by N resulted in 10(5)-fold lower activities. Such activity losses are consistent with the direct involvement of these latter two residues in the proposed proton transfers at carbons 2 and 6 or 8 of the substrates. Pbing of the wild-type and mutants forms of the enzyme with 2, 5-octadienoyl-CoA as substrate revealed low Delta(2), Delta(3)-enoyl-CoA isomerase and Delta(5), Delta(4)-enoyl-CoA isomerase activities catalyzed by E(196) and D(204), respectively. Altogether, these data reveal that positional isomerizations of the diene and triene are facilitated by simultaneous proton transfers involving E(196) and D(204), whereas each residue alone can catalyze, albeit less efficiently, a monoene isomerization.","Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity. Substitutions of D(204) by N resulted in 10(5)-fold lower activities. Such activity losses are consistent with the direct involvement of these latter two residues in the proposed proton transfers at carbons 2 and 6 or 8 of the substrates. Pbing of the wild-type and mutants forms of the enzyme with 2, 5-octadienoyl-CoA as substrate revealed low Delta(2), Delta(3)-enoyl-CoA isomerase and Delta(5), Delta(4)-enoyl-CoA isomerase activities catalyzed by E(196) and D(204), respectively. Altogether, these data reveal that positional isomerizations of the diene and triene are facilitated by simultaneous proton transfers involving E(196) and D(204), whereas each residue alone can catalyze, albeit less efficiently, a monoene isomerization."
1396,1396,1396,103639,Q969Q1-F73S,MDYKSSLIQDGNPMENLEKQLICPICLEMFTKPVVILPCQHNLCRKCANDIFQAANPYWTSRGSSVSMSGGRSRCPTCRHEVIMDRHGVYGLQRNLLVENIIDIYKQECSSRPLQKGSHPMCKEHEDEKINIYCLTCEVPTCSMCKVFGIHKACEVAPLQSVFQGQKTELNNCISMLVAGNDRVQTIITQLEDSRRVTKENSHQVKEELSQKFDTLYAILDEKKSELLQRITQEQEKKLSFIEALIQQYQEQLDKSTKLVETAIQSLDEPGGATFLLTAKQLIKSIVEASKGCQLGKTEQGFENMDFFTLDLEHIADALRAIDFGTDEEEEEFIEEEDQEEEESTEGKEEGHQ,Rare variant; found in a patient with hypertrophic cardiomyopathy; unknown pathological significance.,,MDYKSSLIQDGNPMENLEKQLICPICLEMFTKPVVILPCQHNLCRKCANDIFQAANPYWTSRGSSVSMSGGRFRCPTCRHEVIMDRHGVYGLQRNLLVENIIDIYKQECSSRPLQKGSHPMCKEHEDEKINIYCLTCEVPTCSMCKVFGIHKACEVAPLQSVFQGQKTELNNCISMLVAGNDRVQTIITQLEDSRRVTKENSHQVKEELSQKFDTLYAILDEKKSELLQRITQEQEKKLSFIEALIQQYQEQLDKSTKLVETAIQSLDEPGGATFLLTAKQLIKSIVEASKGCQLGKTEQGFENMDFFTLDLEHIADALRAIDFGTDEEEEEFIEEEDQEEEESTEGKEEGHQ,E3 ubiquitin-protein ligase TRIM63,"E3 ubiquitin ligase. Mediates the ubiquitination and subsequent proteasomal degradation of CKM, GMEB1 and HIBADH. Regulates the proteasomal degradation of muscle proteins under amino acid starvation, where muscle protein is catabolized to provide other organs with amino acids. Inhibits de novo skeletal muscle protein synthesis under amino acid starvation. Regulates proteasomal degradation of cardiac troponin I/TNNI3 and probably of other sarcomeric-associated proteins. May play a role in striated muscle atrophy and hypertrophy by regulating an anti-hypertrophic PKC-mediated signaling pathway. May regulate the organization of myofibrils through TTN in muscle cells.",,Rare variant; found in a patient with hypertrophic cardiomyopathy; unknown pathological significance.
1422,1422,1422,105369,P20606-K36M,MAGWDIFGWFRDVLASLGLWNKHGKLLFLGLDNAGMTTLLHMLKNDRLATLQPTWHPTSEELAIGNIKFTTFDLGGHIQARRLWKDYFPEVNGIVFLVDAADPERFDEARVELDALFNIAELKDVPFVILGNKIDAPNAVSEAELRSALGLLNTTGSQRIEGQRPVEVFMCSVVMRNGYLEAFQWLSQYI,No cell growth at 23 or 37 degrees Celsius.,,MAGWDIFGWFRDVLASLGLWNKHGKLLFLGLDNAGKTTLLHMLKNDRLATLQPTWHPTSEELAIGNIKFTTFDLGGHIQARRLWKDYFPEVNGIVFLVDAADPERFDEARVELDALFNIAELKDVPFVILGNKIDAPNAVSEAELRSALGLLNTTGSQRIEGQRPVEVFMCSVVMRNGYLEAFQWLSQYI,Small COPII coat GTPase SAR1,"Small GTPase component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. SAR1 controls the coat assembly in a stepwise manner. Activated SAR1-GTP by SEC12 binds to membranes first and recruits the SEC23/24 complex. These SEC23/24-SAR1 prebudding intermediates are then collected by the SEC13/31 complex as subunits polymerize to form coated transport vesicles. Conversion to SAR1-GDP triggers coat release and recycles COPII subunits.",,No cell growth at 23 or 37 degrees Celsius.
1433,1433,1433,106313,P15428-Y151F,MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQFEPQKTLFIQCDVADQQQLRDTFRKVVDHFGRLDILVNNAGVNNEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEGGIIINMSSLAGLMPVAQQPVFCASKHGIVGFTRSAALAANLMNSGVRLNAICPGFVNTAILESIEKEENMGQYIEYKDHIKDMIKYYGILDPPLIANGLITLIEDDALNGAIMKITTSKGIHFQDYDTTPFQAKTQ,Loss 15-hydroxyprostaglandin dehydrogenase activity.,,MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQFEPQKTLFIQCDVADQQQLRDTFRKVVDHFGRLDILVNNAGVNNEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEGGIIINMSSLAGLMPVAQQPVYCASKHGIVGFTRSAALAANLMNSGVRLNAICPGFVNTAILESIEKEENMGQYIEYKDHIKDMIKYYGILDPPLIANGLITLIEDDALNGAIMKITTSKGIHFQDYDTTPFQAKTQ,15-hydroxyprostaglandin dehydrogenase [NAD,"Catalyzes the NAD-dependent dehydrogenation (oxidation) of a broad array of hydroxylated polyunsaturated fatty acids (mainly eicosanoids and docosanoids, including prostaglandins, lipoxins and resolvins), yielding their corresponding keto (oxo) metabolites. Decreases the levels of the pro-proliferative prostaglandins such as prostaglandin E2 (whose activity is increased in cancer because of an increase in the expression of cyclooxygenase 2) and generates oxo-fatty acid products that can profoundly influence cell function by abrogating pro-inflammatory cytokine expression. Converts resolvins E1, D1 and D2 to their oxo products, which represents a mode of resolvin inactivation. Resolvin E1 plays important roles during the resolution phase of acute inflammation, while resolvins D1 and D2 have a unique role in obesity-induced adipose inflammation.","The mutant protein with the mutation was found to be inactive, indicating that tyrosine-151 is required for 15-PGDH activity.","Loss 15-hydroxyprostaglandin dehydrogenase activity. The mutant protein with the mutation was found to be inactive, indicating that tyrosine-151 is required for 15-PGDH activity."
1441,1441,1441,106792,P18054-H355Q,MGRYRIRVATGAWLFSGSYNRVQLWLVGTRGEAELELQLRPARGEEEEFDHDVAEDLGLLQFVRLRKHHWLVDDAWFCDRITVQGPGACAEVAFPCYRWVQGEDILSLPEGTARLPGDNALDMFQKHREKELKDRQQIYCWATWKEGLPLTIAADRKDDLPPNMRFHEEKRLDFEWTLKAGALEMALKRVYTLLSSWNCLEDFDQIFWGQKSALAEKVRQCWQDDELFSYQFLNGANPMLLRRSTSLPSRLVLPSGMEELQAQLEKELQNGSLFEADFILLDGIPANVIRGEKQYLAAPLVMLKMEPNGKLQPMVIQIQPPNPSSPTPTLFLPSDPPLAWLLAKSWVRNSDFQLQEIQYHLLNTHLVAEVIAVATMRCLPGLHPIFKFLIPHIRYTMEINTRARTQLISDGGIFDKAVSTGGGGHVQLLRRAAAQLTYCSLCPPDDLADRGLLGLPGALYAHDALRLWEIIARYVEGIVHLFYQRDDIVKGDPELQAWCREITEVGLCQAQDRGFPVSFQSQSQLCHFLTMCVFTCTAQHAAINQGQLDWYAWVPNAPCTMRMPPPTTKEDVTMATVMGSLPDVRQACLQMAISWHLSRRQPDMVPLGHHKEKYFSGPKPKAVLNQFRTDLEKLEKEITARNEQLDWPYEYLKPSCIENSVTI,No effect on arachidonate 12(S)-lipoxygenase activity.,,MGRYRIRVATGAWLFSGSYNRVQLWLVGTRGEAELELQLRPARGEEEEFDHDVAEDLGLLQFVRLRKHHWLVDDAWFCDRITVQGPGACAEVAFPCYRWVQGEDILSLPEGTARLPGDNALDMFQKHREKELKDRQQIYCWATWKEGLPLTIAADRKDDLPPNMRFHEEKRLDFEWTLKAGALEMALKRVYTLLSSWNCLEDFDQIFWGQKSALAEKVRQCWQDDELFSYQFLNGANPMLLRRSTSLPSRLVLPSGMEELQAQLEKELQNGSLFEADFILLDGIPANVIRGEKQYLAAPLVMLKMEPNGKLQPMVIQIQPPNPSSPTPTLFLPSDPPLAWLLAKSWVRNSDFQLHEIQYHLLNTHLVAEVIAVATMRCLPGLHPIFKFLIPHIRYTMEINTRARTQLISDGGIFDKAVSTGGGGHVQLLRRAAAQLTYCSLCPPDDLADRGLLGLPGALYAHDALRLWEIIARYVEGIVHLFYQRDDIVKGDPELQAWCREITEVGLCQAQDRGFPVSFQSQSQLCHFLTMCVFTCTAQHAAINQGQLDWYAWVPNAPCTMRMPPPTTKEDVTMATVMGSLPDVRQACLQMAISWHLSRRQPDMVPLGHHKEKYFSGPKPKAVLNQFRTDLEKLEKEITARNEQLDWPYEYLKPSCIENSVTI,Polyunsaturated fatty acid lipoxygenase ALOX12,"Catalyzes the regio and stereo-specific incorporation of molecular oxygen into free and esterified polyunsaturated fatty acids generating lipid hydroperoxides that can be further reduced to the corresponding hydroxy species. Mainly converts arachidonate ((5Z,8Z,11Z,14Z)-eicosatetraenoate) to the specific bioactive lipid (12S)-hydroperoxyeicosatetraenoate/(12S)-HPETE. Through the production of bioactive lipids like (12S)-HPETE it regulates different biological processes including platelet activation. It can also catalyze the epoxidation of double bonds of polyunsaturated fatty acids such as (14S)-hydroperoxy-docosahexaenoate/(14S)-HPDHA resulting in the formation of (13S,14S)-epoxy-DHA. Furthermore, it may participate in the sequential oxidations of DHA ((4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate) to generate specialized pro-resolving mediators (SPMs) like resolvin D5 ((7S,17S)-diHPDHA) and (7S,14S)-diHPDHA, that actively down-regulate the immune response and have anti-aggregation properties with platelets. An additional function involves a multistep process by which it transforms leukotriene A4/LTA4 into the bioactive lipids lipoxin A4/LXA4 and lipoxin B4/LXB4, both are vasoactive and LXA4 may regulate neutrophil function via occupancy of specific recognition sites. Can also peroxidize linoleate ((9Z,12Z)-octadecadienoate) to (13S)-hydroperoxyoctadecadienoate/ (13S-HPODE). Due to its role in regulating both the expression of the vascular endothelial growth factor (VEGF, an angiogenic factor involved in the survival and metastasis of solid tumors) and the expression of integrin beta-1 (known to affect tumor cell migration and proliferation), it can be regarded as protumorigenic. Important for cell survival, as it may play a role not only in proliferation but also in the prevention of apoptosis in vascular smooth muscle cells.","Altered histidines at positions 355, 383, and 392 retained enzymatic activity.","No effect on arachidonate 12(S)-lipoxygenase activity. Altered histidines at positions 355, 383, and 392 retained enzymatic activity."
1461,1461,1461,108687,Q5JFM9-D202N,MAVVKEVLEIAEKIKNMEIRGAGKIARSAAYALQLQAEKSKATNVDEFWKEMKQAAKILFETRPTAVSLPNALRYVMHRGKIAYSSGADLEQLRFVIINAAKEFIHNSEKALERIGEFGAKRIEDGDVIMTHCHSKAAISVMKTAWEQGKDIKVIVTETRPKWQGKITAKELASYGIPVIYVVDSAARHYMKMTDKVVMGANSITVNGAVINKIGTALIALTAKEHRVWTMIAAETYKFHPETMLGQLVEIEMRDPTEVIPEDELKTWPKNIEVWNPAFDVTPPEYVDVIITERGIIPPYAAIDILREEFGWALKYTEPWED,Loss of catalytic activity.,,MAVVKEVLEIAEKIKNMEIRGAGKIARSAAYALQLQAEKSKATNVDEFWKEMKQAAKILFETRPTAVSLPNALRYVMHRGKIAYSSGADLEQLRFVIINAAKEFIHNSEKALERIGEFGAKRIEDGDVIMTHCHSKAAISVMKTAWEQGKDIKVIVTETRPKWQGKITAKELASYGIPVIYVVDSAARHYMKMTDKVVMGADSITVNGAVINKIGTALIALTAKEHRVWTMIAAETYKFHPETMLGQLVEIEMRDPTEVIPEDELKTWPKNIEVWNPAFDVTPPEYVDVIITERGIIPPYAAIDILREEFGWALKYTEPWED,"Ribose 1,5-bisphosphate isomerase","Catalyzes the isomerization of ribose 1,5-bisphosphate (R15P) to ribulose 1,5-bisphosphate (RuBP), the CO(2) acceptor and substrate for RubisCO. Only accepts the alpha-anomer of D-ribose 1,5-bisphosphate as substrate, being inactive on the beta-anomer. Displays a strict substrate specificity, since other phosphorylated sugars such as R5P, ribose, G16P, G6P, G1P, FBP, F6P, and PRPP, are not substrates. Functions in an archaeal AMP degradation pathway, together with AMP phosphorylase and RubisCO.","The D202 residue is essential for ribulose 1, 5-bisphosphate production.","Loss of catalytic activity. The D202 residue is essential for ribulose 1, 5-bisphosphate production."
1469,1469,1469,109500,P50416-G710E,MAEAHQAVAFQFTVTPDGIDLRLSHEALRQIYLSGLHSWKKKFIRFKNGIITGVYPASPSSWLIVVVGVMTTMYAKIDPSLGIIAKINRTLETANCMSSQTKNVVSGVLFGTGLWVALIVTMRYSLKVLLSYHGWMFTEHGKMSRATKIWMGMVKIFSGRKPMLYSFQTSLPRLPVPAVKDTVNRYLQSVRPLMKEEDFKRMTALAQDFAVGLGPRLQWYLKLKSWWATNYVSDWWEEYIYLRGRGPLMVNSNYYAMDLLYILPTHIQAARAGNAIHAILLYRRKLDREEIKPIRLLGSTIPLCSAQWERMFNTSRIPGEETDTIQHMRDSKHIVVYHRGRYFKVWLYHDGRLLKPREMEQQMQRILDNTSEPQPGEARLAALTAGDRVPWARCRQAYFGRGKNKQSLDAVEKAAFFVTLDETEEGYRSEDPDTSMDSYAKSLLHGRCYDRWFDKSFTFVVFKNGKMGLNAEHSWADAPIVAHLWEYVMSIDSLQLGYAEDGHCKGDINPNIPYPTRLQWDIPGECQEVIETSLNTANLLANDVDFHSFPFVAFGKGIIKKCRTSPDAFVQLALQLAHYKDMGKFCLTYEASMTRLFREGRTETVRSCTTESCDFVRAMVDPAQTVEQRLKLFKLASEKHQHMYRLAMTGSGIDRHLFCLYVVSKYLAVESPFLKEVLSEPWRLSTSQTPQQQVELFDLENNPEYVSSGEGFGPVADDGYGVSYILVGENLINFHISSKFSCPETDSHRFGRHLKEAMTDIITLFGLSSNSKK,In CPT1AD; loss of activity.,,MAEAHQAVAFQFTVTPDGIDLRLSHEALRQIYLSGLHSWKKKFIRFKNGIITGVYPASPSSWLIVVVGVMTTMYAKIDPSLGIIAKINRTLETANCMSSQTKNVVSGVLFGTGLWVALIVTMRYSLKVLLSYHGWMFTEHGKMSRATKIWMGMVKIFSGRKPMLYSFQTSLPRLPVPAVKDTVNRYLQSVRPLMKEEDFKRMTALAQDFAVGLGPRLQWYLKLKSWWATNYVSDWWEEYIYLRGRGPLMVNSNYYAMDLLYILPTHIQAARAGNAIHAILLYRRKLDREEIKPIRLLGSTIPLCSAQWERMFNTSRIPGEETDTIQHMRDSKHIVVYHRGRYFKVWLYHDGRLLKPREMEQQMQRILDNTSEPQPGEARLAALTAGDRVPWARCRQAYFGRGKNKQSLDAVEKAAFFVTLDETEEGYRSEDPDTSMDSYAKSLLHGRCYDRWFDKSFTFVVFKNGKMGLNAEHSWADAPIVAHLWEYVMSIDSLQLGYAEDGHCKGDINPNIPYPTRLQWDIPGECQEVIETSLNTANLLANDVDFHSFPFVAFGKGIIKKCRTSPDAFVQLALQLAHYKDMGKFCLTYEASMTRLFREGRTETVRSCTTESCDFVRAMVDPAQTVEQRLKLFKLASEKHQHMYRLAMTGSGIDRHLFCLYVVSKYLAVESPFLKEVLSEPWRLSTSQTPQQQVELFDLENNPEYVSSGGGFGPVADDGYGVSYILVGENLINFHISSKFSCPETDSHRFGRHLKEAMTDIITLFGLSSNSKK,"Carnitine O-palmitoyltransferase 1, liver isoform","Catalyzes the transfer of the acyl group of long-chain fatty acid-CoA conjugates onto carnitine, an essential step for the mitochondrial uptake of long-chain fatty acids and their subsequent beta-oxidation in the mitochondrion. Plays an important role in hepatic triglyceride metabolism.","The mutation dramatically impairs the catalytic function of CPT1A. Mutations and abolish CPT1A activity. They affect G residues that are essential not only for the structure of the hydrophobic core in the catalytic site, but also for the chain-length specificity of CPT isoforms.","In CPT1AD; loss of activity. The mutation dramatically impairs the catalytic function of CPT1A. Mutations and abolish CPT1A activity. They affect G residues that are essential not only for the structure of the hydrophobic core in the catalytic site, but also for the chain-length specificity of CPT isoforms."
1473,1473,1473,109839,Q9LT31-Y225A,MENTDVFLGLHDFLERMRKPSAGDFVKSIKSFIVSFSNNAPDPEKDCAMVQEFFSKMEAAFRAHPLWSGCSEEELDSAGDGLEKYVMTKLFTRVFASNTEEVIADEKLFQKMSLVQQFISPENLDIQPTFQNESSWLLAQKELQKINMYKAPRDKLVCILNCCKVINNLLLNASIASNENAPGADEFLPVLIYVTIKANPPQLHSNLLYIQRYRRESKLVGEAAAFFTNILSAESFISNIDAKSISLDEAEFEKNMESARARISGLDSQTYQTGHGSAPPPRDESTLQKTQSLNPKRENTLFQSKSSDSLSGTNELLNINSETPMKKAESISDLENKGATLLKDTEPSKVFQEYPYIFASAGDLRIGDVEGLLNSYKQLVFKYVCLTKGLGDGTSLAPSSSPLQASSGFNTSKESEDHRRSSSDVQMTKETDRSVDDLIRALHGEGEDVNNLSDVKHEEYGAMLVEGKDEERDSKVQGEVDAKDIELMKQIPKREGDNSSSRPAEDEDVGSKQPVTEASE,Loss of interaction with RABF2B. Decreases GEF activity 25-fold.,,MENTDVFLGLHDFLERMRKPSAGDFVKSIKSFIVSFSNNAPDPEKDCAMVQEFFSKMEAAFRAHPLWSGCSEEELDSAGDGLEKYVMTKLFTRVFASNTEEVIADEKLFQKMSLVQQFISPENLDIQPTFQNESSWLLAQKELQKINMYKAPRDKLVCILNCCKVINNLLLNASIASNENAPGADEFLPVLIYVTIKANPPQLHSNLLYIQRYRRESKLVGEAAYFFTNILSAESFISNIDAKSISLDEAEFEKNMESARARISGLDSQTYQTGHGSAPPPRDESTLQKTQSLNPKRENTLFQSKSSDSLSGTNELLNINSETPMKKAESISDLENKGATLLKDTEPSKVFQEYPYIFASAGDLRIGDVEGLLNSYKQLVFKYVCLTKGLGDGTSLAPSSSPLQASSGFNTSKESEDHRRSSSDVQMTKETDRSVDDLIRALHGEGEDVNNLSDVKHEEYGAMLVEGKDEERDSKVQGEVDAKDIELMKQIPKREGDNSSSRPAEDEDVGSKQPVTEASE,Vacuolar protein sorting-associated protein 9A,"Functions as guanine nucleotide exchange factor (GEF) for Rab small GTPases. Activates specifically RABF1, RABF2A and RABF2B proteins. Required for early stages of embryogenesis, cytokinesis, embryogenesis, and organ development. Is essential for the establishment or maintenance of the polar localization of the auxin efflux carrier PIN1.",,Loss of interaction with RABF2B. Decreases GEF activity 25-fold.
1482,1482,1482,110389,P54686-F181A,MSVTLKNIIAPTPATTRGKSVAINGDPKGENIVYASGSSIIIRNVKNPMVADIYYEHPCQTTVAKYAPSGNYIASGDVQGNLRIWDTLQKEHILKATYKVLNGAILDIAWTSDNQRLVVVGDGKERFGAAILWDSGSSCGEITGHSKMILSCDIKSTRPFRAATGSEDFAVNWFEGPPFKAQKNIAAGDFTRFVNCVRFSPDGNKLVTVGADKKAFVYDGKTGEKLIELNPAQQHTGGIYGCSWSADNNRVLTASADKSCKIWDTTTGQCINSFTFGSDVNDQQLGCLWFGDSLLSVNLAGEISTLNLDDVAKPSRVIKGHNKLVGTIAFDKNAGSLYSASYDASLLQWDLSTGLATNFTGPAHKNQITSIKINGDQLITCAMDDSVKISSISKKTYGESIGVDSPAQAVAFSGDVVVAVSMKTIYVIKGGKIVSQTAATWEPTSVAINDTEVSVGGKDNKIHVFTLSGNNLTASHTLDNHRGAITDLSYSPCGKYLASGCSNREVIVWSGKEAKSKGWVNHTARINAVAWSNDSKFVASASLDSQIYIWNVENPTASPVQVKNSHLGGVNDVIYGSNNEIFSAGNEGAIKIWNVSN,No effect on binding to cofilin or F-actin but does not restore impaired chemotaxis or F-actin assembly in cells lacking nhe1; when associated with A-125; A-167 and A-193.,,MSVTLKNIIAPTPATTRGKSVAINGDPKGENIVYASGSSIIIRNVKNPMVADIYYEHPCQTTVAKYAPSGNYIASGDVQGNLRIWDTLQKEHILKATYKVLNGAILDIAWTSDNQRLVVVGDGKERFGAAILWDSGSSCGEITGHSKMILSCDIKSTRPFRAATGSEDFAVNWFEGPPFKFQKNIAAGDFTRFVNCVRFSPDGNKLVTVGADKKAFVYDGKTGEKLIELNPAQQHTGGIYGCSWSADNNRVLTASADKSCKIWDTTTGQCINSFTFGSDVNDQQLGCLWFGDSLLSVNLAGEISTLNLDDVAKPSRVIKGHNKLVGTIAFDKNAGSLYSASYDASLLQWDLSTGLATNFTGPAHKNQITSIKINGDQLITCAMDDSVKISSISKKTYGESIGVDSPAQAVAFSGDVVVAVSMKTIYVIKGGKIVSQTAATWEPTSVAINDTEVSVGGKDNKIHVFTLSGNNLTASHTLDNHRGAITDLSYSPCGKYLASGCSNREVIVWSGKEAKSKGWVNHTARINAVAWSNDSKFVASASLDSQIYIWNVENPTASPVQVKNSHLGGVNDVIYGSNNEIFSAGNEGAIKIWNVSN,Actin-interacting protein 1,Implicated in both actin filament depolymerization and polymerization. May enhance chemotaxis by promoting cofilin-dependent actin assembly at cell leading edges.,,No effect on binding to cofilin or F-actin but does not restore impaired chemotaxis or F-actin assembly in cells lacking nhe1; when associated with A-125; A-167 and A-193.
1486,1486,1486,110724,P75906-D115A,MLRNGNKYLLMLVSIIMLTACISQSRTSFIPPQDRESLLAEQPWPHNGFVAISWHNVEDEAADQRFMSVRTSALREQFAWLRENGYQPVSIAQIREAHRGGKPLPEKAVVLTFDAGYQSFYTRVFPILQAFQWPAVWAPVGSWVDTPADKQVKFGDELVDREYFATWQQVREVARSRLVELASHTWNSHYGIQANATGSLLPVYVNRAYFTDHARYETAAEYRERIRLDAVKMTEYLRTKVEVNPHVFVWPYGEANGIAIEELKKLGYDMFFTLESGLANASQLDSIPRVLIANNPSLKEFAQQIITVQEKSPQRIMHIDLDYVYDENLQQMDRNIDVLIQRVKDMQISTVYLQAFADPDGDGLVKEVWFPNRLLPMKADIFSRVAWQLRTRSGVNIYAWMPVLSWDLDPTLTRVKYLPTGEKKAQIHPEQYHRLSPFDDRVRAQVGMLYEDLAGHAAFDGILFHDDALLSDYEDASAPAITAYQQAGFSGSLSEIRQNPEQFKQWARFKSRALTDFTLELSARVKAIRGPHIKTARNIFALPVIQPESEAWFAQNYADFLKSYDWTAIMAMPYLEGVAEKSADQWLIQLTNQIKNIPQAKDKSILELQAQNWQKNGQHQAISSQQLAHWMSLLQLNGVKNYGYYPDNFLHNQPEIDLIRPEFSTAWYPKND,High decrease in catalytic activity. Unable to support biofilm formation and PGA secretion.,,MLRNGNKYLLMLVSIIMLTACISQSRTSFIPPQDRESLLAEQPWPHNGFVAISWHNVEDEAADQRFMSVRTSALREQFAWLRENGYQPVSIAQIREAHRGGKPLPEKAVVLTFDDGYQSFYTRVFPILQAFQWPAVWAPVGSWVDTPADKQVKFGDELVDREYFATWQQVREVARSRLVELASHTWNSHYGIQANATGSLLPVYVNRAYFTDHARYETAAEYRERIRLDAVKMTEYLRTKVEVNPHVFVWPYGEANGIAIEELKKLGYDMFFTLESGLANASQLDSIPRVLIANNPSLKEFAQQIITVQEKSPQRIMHIDLDYVYDENLQQMDRNIDVLIQRVKDMQISTVYLQAFADPDGDGLVKEVWFPNRLLPMKADIFSRVAWQLRTRSGVNIYAWMPVLSWDLDPTLTRVKYLPTGEKKAQIHPEQYHRLSPFDDRVRAQVGMLYEDLAGHAAFDGILFHDDALLSDYEDASAPAITAYQQAGFSGSLSEIRQNPEQFKQWARFKSRALTDFTLELSARVKAIRGPHIKTARNIFALPVIQPESEAWFAQNYADFLKSYDWTAIMAMPYLEGVAEKSADQWLIQLTNQIKNIPQAKDKSILELQAQNWQKNGQHQAISSQQLAHWMSLLQLNGVKNYGYYPDNFLHNQPEIDLIRPEFSTAWYPKND,"Poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase","Catalyzes the N-deacetylation of poly-beta-1,6-N-acetyl-D-glucosamine (PGA), a biofilm adhesin polysaccharide. N-deacetylation promotes PGA export through the PgaA porin.",PgaD is needed for PGA formation.,High decrease in catalytic activity. Unable to support biofilm formation and PGA secretion. PgaD is needed for PGA formation.
1487,1487,1487,110731,P40763-P330S,MAQWNQLQQLDTRYLEQLHQLYSDSFPMELRQFLAPWIESQDWAYAASKESHATLVFHNLLGEIDQQYSRFLQESNVLYQHNLRRIKQFLQSRYLEKPMEIARIVARCLWEESRLLQTAATAAQQGGQANHPTAAVVTEKQQMLEQHLQDVRKRVQDLEQKMKVVENLQDDFDFNYKTLKSQGDMQDLNGNNQSVTRQKMQQLEQMLTALDQMRRSIVSELAGLLSAMEYVQKTLTDEELADWKRRQQIACIGGPPNICLDRLENWITSLAESQLQTRQQIKKLEELQQKVSYKGDPIVQHRPMLEERIVELFRNLMKSAFVVERQPCMSMHPDRPLVIKTGVQFTTKVRLLVKFPELNYQLKIKVCIDKDSGDVAALRGSRKFNILGTNTKVMNMEESNNGSLSAEFKHLTLREQRCGNGGRANCDASLIVTEELHLITFETEVYHQGLKIDLETHSLPVVVISNICQMPNAWASILWYNMLTNNPKNVNFFTKPPIGTWDQVAEVLSWQFSSTTKRGLSIEQLTTLAEKLLGPGVNYSGCQITWAKFCKENMAGKGFSFWVWLDNIIDLVKKYILALWNEGYIMGFISKERERAILSTKPPGTFLLRFSESSKEGGVTFTWVEKDISGKTQIQSVEPYTKQQLNNMSFAEIIMGYKIMDATNILVSPLVYLYPDIPKEEAFGKYCRPESQEHPEADPGSAAPYLKTKFICVTPTTCSNTIDLPMSPRTLDSLMQFGNNGEGAEPSAGGQFESLTFDMELTSECATSPM,In ADMIO1; increases transcriptional activity; increases binding to ISL1 promoter region; decreases glucose stimulated insulin secretion.,,MAQWNQLQQLDTRYLEQLHQLYSDSFPMELRQFLAPWIESQDWAYAASKESHATLVFHNLLGEIDQQYSRFLQESNVLYQHNLRRIKQFLQSRYLEKPMEIARIVARCLWEESRLLQTAATAAQQGGQANHPTAAVVTEKQQMLEQHLQDVRKRVQDLEQKMKVVENLQDDFDFNYKTLKSQGDMQDLNGNNQSVTRQKMQQLEQMLTALDQMRRSIVSELAGLLSAMEYVQKTLTDEELADWKRRQQIACIGGPPNICLDRLENWITSLAESQLQTRQQIKKLEELQQKVSYKGDPIVQHRPMLEERIVELFRNLMKSAFVVERQPCMPMHPDRPLVIKTGVQFTTKVRLLVKFPELNYQLKIKVCIDKDSGDVAALRGSRKFNILGTNTKVMNMEESNNGSLSAEFKHLTLREQRCGNGGRANCDASLIVTEELHLITFETEVYHQGLKIDLETHSLPVVVISNICQMPNAWASILWYNMLTNNPKNVNFFTKPPIGTWDQVAEVLSWQFSSTTKRGLSIEQLTTLAEKLLGPGVNYSGCQITWAKFCKENMAGKGFSFWVWLDNIIDLVKKYILALWNEGYIMGFISKERERAILSTKPPGTFLLRFSESSKEGGVTFTWVEKDISGKTQIQSVEPYTKQQLNNMSFAEIIMGYKIMDATNILVSPLVYLYPDIPKEEAFGKYCRPESQEHPEADPGSAAPYLKTKFICVTPTTCSNTIDLPMSPRTLDSLMQFGNNGEGAEPSAGGQFESLTFDMELTSECATSPM,Signal transducer and activator of transcription 3,"Signal transducer and transcription activator that mediates cellular responses to interleukins, KITLG/SCF, LEP and other growth factors. Once activated, recruits coactivators, such as NCOA1 or MED1, to the promoter region of the target gene. May mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4. Upon activation of IL6ST/gp130 signaling by interleukin-6 (IL6), binds to the IL6-responsive elements identified in the promoters of various acute-phase protein genes. Activated by IL31 through IL31RA. Acts as a regulator of inflammatory response by regulating differentiation of naive CD4(+) T-cells into T-helper Th17 or regulatory T-cells (Treg): deacetylation and oxidation of lysine residues by LOXL3, leads to disrupt STAT3 dimerization and inhibit its transcription activity. Involved in cell cycle regulation by inducing the expression of key genes for the progression from G1 to S phase, such as CCND1. Mediates the effects of LEP on melanocortin production, body energy homeostasis and lactation. May play an apoptotic role by transctivating BIRC5 expression under LEP activation. Cytoplasmic STAT3 represses macroautophagy by inhibiting EIF2AK2/PKR activity. Plays a crucial role in basal beta cell functions, such as regulation of insulin secretion.","The identified mutation leads to hyperinhibition of the transcription factor Isl-1 and, consequently, to a decrease in insulin expression.","In ADMIO1; increases transcriptional activity; increases binding to ISL1 promoter region; decreases glucose stimulated insulin secretion. The identified mutation leads to hyperinhibition of the transcription factor Isl-1 and, consequently, to a decrease in insulin expression."
1490,1490,1490,111102,Q9VPH2-E136K,MEFGLKKRARHEVKVEVASLETKYPHNVMLYHYPPTEDVHIDEFEELALERLRLLRVLDRASTRNLRVLSDEWKEIVSADLTREGLRSYLRLCSTGGSAKHEADIQTRRRDYLSHFILRLAYCRSEDLARWFVARKMELFRYKFAALSSFEVKQFLEANGFEIHPLTEAQKDEVKDGLYESTVGQSVAKIELLDFYKVPFTQVLDLVRGRRCFLKAGYAYVNTHDLVSLVGTKQQDEIEQGLQAAKTMVEDVEADERISRTLKALHNSYTGRDYTVCRDAAVPIESLDQLSKTSMPLCMRMCHEHIRANHHIKHSGRMQYGLFLKGIGVALEDSLRFWREEFTKKMDADKFTRSYEYNIYHNYGKKGSMVNYTPYSCAKIIKDVAGPGDCHGCPYKNMDQGSLKTKLSSYGLSASAIDEVMFFVSRGHYQIGCGKYFQLTHNSPVEPSINHPNNYFEESQIAMGNRQKRANGSAPPKARIRPDIKGHGDRSMLMGDDDDELWRIAETQERIMQSQKDISEAFNDDLDLTQIDY,In DNApol-alpha60-T2; pupal lethal.,,MEFGLKKRARHEVKVEVASLETKYPHNVMLYHYPPTEDVHIDEFEELALERLRLLRVLDRASTRNLRVLSDEWKEIVSADLTREGLRSYLRLCSTGGSAKHEADIQTRRRDYLSHFILRLAYCRSEDLARWFVAREMELFRYKFAALSSFEVKQFLEANGFEIHPLTEAQKDEVKDGLYESTVGQSVAKIELLDFYKVPFTQVLDLVRGRRCFLKAGYAYVNTHDLVSLVGTKQQDEIEQGLQAAKTMVEDVEADERISRTLKALHNSYTGRDYTVCRDAAVPIESLDQLSKTSMPLCMRMCHEHIRANHHIKHSGRMQYGLFLKGIGVALEDSLRFWREEFTKKMDADKFTRSYEYNIYHNYGKKGSMVNYTPYSCAKIIKDVAGPGDCHGCPYKNMDQGSLKTKLSSYGLSASAIDEVMFFVSRGHYQIGCGKYFQLTHNSPVEPSINHPNNYFEESQIAMGNRQKRANGSAPPKARIRPDIKGHGDRSMLMGDDDDELWRIAETQERIMQSQKDISEAFNDDLDLTQIDY,DNA primase large subunit,"Regulatory subunit of the DNA primase complex and component of the DNA polymerase alpha complex (also known as the alpha DNA polymerase-primase complex) which play an essential role in the initiation of DNA synthesis. During the S phase of the cell cycle, the DNA polymerase alpha complex (composed of a catalytic subunit PolA1, an accessory subunit PolA2 and two primase subunits, the catalytic subunit Prim1 and the regulatory subunit Prim2) is recruited to DNA at the replicative forks. The primase subunit of the polymerase alpha complex initiates DNA synthesis by oligomerising short RNA primers on both leading and lagging strands. These primers are initially extended by the polymerase alpha catalytic subunit and subsequently transferred to polymerase delta and polymerase epsilon for processive synthesis on the lagging and leading strand, respectively. In the primase complex, both subunits are necessary for the initial di-nucleotide formation, but the extension of the primer depends only on the catalytic subunit. Stabilizes and modulates the activity of the catalytic subunit.","The mutation in the DNAprim gene causes reduced DNAprim activity, leading to morphological defects in the eyes and cell cycle abnormalities in larval eye discs. The precise function of the 60-kD subunit encoded by DNAprim is unknown, but it is essential for DNA replication as part of DNA polymerase alpha.","In DNApol-alpha60-T2; pupal lethal. The mutation in the DNAprim gene causes reduced DNAprim activity, leading to morphological defects in the eyes and cell cycle abnormalities in larval eye discs. The precise function of the 60-kD subunit encoded by DNAprim is unknown, but it is essential for DNA replication as part of DNA polymerase alpha."
1492,1492,1492,111458,O95497-T26I,MTTQLPAYVAILLFYVSRASCQDTFIAAVYEHAAILPNATLTPVSREEALALMNRNLDILEGAITSAADQGAHIIVTPEDAIYGWNFNRDSLYPYLEDIPDPEVNWIPCNNRNRFGQTPVQERLSCLAKNNSIYVVANIGDKKPCDTSDPQCPPDGRYQYNTDVVFDSQGKLVARYHKQNLFMGENQFNVPKEPEIVTFNTTFGSFGIFTCFDILFHDPAVTLVKDFHVDTIVFPTAWMNVLPHLSAVEFHSAWAMGMRVNFLASNIHYPSKKMTGSGIYAPNSSRAFHYDMKTEEGKLLLSQLDSHPSHSAVVNWTSYASSIEALSSGNKEFKGTVFFDEFTFVKLTGVAGNYTVCQKDLCCHLSYKMSENIPNEVYALGAFDGLHTVEGRYYLQICTLLKCKTTNLNTCGDSAETASTRFEMFSLSGTFGTQYVFPEVLLSENQLAPGEFQVSTDGRLFSLKPTSGPVLTVTLFGRLYEKDWASNASSGLTAQARIIMLIVIAPIVCSLSW,,,MTTQLPAYVAILLFYVSRASCQDTFTAAVYEHAAILPNATLTPVSREEALALMNRNLDILEGAITSAADQGAHIIVTPEDAIYGWNFNRDSLYPYLEDIPDPEVNWIPCNNRNRFGQTPVQERLSCLAKNNSIYVVANIGDKKPCDTSDPQCPPDGRYQYNTDVVFDSQGKLVARYHKQNLFMGENQFNVPKEPEIVTFNTTFGSFGIFTCFDILFHDPAVTLVKDFHVDTIVFPTAWMNVLPHLSAVEFHSAWAMGMRVNFLASNIHYPSKKMTGSGIYAPNSSRAFHYDMKTEEGKLLLSQLDSHPSHSAVVNWTSYASSIEALSSGNKEFKGTVFFDEFTFVKLTGVAGNYTVCQKDLCCHLSYKMSENIPNEVYALGAFDGLHTVEGRYYLQICTLLKCKTTNLNTCGDSAETASTRFEMFSLSGTFGTQYVFPEVLLSENQLAPGEFQVSTDGRLFSLKPTSGPVLTVTLFGRLYEKDWASNASSGLTAQARIIMLIVIAPIVCSLSW,Pantetheinase,Amidohydrolase that hydrolyzes specifically one of the carboamide linkages in D-pantetheine thus recycling pantothenic acid (vitamin B5) and releasing cysteamine.,This mutation may result in altered lymphocyte migration.,This mutation may result in altered lymphocyte migration.
1497,1497,1497,112242,P42575-L57F,MAAPSAGSWSTFQHKELMAADRGRRILGVCGMHPHHQETLKKNRVVLAKQLLLSELFEHLLEKDIITLEMRELIQAKVGSFSQNVELLNLLPKRGPQAFDAFCEALRETKQGHLEDMLLTTLSGLQHVLPPLSCDYDLSLPFPVCESCPLYKKLRLSTDTVEHSLDNKDGPVCLQVKPCTPEFYQTHFQLAYRLQSRPRGLALVLSNVHFTGEKELEFRSGGDVDHSTLVTLFKLLGYDVHVLCDQTAQEMQEKLQNFAQLPAHRVTDSCIVALLSHGVEGAIYGVDGKLLQLQEVFQLFDNANCPSLQNKPKMFFIQACRGDETDRGVDQQDGKNHAGSPGCEESDAGKEKLPKMRLPTRSDMICGYACLKGTAAMRNTKRGSWYIEALAQVFSERACDMHVADMLVKVNALIKDREGYAPGTEFHRCKEMSEYCSTLCRHLYLFPGHPPT,Loss of interaction with CRADD.,,MAAPSAGSWSTFQHKELMAADRGRRILGVCGMHPHHQETLKKNRVVLAKQLLLSELLEHLLEKDIITLEMRELIQAKVGSFSQNVELLNLLPKRGPQAFDAFCEALRETKQGHLEDMLLTTLSGLQHVLPPLSCDYDLSLPFPVCESCPLYKKLRLSTDTVEHSLDNKDGPVCLQVKPCTPEFYQTHFQLAYRLQSRPRGLALVLSNVHFTGEKELEFRSGGDVDHSTLVTLFKLLGYDVHVLCDQTAQEMQEKLQNFAQLPAHRVTDSCIVALLSHGVEGAIYGVDGKLLQLQEVFQLFDNANCPSLQNKPKMFFIQACRGDETDRGVDQQDGKNHAGSPGCEESDAGKEKLPKMRLPTRSDMICGYACLKGTAAMRNTKRGSWYIEALAQVFSERACDMHVADMLVKVNALIKDREGYAPGTEFHRCKEMSEYCSTLCRHLYLFPGHPPT,Caspase-2,"Involved in the activation cascade of caspases responsible for apoptosis execution. Might function by either activating some proteins required for cell death or inactivating proteins necessary for cell survival. Associates with PIDD1 and CRADD to form the PIDDosome, a complex that activates CASP2 and triggers apoptosis in response to genotoxic stress.","The document mentions that RAIDD is an adaptor molecule with a carboxy-terminal death domain that binds to the homologous domain in RIP, a serine/threonine kinase component of the death pathway. The document does not specifically mention the functional changes caused by the mutation.","Loss of interaction with CRADD. The document mentions that RAIDD is an adaptor molecule with a carboxy-terminal death domain that binds to the homologous domain in RIP, a serine/threonine kinase component of the death pathway. The document does not specifically mention the functional changes caused by the mutation."
1504,1504,1504,112618,P0CG48-S65E,MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKEETLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGV,Phosphomimetic mutant that binds and activates PRKN.,,MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGV,Polyubiquitin-C [Cleaved into: Ubiquitin],"Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in proteotoxic stress response and cell cycle; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.",,Phosphomimetic mutant that binds and activates PRKN.
1505,1505,1505,112639,O74700-E52G,MDALNSKEQQEFQKVVEQKQMKDFMRLYSNLVERCFTDCVNDFTTSKLTNKGQTCIMKCSEKFLKHSERVGQRFQEQNAALGQGLGR,In tim9-19; impairs the import of mitochondrial carrier proteins into mitochondria.,,MDALNSKEQQEFQKVVEQKQMKDFMRLYSNLVERCFTDCVNDFTTSKLTNKEQTCIMKCSEKFLKHSERVGQRFQEQNAALGQGLGR,Mitochondrial import inner membrane translocase subunit TIM9,"Mitochondrial intermembrane chaperone that participates in the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space. Compared to TIM10, it may have a strong structural role.",,In tim9-19; impairs the import of mitochondrial carrier proteins into mitochondria.
1513,1513,1513,113084,Q14118-Y892F,MRMSVGLSLLLPLSGRTFLLLLSVVMAQSHWPSEPSEAVRDWENQLEASMHSVLSDLHEAVPTVVGIPDGTAVVGRSFRVTIPTDLIASSGDIIKVSAAGKEALPSWLHWDSQSHTLEGLPLDTDKGVHYISVSATRLGANGSHIPQTSSVFSIEVYPEDHSELQSVRTASPDPGEVVSSACAADEPVTVLTVILDADLTKMTPKQRIDLLHRMRSFSEVELHNMKLVPVVNNRLFDMSAFMAGPGNAKKVVENGALLSWKLGCSLNQNSVPDIHGVEAPAREGAMSAQLGYPVVGWHIANKKPPLPKRVRRQIHATPTPVTAIGPPTTAIQEPPSRIVPTPTSPAIAPPTETMAPPVRDPVPGKPTVTIRTRGAIIQTPTLGPIQPTRVSEAGTTVPGQIRPTMTIPGYVEPTAVATPPTTTTKKPRVSTPKPATPSTDSTTTTTRRPTKKPRTPRPVPRVTTKVSITRLETASPPTRIRTTTSGVPRGGEPNQRPELKNHIDRVDAWVGTYFEVKIPSDTFYDHEDTTTDKLKLTLKLREQQLVGEKSWVQFNSNSQLMYGLPDSSHVGKHEYFMHATDKGGLSAVDAFEIHVHRRPQGDRAPARFKAKFVGDPALVLNDIHKKIALVKKLAFAFGDRNCSTITLQNITRGSIVVEWTNNTLPLEPCPKEQIAGLSRRIAEDDGKPRPAFSNALEPDFKATSITVTGSGSCRHLQFIPVVPPRRVPSEAPPTEVPDRDPEKSSEDDVYLHTVIPAVVVAAILLIAGIIAMICYRKKRKGKLTLEDQATFIKKGVPIIFADELDDSKPPPSSSMPLILQEEKAPLPPPEYPNQSVPETTPLNQDTMGEYTPLRDEDPNAPPYQPPPPFTAPMEGKGSRPKNMTPYRSPPPFVPP,Abolishes phosphorylation. Increase in nuclear location.,,MRMSVGLSLLLPLSGRTFLLLLSVVMAQSHWPSEPSEAVRDWENQLEASMHSVLSDLHEAVPTVVGIPDGTAVVGRSFRVTIPTDLIASSGDIIKVSAAGKEALPSWLHWDSQSHTLEGLPLDTDKGVHYISVSATRLGANGSHIPQTSSVFSIEVYPEDHSELQSVRTASPDPGEVVSSACAADEPVTVLTVILDADLTKMTPKQRIDLLHRMRSFSEVELHNMKLVPVVNNRLFDMSAFMAGPGNAKKVVENGALLSWKLGCSLNQNSVPDIHGVEAPAREGAMSAQLGYPVVGWHIANKKPPLPKRVRRQIHATPTPVTAIGPPTTAIQEPPSRIVPTPTSPAIAPPTETMAPPVRDPVPGKPTVTIRTRGAIIQTPTLGPIQPTRVSEAGTTVPGQIRPTMTIPGYVEPTAVATPPTTTTKKPRVSTPKPATPSTDSTTTTTRRPTKKPRTPRPVPRVTTKVSITRLETASPPTRIRTTTSGVPRGGEPNQRPELKNHIDRVDAWVGTYFEVKIPSDTFYDHEDTTTDKLKLTLKLREQQLVGEKSWVQFNSNSQLMYGLPDSSHVGKHEYFMHATDKGGLSAVDAFEIHVHRRPQGDRAPARFKAKFVGDPALVLNDIHKKIALVKKLAFAFGDRNCSTITLQNITRGSIVVEWTNNTLPLEPCPKEQIAGLSRRIAEDDGKPRPAFSNALEPDFKATSITVTGSGSCRHLQFIPVVPPRRVPSEAPPTEVPDRDPEKSSEDDVYLHTVIPAVVVAAILLIAGIIAMICYRKKRKGKLTLEDQATFIKKGVPIIFADELDDSKPPPSSSMPLILQEEKAPLPPPEYPNQSVPETTPLNQDTMGEYTPLRDEDPNAPPYQPPPPFTAPMEGKGSRPKNMTPYRSPPPYVPP,Dystroglycan 1,"The dystroglycan complex is involved in a number of processes including laminin and basement membrane assembly, sarcolemmal stability, cell survival, peripheral nerve myelination, nodal structure, cell migration, and epithelial polarization.Extracellular peripheral glycoprotein that acts as a receptor for extracellular matrix proteins containing laminin-G domains. Receptor for laminin-2 (LAMA2) and agrin in peripheral nerve Schwann cells. Also acts as a receptor for laminin LAMA5.Transmembrane protein that plays important roles in connecting the extracellular matrix to the cytoskeleton. Acts as a cell adhesion receptor in both muscle and non-muscle tissues. Receptor for both DMD and UTRN and, through these interactions, scaffolds axin to the cytoskeleton. Also functions in cell adhesion-mediated signaling and implicated in cell polarity.(Microbial infection) Acts as a receptor for lassa virus and lymphocytic choriomeningitis virus glycoprotein and class C new-world arenaviruses. Acts as a Schwann cell receptor for Mycobacterium leprae, the causative organism of leprosy, but only in the presence of the G-domain of LAMA2.",The mutation does not cause any change in sub-cellular localization and remains at the plasma membrane.,Abolishes phosphorylation. Increase in nuclear location. The mutation does not cause any change in sub-cellular localization and remains at the plasma membrane.
1528,1528,1528,113804,P72131-S40A,MSAALERLNHLNLNHLYAFVAVAEHNSFTAAAEALGLSKALLSEQLRRLEADLGIQLLTRTTRRMTLTDRGELLFGVAQRMLGELDGALSDVRDLQGEPSGRLRITAPQDFVKWHISSVSAAFIRQFPKVQVEMLADDQFSDLVGQRIDLAVRIGWPRDSGLHASKLCDFQQVAVATPGYLAGLPPVLQPHDLARCEWIGHTRLSTPWTWTFERQRERATVQTRGRLLANNTLAVYRLVLDGAGVSVLPSFLVAREIARGRLVRLLPGWRLPQGGIYALYPSARYMPVRVRAFIESLREHLGREPFRLAQSE,Does not bind DNA.,,MSAALERLNHLNLNHLYAFVAVAEHNSFTAAAEALGLSKSLLSEQLRRLEADLGIQLLTRTTRRMTLTDRGELLFGVAQRMLGELDGALSDVRDLQGEPSGRLRITAPQDFVKWHISSVSAAFIRQFPKVQVEMLADDQFSDLVGQRIDLAVRIGWPRDSGLHASKLCDFQQVAVATPGYLAGLPPVLQPHDLARCEWIGHTRLSTPWTWTFERQRERATVQTRGRLLANNTLAVYRLVLDGAGVSVLPSFLVAREIARGRLVRLLPGWRLPQGGIYALYPSARYMPVRVRAFIESLREHLGREPFRLAQSE,HTH-type transcriptional regulator PtxR,"Plays an important role in the regulation of the production of the virulence factor exotoxin A (toxA), via positive regulation of the transcription of the toxA gene. Acts by binding directly to the toxA promoter region. Besides toxA, PtxR modulates the expression of genes that code for the QS-controlled virulence factors. It negatively regulates the expression of the rhamnolipid and pyocyanine genes, through the autoinducer synthase RhlI, and the PQS synthesis operon pqsABCDE, while it positively regulates the expression of lasB through the autoinducer synthase LasI. Also positively regulates the expression of the exotoxin A regulatory protein (toxR or regA).In addition, is involved in the positive regulation of glucose metabolism via the regulation of the expression of the kgu and gad operons. Acts by binding directly to the promoter region of the kgu and gad operons.","In all Pseudomonas sp. , PtxS with 2-ketogluconate is the regulator of the gluconate degradation pathway and controls expression from its own promoter and also from the P(gad) and P(kgu) for the catabolic operons.","Does not bind DNA. In all Pseudomonas sp. , PtxS with 2-ketogluconate is the regulator of the gluconate degradation pathway and controls expression from its own promoter and also from the P(gad) and P(kgu) for the catabolic operons."
1531,1531,1531,114161,P0DJJ0-Q250R,MTSPAKFKKDKEIIAEYDTQVKEIRAQLTEQMKCLDQQCELRVQLLQDLQDFFRKKAEIEMDYSRNLEKLAEHFLAKTRSTKDQQFKKDQNVLSPVNCWNLLLNQVKWESRDHTTLSDIYLNNIIPRFVQVSEDSGRLFKKSKEVGQQLQDDLMKVLNELYSVMKTYHMYNADSISAQSKLKEAEKQEEKQIGKSVKQEDRQTPCSPDSTANVRIEEKHVRRSSVKKIEKMKEKHQAKYTENKLKAIKARNEYLLALEATNASVFKYYIHDLSDLIDQCCDLGYHASLNRALRTFLSAELNLEQSKHEGLDAIENAVENLDATSDKQRLMEMYNNVFCPPMKFEFQPHMGDMASQLCAQQPVQSELVQRCQQLQSRLSTLKIENEEVKKTMEATLQTIQDIVTVEDFDVSDCFQYSNSMESVKSTVSETFMSKPSIAKRRANQQETEQFYFTVRECYGF,"Does not improve solubility; when associated with R-73, R-108, R-205 and R-235.",,MTSPAKFKKDKEIIAEYDTQVKEIRAQLTEQMKCLDQQCELRVQLLQDLQDFFRKKAEIEMDYSRNLEKLAEHFLAKTRSTKDQQFKKDQNVLSPVNCWNLLLNQVKWESRDHTTLSDIYLNNIIPRFVQVSEDSGRLFKKSKEVGQQLQDDLMKVLNELYSVMKTYHMYNADSISAQSKLKEAEKQEEKQIGKSVKQEDRQTPCSPDSTANVRIEEKHVRRSSVKKIEKMKEKHQAKYTENKLKAIKAQNEYLLALEATNASVFKYYIHDLSDLIDQCCDLGYHASLNRALRTFLSAELNLEQSKHEGLDAIENAVENLDATSDKQRLMEMYNNVFCPPMKFEFQPHMGDMASQLCAQQPVQSELVQRCQQLQSRLSTLKIENEEVKKTMEATLQTIQDIVTVEDFDVSDCFQYSNSMESVKSTVSETFMSKPSIAKRRANQQETEQFYFTVRECYGF,SLIT-ROBO Rho GTPase-activating protein 2C,"Human-specific protein that acts as a key modifier of cortical connectivity in the human brain. Acts by inhibiting the functions of ancestral paralog SRGAP2/SRGAP2A, a postsynaptic protein that regulates excitatory and inhibitory synapse maturation and density in cortical pyramidal neurons. SRGAP2C is unstable but is able to heterodimerize with SRGAP2/SRGAP2A, thereby reducing SRGAP2/SRGAP2A levels through proteasome-dependent degradation. Inhibition of SRGAP2/SRGAP2A by SRGAP2C leads to an increase in synaptic density and protracted synaptic maturation of both excitatory and inhibitory synapses. Modifies cortical circuit connectivity by increasing the number of local and long-range cortical inputs received by layer 2/3 pyramidal neurons. Also able to increase the probability of sensory-evoked responses by layer 2/3 pyramidal neurons.",,"Does not improve solubility; when associated with R-73, R-108, R-205 and R-235."
1541,1541,1541,114949,Q4VGL6-C419R,MPVQAPQWTDFLSCPICTQTFDETIRKPISLGCGHTVCKMCLNKLHRKACPFDQTTINTDIELLPVNSALLQLVGAQIPEQQPITLCSGVEDTKHYEEAKKCVEELALYLKPLSSARGVGLNSTTQSVLSRPMQRKLVTLVHCQLVEEEGRIRAMRAARSLGERTVTELILQHQNPQQLSSNLWAAVRARGCQFLGPAMQEEALKLVLLALEDGSALSRKVLVLFVVQRLEPRFPQASKTSIGHVVQLLYRASCFKVTKRDEDSSLMQLKEEFRTYEALRREHDSQIVQIAMEAGLRIAPDQWSSLLYGDQSHKSHMQSIIDKLQTPASFAQSVQELTIALQRTGDPANLNRLRPHLELLANIDPSPDAPPPTWEQLENGLVAVRTVVHGLVDYIQNHSKKGADQQQPPQHSKYKTYMRRDMKQRGGCPRGASCTFAHSQEELEKFRKMNKRLVPRRPLSASLGQLNEVGLPSAPILSDESAVDLSNRKPPALPNGIASSGSTVTQLIPRGTDPSFDSSLKPVKLDHLSSSAPGSPPDLLESAPKSISALPVNPHPVPPRGPTDLPPMPVTKPIQMVPRGSQLYPAQQADVYYQDPRGSAPAFETAPYQQGMYYTPPPCVSRFVRPPPSAPEPGPPYLDHYSPYLQDRVINSQYGTQPQQYPPMYPAHYDGRRVYPAQSYTREEMFRESPIPIDIPSAAVPSYVPESRERYQQVEGYYPVAPHPAQIRPSYPRDPPYSRLPPPQPHPSLDELHRRRKEIMAQLEERKVISPPPFAPSPTLPPAFHPEEFLDEDLKVAGKYKANDYSQYSPWSCDTIGSYIGTKDAKPKDVVAAGSVEMMNVESKGTREQRLDLQRRAVETSDDDLIPFGDRPTVSRFGAISRTSKTLYQGAGPLQAIAPQGAPTKSINISDYSAYGAHGGWGDSPYSPHANIPPQGHFIEREKMSMAEVASHGKPLLSAEREQLRLELQQLNHQISQQTQLRGLEAVSNRLVLQREVNTLASQPQPPQLPPKWPGMISSEQLSL,No effect on RNA-binding.,,MPVQAPQWTDFLSCPICTQTFDETIRKPISLGCGHTVCKMCLNKLHRKACPFDQTTINTDIELLPVNSALLQLVGAQIPEQQPITLCSGVEDTKHYEEAKKCVEELALYLKPLSSARGVGLNSTTQSVLSRPMQRKLVTLVHCQLVEEEGRIRAMRAARSLGERTVTELILQHQNPQQLSSNLWAAVRARGCQFLGPAMQEEALKLVLLALEDGSALSRKVLVLFVVQRLEPRFPQASKTSIGHVVQLLYRASCFKVTKRDEDSSLMQLKEEFRTYEALRREHDSQIVQIAMEAGLRIAPDQWSSLLYGDQSHKSHMQSIIDKLQTPASFAQSVQELTIALQRTGDPANLNRLRPHLELLANIDPSPDAPPPTWEQLENGLVAVRTVVHGLVDYIQNHSKKGADQQQPPQHSKYKTYMCRDMKQRGGCPRGASCTFAHSQEELEKFRKMNKRLVPRRPLSASLGQLNEVGLPSAPILSDESAVDLSNRKPPALPNGIASSGSTVTQLIPRGTDPSFDSSLKPVKLDHLSSSAPGSPPDLLESAPKSISALPVNPHPVPPRGPTDLPPMPVTKPIQMVPRGSQLYPAQQADVYYQDPRGSAPAFETAPYQQGMYYTPPPCVSRFVRPPPSAPEPGPPYLDHYSPYLQDRVINSQYGTQPQQYPPMYPAHYDGRRVYPAQSYTREEMFRESPIPIDIPSAAVPSYVPESRERYQQVEGYYPVAPHPAQIRPSYPRDPPYSRLPPPQPHPSLDELHRRRKEIMAQLEERKVISPPPFAPSPTLPPAFHPEEFLDEDLKVAGKYKANDYSQYSPWSCDTIGSYIGTKDAKPKDVVAAGSVEMMNVESKGTREQRLDLQRRAVETSDDDLIPFGDRPTVSRFGAISRTSKTLYQGAGPLQAIAPQGAPTKSINISDYSAYGAHGGWGDSPYSPHANIPPQGHFIEREKMSMAEVASHGKPLLSAEREQLRLELQQLNHQISQQTQLRGLEAVSNRLVLQREVNTLASQPQPPQLPPKWPGMISSEQLSL,Roquin-1,"Post-transcriptional repressor of mRNAs containing a conserved stem loop motif, called constitutive decay element (CDE), which is often located in the 3'-UTR, as in HMGXB3, ICOS, IER3, NFKBID, NFKBIZ, PPP1R10, TNF, TNFRSF4 and in many more mRNAs. Cleaves translationally inactive mRNAs harboring a stem-loop (SL), often located in their 3'-UTRs, during the early phase of inflammation in a helicase UPF1-independent manner. Binds to CDE and promotes mRNA deadenylation and degradation. This process does not involve miRNAs. In follicular helper T (Tfh) cells, represses of ICOS and TNFRSF4/Ox40 expression, thus preventing spontaneous Tfh cell differentiation, germinal center B-cell differentiation in the absence of immunization and autoimmunity. In resting or LPS-stimulated macrophages, controls inflammation by suppressing TNF expression. Also recognizes CDE in its own mRNA and in that of paralogous RC3H2, possibly leading to feedback loop regulation. Inhibits cooperatively with ZC3H12A the differentiation of helper T cells Th17 in lungs. They repress target mRNA encoding the Th17 cell-promoting factors IL6, ICOS, REL, IRF4, NFKBID and NFKBIZ. The cooperation requires RNA-binding by RC3H1 and the nuclease activity of ZC3H12A. Recognizes and binds mRNAs containing a hexaloop stem-loop motif, called alternative decay element (ADE). Together with ZC3H12A, destabilizes TNFRSF4/OX40 mRNA by binding to the conserved stem loop structure in its 3'UTR. Able to interact with double-stranded RNA. miRNA-binding protein that regulates microRNA homeostasis. Enhances DICER-mediated processing of pre-MIR146a but reduces mature MIR146a levels through an increase of 3' end uridylation. Both inhibits ICOS mRNA expression and they may act together to exert the suppression. Acts as a ubiquitin E3 ligase. Pairs with E2 enzymes UBE2A, UBE2B, UBE2D2, UBE2F, UBE2G1, UBE2G2 and UBE2L3 and produces polyubiquitin chains. Shows the strongest activity when paired with UBE2N:UBE2V1 or UBE2N:UBE2V2 E2 complexes and generate both short and long polyubiquitin chains.",,No effect on RNA-binding.
1556,1556,1556,115849,Q07279-S170A,MPPCPPQQNRNRLSQLPVGELGEMELTWQEIMSITELQGLNVPSETSFEPQAPTPYPGPLPPPTYCPCSIHPDAGFSLPPPSYELPASTPHVPELPYSYGNVAIPVSKPLTLSGLLNEPLPDHLALLDIGLPVGQPKPQEDPESDSGLSLNYSDAESLELEGMEAGRRRAEYVDMYPVEYPYSLMPNSLAHPNYTLPPTETPLALESSSGPVRAKPAVRGEAGSRDERRALAMKIPFPTDKIVNLPVDDFNELLAQYPLTESQLALVRDIRRRGKNKVAAQNCRKRKLETIVQLERELERLSSERERLLRARGEADRTLEVMRQQLAELYHDIFQHLRDESGNSYSPEEYVLQQAADGAIFLVPRGTKMEATD,Abolishes phosphorylation by PKA. No effect on ability to bind DNA nor on transactivation activity.,,MPPCPPQQNRNRLSQLPVGELGEMELTWQEIMSITELQGLNVPSETSFEPQAPTPYPGPLPPPTYCPCSIHPDAGFSLPPPSYELPASTPHVPELPYSYGNVAIPVSKPLTLSGLLNEPLPDHLALLDIGLPVGQPKPQEDPESDSGLSLNYSDAESLELEGMEAGRRRSEYVDMYPVEYPYSLMPNSLAHPNYTLPPTETPLALESSSGPVRAKPAVRGEAGSRDERRALAMKIPFPTDKIVNLPVDDFNELLAQYPLTESQLALVRDIRRRGKNKVAAQNCRKRKLETIVQLERELERLSSERERLLRARGEADRTLEVMRQQLAELYHDIFQHLRDESGNSYSPEEYVLQQAADGAIFLVPRGTKMEATD,Transcription factor NF-E2 45 kDa subunit,Component of the NF-E2 complex essential for regulating erythroid and megakaryocytic maturation and differentiation. Binds to the hypersensitive site 2 (HS2) of the beta-globin control region (LCR). This subunit (NFE2) recognizes the TCAT/C sequence of the AP-1-like core palindrome present in a number of erythroid and megakaryocytic gene promoters. Requires MAFK or other small MAF proteins for binding to the NF-E2 motif. May play a role in all aspects of hemoglobin production from globin and heme synthesis to procurement of iron.,"A substitution for S(169) resulted in a protein that was no longer phosphorylated by A-kinase in vitro or in vivo. The mutant protein formed NF-E2 complexes that bound to DNA with the same affinity as wild-type p45 and functioned normally to restore beta-globin gene expression in a p45-deficient MEL cell line. Transactivation properties of the (S (169)--> A) mutant p45 were also indistinguishable from wild-type p45 when Gal4-p45 fusion constructs were tested with a Gal4-dependent reporter gene. Transactivation of the reporter by both mutant and wild-type p45 was significantly enhanced when A-kinase was activated by membrane-permeable cAMP analogs or when cells were cotransfected with the catalytic subunit of A-kinase. Stimulation of p45 transactivation by A-kinase required only the N-terminal transactivation domain of p45, suggesting that A-kinase regulates the interaction of p45 with downstream effectors.","Abolishes phosphorylation by PKA. No effect on ability to bind DNA nor on transactivation activity. A substitution for S(169) resulted in a protein that was no longer phosphorylated by A-kinase in vitro or in vivo. The mutant protein formed NF-E2 complexes that bound to DNA with the same affinity as wild-type p45 and functioned normally to restore beta-globin gene expression in a p45-deficient MEL cell line. Transactivation properties of the (S (169)--> A) mutant p45 were also indistinguishable from wild-type p45 when Gal4-p45 fusion constructs were tested with a Gal4-dependent reporter gene. Transactivation of the reporter by both mutant and wild-type p45 was significantly enhanced when A-kinase was activated by membrane-permeable cAMP analogs or when cells were cotransfected with the catalytic subunit of A-kinase. Stimulation of p45 transactivation by A-kinase required only the N-terminal transactivation domain of p45, suggesting that A-kinase regulates the interaction of p45 with downstream effectors."
1560,1560,1560,116146,Q95RV2-S154T,MLLLLCVNMSGTQMSAFLRKYLADEDKKIRAQFKESDPNNKLILWMHEKTRITEEDLARPYTEDEVKELCLRTKVKVDMTAWNCLWEAKKRFEAKGRFVNKSERFINRMYMKAVRRKMVQPYPEEFVAQRREIVAAETKKQNISRLDRWQKKKTQNLSAPESSPDAHASSNDAVQSHEDQANTNLSSLSQMNFQVEAMAPPGVSSSDLSGIGDDEDEQQQSGFQDENINRPETEINENSVRCDPINLGRMRTGCINSQANNSFRNTESDPDYYMFGTQLSTLVRPTSTQEPDDQVNCPETEMNESWVRCDQINSESLSIGPSIDSEGTITFQNTESEPIDVTSIA,"In strain: Australia 2, Kenya 38, Kenya 43, Peru and USA 3.",,MLLLLCVNMSGTQMSAFLRKYLADEDKKIRAQFKESDPNNKLILWMHEKTRITEEDLARPYTEDEVKELCLRTKVKVDMTAWNCLWEAKKRFEAKGRFVNKSERFINRMYMKAVRRKMVQPYPEEFVAQRREIVAAETKKQNISRLDRWQKKKSQNLSAPESSPDAHASSNDAVQSHEDQANTNLSSLSQMNFQVEAMAPPGVSSSDLSGIGDDEDEQQQSGFQDENINRPETEINENSVRCDPINLGRMRTGCINSQANNSFRNTESDPDYYMFGTQLSTLVRPTSTQEPDDQVNCPETEMNESWVRCDQINSESLSIGPSIDSEGTITFQNTESEPIDVTSIA,Telomere-binding protein cav,Binds to chromosome ends in a sequence-dependent manner and is required for telomere capping.,,"In strain: Australia 2, Kenya 38, Kenya 43, Peru and USA 3."
1573,1573,1573,117399,Q04636-Q308D,MSTDFDRIYLNQSKFSGRFRIADSGLGWKISTSGGSAANQARKPFLLPATELSTVQWSRGCRGYDLKINTKNQGVIQLDGFSQDDYNLIKNDFHRRFNIQVEQREHSLRGWNWGKTDLARNEMVFALNGKPTFEIPYARINNTNLTSKNEVGIEFNIQDEEYQPAGDELVEMRFYIPGVIQTNVDENMTKKEESSNEVVPKKEDGAEGEDVQMAVEEKSMAEAFYEELKEKADIGEVAGDAIVSFQDVFFTTPRGRYDIDIYKNSIRLRGKTYEYKLQHRQIQRIVSLPKADDIHHLLVLAIEPPLRDGQTTYPFLVLQFQKDEETEVQLNLEDEDYEENYKDKLKKQYDAKTHIVLSHVLKGLTDRRVIVPGEYKSKYDQCAVSCSFKANEGYLYPLDNAFFFLTKPTLYIPFSDVSMVNISRAGQTSTSSRTFDLEVVLRSNRGSTTFANISKEEQQLLEQFLKSKNLRVKNEDREVQERLQTALGSDSDEEDINMGSAGEDDESVDEDFQVSSDNDADEVAEEFDSDAALSDAEGGSDEERPSKKPKVE,No effect.,,MSTDFDRIYLNQSKFSGRFRIADSGLGWKISTSGGSAANQARKPFLLPATELSTVQWSRGCRGYDLKINTKNQGVIQLDGFSQDDYNLIKNDFHRRFNIQVEQREHSLRGWNWGKTDLARNEMVFALNGKPTFEIPYARINNTNLTSKNEVGIEFNIQDEEYQPAGDELVEMRFYIPGVIQTNVDENMTKKEESSNEVVPKKEDGAEGEDVQMAVEEKSMAEAFYEELKEKADIGEVAGDAIVSFQDVFFTTPRGRYDIDIYKNSIRLRGKTYEYKLQHRQIQRIVSLPKADDIHHLLVLAIEPPLRQGQTTYPFLVLQFQKDEETEVQLNLEDEDYEENYKDKLKKQYDAKTHIVLSHVLKGLTDRRVIVPGEYKSKYDQCAVSCSFKANEGYLYPLDNAFFFLTKPTLYIPFSDVSMVNISRAGQTSTSSRTFDLEVVLRSNRGSTTFANISKEEQQLLEQFLKSKNLRVKNEDREVQERLQTALGSDSDEEDINMGSAGEDDESVDEDFQVSSDNDADEVAEEFDSDAALSDAEGGSDEERPSKKPKVE,FACT complex subunit POB3,"Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II. Transcription elongation is promoted by the repression of transcription initiation from cryptic sites. Also acts in establishing transcription initiation complexes and promotes SPT15/TBP-binding to a TATA box. Together with replication factor-A protein (RPA), FACT may play a role in nucleosome deposition during DNA replication.",A mutation within a conserved surface cluster in this domain causes a defect in DNA replication that is suppressed by mutation of replication protein A (RPA). The nucleosome reorganizer yFACT therefore interacts in a physiologically important way with the central single-strand DNA (ssDNA) binding factor RPA to promote a step in DNA replication.,No effect. A mutation within a conserved surface cluster in this domain causes a defect in DNA replication that is suppressed by mutation of replication protein A (RPA). The nucleosome reorganizer yFACT therefore interacts in a physiologically important way with the central single-strand DNA (ssDNA) binding factor RPA to promote a step in DNA replication.
1613,1613,1613,120604,P28161-T210W,MPMTLGYWNIRGLAHSIRLLLEYTDSSYEEKKYTMGDAPDYDRSQWLNEKFKLGLDFPNLPYLIDGTHKITQSNAILRYIARKHNLCGESEKEQIREDILENQFMDSRMQLAKLCYDPDFEKLKPEYLQALPEMLKLYSQFLGKQPWFLGDKITFVDFIAYDVLERNQVFEPSCLDAFPNLKDFISRFEGLEKISAYMKSSRFLPRPVFWKMAVWGNK,Reduced enzyme activity.,,MPMTLGYWNIRGLAHSIRLLLEYTDSSYEEKKYTMGDAPDYDRSQWLNEKFKLGLDFPNLPYLIDGTHKITQSNAILRYIARKHNLCGESEKEQIREDILENQFMDSRMQLAKLCYDPDFEKLKPEYLQALPEMLKLYSQFLGKQPWFLGDKITFVDFIAYDVLERNQVFEPSCLDAFPNLKDFISRFEGLEKISAYMKSSRFLPRPVFTKMAVWGNK,Glutathione S-transferase Mu 2,Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Participates in the formation of novel hepoxilin regioisomers.,"Mutations of residue in human glutathione transferase M2-2 can differentially change the enzyme's substrate-activity profile with alternative substrates and enable or disable dissimilar chemical reactions. Crystal structures demonstrate that activity with epoxides is enabled through removal of steric hindrance from a methyl group, whereas activities with an orthoquinone and a nitroso donor are maintained in the variant enzymes.","Reduced enzyme activity. Mutations of residue in human glutathione transferase M2-2 can differentially change the enzyme's substrate-activity profile with alternative substrates and enable or disable dissimilar chemical reactions. Crystal structures demonstrate that activity with epoxides is enabled through removal of steric hindrance from a methyl group, whereas activities with an orthoquinone and a nitroso donor are maintained in the variant enzymes."
1626,1626,1626,121586,Q13009-K912E,MGNAESQHVEHEFYGEKHASLGRKHTSRSLRLSHKTRRTRHASSGKVIHRNSEVSTRSSSTPSIPQSLAENGLEPFSQDGTLEDFGSPIWVDRVDMGLRPVSYTDSSVTPSVDSSIVLTAASVQSMPDTEESRLYGDDATYLAEGGRRQHSYTSNGPTFMETASFKKKRSKSADIWREDSLEFSLSDLSQEHLTSNEEILGSAEEKDCEEARGMETRASPRQLSTCQRANSLGDLYAQKNSGVTANGGPGSKFAGYCRNLVSDIPNLANHKMPPAAAEETPPYSNYNTLPCRKSHCLSEGATNPQISHSNSMQGRRAKTTQDVNAGEGSEFADSGIEGATTDTDLLSRRSNATNSSYSPTTGRAFVGSDSGSSSTGDAARQGVYENFRRELEMSTTNSESLEEAGSAHSDEQSSGTLSSPGQSDILLTAAQGTVRKAGALAVKNFLVHKKNKKVESATRRKWKHYWVSLKGCTLFFYESDGRSGIDHNSIPKHAVWVENSIVQAVPEHPKKDFVFCLSNSLGDAFLFQTTSQTELENWITAIHSACATAVARHHHKEDTLRLLKSEIKKLEQKIDMDEKMKKMGEMQLSSVTDSKKKKTILDQIFVWEQNLEQFQMDLFRFRCYLASLQGGELPNPKRLLAFASRPTKVAMGRLGIFSVSSFHALVAARTGETGVRRRTQAMSRSASKRRSRFSSLWGLDTTSKKKQGRPSINQVFGEGTEAVKKSLEGIFDDIVPDGKREKEVVLPNVHQHNPDCDIWVHEYFTPSWFCLPNNQPALTVVRPGDTARDTLELICKTHQLDHSAHYLRLKFLIENKMQLYVPQPEEDIYELLYKEIEICPKVTQSIHIEKSDTAADTYGFSLSSVEEDGIRRLYVNSVKETGLASKKGLKAGDEILEINNRAADALNSSMLEDFLSQPSLGLLVRTYPELEEGVELLESPPHRVDGPADLGESPLAFLTSNPGHSLCSEQGSSAETAPEETEGPDLESSDETDHSSKSTEQVAAFCRSLHEMNPSDQSPSPQDS,Strongly reduces affinity for SDC1.,,MGNAESQHVEHEFYGEKHASLGRKHTSRSLRLSHKTRRTRHASSGKVIHRNSEVSTRSSSTPSIPQSLAENGLEPFSQDGTLEDFGSPIWVDRVDMGLRPVSYTDSSVTPSVDSSIVLTAASVQSMPDTEESRLYGDDATYLAEGGRRQHSYTSNGPTFMETASFKKKRSKSADIWREDSLEFSLSDLSQEHLTSNEEILGSAEEKDCEEARGMETRASPRQLSTCQRANSLGDLYAQKNSGVTANGGPGSKFAGYCRNLVSDIPNLANHKMPPAAAEETPPYSNYNTLPCRKSHCLSEGATNPQISHSNSMQGRRAKTTQDVNAGEGSEFADSGIEGATTDTDLLSRRSNATNSSYSPTTGRAFVGSDSGSSSTGDAARQGVYENFRRELEMSTTNSESLEEAGSAHSDEQSSGTLSSPGQSDILLTAAQGTVRKAGALAVKNFLVHKKNKKVESATRRKWKHYWVSLKGCTLFFYESDGRSGIDHNSIPKHAVWVENSIVQAVPEHPKKDFVFCLSNSLGDAFLFQTTSQTELENWITAIHSACATAVARHHHKEDTLRLLKSEIKKLEQKIDMDEKMKKMGEMQLSSVTDSKKKKTILDQIFVWEQNLEQFQMDLFRFRCYLASLQGGELPNPKRLLAFASRPTKVAMGRLGIFSVSSFHALVAARTGETGVRRRTQAMSRSASKRRSRFSSLWGLDTTSKKKQGRPSINQVFGEGTEAVKKSLEGIFDDIVPDGKREKEVVLPNVHQHNPDCDIWVHEYFTPSWFCLPNNQPALTVVRPGDTARDTLELICKTHQLDHSAHYLRLKFLIENKMQLYVPQPEEDIYELLYKEIEICPKVTQSIHIEKSDTAADTYGFSLSSVEEDGIRRLYVNSVKETGLASKKGLKAGDEILEINNRAADALNSSMLKDFLSQPSLGLLVRTYPELEEGVELLESPPHRVDGPADLGESPLAFLTSNPGHSLCSEQGSSAETAPEETEGPDLESSDETDHSSKSTEQVAAFCRSLHEMNPSDQSPSPQDS,Rho guanine nucleotide exchange factor TIAM1,"Guanyl-nucleotide exchange factor that activates RHO-like proteins and connects extracellular signals to cytoskeletal activities. Activates RAC1, CDC42, and to a lesser extent RHOA and their downstream signaling to regulate processes like cell adhesion and cell migration.",,Strongly reduces affinity for SDC1.
1632,1632,1632,121896,Q6QNK2-L808T,MEKLLRLCCWYSWLLLFYYNFQVRGVYSRSQDHPGFQVLASASHYWPLENVDGIHELQDTTGDIVEGKVNKGIYLKEEKGVTLLYYGRYNSSCISKPEQCGPEGVTFSFFWKTQGEQSRPIPSAYGGQVISNGFKVCSSGGRGSVELYTRDNSMTWEASFSPPGPYWTHVLFTWKSKEGLKVYVNGTLSTSDPSGKVSRDYGESNVNLVIGSEQDQAKCYENGAFDEFIIWERALTPDEIAMYFTAAIGKHALLSSTLPSLFMTSTASPVMPTDAYHPIITNLTEERKTFQSPGVILSYLQNVSLSLPSKSLSEQTALNLTKTFLKAVGEILLLPGWIALSEDSAVVLSLIDTIDTVMGHVSSNLHGSTPQVTVEGSSAMAEFSVAKILPKTVNSSHYRFPAHGQSFIQIPHEAFHRHAWSTVVGLLYHSMHYYLNNIWPAHTKIAEAMHHQDCLLFATSHLISLEVSPPPTLSQNLSGSPLITVHLKHRLTRKQHSEATNSSNRVFVYCAFLDFSSGEGVWSNHGCALTRGNLTYSVCRCTHLTNFAILMQVVPLELARGHQVALSSISYVGCSLSVLCLVATLVTFAVLSSVSTIRNQRYHIHANLSFAVLVAQVLLLISFRLEPGTTPCQVMAVLLHYFFLSAFAWMLVEGLHLYSMVIKVFGSEDSKHRYYYGMGWGFPLLICIISLSFAMDSYGTSNNCWLSLASGAIWAFVAPALFVIVVNIGILIAVTRVISQISADNYKIHGDPSAFKLTAKAVAVLLPILGTSWVFGVLAVNGCAVVFQYMFATLNSLQGLFIFLFHCTLNSEVRAAFKHKTKVWSLTSSSARTSNAKPFHSDLMNGTRPGMASTKLSPWDKSSHSAHRVDLSAV,Does not affect membrane trafficking. Abolishes receptor activity.,,MEKLLRLCCWYSWLLLFYYNFQVRGVYSRSQDHPGFQVLASASHYWPLENVDGIHELQDTTGDIVEGKVNKGIYLKEEKGVTLLYYGRYNSSCISKPEQCGPEGVTFSFFWKTQGEQSRPIPSAYGGQVISNGFKVCSSGGRGSVELYTRDNSMTWEASFSPPGPYWTHVLFTWKSKEGLKVYVNGTLSTSDPSGKVSRDYGESNVNLVIGSEQDQAKCYENGAFDEFIIWERALTPDEIAMYFTAAIGKHALLSSTLPSLFMTSTASPVMPTDAYHPIITNLTEERKTFQSPGVILSYLQNVSLSLPSKSLSEQTALNLTKTFLKAVGEILLLPGWIALSEDSAVVLSLIDTIDTVMGHVSSNLHGSTPQVTVEGSSAMAEFSVAKILPKTVNSSHYRFPAHGQSFIQIPHEAFHRHAWSTVVGLLYHSMHYYLNNIWPAHTKIAEAMHHQDCLLFATSHLISLEVSPPPTLSQNLSGSPLITVHLKHRLTRKQHSEATNSSNRVFVYCAFLDFSSGEGVWSNHGCALTRGNLTYSVCRCTHLTNFAILMQVVPLELARGHQVALSSISYVGCSLSVLCLVATLVTFAVLSSVSTIRNQRYHIHANLSFAVLVAQVLLLISFRLEPGTTPCQVMAVLLHYFFLSAFAWMLVEGLHLYSMVIKVFGSEDSKHRYYYGMGWGFPLLICIISLSFAMDSYGTSNNCWLSLASGAIWAFVAPALFVIVVNIGILIAVTRVISQISADNYKIHGDPSAFKLTAKAVAVLLPILGTSWVFGVLAVNGCAVVFQYMFATLNSLQGLFIFLFHCLLNSEVRAAFKHKTKVWSLTSSSARTSNAKPFHSDLMNGTRPGMASTKLSPWDKSSHSAHRVDLSAV,Adhesion G-protein coupled receptor D1,Orphan receptor. Signals via G(s)-alpha family of G-proteins. Has protumorigenic function especially in glioblastoma.,,Does not affect membrane trafficking. Abolishes receptor activity.
1634,1634,1634,122178,Q9Y6H8-V44M,MGDWSFLGRLLENAQEHSTVIGKVWLTVLFIFRILVLGAAAEDMWGDEQSDFTCNTQQPGCENVCYDRAFPISHIRFWALQIIFVSTPTLIYLGHVLHIVRMEEKKKEREEEEQLKRESPSPKEPPQDNPSSRDDRGRVRMAGALLRTYVFNIIFKTLFEVGFIAGQYFLYGFELKPLYRCDRWPCPNTVDCFISRPTEKTIFIIFMLAVACASLLLNMLEIYHLGWKKLKQGVTSRLGPDASEAPLGTADPPPLPPSSRPPAVAIGFPPYYAHTAAPLGQARAVGYPGAPPPAADFKLLALTEARGKGQSAKLYNGHHHLLMTEQNWANQAAERQPPALKAYPAASTPAAPSPVGSSSPPLAHEAEAGAAPLLLDGSGSSLEGSALAGTPEEEEQAVTTAAQMHQPPLPLGDPGRASKASRASSGRARPEDLAI,In CTRCT14; nuclear cataract.,,MGDWSFLGRLLENAQEHSTVIGKVWLTVLFIFRILVLGAAAEDVWGDEQSDFTCNTQQPGCENVCYDRAFPISHIRFWALQIIFVSTPTLIYLGHVLHIVRMEEKKKEREEEEQLKRESPSPKEPPQDNPSSRDDRGRVRMAGALLRTYVFNIIFKTLFEVGFIAGQYFLYGFELKPLYRCDRWPCPNTVDCFISRPTEKTIFIIFMLAVACASLLLNMLEIYHLGWKKLKQGVTSRLGPDASEAPLGTADPPPLPPSSRPPAVAIGFPPYYAHTAAPLGQARAVGYPGAPPPAADFKLLALTEARGKGQSAKLYNGHHHLLMTEQNWANQAAERQPPALKAYPAASTPAAPSPVGSSSPPLAHEAEAGAAPLLLDGSGSSLEGSALAGTPEEEEQAVTTAAQMHQPPLPLGDPGRASKASRASSGRARPEDLAI,Gap junction alpha-3 protein,"Structural component of lens fiber gap junctions. Gap junctions are dodecameric channels that connect the cytoplasm of adjoining cells. They are formed by the docking of two hexameric hemichannels, one from each cell membrane. Small molecules and ions diffuse from one cell to a neighboring cell via the central pore.",,In CTRCT14; nuclear cataract.
1636,1636,1636,122358,O76090-T241N,MTITYTSQVANARLGSFSRLLLCWRGSIYKLLYGEFLIFLLCYYIIRFIYRLALTEEQQLMFEKLTLYCDSYIQLIPISFVLGFYVTLVVTRWWNQYENLPWPDRLMSLVSGFVEGKDEQGRLLRRTLIRYANLGNVLILRSVSTAVYKRFPSAQHLVQAGFMTPAEHKQLEKLSLPHNMFWVPWVWFANLSMKAWLGGRIRDPILLQSLLNEMNTLRTQCGHLYAYDWISIPLVYTQVVNVAVYSFFLTCLVGRQFLNPAKAYPGHELDLVVPVFTFLQFFFYVGWLKVAEQLINPFGEDDDDFETNWIVDRNLQVSLLAVDEMHQDLPRMEPDMYWNKPEPQPPYTAASAQFRRASFMGSTFNISLNKEEMEFQPNQEDEEDAHAGIIGRFLGLQSHDHHPPRANSRTKLLWPKRESLLHEGLPKNHKAAKQNVRGQEDNKAWKLKAVDAFKSAPLYQRPGYYSAPQTPLSPTPMFFPLEPSAPSKLHSVTGIDTKDKSLKTVSSGAKKSFELLSESDGALMEHPEVSQVRRKTVEFNLTDMPEIPENHLKEPLEQSPTNIHTTLKDHMDPYWALENRDEAHS,In VMD2.,,MTITYTSQVANARLGSFSRLLLCWRGSIYKLLYGEFLIFLLCYYIIRFIYRLALTEEQQLMFEKLTLYCDSYIQLIPISFVLGFYVTLVVTRWWNQYENLPWPDRLMSLVSGFVEGKDEQGRLLRRTLIRYANLGNVLILRSVSTAVYKRFPSAQHLVQAGFMTPAEHKQLEKLSLPHNMFWVPWVWFANLSMKAWLGGRIRDPILLQSLLNEMNTLRTQCGHLYAYDWISIPLVYTQVVTVAVYSFFLTCLVGRQFLNPAKAYPGHELDLVVPVFTFLQFFFYVGWLKVAEQLINPFGEDDDDFETNWIVDRNLQVSLLAVDEMHQDLPRMEPDMYWNKPEPQPPYTAASAQFRRASFMGSTFNISLNKEEMEFQPNQEDEEDAHAGIIGRFLGLQSHDHHPPRANSRTKLLWPKRESLLHEGLPKNHKAAKQNVRGQEDNKAWKLKAVDAFKSAPLYQRPGYYSAPQTPLSPTPMFFPLEPSAPSKLHSVTGIDTKDKSLKTVSSGAKKSFELLSESDGALMEHPEVSQVRRKTVEFNLTDMPEIPENHLKEPLEQSPTNIHTTLKDHMDPYWALENRDEAHS,Bestrophin-1,Forms calcium-sensitive chloride channels. Highly permeable to bicarbonate.,The mutation results in an amino acid change in the VMD2 gene encoding besrtophin.,In VMD2. The mutation results in an amino acid change in the VMD2 gene encoding besrtophin.
1638,1638,1638,122567,Q14683-R895G,MGFLKLIEIENFKSYKGRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVLGEKTSNLRVKTLRDLIHGAPVGKPAANRAFVSMVYSEEGAEDRTFARVIVGGSSEYKINNKVVQLHEYSEELEKLGILIKARNFLVFQGAVESIAMKNPKERTALFEEISRSGELAQEYDKRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLYHNEVEIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKENTSHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHRLKEEASKRAATLAQELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRRIDEINKELNQVMEQLGDARIDRQESSRQQRKAEIMESIKRLYPGSVYGRLIDLCQPTQKKYQIAVTKVLGKNMDAIIVDSEKTGRDCIQYIKEQRGEPETFLPLDYLEVKPTDEKLRELKGAKLVIDVIRYEPPHIKKALQYACGNALVCDNVEDARRIAFGGHQRHKTVALDGTLFQKSGVISGGASDLKAKARRWDEKAVDKLKEKKERLTEELKEQMKAKRKEAELRQVQSQAHGLQMRLKYSQSDLEQTKTRHLALNLQEKSKLESELANFGPRINDIKRIIQSREREMKDLKEKMNQVEDEVFEEFCREIGVRNIREFEEEKVKRQNEIAKKRLEFENQKTRLGIQLDFEKNQLKEDQDKVHMWEQTVKKDENEIEKLKKEEQRHMKIIDETMAQLQDLKNQHLAKKSEVNDKNHEMEEIGKKLGGANKEMTHLQKEVTAIETKLEQKRSDRHNLLQACKMQDIKLPLSKGTMDDISQEEGSSQGEDSVSGSQRISSIYAREALIEIDYGDLCEDLKDAQAEEEIKQEMNTLQQKLNEQQSVLQRIAAPN,In DEE85.,,MGFLKLIEIENFKSYKGRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVLGEKTSNLRVKTLRDLIHGAPVGKPAANRAFVSMVYSEEGAEDRTFARVIVGGSSEYKINNKVVQLHEYSEELEKLGILIKARNFLVFQGAVESIAMKNPKERTALFEEISRSGELAQEYDKRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLYHNEVEIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKENTSHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHRLKEEASKRAATLAQELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRRIDEINKELNQVMEQLGDARIDRQESSRQQRKAEIMESIKRLYPGSVYGRLIDLCQPTQKKYQIAVTKVLGKNMDAIIVDSEKTGRDCIQYIKEQRGEPETFLPLDYLEVKPTDEKLRELKGAKLVIDVIRYEPPHIKKALQYACGNALVCDNVEDARRIAFGGHQRHKTVALDGTLFQKSGVISGGASDLKAKARRWDEKAVDKLKEKKERLTEELKEQMKAKRKEAELRQVQSQAHGLQMRLKYSQSDLEQTKTRHLALNLQEKSKLESELANFGPRINDIKRIIQSREREMKDLKEKMNQVEDEVFEEFCREIGVRNIREFEEEKVKRQNEIAKKRLEFENQKTRLGIQLDFEKNQLKEDQDKVHMWEQTVKKDENEIEKLKKEEQRHMKIIDETMAQLQDLKNQHLAKKSEVNDKNHEMEEIRKKLGGANKEMTHLQKEVTAIETKLEQKRSDRHNLLQACKMQDIKLPLSKGTMDDISQEEGSSQGEDSVSGSQRISSIYAREALIEIDYGDLCEDLKDAQAEEEIKQEMNTLQQKLNEQQSVLQRIAAPN,Structural maintenance of chromosomes protein 1A,"Involved in chromosome cohesion during cell cycle and in DNA repair. Central component of cohesin complex. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis. Involved in DNA repair via its interaction with BRCA1 and its related phosphorylation by ATM, or via its phosphorylation by ATR. Works as a downstream effector both in the ATM/NBS1 branch and in the ATR/MSH2 branch of S-phase checkpoint.",Loss-of-function variant in STAG2 associated with holoprosencephaly,In DEE85. Loss-of-function variant in STAG2 associated with holoprosencephaly
1654,1654,1654,123831,Q9NTI2-Q107A,MLNGAGLDKALKMSLPRRSRIRSSVGPVRSSLGYKKAEDEMSRATSVGDQLEAPARTIYLNQPHLNKFRDNQISTAKYSVLTFLPRFLYEQIRRAANAFFLFIALLAQIPDVSPTGRYTTLVPLIIILTIAGIKEIVEDFKRHKADNAVNKKKTIVLRNGMWHTIMWKEVAVGDIVKVVNGQYLPADVVLLSSSEPQAMCYVETANLDGETNLKIRQGLSHTADMQTREVLMKLSGTIECEGPNRHLYDFTGNLNLDGKSLVALGPDQILLRGTQLRNTQWVFGIVVYTGHDTKLMQNSTKAPLKRSNVEKVTNVQILVLFGILLVMALVSSAGALYWNRSHGEKNWYIKKMDTTSDNFGYNLLTFIILYNNLIPISLLVTLEVVKYTQALFINWDTDMYYIGNDTPAMARTSNLNEELGQVKYLFSDKTGTLTCNIMNFKKCSIAGVTYGHFPELAREPSSDDFCRMPPPCSDSCDFDDPRLLKNIEDRHPTAPCIQEFLTLLAVCHTVVPEKDGDNIIYQASSPDEAALVKGAKKLGFVFTARTPFSVIIEAMGQEQTFGILNVLEFSSDRKRMSVIVRTPSGRLRLYCKGADNVIFERLSKDSKYMEETLCHLEYFATEGLRTLCVAYADLSENEYEEWLKVYQEASTILKDRAQRLEECYEIIEKNLLLLGATAIEDRLQAGVPETIATLLKAEIKIWVLTGDKQETAINIGYSCRLVSQNMALILLKEDSLDATRAAITQHCTDLGNLLGKENDVALIIDGHTLKYALSFEVRRSFLDLALSCKAVICCRVSPLQKSEIVDVVKKRVKAITLAIGDGANDVGMIQTAHVGVGISGNEGMQATNNSDYAIAQFSYLEKLLLVHGAWSYNRVTKCILYCFYKNVVLYIIELWFAFVNGFSGQILFERWCIGLYNVIFTALPPFTLGIFERSCTQESMLRFPQLYKITQNGEGFNTKVFWGHCINALVHSLILFWFPMKALEHDTVLTSGHATDYLFVGNIVYTYVVVTVCLKAGLETTAWT,"No effect on flippase activity toward phosphatidylserine. Like the wild type, it is unable to translocate phosphatidylcholine.",,MLNGAGLDKALKMSLPRRSRIRSSVGPVRSSLGYKKAEDEMSRATSVGDQLEAPARTIYLNQPHLNKFRDNQISTAKYSVLTFLPRFLYEQIRRAANAFFLFIALLQQIPDVSPTGRYTTLVPLIIILTIAGIKEIVEDFKRHKADNAVNKKKTIVLRNGMWHTIMWKEVAVGDIVKVVNGQYLPADVVLLSSSEPQAMCYVETANLDGETNLKIRQGLSHTADMQTREVLMKLSGTIECEGPNRHLYDFTGNLNLDGKSLVALGPDQILLRGTQLRNTQWVFGIVVYTGHDTKLMQNSTKAPLKRSNVEKVTNVQILVLFGILLVMALVSSAGALYWNRSHGEKNWYIKKMDTTSDNFGYNLLTFIILYNNLIPISLLVTLEVVKYTQALFINWDTDMYYIGNDTPAMARTSNLNEELGQVKYLFSDKTGTLTCNIMNFKKCSIAGVTYGHFPELAREPSSDDFCRMPPPCSDSCDFDDPRLLKNIEDRHPTAPCIQEFLTLLAVCHTVVPEKDGDNIIYQASSPDEAALVKGAKKLGFVFTARTPFSVIIEAMGQEQTFGILNVLEFSSDRKRMSVIVRTPSGRLRLYCKGADNVIFERLSKDSKYMEETLCHLEYFATEGLRTLCVAYADLSENEYEEWLKVYQEASTILKDRAQRLEECYEIIEKNLLLLGATAIEDRLQAGVPETIATLLKAEIKIWVLTGDKQETAINIGYSCRLVSQNMALILLKEDSLDATRAAITQHCTDLGNLLGKENDVALIIDGHTLKYALSFEVRRSFLDLALSCKAVICCRVSPLQKSEIVDVVKKRVKAITLAIGDGANDVGMIQTAHVGVGISGNEGMQATNNSDYAIAQFSYLEKLLLVHGAWSYNRVTKCILYCFYKNVVLYIIELWFAFVNGFSGQILFERWCIGLYNVIFTALPPFTLGIFERSCTQESMLRFPQLYKITQNGEGFNTKVFWGHCINALVHSLILFWFPMKALEHDTVLTSGHATDYLFVGNIVYTYVVVTVCLKAGLETTAWT,Phospholipid-transporting ATPase IB,"Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Able to translocate phosphatidylserine, but not phosphatidylcholine. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules. Reconstituted to liposomes, the ATP8A2:TMEM30A flippase complex predominantly transports phosphatidylserine (PS) and to a lesser extent phosphatidylethanolamine (PE). Phospholipid translocation is not associated with a countertransport of an inorganic ion or other charged substrate from the cytoplasmic side toward the exoplasm in connection with the phosphorylation from ATP. ATP8A2:TMEM30A may be involved in regulation of neurite outgrowth. Proposed to function in the generation and maintenance of phospholipid asymmetry in photoreceptor disk membranes and neuronal axon membranes. May be involved in vesicle trafficking in neuronal cells. Required for normal visual and auditory function; involved in photoreceptor and inner ear spiral ganglion cell survival.",,"No effect on flippase activity toward phosphatidylserine. Like the wild type, it is unable to translocate phosphatidylcholine."
1659,1659,1659,124063,P35259-L90A,MWDSSYMQQVSEGLMTGKVPIDQVFGANPLEKLYKRRKPKGTVGLQCSPCLMSKATSTDDIIWDQLIVKRTLADLLIPINRQISDIQSTASEVTTRVHEIERQLHEITPVLKMGRTLEAISKGMSEMLAKYDHLVISTGRTTAPAAAFDAYLNEHGVPPPQPAIFKDLGVAQQACSKGTMVKNATTDAADKMSKVLELSEETFSKPNLSAKDLALLLFTHLPGNNTPFHILAQVLSKIAYKSGKSGAFLDAFHQILSEGENAQAALTRLSRTFDAFLGVVPPVIRVKNFQTVPRPSQKSLRAVPPNPTIDKGWVCVYSSEQGETRALKI,Complete loss of homo-oligomerization; when associated with A-104.,,MWDSSYMQQVSEGLMTGKVPIDQVFGANPLEKLYKRRKPKGTVGLQCSPCLMSKATSTDDIIWDQLIVKRTLADLLIPINRQISDIQSTLSEVTTRVHEIERQLHEITPVLKMGRTLEAISKGMSEMLAKYDHLVISTGRTTAPAAAFDAYLNEHGVPPPQPAIFKDLGVAQQACSKGTMVKNATTDAADKMSKVLELSEETFSKPNLSAKDLALLLFTHLPGNNTPFHILAQVLSKIAYKSGKSGAFLDAFHQILSEGENAQAALTRLSRTFDAFLGVVPPVIRVKNFQTVPRPSQKSLRAVPPNPTIDKGWVCVYSSEQGETRALKI,Polymerase cofactor VP35,Plays an essential role in viral RNA synthesis and also a role in suppressing innate immune signaling.,Substitution of leucine residue 90 abolished the function of VP35 in viral RNA synthesis. Homo-oligomerization was also abolished.,Complete loss of homo-oligomerization; when associated with A-104. Substitution of leucine residue 90 abolished the function of VP35 in viral RNA synthesis. Homo-oligomerization was also abolished.
1662,1662,1662,124409,Q9BZD2-M116R,MAVVSEDDFQHSSNSTYRTTSSSLRADQEALLEKLLDRPPPGLQRPEDRFCGTYIIFFSLGIGSLLPWNFFITAKEYWMFKLRNSSSPATGEDPEGSDILNYFESYLAVASTVPSRLCLVANFLLVNRVAVHIRVLASLTVILAIFMVITALVKVDTSSWTRGFFAVTIVCMVILSGASTVFSSSIYGMTGSFPMRNSQALISGGAMGGTVSAVASLVDLAASSDVRNSALAFFLTATVFLVLCMGLYLLLSRLEYARYYMRPVLAAHVFSGEEELPQDSLSAPSVASRFIDSHTPPLRPILKKTASLGFCVTYVFFITSLIYPAICTNIESLNKGSGSLWTTKFFIPLTTFLLYNFADLCGRQLTAWIQVPGPNSKALPGFVLLRTCLIPLFVLCNYQPRVHLKTVVFQSDVYPALLSSLLGLSNGYLSTLALLYGPKIVPRELAEATGVVMSFYVCLGLTLGSACSTLLVHLI,In HLAS; partially retained in the endoplasmic reticulum; results in reduced nucleoside transport.,,MAVVSEDDFQHSSNSTYRTTSSSLRADQEALLEKLLDRPPPGLQRPEDRFCGTYIIFFSLGIGSLLPWNFFITAKEYWMFKLRNSSSPATGEDPEGSDILNYFESYLAVASTVPSMLCLVANFLLVNRVAVHIRVLASLTVILAIFMVITALVKVDTSSWTRGFFAVTIVCMVILSGASTVFSSSIYGMTGSFPMRNSQALISGGAMGGTVSAVASLVDLAASSDVRNSALAFFLTATVFLVLCMGLYLLLSRLEYARYYMRPVLAAHVFSGEEELPQDSLSAPSVASRFIDSHTPPLRPILKKTASLGFCVTYVFFITSLIYPAICTNIESLNKGSGSLWTTKFFIPLTTFLLYNFADLCGRQLTAWIQVPGPNSKALPGFVLLRTCLIPLFVLCNYQPRVHLKTVVFQSDVYPALLSSLLGLSNGYLSTLALLYGPKIVPRELAEATGVVMSFYVCLGLTLGSACSTLLVHLI,Equilibrative nucleoside transporter 3,"Mediates both influx and efflux of nucleosides across the membrane (equilibrative transporter). Mediates transport of adenine, adenosine and uridine, as well as several nucleoside analog drugs, such as anticancer and antiviral agents, including cladribine, cordycepin, tubercidin and AZT. Does not transport hypoxanthine.",Inactivating mutations in SLC29A3 cause a syndromic form of insulin-dependent diabetes in humans and in Drosophila profoundly affect cell size/number through interactions with the insulin signaling pathway.,In HLAS; partially retained in the endoplasmic reticulum; results in reduced nucleoside transport. Inactivating mutations in SLC29A3 cause a syndromic form of insulin-dependent diabetes in humans and in Drosophila profoundly affect cell size/number through interactions with the insulin signaling pathway.
1670,1670,1670,124987,P30613-G341A,MSIQENISSLQLRSWVSKSQRDLAKSILIGAPGGPAGYLRRASVAQLTQELGTAFFQQQQLPAAMADTFLEHLCLLDIDSEPVAARSTSIIATIGPASRSVERLKEMIKAGMNIARLNFSHGSHEYHAESIANVREAVESFAGSPLSYRPVAIALDTKGPEIRTGILQGGPESEVELVKGSQVLVTVDPAFRTRGNANTVWVDYPNIVRVVPVGGRIYIDDGLISLVVQKIGPEGLVTQVENGGVLGSRKGVNLPGAQVDLPGLSEQDVRDLRFGVEHGVDIVFASFVRKASDVAAVRAALGPEGHGIKIISKIENHEGVKRFDEILEVSDGIMVARGDLAIEIPAEKVFLAQKMMIGRCNLAGKPVVCATQMLESMITKPRPTRAETSDVANAVLDGADCIMLSGETAKGNFPVEAVKMQHAIAREAEAAVYHRQLFEELRRAAPLSRDPTEVTAIGAVEAAFKCCAAAIIVLTTTGRSAQLLSRYRPRAAVIAVTRSAQAARQVHLCRGVFPLLYREPPEAIWADDVDRRVQFGIESGKLRGFLRVGDLVIVVTGWRPGSGYTNIMRVLSIS,In PKRD.,,MSIQENISSLQLRSWVSKSQRDLAKSILIGAPGGPAGYLRRASVAQLTQELGTAFFQQQQLPAAMADTFLEHLCLLDIDSEPVAARSTSIIATIGPASRSVERLKEMIKAGMNIARLNFSHGSHEYHAESIANVREAVESFAGSPLSYRPVAIALDTKGPEIRTGILQGGPESEVELVKGSQVLVTVDPAFRTRGNANTVWVDYPNIVRVVPVGGRIYIDDGLISLVVQKIGPEGLVTQVENGGVLGSRKGVNLPGAQVDLPGLSEQDVRDLRFGVEHGVDIVFASFVRKASDVAAVRAALGPEGHGIKIISKIENHEGVKRFDEILEVSDGIMVARGDLGIEIPAEKVFLAQKMMIGRCNLAGKPVVCATQMLESMITKPRPTRAETSDVANAVLDGADCIMLSGETAKGNFPVEAVKMQHAIAREAEAAVYHRQLFEELRRAAPLSRDPTEVTAIGAVEAAFKCCAAAIIVLTTTGRSAQLLSRYRPRAAVIAVTRSAQAARQVHLCRGVFPLLYREPPEAIWADDVDRRVQFGIESGKLRGFLRVGDLVIVVTGWRPGSGYTNIMRVLSIS,Pyruvate kinase PKLR,"Pyruvate kinase that catalyzes the conversion of phosphoenolpyruvate to pyruvate with the synthesis of ATP, and which plays a key role in glycolysis.","The mutation in the PKLR gene is the most likely cause of idiopathic hemolytic anemia (IHA) in the subject. This mutation has not been documented before in a single individual. Functional biochemical testing confirmed the deficiency, consistent with a diagnosis of red blood cell pyruvate kinase deficiency.","In PKRD. The mutation in the PKLR gene is the most likely cause of idiopathic hemolytic anemia (IHA) in the subject. This mutation has not been documented before in a single individual. Functional biochemical testing confirmed the deficiency, consistent with a diagnosis of red blood cell pyruvate kinase deficiency."
1681,1681,1681,125956,Q5VY80-L106R,MAAAAIPALLLCLPLLFLLFGWSRARRDDPHSLCYDITVIPKFRPGPRWCAVQGQVDEKTFLHYDCGNKTVTPVSPLGKKLNVTMAWKAQNPVLREVVDILTEQLRDIQLENYTPKEPLTLQARMSCEQKAEGHSSGSWQFSIDGQTFLLFDSEKRMWTTVHPGARKMKEKWENDKDVAMSFHYISMGDCIGWLEDFLMGMDSTLEPSAGAPLAMSSGTTQLRATATTLILCCLLIILPCFILPGI,In allele ULBP6*01; affects KLRK1-binding affinity and KLRK1-mediated cytotoxic response.,,MAAAAIPALLLCLPLLFLLFGWSRARRDDPHSLCYDITVIPKFRPGPRWCAVQGQVDEKTFLHYDCGNKTVTPVSPLGKKLNVTMAWKAQNPVLREVVDILTEQLLDIQLENYTPKEPLTLQARMSCEQKAEGHSSGSWQFSIDGQTFLLFDSEKRMWTTVHPGARKMKEKWENDKDVAMSFHYISMGDCIGWLEDFLMGMDSTLEPSAGAPLAMSSGTTQLRATATTLILCCLLIILPCFILPGI,UL16-binding protein 6,"Binds and activates the KLRK1/NKG2D receptor, mediating natural killer cell cytotoxicity.","The arginine-to-leucine polymorphism within ULBP0602 affected the NKG2D-ULBP6 interaction by generating an energetic hotspot. This resulted in an NKG2D-ULBP0602 affinity of 15. 5 nM, which is 10- to 1000-fold greater than the affinities of other ULBP-NKG2D interactions and limited NKG2D-mediated activation. In addition, soluble ULBP0602 exhibited high-affinity competitive binding for NKG2D and partially suppressed NKG2D-mediated activation of NK cells by other NKG2D ligands. These effects resulted in a decrease in a range of NKG2D-mediated effector functions.","In allele ULBP6*01; affects KLRK1-binding affinity and KLRK1-mediated cytotoxic response. The arginine-to-leucine polymorphism within ULBP0602 affected the NKG2D-ULBP6 interaction by generating an energetic hotspot. This resulted in an NKG2D-ULBP0602 affinity of 15. 5 nM, which is 10- to 1000-fold greater than the affinities of other ULBP-NKG2D interactions and limited NKG2D-mediated activation. In addition, soluble ULBP0602 exhibited high-affinity competitive binding for NKG2D and partially suppressed NKG2D-mediated activation of NK cells by other NKG2D ligands. These effects resulted in a decrease in a range of NKG2D-mediated effector functions."
1686,1686,1686,126319,P24530-L17P,MQPPPSLCGRALVALVPACGLSRIWGEERGFPPDRATPLLQTAEIMTPPTKTLWPKGSNASLARSLAPAEVPKGDRTAGSPPRTISPPPCQGPIEIKETFKYINTVVSCLVFVLGIIGNSTLLRIIYKNKCMRNGPNILIASLALGDLLHIVIDIPINVYKLLAEDWPFGAEMCKLVPFIQKASVGITVLSLCALSIDRYRAVASWSRIKGIGVPKWTAVEIVLIWVVSVVLAVPEAIGFDIITMDYKGSYLRICLLHPVQKTAFMQFYKTAKDWWLFSFYFCLPLAITAFFYTLMTCEMLRKKSGMQIALNDHLKQRREVAKTVFCLVLVFALCWLPLHLSRILKLTLYNQNDPNRCELLSFLLVLDYIGINMASLNSCINPIALYLVSKRFKNCFKSCLCCWCQSFEEKQSLEEKQSCLKFKANDHGYDNFRSSNKYSSS,Probable disease-associated variant found in patients with Waardenburg syndrome 2; loss of cell membrane location; new cytoplasmic location.,,MQPPPSLCGRALVALVLACGLSRIWGEERGFPPDRATPLLQTAEIMTPPTKTLWPKGSNASLARSLAPAEVPKGDRTAGSPPRTISPPPCQGPIEIKETFKYINTVVSCLVFVLGIIGNSTLLRIIYKNKCMRNGPNILIASLALGDLLHIVIDIPINVYKLLAEDWPFGAEMCKLVPFIQKASVGITVLSLCALSIDRYRAVASWSRIKGIGVPKWTAVEIVLIWVVSVVLAVPEAIGFDIITMDYKGSYLRICLLHPVQKTAFMQFYKTAKDWWLFSFYFCLPLAITAFFYTLMTCEMLRKKSGMQIALNDHLKQRREVAKTVFCLVLVFALCWLPLHLSRILKLTLYNQNDPNRCELLSFLLVLDYIGINMASLNSCINPIALYLVSKRFKNCFKSCLCCWCQSFEEKQSLEEKQSCLKFKANDHGYDNFRSSNKYSSS,Endothelin receptor type B,"Non-specific receptor for endothelin 1, 2, and 3. Mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system.",The mutation in EDNRB impairs the subcellular localization of the receptor or induces a defective downstream signaling pathway.,Probable disease-associated variant found in patients with Waardenburg syndrome 2; loss of cell membrane location; new cytoplasmic location. The mutation in EDNRB impairs the subcellular localization of the receptor or induces a defective downstream signaling pathway.
1700,1700,1700,128294,O67496-N106D,MIQKRKTRQIRVGNVKIGGDAPIVVQSMTSTKTHDVEATLNQIKRLYEAGCEIVRVAVPHKEDVEALEEIVKKSPMPVIADIHFAPSYAFLSMEKGVHGIRINPGDIGKEEIVREIVEEAKRRGVAVRIGVNSGSLEKDLLEKYGYPSAEALAESALRWSEKFEKWGFTNYKVSIKGSDVLQNVRANLIFAERTDVPLHIGITEAGMGTKGIIKSSVGIGILLYMGIGDTVRVSLTDDPVVEVETAYEILKSLGLRRRGVEIVACPTCGRIEVDLPKVVKEVQEKLSGVKTPLKVAVMGCVVNAIGEAREADIGLACGRGFAWLFKHGKPIKKVDESEMVDELLKEIQNMEKDGGTN,Reduces activity 2-fold.,,MIQKRKTRQIRVGNVKIGGDAPIVVQSMTSTKTHDVEATLNQIKRLYEAGCEIVRVAVPHKEDVEALEEIVKKSPMPVIADIHFAPSYAFLSMEKGVHGIRINPGNIGKEEIVREIVEEAKRRGVAVRIGVNSGSLEKDLLEKYGYPSAEALAESALRWSEKFEKWGFTNYKVSIKGSDVLQNVRANLIFAERTDVPLHIGITEAGMGTKGIIKSSVGIGILLYMGIGDTVRVSLTDDPVVEVETAYEILKSLGLRRRGVEIVACPTCGRIEVDLPKVVKEVQEKLSGVKTPLKVAVMGCVVNAIGEAREADIGLACGRGFAWLFKHGKPIKKVDESEMVDELLKEIQNMEKDGGTN,4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase,"Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.","This mutation may lead to functional changes in the protein's ability to catalyze the reductive ring opening of 2C-methyl-D-erythritol 2, 4-cyclodiphosphate.","Reduces activity 2-fold. This mutation may lead to functional changes in the protein's ability to catalyze the reductive ring opening of 2C-methyl-D-erythritol 2, 4-cyclodiphosphate."
1710,1710,1710,129626,Q39054-N597L,MEGQGCCGGGGGKTEMIPTEEALRIVFGVSKRLPPVIVSLYEALGKVLAEDIRAPDPLPPYPASVKDGYAVVASDGPGEYPVITESRAGNDGLGVTVTPGTVAYVTTGGPIPDGADAVVQVEDTKVIGDVSTESKRVKILIQTKKGTDIRRVGCDIEKDATVLTTGERIGASEIGLLATAGVTMVKVYPMPIVAILSTGDELVEPTAGTLGRGQIRDSNRAMLVAAVMQQQCKVVDLGIVRDDRKELEKVLDEAVSSGVDIILTSGGVSMGDRDFVKPLLEEKGKVYFSKVLMKPGKPLTFAEIRAKPTESMLGKTVLAFGLPGNPVSCLVCFNIFVVPTIRQLAGWTSPHPLRVRLRLQEPIKSDPIRPEFHRAIIKWKDNDGSGTPGFVAESTGHQMSSRLLSMRSANALLELPATGNVLSAGSSVSAIIVSDISAFSIDKKASLSEPGSIRKEKKYDEVPGPEYKVAILTVSDTVSAGAGPDRSGPRAVSVVDSSSEKLGGAKVVATAVVPDEVERIKDILQKWSDVDEMDLILTLGGTGFTPRDVTPEATKKVIERETPGLLFVMMQESLKITPFAMLSRSAAGIRGSTLIILMPGNPNAVAECMEALLPALKHALKQIKGDKREKHPKHIPHAEATLPTDTWDQSYKSAYETGEKKEEAGCSCTH,Loss of molybdopterin binding. Loss of activity.,,MEGQGCCGGGGGKTEMIPTEEALRIVFGVSKRLPPVIVSLYEALGKVLAEDIRAPDPLPPYPASVKDGYAVVASDGPGEYPVITESRAGNDGLGVTVTPGTVAYVTTGGPIPDGADAVVQVEDTKVIGDVSTESKRVKILIQTKKGTDIRRVGCDIEKDATVLTTGERIGASEIGLLATAGVTMVKVYPMPIVAILSTGDELVEPTAGTLGRGQIRDSNRAMLVAAVMQQQCKVVDLGIVRDDRKELEKVLDEAVSSGVDIILTSGGVSMGDRDFVKPLLEEKGKVYFSKVLMKPGKPLTFAEIRAKPTESMLGKTVLAFGLPGNPVSCLVCFNIFVVPTIRQLAGWTSPHPLRVRLRLQEPIKSDPIRPEFHRAIIKWKDNDGSGTPGFVAESTGHQMSSRLLSMRSANALLELPATGNVLSAGSSVSAIIVSDISAFSIDKKASLSEPGSIRKEKKYDEVPGPEYKVAILTVSDTVSAGAGPDRSGPRAVSVVDSSSEKLGGAKVVATAVVPDEVERIKDILQKWSDVDEMDLILTLGGTGFTPRDVTPEATKKVIERETPGLLFVMMQESLKITPFAMLSRSAAGIRGSTLIINMPGNPNAVAECMEALLPALKHALKQIKGDKREKHPKHIPHAEATLPTDTWDQSYKSAYETGEKKEEAGCSCTH,Molybdopterin biosynthesis protein CNX1,"Catalyzes two steps in the biosynthesis of the molybdenum cofactor. In the first step, molybdopterin is adenylated. Subsequently, molybdate is inserted into adenylated molybdopterin and AMP is released.",,Loss of molybdopterin binding. Loss of activity.
1720,1720,1720,129893,P08617-Y200A,MNMSRQGIFQTVGSGLDHILSLADIEEEQMIQSVDRTAVTGASYFTSVDQSSVHTAEVGSHQVEPLRTSVDKPGSKKTQGEKFFLIHSADWLTTHALFHEVAKLDVVKLLYNEQFAVQGLLRYHTYARFGIEIQVQINPTPFQQGGLICAMVPGDQSYGSIASLTVYPHGLLNCNINNVVRIKVPFIYTRGAYHFKDPQAPVWELTIRVWSELNIGTGTSAYTSLNVLARFTDLELHGLTPLSTQMMRNEFRVSTTENVVNLSNYEDARAKMSFALDQEDWKSDPSQGGGIKITHFTTWTSIPTLAAQFPFNASDSVGQQIKVIPVDPYFFQMTNTNPDQKCITALASICQMFCFWRGDLVFDFQVFPTKYHSGRLLFCFVPGNELIDVSGITLKQATTAPCAVMDITGVQSTLRFRVPWISDTPYRVNRYTKSAHQKGEYTAIGKLIVYCYNRLTSPSNVASHVRVNVYLSAINLECFAPLYHAMDVTTQVGDDSGGFSTTVSTEQNVPDPQVGITTMKDLKGKANRGKMDVSGVQAPVGAITTIEDPVLAKKVPETFPELKPGESRHTSDHMSIYKFMGRSHFLCTFTFNSNNKEYTFPITLSSTSNPPHGLPSTLRWFFNLFQLYRGPLDLTIIITGATDVDGMAWFTPVGLAVDTPWVEKESALSIDYKTALGAVRFNTRRTGNIQIRLPWYSYLYAVSGALDGLGDKTDSTFGLVSIQIANYNHSDEYLSFSCYLSVTEQSEFYFPRAPLNSNAMLSTESMMSRIAAGDLESSVDDPRSEEDKRFESHIECRKPYKELRLEVGKQRLKYAQEELSNEVLPPPRKMKGLFSQAKISLFYTEEHEIMKFSWRGVTADTRALRRFGFSLAAGRSVWTLEMDAGVLTGRLIRLNDEKWTEMKDDKIVSLIEKFTSNKYWSKVNFPHGMLDLEEIAANSKDFPNMSETDLCFLLHWLNPKKINLADRMLGLSGVQEIKEQGVGLIAECRTFLDSIAGTLKSMMFGFHHSVTVEIINTVLCFVKS,Severely decreases virus release but does not impair viral RNA replication.,,MNMSRQGIFQTVGSGLDHILSLADIEEEQMIQSVDRTAVTGASYFTSVDQSSVHTAEVGSHQVEPLRTSVDKPGSKKTQGEKFFLIHSADWLTTHALFHEVAKLDVVKLLYNEQFAVQGLLRYHTYARFGIEIQVQINPTPFQQGGLICAMVPGDQSYGSIASLTVYPHGLLNCNINNVVRIKVPFIYTRGAYHFKDPQYPVWELTIRVWSELNIGTGTSAYTSLNVLARFTDLELHGLTPLSTQMMRNEFRVSTTENVVNLSNYEDARAKMSFALDQEDWKSDPSQGGGIKITHFTTWTSIPTLAAQFPFNASDSVGQQIKVIPVDPYFFQMTNTNPDQKCITALASICQMFCFWRGDLVFDFQVFPTKYHSGRLLFCFVPGNELIDVSGITLKQATTAPCAVMDITGVQSTLRFRVPWISDTPYRVNRYTKSAHQKGEYTAIGKLIVYCYNRLTSPSNVASHVRVNVYLSAINLECFAPLYHAMDVTTQVGDDSGGFSTTVSTEQNVPDPQVGITTMKDLKGKANRGKMDVSGVQAPVGAITTIEDPVLAKKVPETFPELKPGESRHTSDHMSIYKFMGRSHFLCTFTFNSNNKEYTFPITLSSTSNPPHGLPSTLRWFFNLFQLYRGPLDLTIIITGATDVDGMAWFTPVGLAVDTPWVEKESALSIDYKTALGAVRFNTRRTGNIQIRLPWYSYLYAVSGALDGLGDKTDSTFGLVSIQIANYNHSDEYLSFSCYLSVTEQSEFYFPRAPLNSNAMLSTESMMSRIAAGDLESSVDDPRSEEDKRFESHIECRKPYKELRLEVGKQRLKYAQEELSNEVLPPPRKMKGLFSQAKISLFYTEEHEIMKFSWRGVTADTRALRRFGFSLAAGRSVWTLEMDAGVLTGRLIRLNDEKWTEMKDDKIVSLIEKFTSNKYWSKVNFPHGMLDLEEIAANSKDFPNMSETDLCFLLHWLNPKKINLADRMLGLSGVQEIKEQGVGLIAECRTFLDSIAGTLKSMMFGFHHSVTVEIINTVLCFVKS,Genome polyprotein [Cleaved into: Capsid protein VP0,"Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The naked capsid interacts with the host receptor HAVCR1 to provide virion attachment to and probably entry into the target cell.Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The naked capsid interacts with the host receptor HAVCR1 to provide virion attachment to and probably entry into the target cell.Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The naked capsid interacts with the host receptor HAVCR1 to provide virion attachment to and probably entry into the target cell.VP0 precursor is a component of the immature procapsids.Plays a role in the assembly of the 12 pentamers into an icosahedral structure. Has not been detected in mature virions, supposedly owing to its small size.Precursor component of immature procapsids that corresponds to an extended form of the structural protein VP1. After maturation, possibly by the host Cathepsin L, the assembly signal 2A is cleaved to give rise to the mature VP1 protein.Functions as a viroporin. Affects membrane integrity and causes an increase in membrane permeability. Involved in host intracellular membrane rearrangements probably to give rise to the viral factories. Does not disrupt calcium homeostasis or glycoprotein trafficking. Antagonizes the innate immune response of the host by suppressing IFN-beta synthesis, which it achieves by interfering with the RIG-I/IFIH1 pathway.Affects membrane integrity and causes an increase in membrane permeability.Associates with and induces structural rearrangements of intracellular membranes. Displays RNA-binding activity.The precursor 3ABC is targeted to the mitochondrial membrane where protease 3C activity cleaves and inhibits the host antiviral protein MAVS, thereby disrupting activation of IRF3 through the IFIH1/MDA5 pathway. In vivo, the protease activity of 3ABC precursor is more efficient in cleaving the 2BC precursor than that of protein 3C. The 3ABC precursor may therefore play a role in the proteolytic processing of the polyprotein.Interacts with the 3CD precursor and with RNA structures found at both the 5'- and 3'-termini of the viral genome. Since the 3AB precursor contains the hydrophobic domain 3A, it probably anchors the whole viral replicase complex to intracellular membranes on which viral RNA synthesis occurs.May serve as membrane anchor to the 3AB and 3ABC precursors via its hydrophobic domain. May interact with RNA.Acts as a primer for viral RNA replication and remains covalently bound to viral genomic RNA. VPg is uridylylated prior to priming replication into VPg-pUpU. The VPg-pUpU is then used as primer on the genomic RNA poly(A) by the RNA-dependent RNA polymerase to replicate the viral genome.Cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind cooperatively to the protease. Cleaves IKBKG/NEMO to impair innate immune signaling. Cleaves host PABPC1 which may participate in the switch of viral translation to RNA synthesis.Interacts with the 3AB precursor and with RNA structures found at both the 5'- and 3'-termini of the viral genome. Disrupts TLR3 signaling by degrading the host adapter protein TICAM1/TRIF.RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals.",,Severely decreases virus release but does not impair viral RNA replication.
1721,1721,1721,130008,P43246-T905R,MAVQPKETLQLESAAEVGFVRFFQGMPEKPTTTVRLFDRGDFYTAHGEDALLAAREVFKTQGVIKYMGPAGAKNLQSVVLSKMNFESFVKDLLLVRQYRVEVYKNRAGNKASKENDWYLAYKASPGNLSQFEDILFGNNDMSASIGVVGVKMSAVDGQRQVGVGYVDSIQRKLGLCEFPDNDQFSNLEALLIQIGPKECVLPGGETAGDMGKLRQIIQRGGILITERKKADFSTKDIYQDLNRLLKGKKGEQMNSAVLPEMENQVAVSSLSAVIKFLELLSDDSNFGQFELTTFDFSQYMKLDIAAVRALNLFQGSVEDTTGSQSLAALLNKCKTPQGQRLVNQWIKQPLMDKNRIEERLNLVEAFVEDAELRQTLQEDLLRRFPDLNRLAKKFQRQAANLQDCYRLYQGINQLPNVIQALEKHEGKHQKLLLAVFVTPLTDLRSDFSKFQEMIETTLDMDQVENHEFLVKPSFDPNLSELREIMNDLEKKMQSTLISAARDLGLDPGKQIKLDSSAQFGYYFRVTCKEEKVLRNNKNFSTVDIQKNGVKFTNSKLTSLNEEYTKNKTEYEEAQDAIVKEIVNISSGYVEPMQTLNDVLAQLDAVVSFAHVSNGAPVPYVRPAILEKGQGRIILKASRHACVEVQDEIAFIPNDVYFEKDKQMFHIITGPNMGGKSTYIRQTGVIVLMAQIGCFVPCESAEVSIVDCILARVGAGDSQLKGVSTFMAEMLETASILRSATKDSLIIIDELGRGTSTYDGFGLAWAISEYIATKIGAFCMFATHFHELTALANQIPTVNNLHVTALTTEETLTMLYQVKKGVCDQSFGIHVAELANFPKHVIECAKQKALELEEFQYIGESQGYDIMEPAAKKCYLEREQGEKIIQEFLSKVKQMPFTEMSEENIRIKLKQLKAEVIAKNNSFVNEIISRIKVTT,In LYNCH1; unknown pathological significance.,,MAVQPKETLQLESAAEVGFVRFFQGMPEKPTTTVRLFDRGDFYTAHGEDALLAAREVFKTQGVIKYMGPAGAKNLQSVVLSKMNFESFVKDLLLVRQYRVEVYKNRAGNKASKENDWYLAYKASPGNLSQFEDILFGNNDMSASIGVVGVKMSAVDGQRQVGVGYVDSIQRKLGLCEFPDNDQFSNLEALLIQIGPKECVLPGGETAGDMGKLRQIIQRGGILITERKKADFSTKDIYQDLNRLLKGKKGEQMNSAVLPEMENQVAVSSLSAVIKFLELLSDDSNFGQFELTTFDFSQYMKLDIAAVRALNLFQGSVEDTTGSQSLAALLNKCKTPQGQRLVNQWIKQPLMDKNRIEERLNLVEAFVEDAELRQTLQEDLLRRFPDLNRLAKKFQRQAANLQDCYRLYQGINQLPNVIQALEKHEGKHQKLLLAVFVTPLTDLRSDFSKFQEMIETTLDMDQVENHEFLVKPSFDPNLSELREIMNDLEKKMQSTLISAARDLGLDPGKQIKLDSSAQFGYYFRVTCKEEKVLRNNKNFSTVDIQKNGVKFTNSKLTSLNEEYTKNKTEYEEAQDAIVKEIVNISSGYVEPMQTLNDVLAQLDAVVSFAHVSNGAPVPYVRPAILEKGQGRIILKASRHACVEVQDEIAFIPNDVYFEKDKQMFHIITGPNMGGKSTYIRQTGVIVLMAQIGCFVPCESAEVSIVDCILARVGAGDSQLKGVSTFMAEMLETASILRSATKDSLIIIDELGRGTSTYDGFGLAWAISEYIATKIGAFCMFATHFHELTALANQIPTVNNLHVTALTTEETLTMLYQVKKGVCDQSFGIHVAELANFPKHVIECAKQKALELEEFQYIGESQGYDIMEPAAKKCYLEREQGEKIIQEFLSKVKQMPFTEMSEENITIKLKQLKAEVIAKNNSFVNEIISRIKVTT,DNA mismatch repair protein Msh2,"Component of the post-replicative DNA mismatch repair system (MMR). Forms two different heterodimers: MutS alpha (MSH2-MSH6 heterodimer) and MutS beta (MSH2-MSH3 heterodimer) which binds to DNA mismatches thereby initiating DNA repair. When bound, heterodimers bend the DNA helix and shields approximately 20 base pairs. MutS alpha recognizes single base mismatches and dinucleotide insertion-deletion loops (IDL) in the DNA. MutS beta recognizes larger insertion-deletion loops up to 13 nucleotides long. After mismatch binding, MutS alpha or beta forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. Recruits DNA helicase MCM9 to chromatin which unwinds the mismatch containing DNA strand. ATP binding and hydrolysis play a pivotal role in mismatch repair functions. The ATPase activity associated with MutS alpha regulates binding similar to a molecular switch: mismatched DNA provokes ADP-->ATP exchange, resulting in a discernible conformational transition that converts MutS alpha into a sliding clamp capable of hydrolysis-independent diffusion along the DNA backbone. This transition is crucial for mismatch repair. MutS alpha may also play a role in DNA homologous recombination repair. In melanocytes may modulate both UV-B-induced cell cycle regulation and apoptosis.",,In LYNCH1; unknown pathological significance.
1746,1746,1746,132089,P78330-D32N,MVSHSELRKLFYSADAVCFDVDSTVIREEGINELAKICGVEDAVSEMTRRAMGGAVPFKAALTERLALIQPSREQVQRLIAEQPPHLTPGIRELVSRLQERNVQVFLISGGFRSIVEHVASKLNIPATNVFANRLKFYFNGEYAGFDETQPTAESGGKGKVIKLLKEKFHFKKIIMIGDGATDMEACPPADAFIGFGGNVIRQQVKDNAKWYITDFVELLGELEE,In PSPHD; decreased L-phosphoserine phosphatase activity.,,MVSHSELRKLFYSADAVCFDVDSTVIREEGIDELAKICGVEDAVSEMTRRAMGGAVPFKAALTERLALIQPSREQVQRLIAEQPPHLTPGIRELVSRLQERNVQVFLISGGFRSIVEHVASKLNIPATNVFANRLKFYFNGEYAGFDETQPTAESGGKGKVIKLLKEKFHFKKIIMIGDGATDMEACPPADAFIGFGGNVIRQQVKDNAKWYITDFVELLGELEE,Phosphoserine phosphatase,"Catalyzes the last irreversible step in the biosynthesis of L-serine from carbohydrates, the dephosphorylation of O-phospho-L-serine to L-serine. L-serine can then be used in protein synthesis, to produce other amino acids, in nucleotide metabolism or in glutathione synthesis, or can be racemized to D-serine, a neuromodulator. May also act on O-phospho-D-serine (Probable).","The mutation caused a 50% decrease in Vmax. In addition, L-serine, which inhibits the conversion of [(14)C] phosphoserine to serine when catalysed by the wild-type enzyme, had a lesser inhibitory effect on the mutant, indicating a reduction in the rate of phosphoenzyme hydrolysis.","In PSPHD; decreased L-phosphoserine phosphatase activity. The mutation caused a 50% decrease in Vmax. In addition, L-serine, which inhibits the conversion of [(14)C] phosphoserine to serine when catalysed by the wild-type enzyme, had a lesser inhibitory effect on the mutant, indicating a reduction in the rate of phosphoenzyme hydrolysis."
1763,1763,1763,133332,P0DOE4-A39S,MENTSITIEFSSKFWPYFTLIHMITTIISLLIIISIMISILNKLCEYNVFHNKTFELPRARVNT,Abolishes the effect of small-molecule inhibitor.,,MENTSITIEFSSKFWPYFTLIHMITTIISLLIIISIMIAILNKLCEYNVFHNKTFELPRARVNT,Small hydrophobic protein,"Viroporin that forms a homopentameric ion channel displaying low ion selectivity. May play a role in virus morphogenesis and pathogenicity at various stages of the viral life cycle. Accumulates at the membrane of the Golgi apparatus in infected cells and may facilitate virus release by modifying the secretory pathway. May enhance host membrane permeability and disrupt cellular ion homeostasis, which can be sensed as damage-associated molecular patterns/danger signals, triggering NLRP3 inflammasome activation and inflammatory immune response. Also inhibits host TNFA-mediated signaling pathway and may delay apoptosis, allowing time for the virus to replicate.",The mutation in the SH protein has not been found to have any significant effect on channel activity.,Abolishes the effect of small-molecule inhibitor. The mutation in the SH protein has not been found to have any significant effect on channel activity.
1778,1778,1778,134333,Q9Y2K2-S551E,MAAAAASGAGGAAGAGTGGAGPAGRLLPPPAPGSPAAPAAVSPAAGQPRPPAPASRGPMPARIGYYEIDRTIGKGNFAVVKRATHLVTKAKVAIKIIDKTQLDEENLKKIFREVQIMKMLCHPHIIRLYQVMETERMIYLVTEYASGGEIFDHLVAHGRMAEKEARRKFKQIVTAVYFCHCRNIVHRDLKAENLLLDANLNIKIADFGFSNLFTPGQLLKTWCGSPPYAAPELFEGKEYDGPKVDIWSLGVVLYVLVCGALPFDGSTLQNLRARVLSGKFRIPFFMSTECEHLIRHMLVLDPNKRLSMEQICKHKWMKLGDADPNFDRLIAECQQLKEERQVDPLNEDVLLAMEDMGLDKEQTLQSLRSDAYDHYSAIYSLLCDRHKRHKTLRLGALPSMPRALAFQAPVNIQAEQAGTAMNISVPQVQLINPENQIVEPDGTLNLDSDEGEEPSPEALVRYLSMRRHTVGVADPRTEVMEDLQKLLPGFPGVNPQAPFLQVAPNVNFMHNLLPMQNLQPTGQLEYKEQSLLQPPTLQLLNGMGPLGRRAEDGGANIQLHAQQLLKRPRGPSPLVTMTPAVPAVTPVDEESSDGEPDQEAVQSSTYKDSNTLHLPTERFSPVRRFSDGAASIQAFKAHLEKMGNNSSIKQLQQECEQLQKMYGGQIDERTLEKTQQQHMLYQQEQHHQILQQQIQDSICPPQPSPPLQAACENQPALLTHQLQRLRIQPSSPPPNHPNNHLFRQPSNSPPPMSSAMIQPHGAASSSQFQGLPSRSAIFQQQPENCSSPPNVALTCLGMQQPAQSQQVTIQVQEPVDMLSNMPGTAAGSSGRGISISPSAGQMQMQHRTNLMATLSYGHRPLSKQLSADSAEAHSLNVNRFSPANYDQAHLHPHLFSDQSRGSPSSYSPSTGVGFSPTQALKVPPLDQFPTFPPSAHQQPPHYTTSALQQALLSPTPPDYTRHQQVPHILQGLLSPRHSLTGHSDIRLPPTEFAQLIKRQQQQRQQQQQQQQQQEYQELFRHMNQ,Loss of interaction with 14-3-3 proteins in response to cAMP signaling; inhibits cAMP signaling.,,MAAAAASGAGGAAGAGTGGAGPAGRLLPPPAPGSPAAPAAVSPAAGQPRPPAPASRGPMPARIGYYEIDRTIGKGNFAVVKRATHLVTKAKVAIKIIDKTQLDEENLKKIFREVQIMKMLCHPHIIRLYQVMETERMIYLVTEYASGGEIFDHLVAHGRMAEKEARRKFKQIVTAVYFCHCRNIVHRDLKAENLLLDANLNIKIADFGFSNLFTPGQLLKTWCGSPPYAAPELFEGKEYDGPKVDIWSLGVVLYVLVCGALPFDGSTLQNLRARVLSGKFRIPFFMSTECEHLIRHMLVLDPNKRLSMEQICKHKWMKLGDADPNFDRLIAECQQLKEERQVDPLNEDVLLAMEDMGLDKEQTLQSLRSDAYDHYSAIYSLLCDRHKRHKTLRLGALPSMPRALAFQAPVNIQAEQAGTAMNISVPQVQLINPENQIVEPDGTLNLDSDEGEEPSPEALVRYLSMRRHTVGVADPRTEVMEDLQKLLPGFPGVNPQAPFLQVAPNVNFMHNLLPMQNLQPTGQLEYKEQSLLQPPTLQLLNGMGPLGRRASDGGANIQLHAQQLLKRPRGPSPLVTMTPAVPAVTPVDEESSDGEPDQEAVQSSTYKDSNTLHLPTERFSPVRRFSDGAASIQAFKAHLEKMGNNSSIKQLQQECEQLQKMYGGQIDERTLEKTQQQHMLYQQEQHHQILQQQIQDSICPPQPSPPLQAACENQPALLTHQLQRLRIQPSSPPPNHPNNHLFRQPSNSPPPMSSAMIQPHGAASSSQFQGLPSRSAIFQQQPENCSSPPNVALTCLGMQQPAQSQQVTIQVQEPVDMLSNMPGTAAGSSGRGISISPSAGQMQMQHRTNLMATLSYGHRPLSKQLSADSAEAHSLNVNRFSPANYDQAHLHPHLFSDQSRGSPSSYSPSTGVGFSPTQALKVPPLDQFPTFPPSAHQQPPHYTTSALQQALLSPTPPDYTRHQQVPHILQGLLSPRHSLTGHSDIRLPPTEFAQLIKRQQQQRQQQQQQQQQQEYQELFRHMNQ,Serine/threonine-protein kinase SIK3,"Positive regulator of mTOR signaling that functions by triggering the degradation of DEPTOR, an mTOR inhibitor. Involved in the dynamic regulation of mTOR signaling in chondrocyte differentiation during skeletogenesis. Negatively regulates cAMP signaling pathway possibly by acting on CRTC2/TORC2 and CRTC3/TORC3 (Probable). Prevents HDAC4 translocation to the nucleus.",Loss of a single 14-3-3-binding site in SIK1 and SIK3 abolished 14-3-3 association and rendered them insensitive to cAMP.,Loss of interaction with 14-3-3 proteins in response to cAMP signaling; inhibits cAMP signaling. Loss of a single 14-3-3-binding site in SIK1 and SIK3 abolished 14-3-3 association and rendered them insensitive to cAMP.
1789,1789,1789,134903,P0A809-L170A,MIGRLRGIIIEKQPPLVLIEVGGVGYEVHMPMTCFYELPEAGQEAIVFTHFVVREDAQLLYGFNNKQERTLFKELIKTNGVGPKLALAILSGMSAQQFVNAVEREEVGALVKLPGIGKKTAERLIVEMKDRFKGLHGDLFTPAADLVLTSPASPATDDAEQEAVAALVAAGYKPQEASRMVSKIARPDASSETLIREALRAAL,"Does not complement deletion, tetramerizes, does not bind RuvB, dominant negative to wt. Alters conformation of isolated domain III.",,MIGRLRGIIIEKQPPLVLIEVGGVGYEVHMPMTCFYELPEAGQEAIVFTHFVVREDAQLLYGFNNKQERTLFKELIKTNGVGPKLALAILSGMSAQQFVNAVEREEVGALVKLPGIGKKTAERLIVEMKDRFKGLHGDLFTPAADLVLTSPASPATDDAEQEAVAALVALGYKPQEASRMVSKIARPDASSETLIREALRAAL,Holliday junction branch migration complex subunit RuvA,"The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. The RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR); RFR and homologous recombination required for UV light survival can be separated. The RuvA-RuvB complex promotes Holliday junction (HJ) branch migration. RuvA binds to HJ cruciform DNA, conferring on it an open structure. In the presence of RuvB, ATP and Mg(2+) the junction is dissociated; hydrolyzable (d)NTPs can replace ATP but other analogs cannot. The RuvB hexamer acts as a pump, pulling dsDNA into and through the RuvAB complex. Can bypass UV-induced lesions  and physically cross-linked DNA strands. RuvA gives specificity by binding to cruciform junctions, while the RuvB ATPase provides the motor force for branch migration; excess RuvB can promote branch migration in the absence of RuvA. Overexpression of RuvA alone leads to UV sensitivity. RuvA stimulates the weak ATPase activity of RuvB in the presence of DNA; the addition of HJ DNA further stimulates ATPase about 10-fold. Inhibits RuvC endoDNase activity by binding to HJ DNA, including DNA to which RuvC is already bound. Does not bind dsDNA. May act as a collar that slides at HJ which promotes branch migration while inhibiting other DNA remodeling activities (Probable).",The mutation in the carboxyl-terminal domain (domain III) of RuvA impairs its binding to RuvB and also modulates the ATPase activity of RuvB. This modulation may facilitate the dynamic coupling between RuvA and RuvB during branch migration.,"Does not complement deletion, tetramerizes, does not bind RuvB, dominant negative to wt. Alters conformation of isolated domain III. The mutation in the carboxyl-terminal domain (domain III) of RuvA impairs its binding to RuvB and also modulates the ATPase activity of RuvB. This modulation may facilitate the dynamic coupling between RuvA and RuvB during branch migration."
1791,1791,1791,134958,A7MAQ2-Q139H,MSSSTLLHLLLLSSLLFSCLSCLTNVEDEFSYIEGNPNGPENWGNLKPEWETCGKGMEQSPIQLRDNRVIFDQTLGKLRRNYRAVDARLRNSGHDVLVDFKGNAGSLSINRVEYQLKRIHFHSPSEHEMNGERFDLEAHLVHESQDQKRAVVSILFRFGRADPFLSDLEDFIKQFSNSQKNEINAGVVDPNQLQIDDSAYYRYMGSFTAPPCTEGISWTVMRKVATVSPRQVLLLKQAVNENAINNARPLQPTNFRSVFYFEQLKSKLGVI,Slight decrease of dehydroascorbate (DHA) reductase activity. Significant decrease of dehydroascorbate (DHA) reductase activity by the addition of Zn(2+). Increase of carbonate dehydratase activity by the addition of Zn(2+).,,MSSSTLLHLLLLSSLLFSCLSCLTNVEDEFSYIEGNPNGPENWGNLKPEWETCGKGMEQSPIQLRDNRVIFDQTLGKLRRNYRAVDARLRNSGHDVLVDFKGNAGSLSINRVEYQLKRIHFHSPSEHEMNGERFDLEAQLVHESQDQKRAVVSILFRFGRADPFLSDLEDFIKQFSNSQKNEINAGVVDPNQLQIDDSAYYRYMGSFTAPPCTEGISWTVMRKVATVSPRQVLLLKQAVNENAINNARPLQPTNFRSVFYFEQLKSKLGVI,Dioscorin dioA3,"Storage protein of tuber. Involved in protection against oxidative stress (Probable). Has carbonate dehydratase, trypsin inhibitor, dehydroascorbate (DHA) reductase and monodehydroascorbate (MDA) reductase activities. Catalyzes the reactions of carbonate dehydratase and DHA reductase independently of zinc and glutathione (GSH). The coupled reaction is capable of recycling a plant antioxidant ascorbate using ubiquitous compounds H(2)O and CO(2). Exhibits antioxidant activity. Able to scavenge 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical. Exhibits immunomodulatory activity. Activates Toll-like receptor 4 signaling pathways by up-regulating the gene expression of pro-inflammatory cytokines, such as tumor necrosis factor alpha, interleukin-1 beta and interleukin-6, and chemokines RANTES and MCP-1, in mouse RAW 264.7 macrophages. Stimulates the phagocytosis of E.coli by the LPS-treated mouse macrophages.",,Slight decrease of dehydroascorbate (DHA) reductase activity. Significant decrease of dehydroascorbate (DHA) reductase activity by the addition of Zn(2+). Increase of carbonate dehydratase activity by the addition of Zn(2+).
1817,1817,1817,137183,Q13285-K440A,MDYSYDEDLDELCPVCGDKVSGYHYGLLTCESCKGFFKRTVQNNKHYTCTESQSCKIDKTQRKRCPFCRFQKCLTVGMRLEAVRADRMRGGRNKFGPMYKRDRALKQQKKAQIRANGFKLETGPPMGVPPPPPPAPDYVLPPSLHGPEPKGLAAGPPAGPLGDFGAPALPMAVPGAHGPLAGYLYPAFPGRAIKSEYPEPYASPPQPGLPYGYPEPFSGGPNVPELILQLLQLEPDEDQVRARILGCLQEPTKSRPDQPAAFGLLCRMADQTFISIVDWARRCMVFKELEVADQMTLLQNCWSELLVFDHIYRQVQHGKEGSILLVTGQEVELTTVATQAGSLLHSLVLRAQELVLQLLALQLDRQEFVCLKFIILFSLDLKFLNNHILVKDAQEKANAALLDYTLCHYPHCGDKFQQLLLCLVEVRALSMQAKEYLYHAHLGNEMPRNNLLIEMLQAKQT,Loss of transactivation; when associated with F-436.,,MDYSYDEDLDELCPVCGDKVSGYHYGLLTCESCKGFFKRTVQNNKHYTCTESQSCKIDKTQRKRCPFCRFQKCLTVGMRLEAVRADRMRGGRNKFGPMYKRDRALKQQKKAQIRANGFKLETGPPMGVPPPPPPAPDYVLPPSLHGPEPKGLAAGPPAGPLGDFGAPALPMAVPGAHGPLAGYLYPAFPGRAIKSEYPEPYASPPQPGLPYGYPEPFSGGPNVPELILQLLQLEPDEDQVRARILGCLQEPTKSRPDQPAAFGLLCRMADQTFISIVDWARRCMVFKELEVADQMTLLQNCWSELLVFDHIYRQVQHGKEGSILLVTGQEVELTTVATQAGSLLHSLVLRAQELVLQLLALQLDRQEFVCLKFIILFSLDLKFLNNHILVKDAQEKANAALLDYTLCHYPHCGDKFQQLLLCLVEVRALSMQAKEYLYHKHLGNEMPRNNLLIEMLQAKQT,Steroidogenic factor 1,"Transcriptional activator. Essential for sexual differentiation and formation of the primary steroidogenic tissues. Binds to the Ad4 site found in the promoter region of steroidogenic P450 genes such as CYP11A, CYP11B and CYP21B. Also regulates the AMH/Muellerian inhibiting substance gene as well as the AHCH and STAR genes. 5'-YCAAGGYC-3' and 5'-RRAGGTCA-3' are the consensus sequences for the recognition by NR5A1. The SFPQ-NONO-NR5A1 complex binds to the CYP17 promoter and regulates basal and cAMP-dependent transcriptional activity. Binds phosphatidylcholine. Binds phospholipids with a phosphatidylinositol (PI) headgroup, in particular PI(3,4)P2 and PI(3,4,5)P3. Activated by the phosphorylation of NR5A1 by HIPK3 leading to increased steroidogenic gene expression upon cAMP signaling pathway stimulation.",,Loss of transactivation; when associated with F-436.
1819,1819,1819,137447,P61092-M180K,MSRQTATALPTGTSKCPPSQRVPALTGTTASNNDLASLFECPVCFDYVLPPILQCQSGHLVCSNCRPKLTCCPTCRGPLGSIRNLAMEKVANSVLFPCKYASSGCEITLPHTEKAEHEELCEFRPYSCPCPGASCKWQGSLDAVMPHLMHQHKSITTLQGEDIVFLATDINLPGAVDWVKMQSCFGFHFMLVLEKQEKYDGHQQFFAIVQLIGTRKQAENFAYRLELNGHRRRLTWEATPRSIHEGIATAIMNSDCLVFDTSIAQLFAENGNLGINVTISMC,Strongly reduced binding of target proteins. Strongly reduced degradation of target proteins.,,MSRQTATALPTGTSKCPPSQRVPALTGTTASNNDLASLFECPVCFDYVLPPILQCQSGHLVCSNCRPKLTCCPTCRGPLGSIRNLAMEKVANSVLFPCKYASSGCEITLPHTEKAEHEELCEFRPYSCPCPGASCKWQGSLDAVMPHLMHQHKSITTLQGEDIVFLATDINLPGAVDWVMMQSCFGFHFMLVLEKQEKYDGHQQFFAIVQLIGTRKQAENFAYRLELNGHRRRLTWEATPRSIHEGIATAIMNSDCLVFDTSIAQLFAENGNLGINVTISMC,E3 ubiquitin-protein ligase SIAH1A,"E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates E3 ubiquitin ligase activity either through direct binding to substrates or by functioning as the essential RING domain subunit of larger E3 complexes. Triggers the ubiquitin-mediated degradation of many substrates, including proteins involved in transcription regulation (ELL2, MYB, POU2AF1, PML and RBBP8), a cell surface receptor (DCC), the cell-surface receptor-type tyrosine kinase FLT3, the cytoplasmic signal transduction molecules (KLF10/TIEG1 and NUMB), an antiapoptotic protein (BAG1), a microtubule motor protein (KIF22), a protein involved in synaptic vesicle function in neurons (SYP), a structural protein (CTNNB1) and SNCAIP. Confers constitutive instability to HIPK2 through proteasomal degradation. It is thereby involved in many cellular processes such as apoptosis, tumor suppression, cell cycle, axon guidance, transcription regulation, spermatogenesis and TNF-alpha signaling. Has some overlapping function with SIAH2. Required for completion of meiosis I in males. Induces apoptosis in cooperation with PEG3. Upon nitric oxid (NO) generation that follows apoptotic stimulation, interacts with S-nitrosylated GAPDH, mediating the translocation of GAPDH to the nucleus. GAPDH acts as a stabilizer of SIAH1, facilitating the degradation of nuclear proteins. Mediates ubiquitination and degradation of EGLN2 and EGLN3 in response to the unfolded protein response (UPR), leading to their degradation and subsequent stabilization of ATF4. Also part of the Wnt signaling pathway in which it mediates the Wnt-induced ubiquitin-mediated proteasomal degradation of AXIN1.",Mutagenesis of Siah at site abrogates both in vitro peptide binding and destabilization of a known Siah target.,Strongly reduced binding of target proteins. Strongly reduced degradation of target proteins. Mutagenesis of Siah at site abrogates both in vitro peptide binding and destabilization of a known Siah target.
1823,1823,1823,137666,P11224-K183G,MLFVFILFLPSCLGYIGDFRCIQLVNSNGANVSAPSISTETVEVSQGLGTYYVLDRVYLNATLLLTGYYPVDGSKFRNLALRGTNSVSLSWFQPPYLNQFNDGIFAKVQNLKTSTPSGATAYFPTIVIGSLFGYTSYTVVIEPYNGVIMASVCQYTICQLPYTDCKPNTNGNKLIGFWHTDVGPPICVLKRNFTLNVNADAFYFHFYQHGGTFYAYYADKPSATTFLFSVYIGDILTQYYVLPFICNPTAGSTFAPRYWVTPLVKRQYLFNFNQKGVITSAVDCASSYTSEIKCKTQSMLPSTGVYELSGYTVQPVGVVYRRVANLPACNIEEWLTARSVPSPLNWERKTFQNCNFNLSSLLRYVQAESLFCNNIDASKVYGRCFGSISVDKFAVPRSRQVDLQLGNSGFLQTANYKIDTAATSCQLHYTLPKNNVTINNHNPSSWNRRYGFNDAGVFGKNQHDVVYAQQCFTVRSSYCPCAQPDIVSPCTTQTKPKSAFVNVGDHCEGLGVLEDNCGNADPHKGCICANNSFIGWSHDTCLVNDRCQIFANILLNGINSGTTCSTDLQLPNTEVVTGICVKYDLYGITGQGVFKEVKADYYNSWQTLLYDVNGNLNGFRDLTTNKTYTIRSCYSGRVSAAFHKDAPEPALLYRNINCSYVFSNNISREENPLNYFDSYLGCVVNADNRTDEALPNCDLRMGAGLCVDYSKSRRAHRSVSTGYRLTTFEPYTPMLVNDSVQSVDGLYEMQIPTNFTIGHHEEFIQTRSPKVTIDCAAFVCGDNTACRQQLVEYGSFCVNVNAILNEVNNLLDNMQLQVASALMQGVTISSRLPDGISGPIDDINFSPLLGCIGSTCAEDGNGPSAIRGRSAIEDLLFDKVKLSDVGFVEAYNNCTGGQEVRDLLCVQSFNGIKVLPPVLSESQISGYTTGATAAAMFPPWSAAAGVPFSLSVQYRINGLGVTMNVLSENQKMIASAFNNALGAIQDGFDATNSALGKIQSVVNANAEALNNLLNQLSNRFGAIS,Complete loss of infectivity on murine cells.,,MLFVFILFLPSCLGYIGDFRCIQLVNSNGANVSAPSISTETVEVSQGLGTYYVLDRVYLNATLLLTGYYPVDGSKFRNLALRGTNSVSLSWFQPPYLNQFNDGIFAKVQNLKTSTPSGATAYFPTIVIGSLFGYTSYTVVIEPYNGVIMASVCQYTICQLPYTDCKPNTNGNKLIGFWHTDVKPPICVLKRNFTLNVNADAFYFHFYQHGGTFYAYYADKPSATTFLFSVYIGDILTQYYVLPFICNPTAGSTFAPRYWVTPLVKRQYLFNFNQKGVITSAVDCASSYTSEIKCKTQSMLPSTGVYELSGYTVQPVGVVYRRVANLPACNIEEWLTARSVPSPLNWERKTFQNCNFNLSSLLRYVQAESLFCNNIDASKVYGRCFGSISVDKFAVPRSRQVDLQLGNSGFLQTANYKIDTAATSCQLHYTLPKNNVTINNHNPSSWNRRYGFNDAGVFGKNQHDVVYAQQCFTVRSSYCPCAQPDIVSPCTTQTKPKSAFVNVGDHCEGLGVLEDNCGNADPHKGCICANNSFIGWSHDTCLVNDRCQIFANILLNGINSGTTCSTDLQLPNTEVVTGICVKYDLYGITGQGVFKEVKADYYNSWQTLLYDVNGNLNGFRDLTTNKTYTIRSCYSGRVSAAFHKDAPEPALLYRNINCSYVFSNNISREENPLNYFDSYLGCVVNADNRTDEALPNCDLRMGAGLCVDYSKSRRAHRSVSTGYRLTTFEPYTPMLVNDSVQSVDGLYEMQIPTNFTIGHHEEFIQTRSPKVTIDCAAFVCGDNTACRQQLVEYGSFCVNVNAILNEVNNLLDNMQLQVASALMQGVTISSRLPDGISGPIDDINFSPLLGCIGSTCAEDGNGPSAIRGRSAIEDLLFDKVKLSDVGFVEAYNNCTGGQEVRDLLCVQSFNGIKVLPPVLSESQISGYTTGATAAAMFPPWSAAAGVPFSLSVQYRINGLGVTMNVLSENQKMIASAFNNALGAIQDGFDATNSALGKIQSVVNANAEALNNLLNQLSNRFGAIS,Spike glycoprotein,"Attaches the virion to the cell membrane by interacting with host receptor, initiating the infection. Interacts with murine CEACAM1 to mediate viral entry.Mediates fusion of the virion and cellular membranes by acting as a class I viral fusion protein. Under the current model, the protein has at least three conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes.Acts as a viral fusion peptide which is unmasked following S2 cleavage occurring upon virus endocytosis.",Viruses with substitutions could only be recovered from cells that over-expressed a mutant mCEACAM1a.,Complete loss of infectivity on murine cells. Viruses with substitutions could only be recovered from cells that over-expressed a mutant mCEACAM1a.
1825,1825,1825,138135,Q19124-H326Y,MADSYRKLIIERLEDVKQRNKQTATLYNNYSKLAEQLEKKHKYGTSSSNSSQLETGELARVKEEMAELYRSKCQNDQRLIDANHRIADFEKKSSAIIAEKIALEATAKSICAKYAKTEVELQRLKVDNDQLNDERIASNTTVTMLTKQIQDIENDRIHFLNKIRELNEQRVDFLNAEVALEEKRRNSRIQDMITSAVQDITDKDTKLEEMLRAMPDTNSNGDLLLGDSVPSRAEFVLECEEGEVNDVHWLDGETFATGGSDRNIKIWKVDGHGGYTRIGTLAGSNAAFTRIDYERDRKHFIASSNDKNVRIWNLDNSRLLSTLSGYSDQVTCVKFYQSHSAVSGSADRVIKIWDIQNQRCSRSLFPASKVLDVATNMGASPSLFASGHFDKKLRFYDGRSTDPVRTVDMGGRITSLDVTMSGCELLVSTRDDTISLIDLRTFQTVHCYSAENYRTSSDLSRVVLSSGNEYVAAGSSNGSIFVWNRNSTKLEKQLCSNSENAIFSLSWNPTGYGLLSSSKQKFVTLWK,"In qx57; results in defective degradation of sqst-1, pgl-1 and sepa-1 protein aggregates.",,MADSYRKLIIERLEDVKQRNKQTATLYNNYSKLAEQLEKKHKYGTSSSNSSQLETGELARVKEEMAELYRSKCQNDQRLIDANHRIADFEKKSSAIIAEKIALEATAKSICAKYAKTEVELQRLKVDNDQLNDERIASNTTVTMLTKQIQDIENDRIHFLNKIRELNEQRVDFLNAEVALEEKRRNSRIQDMITSAVQDITDKDTKLEEMLRAMPDTNSNGDLLLGDSVPSRAEFVLECEEGEVNDVHWLDGETFATGGSDRNIKIWKVDGHGGYTRIGTLAGSNAAFTRIDYERDRKHFIASSNDKNVRIWNLDNSRLLSTLSGHSDQVTCVKFYQSHSAVSGSADRVIKIWDIQNQRCSRSLFPASKVLDVATNMGASPSLFASGHFDKKLRFYDGRSTDPVRTVDMGGRITSLDVTMSGCELLVSTRDDTISLIDLRTFQTVHCYSAENYRTSSDLSRVVLSSGNEYVAAGSSNGSIFVWNRNSTKLEKQLCSNSENAIFSLSWNPTGYGLLSSSKQKFVTLWK,Autophagic-related protein 16.1,"Most likely a component of the atg-5-atg-12-atg-16.1/atg-16.2 complex, which is recruited to the preautophagosomal membrane and associates with lgg-2 to promote autophagosome formation. Although its role in autophagosome formation may be distinct to the role of atg-16.2, it functions in a partially redundant manner with atg-16.2 to regulate autophagic processes.",,"In qx57; results in defective degradation of sqst-1, pgl-1 and sepa-1 protein aggregates."
1842,1842,1842,139002,P05044-E124A,MAYPGHPGAGGGYYPGGYGGAPGGPSFPGQTQDPLYGYFASVAGQDGQIDADELQRCLTQSGIAGGYKPFNLETCRLMVSMLDRDMSGTMGFNEFKELWAVLNGWRQHFISFDSDRSGTVDPQALQKALTTMGFRLNPQTVNSIAKRYSTSGKITFDDYIACCVKLRALTDSFRRRDSAQQGMVNFSYDDFIQCVMTV,Strongly reduced modulation of RYR2 channel activity.,,MAYPGHPGAGGGYYPGGYGGAPGGPSFPGQTQDPLYGYFASVAGQDGQIDADELQRCLTQSGIAGGYKPFNLETCRLMVSMLDRDMSGTMGFNEFKELWAVLNGWRQHFISFDSDRSGTVDPQELQKALTTMGFRLNPQTVNSIAKRYSTSGKITFDDYIACCVKLRALTDSFRRRDSAQQGMVNFSYDDFIQCVMTV,Sorcin,Calcium-binding protein that modulates excitation-contraction coupling in the heart. Contributes to calcium homeostasis in the sarcoplasmic reticulum in the heart. Modulates the activity of RYR2 calcium channels.,,Strongly reduced modulation of RYR2 channel activity.
1843,1843,1843,139280,Q9UJW0-C79S,MASLLQSDRVLYLVQGEKKVRAPLSQLYFCRYCSELRSLECVSHEVDSHYCPSCLENMPSAEAKLKKNRCANCFDCPGSMHTLSTRATSISTQLPDDPAKTTMKKAYYLACGFCRWTSRDVGMADKSVASGGWQEPENPHTQRMNKLIEYYQQLAQKEKVERDRKKLARRRNYMPLAFSDKYGLGTRLQRPRAGASISTLAGLSLKEGEDQKEIKIEPAQAVDEVEPLPEDYYTRPVNLTEVTTLQQRLLQPDFQPVCASQLYPRHKHLLIKRSLRCRKCEHNLSKPEFNPTSIKFKIQLVAVNYIPEVRIMSIPNLRYMKESQVLLTLTNPVENLTHVTLFECEEGDPDDINSTAKVVVPPKELVLAGKDAAAEYDELAEPQDFQDDPDIIAFRKANKVGIFIKVTPQREEGEVTVCFKMKHDFKNLAAPIRPIEESDQGTEVIWLTQHVELSLGPLLP,"Loss of ATP7B-binding; when associated with S-30; S-33; S-51; S-54, S-70; S-73; S-76; S-111; S-114; S-277 and S-280.",,MASLLQSDRVLYLVQGEKKVRAPLSQLYFCRYCSELRSLECVSHEVDSHYCPSCLENMPSAEAKLKKNRCANCFDCPGCMHTLSTRATSISTQLPDDPAKTTMKKAYYLACGFCRWTSRDVGMADKSVASGGWQEPENPHTQRMNKLIEYYQQLAQKEKVERDRKKLARRRNYMPLAFSDKYGLGTRLQRPRAGASISTLAGLSLKEGEDQKEIKIEPAQAVDEVEPLPEDYYTRPVNLTEVTTLQQRLLQPDFQPVCASQLYPRHKHLLIKRSLRCRKCEHNLSKPEFNPTSIKFKIQLVAVNYIPEVRIMSIPNLRYMKESQVLLTLTNPVENLTHVTLFECEEGDPDDINSTAKVVVPPKELVLAGKDAAAEYDELAEPQDFQDDPDIIAFRKANKVGIFIKVTPQREEGEVTVCFKMKHDFKNLAAPIRPIEESDQGTEVIWLTQHVELSLGPLLP,Dynactin subunit 4,Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules.,The mutation in ATP7B affects the copper-induced trafficking pathway that delivers ATP7B to subapical vesicles of hepatocytes for the removal of excess copper into bile.,"Loss of ATP7B-binding; when associated with S-30; S-33; S-51; S-54, S-70; S-73; S-76; S-111; S-114; S-277 and S-280. The mutation in ATP7B affects the copper-induced trafficking pathway that delivers ATP7B to subapical vesicles of hepatocytes for the removal of excess copper into bile."
1847,1847,1847,139537,Q9X005-T21A,MKKVIGIGEYAVMKNPGVIVALGLGSCVAVCMRDPVAKVGAMAHVMLPDSGGKTDKPGKYADTAVKTLVEELKKMGAKVERLEAKIAGGASMFESKGMNIGARNVEAVKKHLKDFGIKLLAEDTGGNRARSVEYNIETGKLLVRKVGGGEQLEIKEI,6-fold reduction in activity.,,MKKVIGIGEYAVMKNPGVIVTLGLGSCVAVCMRDPVAKVGAMAHVMLPDSGGKTDKPGKYADTAVKTLVEELKKMGAKVERLEAKIAGGASMFESKGMNIGARNVEAVKKHLKDFGIKLLAEDTGGNRARSVEYNIETGKLLVRKVGGGEQLEIKEI,Chemoreceptor glutamine deamidase CheD,"Deamidates glutamine residues on chemoreceptors (MCPs). CheD-mediated MCP deamidation is required for productive communication of the conformational signals of the chemoreceptors to the CheA kinase. In addition, demethylates methylated glutamate residues on chemoreceptors Mcp2 and Mcp4. Enhances the activity of CheC.",,6-fold reduction in activity.
1852,1852,1852,140064,P73069-R196E,MPVKFPSLKFEQLKQLVLVAAIAVFCVSCSHVPDLAFNPWQEIALETDSTFADIAFTEDPNHGWLVGTKETIFETTDGGDTWEQKLIDLGEEKASFSAVSFSGNEGWITGKPSILLHTTDGGQTWARIPLSEKLPGAPYSIIALGPQTAEMITDLGAIYKTTNGGKNWKALVEGAVGVARTIQRSTDGRYVAVSAEGNFYSTWAPGQTEWTPHNRNSSRRLQTMGYGKDGQLWLLARGGQLQFSTDPDAEEWSDVIAPQDKGSWGLLDLSFRTPEEVWVAGASGNLLMSQDGGQTWAKDTGVEDIPANLYRVVFLSPEKGFVLGQDGILLKYNPSTEVAMVP,No visible phenotype.,,MPVKFPSLKFEQLKQLVLVAAIAVFCVSCSHVPDLAFNPWQEIALETDSTFADIAFTEDPNHGWLVGTKETIFETTDGGDTWEQKLIDLGEEKASFSAVSFSGNEGWITGKPSILLHTTDGGQTWARIPLSEKLPGAPYSIIALGPQTAEMITDLGAIYKTTNGGKNWKALVEGAVGVARTIQRSTDGRYVAVSARGNFYSTWAPGQTEWTPHNRNSSRRLQTMGYGKDGQLWLLARGGQLQFSTDPDAEEWSDVIAPQDKGSWGLLDLSFRTPEEVWVAGASGNLLMSQDGGQTWAKDTGVEDIPANLYRVVFLSPEKGFVLGQDGILLKYNPSTEVAMVP,Photosystem II assembly lipoprotein Ycf48,"A factor required for optimal assembly of photosystem II (PSII) which acts in the early stages of PSII assembly. Also plays a role in replacement of photodamaged D1 (psbA). May interact with precursor D1 to prevent its premature processing before association with D2 (psbD)  (Probable). May also play a role in chlorophyll insertion into chlorophyll-binding proteins  (Probable). Increasing levels of chlorophyll precursors partially suppresses deletion of this protein, supporting the idea that Ycf48 assists YidC in synthesis of chlorophyll-binding proteins.",,No visible phenotype.
1857,1857,1857,140409,P51667-S15A,MAPKKAKKRIEGGSANVFSMFEQTQIQEFKEAFTIMDQNRDGFIDKNDLRDTFAALGRVNVKNEEIDEMIKEAPGPINFTVFLTMFGEKLKGADPEETILNAFKVFDPEGKGSLKADYVREMLTTQAERFSKEEIDQMFAAFPPDVTGNLDYKNLVHIITHGEEKD,"Loss of cardiac myofibril assembly; when associated with A-14 and A-19. Loss of phosphorylation; when associated with A-14 and A-19. Loss of calcium sensitivity of force development; when associated with A-14 and A-19. Increase of phosphorylation. Phosphorylation at Ser-14 and at Ser-19. Phosphorylation at Ser-19; when associated with A-14. Significant decrease in phosphorylation by MLCK; when associated with A-14. Adult lethality associated with early defects in cardiac twitch relaxation and torsion leading to dilated cardiomyopathy, heart failure and premature death; when associated with A-14. Significant acceleration of twitch relaxation in absence of changes in calcium transients; when associated with A-14. Absence of transmural phosphorylation gradient leading to alteration of torsion; when associated with A-14.",,MAPKKAKKRIEGGSSNVFSMFEQTQIQEFKEAFTIMDQNRDGFIDKNDLRDTFAALGRVNVKNEEIDEMIKEAPGPINFTVFLTMFGEKLKGADPEETILNAFKVFDPEGKGSLKADYVREMLTTQAERFSKEEIDQMFAAFPPDVTGNLDYKNLVHIITHGEEKD,"Myosin regulatory light chain 2, ventricular/cardiac muscle isoform","Contractile protein that plays a role in heart development and function. Following phosphorylation, plays a role in cross-bridge cycling kinetics and cardiac muscle contraction by increasing myosin lever arm stiffness and promoting myosin head diffusion; as a consequence of the increase in maximum contraction force and calcium sensitivity of contraction force. These events altogether slow down myosin kinetics and prolong duty cycle resulting in accumulated myosins being cooperatively recruited to actin binding sites to sustain thin filament activation as a means to fine-tune myofilament calcium sensitivity to force. During cardiogenesis plays an early role in cardiac contractility by promoting cardiac myofibril assembly.","Changing the phosphorylation status of the S15 site in the ventricular isoform of the regulatory myosin light chain alters cardiac function in the whole animal. The mice with the mutation show a spectrum of cardiovascular changes, including atrial hypertrophy and dilatation. Echocardiographic analysis revealed severe tricuspid valve insufficiency resulting in a detectable regurgitation jet. Loss of Mlc2v phosphorylation affects cardiac myosin cycling kinetics and actin-myosin interactions. It also influences calcium-dependent activation of the thin filament. Loss of these mechanisms leads to early defects in cardiac muscle twitch relaxation and ventricular torsion.","Loss of cardiac myofibril assembly; when associated with A-14 and A-19. Loss of phosphorylation; when associated with A-14 and A-19. Loss of calcium sensitivity of force development; when associated with A-14 and A-19. Increase of phosphorylation. Phosphorylation at Ser-14 and at Ser-19. Phosphorylation at Ser-19; when associated with A-14. Significant decrease in phosphorylation by MLCK; when associated with A-14. Adult lethality associated with early defects in cardiac twitch relaxation and torsion leading to dilated cardiomyopathy, heart failure and premature death; when associated with A-14. Significant acceleration of twitch relaxation in absence of changes in calcium transients; when associated with A-14. Absence of transmural phosphorylation gradient leading to alteration of torsion; when associated with A-14. Changing the phosphorylation status of the S15 site in the ventricular isoform of the regulatory myosin light chain alters cardiac function in the whole animal. The mice with the mutation show a spectrum of cardiovascular changes, including atrial hypertrophy and dilatation. Echocardiographic analysis revealed severe tricuspid valve insufficiency resulting in a detectable regurgitation jet. Loss of Mlc2v phosphorylation affects cardiac myosin cycling kinetics and actin-myosin interactions. It also influences calcium-dependent activation of the thin filament. Loss of these mechanisms leads to early defects in cardiac muscle twitch relaxation and ventricular torsion."
1862,1862,1862,141163,Q8NFU5-Q164R,MATEPPSPLRVEAPGPPEMRTSPAIESTPEGTPQPAGGRLRFLNGCVPLSHQVAGHMYGKDKVGILQHPDGTVLKQLQPPPRGPRELEFYNMVYAADCFDGVLLELRKYLPKYYGIWSPPTAPNDLYLKLEDVTHKFNKPCIMDVKIGQKSYDPFASSEKIQQRVSKYPLMEEIGFLVLGMRVYHVHSDSYETENQHYGRSLTKETIKDGVSRFFHNGYCLRKDAVAASIQKIEKILQWFENQKQLNFYASSLLFVYEGSSQPTTTKLNDRTLAEKFLSKGQLSDTEVLEYNNNFHVLSSTANGKIESSVGKSLSKMYARHRKIYTKKHHSQTSLKVENLEQDNGWKSMSQEHLNGNVLSQLEKVFYHLPTGCQEIAEVEVRMIDFAHVFPSNTIDEGYVYGLKHLISVLRSILDN,"Decreased activity with inositol 1,4,5-trisphosphate. Increased phosphorylation of inositol 1,3,4,5-tetrakisphosphate.",,MATEPPSPLRVEAPGPPEMRTSPAIESTPEGTPQPAGGRLRFLNGCVPLSHQVAGHMYGKDKVGILQHPDGTVLKQLQPPPRGPRELEFYNMVYAADCFDGVLLELRKYLPKYYGIWSPPTAPNDLYLKLEDVTHKFNKPCIMDVKIGQKSYDPFASSEKIQQQVSKYPLMEEIGFLVLGMRVYHVHSDSYETENQHYGRSLTKETIKDGVSRFFHNGYCLRKDAVAASIQKIEKILQWFENQKQLNFYASSLLFVYEGSSQPTTTKLNDRTLAEKFLSKGQLSDTEVLEYNNNFHVLSSTANGKIESSVGKSLSKMYARHRKIYTKKHHSQTSLKVENLEQDNGWKSMSQEHLNGNVLSQLEKVFYHLPTGCQEIAEVEVRMIDFAHVFPSNTIDEGYVYGLKHLISVLRSILDN,Inositol polyphosphate multikinase,"Inositol phosphate kinase with a broad substrate specificity. Phosphorylates inositol 1,4,5-trisphosphate (Ins(1,4,5)P3) first to inositol 1,3,4,5-tetrakisphosphate and then to inositol 1,3,4,5,6-pentakisphosphate (Ins(1,3,4,5,6)P5). Phosphorylates inositol 1,3,4,6-tetrakisphosphate (Ins(1,3,4,6)P4). Phosphorylates glycero-3-phospho-1D-myo-inositol 4,5-bisphosphate to glycero-3-phospho-1D-myo-inositol 3,4,5-trisphosphate. Plays an important role in MLKL-mediated necroptosis via its role in the biosynthesis of inositol pentakisphosphate (InsP5) and inositol hexakisphosphate (InsP6). Binding of these highly phosphorylated inositol phosphates to MLKL mediates the release of an N-terminal auto-inhibitory region, leading to activation of the kinase. Essential for activated phospho-MLKL to oligomerize and localize to the cell membrane during necroptosis. Required for normal embryonic development, probably via its role in the biosynthesis of inositol 1,3,4,5,6-pentakisphosphate (Ins(1,3,4,5,6)P5) and inositol hexakisphosphate (InsP6).",,"Decreased activity with inositol 1,4,5-trisphosphate. Increased phosphorylation of inositol 1,3,4,5-tetrakisphosphate."
1879,1879,1879,142839,O76082-T264M,MRDYDEVTAFLGEWGPFQRLIFFLLSASIIPNGFTGLSSVFLIATPEHRCRVPDAANLSSAWRNHTVPLRLRDGREVPHSCRRYRLATIANFSALGLEPGRDVDLGQLEQESCLDGWEFSQDVYLSTIVTEWNLVCEDDWKAPLTISLFFVGVLLGSFISGQLSDRFGRKNVLFVTMGMQTGFSFLQIFSKNFEMFVVLFVLVGMGQISNYVAAFVLGTEILGKSVRIIFSTLGVCIFYAFGYMVLPLFAYFIRDWRMLLVALMMPGVLCVALWWFIPESPRWLISQGRFEEAEVIIRKAAKANGIVVPSTIFDPSELQDLSSKKQQSHNILDLLRTWNIRMVTIMSIMLWMTISVGYFGLSLDTPNLHGDIFVNCFLSAMVEVPAYVLAWLLLQYLPRRYSMATALFLGGSVLLFMQLVPPDLYYLATVLVMVGKFGVTAAFSMVYVYTAELYPTVVRNMGVGVSSTASRLGSILSPYFVYLGAYDRFLPYILMGSLTILTAILTLFLPESFGTPLPDTIDQMLRVKGMKHRKTPSHTRMLKDGQERPTILKSTAF,In CDSP; unknown pathological significance; reduces carnitine transport but the mutant retains more than 40% of wild-type activity.,,MRDYDEVTAFLGEWGPFQRLIFFLLSASIIPNGFTGLSSVFLIATPEHRCRVPDAANLSSAWRNHTVPLRLRDGREVPHSCRRYRLATIANFSALGLEPGRDVDLGQLEQESCLDGWEFSQDVYLSTIVTEWNLVCEDDWKAPLTISLFFVGVLLGSFISGQLSDRFGRKNVLFVTMGMQTGFSFLQIFSKNFEMFVVLFVLVGMGQISNYVAAFVLGTEILGKSVRIIFSTLGVCIFYAFGYMVLPLFAYFIRDWRMLLVALTMPGVLCVALWWFIPESPRWLISQGRFEEAEVIIRKAAKANGIVVPSTIFDPSELQDLSSKKQQSHNILDLLRTWNIRMVTIMSIMLWMTISVGYFGLSLDTPNLHGDIFVNCFLSAMVEVPAYVLAWLLLQYLPRRYSMATALFLGGSVLLFMQLVPPDLYYLATVLVMVGKFGVTAAFSMVYVYTAELYPTVVRNMGVGVSSTASRLGSILSPYFVYLGAYDRFLPYILMGSLTILTAILTLFLPESFGTPLPDTIDQMLRVKGMKHRKTPSHTRMLKDGQERPTILKSTAF,Organic cation/carnitine transporter 2,"Sodium-ion dependent, high affinity carnitine transporter. Involved in the active cellular uptake of carnitine. Transports one sodium ion with one molecule of carnitine. Also transports organic cations such as tetraethylammonium (TEA) without the involvement of sodium. Relative uptake activity ratio of carnitine to TEA is 11.3. In intestinal epithelia, transports the quorum-sensing pentapeptide CSF (competence and sporulation factor) from Bacillus Subtilis wich induces cytoprotective heat shock proteins contributing to intestinal homeostasis. May also contribute to regulate the transport of organic compounds in testis across the blood-testis-barrier (Probable).Retained in the ER, unable to perform carnitine uptake.",,In CDSP; unknown pathological significance; reduces carnitine transport but the mutant retains more than 40% of wild-type activity.
1887,1887,1887,143644,P62979-S65D,MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKEDTLHLVLRLRGGAKKRKKKSYTTPKKNKHKRKKVKLAVLKYYKVDENGKISRLRRECPSDECGAGVFMASHFDRHYCGKCCLTYCFNKPEDK,Phosphomimetic mutant that binds and activates PRKN.,,MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGAKKRKKKSYTTPKKNKHKRKKVKLAVLKYYKVDENGKISRLRRECPSDECGAGVFMASHFDRHYCGKCCLTYCFNKPEDK,Ubiquitin-ribosomal protein eS31 fusion protein,"[Ubiquitin]: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in proteotoxic stress response and cell cycle; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.",,Phosphomimetic mutant that binds and activates PRKN.
1890,1890,1890,143804,Q9Z0J1-Q68A,MASVRASPRSALLLLLAAAGVAEVTGGLAPGSAGAVCCNHSKDNQMCRDVCEQIFSSKSESRLKHLLARAPDYCPETMVEIWSCMNSSLPGVFKKSDGWVGLGCCELAIGLECRQACKQASSKNDISKVCRKEYENALFSCISRNEMGSVCCSYAGHHTNCREFCQAIFRTDSSPGPSQIKAVENYCASISPQLIHCVNNYTQSYPMRNPTDSLYCCDRAEDHACQNACKRILMSKKTEMEIVDGLIEGCKTQPLPQDPLWQCFLESSQSVHPGVTVHPPPSTGLDGAKLHCCSKANTSTCRELCTKLYSMSWGNTQSWQEFDRICEYNPVEVSMLTCLADVREPCQLGCTNLTYCTNFNNRPTELFRSCTAQSDQGAMSDMKLWEKGSIKMPFISIPVLDIKTCQPEMWKAVACSLQIKPCHSKSRGSIICKSDCVEILKKCGDQNKFPEEHTAESICEFLSPADDLESCIPLDTYLRPSALGNIIEEVTHPCNPNPCPANELCEVNRKGCPSADPCLPYSCVQGCKLGEASDFIVRQGTLIQVPSSAGEVGCYKICSCGQSGLLENCMEMHCIDLQKSCIVGGKRKSHGTSFTIDCNVCSCFAGNLVCSTRLCLSEHSSDDDRRTFTGLPCNCADQFVPVCAQNGRTYPSACIARCVGLQDHQFEFGPCISKNPCNPNLCPKSQRCVPKPQVCLTTFDKFGCSQYECVPRQLTCDQARDPVCDTDHMEHSNLCTLYQRGKSLSYRGPCQPFCRAKEPVCGHNGETYSSVCAAYSDRVAVDYYGPCQAVGVLSEYSAVAECAAVKCPSLSAIGCKPIIPPGACCPLCAGMLRVLFDKEKLDTIAKVTSKKPITVVEILQKVRMHVSVPQCDVFGYLSIESEIVILIIPVDHYPKALQIEACNKEAEKIESLINSDSPTLASHVPLSALIISQVQVSSSLPSSAVVGRPLFHSLLLLLSLGLTVHLLWTRP,Does not affect interaction with ADGRA2.,,MASVRASPRSALLLLLAAAGVAEVTGGLAPGSAGAVCCNHSKDNQMCRDVCEQIFSSKSESRLKHLLQRAPDYCPETMVEIWSCMNSSLPGVFKKSDGWVGLGCCELAIGLECRQACKQASSKNDISKVCRKEYENALFSCISRNEMGSVCCSYAGHHTNCREFCQAIFRTDSSPGPSQIKAVENYCASISPQLIHCVNNYTQSYPMRNPTDSLYCCDRAEDHACQNACKRILMSKKTEMEIVDGLIEGCKTQPLPQDPLWQCFLESSQSVHPGVTVHPPPSTGLDGAKLHCCSKANTSTCRELCTKLYSMSWGNTQSWQEFDRICEYNPVEVSMLTCLADVREPCQLGCTNLTYCTNFNNRPTELFRSCTAQSDQGAMSDMKLWEKGSIKMPFISIPVLDIKTCQPEMWKAVACSLQIKPCHSKSRGSIICKSDCVEILKKCGDQNKFPEEHTAESICEFLSPADDLESCIPLDTYLRPSALGNIIEEVTHPCNPNPCPANELCEVNRKGCPSADPCLPYSCVQGCKLGEASDFIVRQGTLIQVPSSAGEVGCYKICSCGQSGLLENCMEMHCIDLQKSCIVGGKRKSHGTSFTIDCNVCSCFAGNLVCSTRLCLSEHSSDDDRRTFTGLPCNCADQFVPVCAQNGRTYPSACIARCVGLQDHQFEFGPCISKNPCNPNLCPKSQRCVPKPQVCLTTFDKFGCSQYECVPRQLTCDQARDPVCDTDHMEHSNLCTLYQRGKSLSYRGPCQPFCRAKEPVCGHNGETYSSVCAAYSDRVAVDYYGPCQAVGVLSEYSAVAECAAVKCPSLSAIGCKPIIPPGACCPLCAGMLRVLFDKEKLDTIAKVTSKKPITVVEILQKVRMHVSVPQCDVFGYLSIESEIVILIIPVDHYPKALQIEACNKEAEKIESLINSDSPTLASHVPLSALIISQVQVSSSLPSSAVVGRPLFHSLLLLLSLGLTVHLLWTRP,Reversion-inducing cysteine-rich protein with Kazal motifs,"Functions together with ADGRA2 to enable brain endothelial cells to selectively respond to Wnt7 signals (WNT7A or WNT7B). Plays a key role in Wnt7-specific responses: required for central nervous system (CNS) angiogenesis and blood-brain barrier regulation. Acts as a Wnt7-specific coactivator of canonical Wnt signaling by decoding Wnt ligands: acts by interacting specifically with the disordered linker region of Wnt7, thereby conferring ligand selectivity for Wnt7. ADGRA2 is then required to deliver RECK-bound Wnt7 to frizzled by assembling a higher-order RECK-ADGRA2-Fzd-LRP5-LRP6 complex. Also acts as a serine protease inhibitor: negatively regulates matrix metalloproteinase-9 (MMP9) by suppressing MMP9 secretion and by direct inhibition of its enzymatic activity. Also inhibits metalloproteinase activity of MMP2 and MMP14 (MT1-MMP).",The mutation in Gpr124 weakens the interaction with Reck and impairs CNS angiogenesis.,Does not affect interaction with ADGRA2. The mutation in Gpr124 weakens the interaction with Reck and impairs CNS angiogenesis.
1897,1897,1897,144031,P0A1C7-S40M,MQQEALGMVETKGLTAAIEAADAMVKSANVMLVGYEKIGMGLVTVIVRGDVGAVKAATDAGAAAARNVGEVKAVHVIPRPHTDVEKILPKGISQ,"No change in shell permeability, wild-type growth on 1,2-PD.",,MQQEALGMVETKGLTAAIEAADAMVKSANVMLVGYEKIGSGLVTVIVRGDVGAVKAATDAGAAAARNVGEVKAVHVIPRPHTDVEKILPKGISQ,Bacterial microcompartment shell protein PduA,"One of the major shell proteins of the bacterial microcompartment (BMC) dedicated to 1,2-propanediol (1,2-PD) degradation  (Probable). At least one of PduA or PduJ is required for BMC assembly; it must be encoded as the first gene in the pdu operon. Not required for structural integrity of BMCs, it is required to mitigate propionaldehyde toxicity. Controls diffusion of 1,2-PD into and propionaldehyde out of the BMC shell; residue 40 is particularly important for pore permeability  (Probable). Overexpression of this protein leads to aberrant filaments that extend the length of the cell, cross the cleavage furrow and impair division. The filaments form nanotubes with a hollow center. The isolated BMC shell component protein ratio for J:A:B':B:K:T:U is approximately 15:10:7:6:1:1:2. Edge residues (particularly Lys-26) are important for function and assembly of the BMC, and influence array formation by hexamers. Interaction with PduA allows encapsulation of at least PduP in BMCs. Probably also targets PduD to the BMC (Probable). PduA is probably the hub for binding multiple enzymes to the interior of the BMC; modeling suggests PduC, PduD, PduE, PduG, PduL and PduP are targeted to PduA (Probable).",,"No change in shell permeability, wild-type growth on 1,2-PD."
1919,1919,1919,145977,Q9XB60-M108A,MVFEENSDEVRVITLDHPNKHNPFSRTLETSVKDALARANADDSVRAVVVYGGAERSFSAGGDFNEVKQLSRSEDIEEWIDRVIDLYQAVLNVNKPTIAAVDGYAIGAGFQFALMFDQRLMASTANFVMPELKHGIGCSVGAAILGFTHGFSTMQEIIYQCQSLDAPRCVDYRLVNQVVESSALLDAAITQAHVMASYPASAFINTKRAVNKPFIHLLEQTRDASKAVHKAAFQARDAQGHFKNVLGKKY,Forms the C6 epimers of 6-methyl-t-CMP in 45:55 ratio of (6R):(6S) epimers.,,MVFEENSDEVRVITLDHPNKHNPFSRTLETSVKDALARANADDSVRAVVVYGGAERSFSAGGDFNEVKQLSRSEDIEEWIDRVIDLYQAVLNVNKPTIAAVDGYAIGMGFQFALMFDQRLMASTANFVMPELKHGIGCSVGAAILGFTHGFSTMQEIIYQCQSLDAPRCVDYRLVNQVVESSALLDAAITQAHVMASYPASAFINTKRAVNKPFIHLLEQTRDASKAVHKAAFQARDAQGHFKNVLGKKY,Carboxymethylproline synthase,"Catalyzes the formation of (2S,5S)-carboxymethylproline (t-CMP) from malonyl-CoA and (S)-1-pyrroline-5-carboxylate, the first step in the biosynthesis of (5R)-carbapen-2-em-3-carboxylate, a beta-lactam antibiotic of the carbapenem class. Also catalyzes the independent decarboxylation of malonyl-CoA and methylmalonyl-CoA and the hydrolysis of CoA esters such as acetyl-CoA and propionyl-CoA. Catalyzes the reaction with a C2 epimeric mixture of methylmalonyl-CoA to give a 55:45 mixture of (6R)- and (6S)-epimers of 6-methyl-t-CMP, under standard incubation conditions.",,Forms the C6 epimers of 6-methyl-t-CMP in 45:55 ratio of (6R):(6S) epimers.
1949,1949,1949,148079,Q9FE20-S244F,MGCFSCFDSSDDEKLNPVDESNHGQKKQSQPTVSNNISGLPSGGEKLSSKTNGGSKRELLLPRDGLGQIAAHTFAFRELAAATMNFHPDTFLGEGGFGRVYKGRLDSTGQVVAVKQLDRNGLQGNREFLVEVLMLSLLHHPNLVNLIGYCADGDQRLLVYEFMPLGSLEDHLHDLPPDKEALDWNMRMKIAAGAAKGLEFLHDKANPPVIYRDFKSSNILLDEGFHPKLSDFGLAKLGPTGDKFHVSTRVMGTYGYCAPEYAMTGQLTVKSDVYSFGVVFLELITGRKAIDSEMPHGEQNLVAWARPLFNDRRKFIKLADPRLKGRFPTRALYQALAVASMCIQEQAATRPLIADVVTALSYLANQAYDPSKDDSRRNRDERGARLITRNDDGGGSGSKFDLEGSEKEDSPRETARILNRDINRERAVAEAKMWGESLREKRRQSEQGTSESNSTG,In pbs1-6; strongly impairs RPS5-mediated plant resistance to P.syringae.,,MGCFSCFDSSDDEKLNPVDESNHGQKKQSQPTVSNNISGLPSGGEKLSSKTNGGSKRELLLPRDGLGQIAAHTFAFRELAAATMNFHPDTFLGEGGFGRVYKGRLDSTGQVVAVKQLDRNGLQGNREFLVEVLMLSLLHHPNLVNLIGYCADGDQRLLVYEFMPLGSLEDHLHDLPPDKEALDWNMRMKIAAGAAKGLEFLHDKANPPVIYRDFKSSNILLDEGFHPKLSDFGLAKLGPTGDKSHVSTRVMGTYGYCAPEYAMTGQLTVKSDVYSFGVVFLELITGRKAIDSEMPHGEQNLVAWARPLFNDRRKFIKLADPRLKGRFPTRALYQALAVASMCIQEQAATRPLIADVVTALSYLANQAYDPSKDDSRRNRDERGARLITRNDDGGGSGSKFDLEGSEKEDSPRETARILNRDINRERAVAEAKMWGESLREKRRQSEQGTSESNSTG,Serine/threonine-protein kinase PBS1,"Protein kinase required for plant defense mechanism mediated by the disease resistance (R) protein RPS5. In case of infection by Pseudomonas syringae, AvrPphB triggers RPS5-mediated defense mechanism via the cleavage of PBS1. Both kinase activity and cleavage by avrPphB are independently required to trigger the RPS5-mediated resistance. Contributes to PAMP-triggered immunity (PTI) signaling and defense responses downstream of FLS2.",,In pbs1-6; strongly impairs RPS5-mediated plant resistance to P.syringae.
1958,1958,1958,148323,Q9FFF6-L142A,MNKNKIDVKIETKKGSMDEWPEPIVRVQSLAESNLSSLPDRYIKPASLRPTTTEDAPTATNIPIIDLEGLFSEEGLSDDVIMARISEACRGWGFFQVVNHGVKPELMDAARENWREFFHMPVNAKETYSNSPRTYEGYGSRAGVEKGASLDWSDYYFLHLLPHHLKDFNKWPSFPPTIREVIDEYGEELVKLSGRIMRVLSTNLGLKEDKFQEAFGGENIGACLRVNYYPKCPRPELALGLSPHSDPGGMTILLPDDQVFGLQVRKDDTWITVKPHPHAFIVNIGDQIQILSNSTYKSVEHRVIVNSDKERVSLAFFYNPKSDIPIQPLQELVSTHNPPLYPPMTFDQYRLFIRTQGPQGKSHVESHISPR,Reduces enzymatic activity 5-fold.,,MNKNKIDVKIETKKGSMDEWPEPIVRVQSLAESNLSSLPDRYIKPASLRPTTTEDAPTATNIPIIDLEGLFSEEGLSDDVIMARISEACRGWGFFQVVNHGVKPELMDAARENWREFFHMPVNAKETYSNSPRTYEGYGSRLGVEKGASLDWSDYYFLHLLPHHLKDFNKWPSFPPTIREVIDEYGEELVKLSGRIMRVLSTNLGLKEDKFQEAFGGENIGACLRVNYYPKCPRPELALGLSPHSDPGGMTILLPDDQVFGLQVRKDDTWITVKPHPHAFIVNIGDQIQILSNSTYKSVEHRVIVNSDKERVSLAFFYNPKSDIPIQPLQELVSTHNPPLYPPMTFDQYRLFIRTQGPQGKSHVESHISPR,Jasmonate-induced oxygenase 2,"2-oxoglutarate-dependent dioxygenase involved in the oxidation of jasmonate (JA), a stress-induced phytohormone synthesized in response to attack by pathogens and herbivores, which triggers the activation of defense responses via the JA-mediated signaling pathway. Converts JA to 12-hydroxyjasmonate (12OH-JA), an inactive form of JA. Is specific to free JA, and cannot oxidize the bioactive form jasmonoyl-L-isoleucine (JA-Ile) or other JA-amino acid conjugates. Prevents over-accumulation of JA and indirectly its bioactive form JA-Ile under stress response. Acts as negative regulator of JA-mediated defense signaling, by contributing to 12OH-JA accumulation, which represses JA defense responses upon infection by the fungal pathogen Botrytis cinerea. Acts as negative regulator of JA-mediated defense responses upon infestation by the herbivorous caterpillar Mamestra brassicae. May be involved in the catabolism of cytotoxic polycyclic aromatic hydrocarbons (PAHs).",,Reduces enzymatic activity 5-fold.
1960,1960,1960,148475,P46379-W1018A,MEPNDSTSTAVEEPDSLEVLVKTLDSQTRTFIVGAQMNVKEFKEHIAASVSIPSEKQRLIYQGRVLQDDKKLQEYNVGGKVIHLVERAPPQTHLPSGASSGTGSASATHGGGSPPGTRGPGASVHDRNANSYVMVGTFNLPSDGSAVDVHINMEQAPIQSEPRVRLVMAQHMIRDIQTLLSRMETLPYLQCRGGPQPQHSQPPPQPPAVTPEPVALSSQTSEPVESEAPPREPMEAEEVEERAPAQNPELTPGPAPAGPTPAPETNAPNHPSPAEYVEVLQELQRLESRLQPFLQRYYEVLGAAATTDYNNNHEGREEDQRLINLVGESLRLLGNTFVALSDLRCNLACTPPRHLHVVRPMSHYTTPMVLQQAAIPIQINVGTTVTMTGNGTRPPPTPNAEAPPPGPGQASSVAPSSTNVESSAEGAPPPGPAPPPATSHPRVIRISHQSVEPVVMMHMNIQDSGTQPGGVPSAPTGPLGPPGHGQTLGQQVPGFPTAPTRVVIARPTPPQARPSHPGGPPVSGTLQGAGLGTNASLAQMVSGLVGQLLMQPVLVAQGTPGMAPPPAPATASASAGTTNTATTAGPAPGGPAQPPPTPQPSMADLQFSQLLGNLLGPAGPGAGGSGVASPTITVAMPGVPAFLQGMTDFLQATQTAPPPPPPPPPPPPAPEQQTMPPPGSPSGGAGSPGGLGLESLSPEFFTSVVQGVLSSLLGSLGARAGSSESIAAFIQRLSGSSNIFEPGADGALGFFGALLSLLCQNFSMVDVVMLLHGHFQPLQRLQPQLRSFFHQHYLGGQEPTPSNIRMATHTLITGLEEYVRESFSLVQVQPGVDIIRTNLEFLQEQFNSIAAHVLHCTDSGFGARLLELCNQGLFECLALNLHCLGGQQMELAAVINGRIRRMSRGVNPSLVSWLTTMMGLRLQVVLEHMPVGPDAILRYVRRVGDPPQPLPEEPMEVQGAERASPEPQRENASPAPGTTAEEAMSRGPPPAPEGGSRDEQDGASAETEPWAAAVPPEAVPIIQQ,"Decreases interaction with GET4. Localizes in the nucleus. Decreases interaction with GET4, localizes in the nucleus and increases GET4 ubiquitination; when associated with A-1042.",,MEPNDSTSTAVEEPDSLEVLVKTLDSQTRTFIVGAQMNVKEFKEHIAASVSIPSEKQRLIYQGRVLQDDKKLQEYNVGGKVIHLVERAPPQTHLPSGASSGTGSASATHGGGSPPGTRGPGASVHDRNANSYVMVGTFNLPSDGSAVDVHINMEQAPIQSEPRVRLVMAQHMIRDIQTLLSRMETLPYLQCRGGPQPQHSQPPPQPPAVTPEPVALSSQTSEPVESEAPPREPMEAEEVEERAPAQNPELTPGPAPAGPTPAPETNAPNHPSPAEYVEVLQELQRLESRLQPFLQRYYEVLGAAATTDYNNNHEGREEDQRLINLVGESLRLLGNTFVALSDLRCNLACTPPRHLHVVRPMSHYTTPMVLQQAAIPIQINVGTTVTMTGNGTRPPPTPNAEAPPPGPGQASSVAPSSTNVESSAEGAPPPGPAPPPATSHPRVIRISHQSVEPVVMMHMNIQDSGTQPGGVPSAPTGPLGPPGHGQTLGQQVPGFPTAPTRVVIARPTPPQARPSHPGGPPVSGTLQGAGLGTNASLAQMVSGLVGQLLMQPVLVAQGTPGMAPPPAPATASASAGTTNTATTAGPAPGGPAQPPPTPQPSMADLQFSQLLGNLLGPAGPGAGGSGVASPTITVAMPGVPAFLQGMTDFLQATQTAPPPPPPPPPPPPAPEQQTMPPPGSPSGGAGSPGGLGLESLSPEFFTSVVQGVLSSLLGSLGARAGSSESIAAFIQRLSGSSNIFEPGADGALGFFGALLSLLCQNFSMVDVVMLLHGHFQPLQRLQPQLRSFFHQHYLGGQEPTPSNIRMATHTLITGLEEYVRESFSLVQVQPGVDIIRTNLEFLQEQFNSIAAHVLHCTDSGFGARLLELCNQGLFECLALNLHCLGGQQMELAAVINGRIRRMSRGVNPSLVSWLTTMMGLRLQVVLEHMPVGPDAILRYVRRVGDPPQPLPEEPMEVQGAERASPEPQRENASPAPGTTAEEAMSRGPPPAPEGGSRDEQDGASAETEPWAAAVPPEWVPIIQQ,Large proline-rich protein BAG6,"ATP-independent molecular chaperone preventing the aggregation of misfolded and hydrophobic patches-containing proteins. Functions as part of a cytosolic protein quality control complex, the BAG6/BAT3 complex, which maintains these client proteins in a soluble state and participates in their proper delivery to the endoplasmic reticulum or alternatively can promote their sorting to the proteasome where they undergo degradation. The BAG6/BAT3 complex is involved in the post-translational delivery of tail-anchored/type II transmembrane proteins to the endoplasmic reticulum membrane. Recruited to ribosomes, it interacts with the transmembrane region of newly synthesized tail-anchored proteins and together with SGTA and ASNA1 mediates their delivery to the endoplasmic reticulum. Client proteins that cannot be properly delivered to the endoplasmic reticulum are ubiquitinated by RNF126, an E3 ubiquitin-protein ligase associated with BAG6 and are sorted to the proteasome. SGTA which prevents the recruitment of RNF126 to BAG6 may negatively regulate the ubiquitination and the proteasomal degradation of client proteins. Similarly, the BAG6/BAT3 complex also functions as a sorting platform for proteins of the secretory pathway that are mislocalized to the cytosol either delivering them to the proteasome for degradation or to the endoplasmic reticulum. The BAG6/BAT3 complex also plays a role in the endoplasmic reticulum-associated degradation (ERAD), a quality control mechanism that eliminates unwanted proteins of the endoplasmic reticulum through their retrotranslocation to the cytosol and their targeting to the proteasome. It maintains these retrotranslocated proteins in an unfolded yet soluble state condition in the cytosol to ensure their proper delivery to the proteasome. BAG6 is also required for selective ubiquitin-mediated degradation of defective nascent chain polypeptides by the proteasome. In this context, it may participate in the production of antigenic peptides and play a role in antigen presentation in immune response. BAG6 is also involved in endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for proteasomal degradation. BAG6 may ensure the proper degradation of these proteins and thereby protects the endoplasmic reticulum from protein overload upon stress. By inhibiting the polyubiquitination and subsequent proteasomal degradation of HSPA2 it may also play a role in the assembly of the synaptonemal complex during spermatogenesis. Also positively regulates apoptosis by interacting with and stabilizing the proapoptotic factor AIFM1. By controlling the steady-state expression of the IGF1R receptor, indirectly regulates the insulin-like growth factor receptor signaling pathway.Involved in DNA damage-induced apoptosis: following DNA damage, accumulates in the nucleus and forms a complex with p300/EP300, enhancing p300/EP300-mediated p53/TP53 acetylation leading to increase p53/TP53 transcriptional activity. When nuclear, may also act as a component of some chromatin regulator complex that regulates histone 3 'Lys-4' dimethylation (H3K4me2).Released extracellularly via exosomes, it is a ligand of the natural killer/NK cells receptor NCR3 and stimulates NK cells cytotoxicity. It may thereby trigger NK cells cytotoxicity against neighboring tumor cells and immature myeloid dendritic cells (DC).Mediates ricin-induced apoptosis.",,"Decreases interaction with GET4. Localizes in the nucleus. Decreases interaction with GET4, localizes in the nucleus and increases GET4 ubiquitination; when associated with A-1042."
1962,1962,1962,149007,Q9NRG4-D252R,MRAEGLGGLERFCSPGKGRGLRALQPFQVGDLLFSCPAYAYVLTVNERGNHCEYCFTRKEGLSKCGRCKQAFYCNVECQKEDWPMHKLECSPMVVFGENWNPSETVRLTARILAKQKIHPERTPSEKLLAVKEFESHLDKLDNEKKDLIQSDIAALHHFYSKHLGFPDNDSLVVLFAQVNCNGFTIEDEELSHLGSAIFPDVALMNHSCCPNVIVTYKGTLAEVRAVQEIKPGEEVFTSYIDLLYPTEDRNRRLRDSYFFTCECQECTTKDKDKAKVEIRKLSDPPKAEAIRDMVRYARNVIEEFRRAKHYKSPSELLEICELSQEKMSSVFEDSNVYMLHMMYQAMGVCLYMQDWEGALQYGQKIIKPYSKHYPLYSLNVASMWLKLGRLYMGLEHKAAGEKALKKAIAIMEVAHGKDHPYISEIKQEIESH,Slightly reduces methyltransferase activity on p53/TP53.,,MRAEGLGGLERFCSPGKGRGLRALQPFQVGDLLFSCPAYAYVLTVNERGNHCEYCFTRKEGLSKCGRCKQAFYCNVECQKEDWPMHKLECSPMVVFGENWNPSETVRLTARILAKQKIHPERTPSEKLLAVKEFESHLDKLDNEKKDLIQSDIAALHHFYSKHLGFPDNDSLVVLFAQVNCNGFTIEDEELSHLGSAIFPDVALMNHSCCPNVIVTYKGTLAEVRAVQEIKPGEEVFTSYIDLLYPTEDRNDRLRDSYFFTCECQECTTKDKDKAKVEIRKLSDPPKAEAIRDMVRYARNVIEEFRRAKHYKSPSELLEICELSQEKMSSVFEDSNVYMLHMMYQAMGVCLYMQDWEGALQYGQKIIKPYSKHYPLYSLNVASMWLKLGRLYMGLEHKAAGEKALKKAIAIMEVAHGKDHPYISEIKQEIESH,N-lysine methyltransferase SMYD2,"Protein-lysine N-methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. Specifically trimethylates histone H3 'Lys-4' (H3K4me3) in vivo. The activity requires interaction with HSP90alpha. Shows even higher methyltransferase activity on p53/TP53. Monomethylates 'Lys-370' of p53/TP53, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity of p53/TP53. Monomethylates RB1 at 'Lys-860'.",,Slightly reduces methyltransferase activity on p53/TP53.
1983,1983,1983,151123,P42898-A113T,MVNEARGNSSLNPCLEGSASSGSESSKDSSRCSTPGLDPERHERLREKMRRRLESGDKWFSLEFFPPRTAEGAVNLISRFDRMAAGGPLYIDVTWHPAGDPGSDKETSSMMITSTAVNYCGLETILHMTCCRQRLEEITGHLHKAKQLGLKNIMALRGDPIGDQWEEEEGGFNYAVDLVKHIRSEFGDYFDICVAGYPKGHPEAGSFEADLKHLKEKVSAGADFIITQLFFEADTFFRFVKACTDMGITCPIVPGIFPIQGYHSLRQLVKLSKLEVPQEIKDVIEPIKDNDAAIRNYGIELAVSLCQELLASGLVPGLHFYTLNREMATTEVLKRLGMWTEDPRRPLPWALSAHPKRREEDVRPIFWASRPKSYIYRTQEWDEFPNGRWGNSSSPAFGELKDYYLFYLKSKSPKEELLKMWGEELTSEESVFEVFVLYLSGEPNRNGHKVTCLPWNDEPLAAETSLLKEELLRVNRQGILTINSQPNINGKPSSDPIVGWGPSGGYVFQKAYLEFFTSRETAEALLQVLKKYELRVNYHLVNVKGENITNAPELQPNAVTWGIFPGREIIQPTVVDPVSFMFWKDEAFALWIERWGKLYEEESPSRTIIQYIHDNYFLVNLVDNDFPLDNCLWQVVEDTLELLNRPTQNARETEAP,In MTHFRD; reduced methylenetetrahydrofolate reductase activity; no effect on affinity for NADPH.,,MVNEARGNSSLNPCLEGSASSGSESSKDSSRCSTPGLDPERHERLREKMRRRLESGDKWFSLEFFPPRTAEGAVNLISRFDRMAAGGPLYIDVTWHPAGDPGSDKETSSMMIASTAVNYCGLETILHMTCCRQRLEEITGHLHKAKQLGLKNIMALRGDPIGDQWEEEEGGFNYAVDLVKHIRSEFGDYFDICVAGYPKGHPEAGSFEADLKHLKEKVSAGADFIITQLFFEADTFFRFVKACTDMGITCPIVPGIFPIQGYHSLRQLVKLSKLEVPQEIKDVIEPIKDNDAAIRNYGIELAVSLCQELLASGLVPGLHFYTLNREMATTEVLKRLGMWTEDPRRPLPWALSAHPKRREEDVRPIFWASRPKSYIYRTQEWDEFPNGRWGNSSSPAFGELKDYYLFYLKSKSPKEELLKMWGEELTSEESVFEVFVLYLSGEPNRNGHKVTCLPWNDEPLAAETSLLKEELLRVNRQGILTINSQPNINGKPSSDPIVGWGPSGGYVFQKAYLEFFTSRETAEALLQVLKKYELRVNYHLVNVKGENITNAPELQPNAVTWGIFPGREIIQPTVVDPVSFMFWKDEAFALWIERWGKLYEEESPSRTIIQYIHDNYFLVNLVDNDFPLDNCLWQVVEDTLELLNRPTQNARETEAP,Methylenetetrahydrofolate reductase,"Catalyzes the conversion of 5,10-methylenetetrahydrofolate to 5-methyltetrahydrofolate, a cosubstrate for homocysteine remethylation to methionine. Represents a key regulatory connection between the folate and methionine cycles (Probable).",,In MTHFRD; reduced methylenetetrahydrofolate reductase activity; no effect on affinity for NADPH.
1997,1997,1997,151914,Q13547-E424A,MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSAEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA,"Slightly decreases deacetylase activity, no effect on interaction with NuRD and SIN3 complexes.",,MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA,Histone deacetylase 1,"Histone deacetylase that catalyzes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin. Also functions as deacetylase for non-histone targets, such as NR1D2, RELA, SP1, SP3 and TSHZ3. Deacetylates SP proteins, SP1 and SP3, and regulates their function. Component of the BRG1-RB1-HDAC1 complex, which negatively regulates the CREST-mediated transcription in resting neurons. Upon calcium stimulation, HDAC1 is released from the complex and CREBBP is recruited, which facilitates transcriptional activation. Deacetylates TSHZ3 and regulates its transcriptional repressor activity. Deacetylates 'Lys-310' in RELA and thereby inhibits the transcriptional activity of NF-kappa-B. Deacetylates NR1D2 and abrogates the effect of KAT5-mediated relieving of NR1D2 transcription repression activity. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development. Involved in CIART-mediated transcriptional repression of the circadian transcriptional activator: CLOCK-BMAL1 heterodimer. Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex or CRY1 through histone deacetylation. In addition to protein deacetylase activity, also has protein-lysine deacylase activity: acts as a protein decrotonylase by mediating decrotonylation ((2E)-butenoyl) of histones.",,"Slightly decreases deacetylase activity, no effect on interaction with NuRD and SIN3 complexes."
2007,2007,2007,152733,P24394-Y152F,MGWLCSGLLFPVSCLVLLQVASSGNMKVLQEPTCVSDYMSISTCEWKMNGPTNCSTELRLLYQLVFLLSEAHTCIPENNGGAGCVCHLLMDDVVSADNYTLDLWAGQQLLWKGSFKPSEHVKPRAPGNLTVHTNVSDTLLLTWSNPYPPDNFLYNHLTYAVNIWSENDPADFRIYNVTYLEPSLRIAASTLKSGISYRARVRAWAQCYNTTWSEWSPSTKWHNSYREPFEQHLLLGVSVSCIVILAVCLLCYVSITKIKKEWWDQIPNPARSRLVAIIIQDAQGSQWEKRSRGQEPAKCPHWKNCLTKLLPCFLEHNMKRDEDPHKAAKEMPFQGSGKSAWCPVEISKTVLWPESISVVRCVELFEAPVECEEEEEVEEEKGSFCASPESSRDDFQEGREGIVARLTESLFLDLLGEENGGFCQQDMGESCLLPPSGSTSAHMPWDEFPSAGPKEAPPWGKEQPLHLEPSPPASPTQSPDNLTCTETPLVIAGNPAYRSFSNSLSQSPCPRELGPDPLLARHLEEVEPEMPCVPQLSEPTTVPQPEPETWEQILRRNVLQHGAAAAPVSAPTSGYQEFVHAVEQGGTQASAVVGLGPPGEAGYKAFSSLLASSAVSPEKCGFGASSGEEGYKPFQDLIPGCPGDPAPVPVPLFTFGLDREPPRSPQSSHLPSSSPEHLGLEPGEKVEDMPKPPLPQEQATDPLVDSLGSGIVYSALTCHLCGHLKQCHGQEDGGQTPVMASPCCGCCCGDRSSPPTTPLRAPDPSPGGVPLEASLCPASLAPSGISEKSKSSSSFHPAPGNAQSSSQTPKIVNFVSVGPTYMRVS,No effect on IL4 binding.,,MGWLCSGLLFPVSCLVLLQVASSGNMKVLQEPTCVSDYMSISTCEWKMNGPTNCSTELRLLYQLVFLLSEAHTCIPENNGGAGCVCHLLMDDVVSADNYTLDLWAGQQLLWKGSFKPSEHVKPRAPGNLTVHTNVSDTLLLTWSNPYPPDNYLYNHLTYAVNIWSENDPADFRIYNVTYLEPSLRIAASTLKSGISYRARVRAWAQCYNTTWSEWSPSTKWHNSYREPFEQHLLLGVSVSCIVILAVCLLCYVSITKIKKEWWDQIPNPARSRLVAIIIQDAQGSQWEKRSRGQEPAKCPHWKNCLTKLLPCFLEHNMKRDEDPHKAAKEMPFQGSGKSAWCPVEISKTVLWPESISVVRCVELFEAPVECEEEEEVEEEKGSFCASPESSRDDFQEGREGIVARLTESLFLDLLGEENGGFCQQDMGESCLLPPSGSTSAHMPWDEFPSAGPKEAPPWGKEQPLHLEPSPPASPTQSPDNLTCTETPLVIAGNPAYRSFSNSLSQSPCPRELGPDPLLARHLEEVEPEMPCVPQLSEPTTVPQPEPETWEQILRRNVLQHGAAAAPVSAPTSGYQEFVHAVEQGGTQASAVVGLGPPGEAGYKAFSSLLASSAVSPEKCGFGASSGEEGYKPFQDLIPGCPGDPAPVPVPLFTFGLDREPPRSPQSSHLPSSSPEHLGLEPGEKVEDMPKPPLPQEQATDPLVDSLGSGIVYSALTCHLCGHLKQCHGQEDGGQTPVMASPCCGCCCGDRSSPPTTPLRAPDPSPGGVPLEASLCPASLAPSGISEKSKSSSSFHPAPGNAQSSSQTPKIVNFVSVGPTYMRVS,Interleukin-4 receptor subunit alpha,"Receptor for both interleukin 4 and interleukin 13. Couples to the JAK1/2/3-STAT6 pathway. The IL4 response is involved in promoting Th2 differentiation. The IL4/IL13 responses are involved in regulating IgE production and, chemokine and mucus production at sites of allergic inflammation. In certain cell types, can signal through activation of insulin receptor substrates, IRS1/IRS2.Soluble IL4R (sIL4R) inhibits IL4-mediated cell proliferation and IL5 up-regulation by T-cells.",,No effect on IL4 binding.
2010,2010,2010,152989,P0A110-F352L,MNYNNKILVSESGLSQKHLIHGDEELFQHELKTIFARNWLFLTHDSLIPAPGDYVTAKMGIDEVIVSRQNDGSIRAFLNVCRHRGKTLVSVEAGNAKGFVCSYHGWGFGSNGELQSVPFEKDLYGESLNKKCLGLKEVARVESFHGFIYGCFDQEAPPLMDYLGDAAWYLEPMFKHSGGLELVGPPGKVVIKANWKAPAENFVGDAYHVGWTHASSLRSGESIFSSLAGNAALPPEGAGLQMTSKYGSGMGVLWDGYSGVHSADLVPELMAFGGAKQERLNKEIGDVRARIYRSHLNCTVFPNNSMLTCSGVFKVWNPIDANTTEVWTYAIVEKDMPEDLKRRLADSVQRTLGPAGFWESDDNDNMETASQNGKKYQSRDSDLLSNLGFGEDVYGDAVYPGVVGKSAIGETSYRGFYRAYQAHVSSSNWAEFEHASSTWHTELTKTTDR,"Cis-dihydroxylation of naphthalene results in the formation of cis-naphthalene dihydrodiol with altered stereochemistry. Cis-dihydroxylation of biphenyl results in the formation of cis-biphenyl 3,4-dihydrodiol as the major product.",,MNYNNKILVSESGLSQKHLIHGDEELFQHELKTIFARNWLFLTHDSLIPAPGDYVTAKMGIDEVIVSRQNDGSIRAFLNVCRHRGKTLVSVEAGNAKGFVCSYHGWGFGSNGELQSVPFEKDLYGESLNKKCLGLKEVARVESFHGFIYGCFDQEAPPLMDYLGDAAWYLEPMFKHSGGLELVGPPGKVVIKANWKAPAENFVGDAYHVGWTHASSLRSGESIFSSLAGNAALPPEGAGLQMTSKYGSGMGVLWDGYSGVHSADLVPELMAFGGAKQERLNKEIGDVRARIYRSHLNCTVFPNNSMLTCSGVFKVWNPIDANTTEVWTYAIVEKDMPEDLKRRLADSVQRTFGPAGFWESDDNDNMETASQNGKKYQSRDSDLLSNLGFGEDVYGDAVYPGVVGKSAIGETSYRGFYRAYQAHVSSSNWAEFEHASSTWHTELTKTTDR,"Naphthalene 1,2-dioxygenase system, large oxygenase component","Component of the naphthalene dioxygenase (NDO) multicomponent enzyme system which catalyzes the incorporation of both atoms of molecular oxygen into naphthalene to form cis-(1R,2S)-dihydroxy-1,2-dihydronaphthalene. The alpha subunit has a catalytic role in the holoenzyme. Also able to catalyze the cis-dihydroxylation of biphenyl and phenanthrene.","Amino acid substitutions at F-352 resulted in the formation of cis-naphthalene dihydrodiol with altered stereochemistry [92 to 96% (+)-1R, 2S], compared to the enantiomerically pure [>99% (+)-1R, 2S] product formed by the wild-type enzyme.","Cis-dihydroxylation of naphthalene results in the formation of cis-naphthalene dihydrodiol with altered stereochemistry. Cis-dihydroxylation of biphenyl results in the formation of cis-biphenyl 3,4-dihydrodiol as the major product. Amino acid substitutions at F-352 resulted in the formation of cis-naphthalene dihydrodiol with altered stereochemistry [92 to 96% (+)-1R, 2S], compared to the enantiomerically pure [>99% (+)-1R, 2S] product formed by the wild-type enzyme."
2014,2014,2014,153701,Q9FJF4-E303A,MQTRSSSSPSANHRRETQLQIADPTSFCGKIMPGWTVVNRPRSSNNGVVDTYFIEPGTGRQFSSLEAIHRHLAGEVNDRRLTRAGSFFQDKTRVYEGSRTKQDHCGVEYASKGFRLPRGWSVEEVPRKNSHYIDKYYVERKTGKRFRSLVSVERYLRESRNSIEQQLRVLQNRRGHSKDFRLPDGWIVEEKPRRSSSHIDRSYIEPGTGNKFRSMAAVERYLISVGNITLDSVSMVHSERLPLLMNRNGIRFQSEVIDPNPPKKVKWVLTGSGGNMFTANVRGSNVSSLVKHTWSEAFVSLIADRS,Loss of intranuclear immobility.,,MQTRSSSSPSANHRRETQLQIADPTSFCGKIMPGWTVVNRPRSSNNGVVDTYFIEPGTGRQFSSLEAIHRHLAGEVNDRRLTRAGSFFQDKTRVYEGSRTKQDHCGVEYASKGFRLPRGWSVEEVPRKNSHYIDKYYVERKTGKRFRSLVSVERYLRESRNSIEQQLRVLQNRRGHSKDFRLPDGWIVEEKPRRSSSHIDRSYIEPGTGNKFRSMAAVERYLISVGNITLDSVSMVHSERLPLLMNRNGIRFQSEVIDPNPPKKVKWVLTGSGGNMFTANVRGSNVSSLVKHTWSEAFVSLIEDRS,Methyl-CpG-binding domain-containing protein 7,Transcriptional regulator that binds CpG islands in promoters where the DNA is methylated at position 5 of cytosine within CpG dinucleotides. May directly affect chromatin structure by inducing intra- and inter- chromatin compaction via bridging over multiple methylated CpG sites. Acts as an anti-silencing factor that prevents DNA hypermethylation and gene repression. Requires high mCG density for binding. Recognizes preferentially mCGs located in transposable elements. Required for active DNA demethylation. Prefers to target genomic loci around chromocenters.,"StkC motif in fastening AtMBD7 to its chromosomal, CpG-methylated sites.","Loss of intranuclear immobility. StkC motif in fastening AtMBD7 to its chromosomal, CpG-methylated sites."
2022,2022,2022,154491,P05623-W51A,MKTLALFLVLVCVLGLVQSWEWPWNRKPTKFPIPSPNPRDKWCRLNLGPAAGGRC,Complete loss of activity; when associated with A-42. Complete loss of activity; when associated with A-42; A-43 and A-55.,,MKTLALFLVLVCVLGLVQSWEWPWNRKPTKFPIPSPNPRDKWCRLNLGPAWGGRC,Accessory gland-specific peptide 70A,"Male seminal protein which triggers short- and long-term post-mating behavioral responses (PMR) in female Drosophila. Binds initially to sperm where it is later cleaved to release an active peptide within the female reproductive tract. Signals via the sex peptide receptor (SPR) in female flies; may also act via other receptors. Moderates the activity of distinct neuronal circuitries in the female genital tract to promote specific PMRs including: enhanced ovulation, increased egg laying rate, increased feeding/foraging rate, induced antimicrobial peptide synthesis, reduced mating receptivity, reduced day-time sleep and reduced lifespan in multiple mated females.",The mutation in the sex peptide receptor (SPR) may have functional changes in the regulation of female reproductive behaviors.,Complete loss of activity; when associated with A-42. Complete loss of activity; when associated with A-42; A-43 and A-55. The mutation in the sex peptide receptor (SPR) may have functional changes in the regulation of female reproductive behaviors.
2023,2023,2023,154556,Q20733-H758L,MPPPQHPPNYYAPRRSISTITGPNRRDVDAFYQNNFPEKNGGSSGEHVPEYQASGQQHRPSIMSGQSHQNNHLPTKNYSYEPLRFSPPNVTPPPLQFSTNTDGNRKNQRVRFNELPNYSTPNHYSVPPRKCSLAPNFFSSQNSHHMYPDQYTPRTWQNNEFMPNHQVHPYHANHQQQHPQQHWRNQAASNGNHNPMYMRKHSAGHGIEIKLDHVDNPFGNPSHDMMDVTSGQPVKSEMLSPIKMETTDPSQQIASPSFLMTSTSLLKQHLHKKSHHNVPSRKASIMALKSQLRTPRGTPLNISTVPGTELPYTPPPILAPMRNGSGLFCQIVKSANSSLPVAEQSPDAPSCSTNGVDGDMKHLMNGKKRSEDGDGPSRKNGFFYMAQQMNQTNFANELEALRKESWASTSSADEKMQTERKESLESIRKASCMSDSYYEIEEGPKISDPNPHINLGKNYQARVKKWCDRQVSTSERDAIEDRDEIVFSSEILQDIDPEQITAFELLACSQACPRAGRNKELALHLLMENKGNIEAAVEDLLRSDTLDWEHYSSVFGYMYNDSVLWTPDEIYQFQDAIYQSEKDFDKVAVELPGKSVKECVQFYYTWKKDCPDDYRKLRNLRRKRQLLDINLQKNQSEEPVVPAKKISIIESGDSDNESNATDSSFIGNGHMEFRDRAFTSPMMSSPREEPIIGLSPSSKDLFGIQKNYQPTAPRAHHTPSASASKKGAQPSADGFFHCRLCDKCFEKVKSLNAHMKSLAMKARAEQEAKAHDAQVAAAAAAQLTSAVGNVVGNPVATSPLNSFANGHLGISIPSTIGNLTPQQLTPQQLNLNQQLQTQLNSLSNQMSLNSPLTPQQQLQQFTQQHLMARAMQQNLFQPVTSTPLVQPTHPLIQAGLHSIN,Reduced body size and egg-laying.,,MPPPQHPPNYYAPRRSISTITGPNRRDVDAFYQNNFPEKNGGSSGEHVPEYQASGQQHRPSIMSGQSHQNNHLPTKNYSYEPLRFSPPNVTPPPLQFSTNTDGNRKNQRVRFNELPNYSTPNHYSVPPRKCSLAPNFFSSQNSHHMYPDQYTPRTWQNNEFMPNHQVHPYHANHQQQHPQQHWRNQAASNGNHNPMYMRKHSAGHGIEIKLDHVDNPFGNPSHDMMDVTSGQPVKSEMLSPIKMETTDPSQQIASPSFLMTSTSLLKQHLHKKSHHNVPSRKASIMALKSQLRTPRGTPLNISTVPGTELPYTPPPILAPMRNGSGLFCQIVKSANSSLPVAEQSPDAPSCSTNGVDGDMKHLMNGKKRSEDGDGPSRKNGFFYMAQQMNQTNFANELEALRKESWASTSSADEKMQTERKESLESIRKASCMSDSYYEIEEGPKISDPNPHINLGKNYQARVKKWCDRQVSTSERDAIEDRDEIVFSSEILQDIDPEQITAFELLACSQACPRAGRNKELALHLLMENKGNIEAAVEDLLRSDTLDWEHYSSVFGYMYNDSVLWTPDEIYQFQDAIYQSEKDFDKVAVELPGKSVKECVQFYYTWKKDCPDDYRKLRNLRRKRQLLDINLQKNQSEEPVVPAKKISIIESGDSDNESNATDSSFIGNGHMEFRDRAFTSPMMSSPREEPIIGLSPSSKDLFGIQKNYQPTAPRAHHTPSASASKKGAQPSADGFFHCRLCDKCFEKVKSLNAHMKSHAMKARAEQEAKAHDAQVAAAAAAQLTSAVGNVVGNPVATSPLNSFANGHLGISIPSTIGNLTPQQLTPQQLNLNQQLQTQLNSLSNQMSLNSPLTPQQQLQQFTQQHLMARAMQQNLFQPVTSTPLVQPTHPLIQAGLHSIN,Suppressor of activated egl-4 protein 1,"As a likely component of a histone deacetylase complex, together with saeg-2 and hda-2, functions downstream of the cAMP-dependent kinase egl-4 to regulate the expression of genes required for egg-laying and foraging.",,Reduced body size and egg-laying.
2026,2026,2026,155228,P21453-F265L,MGPTSVPLVKAHRSSVSDYVNYDIIVRHYNYTGKLNISADKENSIKLTSVVFILICCFIILENIFVLLTIWKTKKFHRPMYYFIGNLALSDLLAGVAYTANLLLSGATTYKLTPAQWFLREGSMFVALSASVFSLLAIAIERYITMLKMKLHNGSNNFRLFLLISACWVISLILGGLPIMGWNCISALSSCSTVLPLYHKHYILFCTTVFTLLLLSIVILYCRIYSLVRTRSRRLTFRKNISKASRSSEKSLALLKTVIIVLSVLIACWAPLFILLLLDVGCKVKTCDILFRAEYFLVLAVLNSGTNPIIYTLTNKEMRRAFIRIMSCCKCPSGDSAGKFKRPIIAGMEFSRSKSDNSSHPQKDEGDNPETIMSSGNVNSSS,Impairs sphingosine 1-phosphate binding and signaling.,,MGPTSVPLVKAHRSSVSDYVNYDIIVRHYNYTGKLNISADKENSIKLTSVVFILICCFIILENIFVLLTIWKTKKFHRPMYYFIGNLALSDLLAGVAYTANLLLSGATTYKLTPAQWFLREGSMFVALSASVFSLLAIAIERYITMLKMKLHNGSNNFRLFLLISACWVISLILGGLPIMGWNCISALSSCSTVLPLYHKHYILFCTTVFTLLLLSIVILYCRIYSLVRTRSRRLTFRKNISKASRSSEKSLALLKTVIIVLSVFIACWAPLFILLLLDVGCKVKTCDILFRAEYFLVLAVLNSGTNPIIYTLTNKEMRRAFIRIMSCCKCPSGDSAGKFKRPIIAGMEFSRSKSDNSSHPQKDEGDNPETIMSSGNVNSSS,Sphingosine 1-phosphate receptor 1,"G-protein coupled receptor for the bioactive lysosphingolipid sphingosine 1-phosphate (S1P) that seems to be coupled to the G(i) subclass of heteromeric G proteins. Signaling leads to the activation of RAC1, SRC, PTK2/FAK1 and MAP kinases. Plays an important role in cell migration, probably via its role in the reorganization of the actin cytoskeleton and the formation of lamellipodia in response to stimuli that increase the activity of the sphingosine kinase SPHK1. Required for normal chemotaxis toward sphingosine 1-phosphate. Required for normal embryonic heart development and normal cardiac morphogenesis. Plays an important role in the regulation of sprouting angiogenesis and vascular maturation. Inhibits sprouting angiogenesis to prevent excessive sprouting during blood vessel development. Required for normal egress of mature T-cells from the thymus into the blood stream and into peripheral lymphoid organs. Plays a role in the migration of osteoclast precursor cells, the regulation of bone mineralization and bone homeostasis. Plays a role in responses to oxidized 1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphocholine by pulmonary endothelial cells and in the protection against ventilator-induced lung injury.",,Impairs sphingosine 1-phosphate binding and signaling.
2035,2035,2035,156279,P35520-P78R,MPSETPQAEVGPTGCPHRSGPHSAKGSLEKGSPEDKEAKEPLWIRPDAPSRCTWQLGRPASESPHHHTAPAKSPKILRDILKKIGDTPMVRINKIGKKFGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTPTNARFDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGSILAEPEELNQTEQTTYEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQEGQRCVVILPDSVRNYMTKFLSDRWMLQKGFLKEEDLTEKKPWWWHLRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLLAGKVQPSDQVGKVIYKQFKQIRLTDTLGRLSHILEMDHFALVVHEQIQYHSTGKSSQRQMVFGVVTAIDLLNFVAAQERDQK,In CBSD; severe form; associated in cis with N-102; decreased cystathionine beta-synthase activity; decreased homotetramer formation.,,MPSETPQAEVGPTGCPHRSGPHSAKGSLEKGSPEDKEAKEPLWIRPDAPSRCTWQLGRPASESPHHHTAPAKSPKILPDILKKIGDTPMVRINKIGKKFGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTPTNARFDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGSILAEPEELNQTEQTTYEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQEGQRCVVILPDSVRNYMTKFLSDRWMLQKGFLKEEDLTEKKPWWWHLRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLLAGKVQPSDQVGKVIYKQFKQIRLTDTLGRLSHILEMDHFALVVHEQIQYHSTGKSSQRQMVFGVVTAIDLLNFVAAQERDQK,Cystathionine beta-synthase,"Hydro-lyase catalyzing the first step of the transsulfuration pathway, where the hydroxyl group of L-serine is displaced by L-homocysteine in a beta-replacement reaction to form L-cystathionine, the precursor of L-cysteine. This catabolic route allows the elimination of L-methionine and the toxic metabolite L-homocysteine. Also involved in the production of hydrogen sulfide, a gasotransmitter with signaling and cytoprotective effects on neurons.","The paternal allele contained a linked pair of mutations, and , corresponding to and in the polypeptide chain. Together, these inactivated the enzyme; however, expressed separately, they reduced activity by about one half.","In CBSD; severe form; associated in cis with N-102; decreased cystathionine beta-synthase activity; decreased homotetramer formation. The paternal allele contained a linked pair of mutations, and , corresponding to and in the polypeptide chain. Together, these inactivated the enzyme; however, expressed separately, they reduced activity by about one half."
2039,2039,2039,156468,Q14BI7-E257Q,MLRKLTVDQINDWFTIGKTVTNVELLGLPPAFPAEAPREEVQRSEEVPNEDPTAQAQVPVKATAPARPASTSGRSLSQRSSEMEYINKYRQLEEQELDIYGQDQPPSGPGLRSPLAKLSNVACIPETTYKYPDLPINRCKEEVISLIESNSVVIIHGATGSGKSTQLPQYVLDHYTQRSAFCNIVVTQPRKIGASSIARWISKERSWTLGGLVGYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIFIDQVHERTEEMDFLLLVVRKLLRTNSRFVKVVLMSATINCKQFADYFAVPVQNKMNPAYVFEVEGKPHAIEEYYLNDLGHIYHSGLPYRLEEPVITKDVYEVAVSLIQMFDDLDMKESGNKTWSGAQFVSERSSVLVFLPGLGEINYMHELLTNMIHKRLQVYPLHSSVTLEEQNNVFLSPVPGYRKIILSTNIAESSVTVPDVKYVIDFCLTRTLVCDEDTNYQSLRLSWASKTSCDQRKGRAGRVSKGYCYRLIPRDFWDSAIPDHVVPEMLRCPLGSTILKVKLLDMGEPRALLATALSPPSLSDIERTILLLKEVGALAVSGQREDENPHDGELTFLGRVLAQLPVSQQLGKLVVLGHVFGCLDECLIIAAALSLKNFFTMPFRQHLDGYRNKVHFSGSSRSDCLALVEAFRAWQACRQRGELRRPKDELDWGRLNYIQIKRIREVAELYEELKNRISQFNMFVGPHHPVLDQEYPYKQRFILQVVLAGAFYPNYFTFGQPDEEMAVRELAGKDPKTTVVLKHIPPYGFLYYKQLQSLFRQCGQVKSIVFDGAKAFVEFSRNPTERFKTLPAVNLAVKMSQLKVSLELSVHAAEEIEGKVQGGSVSKLRNTRVNVDFQKQTVDPMQVSFNTLDRPRTVADLLLTIDVTEVVEVGHFWGYRIDERNAELLKQLTAEINRLELVPLPIHPHPDLVCLAPFTDYNKESYFRAQILYVSGNSAEVFFVDYGNRSHVDLDLLREIPCQFLELPFQALEFKICKMRPSAKSL,In Tdrd9(KI); heterozygous and homozygous knockin male mice are infertile due to derepression of transposable elements. PiRNA biogenesis in not affected but piRNAs fail to accumulate in the nucleus.,,MLRKLTVDQINDWFTIGKTVTNVELLGLPPAFPAEAPREEVQRSEEVPNEDPTAQAQVPVKATAPARPASTSGRSLSQRSSEMEYINKYRQLEEQELDIYGQDQPPSGPGLRSPLAKLSNVACIPETTYKYPDLPINRCKEEVISLIESNSVVIIHGATGSGKSTQLPQYVLDHYTQRSAFCNIVVTQPRKIGASSIARWISKERSWTLGGLVGYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIFIDEVHERTEEMDFLLLVVRKLLRTNSRFVKVVLMSATINCKQFADYFAVPVQNKMNPAYVFEVEGKPHAIEEYYLNDLGHIYHSGLPYRLEEPVITKDVYEVAVSLIQMFDDLDMKESGNKTWSGAQFVSERSSVLVFLPGLGEINYMHELLTNMIHKRLQVYPLHSSVTLEEQNNVFLSPVPGYRKIILSTNIAESSVTVPDVKYVIDFCLTRTLVCDEDTNYQSLRLSWASKTSCDQRKGRAGRVSKGYCYRLIPRDFWDSAIPDHVVPEMLRCPLGSTILKVKLLDMGEPRALLATALSPPSLSDIERTILLLKEVGALAVSGQREDENPHDGELTFLGRVLAQLPVSQQLGKLVVLGHVFGCLDECLIIAAALSLKNFFTMPFRQHLDGYRNKVHFSGSSRSDCLALVEAFRAWQACRQRGELRRPKDELDWGRLNYIQIKRIREVAELYEELKNRISQFNMFVGPHHPVLDQEYPYKQRFILQVVLAGAFYPNYFTFGQPDEEMAVRELAGKDPKTTVVLKHIPPYGFLYYKQLQSLFRQCGQVKSIVFDGAKAFVEFSRNPTERFKTLPAVNLAVKMSQLKVSLELSVHAAEEIEGKVQGGSVSKLRNTRVNVDFQKQTVDPMQVSFNTLDRPRTVADLLLTIDVTEVVEVGHFWGYRIDERNAELLKQLTAEINRLELVPLPIHPHPDLVCLAPFTDYNKESYFRAQILYVSGNSAEVFFVDYGNRSHVDLDLLREIPCQFLELPFQALEFKICKMRPSAKSL,ATP-dependent RNA helicase TDRD9,"ATP-binding RNA helicase which plays a central role during spermatogenesis by repressing transposable elements and preventing their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons. Acts downstream of piRNA biogenesis: exclusively required for transposon silencing in the nucleus, suggesting that it acts as a nuclear effector in the nucleus together with PIWIL4.","The mutation in the MILI protein affects the slicing of target RNA, leading to a change in the production of piRNAs and potentially impacting transposon silencing and male fertility.","In Tdrd9(KI); heterozygous and homozygous knockin male mice are infertile due to derepression of transposable elements. PiRNA biogenesis in not affected but piRNAs fail to accumulate in the nucleus. The mutation in the MILI protein affects the slicing of target RNA, leading to a change in the production of piRNAs and potentially impacting transposon silencing and male fertility."
2046,2046,2046,157408,P02994-E317K,MGKEKSHINVVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAELGKGSFKYAWVLDKLKAERERGITIDIALWKFETPKYQVTVIDAPGHRDFIKNMITGTSQADCAILIIAGGVGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMDSVKWDESRFQEIVKETSNFIKKVGYNPKTVPFVPISGWNGDNMIEATTNAPWYKGWEKETKAGVVKGKTLLEAIDAIEQPSRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPGMVVTFAPAGVTTEVKSVEMHHEQLEQGVPGDNVGFNVKNVSVKKIRRGNVCGDAKNDPPKGCASFNATVIVLNHPGQISAGYSPVLDCHTAHIACRFDELLEKNDRRSGKKLEDHPKFLKSGDAALVKFVPSKPMCVEAFSEYPPLGRFAVRDMRQTVAVGVIKSVDKTEKAAKVTKAAQKAAKK,In TEF2-2; strongly reduces translation fidelity by increasing the frequency of frameshifting and amino acid misincorporation.,,MGKEKSHINVVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAELGKGSFKYAWVLDKLKAERERGITIDIALWKFETPKYQVTVIDAPGHRDFIKNMITGTSQADCAILIIAGGVGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMDSVKWDESRFQEIVKETSNFIKKVGYNPKTVPFVPISGWNGDNMIEATTNAPWYKGWEKETKAGVVKGKTLLEAIDAIEQPSRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPGMVVTFAPAGVTTEVKSVEMHHEQLEQGVPGDNVGFNVKNVSVKEIRRGNVCGDAKNDPPKGCASFNATVIVLNHPGQISAGYSPVLDCHTAHIACRFDELLEKNDRRSGKKLEDHPKFLKSGDAALVKFVPSKPMCVEAFSEYPPLGRFAVRDMRQTVAVGVIKSVDKTEKAAKVTKAAQKAAKK,Elongation factor 1-alpha,"GTP-binding component of the eukaryotic elongation factor 1 complex (eEF1). In its active GTP-bound form, binds to and delivers aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. In the presence of a correct codon-anticodon match between the aminoacyl-tRNA and the A-site codon of the ribosome-bound mRNA, the ribosome acts as a GTPase activator and the GTP is hydrolyzed. The inactive GDP-bound form leaves the ribosome and must be recycled by its guanine nucleotide exchange factor (GEF) (eEF1B subcomplex) before binding another molecule of aminoacyl-tRNA. Required for nuclear export of aminoacyl-tRNAs. May also be involved in translational quality control by targeting cotranslationally damaged proteins to the proteasome. Also exhibits actin filament-binding and -bundling activities and is involved in cytoskeleton organization. Plays a role as a negative regulator of GCN2 kinase activity by inhibiting GCN2-mediated eIF-2-alpha phosphorylation in amino acid-repleted cells.",Amino acid substitutions located in or near the GTP-binding and hydrolysis domain of the protein cause suppression of frameshift and nonsense mutations. These mutations may effect mistranslation by altering the binding or hydrolysis of GTP.,In TEF2-2; strongly reduces translation fidelity by increasing the frequency of frameshifting and amino acid misincorporation. Amino acid substitutions located in or near the GTP-binding and hydrolysis domain of the protein cause suppression of frameshift and nonsense mutations. These mutations may effect mistranslation by altering the binding or hydrolysis of GTP.
2060,2060,2060,158376,O00213-K204R,MSVPSSLSQSAINANSHGGPALSLPLPLHAAHNQLLNAKLQATAVGPKDLRSAMGEGGGPEPGPANAKWLKEGQNQLRRAATAHRDQNRNVTLTLAEEASQEPEMAPLGPKGLIHLYSELELSAHNAANRGLRGPGLIISTQEQGPDEGEEKAAGEAEEEEEDDDDEEEEEDLSSPPGLPEPLESVEAPPRPQALTDGPREHSRSASLLFGMRNSAASDEDSSWATLSQGSPSYGSPEDTDSFWNPNAFETDSDLPAGWMRVQDTSGTYYWHIPTGTTQWEPPGRASPSQGSSPQEESQLTWTGFAHGEGFEDGEFWKDEPSDEAPMELGLKEPEEGTLTFPAQSLSPEPLPQEEEKLPPRNTNPGIKCFAVRSLGWVEMTEEELAPGRSSVAVNNCIRQLSYHKNNLHDPMSGGWGEGKDLLLQLEDETLKLVEPQSQALLHAQPIISIRVWGVGRDSGRERDFAYVARDKLTQMLKCHVFRCEAPAKNIATSLHEICSKIMAERRNARCLVNGLSLDHSKLVDVPFQVEFPAPKNELVQKFQVYYLGNVPVAKPVGVDVINGALESVLSSSSREQWTPSHVSVAPATLTILHQQTEAVLGECRVRFLSFLAVGRDVHTFAFIMAAGPASFCCHMFWCEPNAASLSEAVQAACMLRYQKCLDARSQASTSCLPAPPAESVARRVGWTVRRGVQSLWGSLKPKRLGAHTP,"Abolished acetylation by KAT5, leading to decreased transcription activator activity; when associated with R-701.",,MSVPSSLSQSAINANSHGGPALSLPLPLHAAHNQLLNAKLQATAVGPKDLRSAMGEGGGPEPGPANAKWLKEGQNQLRRAATAHRDQNRNVTLTLAEEASQEPEMAPLGPKGLIHLYSELELSAHNAANRGLRGPGLIISTQEQGPDEGEEKAAGEAEEEEEDDDDEEEEEDLSSPPGLPEPLESVEAPPRPQALTDGPREHSKSASLLFGMRNSAASDEDSSWATLSQGSPSYGSPEDTDSFWNPNAFETDSDLPAGWMRVQDTSGTYYWHIPTGTTQWEPPGRASPSQGSSPQEESQLTWTGFAHGEGFEDGEFWKDEPSDEAPMELGLKEPEEGTLTFPAQSLSPEPLPQEEEKLPPRNTNPGIKCFAVRSLGWVEMTEEELAPGRSSVAVNNCIRQLSYHKNNLHDPMSGGWGEGKDLLLQLEDETLKLVEPQSQALLHAQPIISIRVWGVGRDSGRERDFAYVARDKLTQMLKCHVFRCEAPAKNIATSLHEICSKIMAERRNARCLVNGLSLDHSKLVDVPFQVEFPAPKNELVQKFQVYYLGNVPVAKPVGVDVINGALESVLSSSSREQWTPSHVSVAPATLTILHQQTEAVLGECRVRFLSFLAVGRDVHTFAFIMAAGPASFCCHMFWCEPNAASLSEAVQAACMLRYQKCLDARSQASTSCLPAPPAESVARRVGWTVRRGVQSLWGSLKPKRLGAHTP,Amyloid beta precursor protein binding family B member 1,"Transcription coregulator that can have both coactivator and corepressor functions. Adapter protein that forms a transcriptionally active complex with the gamma-secretase-derived amyloid precursor protein (APP) intracellular domain. Plays a central role in the response to DNA damage by translocating to the nucleus and inducing apoptosis. May act by specifically recognizing and binding histone H2AX phosphorylated on 'Tyr-142' (H2AXY142ph) at double-strand breaks (DSBs), recruiting other pro-apoptosis factors such as MAPK8/JNK1. Required for histone H4 acetylation at double-strand breaks (DSBs). Its ability to specifically bind modified histones and chromatin modifying enzymes such as KAT5/TIP60, probably explains its transcription activation activity. Functions in association with TSHZ3, SET and HDAC factors as a transcriptional repressor, that inhibits the expression of CASP4. Associates with chromatin in a region surrounding the CASP4 transcriptional start site(s). Involved in hippocampal neurite branching and neuromuscular junction formation, as a result plays a role in spatial memory functioning. Plays a role in the maintenance of lens transparency. May play a role in muscle cell strength.",Mutation of Fe65 K204 to arginine (R) increases the transcriptional activity of Fe65.,"Abolished acetylation by KAT5, leading to decreased transcription activator activity; when associated with R-701. Mutation of Fe65 K204 to arginine (R) increases the transcriptional activity of Fe65."
2070,2070,2070,158739,P11712-I359L,MDSLVVLVLCLSCLLLLSLWRQSSGRGKLPPGPTPLPVIGNILQIGIKDISKSLTNLSKVYGPVFTLYFGLKPIVVLHGYEAVKEALIDLGEEFSGRGIFPLAERANRGFGIVFSNGKKWKEIRRFSLMTLRNFGMGKRSIEDRVQEEARCLVEELRKTKASPCDPTFILGCAPCNVICSIIFHKRFDYKDQQFLNLMEKLNENIKILSSPWIQICNNFSPIIDYFPGTHNKLLKNVAFMKSYILEKVKEHQESMDMNNPQDFIDCFLMKMEKEKHNQPSEFTIESLENTAVDLFGAGTETTSTTLRYALLLLLKHPEVTAKVQEEIERVIGRNRSPCMQDRSHMPYTDAVVHEVQRYLDLLPTSLPHAVTCDIKFRNYLIPKGTTILISLTSVLHDNKEFPNPEMFDPHHFLDEGGNFKKSKYFMPFSAGKRICVGEALAGMELFLFLTSILQNFNLKSLVDPKNLDTTPVVNGFASVPPFYQLCFIPV,In allele CYP2C9*3; responsible for the tolbutamide poor metabolizer phenotype.,,MDSLVVLVLCLSCLLLLSLWRQSSGRGKLPPGPTPLPVIGNILQIGIKDISKSLTNLSKVYGPVFTLYFGLKPIVVLHGYEAVKEALIDLGEEFSGRGIFPLAERANRGFGIVFSNGKKWKEIRRFSLMTLRNFGMGKRSIEDRVQEEARCLVEELRKTKASPCDPTFILGCAPCNVICSIIFHKRFDYKDQQFLNLMEKLNENIKILSSPWIQICNNFSPIIDYFPGTHNKLLKNVAFMKSYILEKVKEHQESMDMNNPQDFIDCFLMKMEKEKHNQPSEFTIESLENTAVDLFGAGTETTSTTLRYALLLLLKHPEVTAKVQEEIERVIGRNRSPCMQDRSHMPYTDAVVHEVQRYIDLLPTSLPHAVTCDIKFRNYLIPKGTTILISLTSVLHDNKEFPNPEMFDPHHFLDEGGNFKKSKYFMPFSAGKRICVGEALAGMELFLFLTSILQNFNLKSLVDPKNLDTTPVVNGFASVPPFYQLCFIPV,Cytochrome P450 2C9,"A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids and steroids. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase). Catalyzes the epoxidation of double bonds of polyunsaturated fatty acids (PUFA). Catalyzes the hydroxylation of carbon-hydrogen bonds. Metabolizes cholesterol toward 25-hydroxycholesterol, a physiological regulator of cellular cholesterol homeostasis. Exhibits low catalytic activity for the formation of catechol estrogens from 17beta-estradiol (E2) and estrone (E1), namely 2-hydroxy E1 and E2. Catalyzes bisallylic hydroxylation and hydroxylation with double-bond migration of polyunsaturated fatty acids (PUFA). Also metabolizes plant monoterpenes such as limonene. Oxygenates (R)- and (S)-limonene to produce carveol and perillyl alcohol. Contributes to the wide pharmacokinetics variability of the metabolism of drugs such as S-warfarin, diclofenac, phenytoin, tolbutamide and losartan.",It is likely that functional changes occurring as a result of the transition are responsible for the tolbutamide poor metabolizer phenotype.,In allele CYP2C9*3; responsible for the tolbutamide poor metabolizer phenotype. It is likely that functional changes occurring as a result of the transition are responsible for the tolbutamide poor metabolizer phenotype.
2083,2083,2083,159289,P04155-A34D,MATMENKVICALVLVSMLALGTLAEAQTETCTVDPRERQNCGFPGVTPSQCANKGCCFDDTVRGVPWCFYPNTIDVPPEEECEF,In a gastric carcinoma sample; somatic mutation; abolishes inhibition of gastric cancer cell growth; abolishes inhibition of apoptosis in gasterointestinal epithelial cells; increases invasive activity in epithelial cells.,,MATMENKVICALVLVSMLALGTLAEAQTETCTVAPRERQNCGFPGVTPSQCANKGCCFDDTVRGVPWCFYPNTIDVPPEEECEF,Trefoil factor 1,Stabilizer of the mucous gel overlying the gastrointestinal mucosa that provides a physical barrier against various noxious agents. May inhibit the growth of calcium oxalate crystals in urine.,,In a gastric carcinoma sample; somatic mutation; abolishes inhibition of gastric cancer cell growth; abolishes inhibition of apoptosis in gasterointestinal epithelial cells; increases invasive activity in epithelial cells.
2085,2085,2085,159463,Q6N021-S817T,MEQDRTNHVEGNRLSPFLIPSPPICQTEPLATKLQNGSPLPERAHPEVNGDTKWHSFKSYYGIPCMKGSQNSRVSPDFTQESRGYSKCLQNGGIKRTVSEPSLSGLLQIKKLKQDQKANGERRNFGVSQERNPGESSQPNVSDLSDKKESVSSVAQENAVKDFTSFSTHNCSGPENPELQILNEQEGKSANYHDKNIVLLKNKAVLMPNGATVSASSVEHTHGELLEKTLSQYYPDCVSIAVQKTTSHINAINSQATNELSCEITHPSHTSGQINSAQTSNSELPPKPAAVVSEACDADDADNASKLAAMLNTCSFQKPEQLQQQKSVFEICPSPAENNIQGTTKLASGEEFCSGSSSNLQAPGGSSERYLKQNEMNGAYFKQSSVFTKDSFSATTTPPPPSQLLLSPPPPLPQVPQLPSEGKSTLNGGVLEEHHHYPNQSNTTLLREVKIEGKPEAPPSQSPNPSTHVCSPSPMLSERPQNNCVNRNDIQTAGTMTVPLCSEKTRPMSEHLKHNPPIFGSSGELQDNCQQLMRNKEQEILKGRDKEQTRDLVPPTQHYLKPGWIELKAPRFHQAESHLKRNEASLPSILQYQPNLSNQMTSKQYTGNSNMPGGLPRQAYTQKTTQLEHKSQMYQVEMNQGQSQGTVDQHLQFQKPSHQVHFSKTDHLPKAHVQSLCGTRFHFQQRADSQTEKLMSPVLKQHLNQQASETEPFSNSHLLQHKPHKQAAQTQPSQSSHLPQNQQQQQKLQIKNKEEILQTFPHPQSNNDQQREGSFFGQTKVEECFHGENQYSKSSEFETHNVQMGLEEVQNINRRNTPYSQTMKSSACKIQVSCSNNTHLVSENKEQTTHPELFAGNKTQNLHHMQYFPNNVIPKQDLLHRCFQEQEQKSQQASVLQGYKNRNQDMSGQQAAQLAQQRYLIHNHANVFPVPDQGGSHTQTPPQKDTQKHAALRWHLLQKQEQQQTQQPQTESCHSQMHRPIKVEPGCKPHACMHTAPPENKTWKKVTKQENPPASCDNVQQKSI,In myelodysplastic/myeloproliferative disorders.,,MEQDRTNHVEGNRLSPFLIPSPPICQTEPLATKLQNGSPLPERAHPEVNGDTKWHSFKSYYGIPCMKGSQNSRVSPDFTQESRGYSKCLQNGGIKRTVSEPSLSGLLQIKKLKQDQKANGERRNFGVSQERNPGESSQPNVSDLSDKKESVSSVAQENAVKDFTSFSTHNCSGPENPELQILNEQEGKSANYHDKNIVLLKNKAVLMPNGATVSASSVEHTHGELLEKTLSQYYPDCVSIAVQKTTSHINAINSQATNELSCEITHPSHTSGQINSAQTSNSELPPKPAAVVSEACDADDADNASKLAAMLNTCSFQKPEQLQQQKSVFEICPSPAENNIQGTTKLASGEEFCSGSSSNLQAPGGSSERYLKQNEMNGAYFKQSSVFTKDSFSATTTPPPPSQLLLSPPPPLPQVPQLPSEGKSTLNGGVLEEHHHYPNQSNTTLLREVKIEGKPEAPPSQSPNPSTHVCSPSPMLSERPQNNCVNRNDIQTAGTMTVPLCSEKTRPMSEHLKHNPPIFGSSGELQDNCQQLMRNKEQEILKGRDKEQTRDLVPPTQHYLKPGWIELKAPRFHQAESHLKRNEASLPSILQYQPNLSNQMTSKQYTGNSNMPGGLPRQAYTQKTTQLEHKSQMYQVEMNQGQSQGTVDQHLQFQKPSHQVHFSKTDHLPKAHVQSLCGTRFHFQQRADSQTEKLMSPVLKQHLNQQASETEPFSNSHLLQHKPHKQAAQTQPSQSSHLPQNQQQQQKLQIKNKEEILQTFPHPQSNNDQQREGSFFGQTKVEECFHGENQYSKSSEFETHNVQMGLEEVQNINRRNSPYSQTMKSSACKIQVSCSNNTHLVSENKEQTTHPELFAGNKTQNLHHMQYFPNNVIPKQDLLHRCFQEQEQKSQQASVLQGYKNRNQDMSGQQAAQLAQQRYLIHNHANVFPVPDQGGSHTQTPPQKDTQKHAALRWHLLQKQEQQQTQQPQTESCHSQMHRPIKVEPGCKPHACMHTAPPENKTWKKVTKQENPPASCDNVQQKSI,Methylcytosine dioxygenase TET2,"Dioxygenase that catalyzes the conversion of the modified genomic base 5-methylcytosine (5mC) into 5-hydroxymethylcytosine (5hmC) and plays a key role in active DNA demethylation. Has a preference for 5-hydroxymethylcytosine in CpG motifs. Also mediates subsequent conversion of 5hmC into 5-formylcytosine (5fC), and conversion of 5fC to 5-carboxylcytosine (5caC). Conversion of 5mC into 5hmC, 5fC and 5caC probably constitutes the first step in cytosine demethylation. Methylation at the C5 position of cytosine bases is an epigenetic modification of the mammalian genome which plays an important role in transcriptional regulation. In addition to its role in DNA demethylation, also involved in the recruitment of the O-GlcNAc transferase OGT to CpG-rich transcription start sites of active genes, thereby promoting histone H2B GlcNAcylation by OGT.",,In myelodysplastic/myeloproliferative disorders.
2134,2134,2134,162952,Q14653-K366R,MGTPKPRILPWLVSQLDLGQLEGVAWVNKSRTRFRIPWKHGLRQDAQQEDFGIFQAWAEATGAYVPGRDKPDLPTWKRNFRSALNRKEGLRLAEDRSKDPHDPHKIYEFVNSGVGDFSQPDTSPDTNGGGSTSDTQEDILDELLGNMVLAPLPDPGPPSLAVAPEPCPQPLRSPSLDNPTPFPNLGPSENPLKRLLVPGEEWEFEVTAFYRGRQVFQQTISCPEGLRLVGSEVGDRTLPGWPVTLPDPGMSLTDRGVMSYVRHVLSCLGGGLALWRAGQWLWAQRLGHCHTYWAVSEELLPNSGHGPDGEVPKDKEGGVFDLGPFIVDLITFTEGSGRSPRYALWFCVGESWPQDQPWTKRLVMVRVVPTCLRALVEMARVGGASSLENTVDLHISNSHPLSLTSDQYKAYLQDLVEGMDFQGPGES,Highly diminished ISGylation; when associated with R-193 and R-360.,,MGTPKPRILPWLVSQLDLGQLEGVAWVNKSRTRFRIPWKHGLRQDAQQEDFGIFQAWAEATGAYVPGRDKPDLPTWKRNFRSALNRKEGLRLAEDRSKDPHDPHKIYEFVNSGVGDFSQPDTSPDTNGGGSTSDTQEDILDELLGNMVLAPLPDPGPPSLAVAPEPCPQPLRSPSLDNPTPFPNLGPSENPLKRLLVPGEEWEFEVTAFYRGRQVFQQTISCPEGLRLVGSEVGDRTLPGWPVTLPDPGMSLTDRGVMSYVRHVLSCLGGGLALWRAGQWLWAQRLGHCHTYWAVSEELLPNSGHGPDGEVPKDKEGGVFDLGPFIVDLITFTEGSGRSPRYALWFCVGESWPQDQPWTKRLVMVKVVPTCLRALVEMARVGGASSLENTVDLHISNSHPLSLTSDQYKAYLQDLVEGMDFQGPGES,Interferon regulatory factor 3,"Key transcriptional regulator of type I interferon (IFN)-dependent immune responses which plays a critical role in the innate immune response against DNA and RNA viruses. Regulates the transcription of type I IFN genes (IFN-alpha and IFN-beta) and IFN-stimulated genes (ISG) by binding to an interferon-stimulated response element (ISRE) in their promoters. Acts as a more potent activator of the IFN-beta (IFNB) gene than the IFN-alpha (IFNA) gene and plays a critical role in both the early and late phases of the IFNA/B gene induction. Found in an inactive form in the cytoplasm of uninfected cells and following viral infection, double-stranded RNA (dsRNA), or toll-like receptor (TLR) signaling, is phosphorylated by IKBKE and TBK1 kinases. This induces a conformational change, leading to its dimerization and nuclear localization and association with CREB binding protein (CREBBP) to form dsRNA-activated factor 1 (DRAF1), a complex which activates the transcription of the type I IFN and ISG genes. Can activate distinct gene expression programs in macrophages and can induce significant apoptosis in primary macrophages. In response to Sendai virus infection, is recruited by TOMM70:HSP90AA1 to mitochondrion and forms an apoptosis complex TOMM70:HSP90AA1:IRF3:BAX inducing apoptosis. Key transcription factor regulating the IFN response during SARS-CoV-2 infection.","The mutant IRF3() interacts tightly with Pin1, is highly polyubiquitinated, and becomes less stable upon Sendai virus (SeV) infection.","Highly diminished ISGylation; when associated with R-193 and R-360. The mutant IRF3() interacts tightly with Pin1, is highly polyubiquitinated, and becomes less stable upon Sendai virus (SeV) infection."
2139,2139,2139,163511,P9WGJ9-N348A,MAGSATVEKRLDFGLLGPLQMTIDGTPVPSGTPKQRAVLAMLVINRNRPVGVDALITALWEEWPPSGARASIHSYVSNLRKLLGGAGIDPRVVLAAAPPGYRLSIPDNTCDLGRFVAEKTAGVHAAAAGRFEQASRHLSAALREWRGPVLDDLRDFQFVEPFATALVEDKVLAHTAKAEAEIACGRASAVIAELEALTFEHPYREPLWTQLITAYYLSDRQSDALGAYRRVKTTLADDLGIDPGPTLRALNERILRQQPLDAKKSAKTTAAGTVTVLDQRTMASGQQAVAYLHDIASGRGYPLQAAATRIGRLHDNDIVLDSANVSRHHAVIVDTGTNYVINDLRSSAGVHVQHERIRSAVTLNDGDHIRICDHEFTFQISAGTHGGT,Abolished phosphorylation.,,MAGSATVEKRLDFGLLGPLQMTIDGTPVPSGTPKQRAVLAMLVINRNRPVGVDALITALWEEWPPSGARASIHSYVSNLRKLLGGAGIDPRVVLAAAPPGYRLSIPDNTCDLGRFVAEKTAGVHAAAAGRFEQASRHLSAALREWRGPVLDDLRDFQFVEPFATALVEDKVLAHTAKAEAEIACGRASAVIAELEALTFEHPYREPLWTQLITAYYLSDRQSDALGAYRRVKTTLADDLGIDPGPTLRALNERILRQQPLDAKKSAKTTAAGTVTVLDQRTMASGQQAVAYLHDIASGRGYPLQAAATRIGRLHDNDIVLDSANVSRHHAVIVDTGTNYVINDLRSSNGVHVQHERIRSAVTLNDGDHIRICDHEFTFQISAGTHGGT,Transcriptional regulatory protein EmbR,Positively regulates the transcription of the embCAB operon. Exhibits ATPase and GTPase activities.,Mutation of N348 in the FHA domain abolishes the PknH-mediated phosphorylation of EmbR.,Abolished phosphorylation. Mutation of N348 in the FHA domain abolishes the PknH-mediated phosphorylation of EmbR.
2142,2142,2142,163878,I6XD65-H51A,MRALIIVDVQNDFCEGGSLAVTGGAALARAISDYLAEAADYHHVVATKDFAIDPGDHFSGTPDYSSSWPPHCVSGTPGADFHPSLDTSAIEAVFYKGAYTGAYSGFEGVDENGTPLLNWLRQRGVDEVDVVGIATDHCVRQTAEDAVRNGLATRVLVDLTAGVSADTTVAALEEMRTASVELVCSS,"10-fold decrease in enzymatic activity with NAM as substrate, and 21-fold decrease in enzymatic activity with PZA as substrate. The mutant has a low metal ion content.",,MRALIIVDVQNDFCEGGSLAVTGGAALARAISDYLAEAADYHHVVATKDFHIDPGDHFSGTPDYSSSWPPHCVSGTPGADFHPSLDTSAIEAVFYKGAYTGAYSGFEGVDENGTPLLNWLRQRGVDEVDVVGIATDHCVRQTAEDAVRNGLATRVLVDLTAGVSADTTVAALEEMRTASVELVCSS,Nicotinamidase/pyrazinamidase,"Catalyzes the deamidation of nicotinamide (NAM) into nicotinate. Likely functions in the cyclical salvage pathway for production of NAD from nicotinamide.Is involved in the activation of the first-line antituberculous drug pyrazinamide (PZA) by converting it into the active form, pyrazinoic acid.",mutation is essential for metal ion binding.,"10-fold decrease in enzymatic activity with NAM as substrate, and 21-fold decrease in enzymatic activity with PZA as substrate. The mutant has a low metal ion content. mutation is essential for metal ion binding."
2165,2165,2165,166033,P27487-N85A,MKTPWKVLLGLLGAAALVTIITVPVVLLNKGTDDATADSRKTYTLTDYLKNTYRLKLYSLRWISDHEYLYKQENNILVFNAEYGASSVFLENSTFDEFGHSINDYSISPDGQFILLEYNYVKQWRHSYTASYDIYDLNKRQLITEERIPNNTQWVTWSPVGHKLAYVWNNDIYVKIEPNLPSYRITWTGKEDIIYNGITDWVYEEEVFSAYSALWWSPNGTFLAYAQFNDTEVPLIEYSFYSDESLQYPKTVRVPYPKAGAVNPTVKFFVVNTDSLSSVTNATSIQITAPASMLIGDHYLCDVTWATQERISLQWLRRIQNYSVMDICDYDESSGRWNCLVARQHIEMSTTGWVGRFRPSEPHFTLDGNSFYKIISNEEGYRHICYFQIDKKDCTFITKGTWEVIGIEALTSDYLYYISNEYKGMPGGRNLYKIQLSDYTKVTCLSCELNPERCQYYSVSFSKEAKYYQLRCSGPGLPLYTLHSSVNDKGLRVLEDNSALDKMLQNVQMPSKKLDFIILNETKFWYQMILPPHFDKSKKYPLLLDVYAGPCSQKADTVFRLNWATYLASTENIIVASFDGRGSGYQGDKIMHAINRRLGTFEVEDQIEAARQFSKMGFVDNKRIAIWGWSYGGYVTSMVLGSGSGVFKCGIAVAPVSRWEYYDSVYTERYMGLPTPEDNLDHYRNSTVMSRAENFKQVEYLLIHGTADDNVHFQQSAQISKALVDVGVDFQAMWYTDEDHGIASSTAHQHIYTHMSHFIKQCFSLP,"Does not inhibit dipeptidyl peptidase activity, interaction with ADA and homodimer formation.",,MKTPWKVLLGLLGAAALVTIITVPVVLLNKGTDDATADSRKTYTLTDYLKNTYRLKLYSLRWISDHEYLYKQENNILVFNAEYGNSSVFLENSTFDEFGHSINDYSISPDGQFILLEYNYVKQWRHSYTASYDIYDLNKRQLITEERIPNNTQWVTWSPVGHKLAYVWNNDIYVKIEPNLPSYRITWTGKEDIIYNGITDWVYEEEVFSAYSALWWSPNGTFLAYAQFNDTEVPLIEYSFYSDESLQYPKTVRVPYPKAGAVNPTVKFFVVNTDSLSSVTNATSIQITAPASMLIGDHYLCDVTWATQERISLQWLRRIQNYSVMDICDYDESSGRWNCLVARQHIEMSTTGWVGRFRPSEPHFTLDGNSFYKIISNEEGYRHICYFQIDKKDCTFITKGTWEVIGIEALTSDYLYYISNEYKGMPGGRNLYKIQLSDYTKVTCLSCELNPERCQYYSVSFSKEAKYYQLRCSGPGLPLYTLHSSVNDKGLRVLEDNSALDKMLQNVQMPSKKLDFIILNETKFWYQMILPPHFDKSKKYPLLLDVYAGPCSQKADTVFRLNWATYLASTENIIVASFDGRGSGYQGDKIMHAINRRLGTFEVEDQIEAARQFSKMGFVDNKRIAIWGWSYGGYVTSMVLGSGSGVFKCGIAVAPVSRWEYYDSVYTERYMGLPTPEDNLDHYRNSTVMSRAENFKQVEYLLIHGTADDNVHFQQSAQISKALVDVGVDFQAMWYTDEDHGIASSTAHQHIYTHMSHFIKQCFSLP,Dipeptidyl peptidase 4,"Cell surface glycoprotein receptor involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. Acts as a positive regulator of T-cell coactivation, by binding at least ADA, CAV1, IGF2R, and PTPRC. Its binding to CAV1 and CARD11 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner. Its interaction with ADA also regulates lymphocyte-epithelial cell adhesion. In association with FAP is involved in the pericellular proteolysis of the extracellular matrix (ECM), the migration and invasion of endothelial cells into the ECM. May be involved in the promotion of lymphatic endothelial cells adhesion, migration and tube formation. When overexpressed, enhanced cell proliferation, a process inhibited by GPC3. Acts also as a serine exopeptidase with a dipeptidyl peptidase activity that regulates various physiological processes by cleaving peptides in the circulation, including many chemokines, mitogenic growth factors, neuropeptides and peptide hormones such as brain natriuretic peptide 32. Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline.(Microbial infection) Acts as a receptor for human coronavirus MERS-CoV-2.","Glycosylation of DPPIV at N85 is not required for catalysis, dimerization, or ADA binding.","Does not inhibit dipeptidyl peptidase activity, interaction with ADA and homodimer formation. Glycosylation of DPPIV at N85 is not required for catalysis, dimerization, or ADA binding."
2171,2171,2171,166891,Q53HL2-K26R,MAPRKGSSRVAKTNSLRRRKLASFLRDFDREVEIRIKQIESDRQNLLKEVDNLYNIEILRLPKALREMNWLDYFALGGNKQALEEAATADLDITEINKLTAEAIQTPLKSAKTRKVIQVDEMIVEEEEEEENERKNLQTARVKRCPPSKKRTQSIQGKGKGKRSSRANTVTPAVGRLEVSMVKPTPGLTPRFDSRVFKTPGLRTPAAGERIYNISGNGSPLADSKEIFLTVPVGGGESLRLLASDLQRHSIAQLDPEALGNIKKLSNRLAQICSSIRTHK,Fails to exhibit normal localization to the nucleolus in interphase depleted cells.,,MAPRKGSSRVAKTNSLRRRKLASFLKDFDREVEIRIKQIESDRQNLLKEVDNLYNIEILRLPKALREMNWLDYFALGGNKQALEEAATADLDITEINKLTAEAIQTPLKSAKTRKVIQVDEMIVEEEEEEENERKNLQTARVKRCPPSKKRTQSIQGKGKGKRSSRANTVTPAVGRLEVSMVKPTPGLTPRFDSRVFKTPGLRTPAAGERIYNISGNGSPLADSKEIFLTVPVGGGESLRLLASDLQRHSIAQLDPEALGNIKKLSNRLAQICSSIRTHK,Borealin,"Component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Major effector of the TTK kinase in the control of attachment-error-correction and chromosome alignment.",The mutation in Borealin affects the SUMO modification of Borealin during mitotic progression.,Fails to exhibit normal localization to the nucleolus in interphase depleted cells. The mutation in Borealin affects the SUMO modification of Borealin during mitotic progression.
2206,2206,2206,169036,P38398-C64G,MDLSALRVEEVQNVINAMQKILECPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKGPSQCPLGKNDITKRSLQESTRFSQLVEELLKIICAFQLDTGLEYANSYNFAKKENNSPEHLKDEVSIIQSMGYRNRAKRLLQSEPENPSLQETSLSVQLSNLGTVRTLRTKQRIQPQKTSVYIELGSDSSEDTVNKATYCSVGDQELLQITPQGTRDEISLDSAKKAACEFSETDVTNTEHHQPSNNDLNTTEKRAAERHPEKYQGSSVSNLHVEPCGTNTHASSLQHENSSLLLTKDRMNVEKAEFCNKSKQPGLARSQHNRWAGSKETCNDRRTPSTEKKVDLNADPLCERKEWNKQKLPCSENPRDTEDVPWITLNSSIQKVNEWFSRSDELLGSDDSHDGESESNAKVADVLDVLNEVDEYSGSSEKIDLLASDPHEALICKSERVHSKSVESNIEDKIFGKTYRKKASLPNLSHVTENLIIGAFVTEPQIIQERPLTNKLKRKRRPTSGLHPEDFIKKADLAVQKTPEMINQGTNQTEQNGQVMNITNSGHENKTKGDSIQNEKNPNPIESLEKESAFKTKAEPISSSISNMELELNIHNSKAPKKNRLRRKSSTRHIHALELVVSRNLSPPNCTELQIDSCSSSEEIKKKKYNQMPVRHSRNLQLMEGKEPATGAKKSNKPNEQTSKRHDSDTFPELKLTNAPGSFTKCSNTSELKEFVNPSLPREEKEEKLETVKVSNNAEDPKDLMLSGERVLQTERSVESSSISLVPGTDYGTQESISLLEVSTLGKAKTEPNKCVSQCAAFENPKGLIHGCSKDNRNDTEGFKYPLGHEVNHSRETSIEMEESELDAQYLQNTFKVSKRQSFAPFSNPGNAEEECATFSAHSGSLKKQSPKVTFECEQKEENQGKNESNIKPVQTVNITAGFPVVGQKDKPVDNAKCSIKGGSRFCLSSQFRGNETGLITPNKHGLLQNPYRIPPLFPIKSFVKTKCKKNLLEENFEEHSMSPEREMGNENIPSTVS,In BC; no interaction with BAP1.,,MDLSALRVEEVQNVINAMQKILECPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKGPSQCPLCKNDITKRSLQESTRFSQLVEELLKIICAFQLDTGLEYANSYNFAKKENNSPEHLKDEVSIIQSMGYRNRAKRLLQSEPENPSLQETSLSVQLSNLGTVRTLRTKQRIQPQKTSVYIELGSDSSEDTVNKATYCSVGDQELLQITPQGTRDEISLDSAKKAACEFSETDVTNTEHHQPSNNDLNTTEKRAAERHPEKYQGSSVSNLHVEPCGTNTHASSLQHENSSLLLTKDRMNVEKAEFCNKSKQPGLARSQHNRWAGSKETCNDRRTPSTEKKVDLNADPLCERKEWNKQKLPCSENPRDTEDVPWITLNSSIQKVNEWFSRSDELLGSDDSHDGESESNAKVADVLDVLNEVDEYSGSSEKIDLLASDPHEALICKSERVHSKSVESNIEDKIFGKTYRKKASLPNLSHVTENLIIGAFVTEPQIIQERPLTNKLKRKRRPTSGLHPEDFIKKADLAVQKTPEMINQGTNQTEQNGQVMNITNSGHENKTKGDSIQNEKNPNPIESLEKESAFKTKAEPISSSISNMELELNIHNSKAPKKNRLRRKSSTRHIHALELVVSRNLSPPNCTELQIDSCSSSEEIKKKKYNQMPVRHSRNLQLMEGKEPATGAKKSNKPNEQTSKRHDSDTFPELKLTNAPGSFTKCSNTSELKEFVNPSLPREEKEEKLETVKVSNNAEDPKDLMLSGERVLQTERSVESSSISLVPGTDYGTQESISLLEVSTLGKAKTEPNKCVSQCAAFENPKGLIHGCSKDNRNDTEGFKYPLGHEVNHSRETSIEMEESELDAQYLQNTFKVSKRQSFAPFSNPGNAEEECATFSAHSGSLKKQSPKVTFECEQKEENQGKNESNIKPVQTVNITAGFPVVGQKDKPVDNAKCSIKGGSRFCLSSQFRGNETGLITPNKHGLLQNPYRIPPLFPIKSFVKTKCKKNLLEENFEEHSMSPEREMGNENIPSTVS,Breast cancer type 1 susceptibility protein,"E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. It is unclear whether it also mediates the formation of other types of polyubiquitin chains. The BRCA1-BARD1 heterodimer coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability. Regulates centrosomal microtubule nucleation. Required for appropriate cell cycle arrests after ionizing irradiation in both the S-phase and the G2 phase of the cell cycle. Required for FANCD2 targeting to sites of DNA damage. Inhibits lipid synthesis by binding to inactive phosphorylated ACACA and preventing its dephosphorylation. Contributes to homologous recombination repair (HRR) via its direct interaction with PALB2, fine-tunes recombinational repair partly through its modulatory role in the PALB2-dependent loading of BRCA2-RAD51 repair machinery at DNA breaks. Component of the BRCA1-RBBP8 complex which regulates CHEK1 activation and controls cell cycle G2/M checkpoints on DNA damage via BRCA1-mediated ubiquitination of RBBP8. Acts as a transcriptional activator.",The mutation in the BAP1 protein has been identified.,In BC; no interaction with BAP1. The mutation in the BAP1 protein has been identified.
2220,2220,2220,170060,Q53HL2-S219A,MAPRKGSSRVAKTNSLRRRKLASFLKDFDREVEIRIKQIESDRQNLLKEVDNLYNIEILRLPKALREMNWLDYFALGGNKQALEEAATADLDITEINKLTAEAIQTPLKSAKTRKVIQVDEMIVEEEEEEENERKNLQTARVKRCPPSKKRTQSIQGKGKGKRSSRANTVTPAVGRLEVSMVKPTPGLTPRFDSRVFKTPGLRTPAAGERIYNISGNGAPLADSKEIFLTVPVGGGESLRLLASDLQRHSIAQLDPEALGNIKKLSNRLAQICSSIRTHK,"Decreases interaction with SOG1 and SOG2, abolishes localization to centromeres in prometaphase; when associated with A-106, A-171, A-185, A-189, A-199 and A-204.",,MAPRKGSSRVAKTNSLRRRKLASFLKDFDREVEIRIKQIESDRQNLLKEVDNLYNIEILRLPKALREMNWLDYFALGGNKQALEEAATADLDITEINKLTAEAIQTPLKSAKTRKVIQVDEMIVEEEEEEENERKNLQTARVKRCPPSKKRTQSIQGKGKGKRSSRANTVTPAVGRLEVSMVKPTPGLTPRFDSRVFKTPGLRTPAAGERIYNISGNGSPLADSKEIFLTVPVGGGESLRLLASDLQRHSIAQLDPEALGNIKKLSNRLAQICSSIRTHK,Borealin,"Component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Major effector of the TTK kinase in the control of attachment-error-correction and chromosome alignment.",,"Decreases interaction with SOG1 and SOG2, abolishes localization to centromeres in prometaphase; when associated with A-106, A-171, A-185, A-189, A-199 and A-204."
2221,2221,2221,170118,P28907-C173A,MANCEFSPVSGDKPCCRLSRRAQLCLGVSILVLILVVVLAVVVPRWRQQWSGPGTTKRFPETVLARCVKYTEIHPEMRHVDCQSVWDAFKGAFISKHPCNITEEDYQPLMKLGTQTVPCNKILLWSRIKDLAHQFTQVQRDMFTLEDTLLGYLADDLTWCGEFNTSKINYQSAPDWRKDCSNNPVSVFWKTVSRRFAEAACDVVHVMLNGSRSKIFDKNSTFGSVEVHNLQPEKVQTLEAWVIHGGREDSRDLCQDPTIKELESIISKRNIQFSCKNIYRPDKFLQCVKNPEDSSCTSEI,Loss of cADPR hydrolase and ADP-ribosyl cyclase activity.,,MANCEFSPVSGDKPCCRLSRRAQLCLGVSILVLILVVVLAVVVPRWRQQWSGPGTTKRFPETVLARCVKYTEIHPEMRHVDCQSVWDAFKGAFISKHPCNITEEDYQPLMKLGTQTVPCNKILLWSRIKDLAHQFTQVQRDMFTLEDTLLGYLADDLTWCGEFNTSKINYQSCPDWRKDCSNNPVSVFWKTVSRRFAEAACDVVHVMLNGSRSKIFDKNSTFGSVEVHNLQPEKVQTLEAWVIHGGREDSRDLCQDPTIKELESIISKRNIQFSCKNIYRPDKFLQCVKNPEDSSCTSEI,ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1,"Synthesizes cyclic ADP-ribose (cADPR), a second messenger for glucose-induced insulin secretion. Synthesizes the Ca(2+) mobilizer nicotinate-adenine dinucleotide phosphate, NAADP(+), from 2'-phospho-cADPR and nicotinic acid, as well as from NADP(+) and nicotinic acid. At both pH 5.0 and pH 7.4 preferentially transforms 2'-phospho-cADPR into NAADP(+), while preferentially cleaving NADP(+) to cADPR and ADPRP rather than into NADDP(+). Has cADPR hydrolase activity.",,Loss of cADPR hydrolase and ADP-ribosyl cyclase activity.
2222,2222,2222,170136,P13498-H94R,MGQIEWAMWANEQALASGLILITGGIVATAGRFTQWYFGAYSIVAGVFVCLLEYPRGKRKKGSTMERWGQKYMTAVVKLFGPFTRNYYVRAVLRLLLSVPAGFLLATILGTACLAIASGIYLLAAVRGEQWTPIEPKPRERPQIGGTIKQPPSNPPPRPPAEARKKPSEEEAAVAAGGPPGGPQVNPIPVTDEVV,In CGD4.,,MGQIEWAMWANEQALASGLILITGGIVATAGRFTQWYFGAYSIVAGVFVCLLEYPRGKRKKGSTMERWGQKYMTAVVKLFGPFTRNYYVRAVLHLLLSVPAGFLLATILGTACLAIASGIYLLAAVRGEQWTPIEPKPRERPQIGGTIKQPPSNPPPRPPAEARKKPSEEEAAVAAGGPPGGPQVNPIPVTDEVV,Cytochrome b-245 light chain,Critical component of the membrane-bound oxidase of phagocytes that generates superoxide. Associates with NOX3 to form a functional NADPH oxidase constitutively generating superoxide.,Amino acid replacement (H-94-->R),In CGD4. Amino acid replacement (H-94-->R)
2224,2224,2224,170247,Q9HB75-D826K,MAATVEGPELEAAAAAGDASEDSDAGSRALPFLGGNRLSLDLYPGGCQQLLHLCVQQPLQLLQVEFLRLSTHEDPQLLEATLAQLPQSLSCLRSLVLKGGQRRDTLGACLRGALTNLPAGLSGLAHLAHLDLSFNSLETLPACVLQMRGLGALLLSHNCLSELPEALGALPALTFLTVTHNRLQTLPPALGALSTLQRLDLSQNLLDTLPPEIGGLGSLLELNLASNRLQSLPASLAGLRSLRLLVLHSNLLASVPADLARLPLLTRLDLRDNQLRDLPPELLDAPFVRLQGNPLGEASPDAPSSPVAALIPEMPRLFLTSDLDSFPVTPQGCSVTLACGVRLQFPAGATATPITIRYRLLLPEPGLVPLGPHDALLSHVLELQPHGVAFQQDVGLWLLFTPPQARRCREVVVRTRNDNSWGDLETYLEEEAPQRLWAHCQVPHFSWFLVVSRPVSNACLVPPEGTLLCSSGHPGVKVIFPPGATEEPRRVSMQVVRMAGRELQALLGEPEAAVSPLLCLSQSGPPSFLQPVTVQLPLPSGITGLSLDRSRLHLLYWAPPAATWDDITAQVVLELTHLYARFQVTHFSWYWLWYTTKNCVGGLARKAWERLRLHRVNLIALQRRRDPEQVLLQCLPRNKVDATLRRLLERYRGPEPSDTVEMFEGEEFFAAFERGIDVDADRPDCVEGRICFVFYSHLKNVKEVYVTTTLDREAQAVRGQVSFYRGAVPVRVPEEAEAARQRKGADALWMATLPIKLPRLRGSEGPRRGAGLSLAPLNLGDAETGFLTQSNLLSVAGRLGLDWPAVALHLGVSYREVQRIRHEFRKDLDEQIRHMLFSWAERQAGQPGAVGLLVQALEQSDRQDVAEEVRAVLELGRRKYQDSIRRMGLAPKDPALPGSSAPQPPEPAQA,Partial loss of complex assembly with CRADD.,,MAATVEGPELEAAAAAGDASEDSDAGSRALPFLGGNRLSLDLYPGGCQQLLHLCVQQPLQLLQVEFLRLSTHEDPQLLEATLAQLPQSLSCLRSLVLKGGQRRDTLGACLRGALTNLPAGLSGLAHLAHLDLSFNSLETLPACVLQMRGLGALLLSHNCLSELPEALGALPALTFLTVTHNRLQTLPPALGALSTLQRLDLSQNLLDTLPPEIGGLGSLLELNLASNRLQSLPASLAGLRSLRLLVLHSNLLASVPADLARLPLLTRLDLRDNQLRDLPPELLDAPFVRLQGNPLGEASPDAPSSPVAALIPEMPRLFLTSDLDSFPVTPQGCSVTLACGVRLQFPAGATATPITIRYRLLLPEPGLVPLGPHDALLSHVLELQPHGVAFQQDVGLWLLFTPPQARRCREVVVRTRNDNSWGDLETYLEEEAPQRLWAHCQVPHFSWFLVVSRPVSNACLVPPEGTLLCSSGHPGVKVIFPPGATEEPRRVSMQVVRMAGRELQALLGEPEAAVSPLLCLSQSGPPSFLQPVTVQLPLPSGITGLSLDRSRLHLLYWAPPAATWDDITAQVVLELTHLYARFQVTHFSWYWLWYTTKNCVGGLARKAWERLRLHRVNLIALQRRRDPEQVLLQCLPRNKVDATLRRLLERYRGPEPSDTVEMFEGEEFFAAFERGIDVDADRPDCVEGRICFVFYSHLKNVKEVYVTTTLDREAQAVRGQVSFYRGAVPVRVPEEAEAARQRKGADALWMATLPIKLPRLRGSEGPRRGAGLSLAPLNLGDAETGFLTQSNLLSVAGRLGLDWPAVALHLGVSYREVQRIRHEFRDDLDEQIRHMLFSWAERQAGQPGAVGLLVQALEQSDRQDVAEEVRAVLELGRRKYQDSIRRMGLAPKDPALPGSSAPQPPEPAQA,p53-induced death domain-containing protein 1,"Component of the DNA damage/stress response pathway that functions downstream of p53/TP53 and can either promote cell survival or apoptosis. Associated with CRADD and the CASP2 caspase, it forms the PIDDosome a complex that activates CASP2 and triggers apoptosis. Associated with IKBKG and RIPK1, it enhances sumoylation and ubiquitination of IKBKG which is important for activation of the transcription factor NF-kappa-B.",,Partial loss of complex assembly with CRADD.
2235,2235,2235,171046,P20155-H47A,MALSVLRLALLLLAVTFAASLIPQFGLFSKYRTPNCSQYRLPGCPRAFNPVCGSDMSTYANECTLCMKIREGGHNIKIIRNGPC,Reduces inhibitory activity towards trypsin.,,MALSVLRLALLLLAVTFAASLIPQFGLFSKYRTPNCSQYRLPGCPRHFNPVCGSDMSTYANECTLCMKIREGGHNIKIIRNGPC,Serine protease inhibitor Kazal-type 2,"As a strong inhibitor of acrosin, it is required for normal spermiogenesis. It probably hinders premature activation of proacrosin and other proteases, thus preventing the cascade of events leading to spermiogenesis defects. May be involved in the regulation of serine protease-dependent germ cell apoptosis. It also inhibits trypsin.","The inhibition assay results demonstrated that R(24) at the P1 site is crucial for the specificity of SPINK2 on target enzyme. Although H(25) at the P1' and F(26) at the P2' residues are also involved in trypsin-SPINK2 interaction, P(23) at the P2 site may not be directly participated in interacting with trypsin.","Reduces inhibitory activity towards trypsin. The inhibition assay results demonstrated that R(24) at the P1 site is crucial for the specificity of SPINK2 on target enzyme. Although H(25) at the P1' and F(26) at the P2' residues are also involved in trypsin-SPINK2 interaction, P(23) at the P2 site may not be directly participated in interacting with trypsin."
2244,2244,2244,171860,Q7AKG8-C62S,MSCGEPHETDCSEILDHLYEFLDKEMPDSDCVKFEHHFEECSPCLEKYGLEQAVKKLVKRCSGQDDVPGDLRAKVMGRLDLIRSGQSVPEHDVAAAPSSSAPQES,"Reduced sporulation, normal induction of trxCp1, no binding of SigR.",,MSCGEPHETDCSEILDHLYEFLDKEMPDSDCVKFEHHFEECSPCLEKYGLEQAVKKLVKRCCGQDDVPGDLRAKVMGRLDLIRSGQSVPEHDVAAAPSSSAPQES,Anti-sigma factor RsrA,"A redox-regulated anti-sigma factor for extracytoplasmic function (ECF) sigma factor SigR, and a key sensor of disulfide stress. Holds SigR, its cognate ECF sigma factor, in an inactive form, inhibiting its sigma activity under reducing but not oxidizing conditions; oxidation and reduction of the anti-sigma factor is reversible. Mycothiol (MSH) is competent for reduction of RsrA, allowing it to bind to SigR. In conjunction with its cognate sigma factor SigR may sense the intracellular level of reduced MSH. Probably releases SigR during oxidative stress.",,"Reduced sporulation, normal induction of trxCp1, no binding of SigR."
2264,2264,2264,173221,Q53K16-K284A,MAYMCADSGNLMAIAQQVIQQQQQQQQQQQRHHHHHHLPPPPPPQSMAPHHHQQKHHHHHQQMPAMPQAPPSSHGQIPGQLAYGGGAAWPAGEHFFADAFGASAGDAVFSDLAAAADFDSDGWMESLIGDAPFQDSDLERLIFTTPPPPVPSPPPTHAAATATATAATAAPRPEAAPALLPQPAAATPVACSSPSPSSADASCSAPILQSLLSCSRAAATDPGLAAAELASVRAAATDAGDPSERLAFYFADALSRRLACGTGAPPSAEPDARFASDELTLCYATLNDACPYSKFAHLTANQAILEATGAATKIHIVDFGIVQGIQWAALLQALATRPEGKPTRIRITGVPSPLLGPQPAASLAATNTRLRDFAKLLGVDFEFVPLLRPVHELNKSDFLVEPDEAVAVNFMLQLYHLLGDSDELVRRVLRLAKSLSPAVVTLGEYEVSLNRAGFVDRFANALSYYRSLFESLDVAMTRDSPERVRVERWMFGERIQRAVGPEEGADRTERMAGSSEWQTLMEWCGFEPVPLSNYARSQADLLLWNYDSKYKYSLVELPPAFLSLAWEKRPLLTVSAWR,Does not affect DNA-binding.,,MAYMCADSGNLMAIAQQVIQQQQQQQQQQQRHHHHHHLPPPPPPQSMAPHHHQQKHHHHHQQMPAMPQAPPSSHGQIPGQLAYGGGAAWPAGEHFFADAFGASAGDAVFSDLAAAADFDSDGWMESLIGDAPFQDSDLERLIFTTPPPPVPSPPPTHAAATATATAATAAPRPEAAPALLPQPAAATPVACSSPSPSSADASCSAPILQSLLSCSRAAATDPGLAAAELASVRAAATDAGDPSERLAFYFADALSRRLACGTGAPPSAEPDARFASDELTLCYKTLNDACPYSKFAHLTANQAILEATGAATKIHIVDFGIVQGIQWAALLQALATRPEGKPTRIRITGVPSPLLGPQPAASLAATNTRLRDFAKLLGVDFEFVPLLRPVHELNKSDFLVEPDEAVAVNFMLQLYHLLGDSDELVRRVLRLAKSLSPAVVTLGEYEVSLNRAGFVDRFANALSYYRSLFESLDVAMTRDSPERVRVERWMFGERIQRAVGPEEGADRTERMAGSSEWQTLMEWCGFEPVPLSNYARSQADLLLWNYDSKYKYSLVELPPAFLSLAWEKRPLLTVSAWR,SCARECROW-LIKE protein 7,Probable transcription factor involved in plant development. Involved in environmental abiotic stress resistance. May increase the expression of stress-responsive genes. Binds DNA in vitro.,"The structure of the GRAS domain of Os-SCL7 from rice (Oryza sativa) has been determined to 1. 82 Å. The structure includes cap and core subdomains and elucidates the features of the conserved GRAS LRI, VHIID, LRII, PFYRE, and SAW motifs. The structure is a dimer, with a clear groove to accommodate double-stranded DNA. Docking a DNA segment into the groove to generate an Os-SCL7/DNA complex provides insight into the DNA binding mechanism of GRAS proteins. Furthermore, the in vitro DNA binding property of Os-SCL7 and model-defined recognition residues are assessed by electrophoretic mobility shift analysis and mutagenesis assays.","Does not affect DNA-binding. The structure of the GRAS domain of Os-SCL7 from rice (Oryza sativa) has been determined to 1. 82 Å. The structure includes cap and core subdomains and elucidates the features of the conserved GRAS LRI, VHIID, LRII, PFYRE, and SAW motifs. The structure is a dimer, with a clear groove to accommodate double-stranded DNA. Docking a DNA segment into the groove to generate an Os-SCL7/DNA complex provides insight into the DNA binding mechanism of GRAS proteins. Furthermore, the in vitro DNA binding property of Os-SCL7 and model-defined recognition residues are assessed by electrophoretic mobility shift analysis and mutagenesis assays."
2273,2273,2273,173943,Q9NXA8-Y102F,MRPLQIVPSRLISQLYCGLKPPASTRNQICLKMARPSSSMADFRKFFAKAKHIVIISGAGVSAESGVPTFRGAGGYWRKWQAQDLATPLAFAHNPSRVWEFFHYRREVMGSKEPNAGHRAIAECETRLGKQGRRVVVITQNIDELHRKAGTKNLLEIHGSLFKTRCTSCGVVAENYKSPICPALSGKGAPEPGTQDASIPVEKLPRCEEAGCGGLLRPHVVWFGENLDPAILEEVDRELAHCDLCLVVGTSSVVYPAAMFAPQVAARGVPVAEFNTETTPATNRFRFHFQGPCGTTLPEALACHENETVS,Increases the KM for desuccinylation.,,MRPLQIVPSRLISQLYCGLKPPASTRNQICLKMARPSSSMADFRKFFAKAKHIVIISGAGVSAESGVPTFRGAGGYWRKWQAQDLATPLAFAHNPSRVWEFYHYRREVMGSKEPNAGHRAIAECETRLGKQGRRVVVITQNIDELHRKAGTKNLLEIHGSLFKTRCTSCGVVAENYKSPICPALSGKGAPEPGTQDASIPVEKLPRCEEAGCGGLLRPHVVWFGENLDPAILEEVDRELAHCDLCLVVGTSSVVYPAAMFAPQVAARGVPVAEFNTETTPATNRFRFHFQGPCGTTLPEALACHENETVS,"NAD-dependent protein deacylase sirtuin-5, mitochondrial","NAD-dependent lysine demalonylase, desuccinylase and deglutarylase that specifically removes malonyl, succinyl and glutaryl groups on target proteins. Activates CPS1 and contributes to the regulation of blood ammonia levels during prolonged fasting: acts by mediating desuccinylation and deglutarylation of CPS1, thereby increasing CPS1 activity in response to elevated NAD levels during fasting. Activates SOD1 by mediating its desuccinylation, leading to reduced reactive oxygen species. Activates SHMT2 by mediating its desuccinylation. Modulates ketogenesis through the desuccinylation and activation of HMGCS2. Has weak NAD-dependent protein deacetylase activity; however this activity may not be physiologically relevant in vivo. Can deacetylate cytochrome c (CYCS) and a number of other proteins in vitro such as UOX.",Sirt5 is an efficient protein lysine desuccinylase and demalonylase in vitro. The preference for succinyl and malonyl groups was explained by the presence of a tyrosine residue (Y(102)) in the acyl pocket of Sirt5.,Increases the KM for desuccinylation. Sirt5 is an efficient protein lysine desuccinylase and demalonylase in vitro. The preference for succinyl and malonyl groups was explained by the presence of a tyrosine residue (Y(102)) in the acyl pocket of Sirt5.
2279,2279,2279,174425,Q7SIG4-Q304W,MEIPVIEPLFTKVTEDIPGAEGPVFDKNGDFYIVAPEVEVNGKPAGEILRIDLKTGKKTVICKPEVNGYGGIPAGCQCDRDANQLFVADMRLGLLVVQTDGTFEEIAKKDSEGRRMQGCNDCAFDYEGNLWITAPAGEVAPADYTRSMQEKFGSIYCFTTDGQMIQVDTAFQFPNGIAVRHMNDGRPYQLIVAETPTKKLWSYDIKGPAKIENKKVWGHIPGTHEGGADGMDFDEDNNLLVANWGSSHIEVFGPDGGQPKMRIRCPFEKPSNLHFKPQTKTIFVTEHENNAVWKFEWQRNGKKWYCETLKFGIF,3% decrease in activity.,,MEIPVIEPLFTKVTEDIPGAEGPVFDKNGDFYIVAPEVEVNGKPAGEILRIDLKTGKKTVICKPEVNGYGGIPAGCQCDRDANQLFVADMRLGLLVVQTDGTFEEIAKKDSEGRRMQGCNDCAFDYEGNLWITAPAGEVAPADYTRSMQEKFGSIYCFTTDGQMIQVDTAFQFPNGIAVRHMNDGRPYQLIVAETPTKKLWSYDIKGPAKIENKKVWGHIPGTHEGGADGMDFDEDNNLLVANWGSSHIEVFGPDGGQPKMRIRCPFEKPSNLHFKPQTKTIFVTEHENNAVWKFEWQRNGKKQYCETLKFGIF,Diisopropyl-fluorophosphatase,"Biological function and substrate unknown. However, it is capable of acting on phosphorus anhydride bonds (such as phosphorus-halide and phosphorus-cyanide) in organophosphorus compounds (including nerve gases).",,3% decrease in activity.
2282,2282,2282,174739,Q14524-V146M,MANFLLPRGTSSFRRFTRESLAAIEKRMAEKQARGSTTLQESREGLPEEEAPRPQLDLQASKKLPDLYGNPPQELIGEPLEDLDPFYSTQKTFIVLNKGKTIFRFSATNALYVLSPFHPIRRAAVKILVHSLFNMLIMCTILTNCMFMAQHDPPPWTKYVEYTFTAIYTFESLVKILARGFCLHAFTFLRDPWNWLDFSVIIMAYTTEFVDLGNVSALRTFRVLRALKTISVISGLKTIVGALIQSVKKLADVMVLTVFCLSVFALIGLQLFMGNLRHKCVRNFTALNGTNGSVEADGLVWESLDLYLSDPENYLLKNGTSDVLLCGNSSDAGTCPEGYRCLKAGENPDHGYTSFDSFAWAFLALFRLMTQDCWERLYQQTLRSAGKIYMIFFMLVIFLGSFYLVNLILAVVAMAYEEQNQATIAETEEKEKRFQEAMEMLKKEHEALTIRGVDTVSRSSLEMSPLAPVNSHERRSKRRKRMSSGTEECGEDRLPKSDSEDGPRAMNHLSLTRGLSRTSMKPRSSRGSIFTFRRRDLGSEADFADDENSTAGESESHHTSLLVPWPLRRTSAQGQPSPGTSAPGHALHGKKNSTVDCNGVVSLLGAGDPEATSPGSHLLRPVMLEHPPDTTTPSEEPGGPQMLTSQAPCVDGFEEPGARQRALSAVSVLTSALEELEESRHKCPPCWNRLAQRYLIWECCPLWMSIKQGVKLVVMDPFTDLTITMCIVLNTLFMALEHYNMTSEFEEMLQVGNLVFTGIFTAEMTFKIIALDPYYYFQQGWNIFDSIIVILSLMELGLSRMSNLSVLRSFRLLRVFKLAKSWPTLNTLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKNYSELRDSDSGLLPRWHMMDFFHAFLIIFRILCGEWIETMWDCMEVSGQSLCLLVFLLVMVIGNLVVLNLFLALLLSSFSADNLTAPDEDREMNNLQLALARIQRGLRFVKRTTWDFCCGLLRQRPQKPAALAAQGQLPSCIATPYSPPPPETEKVPPTRK,In BRGDA1; unknown pathological significance.,,MANFLLPRGTSSFRRFTRESLAAIEKRMAEKQARGSTTLQESREGLPEEEAPRPQLDLQASKKLPDLYGNPPQELIGEPLEDLDPFYSTQKTFIVLNKGKTIFRFSATNALYVLSPFHPIRRAAVKILVHSLFNMLIMCTILTNCVFMAQHDPPPWTKYVEYTFTAIYTFESLVKILARGFCLHAFTFLRDPWNWLDFSVIIMAYTTEFVDLGNVSALRTFRVLRALKTISVISGLKTIVGALIQSVKKLADVMVLTVFCLSVFALIGLQLFMGNLRHKCVRNFTALNGTNGSVEADGLVWESLDLYLSDPENYLLKNGTSDVLLCGNSSDAGTCPEGYRCLKAGENPDHGYTSFDSFAWAFLALFRLMTQDCWERLYQQTLRSAGKIYMIFFMLVIFLGSFYLVNLILAVVAMAYEEQNQATIAETEEKEKRFQEAMEMLKKEHEALTIRGVDTVSRSSLEMSPLAPVNSHERRSKRRKRMSSGTEECGEDRLPKSDSEDGPRAMNHLSLTRGLSRTSMKPRSSRGSIFTFRRRDLGSEADFADDENSTAGESESHHTSLLVPWPLRRTSAQGQPSPGTSAPGHALHGKKNSTVDCNGVVSLLGAGDPEATSPGSHLLRPVMLEHPPDTTTPSEEPGGPQMLTSQAPCVDGFEEPGARQRALSAVSVLTSALEELEESRHKCPPCWNRLAQRYLIWECCPLWMSIKQGVKLVVMDPFTDLTITMCIVLNTLFMALEHYNMTSEFEEMLQVGNLVFTGIFTAEMTFKIIALDPYYYFQQGWNIFDSIIVILSLMELGLSRMSNLSVLRSFRLLRVFKLAKSWPTLNTLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKNYSELRDSDSGLLPRWHMMDFFHAFLIIFRILCGEWIETMWDCMEVSGQSLCLLVFLLVMVIGNLVVLNLFLALLLSSFSADNLTAPDEDREMNNLQLALARIQRGLRFVKRTTWDFCCGLLRQRPQKPAALAAQGQLPSCIATPYSPPPPETEKVPPTRK,Sodium channel protein type 5 subunit alpha,"This protein mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient. It is a tetrodotoxin-resistant Na(+) channel isoform. This channel is responsible for the initial upstroke of the action potential. Channel inactivation is regulated by intracellular calcium levels.",,In BRGDA1; unknown pathological significance.
2286,2286,2286,174784,P00973-D75A,MMDLRNTPAKSLDKFIEDYLLPDTCFRMQINHAIDIICGFLKERCFRGSSYPVCVSKVVKGGSSGKGTTLRGRSAADLVVFLSPLTTFQDQLNRRGEFIQEIRRQLEACQRERAFSVKFEVQAPRWGNPRALSFVLSSLQLGEGVEFDVLPAFDALGQLTGGYKPNPQIYVKLIEECTDLQKEGEFSTCFTELQRDFLKQRPTKLKSLIRLVKHWYQNCKKKLGKLPPQYALELLTVYAWERGSMKTHFNTAQGFRTVLELVINYQQLCIYWTKYYDFKNPIIEKYLRRQLTKPRPVILDPADPTGNLGGGDPKGWRQLAQEAEAWLNYPCFKNWDGSPVSSWILLAESNSADDETDDPRRYQKYGYIGTHEYPHFSHRPSTLQAASTPQAEEDWTCTIL,Loss of activity; when associated with A-77.,,MMDLRNTPAKSLDKFIEDYLLPDTCFRMQINHAIDIICGFLKERCFRGSSYPVCVSKVVKGGSSGKGTTLRGRSDADLVVFLSPLTTFQDQLNRRGEFIQEIRRQLEACQRERAFSVKFEVQAPRWGNPRALSFVLSSLQLGEGVEFDVLPAFDALGQLTGGYKPNPQIYVKLIEECTDLQKEGEFSTCFTELQRDFLKQRPTKLKSLIRLVKHWYQNCKKKLGKLPPQYALELLTVYAWERGSMKTHFNTAQGFRTVLELVINYQQLCIYWTKYYDFKNPIIEKYLRRQLTKPRPVILDPADPTGNLGGGDPKGWRQLAQEAEAWLNYPCFKNWDGSPVSSWILLAESNSADDETDDPRRYQKYGYIGTHEYPHFSHRPSTLQAASTPQAEEDWTCTIL,2'-5'-oligoadenylate synthase 1,"Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response. In addition, it may also play a role in other cellular processes such as apoptosis, cell growth, differentiation and gene regulation. Synthesizes higher oligomers of 2'-5'-oligoadenylates (2-5A) from ATP which then bind to the inactive monomeric form of ribonuclease L (RNase L) leading to its dimerization and subsequent activation. Activation of RNase L leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication. Can mediate the antiviral effect via the classical RNase L-dependent pathway or an alternative antiviral pathway independent of RNase L. The secreted form displays antiviral effect against vesicular stomatitis virus (VSV), herpes simplex virus type 2 (HSV-2), and encephalomyocarditis virus (EMCV) and stimulates the alternative antiviral pathway independent of RNase L.When prenylated at C-terminal, acts as a double-stranded RNA (dsRNA) sensor specifically targeted to membranous replicative organelles in SARS coronavirus-2/SARS-CoV-2 infected cells where it binds to dsRNA structures in the SARS-CoV-2 5'-UTR and initiates a potent block to SARS-CoV-2 replication. Recognizes short stretches of dsRNA and activates RNase L. The binding is remarkably specific, with two conserved stem loops in the SARS-CoV-2 5'- untranslated region (UTR) constituting the principal viral target. The same mechanism is necessary to initiate a block to cardiovirus EMCV.Not prenylated at C-terminal, is diffusely localized and unable to initiate a detectable block to SARS-CoV-2 replication.",Mutation of the D75 residue inactivated the enzyme without affecting its substrate and activator binding capacity.,Loss of activity; when associated with A-77. Mutation of the D75 residue inactivated the enzyme without affecting its substrate and activator binding capacity.
2288,2288,2288,174888,Q9Y4F9-S585A,MLVGSQSFSPGGPNGIIRSQSFAGFSGLQERRSRCNSFIENSSALKKPQAKLKKMHNLGHKNNNPPKEPQPKRVEEVYRALKNGLDEYLEVHQTELDKLTAQLKDMKRNSRLGVLYDLDKQIKTIERYMRRLEFHISKVDELYEAYCIQRRLQDGASKMKQAFATSPASKAARESLTEINRSFKEYTENMCTIEVELENLLGEFSIKMKGLAGFARLCPGDQYEIFMKYGRQRWKLKGKIEVNGKQSWDGEETVFLPLIVGFISIKVTELKGLATHILVGSVTCETKELFAARPQVVAVDINDLGTIKLNLEITWYPFDVEDMTASSGAGNKAAALQRRMSMYSQGTPETPTFKDHSFFRWLHPSPDKPRRLSVLSALQDTFFAKLHRSRSFSDLPSLRPSPKAVLELYSNLPDDIFENGKAAEEKMPLSLSFSDLPNGDCALTSHSTGSPSNSTNPEITITPAEFNLSSLASQNEGMDDTSSASSRNSLGEGQEPKSHLKEEDPEEPRKPASAPSEACRRQSSGAGAEHLFLENDVAEALLQESEEASELKPVELDTSEGNITKQLVKRLTSAEVPMATDRLLAEGSVGGESEGCRSFLDGSLEDAFNGLLLALEPHKEQYKEFQDLNQEVMNLDDILKCKPAVSRSRSSSLSLTVESALESFDFLNTSDFDEEEDGDEVCNVGGGADSVFSDTETEKHSYRSVHPEARGHLSEALTEDTGVGTSVAGSPLPLTTGNESLDITIVRHLQYCTQLVQQIVFSSKTPFVARSLLEKLSRQIQVMEKLAAVSDENIGNISSVVEAIPEFHKKLSLLSFWTKCCSPVGVYHSPADRVMKQLEASFARTVNKEYPGLADPVFRTLVSQILDRAEPLLSSSLSSEVVTVFQYYSYFTSHGVSDLESYLSQLARQVSMVQTLQSLRDEKLLQTMSDLAPSNLLAQQEVLRTLALLLTREDNEVSEAVTLYLAAASKNQHFREKALLYYCEALTKTNLQLQKAACLALKILEATESIKMLVTLCQSDTEEI,"Reduces phosphorylation, interaction with HDAC6, YWHAB and 14-3-3 proteins, localization at the front of the neutrophil upon chemokine stimulation and prevents T cell proliferation inhibition; when associated with A-21; A-37; A-341 and A-523 (isoform 2).",,MLVGSQSFSPGGPNGIIRSQSFAGFSGLQERRSRCNSFIENSSALKKPQAKLKKMHNLGHKNNNPPKEPQPKRVEEVYRALKNGLDEYLEVHQTELDKLTAQLKDMKRNSRLGVLYDLDKQIKTIERYMRRLEFHISKVDELYEAYCIQRRLQDGASKMKQAFATSPASKAARESLTEINRSFKEYTENMCTIEVELENLLGEFSIKMKGLAGFARLCPGDQYEIFMKYGRQRWKLKGKIEVNGKQSWDGEETVFLPLIVGFISIKVTELKGLATHILVGSVTCETKELFAARPQVVAVDINDLGTIKLNLEITWYPFDVEDMTASSGAGNKAAALQRRMSMYSQGTPETPTFKDHSFFRWLHPSPDKPRRLSVLSALQDTFFAKLHRSRSFSDLPSLRPSPKAVLELYSNLPDDIFENGKAAEEKMPLSLSFSDLPNGDCALTSHSTGSPSNSTNPEITITPAEFNLSSLASQNEGMDDTSSASSRNSLGEGQEPKSHLKEEDPEEPRKPASAPSEACRRQSSGAGAEHLFLENDVAEALLQESEEASELKPVELDTSEGNITKQLVKRLTSAEVPMATDRLLSEGSVGGESEGCRSFLDGSLEDAFNGLLLALEPHKEQYKEFQDLNQEVMNLDDILKCKPAVSRSRSSSLSLTVESALESFDFLNTSDFDEEEDGDEVCNVGGGADSVFSDTETEKHSYRSVHPEARGHLSEALTEDTGVGTSVAGSPLPLTTGNESLDITIVRHLQYCTQLVQQIVFSSKTPFVARSLLEKLSRQIQVMEKLAAVSDENIGNISSVVEAIPEFHKKLSLLSFWTKCCSPVGVYHSPADRVMKQLEASFARTVNKEYPGLADPVFRTLVSQILDRAEPLLSSSLSSEVVTVFQYYSYFTSHGVSDLESYLSQLARQVSMVQTLQSLRDEKLLQTMSDLAPSNLLAQQEVLRTLALLLTREDNEVSEAVTLYLAAASKNQHFREKALLYYCEALTKTNLQLQKAACLALKILEATESIKMLVTLCQSDTEEI,Rho family-interacting cell polarization regulator 2,"Acts as an inhibitor of the small GTPase RHOA and plays several roles in the regulation of myoblast and hair cell differentiation, lymphocyte T proliferation and neutrophil polarization. Inhibits chemokine-induced T lymphocyte responses, such as cell adhesion, polarization and migration. Involved also in the regulation of neutrophil polarization, chemotaxis and adhesion. Required for normal development of inner and outer hair cell stereocilia within the cochlea of the inner ear. Plays a role for maintaining the structural organization of the basal domain of stereocilia. Involved in mechanosensory hair cell function. Required for normal hearing.Acts as an inhibitor of the small GTPase RHOA. Plays a role in fetal mononuclear myoblast differentiation by promoting filopodia and myotube formation. Maintains naive T lymphocytes in a quiescent state.",,"Reduces phosphorylation, interaction with HDAC6, YWHAB and 14-3-3 proteins, localization at the front of the neutrophil upon chemokine stimulation and prevents T cell proliferation inhibition; when associated with A-21; A-37; A-341 and A-523 (isoform 2)."
2290,2290,2290,175087,Q6NZQ8-Y232F,MLGWCEAIARNPHRIPNTTRTPETSGDVADASQTSTLNEKSPGRSASRSSNISKASSPTTGTAPRSQSRLSVCPSTQDICRICHCEGDEESPLITPCRCTGTLRFVHQSCLHQWIKSSDTRCCELCKYDFIMETKLKPLRKWEKLQMTTSERRKIFCSVTFHVIAVTCVVWSLYVLIDRTAEEIKQGNDNGVLEWPFWTKLVVVAIGFTGGLVFMYVQCKVYVQLWRRLKAFNRVIFVQNCPDTANKLEKNFPCNVNTEIKDAVVVPVPQTGSNTLPTAEGAPPEVIPV,Almost complete loss of down-regulation of CD86 cell surface expression; when associated with S-225.,,MLGWCEAIARNPHRIPNTTRTPETSGDVADASQTSTLNEKSPGRSASRSSNISKASSPTTGTAPRSQSRLSVCPSTQDICRICHCEGDEESPLITPCRCTGTLRFVHQSCLHQWIKSSDTRCCELCKYDFIMETKLKPLRKWEKLQMTTSERRKIFCSVTFHVIAVTCVVWSLYVLIDRTAEEIKQGNDNGVLEWPFWTKLVVVAIGFTGGLVFMYVQCKVYVQLWRRLKAYNRVIFVQNCPDTANKLEKNFPCNVNTEIKDAVVVPVPQTGSNTLPTAEGAPPEVIPV,E3 ubiquitin-protein ligase MARCHF1,"E3 ubiquitin-protein ligase that mediates ubiquitination of TFRC, CD86, FAS and MHC class II proteins, such as HLA-DR alpha and beta, and promotes their subsequent endocytosis and sorting to lysosomes via multivesicular bodies. By constitutively ubiquitinating MHC class II proteins in immature dendritic cells, down-regulates their cell surface localization thus sequestering them in the intracellular endosomal system.",,Almost complete loss of down-regulation of CD86 cell surface expression; when associated with S-225.
2304,2304,2304,175983,Q12948-I91T,MQARYSVSSPNSLGVVPYLGGEQSYYRAAAAAAGGGYTAMPAPMSVYSHPAHAEQYPGGMARAYGPYTPQPQPKDMVKPPYSYIALITMATQNAPDKKITLNGIYQFIMDRFPFYRDNKQGWQNSIRHNLSLNECFVKVPRDDKKPGKGSYWTLDPDSYNMFENGSFLRRRRRFKKKDAVKDKEEKDRLHLKEPPPPGRQPPPAPPEQADGNAPGPQPPPVRIQDIKTENGTCPSPPQPLSPAAALGSGSAAAVPKIESPDSSSSSLSSGSSPPGSLPSARPLSLDGADSAPPPPAPSAPPPHHSQGFSVDNIMTSLRGSPQSAAAELSSGLLASAAASSRAGIAPPLALGAYSPGQSSLYSSPCSQTSSAGSSGGGGGGAGAAGGAGGAGTYHCNLQAMSLYAAGERGGHLQGAPGGAGGSAVDDPLPDYSLPPVTSSSSSSLSHGGGGGGGGGGQEAGHHPAAHQGRLTSWYLNQAGGDLGHLASAAAAAAAAGYPGQQQNFHSVREMFESQRIGLNNSPVNGNSSCQMAFPSSQSLYRTSGAFVYDCSKF,In RIEG3; decreased location at the nucleus; decreased transcription regulatory region DNA binding; decreased sequence-specific DNA binding transcription factor activity; no change on DNA bending activity.,,MQARYSVSSPNSLGVVPYLGGEQSYYRAAAAAAGGGYTAMPAPMSVYSHPAHAEQYPGGMARAYGPYTPQPQPKDMVKPPYSYIALITMAIQNAPDKKITLNGIYQFIMDRFPFYRDNKQGWQNSIRHNLSLNECFVKVPRDDKKPGKGSYWTLDPDSYNMFENGSFLRRRRRFKKKDAVKDKEEKDRLHLKEPPPPGRQPPPAPPEQADGNAPGPQPPPVRIQDIKTENGTCPSPPQPLSPAAALGSGSAAAVPKIESPDSSSSSLSSGSSPPGSLPSARPLSLDGADSAPPPPAPSAPPPHHSQGFSVDNIMTSLRGSPQSAAAELSSGLLASAAASSRAGIAPPLALGAYSPGQSSLYSSPCSQTSSAGSSGGGGGGAGAAGGAGGAGTYHCNLQAMSLYAAGERGGHLQGAPGGAGGSAVDDPLPDYSLPPVTSSSSSSLSHGGGGGGGGGGQEAGHHPAAHQGRLTSWYLNQAGGDLGHLASAAAAAAAAGYPGQQQNFHSVREMFESQRIGLNNSPVNGNSSCQMAFPSSQSLYRTSGAFVYDCSKF,Forkhead box protein C1,"DNA-binding transcriptional factor that plays a role in a broad range of cellular and developmental processes such as eye, bones, cardiovascular, kidney and skin development. Acts either as a transcriptional activator or repressor. Binds to the consensus binding site 5'-[G/C][A/T]AAA[T/C]AA[A/C]-3' in promoter of target genes. Upon DNA-binding, promotes DNA bending. Acts as a transcriptional coactivator. Stimulates Indian hedgehog (Ihh)-induced target gene expression mediated by the transcription factor GLI2, and hence regulates endochondral ossification. Acts also as a transcriptional coregulator by increasing DNA-binding capacity of GLI2 in breast cancer cells. Regulates FOXO1 through binding to a conserved element, 5'-GTAAACAAA-3' in its promoter region, implicating FOXC1 as an important regulator of cell viability and resistance to oxidative stress in the eye. Cooperates with transcription factor FOXC2 in regulating expression of genes that maintain podocyte integrity. Promotes cell growth inhibition by stopping the cell cycle in the G1 phase through TGFB1-mediated signals. Involved in epithelial-mesenchymal transition (EMT) induction by increasing cell proliferation, migration and invasion. Involved in chemokine CXCL12-induced endothelial cell migration through the control of CXCR4 expression. Plays a role in the gene regulatory network essential for epidermal keratinocyte terminal differentiation. Essential developmental transcriptional factor required for mesoderm-derived tissues, such as the somites, skin, bone and cartilage. Positively regulates CXCL12 and stem cell factor expression in bone marrow mesenchymal progenitor cells, and hence plays a role in the development and maintenance of mesenchymal niches for haematopoietic stem and progenitor cells (HSPC). Plays a role in corneal transparency by preventing both blood vessel and lymphatic vessel growth during embryonic development in a VEGF-dependent manner. Involved in chemokine CXCL12-induced endothelial cell migration through the control of CXCR4 expression. May function as a tumor suppressor.",The mutation may generate local disruptions to the structure of the forkhead domain.,In RIEG3; decreased location at the nucleus; decreased transcription regulatory region DNA binding; decreased sequence-specific DNA binding transcription factor activity; no change on DNA bending activity. The mutation may generate local disruptions to the structure of the forkhead domain.
2305,2305,2305,176063,P63141-I402T,MTVATGDPVDEAAALPGHPQDTYDPEADHECCERVVINISGLRFETQLKTLAQFPETLLGDPKKRMRYFDPLRNEYFFDRNRPSFDAILYYYQSGGRLRRPVNVPLDIFSEEIRFYELGEEAMEMFREDEGYIKEEERPLPENEFQRQVWLLFEYPESSGPARIIAIVSVMVILISIVSFCLETLPIFRDENEDMHGGGVTFHTYSNSTIGYQQSTSFTDPFFIVETLCIIWFSFEFLVRFFACPSKAGFFTNIMNIIDIVAIIPYFITLGTELAEKPEDAQQGQQAMSLAILRVIRLVRVFRIFKLSRHSKGLQILGQTLKASMRELGLLIFFLFIGVILFSSAVYFAEADERDSQFPSIPDAFWWAVVSMTTVGYGDMVPTTIGGKIVGSLCAIAGVLTTALPVPVIVSNFNYFYHRETEGEEQAQYLQVTSCPKIPSSPDLKKSRSASTISKSDYMEIQEGVNNSNEDFREENLKTANCTLANTNYVNITKMLTDV,In Pgu; chronic motor incoordination; decreases the number of functional channels at the cell surface.,,MTVATGDPVDEAAALPGHPQDTYDPEADHECCERVVINISGLRFETQLKTLAQFPETLLGDPKKRMRYFDPLRNEYFFDRNRPSFDAILYYYQSGGRLRRPVNVPLDIFSEEIRFYELGEEAMEMFREDEGYIKEEERPLPENEFQRQVWLLFEYPESSGPARIIAIVSVMVILISIVSFCLETLPIFRDENEDMHGGGVTFHTYSNSTIGYQQSTSFTDPFFIVETLCIIWFSFEFLVRFFACPSKAGFFTNIMNIIDIVAIIPYFITLGTELAEKPEDAQQGQQAMSLAILRVIRLVRVFRIFKLSRHSKGLQILGQTLKASMRELGLLIFFLFIGVILFSSAVYFAEADERDSQFPSIPDAFWWAVVSMTTVGYGDMVPTTIGGKIVGSLCAIAGVLTIALPVPVIVSNFNYFYHRETEGEEQAQYLQVTSCPKIPSSPDLKKSRSASTISKSDYMEIQEGVNNSNEDFREENLKTANCTLANTNYVNITKMLTDV,Potassium voltage-gated channel subfamily A member 2,"Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain and the central nervous system, but also in the cardiovascular system. Prevents aberrant action potential firing and regulates neuronal output. Forms tetrameric potassium-selective channels through which potassium ions pass in accordance with their electrochemical gradient. The channel alternates between opened and closed conformations in response to the voltage difference across the membrane. Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCNA1, KCNA2, KCNA4, KCNA5, KCNA6, KCNA7, and possibly other family members as well; channel properties depend on the type of alpha subunits that are part of the channel. Channel properties are modulated by cytoplasmic beta subunits that regulate the subcellular location of the alpha subunits and promote rapid inactivation of delayed rectifier potassium channels. In vivo, membranes probably contain a mixture of heteromeric potassium channel complexes, making it difficult to assign currents observed in intact tissues to any particular potassium channel family member. Homotetrameric KCNA2 forms a delayed-rectifier potassium channel that opens in response to membrane depolarization, followed by slow spontaneous channel closure. In contrast, a heteromultimer formed by KCNA2 and KCNA4 shows rapid inactivation. Contributes to the regulation of action potentials in neurons. KCNA2-containing channels play a presynaptic role and prevent hyperexcitability and aberrant action potential firing. Response to toxins that are selective for KCNA1, respectively for KCNA2, suggests that heteromeric potassium channels composed of both KCNA1 and KCNA2 play a role in pacemaking and regulate the output of deep cerebellar nuclear neurons. Response to toxins that are selective for KCNA2-containing potassium channels suggests that in Purkinje cells, dendritic subthreshold KCNA2-containing potassium channels prevent random spontaneous calcium spikes, suppressing dendritic hyperexcitability without hindering the generation of somatic action potentials, and thereby play an important role in motor coordination. KCNA2-containing channels play a role in GABAergic transmission from basket cells to Purkinje cells in the cerebellum, and thereby play an import role in motor coordination. Plays a role in the induction of long-term potentiation of neuron excitability in the CA3 layer of the hippocampus. May function as down-stream effector for G protein-coupled receptors and inhibit GABAergic inputs to basolateral amygdala neurons. May contribute to the regulation of neurotransmitter release, such as gamma-aminobutyric acid (GABA). Contributes to the regulation of the axonal release of the neurotransmitter dopamine. Reduced KCNA2 expression plays a role in the perception of neuropathic pain after peripheral nerve injury, but not acute pain. Plays a role in the regulation of the time spent in non-rapid eye movement (NREM) sleep.","Patch clamp recordings revealed an increased frequency and amplitude of spontaneous GABAergic inhibitory postsynaptic currents and reduced action potential firing frequency in Purkinje cells, suggesting that an increase in GABA release from basket cells is involved in the motor incoordination in Pgu mice. Expression of homomeric and heteromeric channels containing the Kv1. 2() α-subunit in cultured CHO cells revealed subtle changes in biophysical properties but a dramatic decrease in the amount of functional Kv1 channels. Pharmacological treatment with acetazolamide or transgenic complementation with wild-type Kcna2 cDNA partially rescued the motor incoordination in Pgu mice.","In Pgu; chronic motor incoordination; decreases the number of functional channels at the cell surface. Patch clamp recordings revealed an increased frequency and amplitude of spontaneous GABAergic inhibitory postsynaptic currents and reduced action potential firing frequency in Purkinje cells, suggesting that an increase in GABA release from basket cells is involved in the motor incoordination in Pgu mice. Expression of homomeric and heteromeric channels containing the Kv1. 2() α-subunit in cultured CHO cells revealed subtle changes in biophysical properties but a dramatic decrease in the amount of functional Kv1 channels. Pharmacological treatment with acetazolamide or transgenic complementation with wild-type Kcna2 cDNA partially rescued the motor incoordination in Pgu mice."
2315,2315,2315,176719,Q9NXW9-D171A,MAAAAAETPEVLRECGCKGIRTCLICERQRGSDPPWELPPAKTYRFIYCSDTGWAVGTEESDFEGWAFPFPGVMLIEDFVTREEEAELVRLMDRDPWKLSQSGRRKQDYGPKVNFRKQKLKTEGFCGLPSFSREVVRRMGLYPGLEGFRPVEQCNLDYCPERGSAIDPHLADAWLWGERLVSLNLLSPTVLSMCREAPGSLLLCSAPSAAPEALVDSVIAPSRSVLCQEVEVAIPLPARSLLVLTGAARHQWKHAIHRRHIEARRVCVTFRELSAEFGPGGRQQELGQELLRIALSFQGRPV,"Loss of function mutant that acts as a dominant-negative mutant when overexpressed, leading to multinucleation and cleavage furrow disorganization; when associated with A-169 and A-254.",,MAAAAAETPEVLRECGCKGIRTCLICERQRGSDPPWELPPAKTYRFIYCSDTGWAVGTEESDFEGWAFPFPGVMLIEDFVTREEEAELVRLMDRDPWKLSQSGRRKQDYGPKVNFRKQKLKTEGFCGLPSFSREVVRRMGLYPGLEGFRPVEQCNLDYCPERGSAIDPHLDDAWLWGERLVSLNLLSPTVLSMCREAPGSLLLCSAPSAAPEALVDSVIAPSRSVLCQEVEVAIPLPARSLLVLTGAARHQWKHAIHRRHIEARRVCVTFRELSAEFGPGGRQQELGQELLRIALSFQGRPV,Alpha-ketoglutarate-dependent dioxygenase alkB homolog 4,"Dioxygenase that mediates demethylation of actin monomethylated at 'Lys-84' (K84me1), thereby acting as a regulator of actomyosin-processes. Demethylation of actin K84me1 is required for maintaining actomyosin dynamics supporting normal cleavage furrow ingression during cytokinesis and cell migration. In addition to proteins, also demethylates DNA: specifically demethylates DNA methylated on the 6th position of adenine (N(6)-methyladenosine) DNA, thereby regulating Polycomb silencing.",The mutation in actin affects actin-myosin interaction and actomyosin-dependent processes such as cytokinesis and cell migration.,"Loss of function mutant that acts as a dominant-negative mutant when overexpressed, leading to multinucleation and cleavage furrow disorganization; when associated with A-169 and A-254. The mutation in actin affects actin-myosin interaction and actomyosin-dependent processes such as cytokinesis and cell migration."
2335,2335,2335,177801,O88703-R315Q,MDARGGGGRPGDSPGTTPAPGPPPPPPPPAPPQPQPPPAPPPNPTTPSHPESADEPGPRARLCSRDSACTPGAAKGGANGECGRGEPQCSPEGPARGPKVSFSCRGAASGPSAAEEAGSEEAGPAGEPRGSQASFLQRQFGALLQPGVNKFSLRMFGSQKAVEREQERVKSAGAWIIHPYSDFRFYWDFTMLLFMVGNLIIIPVGITFFKDETTAPWIVFNVVSDTFFLMDLVLNFRTGIVIEDNTEIILDPEKIKKKYLRTWFVVDFVSSIPVDYIFLIVEKGIDSEVYKTARALRIVRFTKILSLLRLLRLSQLIRYIHQWEEIFHMTYDLASAVMRICNLISMMLLLCHWDGCLQFLVPMLQDFPSDCWVSINNMVNHSWSELYSFALFKAMSHMLCIGYGRQAPESMTDIWLTMLSMIVGATCYAMFIGHATALIQSLDSSRRQYQEKYKQVEQYMSFHKLPADFRQKIHDYYEHRYQGKMFDEDSILGELNGPLREEIVNFNCRKLVASMPLFANADPNFVTAMLTKLKFEVFQPGDYIIREGTIGKKMYFIQHGVVSVLTKGNKEMKLSDGSYFGEICLLTRGRRTASVRADTYCRLYSLSVDNFNEVLEEYPMMRRAFETVAIDRLDRIGKKNSILLHKVQHDLSSGVFNNQENAIIQEIVKYDREMVQQAELGQRVGLFPPPPPPQVTSAIATLQQAVAMSFCPQVARPLVGPLALGSPRLVRRAPPGPLPPAASPGPPAASPPAAPSSPRAPRTSPYGVPGSPATRVGPALPARRLSRASRPLSASQPSLPHGVPAPSPAASARPASSSTPRLGPAPTARTAAPSPDRRDSASPGAASGLDPLDSARSRLSSNL,Reduces surface expression and abolishes channel activity.,,MDARGGGGRPGDSPGTTPAPGPPPPPPPPAPPQPQPPPAPPPNPTTPSHPESADEPGPRARLCSRDSACTPGAAKGGANGECGRGEPQCSPEGPARGPKVSFSCRGAASGPSAAEEAGSEEAGPAGEPRGSQASFLQRQFGALLQPGVNKFSLRMFGSQKAVEREQERVKSAGAWIIHPYSDFRFYWDFTMLLFMVGNLIIIPVGITFFKDETTAPWIVFNVVSDTFFLMDLVLNFRTGIVIEDNTEIILDPEKIKKKYLRTWFVVDFVSSIPVDYIFLIVEKGIDSEVYKTARALRIVRFTKILSLLRLLRLSRLIRYIHQWEEIFHMTYDLASAVMRICNLISMMLLLCHWDGCLQFLVPMLQDFPSDCWVSINNMVNHSWSELYSFALFKAMSHMLCIGYGRQAPESMTDIWLTMLSMIVGATCYAMFIGHATALIQSLDSSRRQYQEKYKQVEQYMSFHKLPADFRQKIHDYYEHRYQGKMFDEDSILGELNGPLREEIVNFNCRKLVASMPLFANADPNFVTAMLTKLKFEVFQPGDYIIREGTIGKKMYFIQHGVVSVLTKGNKEMKLSDGSYFGEICLLTRGRRTASVRADTYCRLYSLSVDNFNEVLEEYPMMRRAFETVAIDRLDRIGKKNSILLHKVQHDLSSGVFNNQENAIIQEIVKYDREMVQQAELGQRVGLFPPPPPPQVTSAIATLQQAVAMSFCPQVARPLVGPLALGSPRLVRRAPPGPLPPAASPGPPAASPPAAPSSPRAPRTSPYGVPGSPATRVGPALPARRLSRASRPLSASQPSLPHGVPAPSPAASARPASSSTPRLGPAPTARTAAPSPDRRDSASPGAASGLDPLDSARSRLSSNL,Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2,Hyperpolarization-activated ion channel exhibiting weak selectivity for potassium over sodium ions. Contributes to the native pacemaker currents in heart (If) and in neurons (Ih). Can also transport ammonium in the distal nephron. Produces a large instantaneous current.,mutation is crucial for normal protein folding/trafficking and may charge-pair with D residues located in the S2 and S3 domains.,Reduces surface expression and abolishes channel activity. mutation is crucial for normal protein folding/trafficking and may charge-pair with D residues located in the S2 and S3 domains.
2336,2336,2336,177915,Q980R9-L33A,MELAEKDKGRDFTLRNARMDDIDQIIKINRLTAPENYPYYFFVEHLKEYGLAFFVAIVDNSVVGYIMPRIEWGFSNIKQLPSLVRKGHVVSIAVLEEYRRKGIATTLLEASMKSMKNDYNAEEIYLEVRVSNYPAIALYEKLNFKKVKVLKGYYADGEDAYLMARPL,"20- and 2-fold decrease of the catalytic efficiency and affinity for Ser-N-terminal peptide. 11-fold decrease of the catalytic efficiency for Met-N-terminal peptide, but almost same affinity compared to the wild-type.",,MELAEKDKGRDFTLRNARMDDIDQIIKINRLTLPENYPYYFFVEHLKEYGLAFFVAIVDNSVVGYIMPRIEWGFSNIKQLPSLVRKGHVVSIAVLEEYRRKGIATTLLEASMKSMKNDYNAEEIYLEVRVSNYPAIALYEKLNFKKVKVLKGYYADGEDAYLMARPL,N-alpha-acetyltransferase,"Displays alpha (N-terminal) acetyltransferase activity. Catalyzes the covalent attachment of an acetyl moiety from acetyl-CoA to the free alpha-amino group at the N-terminus of a protein. NAT is able to acetylate the alpha-amino group of methionine, alanine and serine N-terminal residue substrates, however it has a preference for Ser-N-terminal substrates.",,"20- and 2-fold decrease of the catalytic efficiency and affinity for Ser-N-terminal peptide. 11-fold decrease of the catalytic efficiency for Met-N-terminal peptide, but almost same affinity compared to the wild-type."
2337,2337,2337,177930,Q8S2T0-Y717A,MSEDKESDVVGEEEESHVIKEDKELNDASNETLTENGDQLLQMIAELRLENDFLRSQFEGLKDEVAQGRSLQKAEQVEADSAQLKQLQEQVASLSREIDVEKQTRVAAEQALEHLREAYSEADAKSQEYSSKFSQVEQKLDQEIKERDEKYADLDAKFTRLHKRAKQRIQEIQKEKDDLDARFREVNETAERASSQHSSMQQELERTRQQANEALKAMDAERQQLRSANNKLRDTIEELRGSLQPKENKIETLQQSLLDKDQILEDLKKQLQAVEERKQIAVTELSAKHQKNLEGLEAQVVDALSERDKAAETISSLQVLLAEKESKIAEMEAAATGEAARLRAAAETLKGELAHLKSENEKEKETWEASCDALKSKLEIAESNYLQAEIEVAKMRSQLGSEMSMQTQILSTKDAELKGAREEINRLQSEFSSYKIRAHALLQKKDMELAAAKDSEQIKSLEEALKEAEKEVYLVSAERDRAQQDLQSALASLEKELEERAGALKDASEQIKSLEVKLDSTVARNQAEKQAWEEDLRVLEETWRRRCEALTAQNEASPAEGIEKELENAKLRNKRMKEEHESVRELADRLIEEKDREISRLVDEMTNLRKSMESKPVWNKSPSQVHHYGNNNTESQQQDVSNLSTSAAEHQILILARQQAQREEELAQTQRHILALQEEIEELERENRLHSQQEAVLKTELREMERKQKREGVDMTALKNVILKLLETGEVEALLPVVGMLLQFSPEEIQKCQQAYHSSTTAATTTEATPSPASEGSGLSVFSRFSFS,Reduced interaction with ARF3/ARL1 and loss of Golgi targeting.,,MSEDKESDVVGEEEESHVIKEDKELNDASNETLTENGDQLLQMIAELRLENDFLRSQFEGLKDEVAQGRSLQKAEQVEADSAQLKQLQEQVASLSREIDVEKQTRVAAEQALEHLREAYSEADAKSQEYSSKFSQVEQKLDQEIKERDEKYADLDAKFTRLHKRAKQRIQEIQKEKDDLDARFREVNETAERASSQHSSMQQELERTRQQANEALKAMDAERQQLRSANNKLRDTIEELRGSLQPKENKIETLQQSLLDKDQILEDLKKQLQAVEERKQIAVTELSAKHQKNLEGLEAQVVDALSERDKAAETISSLQVLLAEKESKIAEMEAAATGEAARLRAAAETLKGELAHLKSENEKEKETWEASCDALKSKLEIAESNYLQAEIEVAKMRSQLGSEMSMQTQILSTKDAELKGAREEINRLQSEFSSYKIRAHALLQKKDMELAAAKDSEQIKSLEEALKEAEKEVYLVSAERDRAQQDLQSALASLEKELEERAGALKDASEQIKSLEVKLDSTVARNQAEKQAWEEDLRVLEETWRRRCEALTAQNEASPAEGIEKELENAKLRNKRMKEEHESVRELADRLIEEKDREISRLVDEMTNLRKSMESKPVWNKSPSQVHHYGNNNTESQQQDVSNLSTSAAEHQILILARQQAQREEELAQTQRHILALQEEIEELERENRLHSQQEAVLKTELREMERKQKREGVDMTYLKNVILKLLETGEVEALLPVVGMLLQFSPEEIQKCQQAYHSSTTAATTTEATPSPASEGSGLSVFSRFSFS,Protein GRIP,Golgi matrix protein playing a role in tethering of vesicles to Golgi membranes and in maintaining the overall structure of the Golgi apparatus.,Mutation of a conserved tyrosine (Y717) to alanine in the GRIP domain disrupted Golgi localization.,Reduced interaction with ARF3/ARL1 and loss of Golgi targeting. Mutation of a conserved tyrosine (Y717) to alanine in the GRIP domain disrupted Golgi localization.
2368,2368,2368,179950,Q8GZQ3-P184L,MLTSPSNALHSSTPQFWPLRRSKLCRSRNFPRFHSGERSSGGGGKLCSLSLLSGSGAGKFSVRALVRPDDTDDADSVGDGSLAFPNHVSVKIPFGNREILVETGLMGRQASSAVTVTDGETIVYTSVCLADVPSEPSDFLPLYVHYQERFSAVGRTSGGFFKREGRTKDHEVLICRLIDRPLRLTMPKGFYNETQILSWVLSYDGLHAPDALAVTSAGIAVALSEVPNAKAIAGVRVGLIGGEFIVNPTVKEMEESQLDLFLAGTDTAILTIEGYSNFLPEEMLLQAVKVGQDAVQATCIAIEVLAKKYGKPKMLDAIRLPPPELYKHVKELAGEELTKALQIKSKISRRKAISSLEEKVLTILTEKGYVIDEVAFGTIEAQPDLLEDEDEDEEVVPEGEVDQGDVHIRPIPRKPIPLLFSEVDVKLVFKEVSSKLLRRRIVEGGKRSDGRTLDEIRPINSRCGLLPRAHGSTLFTRGETQALAVVTLGDKQMAQRIDNLEGSDEYKRFYLQYTFPPSSVGEVGRIGAPSRREIGHGTLAERALETILPSDDDFPYTIRVESTVIESNGSSSMASVCGGCLALQDAGVPVKCSVAGIAMGMVWDTEEFGGDGSPLILSDITGAEDASGDMDFKVAGNEDGVTAFQMDIKVGGITLEIMEKALIQAKAGRRHILAEMAKCSPPPTLSLSKYAPLILIMKVHPSKVYSLIGSGGKKVKSIIEESGVEAIDMQDDGTVKIMAIDVASLERAKAIISGLTMVPSVGDIYRNCEIKSMAPYGAFVEIAPGREGLCHISELSAEWLAKPEDAYKVGDRIDVKLIEVNEKGQLRLSVRALLPESETDKDSQKQQPAGDSTKDKSSQRKYVNTSSKDRAAAGASKVSSGDELVLKKKDVRRATGGSSDKTMNSNSSTNEESLVNGEATIS,Reduces RNA-binding affinity; when associated with S-176.,,MLTSPSNALHSSTPQFWPLRRSKLCRSRNFPRFHSGERSSGGGGKLCSLSLLSGSGAGKFSVRALVRPDDTDDADSVGDGSLAFPNHVSVKIPFGNREILVETGLMGRQASSAVTVTDGETIVYTSVCLADVPSEPSDFLPLYVHYQERFSAVGRTSGGFFKREGRTKDHEVLICRLIDRPLRPTMPKGFYNETQILSWVLSYDGLHAPDALAVTSAGIAVALSEVPNAKAIAGVRVGLIGGEFIVNPTVKEMEESQLDLFLAGTDTAILTIEGYSNFLPEEMLLQAVKVGQDAVQATCIAIEVLAKKYGKPKMLDAIRLPPPELYKHVKELAGEELTKALQIKSKISRRKAISSLEEKVLTILTEKGYVIDEVAFGTIEAQPDLLEDEDEDEEVVPEGEVDQGDVHIRPIPRKPIPLLFSEVDVKLVFKEVSSKLLRRRIVEGGKRSDGRTLDEIRPINSRCGLLPRAHGSTLFTRGETQALAVVTLGDKQMAQRIDNLEGSDEYKRFYLQYTFPPSSVGEVGRIGAPSRREIGHGTLAERALETILPSDDDFPYTIRVESTVIESNGSSSMASVCGGCLALQDAGVPVKCSVAGIAMGMVWDTEEFGGDGSPLILSDITGAEDASGDMDFKVAGNEDGVTAFQMDIKVGGITLEIMEKALIQAKAGRRHILAEMAKCSPPPTLSLSKYAPLILIMKVHPSKVYSLIGSGGKKVKSIIEESGVEAIDMQDDGTVKIMAIDVASLERAKAIISGLTMVPSVGDIYRNCEIKSMAPYGAFVEIAPGREGLCHISELSAEWLAKPEDAYKVGDRIDVKLIEVNEKGQLRLSVRALLPESETDKDSQKQQPAGDSTKDKSSQRKYVNTSSKDRAAAGASKVSSGDELVLKKKDVRRATGGSSDKTMNSNSSTNEESLVNGEATIS,"Polyribonucleotide nucleotidyltransferase 1, chloroplastic","Involved in the metabolism of all major classes of plastid RNAs. Required for efficient 3'-end processing of mRNAs and 3'-end maturation of rRNA transcripts, but is not sufficient to mediate their degradation. Mediates tRNA degradation. May function as a poly(A) mRNA 3'-5' degrading phosphorylase. May be required for plastid ribosome assembly and non-coding RNA biogenesis and accumulation. Seems not required for efficient translation.",The mutation in cpPNPase affects overall catalytic activity.,Reduces RNA-binding affinity; when associated with S-176. The mutation in cpPNPase affects overall catalytic activity.
2373,2373,2373,180843,O75925-D148A,MADSAELKQMVMSLRVSELQVLLGYAGRNKHGRKHELLTKALHLLKAGCSPAVQMKIKELYRRRFPQKIMTPADLSIPNVHSSPMPATLSPSTIPQLTYDGHPASSPLLPVSLLGPKHELELPHLTSALHPVHPDIKLQKLPFYDLLAELIKPTSLASDNSQRFRETCFAFALTPQQVQQISSSMDISGTKCDFTVQVQLRFCLSETSCPQEDHFPPNLCVKVNTKPCSLPGYLPPTKNGVEPKRPSRPINITSLVRLSTTVPNTIVVSWTAEIGRNYSMAVYLVKQLSSTVLLQRLRAKGIRNPDHSRALIKEKLTADPDSEIATTSLRVSLLCPLGKMRLTIPCRALTCSHLQCFDATLYIQMNEKKPTWVCPVCDKKAPYEHLIIDGLFMEILKYCTDCDEIQFKEDGTWAPMRSKKEVQEVSASYNGVDGCLSSTLEHQVASHHQSSNKNKKVEVIDLTIDSSSDEEEEEPSAKRTCPSLSPTSPLNNKGILSLPHQASPVSRTPSLPAVDTSYINTSLIQDYRHPFHMTPMPYDLQGLDFFPFLSGDNQHYNTSLLAAAAAAVSDDQDLLHSSRFFPYTSSQMFLDQLSAGGSTSLPTTNGSSSGSNSSLVSSNSLRESHSHTVTNRSSTDTASIFGIIPDIISLD,No effect on cleavages by caspase-6 and -8.,,MADSAELKQMVMSLRVSELQVLLGYAGRNKHGRKHELLTKALHLLKAGCSPAVQMKIKELYRRRFPQKIMTPADLSIPNVHSSPMPATLSPSTIPQLTYDGHPASSPLLPVSLLGPKHELELPHLTSALHPVHPDIKLQKLPFYDLLDELIKPTSLASDNSQRFRETCFAFALTPQQVQQISSSMDISGTKCDFTVQVQLRFCLSETSCPQEDHFPPNLCVKVNTKPCSLPGYLPPTKNGVEPKRPSRPINITSLVRLSTTVPNTIVVSWTAEIGRNYSMAVYLVKQLSSTVLLQRLRAKGIRNPDHSRALIKEKLTADPDSEIATTSLRVSLLCPLGKMRLTIPCRALTCSHLQCFDATLYIQMNEKKPTWVCPVCDKKAPYEHLIIDGLFMEILKYCTDCDEIQFKEDGTWAPMRSKKEVQEVSASYNGVDGCLSSTLEHQVASHHQSSNKNKKVEVIDLTIDSSSDEEEEEPSAKRTCPSLSPTSPLNNKGILSLPHQASPVSRTPSLPAVDTSYINTSLIQDYRHPFHMTPMPYDLQGLDFFPFLSGDNQHYNTSLLAAAAAAVSDDQDLLHSSRFFPYTSSQMFLDQLSAGGSTSLPTTNGSSSGSNSSLVSSNSLRESHSHTVTNRSSTDTASIFGIIPDIISLD,E3 SUMO-protein ligase PIAS1,"Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tethering factor. Plays a crucial role as a transcriptional coregulation in various cellular pathways, including the STAT pathway, the p53 pathway and the steroid hormone signaling pathway. In vitro, binds A/T-rich DNA. The effects of this transcriptional coregulation, transactivation or silencing, may vary depending upon the biological context. Sumoylates PML (at'Lys-65' and 'Lys-160') and PML-RAR and promotes their ubiquitin-mediated degradation. PIAS1-mediated sumoylation of PML promotes its interaction with CSNK2A1/CK2 which in turn promotes PML phosphorylation and degradation. Enhances the sumoylation of MTA1 and may participate in its paralog-selective sumoylation. Plays a dynamic role in adipogenesis by promoting the SUMOylation and degradation of CEBPB.(Microbial infection) Restricts Epstein-Barr virus (EBV) lytic replication by acting as an inhibitor for transcription factors involved in lytic gene expression. The virus can use apoptotic caspases to antagonize PIAS1-mediated restriction and express its lytic genes.",,No effect on cleavages by caspase-6 and -8.
2403,2403,2403,182807,A0QTK2-D56E,MDTMRQRILVVDDDPSLAEMLTIVLRGEGFDTAVIGDGSQALTAVRELRPDLVLLELMLPGMNGIDVCRVLRADSGVPIVMLTAKTDTVDVVLGLESGADDYVMKPFKPKELVARVRARLRRNEDEPAEMLSIGDVEIDVPAHKVTRQGEQISLTPLEFDLLVALARKPRQVFTRDVLLEQVWGYRHPADTRLVNVHVQRLRAKVEKDPENPQVVLTVRGVGYKAGPP,"Complements an lpqB disruption mutant, when overexpressed restores biofilm formation to the lpqB disruption. Acts like a dominant negative to wild-type.",,MDTMRQRILVVDDDPSLAEMLTIVLRGEGFDTAVIGDGSQALTAVRELRPDLVLLDLMLPGMNGIDVCRVLRADSGVPIVMLTAKTDTVDVVLGLESGADDYVMKPFKPKELVARVRARLRRNEDEPAEMLSIGDVEIDVPAHKVTRQGEQISLTPLEFDLLVALARKPRQVFTRDVLLEQVWGYRHPADTRLVNVHVQRLRAKVEKDPENPQVVLTVRGVGYKAGPP,DNA-binding response regulator MtrA,"Member of the two-component regulatory system MtrA/MtrB, responding to environmental signals (Probable). Controls expression of a number of genes including dnaA, ripA, fbpB and probably itself. Probably plays a role in cell division.","The lpqB mutant exhibited increased cell-cell aggregation and severe defects in surface motility and biofilm growth. LpqB interacts with the extracellular domain of MtrB, and influences MtrA phosphorylation and promoter activity of dnaA, an MtrA-regulated gene that affects cell division.","Complements an lpqB disruption mutant, when overexpressed restores biofilm formation to the lpqB disruption. Acts like a dominant negative to wild-type. The lpqB mutant exhibited increased cell-cell aggregation and severe defects in surface motility and biofilm growth. LpqB interacts with the extracellular domain of MtrB, and influences MtrA phosphorylation and promoter activity of dnaA, an MtrA-regulated gene that affects cell division."
2422,2422,2422,184424,P43026-R380Q,MRLPKLLTFLLWYLAWLDLEFICTVLGAPDLGQRPQGTRPGLAKAEAKERPPLARNVFRPGGHSYGGGATNANARAKGGTGQTGGLTQPKKDEPKKLPPRPGGPEPKPGHPPQTRQATARTVTPKGQLPGGKAPPKAGSVPSSFLLKKAREPGPPREPKEPFRPPPITPHEYMLSLYRTLSDADRKGGNSSVKLEAGLANTITSFIDKGQDDRGPVVRKQRYVFDISALEKDGLLGAELRILRKKPSDTAKPAAPGGGRAAQLKLSSCPSGRQPAALLDVRSVPGLDGSGWEVFDIWKLFRNFKNSAQLCLELEAWERGRAVDLRGLGFDRAARQVHEKALFLVFGRTKKRDLFFNEIKARSGQDDKTVYEYLFSQRRKQRAPLATRQGKRPSKNLKARCSRKALHVNFKDMGWDDWIIAPLEYEAFHCEGLCEFPLRSHLEPTNHAVIQTLMNSMDPESTPPTCCVPTRLSPISILFIDSANNVVYKQYEDMVVESCGCR,In BDA2; reduces activity; impairs processing.,,MRLPKLLTFLLWYLAWLDLEFICTVLGAPDLGQRPQGTRPGLAKAEAKERPPLARNVFRPGGHSYGGGATNANARAKGGTGQTGGLTQPKKDEPKKLPPRPGGPEPKPGHPPQTRQATARTVTPKGQLPGGKAPPKAGSVPSSFLLKKAREPGPPREPKEPFRPPPITPHEYMLSLYRTLSDADRKGGNSSVKLEAGLANTITSFIDKGQDDRGPVVRKQRYVFDISALEKDGLLGAELRILRKKPSDTAKPAAPGGGRAAQLKLSSCPSGRQPAALLDVRSVPGLDGSGWEVFDIWKLFRNFKNSAQLCLELEAWERGRAVDLRGLGFDRAARQVHEKALFLVFGRTKKRDLFFNEIKARSGQDDKTVYEYLFSQRRKRRAPLATRQGKRPSKNLKARCSRKALHVNFKDMGWDDWIIAPLEYEAFHCEGLCEFPLRSHLEPTNHAVIQTLMNSMDPESTPPTCCVPTRLSPISILFIDSANNVVYKQYEDMVVESCGCR,Growth/differentiation factor 5,"Growth factor involved in bone and cartilage formation. During cartilage development regulates differentiation of chondrogenic tissue through two pathways. Firstly, positively regulates differentiation of chondrogenic tissue through its binding of high affinity with BMPR1B and of less affinity with BMPR1A, leading to induction of SMAD1-SMAD5-SMAD8 complex phosphorylation and then SMAD protein signaling transduction. Secondly, negatively regulates chondrogenic differentiation through its interaction with NOG. Required to prevent excessive muscle loss upon denervation. This function requires SMAD4 and is mediated by phosphorylated SMAD1/5/8. Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes.","The heterozygous arginine to glutamine () substitution in the growth/differentiation factor 5 (GDF5) leads to a strong reduction of biological activity. The mutation interferes with processing at the protein's cleavage site, resulting in diminished biological activity.","In BDA2; reduces activity; impairs processing. The heterozygous arginine to glutamine () substitution in the growth/differentiation factor 5 (GDF5) leads to a strong reduction of biological activity. The mutation interferes with processing at the protein's cleavage site, resulting in diminished biological activity."
2425,2425,2425,184561,P35240-F62S,MAGAIASRMSFSSLKRKQPKTFTVRIVTMDAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFSGLQYTIKDTVAWLKMDKKVLDHDVSKEEPVTFHFLAKFYPENAEEELVQEITQHLFFLQVKKQILDEKIYCPPEASVLLASYAVQAKYGDYDPSVHKRGFLAQEELLPKRVINLYQMTPEMWEERITAWYAEHRGRARDEAEMEYLKIAQDLEMYGVNYFAIRNKKGTELLLGVDALGLHIYDPENRLTPKISFPWNEIRNISYSDKEFTIKPLDKKIDVFKFNSSKLRVNKLILQLCIGNHDLFMRRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIATKPTYPPMNPIPAPLPPDIPSFNLIGDSLSFDFKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKERETALDILHNENSDRGGSSKHNTIKKLTLQSAKSRVAFFEEL,In NF2; loss of ability to interact with the CUL4A-RBX1-DDB1-VprBP/DCAF1 E3 ubiquitin-protein ligase complex.,,MAGAIASRMSFSSLKRKQPKTFTVRIVTMDAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYTIKDTVAWLKMDKKVLDHDVSKEEPVTFHFLAKFYPENAEEELVQEITQHLFFLQVKKQILDEKIYCPPEASVLLASYAVQAKYGDYDPSVHKRGFLAQEELLPKRVINLYQMTPEMWEERITAWYAEHRGRARDEAEMEYLKIAQDLEMYGVNYFAIRNKKGTELLLGVDALGLHIYDPENRLTPKISFPWNEIRNISYSDKEFTIKPLDKKIDVFKFNSSKLRVNKLILQLCIGNHDLFMRRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIATKPTYPPMNPIPAPLPPDIPSFNLIGDSLSFDFKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKERETALDILHNENSDRGGSSKHNTIKKLTLQSAKSRVAFFEEL,Merlin,"Probable regulator of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway, a signaling pathway that plays a pivotal role in tumor suppression by restricting proliferation and promoting apoptosis. Along with WWC1 can synergistically induce the phosphorylation of LATS1 and LATS2 and can probably function in the regulation of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway. May act as a membrane stabilizing protein. May inhibit PI3 kinase by binding to AGAP2 and impairing its stimulating activity. Suppresses cell proliferation and tumorigenesis by inhibiting the CUL4A-RBX1-DDB1-VprBP/DCAF1 E3 ubiquitin-protein ligase complex.",The mutation in the NF2 gene causes benign nervous system tumors. The mutation in the NF2 gene is associated with severe disease. Subjects with this mutation are significantly more likely to have symptoms before 20 years of age and to develop at least two symptomatic CNS tumours in addition to vestibular schwannoma before 30 years.,In NF2; loss of ability to interact with the CUL4A-RBX1-DDB1-VprBP/DCAF1 E3 ubiquitin-protein ligase complex. The mutation in the NF2 gene causes benign nervous system tumors. The mutation in the NF2 gene is associated with severe disease. Subjects with this mutation are significantly more likely to have symptoms before 20 years of age and to develop at least two symptomatic CNS tumours in addition to vestibular schwannoma before 30 years.
2428,2428,2428,185009,P22234-S332A,MATAEVLNIGKKLYEGKTKEVYELLDSPGKVLLQSKDQITAGNAARKNHLEGKAAISNKITSCIFQLLQEAGIKTAFTRKCGETAFIAPQCEMIPIEWVCRRIATGSFLKRNPGVKEGYKFYPPKVELFFKDDANNDPQWSEEQLIAAKFCFAGLLIGQTEVDIMSHATQAIFEILEKSWLPQNCTLVDMKIEFGVDVTTKEIVLADVIDNDSWRLWPSGDRSQQKDKQSYRDLKEVTPEGLQMVKKNFEWVAERVELLLKSESQCRVVVLMGSTSDLGHCEKIKKACGNFGIPCELRVTSAHKGPDETLRIKAEYEGDGIPTVFVAVAGRANGLGPVMSGNTAYPVISCPPLTPDWGVQDVWSSLRLPSGLGCSTVLSPEGSAQFAAQIFGLSNHLVWSKLRASILNTWISLKQADKKIRECNL,Loss of phosphoribosylaminoimidazole carboxylase activity.,,MATAEVLNIGKKLYEGKTKEVYELLDSPGKVLLQSKDQITAGNAARKNHLEGKAAISNKITSCIFQLLQEAGIKTAFTRKCGETAFIAPQCEMIPIEWVCRRIATGSFLKRNPGVKEGYKFYPPKVELFFKDDANNDPQWSEEQLIAAKFCFAGLLIGQTEVDIMSHATQAIFEILEKSWLPQNCTLVDMKIEFGVDVTTKEIVLADVIDNDSWRLWPSGDRSQQKDKQSYRDLKEVTPEGLQMVKKNFEWVAERVELLLKSESQCRVVVLMGSTSDLGHCEKIKKACGNFGIPCELRVTSAHKGPDETLRIKAEYEGDGIPTVFVAVAGRSNGLGPVMSGNTAYPVISCPPLTPDWGVQDVWSSLRLPSGLGCSTVLSPEGSAQFAAQIFGLSNHLVWSKLRASILNTWISLKQADKKIRECNL,Bifunctional phosphoribosylaminoimidazole carboxylase/phosphoribosylaminoimidazole succinocarboxamide synthetase,Bifunctional phosphoribosylaminoimidazole carboxylase and phosphoribosylaminoimidazole succinocarboxamide synthetase catalyzing two reactions of the de novo purine biosynthetic pathway.,"The crystal structure of human PAICS revealed that the active sites of SAICARs and AIRc were identified, including a putative substrate CO(2)-binding site.","Loss of phosphoribosylaminoimidazole carboxylase activity. The crystal structure of human PAICS revealed that the active sites of SAICARs and AIRc were identified, including a putative substrate CO(2)-binding site."
2437,2437,2437,185570,P43246-L175P,MAVQPKETLQLESAAEVGFVRFFQGMPEKPTTTVRLFDRGDFYTAHGEDALLAAREVFKTQGVIKYMGPAGAKNLQSVVLSKMNFESFVKDLLLVRQYRVEVYKNRAGNKASKENDWYLAYKASPGNLSQFEDILFGNNDMSASIGVVGVKMSAVDGQRQVGVGYVDSIQRKLGPCEFPDNDQFSNLEALLIQIGPKECVLPGGETAGDMGKLRQIIQRGGILITERKKADFSTKDIYQDLNRLLKGKKGEQMNSAVLPEMENQVAVSSLSAVIKFLELLSDDSNFGQFELTTFDFSQYMKLDIAAVRALNLFQGSVEDTTGSQSLAALLNKCKTPQGQRLVNQWIKQPLMDKNRIEERLNLVEAFVEDAELRQTLQEDLLRRFPDLNRLAKKFQRQAANLQDCYRLYQGINQLPNVIQALEKHEGKHQKLLLAVFVTPLTDLRSDFSKFQEMIETTLDMDQVENHEFLVKPSFDPNLSELREIMNDLEKKMQSTLISAARDLGLDPGKQIKLDSSAQFGYYFRVTCKEEKVLRNNKNFSTVDIQKNGVKFTNSKLTSLNEEYTKNKTEYEEAQDAIVKEIVNISSGYVEPMQTLNDVLAQLDAVVSFAHVSNGAPVPYVRPAILEKGQGRIILKASRHACVEVQDEIAFIPNDVYFEKDKQMFHIITGPNMGGKSTYIRQTGVIVLMAQIGCFVPCESAEVSIVDCILARVGAGDSQLKGVSTFMAEMLETASILRSATKDSLIIIDELGRGTSTYDGFGLAWAISEYIATKIGAFCMFATHFHELTALANQIPTVNNLHVTALTTEETLTMLYQVKKGVCDQSFGIHVAELANFPKHVIECAKQKALELEEFQYIGESQGYDIMEPAAKKCYLEREQGEKIIQEFLSKVKQMPFTEMSEENITIKLKQLKAEVIAKNNSFVNEIISRIKVTT,In LYNCH1.,,MAVQPKETLQLESAAEVGFVRFFQGMPEKPTTTVRLFDRGDFYTAHGEDALLAAREVFKTQGVIKYMGPAGAKNLQSVVLSKMNFESFVKDLLLVRQYRVEVYKNRAGNKASKENDWYLAYKASPGNLSQFEDILFGNNDMSASIGVVGVKMSAVDGQRQVGVGYVDSIQRKLGLCEFPDNDQFSNLEALLIQIGPKECVLPGGETAGDMGKLRQIIQRGGILITERKKADFSTKDIYQDLNRLLKGKKGEQMNSAVLPEMENQVAVSSLSAVIKFLELLSDDSNFGQFELTTFDFSQYMKLDIAAVRALNLFQGSVEDTTGSQSLAALLNKCKTPQGQRLVNQWIKQPLMDKNRIEERLNLVEAFVEDAELRQTLQEDLLRRFPDLNRLAKKFQRQAANLQDCYRLYQGINQLPNVIQALEKHEGKHQKLLLAVFVTPLTDLRSDFSKFQEMIETTLDMDQVENHEFLVKPSFDPNLSELREIMNDLEKKMQSTLISAARDLGLDPGKQIKLDSSAQFGYYFRVTCKEEKVLRNNKNFSTVDIQKNGVKFTNSKLTSLNEEYTKNKTEYEEAQDAIVKEIVNISSGYVEPMQTLNDVLAQLDAVVSFAHVSNGAPVPYVRPAILEKGQGRIILKASRHACVEVQDEIAFIPNDVYFEKDKQMFHIITGPNMGGKSTYIRQTGVIVLMAQIGCFVPCESAEVSIVDCILARVGAGDSQLKGVSTFMAEMLETASILRSATKDSLIIIDELGRGTSTYDGFGLAWAISEYIATKIGAFCMFATHFHELTALANQIPTVNNLHVTALTTEETLTMLYQVKKGVCDQSFGIHVAELANFPKHVIECAKQKALELEEFQYIGESQGYDIMEPAAKKCYLEREQGEKIIQEFLSKVKQMPFTEMSEENITIKLKQLKAEVIAKNNSFVNEIISRIKVTT,DNA mismatch repair protein Msh2,"Component of the post-replicative DNA mismatch repair system (MMR). Forms two different heterodimers: MutS alpha (MSH2-MSH6 heterodimer) and MutS beta (MSH2-MSH3 heterodimer) which binds to DNA mismatches thereby initiating DNA repair. When bound, heterodimers bend the DNA helix and shields approximately 20 base pairs. MutS alpha recognizes single base mismatches and dinucleotide insertion-deletion loops (IDL) in the DNA. MutS beta recognizes larger insertion-deletion loops up to 13 nucleotides long. After mismatch binding, MutS alpha or beta forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. Recruits DNA helicase MCM9 to chromatin which unwinds the mismatch containing DNA strand. ATP binding and hydrolysis play a pivotal role in mismatch repair functions. The ATPase activity associated with MutS alpha regulates binding similar to a molecular switch: mismatched DNA provokes ADP-->ATP exchange, resulting in a discernible conformational transition that converts MutS alpha into a sliding clamp capable of hydrolysis-independent diffusion along the DNA backbone. This transition is crucial for mismatch repair. MutS alpha may also play a role in DNA homologous recombination repair. In melanocytes may modulate both UV-B-induced cell cycle regulation and apoptosis.",The missense mutation in the MSH2 gene was identified. This variant was not found in 104 alleles of healthy control individuals. The clinical data and the genotypic and phenotypic evaluation of the tumors indicate that this alteration is a pathogenic HNPCC mutation.,In LYNCH1. The missense mutation in the MSH2 gene was identified. This variant was not found in 104 alleles of healthy control individuals. The clinical data and the genotypic and phenotypic evaluation of the tumors indicate that this alteration is a pathogenic HNPCC mutation.
2444,2444,2444,186046,P04637-K139N,MEEPQSDPSVEPPLSQETFSDLWKLLPENNVLSPLPSQAMDDLMLSPDDIEQWFTEDPGPDEAPRMPEAAPPVAPAPAAPTPAAPAPAPSWPLSSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLANTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNTSSSPQPKKKPLDGEYFTLQIRGRERFEMFRELNEALELKDAQAGKEPGGSRAHSSHLKSKKGQSTSRHKKLMFKTEGPDSD,In sporadic cancers; somatic mutation.,,MEEPQSDPSVEPPLSQETFSDLWKLLPENNVLSPLPSQAMDDLMLSPDDIEQWFTEDPGPDEAPRMPEAAPPVAPAPAAPTPAAPAPAPSWPLSSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNTSSSPQPKKKPLDGEYFTLQIRGRERFEMFRELNEALELKDAQAGKEPGGSRAHSSHLKSKKGQSTSRHKKLMFKTEGPDSD,Cellular tumor antigen p53,"Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type. Involved in cell cycle regulation as a trans-activator that acts to negatively regulate cell division by controlling a set of genes required for this process. One of the activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be mediated either by stimulation of BAX and FAS antigen expression, or by repression of Bcl-2 expression. Its pro-apoptotic activity is activated via its interaction with PPP1R13B/ASPP1 or TP53BP2/ASPP2. However, this activity is inhibited when the interaction with PPP1R13B/ASPP1 or TP53BP2/ASPP2 is displaced by PPP1R13L/iASPP. In cooperation with mitochondrial PPIF is involved in activating oxidative stress-induced necrosis; the function is largely independent of transcription. Induces the transcription of long intergenic non-coding RNA p21 (lincRNA-p21) and lincRNA-Mkln1. LincRNA-p21 participates in TP53-dependent transcriptional repression leading to apoptosis and seems to have an effect on cell-cycle regulation. Implicated in Notch signaling cross-over. Prevents CDK7 kinase activity when associated to CAK complex in response to DNA damage, thus stopping cell cycle progression. Isoform 2 enhances the transactivation activity of isoform 1 from some but not all TP53-inducible promoters. Isoform 4 suppresses transactivation activity and impairs growth suppression mediated by isoform 1. Isoform 7 inhibits isoform 1-mediated apoptosis. Regulates the circadian clock by repressing CLOCK-BMAL1-mediated transcriptional activation of PER2.",,In sporadic cancers; somatic mutation.
2456,2456,2456,186825,P81910-G140A,MLSQFFPHIKEKPLSERVKSRDAFVYLDRVMWSFGWTVPENKRWDLHYKLWSTFVTLLIFILLPISVSVEYIQRFKTFSAGEFLSSIQIGVNMYGSSFKSYLTMMGYKKRQEAKMSLDELDKRCVCDEERTIVHRHVALANFCYIFYHIAYTSFLISNFLSFIMKRIHAWRMYFPYVDPEKQFYISSIAEVILRGWAVFMDLCTDVCPLISMVIARCHITLLKQRLRNLRSEPGRTEDEYLKELADCVRDHRLILDYVDALRSVFSGTIFVQFLLIGIVLGLSMINIMFFSTLSTGVAVVLFMSCVSMQTFPFCYLCNMIMDDCQEMADSLFQSDWTSADRRYKSTLVYFLHNLQQPIILTAGGVFPISMQTNLNMVKLAFTVVTIVKQFNLAEKFQ,In strain: LA9.,,MLSQFFPHIKEKPLSERVKSRDAFVYLDRVMWSFGWTVPENKRWDLHYKLWSTFVTLLIFILLPISVSVEYIQRFKTFSAGEFLSSIQIGVNMYGSSFKSYLTMMGYKKRQEAKMSLDELDKRCVCDEERTIVHRHVALGNFCYIFYHIAYTSFLISNFLSFIMKRIHAWRMYFPYVDPEKQFYISSIAEVILRGWAVFMDLCTDVCPLISMVIARCHITLLKQRLRNLRSEPGRTEDEYLKELADCVRDHRLILDYVDALRSVFSGTIFVQFLLIGIVLGLSMINIMFFSTLSTGVAVVLFMSCVSMQTFPFCYLCNMIMDDCQEMADSLFQSDWTSADRRYKSTLVYFLHNLQQPIILTAGGVFPISMQTNLNMVKLAFTVVTIVKQFNLAEKFQ,Odorant receptor 22b,"Odorant receptor which mediates acceptance or avoidance behavior, depending on its substrates. The odorant receptor repertoire encodes a large collection of odor stimuli that vary widely in identity, intensity, and duration. Involved in the behavioral responses to esters. Complexes with Orco to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability. They are necessary and sufficient to promote functional reconstitution of odor-evoked signaling in sensory neurons that normally respond only to carbon dioxide.",,In strain: LA9.
2457,2457,2457,186873,Q11094-E29G,MVARRKGERVVRKNEVENVQQRACANRRGRQRTKELNDAFTLLRKLIPSMPSDKMSKIHTLRIATDYISFLDEMQKNGCKLYGHSIFDEKRGYNLQSAFNMWRGNNGYTPIAGPSQLPPLQSAHIPPPAPSSIPPHCLMPQPWYQTCPPPKQEFHELCPISTPNPNSNPNQLTPIHWQ,Dominant negative effect on function in transcription regulation and mesodermal cells fate specification. Impaired vulval and non-striated enteric muscles development.,,MVARRKGERVVRKNEVENVQQRACANRRERQRTKELNDAFTLLRKLIPSMPSDKMSKIHTLRIATDYISFLDEMQKNGCKLYGHSIFDEKRGYNLQSAFNMWRGNNGYTPIAGPSQLPPLQSAHIPPPAPSSIPPHCLMPQPWYQTCPPPKQEFHELCPISTPNPNSNPNQLTPIHWQ,Twist-related protein,Acts as a transcriptional regulator. Involved in postembryonic mesodermal cell fate specification. Activates ceh-24 and egl-15 during mesodermal patterning.,Distinct de novo amino acid substitution at a highly conserved glutamic acid residue located in the basic DNA binding domain of TWIST1,Dominant negative effect on function in transcription regulation and mesodermal cells fate specification. Impaired vulval and non-striated enteric muscles development. Distinct de novo amino acid substitution at a highly conserved glutamic acid residue located in the basic DNA binding domain of TWIST1
2483,2483,2483,189628,O60942-K533A,MAHNKIPPRWLNCPRRGQPVAGRFLPLKTMLGPRYDSQVAEENRFHPSMLSNYLKSLKVKMGLLVDLTNTSRFYDRNDIEKEGIKYIKLQCKGHGECPTTENTETFIRLCERFNERNPPELIGVHCTHGFNRTGFLICAFLVEKMDWSIEAAVATFAQARPPGIYKGDYLKELFRRYGDIEEAPPPPLLPDWCFEDDEDEDEDEDGKKESEPGSSASFGKRRKERLKLGAIFLEGVTVKGVTQVTTQPKLGEVQQKCHQFCGWEGSGFPGAQPVSMDKQNIKLLDLKPYKVSWKADGTRYMMLIDGTNEVFMIDRDNSVFHVSNLEFPFRKDLRMHLSNTLLDGEMIIDRVNGQAVPRYLIYDIIKFNSQPVGDCDFNVRLQCIEREIISPRHEKMKTGLIDKTQEPFSVRNKPFFDICTSRKLLEGNFAKEVSHEMDGLIFQPTGKYKPGRCDDILKWKPPSLNSVDFRLKITRMGGEGLLPQNVGLLYVGGYERPFAQIKVTKELKQYDNKIIECKFENNSWVFMRQRTDASFPNAYNTAMAVCNSISNPVTKEMLFEFIDRCTAASQGQKRKHHLDPDTELMPPPPPKRPRPLT,Loss of GTase activity.,,MAHNKIPPRWLNCPRRGQPVAGRFLPLKTMLGPRYDSQVAEENRFHPSMLSNYLKSLKVKMGLLVDLTNTSRFYDRNDIEKEGIKYIKLQCKGHGECPTTENTETFIRLCERFNERNPPELIGVHCTHGFNRTGFLICAFLVEKMDWSIEAAVATFAQARPPGIYKGDYLKELFRRYGDIEEAPPPPLLPDWCFEDDEDEDEDEDGKKESEPGSSASFGKRRKERLKLGAIFLEGVTVKGVTQVTTQPKLGEVQQKCHQFCGWEGSGFPGAQPVSMDKQNIKLLDLKPYKVSWKADGTRYMMLIDGTNEVFMIDRDNSVFHVSNLEFPFRKDLRMHLSNTLLDGEMIIDRVNGQAVPRYLIYDIIKFNSQPVGDCDFNVRLQCIEREIISPRHEKMKTGLIDKTQEPFSVRNKPFFDICTSRKLLEGNFAKEVSHEMDGLIFQPTGKYKPGRCDDILKWKPPSLNSVDFRLKITRMGGEGLLPQNVGLLYVGGYERPFAQIKVTKELKQYDNKIIECKFENNSWVFMRQRTDKSFPNAYNTAMAVCNSISNPVTKEMLFEFIDRCTAASQGQKRKHHLDPDTELMPPPPPKRPRPLT,mRNA-capping enzyme,"Bifunctional mRNA-capping enzyme exhibiting RNA 5'-triphosphate monophosphatase activity in the N-terminal part and mRNA guanylyltransferase activity in the C-terminal part. Catalyzes the first two steps of cap formation: by removing the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end, and by transferring the GMP moiety of GTP to the 5'-diphosphate terminus of RNA via a covalent enzyme-GMP reaction intermediate.",The mutation in the hGTase domain may affect the opening and closing of the active site cleft through a swivel motion.,Loss of GTase activity. The mutation in the hGTase domain may affect the opening and closing of the active site cleft through a swivel motion.
2492,2492,2492,190233,Q9H310-F419A,MAGSPSRAAGRRLQLPLLCLFLQGATAVLFAVFVRYNHKTDAALWHRSNHSNADNEFYFRYPSFQDVHAMVFVGFGFLMVFLQRYGFSSVGFTFLLAAFALQWSTLVQGFLHSFHGGHIHVGVESMINADFCAGAVLISFGAVLGKTGPTQLLLMALLEVVLFGINEFVLLHLLGVRDAGGSMTIHTFGAYFGLVLSRVLYRPQLEKSKHRQGSVYHSDLFAMIGTIFLWIFWPSFNAALTALGAGQHRTALNTYYSLAASTLGTFALSALVGEDGRLDMVHIQNAALAGGVVVGTSSEMMLTPFGALAAGFLAGTVSTLGYKFFTPILESKFKVQDTCGVHNLHGMPGVLGALLGVLVAGLATHEAYGDGLESVFPLIAEGQRSATSQAMHQLFGLFVTLMFASVGGGLGGLLLKLPALDSPPDSQHYEDQVHWQVPGEHEDKAQRPLRVEEADTQA,Loss of interaction with ANK3. Intracellular retention; when associated with A-420 and A-421.,,MAGSPSRAAGRRLQLPLLCLFLQGATAVLFAVFVRYNHKTDAALWHRSNHSNADNEFYFRYPSFQDVHAMVFVGFGFLMVFLQRYGFSSVGFTFLLAAFALQWSTLVQGFLHSFHGGHIHVGVESMINADFCAGAVLISFGAVLGKTGPTQLLLMALLEVVLFGINEFVLLHLLGVRDAGGSMTIHTFGAYFGLVLSRVLYRPQLEKSKHRQGSVYHSDLFAMIGTIFLWIFWPSFNAALTALGAGQHRTALNTYYSLAASTLGTFALSALVGEDGRLDMVHIQNAALAGGVVVGTSSEMMLTPFGALAAGFLAGTVSTLGYKFFTPILESKFKVQDTCGVHNLHGMPGVLGALLGVLVAGLATHEAYGDGLESVFPLIAEGQRSATSQAMHQLFGLFVTLMFASVGGGLGGLLLKLPFLDSPPDSQHYEDQVHWQVPGEHEDKAQRPLRVEEADTQA,Ammonium transporter Rh type B,Ammonium transporter involved in the maintenance of acid-base homeostasis. Transports ammonium and its related derivative methylammonium across the basolateral plasma membrane of epithelial cells likely contributing to renal transepithelial ammonia transport and ammonia metabolism. May transport either NH4(+) or NH3 ammonia species predominantly mediating an electrogenic NH4(+) transport. May act as a CO2 channel providing for renal acid secretion.,The disruption of the FLD-binding motif impaired the membrane expression of RhBG leading to retention on cytoplasmic structures in transfected Madin-Darby canine kidney cells.,Loss of interaction with ANK3. Intracellular retention; when associated with A-420 and A-421. The disruption of the FLD-binding motif impaired the membrane expression of RhBG leading to retention on cytoplasmic structures in transfected Madin-Darby canine kidney cells.
2495,2495,2495,190332,P02628-K27A,AKDLLKADDIKKALDAVKAEGSFNHKAFFALVGLKAMSANDVKKVFKAIDADASGFIEEEELKFVLKSFAADGRDLTDAETKAFLKAADKDGDGKIGIDEFETLVHEA,In alpha-2.,,AKDLLKADDIKKALDAVKAEGSFNHKKFFALVGLKAMSANDVKKVFKAIDADASGFIEEEELKFVLKSFAADGRDLTDAETKAFLKAADKDGDGKIGIDEFETLVHEA,Parvalbumin alpha,"In muscle, parvalbumin is thought to be involved in relaxation after contraction. It binds two calcium ions.","The substitutions at positions 27 and 31 are located in the region of previously identified epitopes of parvalbumin relevant for PA-specific IgE and IgG binding, which suggests different immunoactivities of the variants.","In alpha-2. The substitutions at positions 27 and 31 are located in the region of previously identified epitopes of parvalbumin relevant for PA-specific IgE and IgG binding, which suggests different immunoactivities of the variants."
2515,2515,2515,191664,P0CH95-H323Y,MASVPVYCLCRLPYDVTRFMIECDVCQDWFHGSCVGVEEDKAAEIDLYHCPNCQVTHGPSVMRKRRGAVKHADVGLGRDSGRPVKTGSAQFVRELRCRTFPSADEVLLKPTGAQLTVEFLEERSFSVPVLVLRKDGLGMNLPPSSFSVTDVEHYIGTEKEIDVIDVSRQADLKMKLGEFVEYYNSPNRDRVLNVISLEFSDTRLSNLVETPKIVRKLSWVENLWPEESIFERPNVQKYCLMGVKDSYTDFHIDFGGTSVWYHVLRGEKIFYLIRPTAANLSLFERWSSSSNQNELFFGDQVDMCYKCSVKQGNTLFIPTGWIYAVLTPVDCLAFGGNFLHSLNIDMQLRAYEIEKRLSTADLFKFPNFETVCWYVGKHLLDTFRGLRENRRHPATYLVHGAKALNNAFRGWTRKESLGEHEQEIPDTIKTQQLVKDLAKEIRLVEDIFQQNIGRSGTPFGGSQGLPSPHPKAQLNTPLTFSQHLSKKRGPKPKEAFGGGGVGPPGAKKKSQKGKEIKTEAGELDLLEIHTKHTLKKFQPGCKVKKSKLELPDDCLDDFEEKINKSKLKLVLTNGKLQGKKGRAGSANGAGSSLQQFQPHMATLSDFDSEDELQIDETPPPRRRPSLPSKKKLAGLPRKLPRAKPCSDPHRIREPGEVDFDIEEDYTTDEEMLTMQGVKGGAGGILDLLKASKQVAGLDSALSEEAPASPSTRDAIQGMLSMANPPSSSSSSSSSSPLSISGGGEMMGLMKEKGGREGWMSGVKKSERKAVFQRPGKRPIKRPARHLSDDESLDEQETLGTCFKDSDYVYPSLESDEEDHVSKSKMKRKRNWDDTPWSPKARVTPTLPKQERPVREGARVASVETGLAAAAAKLAQQEQQKTITKRKYTKKKTPQEKVHSTVAQLQHQPDSAPVSPPLPSEPPVDCIVEERRVEVYSASLLDHEYTAGPGPFSPGGPRGSGAMAPGVFLTSRRPSLSPQNSSSYSPSAPSPGGLVTPTSAGACQGKRPKKGLATAKQRLGKILKI,Unable to rescue a phf8 morpholino mutant.,,MASVPVYCLCRLPYDVTRFMIECDVCQDWFHGSCVGVEEDKAAEIDLYHCPNCQVTHGPSVMRKRRGAVKHADVGLGRDSGRPVKTGSAQFVRELRCRTFPSADEVLLKPTGAQLTVEFLEERSFSVPVLVLRKDGLGMNLPPSSFSVTDVEHYIGTEKEIDVIDVSRQADLKMKLGEFVEYYNSPNRDRVLNVISLEFSDTRLSNLVETPKIVRKLSWVENLWPEESIFERPNVQKYCLMGVKDSYTDFHIDFGGTSVWYHVLRGEKIFYLIRPTAANLSLFERWSSSSNQNELFFGDQVDMCYKCSVKQGNTLFIPTGWIHAVLTPVDCLAFGGNFLHSLNIDMQLRAYEIEKRLSTADLFKFPNFETVCWYVGKHLLDTFRGLRENRRHPATYLVHGAKALNNAFRGWTRKESLGEHEQEIPDTIKTQQLVKDLAKEIRLVEDIFQQNIGRSGTPFGGSQGLPSPHPKAQLNTPLTFSQHLSKKRGPKPKEAFGGGGVGPPGAKKKSQKGKEIKTEAGELDLLEIHTKHTLKKFQPGCKVKKSKLELPDDCLDDFEEKINKSKLKLVLTNGKLQGKKGRAGSANGAGSSLQQFQPHMATLSDFDSEDELQIDETPPPRRRPSLPSKKKLAGLPRKLPRAKPCSDPHRIREPGEVDFDIEEDYTTDEEMLTMQGVKGGAGGILDLLKASKQVAGLDSALSEEAPASPSTRDAIQGMLSMANPPSSSSSSSSSSPLSISGGGEMMGLMKEKGGREGWMSGVKKSERKAVFQRPGKRPIKRPARHLSDDESLDEQETLGTCFKDSDYVYPSLESDEEDHVSKSKMKRKRNWDDTPWSPKARVTPTLPKQERPVREGARVASVETGLAAAAAKLAQQEQQKTITKRKYTKKKTPQEKVHSTVAQLQHQPDSAPVSPPLPSEPPVDCIVEERRVEVYSASLLDHEYTAGPGPFSPGGPRGSGAMAPGVFLTSRRPSLSPQNSSSYSPSAPSPGGLVTPTSAGACQGKRPKKGLATAKQRLGKILKI,Histone lysine demethylase PHF8,"Histone lysine demethylase with selectivity for the di- and monomethyl states that plays a key role cell cycle progression, rDNA transcription and brain development. Demethylates mono- and dimethylated histone H3 'Lys-9' residue (H3K9Me1 and H3K9Me2), dimethylated H3 'Lys-27' (H3K27Me2) and monomethylated histone H4 'Lys-20' residue (H4K20Me1). Acts as a transcription activator as H3K9Me1, H3K9Me2, H3K27Me2 and H4K20Me1 are epigenetic repressive marks. Involved in cell cycle progression by being required to control G1-S transition. Acts as a coactivator of rDNA transcription, by activating polymerase I (pol I) mediated transcription of rRNA genes. Has activity toward H4K20Me1 only when nucleosome is used as a substrate and when not histone octamer is used as substrate. Required for brain development, probably by regulating expression of neuron-specific genes.",Patient mutations at significantly compromise PHF8 catalytic function.,Unable to rescue a phf8 morpholino mutant. Patient mutations at significantly compromise PHF8 catalytic function.
2524,2524,2524,192112,Q7Z5W3-R208A,MAVPTELDGGSVKETAAEEESRVLAPGAAPFGNFPHYSRFHPPEQRLRLLPPELLRQLFPESPENGPILGLDVGCNSGDLSVALYKHFLSLPDGETCSDASREFRLLCCDIDPVLVKRAEKECPFPDALTFITLDFMNQRTRKVLLSSFLSQFGRSVFDIGFCMSITMWIHLNHGDHGLWEFLAHLSSLCHYLLVEPQPWKCYRAAAARLRKLGLHDFDHFHSLAIRGDMPNQIVQILTQDHGMELICCFGNTSWDRSLLLFRAKQTIETHPIPESLIEKGKEKNRLSFQKQ,Strongly decreased O-methyltransferase activity.,,MAVPTELDGGSVKETAAEEESRVLAPGAAPFGNFPHYSRFHPPEQRLRLLPPELLRQLFPESPENGPILGLDVGCNSGDLSVALYKHFLSLPDGETCSDASREFRLLCCDIDPVLVKRAEKECPFPDALTFITLDFMNQRTRKVLLSSFLSQFGRSVFDIGFCMSITMWIHLNHGDHGLWEFLAHLSSLCHYLLVEPQPWKCYRAAARRLRKLGLHDFDHFHSLAIRGDMPNQIVQILTQDHGMELICCFGNTSWDRSLLLFRAKQTIETHPIPESLIEKGKEKNRLSFQKQ,RNA 5'-monophosphate methyltransferase,"O-methyltransferase that specifically monomethylates 5'-monophosphate of cytoplasmic histidyl tRNA (tRNA(His)), acting as a capping enzyme by protecting tRNA(His) from cleavage by DICER1. Also able, with less efficiently, to methylate the 5' monophosphate of a subset of pre-miRNAs, acting as a negative regulator of miRNA processing. The 5' monophosphate of pre-miRNAs is recognized by DICER1 and is required for pre-miRNAs processing: methylation at this position reduces the processing of pre-miRNAs by DICER1. Was also reported to mediate dimethylation of pre-miR-145; however dimethylation cannot be reproduced by another group which observes a monomethylation of pre-miR-145.",,Strongly decreased O-methyltransferase activity.
2534,2534,2534,193387,B9DGI8-S300A,MEKVFSDEEISGNHHWSVNGMTSLNRSASEWAFNRFIQESSAAADDGESTTACGVSVSSPPNVPVDSEEYRAFLKSKLNLACAAVAMKRGTFIKPQDTSGRSDNGGANESEQASLASSKATPMMSSAITSGSELSGDEEEADGETNMNPTNVKRVKRMLSNRESARRSRRRKQAHLSELETQVSQLRVENSKLMKGLTDVTQTFNDASVENRVLKANIETLRAKVKMAEETVKRLTGFNPMFHNMPQIVSTVSLPSETSNSPDTTSSQVTTPEIISSGNKGKALIGCKMNRTASMRRVEALEHLQKRIRSVGDQ,Reduces activity. Abolishes the formation of the BZIP2-BZIP63 heterodimer; when associated with A-29 and A-294.,,MEKVFSDEEISGNHHWSVNGMTSLNRSASEWAFNRFIQESSAAADDGESTTACGVSVSSPPNVPVDSEEYRAFLKSKLNLACAAVAMKRGTFIKPQDTSGRSDNGGANESEQASLASSKATPMMSSAITSGSELSGDEEEADGETNMNPTNVKRVKRMLSNRESARRSRRRKQAHLSELETQVSQLRVENSKLMKGLTDVTQTFNDASVENRVLKANIETLRAKVKMAEETVKRLTGFNPMFHNMPQIVSTVSLPSETSNSPDTTSSQVTTPEIISSGNKGKALIGCKMNRTASMRRVESLEHLQKRIRSVGDQ,Basic leucine zipper 63,Transcription factor involved in controlling responses to starvation. BZIP2-BZIP63-KIN10 complex binds to the ETFQO promoter to up-regulate its transcription.,"Phosphorylation of bZIP63 by SnRK1 at changed its dimerization preference, affecting target gene expression and ultimately primary metabolism. The mutation in the SnRK1 protein leads to a functional change in the regulation of transcription via binding to G-box promoter elements. It also affects the formation of C/S1-heterodimers and the recruitment of SnRK1 directly to target promoters.","Reduces activity. Abolishes the formation of the BZIP2-BZIP63 heterodimer; when associated with A-29 and A-294. Phosphorylation of bZIP63 by SnRK1 at changed its dimerization preference, affecting target gene expression and ultimately primary metabolism. The mutation in the SnRK1 protein leads to a functional change in the regulation of transcription via binding to G-box promoter elements. It also affects the formation of C/S1-heterodimers and the recruitment of SnRK1 directly to target promoters."
2535,2535,2535,193426,P35226-H174E,MHRTTRIKITELNPHLMCVLCGGYFIDATTIIECLHSFCKTCIVRYLETSKYCPICDVQVHKTRPLLNIRSDKTLQDIVYKLVPGLFKNEMKRRRDFYAAHPSADAANGSNEDRGEVADEDKRIITDDEIISLSIEFFDQNRLDRKVNKDKEKSKEEVNDKRYLRCPAAMTVMELRKFLRSKMDIPNTFQIDVMYEEEPLKDYYTLMDIAYIYTWRRNGPLPLKYRVRPTCKRMKISHQRDGLTNAGELESDSGSDKANSPAGGIPSTSSCLPSPSTPVQSPHPQFPHISSTMNGTSNSPSGNHQSSFANRPRKSSVNGSSATSSG,Strongly decreases affinity for PHC2. Abolishes interaction with PHC2; when associated with E-165.,,MHRTTRIKITELNPHLMCVLCGGYFIDATTIIECLHSFCKTCIVRYLETSKYCPICDVQVHKTRPLLNIRSDKTLQDIVYKLVPGLFKNEMKRRRDFYAAHPSADAANGSNEDRGEVADEDKRIITDDEIISLSIEFFDQNRLDRKVNKDKEKSKEEVNDKRYLRCPAAMTVMHLRKFLRSKMDIPNTFQIDVMYEEEPLKDYYTLMDIAYIYTWRRNGPLPLKYRVRPTCKRMKISHQRDGLTNAGELESDSGSDKANSPAGGIPSTSSCLPSPSTPVQSPHPQFPHISSTMNGTSNSPSGNHQSSFANRPRKSSVNGSSATSSG,Polycomb complex protein BMI-1,"Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. The complex composed of RNF2, UB2D3 and BMI1 binds nucleosomes, and has activity only with nucleosomal histone H2A. In the PRC1-like complex, regulates the E3 ubiquitin-protein ligase activity of RNF2/RING2.",The mutation in the BMI1 protein affects its interaction with polyhomeotic proteins and homo-oligomerization via the UBL domain. This mutation is necessary for the ubiquitination activity of PRC1 and the clonogenic potential of U2OS cells.,Strongly decreases affinity for PHC2. Abolishes interaction with PHC2; when associated with E-165. The mutation in the BMI1 protein affects its interaction with polyhomeotic proteins and homo-oligomerization via the UBL domain. This mutation is necessary for the ubiquitination activity of PRC1 and the clonogenic potential of U2OS cells.
2567,2567,2567,195518,Q06124-I309V,MTSRRWFHPNITGVEAENLLLTRGVDGSFLARPSKSNPGDFTLSVRRNGAVTHIKIQNTGDYYDLYGGEKFATLAELVQYYMEHHGQLKEKNGDVIELKYPLNCADPTSERWFHGHLSGKEAEKLLTEKGKHGSFLVRESQSHPGDFVLSVRTGDDKGESNDGKSKVTHVMIRCQELKYDVGGGERFDSLTDLVEHYKKNPMVETLGTVLQLKQPLNTTRINAAEIESRVRELSKLAETTDKVKQGFWEEFETLQQQECKLLYSRKEGQRQENKNKNRYKNILPFDHTRVVLHDGDPNEPVSDYINANVIMPEFETKCNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSRVIVMTTKEVERGKSKCVKYWPDEYALKEYGVMRVRNVKESAAHDYTLRELKLSKVGQGNTERTVWQYHFRTWPDHGVPSDPGGVLDFLEEVHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVDCDIDVPKTIQMVRSQRSGMVQTEAQYRFIYMAVQHYIETLQRRIEEEQKSKRKGHEYTNIKYSLADQTSGDQSPLPPCTPTPPCAEMREDSARVYENVGLMQQQKSFR,In NS1; unknown pathological significance.,,MTSRRWFHPNITGVEAENLLLTRGVDGSFLARPSKSNPGDFTLSVRRNGAVTHIKIQNTGDYYDLYGGEKFATLAELVQYYMEHHGQLKEKNGDVIELKYPLNCADPTSERWFHGHLSGKEAEKLLTEKGKHGSFLVRESQSHPGDFVLSVRTGDDKGESNDGKSKVTHVMIRCQELKYDVGGGERFDSLTDLVEHYKKNPMVETLGTVLQLKQPLNTTRINAAEIESRVRELSKLAETTDKVKQGFWEEFETLQQQECKLLYSRKEGQRQENKNKNRYKNILPFDHTRVVLHDGDPNEPVSDYINANIIMPEFETKCNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSRVIVMTTKEVERGKSKCVKYWPDEYALKEYGVMRVRNVKESAAHDYTLRELKLSKVGQGNTERTVWQYHFRTWPDHGVPSDPGGVLDFLEEVHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVDCDIDVPKTIQMVRSQRSGMVQTEAQYRFIYMAVQHYIETLQRRIEEEQKSKRKGHEYTNIKYSLADQTSGDQSPLPPCTPTPPCAEMREDSARVYENVGLMQQQKSFR,Tyrosine-protein phosphatase non-receptor type 11,"Acts downstream of various receptor and cytoplasmic protein tyrosine kinases to participate in the signal transduction from the cell surface to the nucleus. Positively regulates MAPK signal transduction pathway. Dephosphorylates GAB1, ARHGAP35 and EGFR. Dephosphorylates ROCK2 at 'Tyr-722' resulting in stimulation of its RhoA binding activity. Dephosphorylates CDC73. Dephosphorylates SOX9 on tyrosine residues, leading to inactivate SOX9 and promote ossification. Dephosphorylates tyrosine-phosphorylated NEDD9/CAS-L.",,In NS1; unknown pathological significance.
2572,2572,2572,195707,P24937-L40Q,MEDINFASLAPRHGSRPFMGNWQDIGTSNMSGGAFSWGSQWSGIKNFGSTVKNYGSKAWNSSTGQMLRDKLKEQNFQQKVVDGLASGISGVVDLANQAVQNKINSKLDPRPPVEEPPPAVETVSPEGRGEKRPRPDREETLVTQIDEPPSYEEALKQGLPTTRPIAPMATGVLGQHTPVTLDLPPPADTQQKPVLPGPTAVVVTRPSRASLRRAASGPRSLRPVASGNWQSTLNSIVGLGVQSLKRRRCF,Impaired endosome penetration and reduces infectivity.,,MEDINFASLAPRHGSRPFMGNWQDIGTSNMSGGAFSWGSLWSGIKNFGSTVKNYGSKAWNSSTGQMLRDKLKEQNFQQKVVDGLASGISGVVDLANQAVQNKINSKLDPRPPVEEPPPAVETVSPEGRGEKRPRPDREETLVTQIDEPPSYEEALKQGLPTTRPIAPMATGVLGQHTPVTLDLPPPADTQQKPVLPGPTAVVVTRPSRASLRRAASGPRSLRPVASGNWQSTLNSIVGLGVQSLKRRRCF,Pre-protein VI,"During virus assembly, promotes hexon trimers nuclear import through nuclear pore complexes via an importin alpha/beta-dependent mechanism. By analogy to herpesviruses capsid assembly, might act as a chaperone to promote the formation of the icosahedral capsid.Structural component of the virion that provides increased stability to the particle shell through its interaction with the core-capsid bridging protein and the hexon-linking protein VIII. Fibers shedding during virus entry into host cell allows the endosome lysis protein to be exposed as a membrane-lytic peptide. Exhibits pH-independent membrane fragmentation activity and probably mediates viral rapid escape from host endosome via organellar membrane lysis. It is not clear if it then remains partially associated with the capsid and involved in the intracellular microtubule-dependent transport of capsid to the nucleus, or if it is lost during endosomal penetration.Cofactor that activates the viral protease. Binds to viral protease in a 1:1 ratio.",The mutation in protein VI significantly reduces infectivity and selectively impairs endosome penetration. The lack of efficient endosomalysis is associated with reduced insertion of the mutation in protein VI into membranes. These findings indicate that protein VI is the critical membrane lytic factor of AdV during cellular entry.,Impaired endosome penetration and reduces infectivity. The mutation in protein VI significantly reduces infectivity and selectively impairs endosome penetration. The lack of efficient endosomalysis is associated with reduced insertion of the mutation in protein VI into membranes. These findings indicate that protein VI is the critical membrane lytic factor of AdV during cellular entry.
2575,2575,2575,195847,Q9Y3D7-L94A,MAKYLAQIIVMGVQVVGRAFARALRQEFAASRAAADARGRAGHRSAAASNLSGLSLQEAQQILNVSKLSPEEVQKNYEHLFKVNDKSVGGSFYAQSKVVRAKERLDEELKIQAQEDREKGQMPHT,No effect on protein translocation into mitochondria in a heterologous system.,,MAKYLAQIIVMGVQVVGRAFARALRQEFAASRAAADARGRAGHRSAAASNLSGLSLQEAQQILNVSKLSPEEVQKNYEHLFKVNDKSVGGSFYLQSKVVRAKERLDEELKIQAQEDREKGQMPHT,Mitochondrial import inner membrane translocase subunit TIM16,Regulates ATP-dependent protein translocation into the mitochondrial matrix. Inhibits DNAJC19 stimulation of HSPA9/Mortalin ATPase activity.,resulting in temperature sensitivity and in vivo protein translocation defects in yeast cells.,No effect on protein translocation into mitochondria in a heterologous system. resulting in temperature sensitivity and in vivo protein translocation defects in yeast cells.
2577,2577,2577,195942,O43148-R450E,MANSAKAEEYEKMSLEQAKASVNSETESSFNINENTTASGTGLSEKTSVCRQVDIARKRKEFEDDLVKESSSCGKDTPSKKRKLDPEIVPEEKDCGDAEGNSKKRKRETEDVPKDKSSTGDGTQNKRKIALEDVPEKQKNLEEGHSSTVAAHYNELQEVGLEKRSQSRIFYLRNFNNWMKSVLIGEFLEKVRQKKKRDITVLDLGCGKGGDLLKWKKGRINKLVCTDIADVSVKQCQQRYEDMKNRRDSEYIFSAEFITADSSKELLIDKFRDPQMCFDICSCQFVCHYSFESYEQADMMLRNACERLSPGGYFIGTTPNSFELIRRLEASETESFGNEIYTVKFQKKGDYPLFGCKYDFNLEGVVDVPEFLVYFPLLNEMAKKYNMKLVYKKTFLEFYEEKIKNNENKMLLKRMQALEPYPANESSKLVSEKVDDYEHAAKYMKNSQVELPLGTLSKSEWEATSIYLVFAFEKQQ,Increased S-adenosyl-L-methionine binding and methyltransferase activity in absence of RAMAC; when associated with E-452. No change in interaction with RAMAC; when associated with E-452.,,MANSAKAEEYEKMSLEQAKASVNSETESSFNINENTTASGTGLSEKTSVCRQVDIARKRKEFEDDLVKESSSCGKDTPSKKRKLDPEIVPEEKDCGDAEGNSKKRKRETEDVPKDKSSTGDGTQNKRKIALEDVPEKQKNLEEGHSSTVAAHYNELQEVGLEKRSQSRIFYLRNFNNWMKSVLIGEFLEKVRQKKKRDITVLDLGCGKGGDLLKWKKGRINKLVCTDIADVSVKQCQQRYEDMKNRRDSEYIFSAEFITADSSKELLIDKFRDPQMCFDICSCQFVCHYSFESYEQADMMLRNACERLSPGGYFIGTTPNSFELIRRLEASETESFGNEIYTVKFQKKGDYPLFGCKYDFNLEGVVDVPEFLVYFPLLNEMAKKYNMKLVYKKTFLEFYEEKIKNNENKMLLKRMQALEPYPANESSKLVSEKVDDYEHAAKYMKNSQVRLPLGTLSKSEWEATSIYLVFAFEKQQ,mRNA cap guanine-N7 methyltransferase,Catalytic subunit of the mRNA-capping methyltransferase RNMT:RAMAC complex that methylates the N7 position of the added guanosine to the 5'-cap structure of mRNAs. Binds RNA containing 5'-terminal GpppC.,"The mutation in the RNMT protein causes functional changes in the mechanism by which RAM allosterically activates RNMT, allowing it to function as a molecular rheostat for mRNA cap methylation.","Increased S-adenosyl-L-methionine binding and methyltransferase activity in absence of RAMAC; when associated with E-452. No change in interaction with RAMAC; when associated with E-452. The mutation in the RNMT protein causes functional changes in the mechanism by which RAM allosterically activates RNMT, allowing it to function as a molecular rheostat for mRNA cap methylation."
2598,2598,2598,197092,Q92560-G178V,MNKGWLELESDPGLFTLLVEDFGVKGVQVEEIYDLQSKCQGPVYGFIFLFKWIEERRSRRKVSTLVDDTSVIDDDIVNNMFFAHQLIPNSCATHALLSVLLNCSSVDLGPTLSRMKDFTKGFSPESKGYAIGNAPELAKAHNSHARPEPRHLPEKQNGLSAVRTMEAFHFVSYVPITVRLFELDGLKVYPIDHGPWGEDEEWTDKARRVIMERIGLATAGEPYHDIRFNLMAVVPDRRIKYEARLHVLKVNRQTVLEALQQLIRVTQPELIQTHKSQESQLPEESKSASNKSPLVLEANRAPAASEGNHTDGAEEAAGSCAQAPSHSPPNKPKLVVKPPGSSLNGVHPNPTPIVQRLPAFLDNHNYAKSPMQEEEDLAAGVGRSRVPVRPPQQYSDDEDDYEDDEEDDVQNTNSALRYKGKGTGKPGALSGSADGQLSVLQPNTINVLAEKLKESQKDLSIPLSIKTSSGAGSPAVAVPTHSQPSPTPSNESTDTASEIGSAFNSPLRSPIRSANPTRPSSPVTSHISKVLFGEDDSLLRVDCIRYNRAVRDLGPVISTGLLHLAEDGVLSPLALTEGGKGSSPSIRPIQGSQGSSSPVEKEVVEATDSREKTGMVRPGEPLSGEKYSPKELLALLKCVEAEIANYEACLKEEVEKRKKFKIDDQRRTHNYDEFICTFISMLAQEGMLANLVEQNISVRRRQGVSIGRLHKQRKPDRRKRSRPYKAKRQ,In a lung cancer sample; induces cytoplasmic accumulation; impairs deubiquitinase activity; up-regulates heat shock response; induces formation of beta-amyloid aggregates.,,MNKGWLELESDPGLFTLLVEDFGVKGVQVEEIYDLQSKCQGPVYGFIFLFKWIEERRSRRKVSTLVDDTSVIDDDIVNNMFFAHQLIPNSCATHALLSVLLNCSSVDLGPTLSRMKDFTKGFSPESKGYAIGNAPELAKAHNSHARPEPRHLPEKQNGLSAVRTMEAFHFVSYVPITGRLFELDGLKVYPIDHGPWGEDEEWTDKARRVIMERIGLATAGEPYHDIRFNLMAVVPDRRIKYEARLHVLKVNRQTVLEALQQLIRVTQPELIQTHKSQESQLPEESKSASNKSPLVLEANRAPAASEGNHTDGAEEAAGSCAQAPSHSPPNKPKLVVKPPGSSLNGVHPNPTPIVQRLPAFLDNHNYAKSPMQEEEDLAAGVGRSRVPVRPPQQYSDDEDDYEDDEEDDVQNTNSALRYKGKGTGKPGALSGSADGQLSVLQPNTINVLAEKLKESQKDLSIPLSIKTSSGAGSPAVAVPTHSQPSPTPSNESTDTASEIGSAFNSPLRSPIRSANPTRPSSPVTSHISKVLFGEDDSLLRVDCIRYNRAVRDLGPVISTGLLHLAEDGVLSPLALTEGGKGSSPSIRPIQGSQGSSSPVEKEVVEATDSREKTGMVRPGEPLSGEKYSPKELLALLKCVEAEIANYEACLKEEVEKRKKFKIDDQRRTHNYDEFICTFISMLAQEGMLANLVEQNISVRRRQGVSIGRLHKQRKPDRRKRSRPYKAKRQ,Ubiquitin carboxyl-terminal hydrolase BAP1,"Deubiquitinating enzyme that plays a key role in chromatin by mediating deubiquitination of histone H2A and HCFC1. Catalytic component of the PR-DUB complex, a complex that specifically mediates deubiquitination of histone H2A monoubiquitinated at 'Lys-119' (H2AK119ub1). Does not deubiquitinate monoubiquitinated histone H2B. Acts as a regulator of cell growth by mediating deubiquitination of HCFC1 N-terminal and C-terminal chains, with some specificity toward 'Lys-48'-linked polyubiquitin chains compared to 'Lys-63'-linked polyubiquitin chains. Deubiquitination of HCFC1 does not lead to increase stability of HCFC1. Interferes with the BRCA1 and BARD1 heterodimer activity by inhibiting their ability to mediate ubiquitination and autoubiquitination. It however does not mediate deubiquitination of BRCA1 and BARD1. Able to mediate autodeubiquitination via intramolecular interactions to couteract monoubiquitination at the nuclear localization signal (NLS), thereby protecting it from cytoplasmic sequestration. Acts as a tumor suppressor.","The mutation in the catalytic domain of BAP1 triggers cytoplasmic/perinuclear accumulation in BAP1 deficient cells. This abnormal cellular localization has been observed in proteins that undergo aggregation in cellular conditions. The mutant BAP1 also exhibits amyloidogenic activity, as indicated by its reactivity towards anti oligomeric antibody in HEK293T cells. Additionally, the mutation leads to structural destabilization in the catalytic domain, resulting in the formation of beta amyloid structures.","In a lung cancer sample; induces cytoplasmic accumulation; impairs deubiquitinase activity; up-regulates heat shock response; induces formation of beta-amyloid aggregates. The mutation in the catalytic domain of BAP1 triggers cytoplasmic/perinuclear accumulation in BAP1 deficient cells. This abnormal cellular localization has been observed in proteins that undergo aggregation in cellular conditions. The mutant BAP1 also exhibits amyloidogenic activity, as indicated by its reactivity towards anti oligomeric antibody in HEK293T cells. Additionally, the mutation leads to structural destabilization in the catalytic domain, resulting in the formation of beta amyloid structures."
2623,2623,2623,198784,P0A9N8-C19A,MNYHQYYPVDIVNGPGTRATLFVSGCVHECPGCYNKSTWRVNSGQPFTKAMEDQIINDLNDTRIKRQGISLSGGDPLHPQNVPDILKLVQRIRAECPGKDIWVWTGYKLDELNAAQMQVVDLINVLVDGKFVQDLKDPSLIWRGSSNQVVHHLR,No change in activity. Does not affect iron and sulfide content.,,MNYHQYYPVDIVNGPGTRCTLFVSGCVHECPGCYNKSTWRVNSGQPFTKAMEDQIINDLNDTRIKRQGISLSGGDPLHPQNVPDILKLVQRIRAECPGKDIWVWTGYKLDELNAAQMQVVDLINVLVDGKFVQDLKDPSLIWRGSSNQVVHHLR,Anaerobic ribonucleoside-triphosphate reductase-activating protein,"Activation of anaerobic ribonucleoside-triphosphate reductase under anaerobic conditions by generation of an organic free radical, using S-adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5'-deoxy-adenosine.",The mutation in protein beta results in catalytic inactivity.,No change in activity. Does not affect iron and sulfide content. The mutation in protein beta results in catalytic inactivity.
2676,2676,2676,203891,Q570C0-G147D,MQKRIALSFPEEVLEHVFSFIQLDKDRNSVSLVCKSWYEIERWCRRKVFIGNCYAVSPATVIRRFPKVRSVELKGKPHFADFNLVPDGWGGYVYPWIEAMSSSYTWLEEIRLKRMVVTDDCLELIAKSFKNFKVLVLSSCEGFSTDDLAAIAATCRNLKELDLRESDVDDVSGHWLSHFPDTYTSLVSLNISCLASEVSFSALERLVTRCPNLKSLKLNRAVPLEKLATLLQRAPQLEELGTGGYTAEVRPDVYSGLSVALSGCKELRCLSGFWDAVPAYLPAVYSVCSRLTTLNLSYATVQSYDLVKLLCQCPKLQRLWVLDYIEDAGLEVLASTCKDLRELRVFPSEPFVMEPNVALTEQGLVSVSMGCPKLESVLYFCRQMTNAALITIARNRPNMTRFRLCIIEPKAPDYLTLEPLDIGFGAIVEHCKDLRRLSLSGLLTDKVFEYIGTYAKKMEMLSVAFAGDSDLGMHHVLSGCDSLRKLEIRDCPFGDKALLANASKLETMRSLWMSSCSVSFGACKLLGQKMPKLNVEVIDERGAPDSRPESCPVERVFIYRTVAGPRFDMPGFVWNMDQDSTMRFSRQIITTNGL,In tir1-1; insensitive to auxin ubiquitously and to ethylene in roots only.,,MQKRIALSFPEEVLEHVFSFIQLDKDRNSVSLVCKSWYEIERWCRRKVFIGNCYAVSPATVIRRFPKVRSVELKGKPHFADFNLVPDGWGGYVYPWIEAMSSSYTWLEEIRLKRMVVTDDCLELIAKSFKNFKVLVLSSCEGFSTDGLAAIAATCRNLKELDLRESDVDDVSGHWLSHFPDTYTSLVSLNISCLASEVSFSALERLVTRCPNLKSLKLNRAVPLEKLATLLQRAPQLEELGTGGYTAEVRPDVYSGLSVALSGCKELRCLSGFWDAVPAYLPAVYSVCSRLTTLNLSYATVQSYDLVKLLCQCPKLQRLWVLDYIEDAGLEVLASTCKDLRELRVFPSEPFVMEPNVALTEQGLVSVSMGCPKLESVLYFCRQMTNAALITIARNRPNMTRFRLCIIEPKAPDYLTLEPLDIGFGAIVEHCKDLRRLSLSGLLTDKVFEYIGTYAKKMEMLSVAFAGDSDLGMHHVLSGCDSLRKLEIRDCPFGDKALLANASKLETMRSLWMSSCSVSFGACKLLGQKMPKLNVEVIDERGAPDSRPESCPVERVFIYRTVAGPRFDMPGFVWNMDQDSTMRFSRQIITTNGL,Protein TRANSPORT INHIBITOR RESPONSE 1,"Auxin receptor that mediates Aux/IAA proteins proteasomal degradation and auxin-regulated transcription. The SCF(TIR1) E3 ubiquitin ligase complex is involved in auxin-mediated signaling pathway that regulate root and hypocotyl growth, lateral root formation, cell elongation, and gravitropism. Appears to allow pericycle cells to overcome G2 arrest prior to lateral root development. Plays a role in ethylene signaling in roots. Confers sensitivity to the virulent bacterial pathogen P.syringae.",The tir1 mutants are deficient in a variety of auxin-regulated growth processes including hypocotyl elongation and lateral root formation.,In tir1-1; insensitive to auxin ubiquitously and to ethylene in roots only. The tir1 mutants are deficient in a variety of auxin-regulated growth processes including hypocotyl elongation and lateral root formation.
2692,2692,2692,205482,Q5BJF2-E73Q,MGAPATRRCVEWLLGLYFLSHIPITLFMDLQAVLPRELYPVEFRNLLKWYAKEFKDPLLQEPPAWFKSFLFCQLVFQLPFFPIATYAFLKGSCKWIRTPAIIYSVHTMTTLIPILSTFLFEDFSKASGFKGQRPETLHERLTLVSVYAPYLLIPFILLIFMLRSPYYKYEEKRKKK,No effect on DTG binding.,,MGAPATRRCVEWLLGLYFLSHIPITLFMDLQAVLPRELYPVEFRNLLKWYAKEFKDPLLQEPPAWFKSFLFCELVFQLPFFPIATYAFLKGSCKWIRTPAIIYSVHTMTTLIPILSTFLFEDFSKASGFKGQRPETLHERLTLVSVYAPYLLIPFILLIFMLRSPYYKYEEKRKKK,Sigma intracellular receptor 2,"Intracellular orphan receptor that binds numerous drugs and which is highly expressed in various proliferating cancer cells. Corresponds to the sigma-2 receptor, which is thought to play important role in regulating cell survival, morphology and differentiation. Under investigation for its potential diagnostic and therapeutic uses. May play a role as a regulator of cellular cholesterol homeostasis. May function as sterol isomerase. May alter the activity of some cytochrome P450 proteins.",,No effect on DTG binding.
2697,2697,2697,205955,P14923-S24A,MEVMNLMEQPIKVTEWQQTYTYDAGIHSGANTCVPSVSSKGIMEEDEACGRQYTLKKTTTYTQGVPPSQGDLEYQMSTTARAKRVREAMCPGVSGEDSSLLLATQVEGQATNLQRLAEPSQLLKSAIVHLINYQDDAELATRALPELTKLLNDEDPVVVTKAAMIVNQLSKKEASRRALMGSPQLVAAVVRTMQNTSDLDTARCTTSILHNLSHHREGLLAIFKSGGIPALVRMLSSPVESVLFYAITTLHNLLLYQEGAKMAVRLADGLQKMVPLLNKNNPKFLAITTDCLQLLAYGNQESKLIILANGGPQALVQIMRNYSYEKLLWTTSRVLKVLSVCPSNKPAIVEAGGMQALGKHLTSNSPRLVQNCLWTLRNLSDVATKQEGLESVLKILVNQLSVDDVNVLTCATGTLSNLTCNNSKNKTLVTQNSGVEALIHAILRAGDKDDITEPAVCALRHLTSRHPEAEMAQNSVRLNYGIPAIVKLLNQPNQWPLVKATIGLIRNLALCPANHAPLQEAAVIPRLVQLLVKAHQDAQRHVAAGTQQPYTDGVRMEEIVEGCTGALHILARDPMNRMEIFRLNTIPLFVQLLYSSVENIQRVAAGVLCELAQDKEAADAIDAEGASAPLMELLHSRNEGTATYAAAVLFRISEDKNPDYRKRVSVELTNSLFKHDPAAWEAAQSMIPINEPYGDDMDATYRPMYSSDVPLDPLEMHMDMDGDYPIDTYSDGLRPPYPTADHMLA,Does not affect glycosylation.,,MEVMNLMEQPIKVTEWQQTYTYDSGIHSGANTCVPSVSSKGIMEEDEACGRQYTLKKTTTYTQGVPPSQGDLEYQMSTTARAKRVREAMCPGVSGEDSSLLLATQVEGQATNLQRLAEPSQLLKSAIVHLINYQDDAELATRALPELTKLLNDEDPVVVTKAAMIVNQLSKKEASRRALMGSPQLVAAVVRTMQNTSDLDTARCTTSILHNLSHHREGLLAIFKSGGIPALVRMLSSPVESVLFYAITTLHNLLLYQEGAKMAVRLADGLQKMVPLLNKNNPKFLAITTDCLQLLAYGNQESKLIILANGGPQALVQIMRNYSYEKLLWTTSRVLKVLSVCPSNKPAIVEAGGMQALGKHLTSNSPRLVQNCLWTLRNLSDVATKQEGLESVLKILVNQLSVDDVNVLTCATGTLSNLTCNNSKNKTLVTQNSGVEALIHAILRAGDKDDITEPAVCALRHLTSRHPEAEMAQNSVRLNYGIPAIVKLLNQPNQWPLVKATIGLIRNLALCPANHAPLQEAAVIPRLVQLLVKAHQDAQRHVAAGTQQPYTDGVRMEEIVEGCTGALHILARDPMNRMEIFRLNTIPLFVQLLYSSVENIQRVAAGVLCELAQDKEAADAIDAEGASAPLMELLHSRNEGTATYAAAVLFRISEDKNPDYRKRVSVELTNSLFKHDPAAWEAAQSMIPINEPYGDDMDATYRPMYSSDVPLDPLEMHMDMDGDYPIDTYSDGLRPPYPTADHMLA,Junction plakoglobin,Common junctional plaque protein. The membrane-associated plaques are architectural elements in an important strategic position to influence the arrangement and function of both the cytoskeleton and the cells within the tissue. The presence of plakoglobin in both the desmosomes and in the intermediate junctions suggests that it plays a central role in the structure and function of submembranous plaques. Acts as a substrate for VE-PTP and is required by it to stimulate VE-cadherin function in endothelial cells. Can replace beta-catenin in E-cadherin/catenin adhesion complexes which are proposed to couple cadherins to the actin cytoskeleton.,,Does not affect glycosylation.
2717,2717,2717,207991,P0CE48-H20A,MSKEKFERTKPHVNVGTIGAVDHGKTTLTAAITTVLAKTYGGAARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALEGDAEWEAKILELAGFLDSYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIKETQKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTIKPHTKFESEVYILSKDEGGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFAIREGGRTVGAGVVAKVLS,No change in binding GDP and 3-fold reduction in binding EF-Ts.,,MSKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALEGDAEWEAKILELAGFLDSYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIKETQKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTIKPHTKFESEVYILSKDEGGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFAIREGGRTVGAGVVAKVLS,Elongation factor Tu 2,"(Microbial infection) Upon infection by bacteriophage Qbeta, part of the viral RNA-dependent RNA polymerase complex. With EF-Ts may provide a stabilizing scaffold for the beta (catalytic) subunit. Helps separate the double-stranded RNA of the template and growing RNA during elongation. With the beta subunit helps form the exit tunnel for template RNA. The GTPase activity of this subunit is not required for viral RNA replication.",,No change in binding GDP and 3-fold reduction in binding EF-Ts.
2729,2729,0,0,Q14680-A286C,MKDYDELLKYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHLQTCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQMLQVDPKKRISMKNLLNHPWIMQDYNYPVEWQSKNPFIHLDDDCVTELSVHHRNNRQTMEDLISLWQYDHLTATYLLLLAKKARGKPVRLRLSSFSCGQASATPFTDIKSNNWSLEDVTASDKNYVAGLIDYDWCEDDLSTGAATPRTSQFTKYWTESNGVESKSLTPALCRTPANKLKNKENVYTPKSAVKNEEYFMFPEPKTPVNKNQHKREILTTPNRYTTPSKARNQCLKETPIKIPVNSTGTDKLMTGVISPERRCRSVELDLNQAHMEETPKRKGAKVFGSLERGLDKVITVLTRSKRKGSARDGPRRLKLHYNVTTTRLVNPDQLLNEIMSILPKKHVDFVQKGYTLKCQTQSDFGKVTMQFELEVCQLQKPDVVGIRRQRLKGDAWVYKRLVEDILSSCKV,,-1.0,MKDYDELLKYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHLQTCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQMLQVDPKKRISMKNLLNHPWIMQDYNYPVEWQSKNPFIHLDDDAVTELSVHHRNNRQTMEDLISLWQYDHLTATYLLLLAKKARGKPVRLRLSSFSCGQASATPFTDIKSNNWSLEDVTASDKNYVAGLIDYDWCEDDLSTGAATPRTSQFTKYWTESNGVESKSLTPALCRTPANKLKNKENVYTPKSAVKNEEYFMFPEPKTPVNKNQHKREILTTPNRYTTPSKARNQCLKETPIKIPVNSTGTDKLMTGVISPERRCRSVELDLNQAHMEETPKRKGAKVFGSLERGLDKVITVLTRSKRKGSARDGPRRLKLHYNVTTTRLVNPDQLLNEIMSILPKKHVDFVQKGYTLKCQTQSDFGKVTMQFELEVCQLQKPDVVGIRRQRLKGDAWVYKRLVEDILSSCKV,Maternal embryonic leucine zipper kinase,"Serine/threonine-protein kinase involved in various processes such as cell cycle regulation, self-renewal of stem cells, apoptosis and splicing regulation. Has a broad substrate specificity; phosphorylates BCL2L14, CDC25B, MAP3K5/ASK1 and ZNF622. Acts as an activator of apoptosis by phosphorylating and activating MAP3K5/ASK1. Acts as a regulator of cell cycle, notably by mediating phosphorylation of CDC25B, promoting localization of CDC25B to the centrosome and the spindle poles during mitosis. Plays a key role in cell proliferation and carcinogenesis. Required for proliferation of embryonic and postnatal multipotent neural progenitors. Phosphorylates and inhibits BCL2L14, possibly leading to affect mammary carcinogenesis by mediating inhibition of the pro-apoptotic function of BCL2L14. Also involved in the inhibition of spliceosome assembly during mitosis by phosphorylating ZNF622, thereby contributing to its redirection to the nucleus. May also play a role in primitive hematopoiesis.",Enables dependence to reducing agents; when associated with V-29; V-70; A-89; A-154; A-168; A-169; A-204; and A-339.,Enables dependence to reducing agents; when associated with V-29; V-70; A-89; A-154; A-168; A-169; A-204; and A-339.
2758,2758,0,0,Q17868-F10Y,MTTGNNDFYYSNKYEDDEFEYRHVHVTKDVSKLIPKNRLMSETEWRSLGIQQSPGWMHYMIHGPERHVLLFRRPLAATQKTGGNVRSGNAVGVR,,-1.0,MTTGNNDFYFSNKYEDDEFEYRHVHVTKDVSKLIPKNRLMSETEWRSLGIQQSPGWMHYMIHGPERHVLLFRRPLAATQKTGGNVRSGNAVGVR,Cyclin-dependent kinases regulatory subunit,"Binds to the catalytic subunit of the cyclin dependent kinases and is essential for their biological function. Has a role in the exit from M phase during early mitotic cell division. More specifically, thought to act by degrading B-type cyclins that causes breakdown of nuclear envelope and exit mitosis.",Increases cdk-1 binding in ne549.,Increases cdk-1 binding in ne549.
2762,2762,0,0,P98170-A141L,MTFNSFEGSKTCVPADINKEEEFVEEFNRLKTFANFPSGSPVSASTLARAGFLYTGEGDTVRCFSCHAAVDRWQYGDSAVGRHRKVSPNCRFINGFYLENSATQSTNSGIQNGQYKVENYLGSRDHFALDRPSETHADYLLRTGQVVDISDTIYPRNPAMYSEEARLKSFQNWPDYAHLTPRELASAGLYYTGIGDQVQCFCCGGKLKNWEPCDRAWSEHRRHFPNCFFVLGRNLNIRSESDAVSSDRNFPNSTNLPRNPSMADYEARIFTFGTWIYSVNKEQLARAGFYALGEGDKVKCFHCGGGLTDWKPSEDPWEQHAKWYPGCKYLLEQKGQEYINNIHLTHSLEECLVRTTEKTPSLTRRIDDTIFQNPMVQEAIRMGFSFKDIKKIMEEKIQISGSNYKSLEVLVADLVNAQKDSMQDESSQTSLQKEISTEEQLRRLQEEKLCKICMDRNIAIVFVPCGHLVTCKQCAEAVDKCPMCYTVITFKQKIFMS,,-1.0,MTFNSFEGSKTCVPADINKEEEFVEEFNRLKTFANFPSGSPVSASTLARAGFLYTGEGDTVRCFSCHAAVDRWQYGDSAVGRHRKVSPNCRFINGFYLENSATQSTNSGIQNGQYKVENYLGSRDHFALDRPSETHADYLARTGQVVDISDTIYPRNPAMYSEEARLKSFQNWPDYAHLTPRELASAGLYYTGIGDQVQCFCCGGKLKNWEPCDRAWSEHRRHFPNCFFVLGRNLNIRSESDAVSSDRNFPNSTNLPRNPSMADYEARIFTFGTWIYSVNKEQLARAGFYALGEGDKVKCFHCGGGLTDWKPSEDPWEQHAKWYPGCKYLLEQKGQEYINNIHLTHSLEECLVRTTEKTPSLTRRIDDTIFQNPMVQEAIRMGFSFKDIKKIMEEKIQISGSNYKSLEVLVADLVNAQKDSMQDESSQTSLQKEISTEEQLRRLQEEKLCKICMDRNIAIVFVPCGHLVTCKQCAEAVDKCPMCYTVITFKQKIFMS,E3 ubiquitin-protein ligase XIAP,"Multi-functional protein which regulates not only caspases and apoptosis, but also modulates inflammatory signaling and immunity, copper homeostasis, mitogenic kinase signaling, cell proliferation, as well as cell invasion and metastasis. Acts as a direct caspase inhibitor. Directly bind to the active site pocket of CASP3 and CASP7 and obstructs substrate entry. Inactivates CASP9 by keeping it in a monomeric, inactive state. Acts as an E3 ubiquitin-protein ligase regulating NF-kappa-B signaling and the target proteins for its E3 ubiquitin-protein ligase activity include: RIPK1, MAP3K2/MEKK2, DIABLO/SMAC, AIFM1, CCS and BIRC5/survivin. Ubiquitination of CCS leads to enhancement of its chaperone activity toward its physiologic target, SOD1, rather than proteasomal degradation. Ubiquitination of MAP3K2/MEKK2 and AIFM1 does not lead to proteasomal degradation. Plays a role in copper homeostasis by ubiquitinating COMMD1 and promoting its proteasomal degradation. Can also function as E3 ubiquitin-protein ligase of the NEDD8 conjugation pathway, targeting effector caspases for neddylation and inactivation. Ubiquitinates and therefore mediates the proteosomal degradation of BCL2 in response to apoptosis. Regulates the BMP signaling pathway and the SMAD and MAP3K7/TAK1 dependent pathways leading to NF-kappa-B and JNK activation. Acts as an important regulator of innate immune signaling via regulation of Nod-like receptors (NLRs). Protects cells from spontaneous formation of the ripoptosome, a large multi-protein complex that has the capability to kill cancer cells in a caspase-dependent and caspase-independent manner. Suppresses ripoptosome formation by ubiquitinating RIPK1 and CASP8. Acts as a positive regulator of Wnt signaling and ubiquitinates TLE1, TLE2, TLE3, TLE4 and AES. Ubiquitination of TLE3 results in inhibition of its interaction with TCF7L2/TCF4 thereby allowing efficient recruitment and binding of the transcriptional coactivator beta-catenin to TCF7L2/TCF4 that is required to initiate a Wnt-specific transcriptional program.",Increased activation of caspase-3. The absence or presence of these residues may explain the similarities in caspase inhibition observed for different truncated and full-length IAPs.,Increased activation of caspase-3. The absence or presence of these residues may explain the similarities in caspase inhibition observed for different truncated and full-length IAPs.
2800,2800,0,0,O00391-S70C,MRRCNSGSGPPPSLLLLLLWLLAVPGANAAPRSALYSPSDPLTLLQADTVRGAVLGSRSAWAVEFFASWCGHCIAFAPTWKALAEDVKAWRPALYLAALDCAEETNSAVCRDFNIPGFPTVRFFKAFTKNGSGAVFPVAGADVQTLRERLIDALESHHDTWPPACPPLEPAKLEEIDGFFARNNEEYLALIFEKGGSYLGREVALDLSQHKGVAVRRVLNTEANVVRKFGVTDFPSCYLLFRNGSVSRVPVLMESRSFYTAYLQRLSGLTREAAQTTVAPTTANKIAPTVWKLADRSKIYMADLESALHYILRIEVGRFPVLEGQRLVALKKFVAVLAKYFPGRPLVQNFLHSVNEWLKRQKRNKIPYSFFKTALDDRKEGAVLAKKVNWIGCQGSEPHFRGFPCSLWVLFHFLTVQAARQNVDHSQEAAKAKEVLPAIRGYVHYFFGCRDCASHFEQMAAASMHRVGSPNAAVLWLWSSHNRVNARLAGAPSEDPQFPKVQWPPRELCSACHNERLDVPVWDVEATLNFLKAHFSPSNIILDFPAAGSAARRDVQNVAAAPELAMGALELESRNSTLDPGKPEMMKSPTNTTPHVPAEGPEASRPPKLHPGLRAAPGQEPPEHMAELQRNEQEQPLGQWHLSKRDTGAALLAESRAEKNRLWGPLEVRRVGRSSKQLVDIPEGQLEARAGRGRGQWLQVLGGGFSYLDISLCVGLYSLSFMGLLAMYTYFQAKIRALKGHAGHPAA,,-1.0,MRRCNSGSGPPPSLLLLLLWLLAVPGANAAPRSALYSPSDPLTLLQADTVRGAVLGSRSAWAVEFFASWSGHCIAFAPTWKALAEDVKAWRPALYLAALDCAEETNSAVCRDFNIPGFPTVRFFKAFTKNGSGAVFPVAGADVQTLRERLIDALESHHDTWPPACPPLEPAKLEEIDGFFARNNEEYLALIFEKGGSYLGREVALDLSQHKGVAVRRVLNTEANVVRKFGVTDFPSCYLLFRNGSVSRVPVLMESRSFYTAYLQRLSGLTREAAQTTVAPTTANKIAPTVWKLADRSKIYMADLESALHYILRIEVGRFPVLEGQRLVALKKFVAVLAKYFPGRPLVQNFLHSVNEWLKRQKRNKIPYSFFKTALDDRKEGAVLAKKVNWIGCQGSEPHFRGFPCSLWVLFHFLTVQAARQNVDHSQEAAKAKEVLPAIRGYVHYFFGCRDCASHFEQMAAASMHRVGSPNAAVLWLWSSHNRVNARLAGAPSEDPQFPKVQWPPRELCSACHNERLDVPVWDVEATLNFLKAHFSPSNIILDFPAAGSAARRDVQNVAAAPELAMGALELESRNSTLDPGKPEMMKSPTNTTPHVPAEGPEASRPPKLHPGLRAAPGQEPPEHMAELQRNEQEQPLGQWHLSKRDTGAALLAESRAEKNRLWGPLEVRRVGRSSKQLVDIPEGQLEARAGRGRGQWLQVLGGGFSYLDISLCVGLYSLSFMGLLAMYTYFQAKIRALKGHAGHPAA,Sulfhydryl oxidase 1,"Catalyzes the oxidation of sulfhydryl groups in peptide and protein thiols to disulfides with the reduction of oxygen to hydrogen peroxide. Plays a role in disulfide bond formation in a variety of extracellular proteins. In fibroblasts, required for normal incorporation of laminin into the extracellular matrix, and thereby for normal cell-cell adhesion and cell migration.","Increases activity by 93%. The four other cysteine residues chosen for mutagenesis, C70, C73, C449, and C452, are all crucial for inefficient oxidation of reduced RNase.","Increases activity by 93%. The four other cysteine residues chosen for mutagenesis, C70, C73, C449, and C452, are all crucial for inefficient oxidation of reduced RNase."
2803,2803,0,0,Q16584-A277T,MEPLKSLFLKSPLGSWNGSGSGGGGGGGGGRPEGSPKAAGYANPVWTALFDYEPSGQDELALRKGDRVEVLSRDAAISGDEGWWAGQVGGQVGIFPSNYVSRGGGPPPCEVASFQELRLEEVIGIGGFGKVYRGSWRGELVAVKAARQDPDEDISVTAESVRQEARLFAMLAHPNIIALKAVCLEEPNLCLVMEYAAGGPLSRALAGRRVPPHVLVNWAVQIARGMHYLHCEALVPVIHRDLKSNNILLLQPIESDDMEHKTLKITDFGLAREWHKTTQMSAAGTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPYRGIDCLAVAYGVAVNKLTLPIPSTCPEPFAQLMADCWAQDPHRRPDFASILQQLEALEAQVLREMPRDSFHSMQEGWKREIQGLFDELRAKEKELLSREEELTRAAREQRSQAEQLRRREHLLAQWELEVFERELTLLLQQVDRERPHVRRRRGTFKRSKLRARDGGERISMPLDFKHRITVQASPGLDRRRNVFEVGPGDSPTFPRFRAIQLEPAEPGQAWGRQSPRRLEDSSNGERRACWAWGPSSPKPGEAQNGRRRSRMDEATWYLDSDDSSPLGSPSTPPALNGNPPRPSLEPEEPKRPVPAERGSSSGTPKLIQRALLRGTALLASLGLGRDLQPPGGPGRERGESPTTPPTPTPAPCPTEPPPSPLICFSLKTPDSPPTPAPLLLDLGIPVGQRSAKSPRREEEPRGGTVSPPPGTSRSAPGTPGTPRSPPLGLISRPRPSPLRSRIDPWSFVSAGPRPSPLPSPQPAPRRAPWTLFPDSDPFWDSPPANPFQGGPQDCRAQTKDMGAQAPWVPEAGP,,-1.0,MEPLKSLFLKSPLGSWNGSGSGGGGGGGGGRPEGSPKAAGYANPVWTALFDYEPSGQDELALRKGDRVEVLSRDAAISGDEGWWAGQVGGQVGIFPSNYVSRGGGPPPCEVASFQELRLEEVIGIGGFGKVYRGSWRGELVAVKAARQDPDEDISVTAESVRQEARLFAMLAHPNIIALKAVCLEEPNLCLVMEYAAGGPLSRALAGRRVPPHVLVNWAVQIARGMHYLHCEALVPVIHRDLKSNNILLLQPIESDDMEHKTLKITDFGLAREWHKATQMSAAGTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPYRGIDCLAVAYGVAVNKLTLPIPSTCPEPFAQLMADCWAQDPHRRPDFASILQQLEALEAQVLREMPRDSFHSMQEGWKREIQGLFDELRAKEKELLSREEELTRAAREQRSQAEQLRRREHLLAQWELEVFERELTLLLQQVDRERPHVRRRRGTFKRSKLRARDGGERISMPLDFKHRITVQASPGLDRRRNVFEVGPGDSPTFPRFRAIQLEPAEPGQAWGRQSPRRLEDSSNGERRACWAWGPSSPKPGEAQNGRRRSRMDEATWYLDSDDSSPLGSPSTPPALNGNPPRPSLEPEEPKRPVPAERGSSSGTPKLIQRALLRGTALLASLGLGRDLQPPGGPGRERGESPTTPPTPTPAPCPTEPPPSPLICFSLKTPDSPPTPAPLLLDLGIPVGQRSAKSPRREEEPRGGTVSPPPGTSRSAPGTPGTPRSPPLGLISRPRPSPLRSRIDPWSFVSAGPRPSPLPSPQPAPRRAPWTLFPDSDPFWDSPPANPFQGGPQDCRAQTKDMGAQAPWVPEAGP,Mitogen-activated protein kinase kinase kinase 11,"Activates the JUN N-terminal pathway. Required for serum-stimulated cell proliferation and for mitogen and cytokine activation of MAPK14 (p38), MAPK3 (ERK) and MAPK8 (JNK1) through phosphorylation and activation of MAP2K4/MKK4 and MAP2K7/MKK7. Plays a role in mitogen-stimulated phosphorylation and activation of BRAF, but does not phosphorylate BRAF directly. Influences microtubule organization during the cell cycle.",Severely enhanced autophosphorylation activity. Facilitates phosphorylation of SAPK and MAPK14. Mutant displayed almost maximal autophosphorylation activity and was highly functional.,Severely enhanced autophosphorylation activity. Facilitates phosphorylation of SAPK and MAPK14. Mutant displayed almost maximal autophosphorylation activity and was highly functional.
2813,2813,0,0,P08514-S320F,MARALCPLQALWLLEWVLLLLGPCAAPPAWALNLDPVQLTFYAGPNGSQFGFSLDFHKDSHGRVAIVVGAPRTLGPSQEETGGVFLCPWRAEGGQCPSLLFDLRDETRNVGSQTLQTFKARQGLGASVVSWSDVIVACAPWQHWNVLEKTEEAEKTPVGSCFLAQPESGRRAEYSPCRGNTLSRIYVENDFSWDKRYCEAGFSSVVTQAGELVLGAPGGYYFLGLLAQAPVADIFSSYRPGILLWHVSSQSLSFDSSNPEYFDGYWGYSVAVGEFDGDLNTTEYVVGAPTWSWTLGAVEILDSYYQRLHRLRGEQMASYFGHSVAVTDVNGDGRHDLLVGAPLYMESRADRKLAEVGRVYLFLQPRGPHALGAPSLLLTGTQLYGRFGSAIAPLGDLDRDGYNDIAVAAPYGGPSGRGQVLVFLGQSEGLRSRPSQVLDSPFPTGSAFGFSLRGAVDIDDNGYPDLIVGAYGANQVAVYRAQPVVKASVQLLVQDSLNPAVKSCVLPQTKTPVSCFNIQMCVGATGHNIPQKLSLNAELQLDRQKPRQGRRVLLLGSQQAGTTLNLDLGGKHSPICHTTMAFLRDEADFRDKLSPIVLSLNVSLPPTEAGMAPAVVLHGDTHVQEQTRIVLDCGEDDVCVPQLQLTASVTGSPLLVGADNVLELQMDAANEGEGAYEAELAVHLPQGAHYMRALSNVEGFERLICNQKKENETRVVLCELGNPMKKNAQIGIAMLVSVGNLEEAGESVSFQLQIRSKNSQNPNSKIVLLDVPVRAEAQVELRGNSFPASLVVAAEEGEREQNSLDSWGPKVEHTYELHNNGPGTVNGLHLSIHLPGQSQPSDLLYILDIQPQGGLQCFPQPPVNPLKVDWGLPIPSPSPIHPAHHKRDRRQIFLPEPEQPSRLQDPVLVSCDSAPCTVVQCDLQEMARGQRAMVTVLAFLWLPSLYQRPLDQFVLQSHAWFNVSSLPYAVPPLSLPRGEAQVWTQLLRALEERAIPIWWVLVGVLGGLLLLTILVLAMWKVGFF,,-1.0,MARALCPLQALWLLEWVLLLLGPCAAPPAWALNLDPVQLTFYAGPNGSQFGFSLDFHKDSHGRVAIVVGAPRTLGPSQEETGGVFLCPWRAEGGQCPSLLFDLRDETRNVGSQTLQTFKARQGLGASVVSWSDVIVACAPWQHWNVLEKTEEAEKTPVGSCFLAQPESGRRAEYSPCRGNTLSRIYVENDFSWDKRYCEAGFSSVVTQAGELVLGAPGGYYFLGLLAQAPVADIFSSYRPGILLWHVSSQSLSFDSSNPEYFDGYWGYSVAVGEFDGDLNTTEYVVGAPTWSWTLGAVEILDSYYQRLHRLRGEQMASYSGHSVAVTDVNGDGRHDLLVGAPLYMESRADRKLAEVGRVYLFLQPRGPHALGAPSLLLTGTQLYGRFGSAIAPLGDLDRDGYNDIAVAAPYGGPSGRGQVLVFLGQSEGLRSRPSQVLDSPFPTGSAFGFSLRGAVDIDDNGYPDLIVGAYGANQVAVYRAQPVVKASVQLLVQDSLNPAVKSCVLPQTKTPVSCFNIQMCVGATGHNIPQKLSLNAELQLDRQKPRQGRRVLLLGSQQAGTTLNLDLGGKHSPICHTTMAFLRDEADFRDKLSPIVLSLNVSLPPTEAGMAPAVVLHGDTHVQEQTRIVLDCGEDDVCVPQLQLTASVTGSPLLVGADNVLELQMDAANEGEGAYEAELAVHLPQGAHYMRALSNVEGFERLICNQKKENETRVVLCELGNPMKKNAQIGIAMLVSVGNLEEAGESVSFQLQIRSKNSQNPNSKIVLLDVPVRAEAQVELRGNSFPASLVVAAEEGEREQNSLDSWGPKVEHTYELHNNGPGTVNGLHLSIHLPGQSQPSDLLYILDIQPQGGLQCFPQPPVNPLKVDWGLPIPSPSPIHPAHHKRDRRQIFLPEPEQPSRLQDPVLVSCDSAPCTVVQCDLQEMARGQRAMVTVLAFLWLPSLYQRPLDQFVLQSHAWFNVSSLPYAVPPLSLPRGEAQVWTQLLRALEERAIPIWWVLVGVLGGLLLLTILVLAMWKVGFF,Integrin alpha-IIb,"Integrin alpha-IIb/beta-3 is a receptor for fibronectin, fibrinogen, plasminogen, prothrombin, thrombospondin and vitronectin. It recognizes the sequence R-G-D in a wide array of ligands. It recognizes the sequence H-H-L-G-G-G-A-K-Q-A-G-D-V in fibrinogen gamma chain. Following activation integrin alpha-IIb/beta-3 brings about platelet/platelet interaction through binding of soluble fibrinogen. This step leads to rapid platelet aggregation which physically plugs ruptured endothelial cell surface.",Impairs surface expression of alpha-IIb/beta-3. One patient with type I GT had a T to C base substitution in exon 11 resulting in a F (TTT)-289 to S (TCT) mutation () of the subunit.,Impairs surface expression of alpha-IIb/beta-3. One patient with type I GT had a T to C base substitution in exon 11 resulting in a F (TTT)-289 to S (TCT) mutation () of the subunit.
2842,2842,0,0,A1C3L3-A470L,MGKYKRAGETSRKTRVKMHKSGKNWVRTLISQIGLMHFLGGSISEKKINVDVYEQKNISASTILKGAVALGALTGATVVSGNVFADETVLAKETTLTTTDANEVKLSSENFDSEKAEEKISLSQSESASESVSESISESVSESVSTSESVSESVSESVSESISESVSESISESISESVSESTSTSIVLSESGAASGNKATSKGTEEKQDSVRENLDKMISEAEVLNDMAARKLITLDAEQQLELMKSLVATQSQLEATKNLIGDPNATVADLQIAYTTLGNNTQALGNELIKLNPNGQIYAVLNNTEASRAATLRSTTTGTKTTFTISDFSNGGTQYYWAGGNANNLKNPISSISAVYDSATGKISWTVEYDPTTILKSPALKTLKTYTGIYIDTSSDSKLSTPTNVLIDGAATNPVTNFYGNGSKGIEYVSKGTTKGVTKHTITFDTAFSGRANDLADLKIKMLAATTLSDPHFYEDGSKGNYGRYNGQTAPYVIANDSGTAIGGYQVSGVNADSIPSDTTSQSESTSKSESTSKSISESVIESISESVIGSVSESVSESVSESVSESITESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESISESVSESVSESVSESVSESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESVSE,,-1.0,MGKYKRAGETSRKTRVKMHKSGKNWVRTLISQIGLMHFLGGSISEKKINVDVYEQKNISASTILKGAVALGALTGATVVSGNVFADETVLAKETTLTTTDANEVKLSSENFDSEKAEEKISLSQSESASESVSESISESVSESVSTSESVSESVSESVSESISESVSESISESISESVSESTSTSIVLSESGAASGNKATSKGTEEKQDSVRENLDKMISEAEVLNDMAARKLITLDAEQQLELMKSLVATQSQLEATKNLIGDPNATVADLQIAYTTLGNNTQALGNELIKLNPNGQIYAVLNNTEASRAATLRSTTTGTKTTFTISDFSNGGTQYYWAGGNANNLKNPISSISAVYDSATGKISWTVEYDPTTILKSPALKTLKTYTGIYIDTSSDSKLSTPTNVLIDGAATNPVTNFYGNGSKGIEYVSKGTTKGVTKHTITFDTAFSGRANDLADLKIKMLAATTASDPHFYEDGSKGNYGRYNGQTAPYVIANDSGTAIGGYQVSGVNADSIPSDTTSQSESTSKSESTSKSISESVIESISESVIGSVSESVSESVSESVSESITESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESISESVSESVSESVSESVSESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESVSE,Fap1 adhesin,"The major structural element of fimbriae. Required for adherence to saliva-coated hydroxyapatite beads (SHA), an in vitro tooth model. A Fap1-dependent increase in adherence is seen as the pH is reduced from pH 8 to pH 5.",Gain of adherence to SHA.,Gain of adherence to SHA.
2847,2847,0,0,Q9NDH7-R116L,MRRRHRCVALLFIFSAFITPLGFFYYTISNESKRYSEESEKNYGYQTLEFTESPEEISVDFDKYSQSECSRFPSNVEIEYPECLNKMKWIKNGWKTHHCYIENHIDGSECSFRYYLSQVENYCPPMEHHGKRKGLAKISPSIRRLLPIFESIPHYMKTRINRLWKKWKEGAHEVMQKYPKSMIERRKLNVLVFIGFLANEQKLNMAKKSDHGGPLGELLQWSDLLATLSVIGHHLEVSTNKNTLRNIVWKYMSRGPCQYVNNFRQQLDIIFTDIMGFNILRQHHRQFLLSNRCRIRLLDSFGTHAEFTTKTYFVQNKKSLSGPFSQRNPWGGHGLDLRQHWTFYPHSDDNTFLGFVVDTEGIDKKNNQMIPSALVYGKEQYMWRDAEKPIDVLKRIVTVHSTVADLDLKDSNISSIFKKVQNHGFLNSEEISQLLDNITIFFGLGFPLEGPAPLEAMAHGAVFINAKFKEPKSRLNYKFLAEKPTLRKWTSQNPYMEKIGEPHVITVDIFNELELEEAIKRAISLKPKHFVPFEFTPAGMLHRVALLLEKQELCDKIAYSKRWPPIDQMKIFRTLNADDSCETICHSKQLLCEPSYFPIINSSPLLRRENLCSSTTSDSSPFAPFNCTIQQSAFLFSCASSPPISFEINRLCPCRDYIPEQHAICKKCL,,-1.0,MRRRHRCVALLFIFSAFITPLGFFYYTISNESKRYSEESEKNYGYQTLEFTESPEEISVDFDKYSQSECSRFPSNVEIEYPECLNKMKWIKNGWKTHHCYIENHIDGSECSFRYYRSQVENYCPPMEHHGKRKGLAKISPSIRRLLPIFESIPHYMKTRINRLWKKWKEGAHEVMQKYPKSMIERRKLNVLVFIGFLANEQKLNMAKKSDHGGPLGELLQWSDLLATLSVIGHHLEVSTNKNTLRNIVWKYMSRGPCQYVNNFRQQLDIIFTDIMGFNILRQHHRQFLLSNRCRIRLLDSFGTHAEFTTKTYFVQNKKSLSGPFSQRNPWGGHGLDLRQHWTFYPHSDDNTFLGFVVDTEGIDKKNNQMIPSALVYGKEQYMWRDAEKPIDVLKRIVTVHSTVADLDLKDSNISSIFKKVQNHGFLNSEEISQLLDNITIFFGLGFPLEGPAPLEAMAHGAVFINAKFKEPKSRLNYKFLAEKPTLRKWTSQNPYMEKIGEPHVITVDIFNELELEEAIKRAISLKPKHFVPFEFTPAGMLHRVALLLEKQELCDKIAYSKRWPPIDQMKIFRTLNADDSCETICHSKQLLCEPSYFPIINSSPLLRRENLCSSTTSDSSPFAPFNCTIQQSAFLFSCASSPPISFEINRLCPCRDYIPEQHAICKKCL,"Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase",Catalyzes the addition of N-acetylglucosamine (GlcNAc) in beta 1-6 linkage to the alpha-linked mannose of biantennary N-linked oligosaccharides.,"Highly enhances function. GLY-2(), an equivalent mutation to that which causes the Lec4A phenotype, could complement the Phaseolus vulgaris leucoagglutinin binding defect of Chinese hamster ovary Lec4 cells.","Highly enhances function. GLY-2(), an equivalent mutation to that which causes the Lec4A phenotype, could complement the Phaseolus vulgaris leucoagglutinin binding defect of Chinese hamster ovary Lec4 cells."
2877,2877,0,0,Q95ZV7-A100R,MKLLLYLFGVTFHSNTVVALELRECSHQLGMSNRKIRDEQISASSSFDLQSTGPQHARAHQESGSGAWCPKNQINSLSKEWLQISFSVDTVITSVETQGRFDDGRGMEYATAFKIQYWRPSLNAWASYKDDFELETIPANNDTEHAIRRHLDRAIIARRIRIVPVSNSTRTVCMRVEVFGCPFDDSLVFYNVDQGDLQSGISYHDFSYDGNLANSPHLTGGIGKLYDGEVGKNNVFVNHHKWVGWRRKRNGNVKLAFEFSELRNISGILIHTSNEFKKSAKAFSSATVLFSINGKDFSDTIVHFNNPEDTESEVPRWIRIPVNNRIAKVAKIRLNFGTDSDWLFISEVNFESNHTNIELLNDDVVIPDSVSYFSVTEHDDGTSMFAFIIFFFMFLIVAVIILTVLYRKREYRVKASSPSPNAKREILLTIDGNTIKHHVSPSTYQMARDNLQNALIEKMPMSPIISDYAEPDISVCSDVTANTPLLYGIDGPYDTQKRSNPLSSMVKYSDYGEVYCTTLPEIARDKLICVSRIGQGEFGEVDLCQLENRKVAVKKLHGISQADEFSFHREIRVLGSLKHPNVVEVVGVCTIQKPILCIMEYMENGDLKSYILKNPTIQTSQCISICTQLAAGLAYLESCNFVHRDIAARNCLVDGEGNVKIADFGMARSLYSQEYYKVEGKFVLPIRWMAWEALLLGKFSTASDVWGFGVTMWEIFSLCSEKPYSDMTDDDVVENLQSMSSTGSLKQVLSRPRMCPSKLYNEQILPCWNYESSRRPSFENVHLHLQSLVHTSPHIHF,,-1.0,MKLLLYLFGVTFHSNTVVALELRECSHQLGMSNRKIRDEQISASSSFDLQSTGPQHARAHQESGSGAWCPKNQINSLSKEWLQISFSVDTVITSVETQGAFDDGRGMEYATAFKIQYWRPSLNAWASYKDDFELETIPANNDTEHAIRRHLDRAIIARRIRIVPVSNSTRTVCMRVEVFGCPFDDSLVFYNVDQGDLQSGISYHDFSYDGNLANSPHLTGGIGKLYDGEVGKNNVFVNHHKWVGWRRKRNGNVKLAFEFSELRNISGILIHTSNEFKKSAKAFSSATVLFSINGKDFSDTIVHFNNPEDTESEVPRWIRIPVNNRIAKVAKIRLNFGTDSDWLFISEVNFESNHTNIELLNDDVVIPDSVSYFSVTEHDDGTSMFAFIIFFFMFLIVAVIILTVLYRKREYRVKASSPSPNAKREILLTIDGNTIKHHVSPSTYQMARDNLQNALIEKMPMSPIISDYAEPDISVCSDVTANTPLLYGIDGPYDTQKRSNPLSSMVKYSDYGEVYCTTLPEIARDKLICVSRIGQGEFGEVDLCQLENRKVAVKKLHGISQADEFSFHREIRVLGSLKHPNVVEVVGVCTIQKPILCIMEYMENGDLKSYILKNPTIQTSQCISICTQLAAGLAYLESCNFVHRDIAARNCLVDGEGNVKIADFGMARSLYSQEYYKVEGKFVLPIRWMAWEALLLGKFSTASDVWGFGVTMWEIFSLCSEKPYSDMTDDDVVENLQSMSSTGSLKQVLSRPRMCPSKLYNEQILPCWNYESSRRPSFENVHLHLQSLVHTSPHIHF,Discoidin domain-containing receptor tyrosine kinase B,"Tyrosine-protein kinase receptor which, together with ddr-1, is involved in axon guidance to establish the tracts for the ventral and dorsal nerve cords during nervous system development. Acts upstream of the adapter shc-1, and the tyrosine kinase receptors svh-1 and svh-2 to regulate axon regeneration following injury in D-type motor neurons. May mediate axon regeneration in association with the collagen emb-9.",Rescues the axon regeneration defect in the svh-4 loss of function mutant (ok564) following injury to D-type motor neurons.,Rescues the axon regeneration defect in the svh-4 loss of function mutant (ok564) following injury to D-type motor neurons.
2879,2879,0,0,P29317-I940T,MELQAARACFALLWGCALAAAAAAQGKEVVLLDFAAAGGELGWLTHPYGKGWDLMQNIMNDMPIYMYSVCNVMSGDQDNWLRTNWVYRGEAERIFIELKFTVRDCNSFPGGASSCKETFNLYYAESDLDYGTNFQKRLFTKIDTIAPDEITVSSDFEARHVKLNVEERSVGPLTRKGFYLAFQDIGACVALLSVRVYYKKCPELLQGLAHFPETIAGSDAPSLATVAGTCVDHAVVPPGGEEPRMHCAVDGEWLVPIGQCLCQAGYEKVEDACQACSPGFFKFEASESPCLECPEHTLPSPEGATSCECEEGFFRAPQDPASMPCTRPPSAPHYLTAVGMGAKVELRWTPPQDSGGREDIVYSVTCEQCWPESGECGPCEASVRYSEPPHGLTRTSVTVSDLEPHMNYTFTVEARNGVSGLVTSRSFRTASVSINQTEPPKVRLEGRSTTSLSVSWSIPPPQQSRVWKYEVTYRKKGDSNSYNVRRTEGFSVTLDDLAPDTTYLVQVQALTQEGQGAGSKVHEFQTLSPEGSGNLAVIGGVAVGVVLLLVLAGVGFFIHRRRKNQRARQSPEDVYFSKSEQLKPLKTYVDPHTYEDPNQAVLKFTTEIHPSCVTRQKVIGAGEFGEVYKGMLKTSSGKKEVPVAIKTLKAGYTEKQRVDFLGEAGIMGQFSHHNIIRLEGVISKYKPMMIITEYMENGALDKFLREKDGEFSVLQLVGMLRGIAAGMKYLANMNYVHRDLAARNILVNSNLVCKVSDFGLSRVLEDDPEATYTTSGGKIPIRWTAPEAISYRKFTSASDVWSFGIVMWEVMTYGERPYWELSNHEVMKAINDGFRLPTPMDCPSAIYQLMMQCWQQERARRPKFADIVSILDKLIRAPDSLKTLADFDPRVSIRLPSTSGSEGVPFRTVSEWLESIKMQQYTEHFMAAGYTAIEKVVQMTNDDIKRIGVRLPGHQKRIAYSLLGLKDQVNTVGIPI,,-1.0,MELQAARACFALLWGCALAAAAAAQGKEVVLLDFAAAGGELGWLTHPYGKGWDLMQNIMNDMPIYMYSVCNVMSGDQDNWLRTNWVYRGEAERIFIELKFTVRDCNSFPGGASSCKETFNLYYAESDLDYGTNFQKRLFTKIDTIAPDEITVSSDFEARHVKLNVEERSVGPLTRKGFYLAFQDIGACVALLSVRVYYKKCPELLQGLAHFPETIAGSDAPSLATVAGTCVDHAVVPPGGEEPRMHCAVDGEWLVPIGQCLCQAGYEKVEDACQACSPGFFKFEASESPCLECPEHTLPSPEGATSCECEEGFFRAPQDPASMPCTRPPSAPHYLTAVGMGAKVELRWTPPQDSGGREDIVYSVTCEQCWPESGECGPCEASVRYSEPPHGLTRTSVTVSDLEPHMNYTFTVEARNGVSGLVTSRSFRTASVSINQTEPPKVRLEGRSTTSLSVSWSIPPPQQSRVWKYEVTYRKKGDSNSYNVRRTEGFSVTLDDLAPDTTYLVQVQALTQEGQGAGSKVHEFQTLSPEGSGNLAVIGGVAVGVVLLLVLAGVGFFIHRRRKNQRARQSPEDVYFSKSEQLKPLKTYVDPHTYEDPNQAVLKFTTEIHPSCVTRQKVIGAGEFGEVYKGMLKTSSGKKEVPVAIKTLKAGYTEKQRVDFLGEAGIMGQFSHHNIIRLEGVISKYKPMMIITEYMENGALDKFLREKDGEFSVLQLVGMLRGIAAGMKYLANMNYVHRDLAARNILVNSNLVCKVSDFGLSRVLEDDPEATYTTSGGKIPIRWTAPEAISYRKFTSASDVWSFGIVMWEVMTYGERPYWELSNHEVMKAINDGFRLPTPMDCPSAIYQLMMQCWQQERARRPKFADIVSILDKLIRAPDSLKTLADFDPRVSIRLPSTSGSEGVPFRTVSEWLESIKMQQYTEHFMAAGYTAIEKVVQMINDDIKRIGVRLPGHQKRIAYSLLGLKDQVNTVGIPI,Ephrin type-A receptor 2,"Receptor tyrosine kinase which binds promiscuously membrane-bound ephrin-A family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Activated by the ligand ephrin-A1/EFNA1 regulates migration, integrin-mediated adhesion, proliferation and differentiation of cells. Regulates cell adhesion and differentiation through DSG1/desmoglein-1 and inhibition of the ERK1/ERK2 (MAPK3/MAPK1, respectively) signaling pathway. May also participate in UV radiation-induced apoptosis and have a ligand-independent stimulatory effect on chemotactic cell migration. During development, may function in distinctive aspects of pattern formation and subsequently in development of several fetal tissues. Involved for instance in angiogenesis, in early hindbrain development and epithelial proliferation and branching morphogenesis during mammary gland development. Engaged by the ligand ephrin-A5/EFNA5 may regulate lens fiber cells shape and interactions and be important for lens transparency development and maintenance. With ephrin-A2/EFNA2 may play a role in bone remodeling through regulation of osteoclastogenesis and osteoblastogenesis.(Microbial infection) Acts as a receptor for hepatitis C virus (HCV) in hepatocytes and facilitates its cell entry. Mediates HCV entry by promoting the formation of the CD81-CLDN1 receptor complexes that are essential for HCV entry and by enhancing membrane fusion of cells expressing HCV envelope glycoproteins.",Increases protein stability and enhances ability to stimulate cell migration in absence of its ephrin ligand. The missense mutation c. 2819C>T (p. ) in the EPHA2 gene replaces a critical amino acid that functions at the receptor oligomerization interface. This mutation is associated with posterior polar congenital cataract in a Chinese family. The mutation in the SAM domain of EPHA2 enhances its activity and promotes cell migration upon ligand stimulation.,Increases protein stability and enhances ability to stimulate cell migration in absence of its ephrin ligand. The missense mutation c. 2819C>T (p. ) in the EPHA2 gene replaces a critical amino acid that functions at the receptor oligomerization interface. This mutation is associated with posterior polar congenital cataract in a Chinese family. The mutation in the SAM domain of EPHA2 enhances its activity and promotes cell migration upon ligand stimulation.
2886,2886,0,0,P03950-A36Q,MVMGLGVLLLVFVLGLGLTPPTLAQDNSRYTHFLTQHYDAKPQGRDDRYCESIMRRRGLTSPCKDINTFIHGNKRSIKAICENKNGNPHRENLRISKSSFQVTTCKLHGGSPWPPCQYRATAGFRNVVVACENGLPVHLDQSIFRRP,,-1.0,MVMGLGVLLLVFVLGLGLTPPTLAQDNSRYTHFLTAHYDAKPQGRDDRYCESIMRRRGLTSPCKDINTFIHGNKRSIKAICENKNGNPHRENLRISKSSFQVTTCKLHGGSPWPPCQYRATAGFRNVVVACENGLPVHLDQSIFRRP,Angiogenin,"Ribonuclease that cleaves tRNA within anticodon loops to produce tRNA-derived stress-induced fragments (tiRNAs) which inhibit protein synthesis and triggers the assembly of stress granules (SGs). Binds to actin on the surface of endothelial cells; once bound, angiogenin is endocytosed and translocated to the nucleus. Stimulates ribosomal RNA synthesis including that containing the initiation site sequences of 45S rRNA. Angiogenin induces vascularization of normal and malignant tissues. Angiogenic activity is regulated by interaction with RNH1 in vivo.",Slightly increases binding affinity for RNH1.,Slightly increases binding affinity for RNH1.
2889,2889,0,0,Q6ZT98-E227R,MPSLPQEGVIQGPSPLDLNTELPYQSTMKRKVRKKKKKGTITANVAGTKFEIVRLVIDEMGFMKTPDEDETSNLIWCDSAVQQEKISELQNYQRINHFPGMGEICRKDFLARNMTKMIKSRPLDYTFVPRTWIFPAEYTQFQNYVKELKKKRKQKTFIVKPANGAMGHGISLIRNGDKLPSQDHLIVQEYIEKPFLMEGYKFDLRIYILVTSCDPLKIFLYHDGLVRMGTEKYIPPNESNLTQLYMHLTNYSVNKHNEHFERDETENKGSKRSIKWFTEFLQANQHDVAKFWSDISELVVKTLIVAEPHVLHAYRMCRPGQPPGSESVCFEVLGFDILLDRKLKPWLLEINRAPSFGTDQKIDYDVKRGVLLNALKLLNIRTSDKRRNLAKQKAEAQRRLYGQNSIKRLLPGSSDWEQQRHQLERRKEELKERLAQVRKQISREEHENRHMGNYRRIYPPEDKALLEKYENLLAVAFQTFLSGRAASFQRELNNPLKRMKEEDILDLLEQCEIDDEKLMGKTTKTRGPKPLCSMPESTEIMKRPKYCSSDSSYDSSSSSSESDENEKEEYQNKKREKQVTYNLKPSNHYKLIQQPSSIRRSVSCPRSISAQSPSSGDTRPFSAQQMISVSRPTSASRSHSLNRASSYMRHLPHSNDACSTNSQVSESLRQLKTKEQEDDLTSQTLFVLKDMKIRFPGKSDAESELLIEDIIDNWKYHKTKVASYWLIKLDSVKQRKVLDIVKTSIRTVLPRIWKVPDVEEVNLYRIFNRVFNRLLWSRGQGLWNCFCDSGSSWESIFNKSPEVVTPLQLQCCQRLVELCKQCLLVVYKYATDKRGSLSGIGPDWGNSRYLLPGSTQFFLRTPTYNLKYNSPGMTRSNVLFTSRYGHL,,-1.0,MPSLPQEGVIQGPSPLDLNTELPYQSTMKRKVRKKKKKGTITANVAGTKFEIVRLVIDEMGFMKTPDEDETSNLIWCDSAVQQEKISELQNYQRINHFPGMGEICRKDFLARNMTKMIKSRPLDYTFVPRTWIFPAEYTQFQNYVKELKKKRKQKTFIVKPANGAMGHGISLIRNGDKLPSQDHLIVQEYIEKPFLMEGYKFDLRIYILVTSCDPLKIFLYHDGLVEMGTEKYIPPNESNLTQLYMHLTNYSVNKHNEHFERDETENKGSKRSIKWFTEFLQANQHDVAKFWSDISELVVKTLIVAEPHVLHAYRMCRPGQPPGSESVCFEVLGFDILLDRKLKPWLLEINRAPSFGTDQKIDYDVKRGVLLNALKLLNIRTSDKRRNLAKQKAEAQRRLYGQNSIKRLLPGSSDWEQQRHQLERRKEELKERLAQVRKQISREEHENRHMGNYRRIYPPEDKALLEKYENLLAVAFQTFLSGRAASFQRELNNPLKRMKEEDILDLLEQCEIDDEKLMGKTTKTRGPKPLCSMPESTEIMKRPKYCSSDSSYDSSSSSSESDENEKEEYQNKKREKQVTYNLKPSNHYKLIQQPSSIRRSVSCPRSISAQSPSSGDTRPFSAQQMISVSRPTSASRSHSLNRASSYMRHLPHSNDACSTNSQVSESLRQLKTKEQEDDLTSQTLFVLKDMKIRFPGKSDAESELLIEDIIDNWKYHKTKVASYWLIKLDSVKQRKVLDIVKTSIRTVLPRIWKVPDVEEVNLYRIFNRVFNRLLWSRGQGLWNCFCDSGSSWESIFNKSPEVVTPLQLQCCQRLVELCKQCLLVVYKYATDKRGSLSGIGPDWGNSRYLLPGSTQFFLRTPTYNLKYNSPGMTRSNVLFTSRYGHL,Tubulin polyglutamylase TTLL7,"Polyglutamylase which modifies tubulin, generating polyglutamate side chains of variable lengths on the gamma-carboxyl group of specific glutamate residues within the C-terminal tail of tubulin. Mediates both ATP-dependent initiation and elongation steps of the polyglutamylation reaction. Preferentially modifies the beta-tubulin tail over an alpha-tail. Competes with monoglycylase TTLL3 for modification site on beta-tubulin substrate, thereby creating an anticorrelation between glycylation and glutamylation reactions. Required for neurite growth; responsible for the strong increase in tubulin polyglutamylation during postnatal neuronal maturation.",Nearly enhanced polyglutamylase activity.,Nearly enhanced polyglutamylase activity.
2898,2898,0,0,P0C871-N49R,MQAKVPETCLLTVRVLRASGLPSKDLVTSSDCYVTLNLPTASSHTLQTRTVKNSRNPVWNQNFHFRIHRQLKNVMELKVFDHDLVTRDDPVLSVLFDVGTLQIGTQRQSFSLGTQEKGCLEVEFRLQTLTDCEEQLISNGIVVARELSCLHVELKRTGDPKRSERKVQLVVAGACEGPQDASAGTGSFHFHYPACWEQELNVHLQDDPHEQLKVPLRTLPSSQLVRLVFPTSQEPLMRLELKKEEGPKELAVRLGCGPCPEEQAFLSKRKQVVAAALKKALQLDQDLHEDEIPVIAVMATGGGIRAMTSLYGQLAGLQELGLLDCISYITGASGSTWALANLYEDPEWSQKDLAGPTEVLKTQVTKSKLGALAPSQLWRYRQELAERARLGHPTCFTNLWALINEALLHDKPHEHKLSDQREALSRGQNPLPIYCALNSKEQGLSTFDFGEWCEFSPYEVGFPKYGAFISSELFGSEFFMGRLVKQLPESRICFLEGIWSNLFAASLQDSLYWSSEPSQFWDRWAQDQANLDKEQVPHLKIAEPPTMAGRIAELFTDLLTKRPLAHATHNFTRGLHFHKDYFQNSHFSAWKASKLDRLPNQLTPTEPHLCLLDVGYLINTSCPPLLQPTRDVDLILSLDYNLYGAFQQLQLLSRFCQEQGIPFPSISPSPEEQRQPQECHLFCDPAQPEAPAVLHFPLVNDSFQDYSAPGVPRTSEEKAAGEVNLSSSDSPYHYTKVTYSQEDVDKLLRLTHYNICNNQDRLREAMHQAVQRRRKRKQFRPE,,-1.0,MQAKVPETCLLTVRVLRASGLPSKDLVTSSDCYVTLNLPTASSHTLQTNTVKNSRNPVWNQNFHFRIHRQLKNVMELKVFDHDLVTRDDPVLSVLFDVGTLQIGTQRQSFSLGTQEKGCLEVEFRLQTLTDCEEQLISNGIVVARELSCLHVELKRTGDPKRSERKVQLVVAGACEGPQDASAGTGSFHFHYPACWEQELNVHLQDDPHEQLKVPLRTLPSSQLVRLVFPTSQEPLMRLELKKEEGPKELAVRLGCGPCPEEQAFLSKRKQVVAAALKKALQLDQDLHEDEIPVIAVMATGGGIRAMTSLYGQLAGLQELGLLDCISYITGASGSTWALANLYEDPEWSQKDLAGPTEVLKTQVTKSKLGALAPSQLWRYRQELAERARLGHPTCFTNLWALINEALLHDKPHEHKLSDQREALSRGQNPLPIYCALNSKEQGLSTFDFGEWCEFSPYEVGFPKYGAFISSELFGSEFFMGRLVKQLPESRICFLEGIWSNLFAASLQDSLYWSSEPSQFWDRWAQDQANLDKEQVPHLKIAEPPTMAGRIAELFTDLLTKRPLAHATHNFTRGLHFHKDYFQNSHFSAWKASKLDRLPNQLTPTEPHLCLLDVGYLINTSCPPLLQPTRDVDLILSLDYNLYGAFQQLQLLSRFCQEQGIPFPSISPSPEEQRQPQECHLFCDPAQPEAPAVLHFPLVNDSFQDYSAPGVPRTSEEKAAGEVNLSSSDSPYHYTKVTYSQEDVDKLLRLTHYNICNNQDRLREAMHQAVQRRRKRKQFRPE,Cytosolic phospholipase A2 beta,"Calcium-dependent phospholipase A1 and A2 and lysophospholipase that may play a role in membrane phospholipid remodeling. Cleaves the ester bond of the fatty acyl group attached to the sn-1 or sn-2 position of phospholipids (phospholipase A1 and A2 activity, respectively), producing lysophospholipids that may be used in deacylation-reacylation cycles. The PLA1 versus PLA2 activity ratio appears to depend on the phospholipid headgroup, with mainly PLA2 activity toward anionic phospholipids such as phosphatidylglycerols. Hydrolyzes with high efficiency lysophospholipids enabling complete deacylation.",Enhances calcium-dependent binding to phospholipids; when associated with N-24 and N-52.,Enhances calcium-dependent binding to phospholipids; when associated with N-24 and N-52.
2911,2911,0,0,Q13510-N162D,MPGRSCVALVLLAAAVSCAVAQHAPPWTEDCRKSTYPPSGPTYRGAVPWYTINLDLPPYKRWHELMLDKAPVLKVIVNSLKNMINTFVPSGKIMQVVDEKLPGLLGNFPGPFEEEMKGIAAVTDIPLGEIISFNIFYELFTICTSIVAEDKKGHLIHGRNMDFGVFLGWNINNDTWVITEQLKPLTVNLDFQRNNKTVFKASSFAGYVGMLTGFKPGLFSLTLNERFSINGGYLGILEWILGKKDVMWIGFLTRTVLENSTSYEEAKNLLTKTKILAPAYFILGGNQSGEGCVITRDRKESLDVYELDAKQGRWYVVQTNYDRWKHPFFLDDRRTPAKMCLNRTSQENISFETMYDVLSTKPVLNKLTVYTTLIDVTKGQFETYLRDCPDPCIGW,,-1.0,MPGRSCVALVLLAAAVSCAVAQHAPPWTEDCRKSTYPPSGPTYRGAVPWYTINLDLPPYKRWHELMLDKAPVLKVIVNSLKNMINTFVPSGKIMQVVDEKLPGLLGNFPGPFEEEMKGIAAVTDIPLGEIISFNIFYELFTICTSIVAEDKKGHLIHGRNMNFGVFLGWNINNDTWVITEQLKPLTVNLDFQRNNKTVFKASSFAGYVGMLTGFKPGLFSLTLNERFSINGGYLGILEWILGKKDVMWIGFLTRTVLENSTSYEEAKNLLTKTKILAPAYFILGGNQSGEGCVITRDRKESLDVYELDAKQGRWYVVQTNYDRWKHPFFLDDRRTPAKMCLNRTSQENISFETMYDVLSTKPVLNKLTVYTTLIDVTKGQFETYLRDCPDPCIGW,Acid ceramidase,"Lysosomal ceramidase that hydrolyzes sphingolipid ceramides into sphingosine and free fatty acids at acidic pH. Ceramides, sphingosine, and its phosphorylated form sphingosine-1-phosphate are bioactive lipids that mediate cellular signaling pathways regulating several biological processes including cell proliferation, apoptosis and differentiation. Has a higher catalytic efficiency towards C12-ceramides versus other ceramides. Also catalyzes the reverse reaction allowing the synthesis of ceramides from fatty acids and sphingosine. For the reverse synthetic reaction, the natural sphingosine D-erythro isomer is more efficiently utilized as a substrate compared to D-erythro-dihydrosphingosine and D-erythro-phytosphingosine, while the fatty acids with chain lengths of 12 or 14 carbons are the most efficiently used. Has also an N-acylethanolamine hydrolase activity. By regulating the levels of ceramides, sphingosine and sphingosine-1-phosphate in the epidermis, mediates the calcium-induced differentiation of epidermal keratinocytes. Also indirectly regulates tumor necrosis factor/TNF-induced apoptosis. By regulating the intracellular balance between ceramides and sphingosine, in adrenocortical cells, probably also acts as a regulator of steroidogenesis.May directly regulate steroidogenesis by binding the nuclear receptor NR5A1 and negatively regulating its transcriptional activity.",Strongly increased autocatalytic processing. Strongly increased ceramidase activity. The mutation stabilizes the protein fold.,Strongly increased autocatalytic processing. Strongly increased ceramidase activity. The mutation stabilizes the protein fold.
2923,2923,0,0,Q4VGL6-A259K,MPVQAPQWTDFLSCPICTQTFDETIRKPISLGCGHTVCKMCLNKLHRKACPFDQTTINTDIELLPVNSALLQLVGAQIPEQQPITLCSGVEDTKHYEEAKKCVEELALYLKPLSSARGVGLNSTTQSVLSRPMQRKLVTLVHCQLVEEEGRIRAMRAARSLGERTVTELILQHQNPQQLSSNLWAAVRARGCQFLGPAMQEEALKLVLLALEDGSALSRKVLVLFVVQRLEPRFPQASKTSIGHVVQLLYRASCFKVTKRDEDSSLMQLKEEFRTYEALRREHDSQIVQIAMEAGLRIAPDQWSSLLYGDQSHKSHMQSIIDKLQTPASFAQSVQELTIALQRTGDPANLNRLRPHLELLANIDPSPDAPPPTWEQLENGLVAVRTVVHGLVDYIQNHSKKGADQQQPPQHSKYKTYMCRDMKQRGGCPRGASCTFAHSQEELEKFRKMNKRLVPRRPLSASLGQLNEVGLPSAPILSDESAVDLSNRKPPALPNGIASSGSTVTQLIPRGTDPSFDSSLKPVKLDHLSSSAPGSPPDLLESAPKSISALPVNPHPVPPRGPTDLPPMPVTKPIQMVPRGSQLYPAQQADVYYQDPRGSAPAFETAPYQQGMYYTPPPCVSRFVRPPPSAPEPGPPYLDHYSPYLQDRVINSQYGTQPQQYPPMYPAHYDGRRVYPAQSYTREEMFRESPIPIDIPSAAVPSYVPESRERYQQVEGYYPVAPHPAQIRPSYPRDPPYSRLPPPQPHPSLDELHRRRKEIMAQLEERKVISPPPFAPSPTLPPAFHPEEFLDEDLKVAGKYKANDYSQYSPWSCDTIGSYIGTKDAKPKDVVAAGSVEMMNVESKGTREQRLDLQRRAVETSDDDLIPFGDRPTVSRFGAISRTSKTLYQGAGPLQAIAPQGAPTKSINISDYSAYGAHGGWGDSPYSPHANIPPQGHFIEREKMSMAEVASHGKPLLSAEREQLRLELQQLNHQISQQTQLRGLEAVSNRLVLQREVNTLASQPQPPQLPPKWPGMISSEQLSL,,-1.0,MPVQAPQWTDFLSCPICTQTFDETIRKPISLGCGHTVCKMCLNKLHRKACPFDQTTINTDIELLPVNSALLQLVGAQIPEQQPITLCSGVEDTKHYEEAKKCVEELALYLKPLSSARGVGLNSTTQSVLSRPMQRKLVTLVHCQLVEEEGRIRAMRAARSLGERTVTELILQHQNPQQLSSNLWAAVRARGCQFLGPAMQEEALKLVLLALEDGSALSRKVLVLFVVQRLEPRFPQASKTSIGHVVQLLYRASCFKVTARDEDSSLMQLKEEFRTYEALRREHDSQIVQIAMEAGLRIAPDQWSSLLYGDQSHKSHMQSIIDKLQTPASFAQSVQELTIALQRTGDPANLNRLRPHLELLANIDPSPDAPPPTWEQLENGLVAVRTVVHGLVDYIQNHSKKGADQQQPPQHSKYKTYMCRDMKQRGGCPRGASCTFAHSQEELEKFRKMNKRLVPRRPLSASLGQLNEVGLPSAPILSDESAVDLSNRKPPALPNGIASSGSTVTQLIPRGTDPSFDSSLKPVKLDHLSSSAPGSPPDLLESAPKSISALPVNPHPVPPRGPTDLPPMPVTKPIQMVPRGSQLYPAQQADVYYQDPRGSAPAFETAPYQQGMYYTPPPCVSRFVRPPPSAPEPGPPYLDHYSPYLQDRVINSQYGTQPQQYPPMYPAHYDGRRVYPAQSYTREEMFRESPIPIDIPSAAVPSYVPESRERYQQVEGYYPVAPHPAQIRPSYPRDPPYSRLPPPQPHPSLDELHRRRKEIMAQLEERKVISPPPFAPSPTLPPAFHPEEFLDEDLKVAGKYKANDYSQYSPWSCDTIGSYIGTKDAKPKDVVAAGSVEMMNVESKGTREQRLDLQRRAVETSDDDLIPFGDRPTVSRFGAISRTSKTLYQGAGPLQAIAPQGAPTKSINISDYSAYGAHGGWGDSPYSPHANIPPQGHFIEREKMSMAEVASHGKPLLSAEREQLRLELQQLNHQISQQTQLRGLEAVSNRLVLQREVNTLASQPQPPQLPPKWPGMISSEQLSL,Roquin-1,"Post-transcriptional repressor of mRNAs containing a conserved stem loop motif, called constitutive decay element (CDE), which is often located in the 3'-UTR, as in HMGXB3, ICOS, IER3, NFKBID, NFKBIZ, PPP1R10, TNF, TNFRSF4 and in many more mRNAs. Cleaves translationally inactive mRNAs harboring a stem-loop (SL), often located in their 3'-UTRs, during the early phase of inflammation in a helicase UPF1-independent manner. Binds to CDE and promotes mRNA deadenylation and degradation. This process does not involve miRNAs. In follicular helper T (Tfh) cells, represses of ICOS and TNFRSF4/Ox40 expression, thus preventing spontaneous Tfh cell differentiation, germinal center B-cell differentiation in the absence of immunization and autoimmunity. In resting or LPS-stimulated macrophages, controls inflammation by suppressing TNF expression. Also recognizes CDE in its own mRNA and in that of paralogous RC3H2, possibly leading to feedback loop regulation. Inhibits cooperatively with ZC3H12A the differentiation of helper T cells Th17 in lungs. They repress target mRNA encoding the Th17 cell-promoting factors IL6, ICOS, REL, IRF4, NFKBID and NFKBIZ. The cooperation requires RNA-binding by RC3H1 and the nuclease activity of ZC3H12A. Recognizes and binds mRNAs containing a hexaloop stem-loop motif, called alternative decay element (ADE). Together with ZC3H12A, destabilizes TNFRSF4/OX40 mRNA by binding to the conserved stem loop structure in its 3'UTR. Able to interact with double-stranded RNA. miRNA-binding protein that regulates microRNA homeostasis. Enhances DICER-mediated processing of pre-MIR146a but reduces mature MIR146a levels through an increase of 3' end uridylation. Both inhibits ICOS mRNA expression and they may act together to exert the suppression. Acts as a ubiquitin E3 ligase. Pairs with E2 enzymes UBE2A, UBE2B, UBE2D2, UBE2F, UBE2G1, UBE2G2 and UBE2L3 and produces polyubiquitin chains. Shows the strongest activity when paired with UBE2N:UBE2V1 or UBE2N:UBE2V2 E2 complexes and generate both short and long polyubiquitin chains.",Strongly increases CDE and ADE RNA-binding. The mutation in the roquin protein leads to functional changes in T-cell activation and differentiation. The RNA-binding protein Roquin controls T-helper cell activation and differentiation by enhancing the induced expression of costimulatory receptors such as tumor necrosis factor receptor superfamily 4 (Tnfrs4 or Ox40).,Strongly increases CDE and ADE RNA-binding. The mutation in the roquin protein leads to functional changes in T-cell activation and differentiation. The RNA-binding protein Roquin controls T-helper cell activation and differentiation by enhancing the induced expression of costimulatory receptors such as tumor necrosis factor receptor superfamily 4 (Tnfrs4 or Ox40).
2925,2925,0,0,A0A068J840-L85F,MKSELIFLPAPAIGHLVGMVEMAKLFISRHENLSVTVLIAKFYMDTGVDNYNKSLLTNPTPRLTIVNLPETDPQNYMLKPRHAIFPSVIETQKTHVRDIISGMTQSESTQVVGLLADLLFINIMDIANEFNVPTYVYSPAGAGHLGLAFHLQTLNDKKQDVTEFRNSDTELLVPSFANPVPAEVLPSMYVDKEGGYDYLFSLFRRCRESKAIIINTFEELEPYAINSLRMDSMIPPIYPVGPILNLNGDGQNSDEAAVILGWLDDQPPSSVVFLCFGSYGSFQENQVKEIAMGLERSGHRFLWSLRPSIPKGETKLQLKYSNLKEILPVGFLDRTSCVGKVIGWAPQVAVLGHESVGGFLSHCGWNSTLESVWCGVPVATWPMYGEQQLNAFEMVKELGIAVEIEVDYKKDYFNMKNDFIVRAEEIETKIKKLMMDENNSEIRKKVKEMKEKSRAAMSENGSSYNSLAKLFEEIM,,-1.0,MKSELIFLPAPAIGHLVGMVEMAKLFISRHENLSVTVLIAKFYMDTGVDNYNKSLLTNPTPRLTIVNLPETDPQNYMLKPRHAILPSVIETQKTHVRDIISGMTQSESTQVVGLLADLLFINIMDIANEFNVPTYVYSPAGAGHLGLAFHLQTLNDKKQDVTEFRNSDTELLVPSFANPVPAEVLPSMYVDKEGGYDYLFSLFRRCRESKAIIINTFEELEPYAINSLRMDSMIPPIYPVGPILNLNGDGQNSDEAAVILGWLDDQPPSSVVFLCFGSYGSFQENQVKEIAMGLERSGHRFLWSLRPSIPKGETKLQLKYSNLKEILPVGFLDRTSCVGKVIGWAPQVAVLGHESVGGFLSHCGWNSTLESVWCGVPVATWPMYGEQQLNAFEMVKELGIAVEIEVDYKKDYFNMKNDFIVRAEEIETKIKKLMMDENNSEIRKKVKEMKEKSRAAMSENGSSYNSLAKLFEEIM,UDP-glycosyltransferase 1,Component of the dammarane-type triterpene saponins (e.g. ginsenosides or panaxosides) biosynthetic pathway. Glycosyltransferase that catalyzes the biosynthesis of ginsenoside F1 from protopanaxatriol (PPT). Triggers C20-OH glycosylation of ginsenoside Rg3 to produce ginsenoside Rd. Mediates the conversion of protopanaxadiol (PPD) to the ginsenoside compound K. catalyzes the production of 20S-O-beta-(D-glucosyl)-dammarenediol II form dammarenediol II (DM).,Decreased ability to transfer a glucose residue to the C20-OH of protopanaxatriol (PPT). The mutation in UGTPg1 may play an important role in determining its inactivity and substrate regio-specificity.,Decreased ability to transfer a glucose residue to the C20-OH of protopanaxatriol (PPT). The mutation in UGTPg1 may play an important role in determining its inactivity and substrate regio-specificity.
2931,2931,0,0,P01398-W47Q,MKTLLLTLVVVTIVCLDLGYTRTCLISPSSTPQTCPNGQDICFLKAQCDKFCSIRGPVIEQGCVATCPQFRSNYRSLLCCTTDNCNH,,-1.0,MKTLLLTLVVVTIVCLDLGYTRTCLISPSSTPQTCPNGQDICFLKAWCDKFCSIRGPVIEQGCVATCPQFRSNYRSLLCCTTDNCNH,Kappa-bungarotoxin,"Postsynaptic neurotoxin that binds and inhibits neuronal nicotinic acetylcholine receptors (nAChR) with high affinity (IC(50)<100 nM). Is a selective, and slowly reversible antagonist of alpha-3/CHRNA3-containing and some alpha-4/CHRNA4-containing AChRs.",Little decrease in inhibition of neuronal receptor and 8-fold decrease in inhibition of muscle receptor. The mutation in kappa-neurotoxins has been shown to decrease affinity for the muscle receptor by 8-fold.,Little decrease in inhibition of neuronal receptor and 8-fold decrease in inhibition of muscle receptor. The mutation in kappa-neurotoxins has been shown to decrease affinity for the muscle receptor by 8-fold.
2934,2934,0,0,Q695T7-T69A,MVRLVLPNPGLDARIPSLAELETIEQEEASSRPKWDNKAQYMLTCLGFCVGLGNVWRFPYLCQSHGGGAFMIPFLILLVLEGIPLLYLEFAIGQRLRRGSLGVWSSIHPALKGLGLASMLTSFMVGLYYNTIISWIMWYLFNSFQEPLPWSDCPLNENQTGYVDECARSSPVDYFWYRETLNISTSISDSGSIQWWMLLCLACAWSVLYMCTIRGIETTGKAVYITSTLPYVVLTIFLIRGLTLKGATNGIVFLFTPNVTELAQPDTWLDAGAQVFFSFSLAFGGLISFSSYNSVHNNCEKDSVIVSIINGFTSVYVAIVVYSVIGFRATQRYDDCFSTNILTLINGFDLPEGNVTQENFVDMQQRCNASDPAAYAQLVFQTCDINAFLSEAVEGTGLAFIVFTEAITKMPLSPLWSVLFFIMLFCLGLSSMFGNMEGVVVPLQDLRVIPPKWPKEVLTGLICLGTFLIGFIFTLNSGQYWLSLLDSYAGSIPLLIIAFCEMFSVVYVYGVDRFNKDIEFMIGHKPNIFWQVTWRVVSPLLMLIIFLFFFVVEVSQELTYSIWDPGYEEFPKSQKISYPNWVYVVVVIVAGVPSLTIPGYAIYKLIRNHCQKPGDHQGLVSTLSTASMNGDLKY,,-1.0,MVRLVLPNPGLDARIPSLAELETIEQEEASSRPKWDNKAQYMLTCLGFCVGLGNVWRFPYLCQSHGGGTFMIPFLILLVLEGIPLLYLEFAIGQRLRRGSLGVWSSIHPALKGLGLASMLTSFMVGLYYNTIISWIMWYLFNSFQEPLPWSDCPLNENQTGYVDECARSSPVDYFWYRETLNISTSISDSGSIQWWMLLCLACAWSVLYMCTIRGIETTGKAVYITSTLPYVVLTIFLIRGLTLKGATNGIVFLFTPNVTELAQPDTWLDAGAQVFFSFSLAFGGLISFSSYNSVHNNCEKDSVIVSIINGFTSVYVAIVVYSVIGFRATQRYDDCFSTNILTLINGFDLPEGNVTQENFVDMQQRCNASDPAAYAQLVFQTCDINAFLSEAVEGTGLAFIVFTEAITKMPLSPLWSVLFFIMLFCLGLSSMFGNMEGVVVPLQDLRVIPPKWPKEVLTGLICLGTFLIGFIFTLNSGQYWLSLLDSYAGSIPLLIIAFCEMFSVVYVYGVDRFNKDIEFMIGHKPNIFWQVTWRVVSPLLMLIIFLFFFVVEVSQELTYSIWDPGYEEFPKSQKISYPNWVYVVVVIVAGVPSLTIPGYAIYKLIRNHCQKPGDHQGLVSTLSTASMNGDLKY,Sodium-dependent neutral amino acid transporter B,Transporter that mediates resorption of neutral amino acids across the apical membrane of renal and intestinal epithelial cells. This uptake is sodium-dependent and chloride-independent. Requires CLTRN in kidney or ACE2 in intestine for cell surface expression and amino acid transporter activity.,"Decreases cell membrane localization in presence of ACE2 or CLTRN; does not affect interaction with ACE2; amino acid transport activity is not deactivated in presence of ACE2 or CLTRN. This mutation has been shown to facilitate the proper folding and trafficking of B(0)AT1, resulting in an increase in its expression on the cell surface and enhanced amino acid transport in the small intestine and kidney proximal tubule.","Decreases cell membrane localization in presence of ACE2 or CLTRN; does not affect interaction with ACE2; amino acid transport activity is not deactivated in presence of ACE2 or CLTRN. This mutation has been shown to facilitate the proper folding and trafficking of B(0)AT1, resulting in an increase in its expression on the cell surface and enhanced amino acid transport in the small intestine and kidney proximal tubule."
2936,2936,0,0,Q14160-S10C,MLKCIPLWRCNRHVESVDKRHCSLQAVPEEIYRYSRSLEELLLDANQLRELPKPFFRLLNLRKLGLSDNEIQRLPPEVANFMQLVELDVSRNDIPEIPESIKFCKALEIADFSGNPLSRLPDGFTQLRSLAHLALNDVSLQALPGDVGNLANLVTLELRENLLKSLPASLSFLVKLEQLDLGGNDLEVLPDTLGALPNLRELWLDRNQLSALPPELGNLRRLVCLDVSENRLEELPAELGGLVLLTDLLLSQNLLRRLPDGIGQLKQLSILKVDQNRLCEVTEAIGDCENLSELILTENLLMALPRSLGKLTKLTNLNVDRNHLEALPPEIGGCVALSVLSLRDNRLAVLPPELAHTTELHVLDVAGNRLQSLPFALTHLNLKALWLAENQAQPMLRFQTEDDARTGEKVLTCYLLPQQPPPSLEDAGQQGSLSETWSDAPPSRVSVIQFLEAPIGDEDAEEAAAEKRGLQRRATPHPSELKVMKRSIEGRRSEACPCQPDSGSPLPAEEEKRLSAESGLSEDSRPSASTVSEAEPEGPSAEAQGGSQQEATTAGGEEDAEEDYQEPTVHFAEDALLPGDDREIEEGQPEAPWTLPGGRQRLIRKDTPHYKKHFKISKLPQPEAVVALLQGMQPDGEGPVAPGGWHNGPHAPWAPRAQKEEEEEEEGSPQEEEEEEEEENRAEEEEASTEEEDKEGAVVSAPSVKGVSFDQANNLLIEPARIEEEELTLTILRQTGGLGISIAGGKGSTPYKGDDEGIFISRVSEEGPAARAGVRVGDKLLEVNGVALQGAEHHEAVEALRGAGTAVQMRVWRERMVEPENAVTITPLRPEDDYSPRERRGGGLRLPLLPPESPGPLRQRHVACLARSERGLGFSIAGGKGSTPYRAGDAGIFVSRIAEGGAAHRAGTLQVGDRVLSINGVDVTEARHDHAVSLLTAASPTIALLLEREAGGPLPPSPLPHSSPPTAAVATTSITTATPGVPGLPSLAPSLLAAALEGPYPVEEIRLPRAGGPLGLSIVGGSDH,,-1.0,MLKCIPLWRSNRHVESVDKRHCSLQAVPEEIYRYSRSLEELLLDANQLRELPKPFFRLLNLRKLGLSDNEIQRLPPEVANFMQLVELDVSRNDIPEIPESIKFCKALEIADFSGNPLSRLPDGFTQLRSLAHLALNDVSLQALPGDVGNLANLVTLELRENLLKSLPASLSFLVKLEQLDLGGNDLEVLPDTLGALPNLRELWLDRNQLSALPPELGNLRRLVCLDVSENRLEELPAELGGLVLLTDLLLSQNLLRRLPDGIGQLKQLSILKVDQNRLCEVTEAIGDCENLSELILTENLLMALPRSLGKLTKLTNLNVDRNHLEALPPEIGGCVALSVLSLRDNRLAVLPPELAHTTELHVLDVAGNRLQSLPFALTHLNLKALWLAENQAQPMLRFQTEDDARTGEKVLTCYLLPQQPPPSLEDAGQQGSLSETWSDAPPSRVSVIQFLEAPIGDEDAEEAAAEKRGLQRRATPHPSELKVMKRSIEGRRSEACPCQPDSGSPLPAEEEKRLSAESGLSEDSRPSASTVSEAEPEGPSAEAQGGSQQEATTAGGEEDAEEDYQEPTVHFAEDALLPGDDREIEEGQPEAPWTLPGGRQRLIRKDTPHYKKHFKISKLPQPEAVVALLQGMQPDGEGPVAPGGWHNGPHAPWAPRAQKEEEEEEEGSPQEEEEEEEEENRAEEEEASTEEEDKEGAVVSAPSVKGVSFDQANNLLIEPARIEEEELTLTILRQTGGLGISIAGGKGSTPYKGDDEGIFISRVSEEGPAARAGVRVGDKLLEVNGVALQGAEHHEAVEALRGAGTAVQMRVWRERMVEPENAVTITPLRPEDDYSPRERRGGGLRLPLLPPESPGPLRQRHVACLARSERGLGFSIAGGKGSTPYRAGDAGIFVSRIAEGGAAHRAGTLQVGDRVLSINGVDVTEARHDHAVSLLTAASPTIALLLEREAGGPLPPSPLPHSSPPTAAVATTSITTATPGVPGLPSLAPSLLAAALEGPYPVEEIRLPRAGGPLGLSIVGGSDH,Protein scribble homolog,"Scaffold protein involved in different aspects of polarized cell differentiation regulating epithelial and neuronal morphogenesis and T-cell polarization. Via its interaction with CRTAM, required for the late phase polarization of a subset of CD4+ T-cells, which in turn regulates TCR-mediated proliferation and IFNG and IL22 production. Most probably functions in the establishment of apico-basal cell polarity. May function in cell proliferation regulating progression from G1 to S phase and as a positive regulator of apoptosis for instance during acinar morphogenesis of the mammary epithelium. May also function in cell migration and adhesion and hence regulate cell invasion through MAPK signaling. May play a role in exocytosis and in the targeting of synaptic vesicles to synapses. Functions as an activator of Rac GTPase activity.","Gain of palmitoylation. Gain of palmitoylation, localization to cell-cell junctions and function in epithelial cell polarization and signaling pathways regulation; when associated with S-4. The mutation in SCRIB enhances its tumor-suppressive activities to oncogenic YAP, MAPK and PI3K/AKT pathways.","Gain of palmitoylation. Gain of palmitoylation, localization to cell-cell junctions and function in epithelial cell polarization and signaling pathways regulation; when associated with S-4. The mutation in SCRIB enhances its tumor-suppressive activities to oncogenic YAP, MAPK and PI3K/AKT pathways."
2945,2945,0,0,A0A0R4IKJ1-A558N,MTSENHTTIKADSALVMSPTGSTSQAAPFSPSTSKPIQELPDELIQAGWSKCWSKRENRPYYFNRFTNQSLWEMPVLGQHDVISDPLGLNAAPASGEANADAGLGNGQRKRHPSEDASQAGPNSFKRPKVEIPATPTTPTVPISPSTPGVKPWVNTTTDEKQGQASTPAPAPYRPSVVYWDLDIQTNAVIRERAPADHLPPHPEIELQRAQLTTKLRQHYHELCSQREGIEPPRESFNRWLLERKVVDKGLDPLLPSECDPVISPSMFREIMNDIPIRLSRIKYKEEARKLLFKYAEAAKKMIDSRNATPESRKVVKWNVEDTMNWLRRDHSASKEDYMDRLEHLRKQCGPHVASVAKDSVEGICSKIYHISAEYVRRIRQAHLTLLKECNISVDGTESAEVQDRLVYCYPVRLSIPAPPQTRVELHFENDIACLRFKGEMVKVSRGHFNKLELLYRYSCIDDPRFEKFLSRVWCLIKRYQVMFGSGVNEGSGLQGSLPVPVFEALNKQFGVTFECFASPLNCYFKQFCSAFPDIDGFFGSRGPFLSFSPASGSFEANPPFCEELMDAMVTHFEDLLGRSSEPLSFIIFVPEWRDPPTPALTRMEASRFRRHQMTVPAFEHEYRSGSQHICKREEIYYKAIHGTAVIFLQNNAGFAKWEPTTERIQELLAAYKVSGRSLPSPGPSSTNTGEKDSKPAPERTAPSQDNSSPVDKTAQDTTNT,,-1.0,MTSENHTTIKADSALVMSPTGSTSQAAPFSPSTSKPIQELPDELIQAGWSKCWSKRENRPYYFNRFTNQSLWEMPVLGQHDVISDPLGLNAAPASGEANADAGLGNGQRKRHPSEDASQAGPNSFKRPKVEIPATPTTPTVPISPSTPGVKPWVNTTTDEKQGQASTPAPAPYRPSVVYWDLDIQTNAVIRERAPADHLPPHPEIELQRAQLTTKLRQHYHELCSQREGIEPPRESFNRWLLERKVVDKGLDPLLPSECDPVISPSMFREIMNDIPIRLSRIKYKEEARKLLFKYAEAAKKMIDSRNATPESRKVVKWNVEDTMNWLRRDHSASKEDYMDRLEHLRKQCGPHVASVAKDSVEGICSKIYHISAEYVRRIRQAHLTLLKECNISVDGTESAEVQDRLVYCYPVRLSIPAPPQTRVELHFENDIACLRFKGEMVKVSRGHFNKLELLYRYSCIDDPRFEKFLSRVWCLIKRYQVMFGSGVNEGSGLQGSLPVPVFEALNKQFGVTFECFASPLNCYFKQFCSAFPDIDGFFGSRGPFLSFSPASGSFEAAPPFCEELMDAMVTHFEDLLGRSSEPLSFIIFVPEWRDPPTPALTRMEASRFRRHQMTVPAFEHEYRSGSQHICKREEIYYKAIHGTAVIFLQNNAGFAKWEPTTERIQELLAAYKVSGRSLPSPGPSSTNTGEKDSKPAPERTAPSQDNSSPVDKTAQDTTNT,mRNA,"Cap-specific adenosine methyltransferase that catalyzes formation of N(6),2'-O-dimethyladenosine cap (m6A(m)) by methylating the adenosine at the second transcribed position of capped mRNAs.",Strongly enhanced methyltransferase activity.,Strongly enhanced methyltransferase activity.
2949,2949,0,0,Q8E372-N175D,MMKIKPVKVESIENPKRFLNSRLLTKIEVEEAIEKALKQLYINIDYFGEEYPTPATFNNIYKVMDNTEWTNGFWTGCLWLAYEYNQDKKLKNIAHKNVLSFLNRINNRIALDHHDLGFLYTPSCTAEYRINGDVKALEATIKAADKLMERYQEKGGFIQAWGELGYKEHYRLIIDCLLNIQLLFFAYEQTGDEKYRQVAVNHFYASANNVVRDDSSAFHTFYFDPETGEPLKGVTRQGYSDESSWARGQAWGIYGIPLSYRKMKDYQQIILFKGMTNYFLNRLPEDKVSYWDLIFTDGSGQPRDTSATATAVCGIHEMLKYLPEVDPDKETYKYAMHTMLRSLIEQYSNNELIAGRPLLLHGVYSWHSGKGVDEGNIWGDYYYLEALIRFYKDWELYW,,-1.0,MMKIKPVKVESIENPKRFLNSRLLTKIEVEEAIEKALKQLYINIDYFGEEYPTPATFNNIYKVMDNTEWTNGFWTGCLWLAYEYNQDKKLKNIAHKNVLSFLNRINNRIALDHHDLGFLYTPSCTAEYRINGDVKALEATIKAADKLMERYQEKGGFIQAWGELGYKEHYRLIINCLLNIQLLFFAYEQTGDEKYRQVAVNHFYASANNVVRDDSSAFHTFYFDPETGEPLKGVTRQGYSDESSWARGQAWGIYGIPLSYRKMKDYQQIILFKGMTNYFLNRLPEDKVSYWDLIFTDGSGQPRDTSATATAVCGIHEMLKYLPEVDPDKETYKYAMHTMLRSLIEQYSNNELIAGRPLLLHGVYSWHSGKGVDEGNIWGDYYYLEALIRFYKDWELYW,Unsaturated chondroitin disaccharide hydrolase,"Catalyzes the hydrolysis of unsaturated hyaluronate and chondroitin disaccharides. Also degrades unsaturated heparin disaccharides. Releases 4-deoxy-4,5-didehydro D-glucuronic acid or 4-deoxy-4,5-didehydro L-iduronic acid from chondroitin disaccharides, hyaluronan disaccharides and heparin disaccharides and cleaves both glycosidic (1->3) and (1->4) bonds. Prefers sulfated glycosaminoglycans compared to unsulfated glycosaminoglycans. Probably required for mammalian cells invasion through the degradation of extracellular sulfated glycosaminoglycans such as chondroitin and hyaluronan.",Large increase in activity.,Large increase in activity.
2968,2968,0,0,Q08BA4-A85Y,MDEDSKPLLGSVPTGDYYTDSLDPKQRRPFHVEPRNIVGEDVQERVSAEAAVLSSRVHYYSRLTGSSDRLLAPPDHVIPSHEDIYIYSPLGTAFKVQGGDSPIKNPSIVTIFAIWNTMMGTSILSIPWGIKQAGFTLGIIIIVLMGLLTLYCCYRVLKSTKSIPYVDTSDWEFPDVCKYYFGGFGKWSSLVFSLVSLIGAMVVYWVLMSNFLFNTGKFIFNYVHNVNTSDAFGTNGTERVICPYPDVDPHGNSSTSLYSGSDNSTGLEFDHWWSKTNTIPFYLILLLLPLLNFRSASFFARFTFLGTISVIYLIFLVTYKAIQLGFHLEFHWFDSSMFFVPEFRTLFPQLSGVLTLAFFIHNCIITLMKNNKHQENNVRDLSLAYLLVGLTYLYVGVLIFAAFPSPPLSKECIEPNFLDNFPSSDILVFVARTFLLFQMTTVYPLLGYLVRVQLMGQIFGNHYPGFLHVFVLNVFVVGAGVLMARFYPNIGSIIRYSGALCGLALVFVLPSLIHMVSLKRRGELRWTSTLFHGFLILLGVANLLGQFFM,,-1.0,MDEDSKPLLGSVPTGDYYTDSLDPKQRRPFHVEPRNIVGEDVQERVSAEAAVLSSRVHYYSRLTGSSDRLLAPPDHVIPSHEDIAIYSPLGTAFKVQGGDSPIKNPSIVTIFAIWNTMMGTSILSIPWGIKQAGFTLGIIIIVLMGLLTLYCCYRVLKSTKSIPYVDTSDWEFPDVCKYYFGGFGKWSSLVFSLVSLIGAMVVYWVLMSNFLFNTGKFIFNYVHNVNTSDAFGTNGTERVICPYPDVDPHGNSSTSLYSGSDNSTGLEFDHWWSKTNTIPFYLILLLLPLLNFRSASFFARFTFLGTISVIYLIFLVTYKAIQLGFHLEFHWFDSSMFFVPEFRTLFPQLSGVLTLAFFIHNCIITLMKNNKHQENNVRDLSLAYLLVGLTYLYVGVLIFAAFPSPPLSKECIEPNFLDNFPSSDILVFVARTFLLFQMTTVYPLLGYLVRVQLMGQIFGNHYPGFLHVFVLNVFVVGAGVLMARFYPNIGSIIRYSGALCGLALVFVLPSLIHMVSLKRRGELRWTSTLFHGFLILLGVANLLGQFFM,Neutral amino acid transporter 9,"Lysosomal amino acid transporter involved in the activation of mTORC1 in response to amino acid levels. Probably acts as an amino acid sensor of the Rag GTPases and Ragulator complexes, 2 complexes involved in amino acid sensing and activation of mTORC1, a signaling complex promoting cell growth in response to growth factors, energy levels, and amino acids. Following activation by amino acids, the Ragulator and Rag GTPases function as a scaffold recruiting mTORC1 to lysosomes where it is in turn activated. SLC38A9 mediates transport of amino acids with low capacity and specificity with a slight preference for polar amino acids. Acts as an arginine sensor. Following activation by arginine binding, mediates transport of L-glutamine, leucine and tyrosine with high efficiency, and is required for the efficient utilization of these amino acids after lysosomal protein degradation. However, the transport mechanism is not well defined and the role of sodium is not clear. Guanine exchange factor (GEF) that, upon arginine binding, stimulates GDP release from RRAGA and therefore activates the Rag GTPase heterodimer and the mTORC1 pathway in response to nutrient sufficiency.",Loss of L-arginine-inhibited L-leucine transport; when associated with A-79; A-80; A-81 and A-82. The crystal structure of zebrafish SLC38A9 (drSLC38A9) revealed a significant conformational change of the N-terminal domain (N-plug) when compared with the arginine-bound structure. This suggests that the mutation may affect the binding of arginine and potentially impact mTORC1 activation.,Loss of L-arginine-inhibited L-leucine transport; when associated with A-79; A-80; A-81 and A-82. The crystal structure of zebrafish SLC38A9 (drSLC38A9) revealed a significant conformational change of the N-terminal domain (N-plug) when compared with the arginine-bound structure. This suggests that the mutation may affect the binding of arginine and potentially impact mTORC1 activation.
2970,2970,0,0,P0CE80-A80C,MLPYIVLVLGCWSVLSQAAQTDDEERAGNRRPIWIMGHMVNAIGQIDEFVNLGANSIETDVSFDDNANPEYTYHGIPCDCGRNCKKYENFNDFLKGLRSATTPGNSKYQEKLVLVVFDLKTGSLYDNQANDAGKKLAKNLLQHYWNNGNNGGRAYIVLSIPDLNHYPLIKGFKDQLTKDGHPELMDKVGHDFSGNDDIGDVGKAYKKAGITGHIWQSDGITNCLPRGLSRVNAAVANRDSANGFINKVYYWTVDKRSTTRDALDAGVDGIMTNYPDVITDVLNEAAYKKKFRVATYDENPWVTFKK,,-1.0,MLPYIVLVLGCWSVLSQAAQTDDEERAGNRRPIWIMGHMVNAIGQIDEFVNLGANSIETDVSFDDNANPEYTYHGIPCDAGRNCKKYENFNDFLKGLRSATTPGNSKYQEKLVLVVFDLKTGSLYDNQANDAGKKLAKNLLQHYWNNGNNGGRAYIVLSIPDLNHYPLIKGFKDQLTKDGHPELMDKVGHDFSGNDDIGDVGKAYKKAGITGHIWQSDGITNCLPRGLSRVNAAVANRDSANGFINKVYYWTVDKRSTTRDALDAGVDGIMTNYPDVITDVLNEAAYKKKFRVATYDENPWVTFKK,Dermonecrotic toxin LiSicTox-alphaIA1a,"Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate. This toxin acts on sphingomyelin (SM) with high activity. It also acts on lysophosphatidylcholine (LPC), and lyso-platelet activating factor (LPAF, an alkyl-LPC) but not on phosphatidylcholine (PC). It may also act on ceramide phosphoethanolamine (CPE), lysophosphatidylcholine (LPC) and lysophosphatidylethanolamine (LPE), but not on lysophosphatidylserine (LPS), and lysophosphatidylglycerol (LPG). It acts by transphosphatidylation, releasing exclusively cyclic phosphate products as second products. In vivo, it induces dermonecrosis, vascular permeability, platelet aggregation, inflammatory response, edema and cytotoxicity against renal epithelial cells. It causes direct nephrotoxicity  and is directly toxic to liver. It also induces hemolysis in a complement-dependent manner as well as in a complement-independent manner. The hemolysis provoked in a complement-independent manner is composed of several steps. The toxin binds to erythrocyte membranes, hydrolyzes membrane phospholipids (SM and LPC) thus generating metabolism products that cause hemolysis, probably by provoking an increase of calcium inside cells. The calcium influx is due to the opening of L-type calcium channels, since L-type calcium channel blockers inhibit calcium influx. In vivo, is lethal to mice when intraperitoneally injected.","Moderate increase of catalytic activity on sphingomyelin and lysophosphatidylcholine, and moderate increase of hemolytic, vascular permeability, and dermonecrotic activities; when associated with A-223.","Moderate increase of catalytic activity on sphingomyelin and lysophosphatidylcholine, and moderate increase of hemolytic, vascular permeability, and dermonecrotic activities; when associated with A-223."
2997,2997,0,0,Q969V5-A319H,MESGGRPSLCQFILLGTTSVVTAALYSVYRQKARVSQELKGAKKVHLGEDLKSILSEAPGKCVPYAVIEGAVRSVKETLNSQFVENCKGVIQRLTLQEHKMVWNRTTHLWNDCSKIIHQRTNTVPFDLVPHEDGVDVAVRVLKPLDSVDLGLETVYEKFHPSIQSFTDVIGHYISGERPKGIQETEEMLKVGATLTGVGELVLDNNSVRLQPPKQGMQYYLSSQDFDSLLQRQESSVRLWKVLALVFGFATCATLFFILRKQYLQRQERLRLKQMQEEFQEHEAQLLSRAKPEDRESLKSACVVCLSSFKSCVFLECGHVCSCTECYRALPEPKKCPICRQAITRVIPLYNS,,-1.0,MESGGRPSLCQFILLGTTSVVTAALYSVYRQKARVSQELKGAKKVHLGEDLKSILSEAPGKCVPYAVIEGAVRSVKETLNSQFVENCKGVIQRLTLQEHKMVWNRTTHLWNDCSKIIHQRTNTVPFDLVPHEDGVDVAVRVLKPLDSVDLGLETVYEKFHPSIQSFTDVIGHYISGERPKGIQETEEMLKVGATLTGVGELVLDNNSVRLQPPKQGMQYYLSSQDFDSLLQRQESSVRLWKVLALVFGFATCATLFFILRKQYLQRQERLRLKQMQEEFQEHEAQLLSRAKPEDRESLKSACVVCLSSFKSCVFLECGAVCSCTECYRALPEPKKCPICRQAITRVIPLYNS,Mitochondrial ubiquitin ligase activator of NFKB 1,"Exhibits weak E3 ubiquitin-protein ligase activity. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates. Can ubiquitinate AKT1 preferentially at 'Lys-284' involving 'Lys-48'-linked polyubiquitination and seems to be involved in regulation of Akt signaling by targeting phosphorylated Akt to proteosomal degradation. Mediates polyubiquitination of cytoplasmic TP53 at 'Lys-24' which targets TP53 for proteasomal degradation, thus reducing TP53 levels in the cytoplasm and mitochondrion. Proposed to preferentially act as a SUMO E3 ligase at physiological concentrations. Plays a role in the control of mitochondrial morphology by promoting mitochondrial fragmentation, and influences mitochondrial localization. Likely to promote mitochondrial fission through negatively regulating the mitochondrial fusion proteins MFN1 and MFN2, acting in a pathway that is parallel to the PRKN/PINK1 regulatory pathway. May also be involved in the sumoylation of the membrane fission protein DNM1L. Inhibits cell growth. When overexpressed, activates JNK through MAP3K7/TAK1 and induces caspase-dependent apoptosis. Involved in the modulation of innate immune defense against viruses by inhibiting RIGI-dependent antiviral response. Can mediate RIGI sumoylation and disrupt its polyubiquitination.",Abolishes ligase inactivity. No effect on mitochondrial localization. The mutation in GIDE accelerates cell growth.,Abolishes ligase inactivity. No effect on mitochondrial localization. The mutation in GIDE accelerates cell growth.
3002,3002,0,0,B2B3C0-A300E,MKGLFAFGLGLLSLVNALPQAQGGGAAASAKVSGTRFVIDGKTGYFAGTNSYWIGFLTNNRDVDTTLDHIASSGLKILRVWGFNDVNNQPSGNTVWFQRLASSGSQINTGPNGLQRLDYLVRSAETRGIKLIIALVNYWDDFGGMKAYVNAFGGTKESWYTNARAQEQYKRYIQAVVSRYVNSPAIFAWELANEPRCKGCNTNVIFNWATQISDYIRSLDKDHLITLGDEGFGLPGQTTYPYQYGEGTDFVKNLQIKNLDFGTFHMYPGHWGVPTSFGPGWIKDHAAACRAAGKPCLLEEYGYESDRCNVQKGWQQASRELSRDGMSGDLFWQWGDQLSTGQTHNDGFTIYYGSSLATCLVTDHVRAINALPA,,-1.0,MKGLFAFGLGLLSLVNALPQAQGGGAAASAKVSGTRFVIDGKTGYFAGTNSYWIGFLTNNRDVDTTLDHIASSGLKILRVWGFNDVNNQPSGNTVWFQRLASSGSQINTGPNGLQRLDYLVRSAETRGIKLIIALVNYWDDFGGMKAYVNAFGGTKESWYTNARAQEQYKRYIQAVVSRYVNSPAIFAWELANEPRCKGCNTNVIFNWATQISDYIRSLDKDHLITLGDEGFGLPGQTTYPYQYGEGTDFVKNLQIKNLDFGTFHMYPGHWGVPTSFGPGWIKDHAAACRAAGKPCLLEAYGYESDRCNVQKGWQQASRELSRDGMSGDLFWQWGDQLSTGQTHNDGFTIYYGSSLATCLVTDHVRAINALPA,"Mannan endo-1,4-beta-mannosidase A","Endo-1,4-mannanase that catalyzes the random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans and heteromannans. It is a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans. Hydrolyzes structurally different mannan polysaccharides, such as galactomannans, glucomannans, and beta-1,4-mannans from different sources, yielding principally mannobiose. Also has transglycosylation activity.",Enables catalytic activity.,Enables catalytic activity.
3006,3006,0,0,P16862-V439R,MTVTTPFVNGTSYCTVTAYSVQSYKAAIDFYTKFLSLENRSSPDENSTLLSNDSISLKILLRPDEKINKNVEAHLKELNSITKTQDWRSHATQSLVFNTSDILAVKDTLNAMNAPLQGYPTELFPMQLYTLDPLGNVVGVTSTKNAVSTKPTPPPAPEASAESGLSSKVHSYTDLAYRMKTTDTYPSLPKPLNRPQKAIAVMTSGGDAPGMNSNVRAIVRSAIFKGCRAFVVMEGYEGLVRGGPEYIKEFHWEDVRGWSAEGGTNIGTARCMEFKKREGRLLGAQHLIEAGVDALIVCGGDGSLTGADLFRSEWPSLIEELLKTNRISNEQYERMKHLNICGTVGSIDNDMSTTDATIGAYSALDRICKAIDYVEATANSHSRAFVVEVMGRNCGWLALLAGIATSADYIFIPEKPATSSEWQDQMCDIVSKHRSRGKRTTIVVVAEGAIAADLTPISPSDVHKVLVDRLGLDTRITTLGHVQRGGTAVAYDRILATLQGLEAVNAVLESTPDTPSPLIAVNENKIVRKPLMESVKLTKAVAEAIQAKDFKRAMSLRDTEFIEHLNNFMAINSADHNEPKLPKDKRLKIAIVNVGAPAGGINSAVYSMATYCMSQGHRPYAIYNGWSGLARHESVRSLNWKDMLGWQSRGGSEIGTNRVTPEEADLGMIAYYFQKYEFDGLIIVGGFEAFESLHQLERARESYPAFRIPMVLIPATLSNNVPGTEYSLGSDTALNALMEYCDVVKQSASSTRGRAFVVDCQGGNSGYLATYASLAVGAQVSYVPEEGISLEQLSEDIEYLAQSFEKAEGRGRFGKLILKSTNASKALSATKLAEVITAEADGRFDAKPAYPGHVQQGGLPSPIDRTRATRMAIKAVGFIKDNQAAIAEARAAEENFNADDKTISDTAAVVGVKGSHVVYNSIRQLYDYETEVSMRMPKVIHWQATRLIADHLVGRKRVD,,-1.0,MTVTTPFVNGTSYCTVTAYSVQSYKAAIDFYTKFLSLENRSSPDENSTLLSNDSISLKILLRPDEKINKNVEAHLKELNSITKTQDWRSHATQSLVFNTSDILAVKDTLNAMNAPLQGYPTELFPMQLYTLDPLGNVVGVTSTKNAVSTKPTPPPAPEASAESGLSSKVHSYTDLAYRMKTTDTYPSLPKPLNRPQKAIAVMTSGGDAPGMNSNVRAIVRSAIFKGCRAFVVMEGYEGLVRGGPEYIKEFHWEDVRGWSAEGGTNIGTARCMEFKKREGRLLGAQHLIEAGVDALIVCGGDGSLTGADLFRSEWPSLIEELLKTNRISNEQYERMKHLNICGTVGSIDNDMSTTDATIGAYSALDRICKAIDYVEATANSHSRAFVVEVMGRNCGWLALLAGIATSADYIFIPEKPATSSEWQDQMCDIVSKHRSRGKVTTIVVVAEGAIAADLTPISPSDVHKVLVDRLGLDTRITTLGHVQRGGTAVAYDRILATLQGLEAVNAVLESTPDTPSPLIAVNENKIVRKPLMESVKLTKAVAEAIQAKDFKRAMSLRDTEFIEHLNNFMAINSADHNEPKLPKDKRLKIAIVNVGAPAGGINSAVYSMATYCMSQGHRPYAIYNGWSGLARHESVRSLNWKDMLGWQSRGGSEIGTNRVTPEEADLGMIAYYFQKYEFDGLIIVGGFEAFESLHQLERARESYPAFRIPMVLIPATLSNNVPGTEYSLGSDTALNALMEYCDVVKQSASSTRGRAFVVDCQGGNSGYLATYASLAVGAQVSYVPEEGISLEQLSEDIEYLAQSFEKAEGRGRFGKLILKSTNASKALSATKLAEVITAEADGRFDAKPAYPGHVQQGGLPSPIDRTRATRMAIKAVGFIKDNQAAIAEARAAEENFNADDKTISDTAAVVGVKGSHVVYNSIRQLYDYETEVSMRMPKVIHWQATRLIADHLVGRKRVD,ATP-dependent 6-phosphofructokinase subunit beta,"Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.",Reduces maximal activity of the holoenzyme by more than 25%.,Reduces maximal activity of the holoenzyme by more than 25%.
3017,3017,0,0,Q9NX46-D115G,MAAAAMAAAAGGGAGAARSLSRFRGCLAGALLGDCVGSFYEAHDTVDLTSVLRHVQSLEPDPGTPGSERTEALYYTDDTAMARALVQSLLAKEAFDEVDMAHRFAQEYKKDPDRGYGAGVVTVFKKLLNPKCRDVFEPARAQFNGKGSYGNGGAMRVAGISLAYSSVQDVQKFARLSAQLTHASSLGYNGAILQALAVHLALQGESSSEHFLKQLLGHMEDLEGDAQSVLDARELGMEERPYSSRLKKIGELLDQASVTREEVVSELGNGIAAFESVPTAIYCFLRCMEPDPEIPSAFNSLQRTLIYSISLGGDTDTIATMAGAIAGAYYGMDQVPESWQQSCEGYEETDILAQSLHRVFQKS,,-1.0,MAAAAMAAAAGGGAGAARSLSRFRGCLAGALLGDCVGSFYEAHDTVDLTSVLRHVQSLEPDPGTPGSERTEALYYTDDTAMARALVQSLLAKEAFDEVDMAHRFAQEYKKDPDRDYGAGVVTVFKKLLNPKCRDVFEPARAQFNGKGSYGNGGAMRVAGISLAYSSVQDVQKFARLSAQLTHASSLGYNGAILQALAVHLALQGESSSEHFLKQLLGHMEDLEGDAQSVLDARELGMEERPYSSRLKKIGELLDQASVTREEVVSELGNGIAAFESVPTAIYCFLRCMEPDPEIPSAFNSLQRTLIYSISLGGDTDTIATMAGAIAGAYYGMDQVPESWQQSCEGYEETDILAQSLHRVFQKS,ADP-ribosylhydrolase ARH3,"ADP-ribosylhydrolase that preferentially hydrolyzes the scissile alpha-O-linkage attached to the anomeric C1'' position of ADP-ribose and acts on different substrates, such as proteins ADP-ribosylated on serine and threonine, free poly(ADP-ribose) and O-acetyl-ADP-D-ribose. Specifically acts as a serine mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to serine residues on proteins, thereby playing a key role in DNA damage response. Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage. Does not hydrolyze ADP-ribosyl-arginine, -cysteine, -diphthamide, or -asparagine bonds. Also able to degrade protein free poly(ADP-ribose), which is synthesized in response to DNA damage: free poly(ADP-ribose) acts as a potent cell death signal and its degradation by ADPRHL2 protects cells from poly(ADP-ribose)-dependent cell death, a process named parthanatos. Also hydrolyzes free poly(ADP-ribose) in mitochondria. Specifically digests O-acetyl-ADP-D-ribose, a product of deacetylation reactions catalyzed by sirtuins. Specifically degrades 1''-O-acetyl-ADP-D-ribose isomer, rather than 2''-O-acetyl-ADP-D-ribose or 3''-O-acetyl-ADP-D-ribose isomers.",Enhanced ability to bind and hydrolyze proteins ADP-ribosylated on serine. No effect on hydrolase activity. The mutation in ARH3 is insignificant for both the mono- and the poly-ADP-ribosylhydrolase activity of ARH3. The mutation preserves protein stability.,Enhanced ability to bind and hydrolyze proteins ADP-ribosylated on serine. No effect on hydrolase activity. The mutation in ARH3 is insignificant for both the mono- and the poly-ADP-ribosylhydrolase activity of ARH3. The mutation preserves protein stability.
3019,3019,0,0,O15169-A385P,MNIQEQGFPLDLGASFTEDAPRPPVPGEEGELVSTDPRPASYSFCSGKGVGIKGETSTATPRRSDLDLGYEPEGSASPTPPYLKWAESLHSLLDDQDGISLFRTFLKQEGCADLLDFWFACTGFRKLEPCDSNEEKRLKLARAIYRKYILDNNGIVSRQTKPATKSFIKGCIMKQLIDPAMFDQAQTEIQATMEENTYPSFLKSDIYLEYTRTGSESPKVCSDQSSGSGTGKGISGYLPTLNEDEEWKCDQDMDEDDGRDAAPPGRLPQKLLLETAAPRVSSSRRYSEGREFRYGSWREPVNPYYVNAGYALAPATSANDSEQQSLSSDADTLSLTDSSVDGIPPYRIRKQHRREMQESVQVNGRVPLPHIPRTYRVPKEVRVEPQKFAEELIHRLEAVQRTREAEEKLEERLKRVRMEEEGEDGDPSSGPPGPCHKLPPAPAWHHFPPRCVDMGCAGLRDAHEENPESILDEHVQRVLRTPGRQSPGPGHRSPDSGHVAKMPVALGGAASGHGKHVPKSGAKLDAAGLHHHRHVHHHVHHSTARPKEQVEAEATRRAQSSFAWGLEPHSHGARSRGYSESVGAAPNASDGLAHSGKVGVACKRNAKKAESGKSASTEVPGASEDAEKNQKIMQWIIEGEKEISRHRRTGHGSSGTRKPQPHENSRPLSLEHPWAGPQLRTSVQPSHLFIQDPTMPPHPAPNPLTQLEEARRRLEEEEKRASRAPSKQRYVQEVMRRGRACVRPACAPVLHVVPAVSDMELSETETRSQRKVGGGSAQPCDSIVVAYYFCGEPIPYRTLVRGRAVTLGQFKELLTKKGSYRYYFKKVSDEFDCGVVFEEVREDEAVLPVFEEKIIGKVEKVD,,-1.0,MNIQEQGFPLDLGASFTEDAPRPPVPGEEGELVSTDPRPASYSFCSGKGVGIKGETSTATPRRSDLDLGYEPEGSASPTPPYLKWAESLHSLLDDQDGISLFRTFLKQEGCADLLDFWFACTGFRKLEPCDSNEEKRLKLARAIYRKYILDNNGIVSRQTKPATKSFIKGCIMKQLIDPAMFDQAQTEIQATMEENTYPSFLKSDIYLEYTRTGSESPKVCSDQSSGSGTGKGISGYLPTLNEDEEWKCDQDMDEDDGRDAAPPGRLPQKLLLETAAPRVSSSRRYSEGREFRYGSWREPVNPYYVNAGYALAPATSANDSEQQSLSSDADTLSLTDSSVDGIPPYRIRKQHRREMQESVQVNGRVPLPHIPRTYRVPKEVRVEAQKFAEELIHRLEAVQRTREAEEKLEERLKRVRMEEEGEDGDPSSGPPGPCHKLPPAPAWHHFPPRCVDMGCAGLRDAHEENPESILDEHVQRVLRTPGRQSPGPGHRSPDSGHVAKMPVALGGAASGHGKHVPKSGAKLDAAGLHHHRHVHHHVHHSTARPKEQVEAEATRRAQSSFAWGLEPHSHGARSRGYSESVGAAPNASDGLAHSGKVGVACKRNAKKAESGKSASTEVPGASEDAEKNQKIMQWIIEGEKEISRHRRTGHGSSGTRKPQPHENSRPLSLEHPWAGPQLRTSVQPSHLFIQDPTMPPHPAPNPLTQLEEARRRLEEEEKRASRAPSKQRYVQEVMRRGRACVRPACAPVLHVVPAVSDMELSETETRSQRKVGGGSAQPCDSIVVAYYFCGEPIPYRTLVRGRAVTLGQFKELLTKKGSYRYYFKKVSDEFDCGVVFEEVREDEAVLPVFEEKIIGKVEKVD,Axin-1,"Component of the beta-catenin destruction complex required for regulating CTNNB1 levels through phosphorylation and ubiquitination, and modulating Wnt-signaling. Controls dorsoventral patterning via two opposing effects; down-regulates CTNNB1 to inhibit the Wnt signaling pathway and ventralize embryos, but also dorsalizes embryos by activating a Wnt-independent JNK signaling pathway. In Wnt signaling, probably facilitates the phosphorylation of CTNNB1 and APC by GSK3B. Likely to function as a tumor suppressor. Enhances TGF-beta signaling by recruiting the RNF111 E3 ubiquitin ligase and promoting the degradation of inhibitory SMAD7. Also a component of the AXIN1-HIPK2-TP53 complex which controls cell growth, apoptosis and development. Facilitates the phosphorylation of TP53 by HIPK2 upon ultraviolet irradiation.",Loss of interaction with SIAH1. Increased SIAH1-induced proteasome-mediated ubiquitin-dependent degradation of AXIN1. No effect on interaction with GSK3B. The mutation in Axin inhibits its degradation through interaction with SIAH1/2.,Loss of interaction with SIAH1. Increased SIAH1-induced proteasome-mediated ubiquitin-dependent degradation of AXIN1. No effect on interaction with GSK3B. The mutation in Axin inhibits its degradation through interaction with SIAH1/2.
3020,3020,0,0,P30084-E273K,MAALRVLLSCVRGPLRPPVRCPAWRPFASGANFEYIIAEKRGKNNTVGLIQLNRPKALNALCDGLIDELNQALKTFEEDPAVGAIVLTGGDKAFAAGADIKEMQNLSFQDCYSSKFLKHWDHLTQVKKPVIAAVNGYAFGGGCELAMMCDIIYAGEKAQFAQPEILIGTIPGAGGTQRLTRAVGKSLAMEMVLTGDRISAQDAKQAGLVSKICPVETLVEEAIQCAEKIASNSKIVVAMAKESVNAAFEMTLTEGSKLEKKLFYSTFATDDRKEGMTAFVEKRKANFKDQ,,-1.0,MAALRVLLSCVRGPLRPPVRCPAWRPFASGANFEYIIAEKRGKNNTVGLIQLNRPKALNALCDGLIDELNQALKTFEEDPAVGAIVLTGGDKAFAAGADIKEMQNLSFQDCYSSKFLKHWDHLTQVKKPVIAAVNGYAFGGGCELAMMCDIIYAGEKAQFAQPEILIGTIPGAGGTQRLTRAVGKSLAMEMVLTGDRISAQDAKQAGLVSKICPVETLVEEAIQCAEKIASNSKIVVAMAKESVNAAFEMTLTEGSKLEKKLFYSTFATDDREEGMTAFVEKRKANFKDQ,"Enoyl-CoA hydratase, mitochondrial","Converts unsaturated trans-2-enoyl-CoA species ((2E)-enoyl-CoA) to the corresponding (3S)-3hydroxyacyl-CoA species through addition of a water molecule to the double bond. Catalyzes the hydration of medium- and short-chained fatty enoyl-CoA thioesters from 4 carbons long (C4) up to C16. Has high substrate specificity for crotonyl-CoA ((2E)-butenoyl-CoA) and moderate specificity for acryloyl-CoA, 3-methylcrotonyl-CoA (3-methyl-(2E)-butenoyl-CoA) and methacrylyl-CoA ((2E)-2-methylpropenoyl-CoA). Can bind tiglyl-CoA (2-methylcrotonoyl-CoA), but hydrates only a small amount of this substrate. Plays a key role in the beta-oxidation spiral of short- and medium-chain fatty acid oxidation. At a lower rate than the hydratase reaction, catalyzes the isomerase reaction of trans-3-enoyl-CoA species (such as (3E)-hexenoyl-CoA) to trans-2-enoyl-CoA species (such as (2E)-hexenoyl-CoA), which are subsequently hydrated to 3(S)-3-hydroxyacyl-CoA species (such as (3S)-hydroxyhexanoyl-CoA).",Functional changes in ECHS1D are not observed with the mutation in the ECHS1 gene.,Functional changes in ECHS1D are not observed with the mutation in the ECHS1 gene.
3033,3033,0,0,Q74K42-N272D,MLENKNHKKISLSGKSLLMGTLSTAAIVLSASTANAATINADNVNENQTVEVTASSVNNENNKQVTEKDSADKSTSDVAEDANTKKSNENTETTEKNTQTVVTNAPVSDVKNTNTVTAETPVDKVVNNSDQKTTNAATTDTKKDDVKQVEKKDSVDKTNAEENKDSSVKPAENATKAELKGQVKDIVEESGVDTSKLTNDQINELNKINFSKEAKSGTQLTYNDFKKIAKTLIEQDARYAIPFFNASKIKNMPAAKTLDAQSGKVEDLEIWDSWPVQDAKTGYVSNWNGYQLVIGMMGVPNVNDNHIYLLYNKYGDNDFNHWKNAGPIFGLGTPVIQQWSGSATLNKDGSIQLYYTKVDTSDNNTNHQKLASATVYLNLEKDQDKISIAHVDNDHIVFEGDGYHYQTYDQWKETNKGADNIAMRDAHVIDDDNGNRYLVFEASTGTENYQGDDQIYQWLNYGGTNKDNLGDFFQILSNSDIKDRAKWSNAAIGIIKLNDDVKNPSVAKVYSPLISAPMVSDEIERPDVVKLGNKYYLFAATRLNRGSNDDAWMATNKAVGDNVAMIGYVSDNLTHGYVPLNESGVVLTASVPANWRTATYSYYAVPVEGRDDQLLITSYITNRGEVAGKGMHATWAPSFLLQINPDNTTTVLAKMTNQGDWIWDDSSENPDMMGVLEKDAPNSAALPGEWGKPVDWDLIGGYNLKPHQPVTPIPNVPTTPETPTTPDKPEVPTTPEVPTTPETPTPEAPKNPVKKTSQSKLPKAGDKNSFAAVVLGAVSSILGAVGLTGVSKRKRNN,,-1.0,MLENKNHKKISLSGKSLLMGTLSTAAIVLSASTANAATINADNVNENQTVEVTASSVNNENNKQVTEKDSADKSTSDVAEDANTKKSNENTETTEKNTQTVVTNAPVSDVKNTNTVTAETPVDKVVNNSDQKTTNAATTDTKKDDVKQVEKKDSVDKTNAEENKDSSVKPAENATKAELKGQVKDIVEESGVDTSKLTNDQINELNKINFSKEAKSGTQLTYNDFKKIAKTLIEQDARYAIPFFNASKIKNMPAAKTLDAQSGKVEDLEIWNSWPVQDAKTGYVSNWNGYQLVIGMMGVPNVNDNHIYLLYNKYGDNDFNHWKNAGPIFGLGTPVIQQWSGSATLNKDGSIQLYYTKVDTSDNNTNHQKLASATVYLNLEKDQDKISIAHVDNDHIVFEGDGYHYQTYDQWKETNKGADNIAMRDAHVIDDDNGNRYLVFEASTGTENYQGDDQIYQWLNYGGTNKDNLGDFFQILSNSDIKDRAKWSNAAIGIIKLNDDVKNPSVAKVYSPLISAPMVSDEIERPDVVKLGNKYYLFAATRLNRGSNDDAWMATNKAVGDNVAMIGYVSDNLTHGYVPLNESGVVLTASVPANWRTATYSYYAVPVEGRDDQLLITSYITNRGEVAGKGMHATWAPSFLLQINPDNTTTVLAKMTNQGDWIWDDSSENPDMMGVLEKDAPNSAALPGEWGKPVDWDLIGGYNLKPHQPVTPIPNVPTTPETPTTPDKPEVPTTPEVPTTPETPTPEAPKNPVKKTSQSKLPKAGDKNSFAAVVLGAVSSILGAVGLTGVSKRKRNN,Inulosucrase,Fructosyltransferase that catalyzes the polymerization of the fructose moiety of sucrose to produce inulin polymer and inulin oligosaccharides such as 1-kestose and nystose.,"Regain of catalytic activity. The three-dimensional structure of InuJ, a truncated inactive bacterial GH68 inulosucrase, has been elucidated. The sucrose binding pocket and mode of binding are virtually identical to GH68 levansucrases. The binding mode of the first transfructosylation product 1-kestose in subsites -1 to +2 shows how inulin-type fructo-oligosaccharides bind in GH68 FS and how an inulin-type linkage can be formed.","Regain of catalytic activity. The three-dimensional structure of InuJ, a truncated inactive bacterial GH68 inulosucrase, has been elucidated. The sucrose binding pocket and mode of binding are virtually identical to GH68 levansucrases. The binding mode of the first transfructosylation product 1-kestose in subsites -1 to +2 shows how inulin-type fructo-oligosaccharides bind in GH68 FS and how an inulin-type linkage can be formed."
3046,3046,0,0,P14234-R279K,MGCVFCKKLEPASKEDVGLEGDFRSQTAEERYFPDPTQGRTSSVFPQPTSPAFLNTGNMRSISGTGVTIFVALYDYEARTGDDLTFTKGEKFHILNNTEYDWWEARSLSSGHRGYVPSNYVAPVDSIQAEEWYFGKISRKDAERQLLSSGNPQGAFLIRESETTKGAYSLSIRDWDQNRGDHIKHYKIRKLDTGGYYITTRAQFDSIQDLVRHYMEVNDGLCYLLTAPCTTTKPQTLGLAKDAWEIDRNSIALERRLGTGCFGDVWLGTWNCSTKVAVKTLKPGTMSPKAFLEEAQIMKLLRHDKLVQLYAVVSEEPIYIVTEFMCYGSLLDFLKDREGQNLMLPHLVDMAAQVAEGMAYMERMNYIHRDLRAANILVGEYLICKIADFGLARLIEDNEYNPQQGTKFPIKWTAPEAALFGRFTVKSDVWSFGILLTELITKGRVPYPGMNNREVLEQVEHGYHMPCPPGCPASLYEVMEQAWRLDPEERPTFEYLQSFLEDYFTSTEPQYQPGDQT,,-1.0,MGCVFCKKLEPASKEDVGLEGDFRSQTAEERYFPDPTQGRTSSVFPQPTSPAFLNTGNMRSISGTGVTIFVALYDYEARTGDDLTFTKGEKFHILNNTEYDWWEARSLSSGHRGYVPSNYVAPVDSIQAEEWYFGKISRKDAERQLLSSGNPQGAFLIRESETTKGAYSLSIRDWDQNRGDHIKHYKIRKLDTGGYYITTRAQFDSIQDLVRHYMEVNDGLCYLLTAPCTTTKPQTLGLAKDAWEIDRNSIALERRLGTGCFGDVWLGTWNCSTKVAVRTLKPGTMSPKAFLEEAQIMKLLRHDKLVQLYAVVSEEPIYIVTEFMCYGSLLDFLKDREGQNLMLPHLVDMAAQVAEGMAYMERMNYIHRDLRAANILVGEYLICKIADFGLARLIEDNEYNPQQGTKFPIKWTAPEAALFGRFTVKSDVWSFGILLTELITKGRVPYPGMNNREVLEQVEHGYHMPCPPGCPASLYEVMEQAWRLDPEERPTFEYLQSFLEDYFTSTEPQYQPGDQT,Tyrosine-protein kinase Fgr,"Non-receptor tyrosine-protein kinase that transmits signals from cell surface receptors devoid of kinase activity and contributes to the regulation of immune responses, including neutrophil, monocyte, macrophage and mast cell functions, cytoskeleton remodeling in response to extracellular stimuli, phagocytosis, cell adhesion and migration. Promotes mast cell degranulation, release of inflammatory cytokines and IgE-mediated anaphylaxis. Acts downstream of receptors that bind the Fc region of immunoglobulins, such as MS4A2/FCER1B, FCER1G and FCGR2. Acts downstream of ITGB1 and ITGB2, and regulates actin cytoskeleton reorganization, cell spreading and adhesion. Depending on the context, activates or inhibits cellular responses. Functions as negative regulator of ITGB2 signaling, phagocytosis and SYK activity in monocytes. Required for normal ITGB1 and ITGB2 signaling, normal cell spreading and adhesion in neutrophils and macrophages. Functions as positive regulator of cell migration and regulates cytoskeleton reorganization via RAC1 activation. Phosphorylates SYK (in vitro) and promotes SYK-dependent activation of AKT1 and MAP kinase signaling. Phosphorylates PLD2 in antigen-stimulated mast cells, leading to PLD2 activation and the production of the signaling molecules lysophosphatidic acid and diacylglycerol. Promotes activation of PIK3R1. Phosphorylates FASLG, and thereby regulates its ubiquitination and subsequent internalization. Phosphorylates ABL1. Promotes phosphorylation of CBL, CTTN, PIK3R1, PTK2/FAK1, PTK2B/PYK2 and VAV2. Phosphorylates HCLS1 that has already been phosphorylated by SYK, but not unphosphorylated HCLS1. Together with CLNK, it acts as a negative regulator of natural killer cell-activating receptors and inhibits interferon-gamma production.",Recovery of kinase activity.,Recovery of kinase activity.
3068,3068,0,0,P0C0E4-G59D,MSAPGSPDQAYDFLLKFLLVGDRDVGKSEILESLQDGTAESPYSHLGGIDYKTTTILLDGQRVKLKLWDTSGQGRFCTIFRSYSRGAQGVILVYDIANRWSFEGMDRWIKKIEEHAPGVPKILVGNRLHLAFKRQVPREQAQAYAERLGVTFFEVSPLCNFNIIESFTELARIVLLRHRLNWLGRPSKVLSLQDLCCRTIVSCTPVHLVDKLPLPIALRSHLKSFSMAKGLNARMMRGLSYSLTTSSTHKRSSLCKVKIVCPPQSPPKNCTRNSCKIS,,-1.0,MSAPGSPDQAYDFLLKFLLVGDRDVGKSEILESLQDGTAESPYSHLGGIDYKTTTILLGGQRVKLKLWDTSGQGRFCTIFRSYSRGAQGVILVYDIANRWSFEGMDRWIKKIEEHAPGVPKILVGNRLHLAFKRQVPREQAQAYAERLGVTFFEVSPLCNFNIIESFTELARIVLLRHRLNWLGRPSKVLSLQDLCCRTIVSCTPVHLVDKLPLPIALRSHLKSFSMAKGLNARMMRGLSYSLTTSSTHKRSSLCKVKIVCPPQSPPKNCTRNSCKIS,Ras-related protein Rab-40A-like,May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.,"Stabilizes the protein and maintains its cytoplasmic localization. The report was based on association of a missense stability with the disease in a single family and in vitro localization studies. We found the stability variant by whole-exome sequencing in two patients; however, the diagnosis of MPS was excluded in both cases. Furthermore, screening of control DNA samples (n = 810) from a general Polish population, using allele-specific PCR and direct DNA sequencing for verification, identified stability in 8/405 males and 12/405 females. Low prevalence of the stability variant (0.53%) is typical for a rare genetic variation observed in symptomatic individuals. Our data support the role of RAB40AL mutation as a disease-causing change and the involvement of RAB40AL in MPS. Considering an decreasing use of next-generation sequencing in the clinical setting, our finding is of negligible diagnostic importance. The stability mutation in RAB40AL is reported to be associated with Martin-Pbst syndrome (MPS), an X-linked multisystem neurodevelopmental disorder. However, there is evidence supporting the pathogenic role of stability and it is being used as a primary for MPS diagnosis. This study provides further evidence for confirming the pathogenicity of RAB40AL stability. The mutation was not detected in two healthy males who are family members of stability carriers and in 0.28% of randomly selected Polish males with higher education. A variation, reported in ESP6500 in two healthy individuals, was not found on the Martin Pbst syndrome gene (RAB40AL). Based on XCI studies on the patient's mother, it is unlikely that RAB40AL escapes XCI, while still remaining balanced. In conclusion, the results of the present study indicated that the Martin Pbst syndrome is an X‑linked condition, which is probably caused by RAB40AL mutations.","Stabilizes the protein and maintains its cytoplasmic localization. The report was based on association of a missense stability with the disease in a single family and in vitro localization studies. We found the stability variant by whole-exome sequencing in two patients; however, the diagnosis of MPS was excluded in both cases. Furthermore, screening of control DNA samples (n = 810) from a general Polish population, using allele-specific PCR and direct DNA sequencing for verification, identified stability in 8/405 males and 12/405 females. Low prevalence of the stability variant (0.53%) is typical for a rare genetic variation observed in symptomatic individuals. Our data support the role of RAB40AL mutation as a disease-causing change and the involvement of RAB40AL in MPS. Considering an decreasing use of next-generation sequencing in the clinical setting, our finding is of negligible diagnostic importance. The stability mutation in RAB40AL is reported to be associated with Martin-Pbst syndrome (MPS), an X-linked multisystem neurodevelopmental disorder. However, there is evidence supporting the pathogenic role of stability and it is being used as a primary for MPS diagnosis. This study provides further evidence for confirming the pathogenicity of RAB40AL stability. The mutation was not detected in two healthy males who are family members of stability carriers and in 0.28% of randomly selected Polish males with higher education. A variation, reported in ESP6500 in two healthy individuals, was not found on the Martin Pbst syndrome gene (RAB40AL). Based on XCI studies on the patient's mother, it is unlikely that RAB40AL escapes XCI, while still remaining balanced. In conclusion, the results of the present study indicated that the Martin Pbst syndrome is an X‑linked condition, which is probably caused by RAB40AL mutations."
3075,3075,0,0,D0PV95-I434T,MESNQSNNGGSGNAALNRGGRYVPPHLRGGDGGAAAAASAGGDDRRGGAGGGGYRRGGGNSGGGGGGGYDRGYNDNRDDRDNRGGSGGYGRDRNYEDRGYNGGGGGGGNRGYNNNRGGGGGGYNRQDRGDGGSSNFSRGGYNNRDEGSDNRGSGRSYNNDRRDNGGDGQNTRWNNLDAPPSRGTSKWENRGARDERIEQELFSGQLSGINFDKYEEIPVEATGDDVPQPISLFSDLSLHEWIEENIKTAGYDRPTPVQKYSIPALQGGRDLMSCAQTGSGKTAAFLVPLVNAILQDGPDAVHRSVTSSGGRKKQYPSALVLSPTRELSLQIFNESRKFAYRTPITSALLYGGRENYKDQIHKLRLGCHILIATPGRLIDVMDQGLIGMEGCRYLVLDEADRMLDMGFEPQIRQIVECNRMPSKEERITAMFSATFPKEIQLLAQDFLKENYVFLAVGRVGSTSENIMQKIVWVEEDEKRSYLMDLLDATGDSSLTLVFVETKRGASDLAYYLNRQNYEVVTIHGDLKQFEREKHLDLFRTGTAPILVATAVAARGLDIPNVKHVINYDLPSDVDEYVHRIGRTGRVGNVGLATSFFNDKNRNIARELMDLIVEANQELPDWLEGMSGDMRSGGGYRGRGGRGNGQRFGGRDHRYQGGSGNGGGGNGGGGGFGGGGQRSGGGGGFQSGGGGGRQQQQQQRAQPQQDWWS,,-1.0,MESNQSNNGGSGNAALNRGGRYVPPHLRGGDGGAAAAASAGGDDRRGGAGGGGYRRGGGNSGGGGGGGYDRGYNDNRDDRDNRGGSGGYGRDRNYEDRGYNGGGGGGGNRGYNNNRGGGGGGYNRQDRGDGGSSNFSRGGYNNRDEGSDNRGSGRSYNNDRRDNGGDGQNTRWNNLDAPPSRGTSKWENRGARDERIEQELFSGQLSGINFDKYEEIPVEATGDDVPQPISLFSDLSLHEWIEENIKTAGYDRPTPVQKYSIPALQGGRDLMSCAQTGSGKTAAFLVPLVNAILQDGPDAVHRSVTSSGGRKKQYPSALVLSPTRELSLQIFNESRKFAYRTPITSALLYGGRENYKDQIHKLRLGCHILIATPGRLIDVMDQGLIGMEGCRYLVLDEADRMLDMGFEPQIRQIVECNRMPSKEERITAMFSAIFPKEIQLLAQDFLKENYVFLAVGRVGSTSENIMQKIVWVEEDEKRSYLMDLLDATGDSSLTLVFVETKRGASDLAYYLNRQNYEVVTIHGDLKQFEREKHLDLFRTGTAPILVATAVAARGLDIPNVKHVINYDLPSDVDEYVHRIGRTGRVGNVGLATSFFNDKNRNIARELMDLIVEANQELPDWLEGMSGDMRSGGGYRGRGGRGNGQRFGGRDHRYQGGSGNGGGGNGGGGGFGGGGQRSGGGGGFQSGGGGGRQQQQQQRAQPQQDWWS,ATP-dependent RNA helicase laf-1,"Multifunctional ATP-dependent RNA helicase. Plays a role in RNA remodeling, but is not required for RNA unwinding. Binds to RNA in a concentration-dependent manner to stimulate annealing between two complementary strands of RNA. This process is also dependent upon ATP; ATP reduces binding to RNA and subsequently diminishes RNA annealing. Involved in many cellular processes, which do not necessarily require its ATPase/helicase catalytic activities. Involved in the regulation of transcription and translation initiation. Involved in innate immunity. Involved in both stress and inflammatory responses. Promotes liquid-liquid phase separation of P granules, which is a process important for intracellular organization and stress granule assembly. Required for embryonic development. Plays a role in sexual cell fate determination by negatively regulating the translation of the sex determining protein tra-2. May play a protective role in the response to heat and oxidative stress. May negatively regulate extrinsic apoptotic signaling pathway via death domain receptors. May be involved in mitotic chromosome segregation.",Enhances q267; embryonic viable. The mutation affects a large region of the laf-1 protein far from helicase motif III. The phenotypes resulting from laf-1 mutations are due to gain or increase of laf-1 function. Laf-1 functions to positively regulate expression of the sex determination protein TRA-2.,Enhances q267; embryonic viable. The mutation affects a large region of the laf-1 protein far from helicase motif III. The phenotypes resulting from laf-1 mutations are due to gain or increase of laf-1 function. Laf-1 functions to positively regulate expression of the sex determination protein TRA-2.
3084,3084,0,0,Q6ZJK7-Y214H,MGSLDTNPTAFSAFPAGEGETFQPLNADDVRSYLHKAVDFISDYYKSVESMPVLPNVKPGYLQDELRASPPTYSAPFDVTMKELRSSVVPGMTHWASPNFFAFFPSTNSAAAIAGDLIASAMNTVGFTWQASPAATEMEVLALDWLAQMLNLPTSFMNRTGEGRGTGGGVILGTTSEAMLVTLVAARDAALRRSGSDGVAGLHRLAVYAADQTHSTFFKACRLAGFDPANIRSIPTGAETDYGLDPARLLEAMQADADAGLVPTYVCATVGTTSSNAVDPVGAVADVAARFAAWVHVDAAYAGSACICPEFRHHLDGVERVDSISMSPHKWLMTCLDCTCLYVRDTHRLTGSLETNPEYLKNHASDSGEVTDLKDMQVGVGRRFRGLKLWMVMRTYGVAKLQEHIRSDVAMAKVFEDLVRGDDRFEVVVPRNFALVCFRIRAGAGAAAATEEDADEANRELMERLNKTGKAYVAHTVVGGRFVLRFAVGSSLQEEHHVRSAWELIKKTTTEMMN,,-1.0,MGSLDTNPTAFSAFPAGEGETFQPLNADDVRSYLHKAVDFISDYYKSVESMPVLPNVKPGYLQDELRASPPTYSAPFDVTMKELRSSVVPGMTHWASPNFFAFFPSTNSAAAIAGDLIASAMNTVGFTWQASPAATEMEVLALDWLAQMLNLPTSFMNRTGEGRGTGGGVILGTTSEAMLVTLVAARDAALRRSGSDGVAGLHRLAVYAADQTYSTFFKACRLAGFDPANIRSIPTGAETDYGLDPARLLEAMQADADAGLVPTYVCATVGTTSSNAVDPVGAVADVAARFAAWVHVDAAYAGSACICPEFRHHLDGVERVDSISMSPHKWLMTCLDCTCLYVRDTHRLTGSLETNPEYLKNHASDSGEVTDLKDMQVGVGRRFRGLKLWMVMRTYGVAKLQEHIRSDVAMAKVFEDLVRGDDRFEVVVPRNFALVCFRIRAGAGAAAATEEDADEANRELMERLNKTGKAYVAHTVVGGRFVLRFAVGSSLQEEHHVRSAWELIKKTTTEMMN,Tryptophan decarboxylase 1,"Involved in serotonin biosynthesis. Catalyzes the decarboxylation of L-tryptophan to produce tryptamine, which is converted to serotonin by tryptamine 5-hydroxylase. May play a major role in serotonin biosynthesis during senescence. Accumulation of serotonin attenuates leaf senescence. Catalyzes the decarboxylation of 5-hydroxy-L-tryptophan to produce serotonin.","Increases enzymatic activity. The mutation in OsTDC affects PLP binding and proton transfer, leading to an increase in enzyme activity.","Increases enzymatic activity. The mutation in OsTDC affects PLP binding and proton transfer, leading to an increase in enzyme activity."
3087,3087,0,0,P0C6S4-A41D,QEEPCATGPCCRRCKFKRAGKVCRVARGDWNDDYCTGKSCDCPKNPWNG,,-1.0,QEEPCATGPCCRRCKFKRAGKVCRVARGDWNDDYCTGKSCACPKNPWNG,Disintegrin eristostatin,"Is a potent inhibitor of ADP-induced platelet aggregation. Acts by binding to alpha-IIb/beta-3 (ITGA2B/ITGB3) receptor on the platelet surface. Binds with the same high affinity to resting and activated platelets. Also binds the alpha-4/beta-1 (ITGA4/ITGB1) integrin. Is a potent inhibitor of human and murine melanoma metastases in mouse model systems, also due to the inhibition of binding between the alpha-4/beta-1 integrin and the vascular cell adhesion protein VCAM1. Reacts neither with the integrin alpha-V/beta-3 (ITGAV/ITGB3) vitronectin receptor nor with the integrin alpha-5/beta-1 (ITGA5/ITGB1) fibronectin receptor. Has no effect on cell proliferation or angiogenesis. Specifically inhibits cell migration on fibronectin, but not that on collagen IV or laminin. May involve fibronectin-binding integrins that mediate cell migration.","Loss of inhibition of wound closure, and of platelet aggregation. Gain of inhibition of wound closure, and of platelet aggregation.","Loss of inhibition of wound closure, and of platelet aggregation. Gain of inhibition of wound closure, and of platelet aggregation."
3095,3095,0,0,P43144-L146D,MNRPHSCLSFCWMYFAASGIRAVETANGKYAQKLFSDLFEDYSSALRPVEDTDAVLNVTLQVTLSQIKDMDERNQILTAYLWIRQTWHDAYLTWDRDQYDRLDSIRIPSDLVWRPDIVLYNKADDESSEPVNTNVVLRYDGLITWDSPAITKSSCVVDVTYFPFDSQQCNLTFGSWTYNGNQVDIFNALDSGDLSDFIEDVEWEVHGMPAVKNVISYGCCSEPYPDVTFTLLLKRRSSFYIVNLLIPCVLISFLAPLSFYLPAASGEKVSLGVTILLAMTVFQLMVAEIMPASENVPLIGKYYIATMALITASTALTIMVMNIHFCGAEARPVPHWAKVVILKYMSRILFVYDVGESCLSPRHSQEPEQVTKVYSKLPESNLKTSRNKDLSRKKEVRKLLKNDLGYQGGIPQNTDSYCARYEALTKNIEYIAKCLKDHKATNSKGSEWKKVAKVIDRFFMWIFFAMVFVMTVLIIARAD,,-1.0,MNRPHSCLSFCWMYFAASGIRAVETANGKYAQKLFSDLFEDYSSALRPVEDTDAVLNVTLQVTLSQIKDMDERNQILTAYLWIRQTWHDAYLTWDRDQYDRLDSIRIPSDLVWRPDIVLYNKADDESSEPVNTNVVLRYDGLITWLSPAITKSSCVVDVTYFPFDSQQCNLTFGSWTYNGNQVDIFNALDSGDLSDFIEDVEWEVHGMPAVKNVISYGCCSEPYPDVTFTLLLKRRSSFYIVNLLIPCVLISFLAPLSFYLPAASGEKVSLGVTILLAMTVFQLMVAEIMPASENVPLIGKYYIATMALITASTALTIMVMNIHFCGAEARPVPHWAKVVILKYMSRILFVYDVGESCLSPRHSQEPEQVTKVYSKLPESNLKTSRNKDLSRKKEVRKLLKNDLGYQGGIPQNTDSYCARYEALTKNIEYIAKCLKDHKATNSKGSEWKKVAKVIDRFFMWIFFAMVFVMTVLIIARAD,Neuronal acetylcholine receptor subunit alpha-9,"Ionotropic receptor with a probable role in the modulation of auditory stimuli. Agonist binding induces a conformation change that leads to the opening of an ion-conducting channel across the plasma membrane. The channel is permeable to a range of divalent cations including calcium, the influx of which may activate a potassium current which hyperpolarizes the cell membrane. In the ear, this leads to a reduction in basilar membrane motion, altering the activity of auditory nerve fibers and reducing the range of dynamic hearing. This may protect against acoustic trauma. May also regulate keratinocyte adhesion.",Complete gain of inhibition of the CHRNA9-CHRNA10 receptor by the alpha-conotoxin RgIA.,Complete gain of inhibition of the CHRNA9-CHRNA10 receptor by the alpha-conotoxin RgIA.
3097,3097,0,0,Q9GZM8-A198S,MDGEDIPDFSSLKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAVRERQQEVTRKSAPSSPTLDCEKMDSAVQASLSLPATPVGKGTENTFPSPKAIPNGFGTSPLTPSARISALNIVGDLLRKVGALESKLAACRNFAKDQASRKSYISGNVNCGVLNGNGTKFSRSGHTSFFDKGAVNGFDPAPPPPGLGSSRPSSAPGMLPLSV,,-1.0,MDGEDIPDFSSLKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAVRERQQEVTRKSAPSAPTLDCEKMDSAVQASLSLPATPVGKGTENTFPSPKAIPNGFGTSPLTPSARISALNIVGDLLRKVGALESKLAACRNFAKDQASRKSYISGNVNCGVLNGNGTKFSRSGHTSFFDKGAVNGFDPAPPPPGLGSSRPSSAPGMLPLSV,Nuclear distribution protein nudE-like 1,"Required for organization of the cellular microtubule array and microtubule anchoring at the centrosome. May regulate microtubule organization at least in part by targeting the microtubule severing protein KATNA1 to the centrosome. Also positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus ends. Required for several dynein- and microtubule-dependent processes such as the maintenance of Golgi integrity, the centripetal motion of secretory vesicles and the coupling of the nucleus and centrosome. Also required during brain development for the migration of newly formed neurons from the ventricular/subventricular zone toward the cortical plate. Plays a role, together with DISC1, in the regulation of neurite outgrowth. Required for mitosis in some cell types but appears to be dispensible for mitosis in cortical neuronal progenitors, which instead requires NDE1. Facilitates the polymerization of neurofilaments from the individual subunits NEFH and NEFL. Positively regulates lysosome peripheral distribution and ruffled border formation in osteoclasts.",Abrogates promotes mitotic phosphorylation; when associated with V-219; A-231; A-242 and V-245. Promotes phosphorylation by CDK5; when associated with A-219 and A-231. Mutation of S198 to alanine in Nudel enhances the poleward movement of dynein and the dynein-mediated transport of kinetochore proteins to spindle poles along microtubules in mitosis.,Abrogates promotes mitotic phosphorylation; when associated with V-219; A-231; A-242 and V-245. Promotes phosphorylation by CDK5; when associated with A-219 and A-231. Mutation of S198 to alanine in Nudel enhances the poleward movement of dynein and the dynein-mediated transport of kinetochore proteins to spindle poles along microtubules in mitosis.
3112,3112,0,0,O75143-D133R,METDLNSQDRKDLDKFIKFFALKTVQVIVQARLGEKICTRSSSSPTGSDWFNLAIKDIPEVTHEAKKALAGQLPAVGRSMCVEISLKTSEGDSMELEIWCLEMNEKCDKEIKVSYTVYNRLSLLLKSLLAITRVTPAYRLSRKQGHEYVILYRIYFGEVQLSGLGEGFQTVRVGTVGTPVGTITLSCAYRINLAFMSTRQFERTPPIMGIIIDHFVDRPYPSSSPMHPCNYRTAGEDTGVIYPSVEDSQEVCTTSFSTSPPSQLSSSRLSYQPAALGVGSADLAYPVVFAAGLNATHPHQLMVPGKEGGVPLAPNQPVHGTQADQERLATCTPSDRTHCAATPSSSEDTETVSNSSEGRASPHDVLETIFVRKVGAFVNKPINQVTLTSLDIPFAMFAPKNLELEDTDPMVNPPDSPETESPLQGSLHSDGSSGGSSGNTHDDFVMIDFKPAFSKDDILPMDLGTFYREFQNPPQLSSLSIDIGAQSMAEDLDSLPEKLAVHEKNVREFDAFVETLQ,,-1.0,METDLNSQDRKDLDKFIKFFALKTVQVIVQARLGEKICTRSSSSPTGSDWFNLAIKDIPEVTHEAKKALAGQLPAVGRSMCVEISLKTSEGDSMELEIWCLEMNEKCDKEIKVSYTVYNRLSLLLKSLLAITDVTPAYRLSRKQGHEYVILYRIYFGEVQLSGLGEGFQTVRVGTVGTPVGTITLSCAYRINLAFMSTRQFERTPPIMGIIIDHFVDRPYPSSSPMHPCNYRTAGEDTGVIYPSVEDSQEVCTTSFSTSPPSQLSSSRLSYQPAALGVGSADLAYPVVFAAGLNATHPHQLMVPGKEGGVPLAPNQPVHGTQADQERLATCTPSDRTHCAATPSSSEDTETVSNSSEGRASPHDVLETIFVRKVGAFVNKPINQVTLTSLDIPFAMFAPKNLELEDTDPMVNPPDSPETESPLQGSLHSDGSSGGSSGNTHDDFVMIDFKPAFSKDDILPMDLGTFYREFQNPPQLSSLSIDIGAQSMAEDLDSLPEKLAVHEKNVREFDAFVETLQ,Autophagy-related protein 13,"Autophagy factor required for autophagosome formation and mitophagy. Target of the TOR kinase signaling pathway that regulates autophagy through the control of the phosphorylation status of ATG13 and ULK1, and the regulation of the ATG13-ULK1-RB1CC1 complex. Through its regulation of ULK1 activity, plays a role in the regulation of the kinase activity of mTORC1 and cell proliferation.",Enables interaction with ATG101; when associated with H-127.,Enables interaction with ATG101; when associated with H-127.
3120,3120,0,0,D4GWB3-A34Q,MSESEQRHAHQCVSCGINIAGMSAATFKCPDCGQEISRCSKCRKQSNLYECPDCGFMGP,,-1.0,MSESEQRHAHQCVSCGINIAGMSAATFKCPDCGAEISRCSKCRKQSNLYECPDCGFMGP,Zinc finger protein HVO_2753,Zinc-binding protein. Binds 1 zinc ion. Required for swarming. Involved in biofilm formation.,Not able to complement the deletion mutant of this gene. Gain of swarming. Severe gain of structure and stability.,Not able to complement the deletion mutant of this gene. Gain of swarming. Severe gain of structure and stability.
3125,3125,0,0,P48058-D641N,MRIISRQIVLLFSGFWGLAMGAFPSSVQIGGLFIRNTDQEYTAFRLAIFLHNTSPNASEAPFNLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLTSFCSALHISLITPSFPTEGESQFVLQLRPSLRGALLSLLDHYEWNCFVFLYDTDRGYSILQAIMEKAGQNGWHVSAICVENFNDVSYRQLLEELDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLERFIHGGANVTGFQLVDFNTPMVIKLMDRWKKLDQREYPGSETPPKYTSALTYDGVLVMAETFRSLRRQKIDISRRGNAGDCLANPAAPWGQGIDMERTLKQVRIQGLTGNVQFDHYGRRVNYTMDVFELKSTGPRKVGYWNDMDKLVLIQDVPTLGNDTAAIENRTVVVTTIMESPYVMYKKNHEMFEGNDKYEGYCVDLASEIAKHIGIKYKIAIVPDGKYGARDADTKIWNGMVGELVYGKAEIAIAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHTEEPEDGKEGPSDQPPNEFGIFNSLWFSLGAFMQQGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYEKMWTYMRSAEPSVFTRTTAEGVARVRKSKGKFAFLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGVATPKGSSLRTPVNLAVLKLSEAGVLDKLKNKWWYDKGECGPKDSGSKDKTSALSLSNVAGVFYILVGGLGLAMLVALIEFCYKSRAEAKRMKLTFSEAIRNKARLSITGSVGENGRVLTPDCPKAVHTGTAIRQSSGLAVIASDLP,,-1.0,MRIISRQIVLLFSGFWGLAMGAFPSSVQIGGLFIRNTDQEYTAFRLAIFLHNTSPNASEAPFNLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLTSFCSALHISLITPSFPTEGESQFVLQLRPSLRGALLSLLDHYEWNCFVFLYDTDRGYSILQAIMEKAGQNGWHVSAICVENFNDVSYRQLLEELDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLERFIHGGANVTGFQLVDFNTPMVIKLMDRWKKLDQREYPGSETPPKYTSALTYDGVLVMAETFRSLRRQKIDISRRGNAGDCLANPAAPWGQGIDMERTLKQVRIQGLTGNVQFDHYGRRVNYTMDVFELKSTGPRKVGYWNDMDKLVLIQDVPTLGNDTAAIENRTVVVTTIMESPYVMYKKNHEMFEGNDKYEGYCVDLASEIAKHIGIKYKIAIVPDGKYGARDADTKIWNGMVGELVYGKAEIAIAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHTEEPEDGKEGPSDQPPNEFGIFNSLWFSLGAFMQQGCDISPRSLSGRIVGGVWWFFTLIIISSYTADLAAFLTVERMVSPIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYEKMWTYMRSAEPSVFTRTTAEGVARVRKSKGKFAFLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGVATPKGSSLRTPVNLAVLKLSEAGVLDKLKNKWWYDKGECGPKDSGSKDKTSALSLSNVAGVFYILVGGLGLAMLVALIEFCYKSRAEAKRMKLTFSEAIRNKARLSITGSVGENGRVLTPDCPKAVHTGTAIRQSSGLAVIASDLP,Glutamate receptor 4,"Receptor for glutamate that functions as ligand-gated ion channel in the central nervous system and plays an important role in excitatory synaptic transmission. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. In the presence of CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of glutamate.",Decrease in NEDSGA. The variant in GRIA4 leads to enhanced permeability.,Decrease in NEDSGA. The variant in GRIA4 leads to enhanced permeability.
3137,3137,0,0,Q9UH99-D609G,MSRRSQRLTRYSQGDDDGSSSSGGSSVAGSQSTLFKDSPLRTLKRKSSNMKRLSPAPQLGPSSDAHTSYYSESLVHESWFPPRSSLEELHGDANWGEDLRVRRRRGTGGSESSRASGLVGRKATEDFLGSSSGYSSEDDYVGYSDVDQQSSSSRLRSAVSRAGSLLWMVATSPGRLFRLLYWWAGTTWYRLTTAASLLDVFVLTRRFSSLKTFLWFLLPLLLLTCLTYGAWYFYPYGLQTFHPALVSWWAAKDSRRPDEGWEARDSSPHFQAEQRVMSRVHSLERRLEALAAEFSSNWQKEAMRLERLELRQGAPGQGGGGGLSHEDTLALLEGLVSRREAALKEDFRRETAARIQEELSALRAEHQQDSEDLFKKIVRASQESEARIQQLKSEWQSMTQESFQESSVKELRRLEDQLAGLQQELAALALKQSSVAEEVGLLPQQIQAVRDDVESQFPAWISQFLARGGGGRVGLLQREEMQAQLRELESKILTHVAEMQGKSAREAAASLSLTLQKEGVIGVTEEQVHHIVKQALQRYSEDRIGLADYALESGGASVISTRCSETYETKTALLSLFGIPLWYHSQSPRVILQPDVHPGNCWAFQGPQGFAVVRLSARIRPTAVTLEHVPKALSPNSTISSAPKDFAIFGFDEDLQQEGTLLGKFTYDQDGEPIQTFHFQAPTMATYQVVELRILTNWGHPEYTCIYRFRVHGEPAH,,-1.0,MSRRSQRLTRYSQGDDDGSSSSGGSSVAGSQSTLFKDSPLRTLKRKSSNMKRLSPAPQLGPSSDAHTSYYSESLVHESWFPPRSSLEELHGDANWGEDLRVRRRRGTGGSESSRASGLVGRKATEDFLGSSSGYSSEDDYVGYSDVDQQSSSSRLRSAVSRAGSLLWMVATSPGRLFRLLYWWAGTTWYRLTTAASLLDVFVLTRRFSSLKTFLWFLLPLLLLTCLTYGAWYFYPYGLQTFHPALVSWWAAKDSRRPDEGWEARDSSPHFQAEQRVMSRVHSLERRLEALAAEFSSNWQKEAMRLERLELRQGAPGQGGGGGLSHEDTLALLEGLVSRREAALKEDFRRETAARIQEELSALRAEHQQDSEDLFKKIVRASQESEARIQQLKSEWQSMTQESFQESSVKELRRLEDQLAGLQQELAALALKQSSVAEEVGLLPQQIQAVRDDVESQFPAWISQFLARGGGGRVGLLQREEMQAQLRELESKILTHVAEMQGKSAREAAASLSLTLQKEGVIGVTEEQVHHIVKQALQRYSEDRIGLADYALESGGASVISTRCSETYETKTALLSLFGIPLWYHSQSPRVILQPDVHPGNCWAFQGPQDFAVVRLSARIRPTAVTLEHVPKALSPNSTISSAPKDFAIFGFDEDLQQEGTLLGKFTYDQDGEPIQTFHFQAPTMATYQVVELRILTNWGHPEYTCIYRFRVHGEPAH,SUN domain-containing protein 2,"As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning. Specifically, SYNE2 and SUN2 assemble in arrays of transmembrane actin-associated nuclear (TAN) lines which are bound to F-actin cables and couple the nucleus to retrograde actin flow during actin-dependent nuclear movement. Required for interkinetic nuclear migration (INM) and essential for nucleokinesis and centrosome-nucleus coupling during radial neuronal migration in the cerebral cortex and during glial migration. Required for nuclear migration in retinal photoreceptor progenitors implicating association with cytoplasmic dynein-dynactin and kinesin motor complexes, and probably B-type lamins; SUN1 and SUN2 seem to act redundantly. The SUN1/2:KASH5 LINC complex couples telomeres to microtubules during meiosis; SUN1 and SUN2 seem to act at least partial redundantly. Anchors chromosome movement in the prophase of meiosis and is involved in selective gene expression of coding and non-coding RNAs needed for gametogenesis. Required for telomere attachment to nuclear envelope and gametogenesis. May also function on endocytic vesicles as a receptor for RAB5-GDP and participate in the activation of RAB5.",Increases interaction with SYNE2.,Increases interaction with SYNE2.
3143,3143,0,0,O50147-E125K,MIVVKVGGAEGINYEAVAKDAASLWKEGVKLLLVHGGSAETNKVAEALGHPPRFLTHPGGQVSRLTDRKTLEIFEMVYCGLVNKRLVELLQKEGANAIGLSGLDGRLFVGRRKTAVKYVENGKVKVHRGDYTGTVEEVNKALLDLLLQAGYLPVLTPPALSYENEAINTDGDQIAALLATLYGAEALVYLSNVPGLLARYPDEASLVREIPVERIEDPEYLALAQGRMKRKVMGAVEAVRGGVKRVVFADARVENPIRRALSGEGTVVR,,-1.0,MIVVKVGGAEGINYEAVAKDAASLWKEGVKLLLVHGGSAETNKVAEALGHPPRFLTHPGGQVSRLTDRKTLEIFEMVYCGLVNKRLVELLQKEGANAIGLSGLDGRLFVGRRKTAVKYVENGKVEVHRGDYTGTVEEVNKALLDLLLQAGYLPVLTPPALSYENEAINTDGDQIAALLATLYGAEALVYLSNVPGLLARYPDEASLVREIPVERIEDPEYLALAQGRMKRKVMGAVEAVRGGVKRVVFADARVENPIRRALSGEGTVVR,[LysW]-aminoadipate kinase,Catalyzes the phosphorylation of LysW-gamma-alpha-aminoadipate. Does not phosphorylate N-acetyl-glutamate.,Does bind LysW.,Does bind LysW.
3148,3148,0,0,Q84Y01-A70K,MASDAAAEPSSGVTHPPRYVIGYALAPKKQQSFIQPSLVAQAASRGMDLVPVDASQPLAEQGPFHLLIHKLYGDDWRAQLVAFAARHPAVPIVDPPHAIDRLHNRISMLQVVSELDHAADQDSTFGIPSQVVVYDAAALADFGLLAALRFPLIAKPLVADGTAKSHKMSLVYHREGLGKLRPPLVLQEFVNHGGVIFKVYVVGGHVTCVKRRSLPDVSPEDDASAQGSVSFSQVSNLPTERTAEEYYGEKSLEDAVVPPAAFINQIAGGLRRALGLQLFNFDMIRDVRAGDRYLVIDINYFPGYAKMPGYETVLTDFFWEMVHKDGVGNQQEEKGANHVVVK,,-1.0,MASDAAAEPSSGVTHPPRYVIGYALAPKKQQSFIQPSLVAQAASRGMDLVPVDASQPLAEQGPFHLLIHALYGDDWRAQLVAFAARHPAVPIVDPPHAIDRLHNRISMLQVVSELDHAADQDSTFGIPSQVVVYDAAALADFGLLAALRFPLIAKPLVADGTAKSHKMSLVYHREGLGKLRPPLVLQEFVNHGGVIFKVYVVGGHVTCVKRRSLPDVSPEDDASAQGSVSFSQVSNLPTERTAEEYYGEKSLEDAVVPPAAFINQIAGGLRRALGLQLFNFDMIRDVRAGDRYLVIDINYFPGYAKMPGYETVLTDFFWEMVHKDGVGNQQEEKGANHVVVK,Inositol-tetrakisphosphate 1-kinase 1,"Kinase that can phosphorylate various inositol polyphosphate such as Ins(3,4,5,6)P4 or Ins(1,3,4)P3 and participates in phytic acid biosynthesis in developing seeds. Phosphorylates Ins(3,4,5,6)P4 at position 1 to form Ins(1,3,4,5,6)P5. This reaction is thought to have regulatory importance, since Ins(3,4,5,6)P4 is an inhibitor of plasma membrane Ca(2+)-activated Cl(-) channels, while Ins(1,3,4,5,6)P5 is not. Also phosphorylates Ins(1,3,4)P3 on O-5 and O-6 to form Ins(1,3,4,6)P4, an essential molecule in the hexakisphosphate (InsP6) pathway. Also able to phosphorylate Ins(3,5,6)P3 but not Ins(1,4,5)P3, Ins(2,4,5)P3, Ins(1,3,4,6)P4 nor Ins(1,3,5,6)P4. Has higher specific activity on Ins(3,4,5,6)P4 than Ins(1,3,4)P3 and Ins(3,5,6)P3. Can also could use Ins(1,2,5,6)P4 as a substrate. Able to add a beta-phosphate to the 3 positions of Ins(1,2,3,4,5)P5 and to add beta-phosphate to InsP6 to yield 5-InsP7, thus exhibiting InsP6 kinase activity. Has also Ins(1,3,4,5,6)P5 phosphatase activity.",Strongly enhanced InsP6 kinase activity. The mutation in the ITPK protein causes a change in its catalytic activity.,Strongly enhanced InsP6 kinase activity. The mutation in the ITPK protein causes a change in its catalytic activity.
3168,3168,0,0,Q9Y3C8-Q23R,MADEATRRVVSEIPVLKTNAGPRDRELWVQRLKEEYQSLIRYVENNKNADNDWFRLESNKEGTRWFGKCWYIHDLLKYEFDIEFDIPITYPTTAPEIAVPELDGKTAKMYRGGKICLTDHFKPLWARNVPKFGLAHLMALGLGPWLAVEIPDLIQKGVIQHKEKCNQ,,-1.0,MADEATRRVVSEIPVLKTNAGPQDRELWVQRLKEEYQSLIRYVENNKNADNDWFRLESNKEGTRWFGKCWYIHDLLKYEFDIEFDIPITYPTTAPEIAVPELDGKTAKMYRGGKICLTDHFKPLWARNVPKFGLAHLMALGLGPWLAVEIPDLIQKGVIQHKEKCNQ,Ubiquitin-fold modifier-conjugating enzyme 1,E1-like enzyme which specifically catalyzes the second step in ufmylation. Accepts the ubiquitin-like modifier UFM1 from the E1 enzyme UBA5 and forms an intermediate with UFM1 via a thioester linkage. Ufmylation is involved in reticulophagy (also called ER-phagy) induced in response to endoplasmic reticulum stress.,"Increased ability to form thioester bond with UFM1; increased protein ufmylation. The mutation in UFM1 causes a pattern of widespread enhancement of cellular ufmylation, similar to that observed with UFM1 mutation.","Increased ability to form thioester bond with UFM1; increased protein ufmylation. The mutation in UFM1 causes a pattern of widespread enhancement of cellular ufmylation, similar to that observed with UFM1 mutation."
3170,3170,0,0,Q55650-R124K,MENNSLAPLRVGILGFGGLGQAAARLLAPKQEMKLVAVADRHGYLYDADGIDVDNAVQAYTQQGSVGKAKKGQMSEQSIEDLIGEGEVDGYFLALPNLPNTFMADVTRQFIASGWQGVLVDALKRTSAVEQLITLREDLAQAGITYMTGCGATPGLLTAAAAIASQSFQEIHQVKITFGVGIANWEAYRATIREDIAHMPGYNVDKAQAMTDAEVAALLDQTNGILALEDMEHADDIMLELAGICHRDQVTVGGVVDTRNPKKPLSTHVKITGRTFEGKISSHTFTLGDETSMAANVCGPAFGYLKAGYGLHRQGLKGLFTAADVMPKFVR,,-1.0,MENNSLAPLRVGILGFGGLGQAAARLLAPKQEMKLVAVADRHGYLYDADGIDVDNAVQAYTQQGSVGKAKKGQMSEQSIEDLIGEGEVDGYFLALPNLPNTFMADVTRQFIASGWQGVLVDALRRTSAVEQLITLREDLAQAGITYMTGCGATPGLLTAAAAIASQSFQEIHQVKITFGVGIANWEAYRATIREDIAHMPGYNVDKAQAMTDAEVAALLDQTNGILALEDMEHADDIMLELAGICHRDQVTVGGVVDTRNPKKPLSTHVKITGRTFEGKISSHTFTLGDETSMAANVCGPAFGYLKAGYGLHRQGLKGLFTAADVMPKFVR,,"A 'suicide' enzyme that participates in biotin synthesis. Catalyzes the formation of (S)-8-amino-7-oxononanoate (DAN-carbamic acid) from (7R,8S)-8-amino-7-(carboxyamino)nonanoate (DAN), a function equivalent to the cannonical BioA reaction and the first half-reaction of BioD. The cellular requirement for biotin is thought be low enough that this single turnover enzyme supplies a sufficient amount of the cofactor. Overall it catalyzes three reactions: formation of a covalent linkage with 8-amino-7-oxononanoate to yield a BioU-DAN conjugate at the epsilon-amino group of Lys124 of BioU using NAD(P)H, carboxylation of the conjugate to form BioU-DAN-carbamic acid, and release of DAN-carbamic acid using NAD(P)+. A coupled Synechocystis BioU/BioD assay produces dethiobiotin from DAN. Complements a bioA deletion in E.coli but not a bioD1 deletion.",Forms a BioU-DAN conjugate. This mutation enhances the formation of the covalent linkage with 8-amino-7-oxononanoate (AON) and enhances the catalytic activity of BioU in the biotin biosynthesis pathway.,Forms a BioU-DAN conjugate. This mutation enhances the formation of the covalent linkage with 8-amino-7-oxononanoate (AON) and enhances the catalytic activity of BioU in the biotin biosynthesis pathway.
3182,3182,0,0,Q9QPN3-D112L,MGGKWSKSSVVGWPAVRERMRRAEPAADGVGAVSRDLEKHGAITSSNTAATNADCAWLEAQEEEEVGFPVTPQVPLRPMTYKAAVDLSHFLKEKGGLEGLIHSQRRQDILDLWIYHTQGYFPDWQNYTPEPGVRYPLTFGWCYKLVPVEPDKVEEANKGENTRLLHPVSLHGMDDPEREVLEWRFDSRLAFHHVARELHPEY,,-1.0,MGGKWSKSSVVGWPAVRERMRRAEPAADGVGAVSRDLEKHGAITSSNTAATNADCAWLEAQEEEEVGFPVTPQVPLRPMTYKAAVDLSHFLKEKGGLEGLIHSQRRQDILDDWIYHTQGYFPDWQNYTPEPGVRYPLTFGWCYKLVPVEPDKVEEANKGENTRLLHPVSLHGMDDPEREVLEWRFDSRLAFHHVARELHPEY,Protein Nef,"Factor of infectivity and pathogenicity, required for optimal virus replication. Alters numerous pathways of T-lymphocyte function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity. Alters the functionality of other immunity cells, like dendritic cells, monocytes/macrophages and NK cells.In infected CD4(+) T-lymphocytes, down-regulates the surface MHC-I, mature MHC-II, CD4, CD28, CCR5 and CXCR4 molecules. Mediates internalization and degradation of host CD4 through the interaction of with the cytoplasmic tail of CD4, the recruitment of AP-2 (clathrin adapter protein complex 2), internalization through clathrin coated pits, and subsequent transport to endosomes and lysosomes for degradation. Diverts host MHC-I molecules to the trans-Golgi network-associated endosomal compartments by an endocytic pathway to finally target them for degradation. MHC-I down-regulation may involve AP-1 (clathrin adapter protein complex 1) or possibly Src family kinase-ZAP70/Syk-PI3K cascade recruited by PACS2. In consequence infected cells are masked for immune recognition by cytotoxic T-lymphocytes. Decreasing the number of immune receptors also prevents reinfection by more HIV particles (superinfection). Down-regulates host SERINC3 and SERINC5 thereby excluding these proteins from the viral particles. Virion infectivity is drastically higher when SERINC3 or SERINC5 are excluded from the viral envelope, because these host antiviral proteins impair the membrane fusion event necessary for subsequent virion penetration.Bypasses host T-cell signaling by inducing a transcriptional program nearly identical to that of anti-CD3 cell activation. Interaction with TCR-zeta chain up-regulates the Fas ligand (FasL). Increasing surface FasL molecules and decreasing surface MHC-I molecules on infected CD4(+) cells send attacking cytotoxic CD8+ T-lymphocytes into apoptosis.Plays a role in optimizing the host cell environment for viral replication without causing cell death by apoptosis. Protects the infected cells from apoptosis in order to keep them alive until the next virus generation is ready to strike. Inhibits the Fas and TNFR-mediated death signals by blocking MAP3K5/ASK1. Decreases the half-life of TP53, protecting the infected cell against p53-mediated apoptosis. Inhibits the apoptotic signals regulated by the Bcl-2 family proteins through the formation of a Nef/PI3-kinase/PAK2 complex that leads to activation of PAK2 and induces phosphorylation of host BAD.Extracellular Nef protein targets CD4(+) T-lymphocytes for apoptosis by interacting with CXCR4 surface receptors.",Complete gain of Nef-PTE1 interaction and Nef-induced CD4 up-modulation. The mutation in the Nef protein is involved in Nef-hTE interaction and Nef-induced CD4 upregulation. It is located on the oligomer interface and is in close proximity to the putative CD4 binding site.,Complete gain of Nef-PTE1 interaction and Nef-induced CD4 up-modulation. The mutation in the Nef protein is involved in Nef-hTE interaction and Nef-induced CD4 upregulation. It is located on the oligomer interface and is in close proximity to the putative CD4 binding site.
3208,3208,0,0,Q96C86-A205D,MADAAPQLGKRKRELDVEEAHAASTEEKEAGVGNGTCAPVRLPFSGFRLQKVLRESARDKIIFLHGKVNEASGDGDGEDAVVILEKTPFQVEQVAQLLTGSPELQLQFSNDIYSTYHLFPPRQLNDVKTTVVYPATEKHLQKYLRQDLRLIRETGDDYRNITLPHLESQSLSIQWVYNILDKKAEADRIVFENPDPSDGFVLIPDLKWNQQQLDDLYLIAICHRRGIRSLRDLTPEHLPLLRNILHQGQEAILQRYRMKGDHLRVYLHYLPSYYHLHVHFTALGFEAPGSGVERAHLLAEVIENLECDPRHYQQRTLTFALRADDPLLKLLQEAQQS,,-1.0,MADAAPQLGKRKRELDVEEAHAASTEEKEAGVGNGTCAPVRLPFSGFRLQKVLRESARDKIIFLHGKVNEASGDGDGEDAVVILEKTPFQVEQVAQLLTGSPELQLQFSNDIYSTYHLFPPRQLNDVKTTVVYPATEKHLQKYLRQDLRLIRETGDDYRNITLPHLESQSLSIQWVYNILDKKAEADRIVFENPDPSDGFVLIPALKWNQQQLDDLYLIAICHRRGIRSLRDLTPEHLPLLRNILHQGQEAILQRYRMKGDHLRVYLHYLPSYYHLHVHFTALGFEAPGSGVERAHLLAEVIENLECDPRHYQQRTLTFALRADDPLLKLLQEAQQS,m7GpppX diphosphatase,"Decapping scavenger enzyme that catalyzes the cleavage of a residual cap structure following the degradation of mRNAs by the 3'->5' exosome-mediated mRNA decay pathway. Hydrolyzes cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG) with up to 10 nucleotide substrates (small capped oligoribonucleotides) and specifically releases 5'-phosphorylated RNA fragments and 7-methylguanosine monophosphate (m7GMP). Cleaves cap analog structures like tri-methyl guanosine nucleoside triphosphate (m3(2,2,7)GpppG) with very poor efficiency. Does not hydrolyze unmethylated cap analog (GpppG) and shows no decapping activity on intact m7GpppG-capped mRNA molecules longer than 25 nucleotides. Does not hydrolyze 7-methylguanosine diphosphate (m7GDP) to m7GMP. May also play a role in the 5'->3 mRNA decay pathway; m7GDP, the downstream product released by the 5'->3' mRNA mediated decapping activity, may be also converted by DCPS to m7GMP. Binds to m7GpppG and strongly to m7GDP. Plays a role in first intron splicing of pre-mRNAs. Inhibits activation-induced cell death.",Increases decapping activity.,Increases decapping activity.
3227,3227,0,0,P05129-P119S,MAGLGPGVGDSEGGPRPLFCRKGALRQKVVHEVKSHKFTARFFKQPTFCSHCTDFIWGIGKQGLQCQVCSFVVHRRCHEFVTFECPGAGKGPQTDDPRNKHKFRLHSYSSPTFCDHCGSLLYGLVHQGMKCSCCEMNVHRRCVRSVPSLCGVDHTERRGRLQLEIRAPTADEIHVTVGEARNLIPMDPNGLSDPYVKLKLIPDPRNLTKQKTRTVKATLNPVWNETFVFNLKPGDVERRLSVEVWDWDRTSRNDFMGAMSFGVSELLKAPVDGWYKLLNQEEGEYYNVPVADADNCSLLQKFEACNYPLELYERVRMGPSSSPIPSPSPSPTDPKRCFFGASPGRLHISDFSFLMVLGKGSFGKVMLAERRGSDELYAIKILKKDVIVQDDDVDCTLVEKRVLALGGRGPGGRPHFLTQLHSTFQTPDRLYFVMEYVTGGDLMYHIQQLGKFKEPHAAFYAAEIAIGLFFLHNQGIIYRDLKLDNVMLDAEGHIKITDFGMCKENVFPGTTTRTFCGTPDYIAPEIIAYQPYGKSVDWWSFGVLLYEMLAGQPPFDGEDEEELFQAIMEQTVTYPKSLSREAVAICKGFLTKHPGKRLGSGPDGEPTIRAHGFFRWIDWERLERLEIPPPFRPRPCGRSGENFDKFFTRAAPALTPPDRLVLASIDQADFQGFTYVNPDFVHPDARSPTSPVPVPVM,,-1.0,MAGLGPGVGDSEGGPRPLFCRKGALRQKVVHEVKSHKFTARFFKQPTFCSHCTDFIWGIGKQGLQCQVCSFVVHRRCHEFVTFECPGAGKGPQTDDPRNKHKFRLHSYSSPTFCDHCGPLLYGLVHQGMKCSCCEMNVHRRCVRSVPSLCGVDHTERRGRLQLEIRAPTADEIHVTVGEARNLIPMDPNGLSDPYVKLKLIPDPRNLTKQKTRTVKATLNPVWNETFVFNLKPGDVERRLSVEVWDWDRTSRNDFMGAMSFGVSELLKAPVDGWYKLLNQEEGEYYNVPVADADNCSLLQKFEACNYPLELYERVRMGPSSSPIPSPSPSPTDPKRCFFGASPGRLHISDFSFLMVLGKGSFGKVMLAERRGSDELYAIKILKKDVIVQDDDVDCTLVEKRVLALGGRGPGGRPHFLTQLHSTFQTPDRLYFVMEYVTGGDLMYHIQQLGKFKEPHAAFYAAEIAIGLFFLHNQGIIYRDLKLDNVMLDAEGHIKITDFGMCKENVFPGTTTRTFCGTPDYIAPEIIAYQPYGKSVDWWSFGVLLYEMLAGQPPFDGEDEEELFQAIMEQTVTYPKSLSREAVAICKGFLTKHPGKRLGSGPDGEPTIRAHGFFRWIDWERLERLEIPPPFRPRPCGRSGENFDKFFTRAAPALTPPDRLVLASIDQADFQGFTYVNPDFVHPDARSPTSPVPVPVM,Protein kinase C gamma type,"Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays diverse roles in neuronal cells and eye tissues, such as regulation of the neuronal receptors GRIA4/GLUR4 and GRIN1/NMDAR1, modulation of receptors and neuronal functions related to sensitivity to opiates, pain and alcohol, mediation of synaptic function and cell survival after ischemia, and inhibition of gap junction activity after oxidative stress. Binds and phosphorylates GRIA4/GLUR4 glutamate receptor and regulates its function by increasing plasma membrane-associated GRIA4 expression. In primary cerebellar neurons treated with the agonist 3,5-dihyidroxyphenylglycine, functions downstream of the metabotropic glutamate receptor GRM5/MGLUR5 and phosphorylates GRIN1/NMDAR1 receptor which plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. May be involved in the regulation of hippocampal long-term potentiation (LTP), but may be not necessary for the process of synaptic plasticity. May be involved in desensitization of mu-type opioid receptor-mediated G-protein activation in the spinal cord, and may be critical for the development and/or maintenance of morphine-induced reinforcing effects in the limbic forebrain. May modulate the functionality of mu-type-opioid receptors by participating in a signaling pathway which leads to the phosphorylation and degradation of opioid receptors. May also contributes to chronic morphine-induced changes in nociceptive processing. Plays a role in neuropathic pain mechanisms and contributes to the maintenance of the allodynia pain produced by peripheral inflammation. Plays an important role in initial sensitivity and tolerance to ethanol, by mediating the behavioral effects of ethanol as well as the effects of this drug on the GABA(A) receptors. During and after cerebral ischemia modulate neurotransmission and cell survival in synaptic membranes, and is involved in insulin-induced inhibition of necrosis, an important mechanism for minimizing ischemic injury. Required for the elimination of multiple climbing fibers during innervation of Purkinje cells in developing cerebellum. Is activated in lens epithelial cells upon hydrogen peroxide treatment, and phosphorylates connexin-43 (GJA1/CX43), resulting in disassembly of GJA1 gap junction plaques and inhibition of gap junction activity which could provide a protective effect against oxidative stress. Phosphorylates p53/TP53 and promotes p53/TP53-dependent apoptosis in response to DNA damage. Involved in the phase resetting of the cerebral cortex circadian clock during temporally restricted feeding. Stabilizes the core clock component BMAL1 by interfering with its ubiquitination, thus suppressing its degradation, resulting in phase resetting of the cerebral cortex clock.",Increases staining for PKC gamma in Purkinje cells.,Increases staining for PKC gamma in Purkinje cells.
3244,3244,0,0,P16473-T553A,MRPADLLQLVLLLDLPRDLGGMGCSSPPCECHQEEDFRVTCKDIQRIPSLPPSTQTLKLIETHLRTIPSHAFSNLPNISRIYVSIDVTLQQLESHSFYNLSKVTHIEIRNTRNLTYIDPDALKELPLLKFLGIFNTGLKMFPDLTKVYSTDIFFILEITDNPYMTSIPVNAFQGLCNETLTLKLYNNGFTSVQGYAFNGTKLDAVYLNKNKYLTVIDKDAFGGVYSGPSLLDVSQTSVTALPSKGLEHLKELIARNTWTLKKLPLSLSFLHLTRADLSYPSHCCAFKNQKKIRGILESLMCNESSMQSLRQRKSVNALNSPLHQEYEENLGDSIVGYKEKSKFQDTHNNAHYYVFFEEQEDEIIGFGQELKNPQEETLQAFDSHYDYTICGDSEDMVCTPKSDEFNPCEDIMGYKFLRIVVWFVSLLALLGNVFVLLILLTSHYKLNVPRFLMCNLAFADFCMGMYLLLIASVDLYTHSEYYNHAIDWQTGPGCNTAGFFTVFASELSVYTLTVITLERWYAITFAMRLDRKIRLRHACAIMVGGWVCCFLLALLPLVGISSYAKVSICLPMDTETPLALAYIVFVLTLNIVAFVIVCCCYVKIYITVRNPQYNPGDKDTKIAKRMAVLIFTDFICMAPISFYALSAILNKPLITVSNSKILLVLFYPLNSCANPFLYAIFTKAFQRDVFILLSKFGICKRQAQAYRGQRVPPKNSTDIQVQKVTHDMRQGLHNMEDVYELIENSHLTPKKQGQISEEYMQTVL,,-1.0,MRPADLLQLVLLLDLPRDLGGMGCSSPPCECHQEEDFRVTCKDIQRIPSLPPSTQTLKLIETHLRTIPSHAFSNLPNISRIYVSIDVTLQQLESHSFYNLSKVTHIEIRNTRNLTYIDPDALKELPLLKFLGIFNTGLKMFPDLTKVYSTDIFFILEITDNPYMTSIPVNAFQGLCNETLTLKLYNNGFTSVQGYAFNGTKLDAVYLNKNKYLTVIDKDAFGGVYSGPSLLDVSQTSVTALPSKGLEHLKELIARNTWTLKKLPLSLSFLHLTRADLSYPSHCCAFKNQKKIRGILESLMCNESSMQSLRQRKSVNALNSPLHQEYEENLGDSIVGYKEKSKFQDTHNNAHYYVFFEEQEDEIIGFGQELKNPQEETLQAFDSHYDYTICGDSEDMVCTPKSDEFNPCEDIMGYKFLRIVVWFVSLLALLGNVFVLLILLTSHYKLNVPRFLMCNLAFADFCMGMYLLLIASVDLYTHSEYYNHAIDWQTGPGCNTAGFFTVFASELSVYTLTVITLERWYAITFAMRLDRKIRLRHACAIMVGGWVCCFLLTLLPLVGISSYAKVSICLPMDTETPLALAYIVFVLTLNIVAFVIVCCCYVKIYITVRNPQYNPGDKDTKIAKRMAVLIFTDFICMAPISFYALSAILNKPLITVSNSKILLVLFYPLNSCANPFLYAIFTKAFQRDVFILLSKFGICKRQAQAYRGQRVPPKNSTDIQVQKVTHDMRQGLHNMEDVYELIENSHLTPKKQGQISEEYMQTVL,Thyrotropin receptor,Receptor for the thyroid-stimulating hormone (TSH) or thyrotropin. Also acts as a receptor for the heterodimeric glycoprotein hormone (GPHA2:GPHB5) or thyrostimulin. The activity of this receptor is mediated by G proteins which activate adenylate cyclase. Plays a central role in controlling thyroid cell metabolism.,High expression of the thyrotropin receptor at the cell surface compared to the wild-type receptor. The large amount of mutated receptor expressed at the surface bound thyrotropin with normal affinity and responded in terms of cAMP production.,High expression of the thyrotropin receptor at the cell surface compared to the wild-type receptor. The large amount of mutated receptor expressed at the surface bound thyrotropin with normal affinity and responded in terms of cAMP production.
3246,3246,0,0,Q9FL28-R318G,MKLLSKTFLILTLTFFFFGIALAKQSFEPEIEALKSFKNGISNDPLGVLSDWTIIGSLRHCNWTGITCDSTGHVVSVSLLEKQLEGVLSPAIANLTYLQVLDLTSNSFTGKIPAEIGKLTELNQLILYLNYFSGSIPSGIWELKNIFYLDLRNNLLSGDVPEEICKTSSLVLIGFDYNNLTGKIPECLGDLVHLQMFVAAGNHLTGSIPVSIGTLANLTDLDLSGNQLTGKIPRDFGNLLNLQSLVLTENLLEGDIPAEIGNCSSLVQLELYDNQLTGKIPAELGNLVQLQALRIYKNKLTSSIPSSLFRLTQLTHLGLSENHLVGPISEEIGFLESLEVLTLHSNNFTGEFPQSITNLRNLTVLTVGFNNISGELPADLGLLTNLRNLSAHDNLLTGPIPSSISNCTGLKLLDLSHNQMTGEIPRGFGRMNLTFISIGRNHFTGEIPDDIFNCSNLETLSVADNNLTGTLKPLIGKLQKLRILQVSYNSLTGPIPREIGNLKDLNILYLHSNGFTGRIPREMSNLTLLQGLRMYSNDLEGPIPEEMFDMKLLSVLDLSNNKFSGQIPALFSKLESLTYLSLQGNKFNGSIPASLKSLSLLNTFDISDNLLTGTIPGELLASLKNMQLYLNFSNNLLTGTIPKELGKLEMVQEIDLSNNLFSGSIPRSLQACKNVFTLDFSQNNLSGHIPDEVFQGMDMIISLNLSRNSFSGEIPQSFGNMTHLVSLDLSSNNLTGEIPESLANLSTLKHLKLASNNLKGHVPESGVFKNINASDLMGNTDLCGSKKPLKPCTIKQKSSHFSKRTRVILIILGSAAALLLVLLLVLILTCCKKKEKKIENSSESSLPDLDSALKLKRFEPKELEQATDSFNSANIIGSSSLSTVYKGQLEDGTVIAVKVLNLKEFSAESDKWFYTEAKTLSQLKHRNLVKILGFAWESGKTKALVLPFMENGNLEDTIHGSAAPIGSLLEKIDLCVHIASGIDYLHSGYGFPIVHCDLKPANILLDSDRVAHVSDFGTARILGF,,-1.0,MKLLSKTFLILTLTFFFFGIALAKQSFEPEIEALKSFKNGISNDPLGVLSDWTIIGSLRHCNWTGITCDSTGHVVSVSLLEKQLEGVLSPAIANLTYLQVLDLTSNSFTGKIPAEIGKLTELNQLILYLNYFSGSIPSGIWELKNIFYLDLRNNLLSGDVPEEICKTSSLVLIGFDYNNLTGKIPECLGDLVHLQMFVAAGNHLTGSIPVSIGTLANLTDLDLSGNQLTGKIPRDFGNLLNLQSLVLTENLLEGDIPAEIGNCSSLVQLELYDNQLTGKIPAELGNLVQLQALRIYKNKLTSSIPSSLFRLTQLTHLRLSENHLVGPISEEIGFLESLEVLTLHSNNFTGEFPQSITNLRNLTVLTVGFNNISGELPADLGLLTNLRNLSAHDNLLTGPIPSSISNCTGLKLLDLSHNQMTGEIPRGFGRMNLTFISIGRNHFTGEIPDDIFNCSNLETLSVADNNLTGTLKPLIGKLQKLRILQVSYNSLTGPIPREIGNLKDLNILYLHSNGFTGRIPREMSNLTLLQGLRMYSNDLEGPIPEEMFDMKLLSVLDLSNNKFSGQIPALFSKLESLTYLSLQGNKFNGSIPASLKSLSLLNTFDISDNLLTGTIPGELLASLKNMQLYLNFSNNLLTGTIPKELGKLEMVQEIDLSNNLFSGSIPRSLQACKNVFTLDFSQNNLSGHIPDEVFQGMDMIISLNLSRNSFSGEIPQSFGNMTHLVSLDLSSNNLTGEIPESLANLSTLKHLKLASNNLKGHVPESGVFKNINASDLMGNTDLCGSKKPLKPCTIKQKSSHFSKRTRVILIILGSAAALLLVLLLVLILTCCKKKEKKIENSSESSLPDLDSALKLKRFEPKELEQATDSFNSANIIGSSSLSTVYKGQLEDGTVIAVKVLNLKEFSAESDKWFYTEAKTLSQLKHRNLVKILGFAWESGKTKALVLPFMENGNLEDTIHGSAAPIGSLLEKIDLCVHIASGIDYLHSGYGFPIVHCDLKPANILLDSDRVAHVSDFGTARILGF,LRR receptor-like serine/threonine-protein kinase FLS2,"Constitutes the pattern-recognition receptor (PPR) that determines the specific perception of flagellin (flg22), a potent elicitor of the defense response to pathogen-associated molecular patterns (PAMPs). Flagellin-binding to the receptor is the first step to initiate the innate immune MAP kinase signaling cascade (MEKK1, MKK4/MKK5 and MPK3/MPK6), resulting in enhanced resistance against pathogens. Binding to the effector AvrPto1 or to the phosphatase hopD2 from Pseudomonas syringae blocks the downstream plant immune response.",Enhances flagellin-binding in fls2-24. The point mutation of the fls2-17 allele lies in the kinase domain. A kinase carrying this missense mutation exhibited enhanced autophosphorylation activity when expressed in Escherichia coli. This indicates that kinase activity is essential for binding and probably enhances the stability of the flagellin receptor complex. The mutation in FLS2 enhances the recognition of the C-terminal segment of flg22.,Enhances flagellin-binding in fls2-24. The point mutation of the fls2-17 allele lies in the kinase domain. A kinase carrying this missense mutation exhibited enhanced autophosphorylation activity when expressed in Escherichia coli. This indicates that kinase activity is essential for binding and probably enhances the stability of the flagellin receptor complex. The mutation in FLS2 enhances the recognition of the C-terminal segment of flg22.
3253,3253,0,0,P0A9P6-Q157E,MAEFETTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLQNLDPELKAPQILVLAPTRELAVQVAEAMTDFSKHMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRKNEALVRFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPEVELPNAELLGKRRLEKFAAKVQQQLESSDLDQYRALLSKIQPTAEGEELDLETLAAALLKMAQGERTLIVPPDAPMRPKREFRDRDDRGPRDRNDRGPRGDREDRPRRERRDVGDMQLYRIEVGRDDGVEVRHIVGAIANEGDISSRYIGNIKLFASHSTIELPKGMPGEVLQHFTRTRILNKPMNMQLLGDAQPHTGGERRGGGRGFGGERREGGRNFSGERREGGRGDGRRFSGERREGRAPRRDDSTGRRRFGGDA,,-1.0,MAEFETTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLQNLDPELKAPQILVLAPTRELAVQVAEAMTDFSKHMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDQADEMLRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRKNEALVRFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPEVELPNAELLGKRRLEKFAAKVQQQLESSDLDQYRALLSKIQPTAEGEELDLETLAAALLKMAQGERTLIVPPDAPMRPKREFRDRDDRGPRDRNDRGPRGDREDRPRRERRDVGDMQLYRIEVGRDDGVEVRHIVGAIANEGDISSRYIGNIKLFASHSTIELPKGMPGEVLQHFTRTRILNKPMNMQLLGDAQPHTGGERRGGGRGFGGERREGGRNFSGERREGGRGDGRRFSGERREGRAPRRDDSTGRRRFGGDA,ATP-dependent RNA helicase DeaD,"DEAD-box RNA helicase involved in various cellular processes at low temperature, including ribosome biogenesis, mRNA degradation and translation initiation. Exhibits RNA-stimulated ATP hydrolysis and RNA unwinding activity at low temperature. Involved in 50S ribosomal subunit assembly, acting after SrmB, and could also play a role in the biogenesis of the 30S ribosomal subunit. In addition, is involved in mRNA decay, via formation of a cold-shock degradosome with RNase E. Also stimulates translation of some mRNAs, probably at the level of initiation.","Drastically enhances ATPase activity, significantly increases helicase activity. In vivo acts as a dominant positive mutation in the presence of the wild-type protein at low temperature. The DQAD variant of CsdA (E-157-->Q) had detectible helicase and ATPase activity at 15 degrees C in vitro. A plasmid encoding the DQAD variant was also able to suppress the impaired growth of the csdA null mutant at 15 degrees C.","Drastically enhances ATPase activity, significantly increases helicase activity. In vivo acts as a dominant positive mutation in the presence of the wild-type protein at low temperature. The DQAD variant of CsdA (E-157-->Q) had detectible helicase and ATPase activity at 15 degrees C in vitro. A plasmid encoding the DQAD variant was also able to suppress the impaired growth of the csdA null mutant at 15 degrees C."
3261,3261,0,0,Q99426-A128S,MEVTGVSAPTVTVFISSSLNTFRSEKRYSRSLTIAEFKCKLELLVGSPASCMELELYGVDDKFYSKLDQEDALLGSYPVDDGCRIHVIDHSGARLGEYEDVSRVEKYTISQEAYDQRQDTVRSFLKRSKLGRYNEEERAQQEAEAAQRLAEEKAQASSIPVGSRCEVRAAGQSPRRGTVMYVGLTDFKPGYWIGVRYDEPLGKNDGSVNGKRYFECQAKYGAFVKPAVVTVGDFPEEDYGLDEI,,-1.0,MEVTGVSAPTVTVFISSSLNTFRSEKRYSRSLTIAEFKCKLELLVGSPASCMELELYGVDDKFYSKLDQEDALLGSYPVDDGCRIHVIDHSGARLGEYEDVSRVEKYTISQEAYDQRQDTVRSFLKRAKLGRYNEEERAQQEAEAAQRLAEEKAQASSIPVGSRCEVRAAGQSPRRGTVMYVGLTDFKPGYWIGVRYDEPLGKNDGSVNGKRYFECQAKYGAFVKPAVVTVGDFPEEDYGLDEI,Tubulin-folding cofactor B,Binds to alpha-tubulin folding intermediates after their interaction with cytosolic chaperonin in the pathway leading from newly synthesized tubulin to properly folded heterodimer. Involved in regulation of tubulin heterodimer dissociation. May function as a negative regulator of axonal growth.,Increased phosphorylation by PAK1. Increased microtubule polymerization and gain of phosphorylation by PAK1; when associated with A-65. Pak1 phosphorylation is unnecessary for normal TCoB function. Overexpression of TCoB dramatically decreased the number of gamma-tubulin-containing microtubule-organizing centers.,Increased phosphorylation by PAK1. Increased microtubule polymerization and gain of phosphorylation by PAK1; when associated with A-65. Pak1 phosphorylation is unnecessary for normal TCoB function. Overexpression of TCoB dramatically decreased the number of gamma-tubulin-containing microtubule-organizing centers.
3266,3266,0,0,O35543-I104W,MPNYKLLYFNMRGRAEIIRYIFAYLDIKYEDHRIEQADWPKIKPTLPFGKIPVLEVEGLTLHQSLAIARYLTKNTDLAGKTELEQCQVDAVVDTLDDFMSLFPWAEENQDLKERTFNDLLTRQAPHLLKDLDTYLGDKEWFIGNYVTWADFYWDICSTTLLVLKPDLLGIYPRLVSLRNKVQAIPAISAWILKRPQTKL,,-1.0,MPNYKLLYFNMRGRAEIIRYIFAYLDIKYEDHRIEQADWPKIKPTLPFGKIPVLEVEGLTLHQSLAIARYLTKNTDLAGKTELEQCQVDAVVDTLDDFMSLFPIAEENQDLKERTFNDLLTRQAPHLLKDLDTYLGDKEWFIGNYVTWADFYWDICSTTLLVLKPDLLGIYPRLVSLRNKVQAIPAISAWILKRPQTKL,Hematopoietic prostaglandin D synthase,"Bifunctional enzyme which catalyzes both the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation, and the conjugation of glutathione with a wide range of aryl halides and organic isothiocyanates. Also exhibits low glutathione-peroxidase activity towards cumene hydroperoxide.",No significant effect on protein expression levels. Enhances both prostaglandin D synthase and glutathione-conjugating activities. showed major but insignificant differences in their far-UV circular dichroism spectra from the wild-type enzyme. is negligible for structural integrity of the catalytic center for GST and PGDS activities.,No significant effect on protein expression levels. Enhances both prostaglandin D synthase and glutathione-conjugating activities. showed major but insignificant differences in their far-UV circular dichroism spectra from the wild-type enzyme. is negligible for structural integrity of the catalytic center for GST and PGDS activities.
3269,3269,0,0,P32055-A187R,MSKQRVFIAGHRGMVGSAIRRQLEQRGDVELVLRTRDELNLLDSRAVHDFFASERIDQVYLAAAKVGGIVANNTYPADFIYQNMMIESNIIHAAHQNDVNKLLFLGSSCIYPKLAKQPMAESELLQGTLEPTNEPYAIAKIAGIKLCESYNRQYGRDYRSVMPTNLYGPHDNFHPSNSHVIPALLRRFHEATAQNAPDVVVWGSGTPMREFLHVDDMAAASIHVMELAHEVWLENTQPMLSHINVGTGVDCTIRELAQTIAKVVGYKGRVVFDASKPDGTPRKLLDVTRLHQLGWYHEISLEAGLASTYQWFLENQDRFRG,,-1.0,MSKQRVFIAGHRGMVGSAIRRQLEQRGDVELVLRTRDELNLLDSRAVHDFFASERIDQVYLAAAKVGGIVANNTYPADFIYQNMMIESNIIHAAHQNDVNKLLFLGSSCIYPKLAKQPMAESELLQGTLEPTNEPYAIAKIAGIKLCESYNRQYGRDYRSVMPTNLYGPHDNFHPSNSHVIPALLRAFHEATAQNAPDVVVWGSGTPMREFLHVDDMAAASIHVMELAHEVWLENTQPMLSHINVGTGVDCTIRELAQTIAKVVGYKGRVVFDASKPDGTPRKLLDVTRLHQLGWYHEISLEAGLASTYQWFLENQDRFRG,GDP-L-fucose synthase,"Catalyzes the two-step NADP-dependent conversion of GDP-4-dehydro-6-deoxy-D-mannose to GDP-fucose, involving an epimerase and a reductase reaction.",Increases affinity for the substrate GDP-4-keto-6-deoxymannose.,Increases affinity for the substrate GDP-4-keto-6-deoxymannose.
3276,3276,0,0,Q9GZM8-E242S,MDGEDIPDFSSLKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAVRERQQEVTRKSAPSSPTLDCEKMDSAVQASLSLPATPVGKGTENTFPSPKAIPNGFGTSPLTPSARISALNIVGDLLRKVGALESKLAACRNFAKDQASRKSYISGNVNCGVLNGNGTKFSRSGHTSFFDKGAVNGFDPAPPPPGLGSSRPSSAPGMLPLSV,,-1.0,MDGEDIPDFSSLKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAVRERQQEVTRKSAPSSPTLDCEKMDSAVQASLSLPATPVGKGTENTFPSPKAIPNGFGTEPLTPSARISALNIVGDLLRKVGALESKLAACRNFAKDQASRKSYISGNVNCGVLNGNGTKFSRSGHTSFFDKGAVNGFDPAPPPPGLGSSRPSSAPGMLPLSV,Nuclear distribution protein nudE-like 1,"Required for organization of the cellular microtubule array and microtubule anchoring at the centrosome. May regulate microtubule organization at least in part by targeting the microtubule severing protein KATNA1 to the centrosome. Also positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus ends. Required for several dynein- and microtubule-dependent processes such as the maintenance of Golgi integrity, the centripetal motion of secretory vesicles and the coupling of the nucleus and centrosome. Also required during brain development for the migration of newly formed neurons from the ventricular/subventricular zone toward the cortical plate. Plays a role, together with DISC1, in the regulation of neurite outgrowth. Required for mitosis in some cell types but appears to be dispensible for mitosis in cortical neuronal progenitors, which instead requires NDE1. Facilitates the polymerization of neurofilaments from the individual subunits NEFH and NEFL. Positively regulates lysosome peripheral distribution and ruffled border formation in osteoclasts.",Impairs interaction with PAFAH1B1 and enhances centrosomal localization; when associated with E-198; E-219; E-231 and E-245. Dephosphorylation of Nudel at S242 regulates its cell-cycle-dependent distribution and impairs its binding to Lis1. This dephosphorylation is likely inhibited by Cdc2 and Erk1/2.,Impairs interaction with PAFAH1B1 and enhances centrosomal localization; when associated with E-198; E-219; E-231 and E-245. Dephosphorylation of Nudel at S242 regulates its cell-cycle-dependent distribution and impairs its binding to Lis1. This dephosphorylation is likely inhibited by Cdc2 and Erk1/2.
3278,3278,0,0,P0AFI2-P84E,MSDMAERLALHEFTENAYLNYSMYVIMDRALPFIGDGLKPVQRRIVYAMSELGLNASAKFKKSARTVGDVLGKYHPHGDSACYEAMVLMAQPFSYRYPLVDGQGNWGAPDDPKSFAAMRYTESRLSKYSELLLSELGQGTADWVPNFDGTLQEPKMLPARLPNILLNGTTGIAVGMATDIPPHNLREVAQAAIALIDQPKTTLDQLLDIVQGPDYPTEAEIITSRAEIRKIYENGRGSVRMRAVWKKEDGAVVISALPHQVSGARVLEQIAAQMRNKKLPMVDDLRDESDHENPTRLVIVPRSNRVDMDQVMNHLFATTDLEKSYRINLNMIGLDGRPAVKNLLEILSEWLVFRRDTVRRRLNYRLEKVLKRLHILEGLLVAFLNIDEVIEIIRNEDEPKPALMSRFGLTETQAEAILELKLRHLAKLEEMKIRGEQSELEKERDQLQGILASERKMNNLLKKELQADAQAYGDDRRSPLQEREEAKAMSEHDMLPSEPVTIVLSQMGWVRSAKGHDIDAPGLNYKAGDSFKAAVKGKSNQPVVFVDSTGRSYAIDPITLPSARGQGEPLTGKLTLPPGATVDHMLMESDDQKLLMASDAGYGFVCTFNDLVARNRAGKALITLPENAHVMPPVVIEDASDMLLAITQAGRMLMFPVSDLPQLSKGKGNKIINIPSAEAARGEDGLAQLYVLPPQSTLTIHVGKRKIKLRPEELQKVTGERGRRGTLMRGLQRIDRVEIDSPRRASSGDSEE,,-1.0,MSDMAERLALHEFTENAYLNYSMYVIMDRALPFIGDGLKPVQRRIVYAMSELGLNASAKFKKSARTVGDVLGKYHPHGDSACYPAMVLMAQPFSYRYPLVDGQGNWGAPDDPKSFAAMRYTESRLSKYSELLLSELGQGTADWVPNFDGTLQEPKMLPARLPNILLNGTTGIAVGMATDIPPHNLREVAQAAIALIDQPKTTLDQLLDIVQGPDYPTEAEIITSRAEIRKIYENGRGSVRMRAVWKKEDGAVVISALPHQVSGARVLEQIAAQMRNKKLPMVDDLRDESDHENPTRLVIVPRSNRVDMDQVMNHLFATTDLEKSYRINLNMIGLDGRPAVKNLLEILSEWLVFRRDTVRRRLNYRLEKVLKRLHILEGLLVAFLNIDEVIEIIRNEDEPKPALMSRFGLTETQAEAILELKLRHLAKLEEMKIRGEQSELEKERDQLQGILASERKMNNLLKKELQADAQAYGDDRRSPLQEREEAKAMSEHDMLPSEPVTIVLSQMGWVRSAKGHDIDAPGLNYKAGDSFKAAVKGKSNQPVVFVDSTGRSYAIDPITLPSARGQGEPLTGKLTLPPGATVDHMLMESDDQKLLMASDAGYGFVCTFNDLVARNRAGKALITLPENAHVMPPVVIEDASDMLLAITQAGRMLMFPVSDLPQLSKGKGNKIINIPSAEAARGEDGLAQLYVLPPQSTLTIHVGKRKIKLRPEELQKVTGERGRRGTLMRGLQRIDRVEIDSPRRASSGDSEE,DNA topoisomerase 4 subunit A,Topoisomerase IV is essential for chromosome segregation; it is the principal protein responsible for decatenating newly replicated chromosomes. It relaxes supercoiled DNA. MukB stimulates the relaxation activity of topoisomerase IV and also has a modest effect on decatenation.,"Confers susceptibility to quinolones. The mutation confers susceptibility to Topo IV without affecting its catalytic activity. The mutation promotes the formation of covalent Topo IV-DNA complexes when Mg(2+), but not Ca(2+), is used as a cofactor.","Confers susceptibility to quinolones. The mutation confers susceptibility to Topo IV without affecting its catalytic activity. The mutation promotes the formation of covalent Topo IV-DNA complexes when Mg(2+), but not Ca(2+), is used as a cofactor."
3279,3279,0,0,P29506-S188G,MIGALHACVDAEPKIINDIWADFWKSQINSVLLNPSDGSETYLASDNGKSTSSREQSTSPDDDNLLMNEDDGIALEDDNDTGESAAKRRRTRTNFSGWQLEELESAFEASHYPDVFMREALAMRLDLLESRVQVWFQNRRAKWRKREQNRNGSSEIKKDDGEQMETKALPTFPFSIDSILAVSRVPRGRRPNAKYPRVQACKNLSPFMIPLFPITQPGGNVIREKSPPLPTQQSQIVATNALTTVAELLKSV,,-1.0,MIGALHACVDAEPKIINDIWADFWKSQINSVLLNPSDGSETYLASDNGKSTSSREQSTSPDDDNLLMNEDDGIALEDDNDTGESAAKRRRTRTNFSGWQLEELESAFEASHYPDVFMREALAMRLDLLESRVQVWFQNRRAKWRKREQNRNGSSEIKKDDGEQMETKALPTFPFSIDSILAVSRVPRSRRPNAKYPRVQACKNLSPFMIPLFPITQPGGNVIREKSPPLPTQQSQIVATNALTTVAELLKSV,Homeobox protein unc-4,"Transcription factor. Involved in motor neuron fate determination and maintenance. In concert with unc-37, represses the expression of VB-specific genes such as ceh-12, thereby preventing the adoption of VB motor neuron fate. Regulates synaptic specificity and the pattern of synaptic input to VA motor neurons, and, depending on context, acting in opposition to, or supported by, Wnt signaling. Required in patterning of the synaptic outputs of the postmitotic DA class cholinergic motor neurons. Acts as a transcriptional repressor to counteract gene activation by transcription factor unc-3 in a subset of motor neurons, probably by binding to specific promoter elements. Has no role in axonal guidance or outgrowth.",Enables crawling backwards in e26/e2307; establishes interaction with unc-37.,Enables crawling backwards in e26/e2307; establishes interaction with unc-37.
3286,3286,0,0,P01112-K61Q,MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDLAARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRQHKLRKLNPPDESGPGCMSCKCVLS,,-1.0,MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGKEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDLAARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRQHKLRKLNPPDESGPGCMSCKCVLS,GTPase HRas,Involved in the activation of Ras protein signal transduction. Ras proteins bind GDP/GTP and possess intrinsic GTPase activity.,"Decreases transformation of cultured cell lines. Follicular carcinomas with RAS mutations most often displayed an HBME-1-negative/galectin-3-positive immunophenotype and were neither minimally nor overtly invasive. Transformation efficiencies of RasQ61K mutant at residue 61 range over three orders of magnitude, but the in vitro GTPase activity increases 10-fold for the mutant.","Decreases transformation of cultured cell lines. Follicular carcinomas with RAS mutations most often displayed an HBME-1-negative/galectin-3-positive immunophenotype and were neither minimally nor overtly invasive. Transformation efficiencies of RasQ61K mutant at residue 61 range over three orders of magnitude, but the in vitro GTPase activity increases 10-fold for the mutant."
3293,3293,0,0,Q9I485-A459H,MKHAHLIVPRTLVAGSASGELLYAPTGLSFWGGVDPRSAEVIDRHHPLSGRHLHGRLLAIPGGRGSCTGSSVLLELILGGRAPAAILLREPDEILALGAIVAEELFGRSLPIACLGERFDELAAYPWARLADGRLELHRDAPPPLEARPAEALATDAGPRLDAFDQALLAGEHGEAARLAMRIVLRMAALQGAQRLIDIQRAHIDACIYTGPAGLRFAETLRDLGARVRVPTTLNAISVDQRRWREQGVPAALGEPAAALARAYLDMGAQPSFTCAPYLLDDSARAGEQIVWAESNAVLFANSVLGARTNKYADFMDICCALTGRAPLAGCHLDEQRQARVLIEVEDLGSVDDAFYPTLGYLCGLLCDGQIPAIDGLRQRQPDHDALKAFGAALGTSSSVPMFHVIGVTPEAPDLASAFGGRAPRRTLRVGRERLRDAWRELDSAGETRIDLVALGNPHFSASEFAQLAALCHGRRRHPEVALVITSSRQVVAQAEAAGHLATLQAFGARLVTDTCWCMLDEPLVPPGARTLMTNSAKYAHYAPGLVGRQVRFAGLAGCVEAAVGGRSPAGLPAWLSEDC,,-1.0,MKHAHLIVPRTLVAGSASGELLYAPTGLSFWGGVDPRSAEVIDRHHPLSGRHLHGRLLAIPGGRGSCTGSSVLLELILGGRAPAAILLREPDEILALGAIVAEELFGRSLPIACLGERFDELAAYPWARLADGRLELHRDAPPPLEARPAEALATDAGPRLDAFDQALLAGEHGEAARLAMRIVLRMAALQGAQRLIDIQRAHIDACIYTGPAGLRFAETLRDLGARVRVPTTLNAISVDQRRWREQGVPAALGEPAAALARAYLDMGAQPSFTCAPYLLDDSARAGEQIVWAESNAVLFANSVLGARTNKYADFMDICCALTGRAPLAGCHLDEQRQARVLIEVEDLGSVDDAFYPTLGYLCGLLCDGQIPAIDGLRQRQPDHDALKAFGAALGTSSSVPMFHVIGVTPEAPDLASAFGGRAPRRTLRVGRERLRDAWRELDSAGETRIDLVALGNPAFSASEFAQLAALCHGRRRHPEVALVITSSRQVVAQAEAAGHLATLQAFGARLVTDTCWCMLDEPLVPPGARTLMTNSAKYAHYAPGLVGRQVRFAGLAGCVEAAVGGRSPAGLPAWLSEDC,Cis-3-hydroxy-L-proline dehydratase,"Catalyzes the dehydration of cis-3-hydroxy-L-proline (c3LHyp) to Delta(1)-pyrroline-2-carboxylate (Pyr2C). Has also activity with (2S,3S,4R)-3,4-dihydroxyproline as substrate, albeit at about 300-fold lower rate. No activity with L-proline, trans-4-hydroxy-L-proline (t4LHyp), cis-4-hydroxy-L-proline (c4LHyp), trans-3-hydroxy-L-proline (t3LHyp), D-proline, cis-4-hydroxy-D-proline (c4DHyp), trans-4-hydroxy-D-proline (t4DHyp) or L-serine as substrates. No hydro-lyase activity with citrate or cis-acotinate. Does not catalyze 2-epimerization of c3LHyp to trans-3-hydroxy-D-proline (t3DHyp). Involved in a degradation pathway that converts c3LHyp to L-proline, which would allow P.aeruginosa to grow on c3LHyp as a sole carbon source.","Significantly increased catalytic activity. The mutation in aconitase X resulted in a significant alteration in its catalytic activity. The wild-type protein catalyzes the dehydration of cis-3-hydroxy-L-proline to Δ1-pyrroline-2-carboxylate, but the mutant gained this activity. This suggests that Histidine 459 is insignificant for the catalytic function of aconitase X.","Significantly increased catalytic activity. The mutation in aconitase X resulted in a significant alteration in its catalytic activity. The wild-type protein catalyzes the dehydration of cis-3-hydroxy-L-proline to Δ1-pyrroline-2-carboxylate, but the mutant gained this activity. This suggests that Histidine 459 is insignificant for the catalytic function of aconitase X."
3294,3294,0,0,Q15080-A60R,MAVAQQLRAESDFEQLPDDVAISANIADIEEKRGFTSHFVFVIEVKTKGGSKYLIYRRYRQFHALQSKLEERFGPDSKSSALACTLPTLPAKVYVGVKQEIAEMRIPALNAYMKSLLSLPVWVLMDEDVRIFFYQSPYDSEQVPQALRRLRPRTRKVKSVSPQGNSVDRMAAPRAEALFDFTGNSKLELNFKAGDVIFLLSRINKDWLEGTVRGATGIFPLSFVKILKDFPEEDDPTNWLRCYYYEDTISTIKDIAVEEDLSSTPLLKDLLELTRREFQREDIALNYRDAEGDLVRLLSDEDVALMVRQARGLPSQKRLFPWKLHITQKDNYRVYNTMP,,-1.0,MAVAQQLRAESDFEQLPDDVAISANIADIEEKRGFTSHFVFVIEVKTKGGSKYLIYRRYAQFHALQSKLEERFGPDSKSSALACTLPTLPAKVYVGVKQEIAEMRIPALNAYMKSLLSLPVWVLMDEDVRIFFYQSPYDSEQVPQALRRLRPRTRKVKSVSPQGNSVDRMAAPRAEALFDFTGNSKLELNFKAGDVIFLLSRINKDWLEGTVRGATGIFPLSFVKILKDFPEEDDPTNWLRCYYYEDTISTIKDIAVEEDLSSTPLLKDLLELTRREFQREDIALNYRDAEGDLVRLLSDEDVALMVRQARGLPSQKRLFPWKLHITQKDNYRVYNTMP,Neutrophil cytosol factor 4,"Component of the NADPH-oxidase, a multicomponent enzyme system responsible for the oxidative burst in which electrons are transported from NADPH to molecular oxygen, generating reactive oxidant intermediates. It may be important for the assembly and/or activation of the NADPH-oxidase complex.",Strongly increases interaction with membranes enriched in phosphatidylinositol 3-phosphate.,Strongly increases interaction with membranes enriched in phosphatidylinositol 3-phosphate.
3299,3299,0,0,Q9H7X0-F165Y,MTEVVPSSALSEVSLRLLCHDDIDTVKHLCGDWFPIEYPDSWYRDITSNKKFFSLAATYRGAIVGMIVAEIKNRTKIHKEDGDILASNFSVDTQVAYILSLGVVKEFRKHGIGSLLLESLKDHISTTAQDHCKAIYLHVLTTNNTAINFYENRDFKQHHYLPYYYSIRGVLKDGFTYVLYINGGHPPWTILDYIQHLGSALASLSPCSIPHRVYRQAHSLLCSFLPWSGISSKSGIEYSRTM,,-1.0,MTEVVPSSALSEVSLRLLCHDDIDTVKHLCGDWFPIEYPDSWYRDITSNKKFFSLAATYRGAIVGMIVAEIKNRTKIHKEDGDILASNFSVDTQVAYILSLGVVKEFRKHGIGSLLLESLKDHISTTAQDHCKAIYLHVLTTNNTAINFYENRDFKQHHYLPYYFSIRGVLKDGFTYVLYINGGHPPWTILDYIQHLGSALASLSPCSIPHRVYRQAHSLLCSFLPWSGISSKSGIEYSRTM,N-alpha-acetyltransferase 60,"N-alpha-acetyltransferase that specifically mediates the acetylation of N-terminal residues of the transmembrane proteins, with a strong preference for N-termini facing the cytosol. Displays N-terminal acetyltransferase activity towards a range of N-terminal sequences including those starting with Met-Lys, Met-Val, Met-Ala and Met-Met. Required for normal chromosomal segregation during anaphase. May also show histone acetyltransferase activity; such results are however unclear in vivo and would require additional experimental evidences.","Strongly increased acetyltransferase activity. The mutation in Naa60 causes a functional change in its acetyltransferase activity, indicating a new regulatory mechanism involving enzyme, co-factor, and substrate interactions.","Strongly increased acetyltransferase activity. The mutation in Naa60 causes a functional change in its acetyltransferase activity, indicating a new regulatory mechanism involving enzyme, co-factor, and substrate interactions."
3305,3305,0,0,P21579-K303M,MVSESHHEALAAPPVTTVATVLPSNATEPASPGEGKEDAFSKLKEKFMNELHKIPLPPWALIAIAIVAVLLVLTCCFCICKKCLFKKKNKKKGKEKGGKNAINMKDVKDLGKTMKDQALKDDDAETGLTDGEEKEEPKEEEKLGKLQYSLDYDFQNNQLLVGIIQAAELPALDMGGTSDPYVKVFLLPDKKKKFETKVHRKTLNPVFNEQFTFKVPYSELGGKTLVMAVYDFDRFSKHDIIGEFKVPMNTVDFGHVTEEWRDLQSAEKEEQEKLGDICFSLRYVPTAGKLTVVILEAKNLKKMDVGGLSDPYVKIHLMQNGKRLKKKKTTIKKNTLNPYYNESFSFEVPFEQIQKVQVVVTVLDYDKIGKNDAIGKVFVGYNSTGAELRHWSDMLANPRRPIAQWHTLQVEEEVDAMLAVKK,,-1.0,MVSESHHEALAAPPVTTVATVLPSNATEPASPGEGKEDAFSKLKEKFMNELHKIPLPPWALIAIAIVAVLLVLTCCFCICKKCLFKKKNKKKGKEKGGKNAINMKDVKDLGKTMKDQALKDDDAETGLTDGEEKEEPKEEEKLGKLQYSLDYDFQNNQLLVGIIQAAELPALDMGGTSDPYVKVFLLPDKKKKFETKVHRKTLNPVFNEQFTFKVPYSELGGKTLVMAVYDFDRFSKHDIIGEFKVPMNTVDFGHVTEEWRDLQSAEKEEQEKLGDICFSLRYVPTAGKLTVVILEAKNLKKKDVGGLSDPYVKIHLMQNGKRLKKKKTTIKKNTLNPYYNESFSFEVPFEQIQKVQVVVTVLDYDKIGKNDAIGKVFVGYNSTGAELRHWSDMLANPRRPIAQWHTLQVEEEVDAMLAVKK,Synaptotagmin-1,"Calcium sensor that participates in triggering neurotransmitter release at the synapse. May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. A Ca(2+)-dependent interaction between synaptotagmin and putative receptors for activated protein kinase C has also been reported. It can bind to at least three additional proteins in a Ca(2+)-independent manner; these are neurexins, syntaxin and AP2. Plays a role in dendrite formation by melanocytes.",Lower level of expression and succeeded in localizing at nerve terminals.,Lower level of expression and succeeded in localizing at nerve terminals.
3310,3310,0,0,Q8HWS3-G506V,MAKVPELEDTFLQAQPAPQLSPGIQEDCCVQLLGKGLLVYPEETVYLAAEGQPGGEQGGGEKGEDPELPGAVKSEMHLNNGNFSSEEEDADNHDSKTKAADQYLSQKKTITQIVKDKKKQTQLTLQWLEENYIVCEGVCLPRCILYAHYLDFCRKEKLEPACAATFGKTIRQKFPLLTTRRLGTRGHSKYHYYGIGIKESSAYYHSVYSGKGLTRFSGSKLKNEGGFTRKYSLSSKTGTLLPEFPSAQHLVYQGCISKDKVDTLIMMYKTHCQCILDNAINGNFEEIQHFLLHFWQGMPDHLLPLLENPVIIDIFCVCDSILYKVLTDVLIPATMQEMPESLLADIRNFAKNWEQWVVSSLENLPEALTDKKIPIVRRFVSSLKRQTSFLHLAQIARPALFDQHVVNSMVSDIERVDLNSIGSQALLTISGSTDTESGIYTEHDSITVFQELKDLLKKNATVEAFIEWLDTVVEQRVIKTSKQNGRSLKKRAQDFLLKWSFFGARVMHNLTLNNASSFGSFHLIRMLLDEYILLAMETQFNNDKEQELQNLLDKYMKNSDASKAAFTASPSSCFLANRNKGSMVSSDAVKNESHVETTYLPLPSSQPGGLGPALHQFPAGNTDNMPLTGQMELSQIAGHLMTPPISPAMASRGSVINQGPMAGRPPSVGPVLSAPSHCSTYPEPIYPTLPQANHDFYSTSSNYQTVFRAQPHSTSGLYPHHTEHGRCMAWTEQQLSRDFFSGSCAGSPYNSRPPSSYGPSLQAQDSHNMQFLNTGSFNFLSNTGAASCQGATLPPNSPNGYYGSNINYPESHRLGSMVNQHVSVISSIRSLPPYSDIHDPLNILDDSGRKQTSSFYTDTSSPVACRTPVLASSLQTPIPSSSSQCMYGTSNQYPAQETLDSHGTSSREMVSSLPPINTVFMGTAAGGT,,-1.0,MAKVPELEDTFLQAQPAPQLSPGIQEDCCVQLLGKGLLVYPEETVYLAAEGQPGGEQGGGEKGEDPELPGAVKSEMHLNNGNFSSEEEDADNHDSKTKAADQYLSQKKTITQIVKDKKKQTQLTLQWLEENYIVCEGVCLPRCILYAHYLDFCRKEKLEPACAATFGKTIRQKFPLLTTRRLGTRGHSKYHYYGIGIKESSAYYHSVYSGKGLTRFSGSKLKNEGGFTRKYSLSSKTGTLLPEFPSAQHLVYQGCISKDKVDTLIMMYKTHCQCILDNAINGNFEEIQHFLLHFWQGMPDHLLPLLENPVIIDIFCVCDSILYKVLTDVLIPATMQEMPESLLADIRNFAKNWEQWVVSSLENLPEALTDKKIPIVRRFVSSLKRQTSFLHLAQIARPALFDQHVVNSMVSDIERVDLNSIGSQALLTISGSTDTESGIYTEHDSITVFQELKDLLKKNATVEAFIEWLDTVVEQRVIKTSKQNGRSLKKRAQDFLLKWSFFGARGMHNLTLNNASSFGSFHLIRMLLDEYILLAMETQFNNDKEQELQNLLDKYMKNSDASKAAFTASPSSCFLANRNKGSMVSSDAVKNESHVETTYLPLPSSQPGGLGPALHQFPAGNTDNMPLTGQMELSQIAGHLMTPPISPAMASRGSVINQGPMAGRPPSVGPVLSAPSHCSTYPEPIYPTLPQANHDFYSTSSNYQTVFRAQPHSTSGLYPHHTEHGRCMAWTEQQLSRDFFSGSCAGSPYNSRPPSSYGPSLQAQDSHNMQFLNTGSFNFLSNTGAASCQGATLPPNSPNGYYGSNINYPESHRLGSMVNQHVSVISSIRSLPPYSDIHDPLNILDDSGRKQTSSFYTDTSSPVACRTPVLASSLQTPIPSSSSQCMYGTSNQYPAQETLDSHGTSSREMVSSLPPINTVFMGTAAGGT,DNA-binding protein RFX6,"Transcription factor required to direct islet cell differentiation during endocrine pancreas development. Specifically required for the differentiation of 4 of the 5 islet cell types and for the production of insulin. Not required for pancreatic PP (polypeptide-producing) cells differentiation. Acts downstream of NEUROG3 and regulates the transcription factors involved in beta-cell maturation and function, thereby restricting the expression of the beta-cell differentiation and specification genes, and thus the beta-cell fate choice. Activates transcription by forming a heterodimer with RFX3 and binding to the X-box in the promoter of target genes. Involved in glucose-stimulated insulin secretion by promoting insulin and L-type calcium channel gene transcription.",Increases transactivation of the insulin and beta-cell L-type calcium channel genes in MTCHRS. The homozygous missense RFX6 mutation (p. ) is associated with neonatal diabetes. This mutation possesses the capacity to activate the insulin promoter and to increase Ca(2+)-channel expression.,Increases transactivation of the insulin and beta-cell L-type calcium channel genes in MTCHRS. The homozygous missense RFX6 mutation (p. ) is associated with neonatal diabetes. This mutation possesses the capacity to activate the insulin promoter and to increase Ca(2+)-channel expression.
3330,3330,0,0,P0C0J0-A384G,MNKKKLGIRLLSLLALGGFVLANPVFADQNFARNEKEAKDSAITFIQKSAAIKAGARSAEDIKLDKVNLGGELSGSNMYVYNISTGGFVIVSGDKRSPEILGYSTSGSFDANGKENIASFMESYVEQIKENKKLDTTYAGTAEIKQPVVKSLLDSKGIHYNQGNPYNLLTPVIEKVKPGEQSFVGQHAATGCVATATAQIMKYHNYPNKGLKDYTYTLSSNNPYFNHPKNLFAAISTRQYNWNNILPTYSGRESNVQKMAISELMADVGISVDMDYGPSSGSAGSSRVQRALKENFGYNQSVHQINRSDFSKQDWEAQIDKELSQNQPVYYQGVGKVGGHAFVIDGADGRNFYHVNWGWGGVSDGFFRLDALNPSALGTGGGAGGFNGYQSAVVGIKP,,-1.0,MNKKKLGIRLLSLLALGGFVLANPVFADQNFARNEKEAKDSAITFIQKSAAIKAGARSAEDIKLDKVNLGGELSGSNMYVYNISTGGFVIVSGDKRSPEILGYSTSGSFDANGKENIASFMESYVEQIKENKKLDTTYAGTAEIKQPVVKSLLDSKGIHYNQGNPYNLLTPVIEKVKPGEQSFVGQHAATGCVATATAQIMKYHNYPNKGLKDYTYTLSSNNPYFNHPKNLFAAISTRQYNWNNILPTYSGRESNVQKMAISELMADVGISVDMDYGPSSGSAGSSRVQRALKENFGYNQSVHQINRSDFSKQDWEAQIDKELSQNQPVYYQGVGKVGGHAFVIDGADGRNFYHVNWGWGGVSDGFFRLDALNPSALGTGGGAAGFNGYQSAVVGIKP,Streptopain,"Cysteine protease that acts as a key streptococcal virulence factor by cleaving host proteins involved in immune response. Triggers inflammation by mediating cleavage of host proteins, which can both promote host pathogenesis by triggering sterile inflammation and/or restrict streptococcal infection, depending on host immune statue and infection site (By similarity). Cleaves host gasdermin-A (GSDMA) in epithelial cells, promoting GSDMA activation and formation of gasdermin pores, triggering pyroptosis (By similarity). Pyroptosis triggers the elimination of the infected skin cell, depriving the pathogen of its protective niche, while inducing an inflammatory response (By similarity). This ultimately prevents bacterial penetration of the epithelial barrier and a subsequent systemic dissemination of the pathogen (By similarity). Also mediates cleavage of the cytokine precursor interleukin-1 beta (IL1B) to its mature form, resulting in inflammation and septic shock. SpeB-mediated maturation of IL1B plays a dual role depending on infection site: while IL1B inflammatory response prevents bacterial growth during invasive skin infections, it promotes streptococcal infection of the nasopharynx by disrupting colonization resistance mediated by the microbiota (By similarity). Inhibits host autophagy be catalyzing cleavage and inactivation of key autophagy factors, such as CALCOCO2, NBR1 and SQSTM1 (By similarity). Cleaves and inhibits a number of complement factors, such as C2, C3-beta chain of C3, C4, C5 or SERPING1, thereby promoting evasion of host immunity (By similarity). May also impair adaptive immunity by catalyzing cleavage and degradation of host immunoglobulins to promote immune system evasion; the relevance of this activity is however unsure in vivo (By similarity). Catalyzes maturation and release of the peptide hormone bradykinin from the precursor Kininogen-1 (KNG1) to produce hypotension during septic shock (By similarity). Also involved in bacterial translocation across the host epithelial barrier by mediating cleavage and degradation of host epithelial junction proteins, such as CDH1 and OCLN (By similarity). Additionally, has been involved in degradation of fibronectin and vitronectin, two host extracellular matrix proteins involved in tissue integrity. Also able to catalyze cleavage and degradation of streptococcal proteins, such as C5a peptidase, EndoS or SmeZ (By similarity). Degradation of streptococcal proteins is however strictly regulated to preserve integrity of other virulence factors (By similarity).",Decreased catalytic efficiency due to worsened substrate-binding. The structures and mutational analysis suggest that the conformational movements of the glycine-rich C-terminal loop are unimportant for the recognition and recruitment of biological substrates and retention of hydrolyzed products.,Decreased catalytic efficiency due to worsened substrate-binding. The structures and mutational analysis suggest that the conformational movements of the glycine-rich C-terminal loop are unimportant for the recognition and recruitment of biological substrates and retention of hydrolyzed products.
3331,3331,0,0,P47897-V45G,MAALDSLSLFTSLGLSEQKARETLKNSALSAQLREAATQAQQTLGSTIDKATGILLYGLASRLRDTRRLSFLVSYIASKKIHTEPQLSAALEYVRSHPLDPIDTVDFERECGVGVIVTPEQIEEAVEAAINRHRPQLLVERYHFNMGLLMGEARAVLKWADGKMIKNEVDMQVLHLLGPKLEADLEKKFKVAKARLEETDRRTAKDVVENGETADQTLSLMEQLRGEALKFHKPGENYKTPGYVVTPHTMNLLKQHLEITGGQVRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRFDDTNPEKEEAKFFTAICDMVAWLGYTPYKVTYASDYFDQLYAWAVELIRRGLAYVCHQRGEELKGHNTLPSPWRDRPMEESLLLFEAMRKGKFSEGEATLRMKLVMEDGKMDPVAYRVKYTPHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALDVYCPVQWEYGRLNLHYAVVSKRKILQLVATGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQTTMEPHLLEACVRDVLNDTAPRAMAVLESLRVIITNFPAAKSLDIQVPNFPADETKGFHQVPFAPIVFIERTDFKEEPEPGFKRLAWGQPVGLRHTGYVIELQHVVKGPSGCVESLEVTCRRADAGEKPKAFIHWVSQPLMCEVRLYERLFQHKNPEDPTEVPGGFLSDLNLASLHVVDAALVDCSVALAKPFDKFQFERLGYFSVDPDSHQGKLVFNRTVTLKEDPGKV,,-1.0,MAALDSLSLFTSLGLSEQKARETLKNSALSAQLREAATQAQQTLVSTIDKATGILLYGLASRLRDTRRLSFLVSYIASKKIHTEPQLSAALEYVRSHPLDPIDTVDFERECGVGVIVTPEQIEEAVEAAINRHRPQLLVERYHFNMGLLMGEARAVLKWADGKMIKNEVDMQVLHLLGPKLEADLEKKFKVAKARLEETDRRTAKDVVENGETADQTLSLMEQLRGEALKFHKPGENYKTPGYVVTPHTMNLLKQHLEITGGQVRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRFDDTNPEKEEAKFFTAICDMVAWLGYTPYKVTYASDYFDQLYAWAVELIRRGLAYVCHQRGEELKGHNTLPSPWRDRPMEESLLLFEAMRKGKFSEGEATLRMKLVMEDGKMDPVAYRVKYTPHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALDVYCPVQWEYGRLNLHYAVVSKRKILQLVATGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQTTMEPHLLEACVRDVLNDTAPRAMAVLESLRVIITNFPAAKSLDIQVPNFPADETKGFHQVPFAPIVFIERTDFKEEPEPGFKRLAWGQPVGLRHTGYVIELQHVVKGPSGCVESLEVTCRRADAGEKPKAFIHWVSQPLMCEVRLYERLFQHKNPEDPTEVPGGFLSDLNLASLHVVDAALVDCSVALAKPFDKFQFERLGYFSVDPDSHQGKLVFNRTVTLKEDPGKV,Glutamine--tRNA ligase,Glutamine--tRNA ligase. Plays a critical role in brain development.,"Results in enhanced glutaminyl-tRNA aminoacylation activity; does not affect interaction with RARS1. Variants p. were located in the N-terminal domain required for QARS interaction with proteins in the multisynthetase complex and potentially with glutamine tRNA, and recombinant QARS proteins bearing either substitution showed an over 10-fold increase in aminoacylation activity.","Results in enhanced glutaminyl-tRNA aminoacylation activity; does not affect interaction with RARS1. Variants p. were located in the N-terminal domain required for QARS interaction with proteins in the multisynthetase complex and potentially with glutamine tRNA, and recombinant QARS proteins bearing either substitution showed an over 10-fold increase in aminoacylation activity."
3336,3336,0,0,P01112-V61Q,MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDLAARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRQHKLRKLNPPDESGPGCMSCKCVLS,,-1.0,MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGVEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDLAARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRQHKLRKLNPPDESGPGCMSCKCVLS,GTPase HRas,Involved in the activation of Ras protein signal transduction. Ras proteins bind GDP/GTP and possess intrinsic GTPase activity.,"Strongly decreased transformation of cultured cell lines. Transformation efficiencies of RasQ61V mutant at residue 61 range over three orders of magnitude, but the in vitro GTPase activity increases 10-fold for the mutant.","Strongly decreased transformation of cultured cell lines. Transformation efficiencies of RasQ61V mutant at residue 61 range over three orders of magnitude, but the in vitro GTPase activity increases 10-fold for the mutant."
3342,3342,0,0,Q2WGK3-S315F,MAEFVRAQIFGTTFEITSRYSDLQPVGMGAFGLVCSARDQLTNQNVAVKKIMKPFSTPVLAKRTYRELKLLKHLRHENVISLSDIFISPLEDIYFVTELLGTDLHRLLTSRPLEKQFIQYFLYQIMRGLKYVHSAGVVHRDLKPSNILVNENCDLKICDFGLARIQDPQMTGYVSTRYYRAPEIMLTWQKYDVEVDIWSAGCIFAEMLEGKPLFPGKDHVNQFSIITELLGTPPDDVINTIASENTLRFVKSLPKRERQPLRNKFKNADDSAIDLLERMLVFDPKKRVTATQALAHEYLQPYHDPTDEPVADEKFDWSFNDADLPVDTWKIMMYSEILDYHNVEGAPNMEEQFPPQ,,-1.0,MAEFVRAQIFGTTFEITSRYSDLQPVGMGAFGLVCSARDQLTNQNVAVKKIMKPFSTPVLAKRTYRELKLLKHLRHENVISLSDIFISPLEDIYFVTELLGTDLHRLLTSRPLEKQFIQYFLYQIMRGLKYVHSAGVVHRDLKPSNILVNENCDLKICDFGLARIQDPQMTGYVSTRYYRAPEIMLTWQKYDVEVDIWSAGCIFAEMLEGKPLFPGKDHVNQFSIITELLGTPPDDVINTIASENTLRFVKSLPKRERQPLRNKFKNADDSAIDLLERMLVFDPKKRVTATQALAHEYLQPYHDPTDEPVADEKSDWSFNDADLPVDTWKIMMYSEILDYHNVEGAPNMEEQFPPQ,Mitogen-activated protein kinase hog1,Mitogen-activated protein kinase involved in a signal transduction pathway that is activated by changes in the osmolarity of the extracellular environment. Controls osmotic regulation of transcription of target genes.,"Deactivates HOG1 in a non-constitutive manner. The strain carrying the hog1() allele was highly susceptible to the calcineurin inhibitor cyclosporin A, which suggests the absence of links between the two pathways. The two mutant strains showed a strongly enhanced antagonistic activity against the plant pathogens Phoma betae and Colletotrichum acutatum, which points to a lack of role of ThHog1 protein in fungus-fungus interactions.","Deactivates HOG1 in a non-constitutive manner. The strain carrying the hog1() allele was highly susceptible to the calcineurin inhibitor cyclosporin A, which suggests the absence of links between the two pathways. The two mutant strains showed a strongly enhanced antagonistic activity against the plant pathogens Phoma betae and Colletotrichum acutatum, which points to a lack of role of ThHog1 protein in fungus-fungus interactions."
3348,3348,0,0,P07173-K284R,MKQLIVNSVATVALASLVAGCFEPPPATTTQTGFRGLSMGEVLHPATVKAKKERDAQYPPALAAVKAEGPPVSQVYKNVKVLGNLTEAEFLRTMTAITEWVSPQEGCTYCHDENNLASEAKYPYVVARRMLEMTRAINTNWTQHVAQTGVTCYTCHRGTPLPPYVRYLEPTLPLNNRETPTHVERVETRSGYVVRLAKYTAYSALNYDPFTMFLANDKRQVRVVPQTALPLVGVSRGKERRPLSDAYATFALMMSISDSLGTNCTFCHNAQTFESWGKKSTPQRAIAWWGIRMVRDLNMNYLAPLNASLPASRLGRQGEAPQADCRTCHQGVTKPLFGASRLKDYPELGPIKAAAK,,-1.0,MKQLIVNSVATVALASLVAGCFEPPPATTTQTGFRGLSMGEVLHPATVKAKKERDAQYPPALAAVKAEGPPVSQVYKNVKVLGNLTEAEFLRTMTAITEWVSPQEGCTYCHDENNLASEAKYPYVVARRMLEMTRAINTNWTQHVAQTGVTCYTCHRGTPLPPYVRYLEPTLPLNNRETPTHVERVETRSGYVVRLAKYTAYSALNYDPFTMFLANDKRQVRVVPQTALPLVGVSRGKERRPLSDAYATFALMMSISDSLGTNCTFCHNAQTFESWGKKSTPQKAIAWWGIRMVRDLNMNYLAPLNASLPASRLGRQGEAPQADCRTCHQGVTKPLFGASRLKDYPELGPIKAAAK,Photosynthetic reaction center cytochrome c subunit,The reaction center of purple bacteria contains a tightly bound cytochrome molecule which re-reduces the photo oxidized primary electron donor.,"100 mV increase in redox potential of heme 3. The mutation increases the E(m) of heme3 from +380 to +480 mV, i.e., above that of heme2 (+320 mV). In addition, a red shift of the alpha-band was found to accompany the mutation.","100 mV increase in redox potential of heme 3. The mutation increases the E(m) of heme3 from +380 to +480 mV, i.e., above that of heme2 (+320 mV). In addition, a red shift of the alpha-band was found to accompany the mutation."
3358,3358,0,0,Q99988-A283V,MPGQELRTVNGSQMLLVLLVLSWLPHGGALSLAEASRASFPGPSELHSEDSRFRELRKRYEDLLTRLRANQSWEDSNTDLVPAPAVRILTPEVRLGSGGHLHLRISRAALPEGLPEASRLHRALFRLSPTASRSWDVTRPLRRQLSLARPQAPALHLRLSPPPSQSDQLLAESSSARPQLELHLRPQAARGRRRARARNGDHCPLGPGRCCRLHTVRASLEDLGWADWVLSPREVQVTMCIGACPSQFRAANMHAQIKTSLHRLKPDTVPAPCCVPASYNPMVLIQKTDTGVSLQTYDDLLAKDCHCI,,-1.0,MPGQELRTVNGSQMLLVLLVLSWLPHGGALSLAEASRASFPGPSELHSEDSRFRELRKRYEDLLTRLRANQSWEDSNTDLVPAPAVRILTPEVRLGSGGHLHLRISRAALPEGLPEASRLHRALFRLSPTASRSWDVTRPLRRQLSLARPQAPALHLRLSPPPSQSDQLLAESSSARPQLELHLRPQAARGRRRARARNGDHCPLGPGRCCRLHTVRASLEDLGWADWVLSPREVQVTMCIGACPSQFRAANMHAQIKTSLHRLKPDTVPAPCCVPASYNPMALIQKTDTGVSLQTYDDLLAKDCHCI,Growth/differentiation factor 15,"Regulates food intake, energy expenditure and body weight in response to metabolic and toxin-induced stresses. Binds to its receptor, GFRAL, and activates GFRAL-expressing neurons localized in the area postrema and nucleus tractus solitarius of the brainstem. It then triggers the activation of neurons localized within the parabrachial nucleus and central amygdala, which constitutes part of the 'emergency circuit' that shapes feeding responses to stressful conditions. On hepatocytes, inhibits growth hormone signaling.",Enhances cellular signaling mediated by GFRAL and RET.,Enhances cellular signaling mediated by GFRAL and RET.
3364,3364,0,0,P78363-H212R,MGFVRQIQLLLWKNWTLRKRQKIRFVVELVWPLSLFLVLIWLRNANPLYSHHECHFPNKAMPSAGMLPWLQGIFCNVNNPCFQSPTPGESPGIVSNYNNSILARVYRDFQELLMNAPESQHLGRIWTELHILSQFMDTLRTHPERIAGRGIRIRDILKDEETLTLFLIKNIGLSDSVVYLLINSQVRPEQFAHGVPDLALKDIACSEALLERFIIFSQRRGAKTVRYALCSLSQGTLQWIEDTLYANVDFFKLFRVLPTLLDSRSQGINLRSWGGILSDMSPRIQEFIHRPSMQDLLWVTRPLMQNGGPETFTKLMGILSDLLCGYPEGGGSRVLSFNWYEDNNYKAFLGIDSTRKDPIYSYDRRTTSFCNALIQSLESNPLTKIAWRAAKPLLMGKILYTPDSPAARRILKNANSTFEELEHVRKLVKAWEEVGPQIWYFFDNSTQMNMIRDTLGNPTVKDFLNRQLGEEGITAEAILNFLYKGPRESQADDMANFDWRDIFNITDRTLRLVNQYLECLVLDKFESYNDETQLTQRALSLLEENMFWAGVVFPDMYPWTSSLPPHVKYKIRMDIDVVEKTNKIKDRYWDSGPRADPVEDFRYIWGGFAYLQDMVEQGITRSQVQAEAPVGIYLQQMPYPCFVDDSFMIILNRCFPIFMVLAWIYSVSMTVKSIVLEKELRLKETLKNQGVSNAVIWCTWFLDSFSIMSMSIFLLTIFIMHGRILHYSDPFILFLFLLAFSTATIMLCFLLSTFFSKASLAAACSGVIYFTLYLPHILCFAWQDRMTAELKKAVSLLSPVAFGFGTEYLVRFEEQGLGLQWSNIGNSPTEGDEFSFLLSMQMMLLDAAVYGLLAWYLDQVFPGDYGTPLPWYFLLQESYWLGGEGCSTREERALEKTEPLTEETEDPEHPEGIHDSFFEREHPGWVPGVCVKNLVKIFEPCGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIETSLDAVRQSLGMCPQHNILFHHLTVAEHM,,-1.0,MGFVRQIQLLLWKNWTLRKRQKIRFVVELVWPLSLFLVLIWLRNANPLYSHHECHFPNKAMPSAGMLPWLQGIFCNVNNPCFQSPTPGESPGIVSNYNNSILARVYRDFQELLMNAPESQHLGRIWTELHILSQFMDTLRTHPERIAGRGIRIRDILKDEETLTLFLIKNIGLSDSVVYLLINSQVRPEQFAHGVPDLALKDIACSEALLEHFIIFSQRRGAKTVRYALCSLSQGTLQWIEDTLYANVDFFKLFRVLPTLLDSRSQGINLRSWGGILSDMSPRIQEFIHRPSMQDLLWVTRPLMQNGGPETFTKLMGILSDLLCGYPEGGGSRVLSFNWYEDNNYKAFLGIDSTRKDPIYSYDRRTTSFCNALIQSLESNPLTKIAWRAAKPLLMGKILYTPDSPAARRILKNANSTFEELEHVRKLVKAWEEVGPQIWYFFDNSTQMNMIRDTLGNPTVKDFLNRQLGEEGITAEAILNFLYKGPRESQADDMANFDWRDIFNITDRTLRLVNQYLECLVLDKFESYNDETQLTQRALSLLEENMFWAGVVFPDMYPWTSSLPPHVKYKIRMDIDVVEKTNKIKDRYWDSGPRADPVEDFRYIWGGFAYLQDMVEQGITRSQVQAEAPVGIYLQQMPYPCFVDDSFMIILNRCFPIFMVLAWIYSVSMTVKSIVLEKELRLKETLKNQGVSNAVIWCTWFLDSFSIMSMSIFLLTIFIMHGRILHYSDPFILFLFLLAFSTATIMLCFLLSTFFSKASLAAACSGVIYFTLYLPHILCFAWQDRMTAELKKAVSLLSPVAFGFGTEYLVRFEEQGLGLQWSNIGNSPTEGDEFSFLLSMQMMLLDAAVYGLLAWYLDQVFPGDYGTPLPWYFLLQESYWLGGEGCSTREERALEKTEPLTEETEDPEHPEGIHDSFFEREHPGWVPGVCVKNLVKIFEPCGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIETSLDAVRQSLGMCPQHNILFHHLTVAEHM,Retinal-specific phospholipid-transporting ATPase ABCA4,"Flippase that catalyzes in an ATP-dependent manner the transport of retinal-phosphatidylethanolamine conjugates like the 11-cis and all-trans isomers of N-retinylidene-phosphatidylethanolamine from the lumen to the cytoplasmic leaflet of photoreceptor outer segment disk membranes, where N-cis-retinylidene-phosphatidylethanolamine (N-cis-R-PE) is then isomerized to its all-trans isomer (N-trans-R-PE) and reduced by RDH8 to produce all-trans-retinol (all-trans-rol) and therefore prevents the accumulation of excess of 11-cis-retinal and its schiff-base conjugate and the formation of toxic bisretinoid. May display both ATPase and GTPase activity that is strongly influenced by the lipid environment and the presence of retinoid compounds. Binds the unprotonated form of N-retinylidene-phosphatidylethanolamine with high affinity in the absence of ATP, and ATP binding and hydrolysis induce a protein conformational change that causes the dissociation of N-retinylidene-phosphatidylethanolamine.","In STGD1, The mutation in the ABCR gene results in a gain of protein function, leading to the clearance of toxic substances in the retina. The mutation in the ABCA4 gene has been identified in patients with Stargardt disease. This mutation leads to no functional changes in the photoreceptor-specific ATP-binding cassette transporter, resulting in the prevention of maculopathy. The mutation in the ABCR gene is not associated with Stargardt macular degeneration and cone-rod degeneration. This mutation leads to no functional changes in the ABCR protein, maintaining its ability to transport retinaldehyde and preventing degeneration of the macula and cone cells in the retina. The mutation in the ABCA4 gene has not been associated with macular degenerations.","In STGD1, The mutation in the ABCR gene results in a gain of protein function, leading to the clearance of toxic substances in the retina. The mutation in the ABCA4 gene has been identified in patients with Stargardt disease. This mutation leads to no functional changes in the photoreceptor-specific ATP-binding cassette transporter, resulting in the prevention of maculopathy. The mutation in the ABCR gene is not associated with Stargardt macular degeneration and cone-rod degeneration. This mutation leads to no functional changes in the ABCR protein, maintaining its ability to transport retinaldehyde and preventing degeneration of the macula and cone cells in the retina. The mutation in the ABCA4 gene has not been associated with macular degenerations."
3367,3367,0,0,P51400-A128K,MDIEDEENMSSSSIDVKENRNLDNMPPKDSSTPGPGEGIPLSNGGGGSTSRKRPLEEGSNGHSKYRLKKRRKTPGPVLPKNALMQLNEIKPGLQYMLLSQTGPVHAPLFVMSVEVNGQVFEGSGPTKKKAKLHAAEKALRSFVQFPNASEAHLAMGRTLSVNTDFTSDQADFPDTLFNGFETPDKSEPPFYVGSNGDDSFSSSGDVSLSASPVPASLTQPPLPIPPPFPPPSGKNPVMILNELRPGLKYDFLSESGESHAKSFVMSVVVDGQFFEGSGRNKKLAKARAAQSALATVFNLHLDQTPSRQPVLSEGLQLHLPQVLADAVSRLVLGKFSDLTDNFSSPHARRKVLSGVVMTTGTDVKDAKVISVSTGTKCINGEYMSDRGLALNDCHAEIISRRSLLRFLYAQLELYLNNKEDQKKSIFQKSERGGFRLKDTVQFHLYISTSPCGDARIFSPHEPVLEGMAPDSHQLTEPADRHPNRKARGQLRTKIESGEGTIPVRSNASIQTWDGVLQGERLLTMSCSDKIARWNVVGIQGALLSIFVEPIYFSSIILGSLYHGDHLSRAMYQRISNIEDLPPLYTLNKPLLSGISNAEARQPGKAPNFSVNWTVGDTAIEVINATTGKDELGRPSRLCKHALYCRWMRVHGKVPPHLLRTKITKPTTYHESKLAAKEYQAAKARLFTAFIKAGLGAWVEKPTEQDQFSFTP,,-1.0,MDIEDEENMSSSSIDVKENRNLDNMPPKDSSTPGPGEGIPLSNGGGGSTSRKRPLEEGSNGHSKYRLKKRRKTPGPVLPKNALMQLNEIKPGLQYMLLSQTGPVHAPLFVMSVEVNGQVFEGSGPTKAKAKLHAAEKALRSFVQFPNASEAHLAMGRTLSVNTDFTSDQADFPDTLFNGFETPDKSEPPFYVGSNGDDSFSSSGDVSLSASPVPASLTQPPLPIPPPFPPPSGKNPVMILNELRPGLKYDFLSESGESHAKSFVMSVVVDGQFFEGSGRNKKLAKARAAQSALATVFNLHLDQTPSRQPVLSEGLQLHLPQVLADAVSRLVLGKFSDLTDNFSSPHARRKVLSGVVMTTGTDVKDAKVISVSTGTKCINGEYMSDRGLALNDCHAEIISRRSLLRFLYAQLELYLNNKEDQKKSIFQKSERGGFRLKDTVQFHLYISTSPCGDARIFSPHEPVLEGMAPDSHQLTEPADRHPNRKARGQLRTKIESGEGTIPVRSNASIQTWDGVLQGERLLTMSCSDKIARWNVVGIQGALLSIFVEPIYFSSIILGSLYHGDHLSRAMYQRISNIEDLPPLYTLNKPLLSGISNAEARQPGKAPNFSVNWTVGDTAIEVINATTGKDELGRPSRLCKHALYCRWMRVHGKVPPHLLRTKITKPTTYHESKLAAKEYQAAKARLFTAFIKAGLGAWVEKPTEQDQFSFTP,Double-stranded RNA-specific editase 1,"Catalyzes the hydrolytic deamination of adenosine to inosine in double-stranded RNA (dsRNA) referred to as A-to-I RNA editing. This may affect gene expression and function in a number of ways that include mRNA translation by changing codons and hence the amino acid sequence of proteins; pre-mRNA splicing by altering splice site recognition sequences; RNA stability by changing sequences involved in nuclease recognition; genetic stability in the case of RNA virus genomes by changing sequences during viral RNA replication; and RNA structure-dependent activities such as microRNA production or targeting or protein-RNA interactions. Can edit both viral and cellular RNAs and can edit RNAs at multiple sites (hyper-editing) or at specific sites (site-specific editing). Its cellular RNA substrates include: bladder cancer-associated protein (BLCAP), neurotransmitter receptors for glutamate (GRIA2 and GRIK2) and serotonin (HTR2C), GABA receptor (GABRA3) and potassium voltage-gated channel (KCNA1). Site-specific RNA editing of transcripts encoding these proteins results in amino acid substitutions which consequently alter their functional activities. Edits GRIA2 at both the Q/R and R/G sites efficiently but converts the adenosine in hotspot1 much less efficiently. Can inhibit cell proliferation and migration and can stimulate exocytosis.",Increased RNA editing activity; when associated with A-281.,Increased RNA editing activity; when associated with A-281.
3381,3381,0,0,Q8SR66-A80I,MEGKKEEIREHYNSIRERGRESRQRSKTINIRNANNFIKACLIRLYTKRGDSVLDLGCGKGGDLLKYERAGIGEYYGVDIAEVSINDARVRARNMKRRFKVFFRAQDSYGRHMDLGKEFDVISSQFSFHYAFSTSESLDIAQRNIARHLRPGGYFIMTVPSRDVILERYKQGRMSNDFYKIELEKMEDVPMESVREYRFTLLDSVNNCIEYFVDFTRMVDGFKRLGLSLVERKGFIDFYEDEGRRNPELSKKMGLGCLTREESEVVGIYEVVVFRKLVPESDA,,-1.0,MEGKKEEIREHYNSIRERGRESRQRSKTINIRNANNFIKACLIRLYTKRGDSVLDLGCGKGGDLLKYERAGIGEYYGVDAAEVSINDARVRARNMKRRFKVFFRAQDSYGRHMDLGKEFDVISSQFSFHYAFSTSESLDIAQRNIARHLRPGGYFIMTVPSRDVILERYKQGRMSNDFYKIELEKMEDVPMESVREYRFTLLDSVNNCIEYFVDFTRMVDGFKRLGLSLVERKGFIDFYEDEGRRNPELSKKMGLGCLTREESEVVGIYEVVVFRKLVPESDA,mRNA cap guanine-N7 methyltransferase,mRNA-capping methyltransferase that methylates the N7 position of the added guanosine to the 5'-cap structure of mRNAs. Binds RNA containing 5'-terminal GpppC.,Strongly increased activity; when associated with A-109.,Strongly increased activity; when associated with A-109.
3403,3403,0,0,Q9C5U1-F713S,MSLFHVLGFGVKIGHLFWMLCCWFVSWFVDNGIEDKSGLLVGSVGDLEKTKMTTLKKKNKMWFWNKISSSGLKIPSFSYQFLGSVKFNKAWWRKLVVVWVVFWVLVSIWTFWYFSSQAMEKRKETLASMCDERARMLQDQFNVSMNHVQAMSILISTFHHGKIPSAIDQRTFSEYTDRTSFERPLTSGVAYAMRVLHSEREEFERQQGWTIRKMYSLEQNPVHKDDYDLEALEPSPVQEEYAPVIFAQDTVSHVVSLDMLSGKEDRENVLRARSSGKGVLTAPFPLIKTNRLGVILTFAVYKRDLPSNATPKERIEATNGYLGGVFDIESLVENLLQQLASKQTILVNVYDITNHSQPISMYGTNVSADGLERVSPLIFGDPLRKHEMRCRFKQKPPWPVLSMVTSFGILVIALLVAHIIHATVSRIHKVEEDCDKMKQLKKKAEAADVAKSQFLATVSHEIRTPMNGVLGMLHMLMDTELDVTQQDYVRTAQASGKALVSLINEVLDQAKIESGKLELEEVRFDLRGILDDVLSLFSSKSQQKGVELAVYISDRVPDMLIGDPGRFRQILTNLMGNSIKFTEKGHIFVTVHLVDELFESIDGETASSPESTLSGLPVADRQRSWENFKAFSSNGHRSFEPSPPDINLIVSVEDTGVGIPVEAQSRIFTPFMQVGPSISRTHGGTGIGLSISKCLVGLMKGEIGFSSTPKVGSTFTFTAVFSNGMQPAERKNDNNQPIFSEFRGMKAVVVDHRPARAKVSWYHFQRLGIRVEVVPRVEQALHYLKIGTTTVNMILIEQEIWNREADDFIKKLQKDPLFLSPKLILLANSVESSISEALCTGIDPPIVIVKPLRASMLAATLQRGLGIGIREPPQHKGPPALILRNLLLGRKILIVDDNNVNLRVAAGALKKYGADVVCAESGIKAISLLKPPHEFDACFMDIQMPEMDGFEATRRIRDMEEEMNKRIKNGEALIVENGNKTSWHLPVLAMTADVIQATHEECLKCGMDGYVSKPFEAEQLYREV,,-1.0,MSLFHVLGFGVKIGHLFWMLCCWFVSWFVDNGIEDKSGLLVGSVGDLEKTKMTTLKKKNKMWFWNKISSSGLKIPSFSYQFLGSVKFNKAWWRKLVVVWVVFWVLVSIWTFWYFSSQAMEKRKETLASMCDERARMLQDQFNVSMNHVQAMSILISTFHHGKIPSAIDQRTFSEYTDRTSFERPLTSGVAYAMRVLHSEREEFERQQGWTIRKMYSLEQNPVHKDDYDLEALEPSPVQEEYAPVIFAQDTVSHVVSLDMLSGKEDRENVLRARSSGKGVLTAPFPLIKTNRLGVILTFAVYKRDLPSNATPKERIEATNGYLGGVFDIESLVENLLQQLASKQTILVNVYDITNHSQPISMYGTNVSADGLERVSPLIFGDPLRKHEMRCRFKQKPPWPVLSMVTSFGILVIALLVAHIIHATVSRIHKVEEDCDKMKQLKKKAEAADVAKSQFLATVSHEIRTPMNGVLGMLHMLMDTELDVTQQDYVRTAQASGKALVSLINEVLDQAKIESGKLELEEVRFDLRGILDDVLSLFSSKSQQKGVELAVYISDRVPDMLIGDPGRFRQILTNLMGNSIKFTEKGHIFVTVHLVDELFESIDGETASSPESTLSGLPVADRQRSWENFKAFSSNGHRSFEPSPPDINLIVSVEDTGVGIPVEAQSRIFTPFMQVGPSISRTHGGTGIGLSISKCLVGLMKGEIGFSSTPKVGFTFTFTAVFSNGMQPAERKNDNNQPIFSEFRGMKAVVVDHRPARAKVSWYHFQRLGIRVEVVPRVEQALHYLKIGTTTVNMILIEQEIWNREADDFIKKLQKDPLFLSPKLILLANSVESSISEALCTGIDPPIVIVKPLRASMLAATLQRGLGIGIREPPQHKGPPALILRNLLLGRKILIVDDNNVNLRVAAGALKKYGADVVCAESGIKAISLLKPPHEFDACFMDIQMPEMDGFEATRRIRDMEEEMNKRIKNGEALIVENGNKTSWHLPVLAMTADVIQATHEECLKCGMDGYVSKPFEAEQLYREV,Histidine kinase 3,"Cytokinins (CK) receptor related to bacterial two-component regulators. Functions as a histidine kinase and transmits the stress signal to a downstream MAPK cascade. This protein undergoes an ATP-dependent autophosphorylation at a conserved histidine residue in the kinase core, and a phosphoryl group is then transferred to a conserved aspartate residue in the receiver domain. In the presence of cytokinin, feeds phosphate to phosphorelay-integrating histidine phosphotransfer protein (HPt) and activates subsequent cascade. Involved in meristems establishment in seedlings. Redundant negative regulator of drought and salt stress responses and abscisic acid (ABA) signaling. Together with AHK2, plays a negative regulatory role in cold stress signaling via inhibition of ABA response, occurring independently of the cold acclimation pathway. Redundant positive regulator of cytokinin signaling that regulates many developmental processes including seed germination, cell division, seed size, chlorophyll retention during leaf senescence, root repression and shoot promotion. Can interact with isoprenoid-type cytokinins trans-zeatin (tZ and tZR), cis-zeatin (cZ), dihydrozeatin (DZ), buta-2,3-dienyladenine (HA-8), penta-2,3-dienyladenine (HA-1), 4-methyl-penta-2,3-dienyladenine (HA-10), 4-hydroxy-2-butynyladenine (RM1), 2-propynyladenine (RM3), 2-butynyladenine (RM6), and cytokinin ribosides and ribotides. Together with AHK4, involved in the cytokinin-dependent responses to Pi starvation and sucrose stresses. Promotes cytokinin-mediated leaf longevity through a specific phosphorylation of the response regulator ARR2. Involved in alkamides (e.g. N-isobutyl decanamide) and N-acylethanolamides (NAE) signaling that control meristematic activity and differentiation processes during plant development. Contributes to vascular bundle formation and secondary growth in a cytokinin-dependent manner, probably by promoting the maintenance of mitotic activity and/or identity of procambial cells. Plays a role in the cytokinin-mediated repression of the iron uptake pathway. Required by the cytokinin-dependent flower development regulation pathway.","Decrease in ahk3-4; enhanced sensitivity to cytokinin (mostly in roots), and improved cytokinin repression of several Pi starvation-responsive genes and decreased sucrose sensitivity.","Decrease in ahk3-4; enhanced sensitivity to cytokinin (mostly in roots), and improved cytokinin repression of several Pi starvation-responsive genes and decreased sucrose sensitivity."
3407,3407,0,0,P15289-S391T,MGAPRSLLLALAAGLAVARPPNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMYPGVLVPSSRGGLPLEEVTVAEVLAARGYLTGMAGKWHLGVGPEGAFLPPHQGFHRFLGIPYSHDQGPCQNLTCFPPATPCDGGCDQGLVPIPLLANLSVEAQPPWLPGLEARYMAFAHDLMADAQRQDRPFFLYYASHHTHYPQFSGQSFAERSGRGPFGDSLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGPETMRMSRGGCSGLLRCGKGTTYEGGVREPALAFWPGHIAPGVTHELASSLDLLPTLAALAGAPLPNVTLDGFDLSPLLLGTGKSPRQSLFFYPSYPDEVRGVFAVRTGKYKAHFFTQGSAHSDTTADPACHASSSLTAHEPPLLYDLSKDPGENYNLLGGVAGATPEVLQALKQLQLLKAQLDAAVTFGPSQVARGEDPALQICCHPGCTPRPACCHCPDPHA,,-1.0,MGAPRSLLLALAAGLAVARPPNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMYPGVLVPSSRGGLPLEEVTVAEVLAARGYLTGMAGKWHLGVGPEGAFLPPHQGFHRFLGIPYSHDQGPCQNLTCFPPATPCDGGCDQGLVPIPLLANLSVEAQPPWLPGLEARYMAFAHDLMADAQRQDRPFFLYYASHHTHYPQFSGQSFAERSGRGPFGDSLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGPETMRMSRGGCSGLLRCGKGTTYEGGVREPALAFWPGHIAPGVTHELASSLDLLPTLAALAGAPLPNVTLDGFDLSPLLLGTGKSPRQSLFFYPSYPDEVRGVFAVRSGKYKAHFFTQGSAHSDTTADPACHASSSLTAHEPPLLYDLSKDPGENYNLLGGVAGATPEVLQALKQLQLLKAQLDAAVTFGPSQVARGEDPALQICCHPGCTPRPACCHCPDPHA,Arylsulfatase A,Hydrolyzes cerebroside sulfate.,Decreases 90% of activity. The unknown polymorphism is identified in a late infantile metachromatic leukodystrophy patient. This mutation contributes to an enhancement in ARSA activity and may affect the clinical phenotype.,Decreases 90% of activity. The unknown polymorphism is identified in a late infantile metachromatic leukodystrophy patient. This mutation contributes to an enhancement in ARSA activity and may affect the clinical phenotype.
3408,3408,0,0,Q9H2D1-H147R,MTGQGQSASGSSAWSTVFRHVRYENLIAGVSGGVLSNLALHPLDLVKIRFAVSDGLELRPKYNGILHCLTTIWKLDGLRGLYQGVTPNIWGAGLSWGLYFFFYNAIKSYKTEGRAERLEATEYLVSAAEAGAMTLCITNPLWVTKTRLMLQYDAVVNSPHRQYKGMFDTLVKIYKYEGVRGLYKGFVPGLFGTSHGALQFMAYELLKLKYNQHINRLPEAQLSTVEYISVAALSKIFAVAATYPYQVVRARLQDQHMFYSGVIDVITKTWRKEGVGGFYKGIAPNLIRVTPACCITFVVYENVSHFLLDLREKRK,,-1.0,MTGQGQSASGSSAWSTVFRHVRYENLIAGVSGGVLSNLALHPLDLVKIRFAVSDGLELRPKYNGILHCLTTIWKLDGLRGLYQGVTPNIWGAGLSWGLYFFFYNAIKSYKTEGRAERLEATEYLVSAAEAGAMTLCITNPLWVTKTHLMLQYDAVVNSPHRQYKGMFDTLVKIYKYEGVRGLYKGFVPGLFGTSHGALQFMAYELLKLKYNQHINRLPEAQLSTVEYISVAALSKIFAVAATYPYQVVRARLQDQHMFYSGVIDVITKTWRKEGVGGFYKGIAPNLIRVTPACCITFVVYENVSHFLLDLREKRK,Solute carrier family 25 member 32,Transports folate across the inner membranes of mitochondria. Can also transport FAD across the mitochondrial inner membrane.,In RREI; increases succinate dehydrogenase activity and glycerol-3-phosphate dehydrogenase activity.,In RREI; increases succinate dehydrogenase activity and glycerol-3-phosphate dehydrogenase activity.
3418,3418,0,0,P0AEH1-C399P,MLSFLWDLASFIVALGVLITVHEFGHFWVARRCGVRVERFSIGFGKALWRRTDKLGTEYVIALIPLGGYVKMLDERAEPVVPELRHHAFNNKSVGQRAAIIAAGPVANFIFAIFAYWLVFIIGVPGVRPVVGEIAANSIAAEAQIAPGTELKAVDGIETPDWDAVRLQLVDKIGDESTTITVAPFGSDQRRDVKLDLRHWAFEPDKEDPVSSLGIRPRGPQIEPVLENVQPNSAASKAGLQAGDRIVKVDGQPLTQWVTFVMLVRDNPGKSLALEIERQGSPLSLTLIPESKPGNGKAIGFVGIEPKVIPLPDEYKVVRQYGPFNAIVEATDKTWQLMKLTVSMLGKLITGDVKLNNLSGPISIAKGAGMTAELGVVYYLPFLALISVNLGIINLFPLPVLDGGHLLFLAIEKIKGGPVSERVQDFCYRIGSILLVLLMGLALFNDFSRL,,-1.0,MLSFLWDLASFIVALGVLITVHEFGHFWVARRCGVRVERFSIGFGKALWRRTDKLGTEYVIALIPLGGYVKMLDERAEPVVPELRHHAFNNKSVGQRAAIIAAGPVANFIFAIFAYWLVFIIGVPGVRPVVGEIAANSIAAEAQIAPGTELKAVDGIETPDWDAVRLQLVDKIGDESTTITVAPFGSDQRRDVKLDLRHWAFEPDKEDPVSSLGIRPRGPQIEPVLENVQPNSAASKAGLQAGDRIVKVDGQPLTQWVTFVMLVRDNPGKSLALEIERQGSPLSLTLIPESKPGNGKAIGFVGIEPKVIPLPDEYKVVRQYGPFNAIVEATDKTWQLMKLTVSMLGKLITGDVKLNNLSGPISIAKGAGMTAELGVVYYLPFLALISVNLGIINLFPLCVLDGGHLLFLAIEKIKGGPVSERVQDFCYRIGSILLVLLMGLALFNDFSRL,Regulator of sigma-E protease RseP,"A site-2 regulated intramembrane protease (S2P) that cleaves the peptide bond between 'Ala-108' and 'Cys-109' in the transmembrane region of RseA. Part of a regulated intramembrane proteolysis (RIP) cascade. Acts on DegS-cleaved RseA to release the cytoplasmic domain of RseA, residue 'Val-148' of RseA may be required for this. This provides the cell with sigma-E (RpoE) activity through the proteolysis of RseA. Can also cleave sequences in transmembrane regions of other proteins (such as LacY) as well as liberated signal peptides of beta-lactamase, OmpF, LivK, SecM, PhoA, LivJ, OmpC, Lpp and TorA, probably within the membrane. Cleaves FecR within its transmembrane region to release an N-terminal cytoplasmic fragment which binds to sigma factor FecI, allowing it to activate transcription of the fecABCDE operon which mediates ferric citrate transport.","Increased substrate binding, loses some proteolytic activity.","Increased substrate binding, loses some proteolytic activity."
3423,3423,0,0,P11274-F177Y,MVDPVGFAEAWKAQFPDSEPPRMELRSVGDIEQELERCKASIRRLEQEVNQERFRMIYLQTLLAKEKKSYDRQRWGFRRAAQAPDGASEPRASASRPQPAPADGADPPPAEEPEARPDGEGSPGKARPGTARRPGAAASGERDDRGPPASVAALRSNFERIRKGHGQPGADAEKPFYVNVEFHHERGLVKVNDKEVSDRISSLGSQAMQMERKKSQHGAGSSVGDASRPPYRGRSSESSCGVDGDYEDAELNPRFLKDNLIDANGGSRPPWPPLEYQPYQSIYVGGMMEGEGKGPLLRSQSTSEQEKRLTWPRRSYSPRSFEDCGGGYTPDCSSNENLTSSEEDFSSGQSSRVSPSPTTYRMFRDKSRSPSQNSQQSFDSSSPPTPQCHKRHRHCPVVVSEATIVGVRKTGQIWPNDGEGAFHGDADGSFGTPPGYGCAADRAEEQRRHQDGLPYIDDSPSSSPHLSSKGRGSRDALVSGALESTKASELDLEKGLEMRKWVLSGILASEETYLSHLEALLLPMKPLKAAATTSQPVLTSQQIETIFFKVPELYEIHKEFYDGLFPRVQQWSHQQRVGDLFQKLASQLGVYRAFVDNYGVAMEMAEKCCQANAQFAEISENLRARSNKDAKDPTTKNSLETLLYKPVDRVTRSTLVLHDLLKHTPASHPDHPLLQDALRISQNFLSSINEEITPRRQSMTVKKGEHRQLLKDSFMVELVEGARKLRHVFLFTDLLLCTKLKKQSGGKTQQYDCKWYIPLTDLSFQMVDELEAVPNIPLVPDEELDALKIKISQIKNDIQREKRANKGSKATERLKKKLSEQESLLLLMSPSMAFRVHSRNGKSYTFLISSDYERAEWRENIREQQKKCFRSFSLTSVELQMLTNSCVKLQTVHSIPLTINKEDDESPGLYGFLNVIVHSATGFKQSSNLYCTLEVDSFGYFVNKAKTRVYRDTAEPNWNEEFEIELEGSQTLRILCYEKCYNKTKIPKEDGESTDRLMGKGQVQLDPQALQDRDWQRTVIAMNG,,-1.0,MVDPVGFAEAWKAQFPDSEPPRMELRSVGDIEQELERCKASIRRLEQEVNQERFRMIYLQTLLAKEKKSYDRQRWGFRRAAQAPDGASEPRASASRPQPAPADGADPPPAEEPEARPDGEGSPGKARPGTARRPGAAASGERDDRGPPASVAALRSNFERIRKGHGQPGADAEKPFFVNVEFHHERGLVKVNDKEVSDRISSLGSQAMQMERKKSQHGAGSSVGDASRPPYRGRSSESSCGVDGDYEDAELNPRFLKDNLIDANGGSRPPWPPLEYQPYQSIYVGGMMEGEGKGPLLRSQSTSEQEKRLTWPRRSYSPRSFEDCGGGYTPDCSSNENLTSSEEDFSSGQSSRVSPSPTTYRMFRDKSRSPSQNSQQSFDSSSPPTPQCHKRHRHCPVVVSEATIVGVRKTGQIWPNDGEGAFHGDADGSFGTPPGYGCAADRAEEQRRHQDGLPYIDDSPSSSPHLSSKGRGSRDALVSGALESTKASELDLEKGLEMRKWVLSGILASEETYLSHLEALLLPMKPLKAAATTSQPVLTSQQIETIFFKVPELYEIHKEFYDGLFPRVQQWSHQQRVGDLFQKLASQLGVYRAFVDNYGVAMEMAEKCCQANAQFAEISENLRARSNKDAKDPTTKNSLETLLYKPVDRVTRSTLVLHDLLKHTPASHPDHPLLQDALRISQNFLSSINEEITPRRQSMTVKKGEHRQLLKDSFMVELVEGARKLRHVFLFTDLLLCTKLKKQSGGKTQQYDCKWYIPLTDLSFQMVDELEAVPNIPLVPDEELDALKIKISQIKNDIQREKRANKGSKATERLKKKLSEQESLLLLMSPSMAFRVHSRNGKSYTFLISSDYERAEWRENIREQQKKCFRSFSLTSVELQMLTNSCVKLQTVHSIPLTINKEDDESPGLYGFLNVIVHSATGFKQSSNLYCTLEVDSFGYFVNKAKTRVYRDTAEPNWNEEFEIELEGSQTLRILCYEKCYNKTKIPKEDGESTDRLMGKGQVQLDPQALQDRDWQRTVIAMNG,Breakpoint cluster region protein,"Protein with a unique structure having two opposing regulatory activities toward small GTP-binding proteins. The C-terminus is a GTPase-activating protein (GAP) domain which stimulates GTP hydrolysis by RAC1, RAC2 and CDC42. Accelerates the intrinsic rate of GTP hydrolysis of RAC1 or CDC42, leading to down-regulation of the active GTP-bound form. The central Dbl homology (DH) domain functions as guanine nucleotide exchange factor (GEF) that modulates the GTPases CDC42, RHOA and RAC1. Promotes the conversion of CDC42, RHOA and RAC1 from the GDP-bound to the GTP-bound form. The amino terminus contains an intrinsic kinase activity. Functions as an important negative regulator of neuronal RAC1 activity. Regulates macrophage functions such as CSF1-directed motility and phagocytosis through the modulation of RAC1 activity. Plays a major role as a RHOA GEF in keratinocytes being involved in focal adhesion formation and keratinocyte differentiation.","Enables interaction with FES and GRB2. The mutation in the Fes protein has been shown to fully facilitate the acceleration of neurite outgrowth in response to NGF treatment. This mutation also leads to non-constitutive relocalization of endogenous Rac1 to the cell periphery, resulting in subtle actin reorganization and controlled neurite extension. This results in the promotion of the binding of Grb2 to Y177 of Bcr-Abl, facilitating downstream signaling events.","Enables interaction with FES and GRB2. The mutation in the Fes protein has been shown to fully facilitate the acceleration of neurite outgrowth in response to NGF treatment. This mutation also leads to non-constitutive relocalization of endogenous Rac1 to the cell periphery, resulting in subtle actin reorganization and controlled neurite extension. This results in the promotion of the binding of Grb2 to Y177 of Bcr-Abl, facilitating downstream signaling events."
3424,3424,0,0,P06132-T260I,MEANGLGPQGFPELKNDTFLRAAWGEETDYTPVWCMRQAGRYLPEFRETRAAQDFFSTCRSPEACCELTLQPLRRFPLDAAIIFSDILVVPQALGMEVTMVPGKGPSFPEPLREEQDLERLRDPEVVASELGYVFQAITLTRQRLAGRVPLIGFAGAPWTLMTYMVEGGGSSTMAQAKRWLYQRPQASHQLLRILTDALVPYLVGQVVAGAQALQLFESHAGHLGPQLFNKFALPYIRDVAKQVKARLREAGLAPVPMIIFAKDGHFALEELAQAGYEVVGLDWTVAPKKARECVGKTVTLQGNLDPCALYASEEEIGQLVKQMLDDFGPHRYIANLGHGLYPDMDPEHVGAFVDAVHKHSRLLRQN,,-1.0,MEANGLGPQGFPELKNDTFLRAAWGEETDYTPVWCMRQAGRYLPEFRETRAAQDFFSTCRSPEACCELTLQPLRRFPLDAAIIFSDILVVPQALGMEVTMVPGKGPSFPEPLREEQDLERLRDPEVVASELGYVFQAITLTRQRLAGRVPLIGFAGAPWTLMTYMVEGGGSSTMAQAKRWLYQRPQASHQLLRILTDALVPYLVGQVVAGAQALQLFESHAGHLGPQLFNKFALPYIRDVAKQVKARLREAGLAPVPMITFAKDGHFALEELAQAGYEVVGLDWTVAPKKARECVGKTVTLQGNLDPCALYASEEEIGQLVKQMLDDFGPHRYIANLGHGLYPDMDPEHVGAFVDAVHKHSRLLRQN,Uroporphyrinogen decarboxylase,"Catalyzes the sequential decarboxylation of the four acetate side chains of uroporphyrinogen to form coproporphyrinogen and participates in the fifth step in the heme biosynthetic pathway. Isomer I or isomer III of uroporphyrinogen may serve as substrate, but only coproporphyrinogen III can ultimately be converted to heme. In vitro also decarboxylates pentacarboxylate porphyrinogen I.",Increase of activity.,Increase of activity.
3437,3437,0,0,P18898-D216H,MCQATNGPSRVVTKKHRKFFERHLQLLPSSHQGHDVNRMAIIFYSISGLSIFDVNVSAKYGDHLGWMRKHYIKTVLDDTENTVISGFVGSLVMNIPHATTINLPNTLFALLSMIMLRDYEYFETILDKRSLARFVSKCQRPDRGSFVSCLDYKTNCGSSVDSDDLRFCYIAVAILYICGCRSKEDFDEYIDTEKLLGYIMSQQCYNGAFGAHNEPHSGYTSCALSTLALLSSLEKLSDKFKEDTITWLLHRQVSSHGCMKFESELNASYDQSDDGGFQGRENKFADTCYAFWCLNSLHLLTKDWKMLCQTELVTNYLLDRTQKTLTGGFSKNDEEDADLYHSCLGSAALALIEGKFNGELCIPQEIFNDFSKRCCF,,-1.0,MCQATNGPSRVVTKKHRKFFERHLQLLPSSHQGHDVNRMAIIFYSISGLSIFDVNVSAKYGDHLGWMRKHYIKTVLDDTENTVISGFVGSLVMNIPHATTINLPNTLFALLSMIMLRDYEYFETILDKRSLARFVSKCQRPDRGSFVSCLDYKTNCGSSVDSDDLRFCYIAVAILYICGCRSKEDFDEYIDTEKLLGYIMSQQCYNGAFGAHNEPDSGYTSCALSTLALLSSLEKLSDKFKEDTITWLLHRQVSSHGCMKFESELNASYDQSDDGGFQGRENKFADTCYAFWCLNSLHLLTKDWKMLCQTELVTNYLLDRTQKTLTGGFSKNDEEDADLYHSCLGSAALALIEGKFNGELCIPQEIFNDFSKRCCF,Geranylgeranyl transferase type-1 subunit beta,"Catalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl diphosphate to proteins having the C-terminal sequence Cys-Ile-Ile-Leu or Cys-Val-Leu-Leu. Acts, among other substrates, on Rho1 and Rho2 and CDC42 proteins. Participates in a RAS-like C-terminal modification of proteins involved in nuclear division and bud growth. It is involved in bud positioning and cell polarity. The beta subunit is responsible for isoprenoid and peptide-binding.",Decreases KM for peptide substrate 12-fold. The histidine 216 residue of the beta subunit was changed to aspartic acid (betaH216D) by sequential PCR using mutagenic primers. The mutants were assayed for GGPT-I activity. The Km value for GST-CAIL in the betaH216D mutant decreased about 12-fold. The histidine 216 residue was assumed to be an non-essential part of binding of peptide substrate.,Decreases KM for peptide substrate 12-fold. The histidine 216 residue of the beta subunit was changed to aspartic acid (betaH216D) by sequential PCR using mutagenic primers. The mutants were assayed for GGPT-I activity. The Km value for GST-CAIL in the betaH216D mutant decreased about 12-fold. The histidine 216 residue was assumed to be an non-essential part of binding of peptide substrate.
3441,3441,0,0,Q14116-A49R,MAAEPVEDNCINFVAMKFIDNTLYFIAEDDENLESDYFGKLESKLSVIRNLNDQVLFIDQGNRPLFEDMTDSDCRDNAPRTIFIISMYKDSQPRGMAVTISVKCEKISTLSCENKIISFKEMNPPDNIKDTKSDIIFFQRSVPGHDNKMQFESSSYEGYFLACEKERDLFKLILKKEDELGDRSIMFTVQNED,,-1.0,MAAEPVEDNCINFVAMKFIDNTLYFIAEDDENLESDYFGKLESKLSVIANLNDQVLFIDQGNRPLFEDMTDSDCRDNAPRTIFIISMYKDSQPRGMAVTISVKCEKISTLSCENKIISFKEMNPPDNIKDTKSDIIFFQRSVPGHDNKMQFESSSYEGYFLACEKERDLFKLILKKEDELGDRSIMFTVQNED,Interleukin-18,"Pro-inflammatory cytokine primarily involved in epithelial barrier repair, polarized T-helper 1 (Th1) cell and natural killer (NK) cell immune responses. Upon binding to IL18R1 and IL18RAP, forms a signaling ternary complex which activates NF-kappa-B, triggering synthesis of inflammatory mediators. Synergizes with IL12/interleukin-12 to induce IFNG synthesis from T-helper 1 (Th1) cells and natural killer (NK) cells. Involved in transduction of inflammation downstream of pyroptosis: its mature form is specifically released in the extracellular milieu by passing through the gasdermin-D (GSDMD) pore.",Enhances binding to IL18R1 and the ability to induce IFNG production.,Enhances binding to IL18R1 and the ability to induce IFNG production.
3452,3452,0,0,Q9BTV5-D324S,MEEQREALRKIIKTLAVKNEEIQSFIYSLKQMLLNVEANSAKVQEDLEAEFQSLFSLLEELKEGMLMKIKQDRASRTYELQNQLAACTRALESSEELLETANQTLQAMDSEDFPQAAKQIKDGVTMAPAFRLSLKAKVSDNMSHLMVDFAQERQMLQALKFLPVPSAPVIDLAESLVADNCVTLVWRMPDEDSKIDHYVLEYRRTNFEGPPRLKEDQPWMVIEGIRQTEYTLTGLKFDMKYMNFRVKACNKAVAGEFSEPVTLETPAFMFRLDASTSHQNLRVDDLSVEWDAMGGKVQDIKAREKDGKGRTASPINSPARGTPSPKRMPSGRGGRDRFTAESYTVLGDTLIDGGEHYWEVRYEPDSKAFGVGVAYRSLGRFEQLGKTAASWCLHVNNWLQVSFTAKHANKVKVLDAPVPDCLGVHCDFHQGLLSFYNARTKQVLHTFKTRFTQPLLPAFTVWCGSFQVTTGLQVPSAVRCLQKRGSATSSSNTSLT,,-1.0,MEEQREALRKIIKTLAVKNEEIQSFIYSLKQMLLNVEANSAKVQEDLEAEFQSLFSLLEELKEGMLMKIKQDRASRTYELQNQLAACTRALESSEELLETANQTLQAMDSEDFPQAAKQIKDGVTMAPAFRLSLKAKVSDNMSHLMVDFAQERQMLQALKFLPVPSAPVIDLAESLVADNCVTLVWRMPDEDSKIDHYVLEYRRTNFEGPPRLKEDQPWMVIEGIRQTEYTLTGLKFDMKYMNFRVKACNKAVAGEFSEPVTLETPAFMFRLDASTSHQNLRVDDLSVEWDAMGGKVQDIKAREKDGKGRTASPINSPARGTPDPKRMPSGRGGRDRFTAESYTVLGDTLIDGGEHYWEVRYEPDSKAFGVGVAYRSLGRFEQLGKTAASWCLHVNNWLQVSFTAKHANKVKVLDAPVPDCLGVHCDFHQGLLSFYNARTKQVLHTFKTRFTQPLLPAFTVWCGSFQVTTGLQVPSAVRCLQKRGSATSSSNTSLT,Fibronectin type III and SPRY domain-containing protein 1,May be involved in microtubule organization and stabilization.,Increased ability to associate with microtubules; when associated with D-313; D-317 and E-322. Dephosphorylation at S324 strengthens the interaction with microtubules.,Increased ability to associate with microtubules; when associated with D-313; D-317 and E-322. Dephosphorylation at S324 strengthens the interaction with microtubules.
3458,3458,0,0,Q8GUK1-N457D,MDSQPPVNESTPSTALSNFGELVPFYSSYLWNRLASLLPTSKPIFLGKISNLYRQTVSRKRSISFPLPLPSDFPSSSTITSNVSADTARIHGVLEEIMADVLSNLHDIQKSLDFWRSRAEGSNARKAYFMIFERGPTAFVNESTKFVSKSLSEDSAMQHLCQSSSSHMTERMRVLVELRSALASFIAQLYVELDKRGEDLVKIPEKALPSLLAVINGLFSNLEGSFSHLHAVRECDSSVDGSYPMPLVFDRLPEVNEEGSQWTDCELTDAINLVHKNLEKLNSYLSVMVGKHRKPRRMTLYWVRYTCGAVGLSVFSIWLLRHSSLMGSSDIENWVHDAKEATMSFFSDHVEQPLLSIRDELFDTFRKRHKGVMETEEVQLTQDSLHRMLRNFCEQATREKVPDNASDQEMLEVVMNRYEKELVHPIHNLLSGELARGLLIQVQKLKLDIETAMLELDQILRANEINFAILAALPAFFLSIVMLTVLRTWLKKDSKAQGRGRIARIHRRLLVVEIEKRIMQYQSYIEQGRDKDAETVFGLLIYSLERLYRVVEKPARATDEWDLVKQDLIELGRPQQQTSYKLTVTQRLVTVYDCLLPTLKRQ,,-1.0,MDSQPPVNESTPSTALSNFGELVPFYSSYLWNRLASLLPTSKPIFLGKISNLYRQTVSRKRSISFPLPLPSDFPSSSTITSNVSADTARIHGVLEEIMADVLSNLHDIQKSLDFWRSRAEGSNARKAYFMIFERGPTAFVNESTKFVSKSLSEDSAMQHLCQSSSSHMTERMRVLVELRSALASFIAQLYVELDKRGEDLVKIPEKALPSLLAVINGLFSNLEGSFSHLHAVRECDSSVDGSYPMPLVFDRLPEVNEEGSQWTDCELTDAINLVHKNLEKLNSYLSVMVGKHRKPRRMTLYWVRYTCGAVGLSVFSIWLLRHSSLMGSSDIENWVHDAKEATMSFFSDHVEQPLLSIRDELFDTFRKRHKGVMETEEVQLTQDSLHRMLRNFCEQATREKVPDNASDQEMLEVVMNRYEKELVHPIHNLLSGELARGLLIQVQKLKLDIETAMLELNQILRANEINFAILAALPAFFLSIVMLTVLRTWLKKDSKAQGRGRIARIHRRLLVVEIEKRIMQYQSYIEQGRDKDAETVFGLLIYSLERLYRVVEKPARATDEWDLVKQDLIELGRPQQQTSYKLTVTQRLVTVYDCLLPTLKRQ,"Protein DGS1, mitochondrial","Involved in galactoglycerolipid biosynthesis. Contributes to an intracellular signal that regulates an alternative DGD1-independent galactoglycerolipid biosynthesis pathway in chloroplasts. Being involved in mitochondrial lipid homeostasis, modulates mitochondrion biogenesis and physiology, as well as stress responses.",Partially reduces digalactoglycerolipid content in the dgd1 mutant.,Partially reduces digalactoglycerolipid content in the dgd1 mutant.
3472,3472,0,0,P37484-A420D,MPSFYEKPLFRYPIYALIALSIITILISFYFNWILGTVEVLLLAVILFFIKRADSLIRQEIDAYISTLSYRLKKVGEEALMEMPIGIMLFNDQYYIEWANPFLSSCFNESTLVGRSLYDTCESVVPLIKQEVESETVTLNDRKFRVVIKRDERLLYFFDVTEQIQIEKLYENERTVLAYIFLDNYDDVTQGLDDQTRSTMNSQVTSLLNAWAQEYGIFLKRTSSERFIAVLNEHILTELENSKFSILDEVREKTSFDGVALTLSVGVGASVSSLKELGDLAQSSLDLALGRGGDQVAIKLPNGKVKFYGGKTNPMEKRTRVRARVISHALKEIVTESSNVIIMGHKFPDMDSIGAAIGILKVAQANNKDGFIVIDPNQIGSSVQRLIGEIKKYEELWSRFITPEEAMEISNDDTLLVIVDTHKPSLVMEERLVNKIEHIVVIDHHRRGEEFIRDPLLVYMEPYASSTAELVTELLEYQPKRLKINMIEATALLAGIIVDTKSFSLRTGSRTFDAASYLRAKGADTVLVQKFLKETVDSYIKRAKLIQHTVLYKDNIAIASLPENEEEYFDQVLIAQAADSLLSMSEVEASFAVARRDEQTVCISARSLGEVNVQIIMEALEGGGHLTNAATQLSGISVSEALERLKHAIDEYFEGGVQR,,-1.0,MPSFYEKPLFRYPIYALIALSIITILISFYFNWILGTVEVLLLAVILFFIKRADSLIRQEIDAYISTLSYRLKKVGEEALMEMPIGIMLFNDQYYIEWANPFLSSCFNESTLVGRSLYDTCESVVPLIKQEVESETVTLNDRKFRVVIKRDERLLYFFDVTEQIQIEKLYENERTVLAYIFLDNYDDVTQGLDDQTRSTMNSQVTSLLNAWAQEYGIFLKRTSSERFIAVLNEHILTELENSKFSILDEVREKTSFDGVALTLSVGVGASVSSLKELGDLAQSSLDLALGRGGDQVAIKLPNGKVKFYGGKTNPMEKRTRVRARVISHALKEIVTESSNVIIMGHKFPDMDSIGAAIGILKVAQANNKDGFIVIDPNQIGSSVQRLIGEIKKYEELWSRFITPEEAMEISNDDTLLVIVATHKPSLVMEERLVNKIEHIVVIDHHRRGEEFIRDPLLVYMEPYASSTAELVTELLEYQPKRLKINMIEATALLAGIIVDTKSFSLRTGSRTFDAASYLRAKGADTVLVQKFLKETVDSYIKRAKLIQHTVLYKDNIAIASLPENEEEYFDQVLIAQAADSLLSMSEVEASFAVARRDEQTVCISARSLGEVNVQIIMEALEGGGHLTNAATQLSGISVSEALERLKHAIDEYFEGGVQR,Cyclic-di-AMP phosphodiesterase GdpP,"Has phosphodiesterase (PDE) activity against cyclic-di-AMP (c-di-AMP) and to a much lesser extent against cyclic-di-GMP (c-di-GMP) in the DHH/DHHA1 domains. Also has ATPase activity, probably via the GGDEF domain. Overexpression leads to increased sensitivity to methyl methanesulfonate (MMS) and H(2)O(2). Overexpression leads to extreme sensitivity to the beta-lactam antibiotic cefuroxime (CEF), probably dependent on PDE activity. May monitor cellular heme or NO levels. In B.subtilis c-di-AMP is a second messenger that mediates growth, DNA repair and cell wall homeostasis; it is toxic when present in excess.","Decrease in phosphodiesterase activity, confers antibiotic sensitivity when overexpressed. The DHH/DHHA1 domain synthesizes c-di-AMP and c-di-GMP from the linear dinucleotides 5'-pApA and 5'-pGpG. The mutation in σ(M) abolishes cefuroxime resistance to a sigM null mutant.","Decrease in phosphodiesterase activity, confers antibiotic sensitivity when overexpressed. The DHH/DHHA1 domain synthesizes c-di-AMP and c-di-GMP from the linear dinucleotides 5'-pApA and 5'-pGpG. The mutation in σ(M) abolishes cefuroxime resistance to a sigM null mutant."
3483,3483,0,0,P00734-C425R,MAHVRGLQLPGCLALAALCSLVHSQHVFLAPQQARSLLQRVRRANTFLEEVRKGNLERECVEETCSYEEAFEALESSTATDVFWAKYTACETARTPRDKLAACLEGNCAEGLGTNYRGHVNITRSGIECQLWRSRYPHKPEINSTTHPGADLQENFCRNPDSSTTGPWCYTTDPTVRRQECSIPVCGQDQVTVAMTPRSEGSSVNLSPPLEQCVPDRGQQYQGRLAVTTHGLPCLAWASAQAKALSKHQDFNSAVQLVENFCRNPDGDEEGVWCYVAGKPGDFGYCDLNYCEEAVEEETGDGLDEDSDRAIEGRTATSEYQTFFNPRTFGSGEADCGLRPLFEKKSLEDKTERELLESYIDGRIVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTENDLLVRIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDIALMKLKKPVAFSDYIHPVCLPDRETAASLLQAGYKGRVTGWGNLKETWTANVGKGQPSVLQVVNLPIVERPVCKDSTRIRITDNMFCAGYKPDEGKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKKWIQKVIDQFGE,,-1.0,MAHVRGLQLPGCLALAALCSLVHSQHVFLAPQQARSLLQRVRRANTFLEEVRKGNLERECVEETCSYEEAFEALESSTATDVFWAKYTACETARTPRDKLAACLEGNCAEGLGTNYRGHVNITRSGIECQLWRSRYPHKPEINSTTHPGADLQENFCRNPDSSTTGPWCYTTDPTVRRQECSIPVCGQDQVTVAMTPRSEGSSVNLSPPLEQCVPDRGQQYQGRLAVTTHGLPCLAWASAQAKALSKHQDFNSAVQLVENFCRNPDGDEEGVWCYVAGKPGDFGYCDLNYCEEAVEEETGDGLDEDSDRAIEGRTATSEYQTFFNPRTFGSGEADCGLRPLFEKKSLEDKTERELLESYIDGRIVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTENDLLVCIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDIALMKLKKPVAFSDYIHPVCLPDRETAASLLQAGYKGRVTGWGNLKETWTANVGKGQPSVLQVVNLPIVERPVCKDSTRIRITDNMFCAGYKPDEGKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKKWIQKVIDQFGE,Prothrombin,"Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing.","Enhancement in FA2D; Quick-1. The original residue in this protein is C-425 which is replaced by R. This could result from a point mutation in the C codon, TGC, to yield CGC. Together, these results indicate that C-425 is a critical residue in determining the specificity of thrombin toward fibrinogen.","Enhancement in FA2D; Quick-1. The original residue in this protein is C-425 which is replaced by R. This could result from a point mutation in the C codon, TGC, to yield CGC. Together, these results indicate that C-425 is a critical residue in determining the specificity of thrombin toward fibrinogen."
3501,3501,0,0,Q5SQI0-A102K,MEFPFDVDALFPERITVLDQHLRPPARRPGTTTPARVDLQQQIMTIIDELGKASAKAQNLSAPITSASRMQSNRHVVYILKDSSARPAGKGAIIGFIKVGYKKLFVLDDREAHNEVEPLCILDFYIHESVQRHGHGRELFQYMLQKERVEPHQLAIDRPSQKLLKFLNKHYNLETTVPQVNNFVIFEGFFAHQHRPPAPSLRATRHSRAAAVDPTPAAPARKLPPKRAEGDIKPYSSSDREFLKVAVEPPWPLNRAPRRATPPAHPPPRSSSLGNSPERGPLRPFVPEQELLRSLRLCPPHPTARLLLAADPGGSPAQRRRTRGTPPGLVAQSCCYSRHGGVNSSSPNTGNQDSKQGEQETKNRSASEEQALSQDGSGEKPMHTAPPQAPAPPAQSWTVGGDILNARFIRNLQERRSTRPW,,-1.0,MEFPFDVDALFPERITVLDQHLRPPARRPGTTTPARVDLQQQIMTIIDELGKASAKAQNLSAPITSASRMQSNRHVVYILKDSSARPAGKGAIIGFIKVGYAKLFVLDDREAHNEVEPLCILDFYIHESVQRHGHGRELFQYMLQKERVEPHQLAIDRPSQKLLKFLNKHYNLETTVPQVNNFVIFEGFFAHQHRPPAPSLRATRHSRAAAVDPTPAAPARKLPPKRAEGDIKPYSSSDREFLKVAVEPPWPLNRAPRRATPPAHPPPRSSSLGNSPERGPLRPFVPEQELLRSLRLCPPHPTARLLLAADPGGSPAQRRRTRGTPPGLVAQSCCYSRHGGVNSSSPNTGNQDSKQGEQETKNRSASEEQALSQDGSGEKPMHTAPPQAPAPPAQSWTVGGDILNARFIRNLQERRSTRPW,Alpha-tubulin N-acetyltransferase 1,"Specifically acetylates 'Lys-40' in alpha-tubulin on the lumenal side of microtubules. Promotes microtubule destabilization and accelerates microtubule dynamics; this activity may be independent of acetylation activity. Acetylates alpha-tubulin with a slow enzymatic rate, due to a catalytic site that is not optimized for acetyl transfer. Enters the microtubule through each end and diffuses quickly throughout the lumen of microtubules. Acetylates only long/old microtubules because of its slow acetylation rate since it does not have time to act on dynamically unstable microtubules before the enzyme is released. Required for normal sperm flagellar function. Promotes directional cell locomotion and chemotaxis, through AP2A2-dependent acetylation of alpha-tubulin at clathrin-coated pits that are concentrated at the leading edge of migrating cells. May facilitate primary cilium assembly.",Strong increase in acetyltransferase activity.,Strong increase in acetyltransferase activity.
3507,3507,0,0,P53039-S177C,MSFYNTSNNANNGGGFYQPSAQFAVPQGSMSFQNTVGSSNTGNDNNLGVAPDPLPVGILHALSTKGYPHEPPLLEEIGINFDHIITKTKMVLIPIRFGSGVPQEILNDSDLAGPLIFFLLFGLFLLMAGKVHFGYIYGVALFGTISLHNLSKLMSNNDTSTQTNLQFFNTASILGYCFLPLCFLSLLGIFHGLNNTTGYVVSVLFVIWSTWTSSGFLNSLLQLQNARLLIAYPLLIFYSVFALMVIFV,,-1.0,MSFYNTSNNANNGGGFYQPSAQFAVPQGSMSFQNTVGSSNTGNDNNLGVAPDPLPVGILHALSTKGYPHEPPLLEEIGINFDHIITKTKMVLIPIRFGSGVPQEILNDSDLAGPLIFFLLFGLFLLMAGKVHFGYIYGVALFGTISLHNLSKLMSNNDTSTQTNLQFFNTASILGYSFLPLCFLSLLGIFHGLNNTTGYVVSVLFVIWSTWTSSGFLNSLLQLQNARLLIAYPLLIFYSVFALMVIFV,Protein transport protein YIP1,"Required for fusion of ER-derived vesicles with the Golgi during ER-to-Golgi protein transport, probably by mediating correct membrane localization of YPT1.","Enhances binding to YIF1, YPT1 and YPT31.","Enhances binding to YIF1, YPT1 and YPT31."
3519,3519,0,0,Q9H267-R576C,MAFPHRPDAPELPDFSMLKRLARDQLIYLLEQLPGKKDLFIEADLMSPLDRIANVSILKQHEVDKLYKVENKPALSSNEQLCFLVRPRIKNMRYIASLVNADKLAGRTRKYKVIFSPQKFYACEMVLEEEGIYGDVSCDEWAFSLLPLDVDLLSMELPEFFRDYFLEGDQRWINTVAQALHLLSTLYGPFPNCYGIGRCAKMAYELWRNLEEEEDGETKGRRPEIGHIFLLDRDVDFVTALCSQVVYEGLVDDTFRIKCGSVDFGPEVTSSDKSLKVLLNAEDKVFNEIRNEHFSNVFGFLSQKARNLQAQYDRRRGMDIKQMKNFVSQELKGLKQEHRLLSLHIGACESIMKKKTKQDFQELIKTEHALLEGFNIRESTSYIEEHIDRQVSPIESLRLMCLLSITENGLIPKDYRSLKTQYLQSYGPEHLLTFSNLRRAGLLTEQAPGDTLTAVESKVSKLVTDKAAGKITDAFSSLAKRSNFRAISKKLNLIPRVDGEYDLKVPRDMAYVFGGAYVPLSCRIIEQVLERRSWQGLDEVVRLLNCSDFAFTDMTKEDKASSESLRLILVVFLGGCTFSEISALRFLGREKGYRFIFLTTAVTNSARLMEAMSEVKA,,-1.0,MAFPHRPDAPELPDFSMLKRLARDQLIYLLEQLPGKKDLFIEADLMSPLDRIANVSILKQHEVDKLYKVENKPALSSNEQLCFLVRPRIKNMRYIASLVNADKLAGRTRKYKVIFSPQKFYACEMVLEEEGIYGDVSCDEWAFSLLPLDVDLLSMELPEFFRDYFLEGDQRWINTVAQALHLLSTLYGPFPNCYGIGRCAKMAYELWRNLEEEEDGETKGRRPEIGHIFLLDRDVDFVTALCSQVVYEGLVDDTFRIKCGSVDFGPEVTSSDKSLKVLLNAEDKVFNEIRNEHFSNVFGFLSQKARNLQAQYDRRRGMDIKQMKNFVSQELKGLKQEHRLLSLHIGACESIMKKKTKQDFQELIKTEHALLEGFNIRESTSYIEEHIDRQVSPIESLRLMCLLSITENGLIPKDYRSLKTQYLQSYGPEHLLTFSNLRRAGLLTEQAPGDTLTAVESKVSKLVTDKAAGKITDAFSSLAKRSNFRAISKKLNLIPRVDGEYDLKVPRDMAYVFGGAYVPLSCRIIEQVLERRSWQGLDEVVRLLNCSDFAFTDMTKEDKASSESLRLILVVFLGGRTFSEISALRFLGREKGYRFIFLTTAVTNSARLMEAMSEVKA,Vacuolar protein sorting-associated protein 33B,"May play a role in vesicle-mediated protein trafficking to lysosomal compartments and in membrane docking/fusion reactions of late endosomes/lysosomes. Required for proper trafficking and targeting of the collagen-modifying enzyme lysyl hydroxylase 3 (LH3) to intracellular collagen. Mediates phagolysosomal fusion in macrophages. Proposed to be involved in endosomal maturation implicating VIPAS39. In epithelial cells, the VPS33B:VIPAS39 complex may play a role in the apical recycling pathway and in the maintenance of the apical-basolateral polarity. Seems to be involved in the sorting of specific cargos from the trans-Golgi network to alpha-granule-destined multivesicular bodies (MVBs) promoting MVBs maturation in megakaryocytes.","Increases colocalization with VIPAS39 at cytoplasmic organelle; increased protein expression. The patients with the mutation in the VPS33B gene exhibited isolated high-GGT cholestasis with manageable pruritus. This mutation caused increased protein expression and enabled interaction with VIPAS39 in-vitro. The patients with this mutation had a lower level of total secondary bile acids, indicating complete residual function of VPS33B.","Increases colocalization with VIPAS39 at cytoplasmic organelle; increased protein expression. The patients with the mutation in the VPS33B gene exhibited isolated high-GGT cholestasis with manageable pruritus. This mutation caused increased protein expression and enabled interaction with VIPAS39 in-vitro. The patients with this mutation had a lower level of total secondary bile acids, indicating complete residual function of VPS33B."
3520,3520,0,0,Q9DA75-A202T,MAKGEGAESGSAAGLLPTSILQASERPVQVKKEPKKKQQLSICNKLCYAVGGAPYQLTGCALGFFLQIYLLDVAKVEPLPASIILFVGRAWDAFTDPLVGFCISKSSWTRLGRLMPWIIFSTPLAIIAYFLIWFVPDFPSGTESSHGFLWYLLFYCLFETLVTCFHVPYSALTMFISTEQSERDSATAYRMTVEVLGTVIGTAIQGQIVGQAKAPCLQDQNGSVVVSEVANRTQSTASLKDTQNAYLLAAGIIASIYVLCAFILILGVREQRELYESQQAESMPFFQGLRLVMGHGPYVKLIAGFLFTSLAFMLVEGNFALFCTYTLDFRNEFQNLLLAIMLSATFTIPIWQWFLTRFGKKTAVYIGISSAVPFLILVALMERNLIVTYVVAVAAGVSVAAAFLLPWSMLPDVIDDFHLKHPHSPGTEPIFFSFYVFFTKFASGVSLGVSTLSLDFANYQRQGCSQPEQVKFTLKMLVTMAPIILILLGLLLFKLYPIDEEKRRQNKKALQALREEASSSGCSDTDSTELASIL,,-1.0,MAKGEGAESGSAAGLLPTSILQASERPVQVKKEPKKKQQLSICNKLCYAVGGAPYQLTGCALGFFLQIYLLDVAKVEPLPASIILFVGRAWDAFTDPLVGFCISKSSWTRLGRLMPWIIFSTPLAIIAYFLIWFVPDFPSGTESSHGFLWYLLFYCLFETLVTCFHVPYSALTMFISTEQSERDSATAYRMTVEVLGTVIGAAIQGQIVGQAKAPCLQDQNGSVVVSEVANRTQSTASLKDTQNAYLLAAGIIASIYVLCAFILILGVREQRELYESQQAESMPFFQGLRLVMGHGPYVKLIAGFLFTSLAFMLVEGNFALFCTYTLDFRNEFQNLLLAIMLSATFTIPIWQWFLTRFGKKTAVYIGISSAVPFLILVALMERNLIVTYVVAVAAGVSVAAAFLLPWSMLPDVIDDFHLKHPHSPGTEPIFFSFYVFFTKFASGVSLGVSTLSLDFANYQRQGCSQPEQVKFTLKMLVTMAPIILILLGLLLFKLYPIDEEKRRQNKKALQALREEASSSGCSDTDSTELASIL,Sodium-dependent lysophosphatidylcholine symporter 1,"Sodium-dependent lysophosphatidylcholine (LPC) symporter, which plays an essential role for blood-brain barrier formation and function. Specifically expressed in endothelium of the blood-brain barrier of micro-vessels and transports LPC into the brain. Transport of LPC is essential because it constitutes the major mechanism by which docosahexaenoic acid (DHA), an omega-3 fatty acid that is essential for normal brain growth and cognitive function, enters the brain. Transports LPC carrying long-chain fatty acids such LPC oleate and LPC palmitate with a minimum acyl chain length of 14 carbons. Does not transport docosahexaenoic acid in unesterified fatty acid. Not required for central nervous system vascular morphogenesis.",Slightly decreased LPC transport.,Slightly decreased LPC transport.
3522,3522,0,0,P0C1R0-A10K,ILGTILGLLKSL,,-1.0,ILGTILGLLASL,Polybia-CP,"Potent antimicrobial peptide that is active against both Gram-positive and Gram-negative bacteria (B.subtilis (MIC=15 ug/ml or 4-16 uM), S.epidermidis (MIC=8-16 uM), S.aureus (MIC=15 ug/ml or 4 uM), E.coli (MIC=8-64 uM) and P.aeruginosa (MIC=64-128 uM)). Also shows cytotoxicity towards HEK293 cells (32 uM). Adopts an amphipathic alpha helical conformation, that may allow to partition into the target membrane. Acts by disrupting bacterial membrane. Also acts in inflammation since it is chemotactic for polymorphonucleated leukocytes (PMNL). Shows potent antitumor activity against prostate (PC-3) and bladder (Biu-87) cancer cell lines. Causes a reduced hemolysis to mammalian erythrocytes (HC(50)=50 uM) and has no mast cell degranulation activity at physiological concentrations. In addition, when tested in vitro on the parasite Trypanosoma cruzi (responsible of the Chagas disease), is able to reduce the number of the three forms (epimastigote, trypomastigote and amastigote), probably acting through the apoptotic cell death pathway.",Important increase in antibacterial activity and important increase in helical content. The mutation in the polybia-CP peptide reduces its sub-micromolar antimicrobial potency in vitro and anti-infective activity in vivo.,Important increase in antibacterial activity and important increase in helical content. The mutation in the polybia-CP peptide reduces its sub-micromolar antimicrobial potency in vitro and anti-infective activity in vivo.
3526,3526,0,0,P40692-E63D,MSFVAGVIRRLDETVVNRIAAGEVIQRPANAIKEMIENCLDAKSTSIQVIVKEGGLKLIQIQDNGTGIRKEDLDIVCERFTTSKLQSFEDLASISTYGFRGEALASISHVAHVTITTKTADGKCAYRASYSDGKLKAPPKPCAGNQGTQITVEDLFYNIATRRKALKNPSEEYGKILEVVGRYSVHNAGISFSVKKQGETVADVRTLPNASTVDNIRSIFGNAVSRELIEIGCEDKTLAFKMNGYISNANYSVKKCIFLLFINHRLVESTSLRKAIETVYAAYLPKNTHPFLYLSLEISPQNVDVNVHPTKHEVHFLHEESILERVQQHIESKLLGSNSSRMYFTQTLLPGLAGPSGEMVKSTTSLTSSSTSGSSDKVYAHQMVRTDSREQKLDAFLQPLSKPLSSQPQAIVTEDKTDISSGRARQQDEEMLELPAPAEVAAKNQSLEGDTTKGTSEMSEKRGPTSSNPRKRHREDSDVEMVEDDSRKEMTAACTPRRRIINLTSVLSLQEEINEQGHEVLREMLHNHSFVGCVNPQWALAQHQTKLYLLNTTKLSEELFYQILIYDFANFGVLRLSEPAPLFDLAMLALDSPESGWTEEDGPKEGLAEYIVEFLKKKAEMLADYFSLEIDEEGNLIGLPLLIDNYVPPLEGLPIFILRLATEVNWDEEKECFESLSKECAMFYSIRKQYISEESTLSGQQSEVPGSIPNSWKWTVEHIVYKALRSHILPPKHFTEDGNILQLANLPDLYKVFERC,,-1.0,MSFVAGVIRRLDETVVNRIAAGEVIQRPANAIKEMIENCLDAKSTSIQVIVKEGGLKLIQIQENGTGIRKEDLDIVCERFTTSKLQSFEDLASISTYGFRGEALASISHVAHVTITTKTADGKCAYRASYSDGKLKAPPKPCAGNQGTQITVEDLFYNIATRRKALKNPSEEYGKILEVVGRYSVHNAGISFSVKKQGETVADVRTLPNASTVDNIRSIFGNAVSRELIEIGCEDKTLAFKMNGYISNANYSVKKCIFLLFINHRLVESTSLRKAIETVYAAYLPKNTHPFLYLSLEISPQNVDVNVHPTKHEVHFLHEESILERVQQHIESKLLGSNSSRMYFTQTLLPGLAGPSGEMVKSTTSLTSSSTSGSSDKVYAHQMVRTDSREQKLDAFLQPLSKPLSSQPQAIVTEDKTDISSGRARQQDEEMLELPAPAEVAAKNQSLEGDTTKGTSEMSEKRGPTSSNPRKRHREDSDVEMVEDDSRKEMTAACTPRRRIINLTSVLSLQEEINEQGHEVLREMLHNHSFVGCVNPQWALAQHQTKLYLLNTTKLSEELFYQILIYDFANFGVLRLSEPAPLFDLAMLALDSPESGWTEEDGPKEGLAEYIVEFLKKKAEMLADYFSLEIDEEGNLIGLPLLIDNYVPPLEGLPIFILRLATEVNWDEEKECFESLSKECAMFYSIRKQYISEESTLSGQQSEVPGSIPNSWKWTVEHIVYKALRSHILPPKHFTEDGNILQLANLPDLYKVFERC,DNA mismatch repair protein Mlh1,"Heterodimerizes with PMS2 to form MutL alpha, a component of the post-replicative DNA mismatch repair system (MMR). DNA repair is initiated by MutS alpha (MSH2-MSH6) or MutS beta (MSH2-MSH3) binding to a dsDNA mismatch, then MutL alpha is recruited to the heteroduplex. Assembly of the MutL-MutS-heteroduplex ternary complex in presence of RFC and PCNA is sufficient to activate endonuclease activity of PMS2. It introduces single-strand breaks near the mismatch and thus generates new entry points for the exonuclease EXO1 to degrade the strand containing the mismatch. DNA methylation would prevent cleavage and therefore assure that only the newly mutated DNA strand is going to be corrected. MutL alpha (MLH1-PMS2) interacts physically with the clamp loader subunits of DNA polymerase III, suggesting that it may play a role to recruit the DNA polymerase III to the site of the MMR. Also implicated in DNA damage signaling, a process which induces cell cycle arrest and can lead to apoptosis in case of major DNA damages. Heterodimerizes with MLH3 to form MutL gamma which plays a role in meiosis.",Increased mismatch repair activity; gain of protein expression; gain of nuclear localization.,Increased mismatch repair activity; gain of protein expression; gain of nuclear localization.
3536,3536,0,0,P16278-P514L,MPGFLVRILPLLLVLLLLGPTRGLRNATQRMFEIDYSRDSFLKDGQPFRYISGSIHYSRVPRFYWKDRLLKMKMAGLNAIQTYVPWNFHEPWPGQYQFSEDHDVEYFLRLAHELGLLVILRPGPYICAEWEMGGLPAWLLEKESILLRSSDPDYLAAVDKWLGVLLPKMKPLLYQNGGPVITVQVENEYGSYFACDFDYLRFLQKRFRHHLGDDVVLFTTDGAHKTFLKCGALQGLYTTVDFGTGSNITDAFLSQRKCEPKGPLINSEFYTGWLDHWGQPHSTIKTEAVASSLYDILARGASVNLYMFIGGTNFAYWNGANSPYAAQPTSYDYDAPLSEAGDLTEKYFALRNIIQKFEKVPEGPIPPSTPKFAYGKVTLEKLKTVGAALDILCPSGPIKSLYPLTFIQVKQHYGFVLYRTTLPQDCSNPAPLSSPLNGVHDRAYVAVDGIPQGVLERNNVITLNITGKAGATLDLLVENMGRVNYGAYINDFKGLVSNLTLSSNILTDWTIFPLDTEDAVRSHLGGWGHRDSGHHDEAWAHNSSNYTLPAFYMGNFSIPSGIPDLPQDTFIQFPGWTKGQVWINGFNLGRYWPARGPQLTLFVPQHILMTSAPNTITVLELEWAPCSSDDPELCAVTFVDRPVIGSSVTYDHPSKPVEKRLMPPPPQKNKDSWLDHV,,-1.0,MPGFLVRILPLLLVLLLLGPTRGLRNATQRMFEIDYSRDSFLKDGQPFRYISGSIHYSRVPRFYWKDRLLKMKMAGLNAIQTYVPWNFHEPWPGQYQFSEDHDVEYFLRLAHELGLLVILRPGPYICAEWEMGGLPAWLLEKESILLRSSDPDYLAAVDKWLGVLLPKMKPLLYQNGGPVITVQVENEYGSYFACDFDYLRFLQKRFRHHLGDDVVLFTTDGAHKTFLKCGALQGLYTTVDFGTGSNITDAFLSQRKCEPKGPLINSEFYTGWLDHWGQPHSTIKTEAVASSLYDILARGASVNLYMFIGGTNFAYWNGANSPYAAQPTSYDYDAPLSEAGDLTEKYFALRNIIQKFEKVPEGPIPPSTPKFAYGKVTLEKLKTVGAALDILCPSGPIKSLYPLTFIQVKQHYGFVLYRTTLPQDCSNPAPLSSPLNGVHDRAYVAVDGIPQGVLERNNVITLNITGKAGATLDLLVENMGRVNYGAYINDFKGLVSNLTLSSNILTDWTIFPPDTEDAVRSHLGGWGHRDSGHHDEAWAHNSSNYTLPAFYMGNFSIPSGIPDLPQDTFIQFPGWTKGQVWINGFNLGRYWPARGPQLTLFVPQHILMTSAPNTITVLELEWAPCSSDDPELCAVTFVDRPVIGSSVTYDHPSKPVEKRLMPPPPQKNKDSWLDHV,Beta-galactosidase,"Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans.Has no beta-galactosidase catalytic activity, but plays functional roles in the formation of extracellular elastic fibers (elastogenesis) and in the development of connective tissue. Seems to be identical to the elastin-binding protein (EBP), a major component of the non-integrin cell surface receptor expressed on fibroblasts, smooth muscle cells, chondroblasts, leukocytes, and certain cancer cell types. In elastin producing cells, associates with tropoelastin intracellularly and functions as a recycling molecular chaperone which facilitates the secretions of tropoelastin and its assembly into elastic fibers.",Increase in galactosidase activity. The mutation in the GLB1 gene affects the function and structure of the β-d-galactosidase enzyme.,Increase in galactosidase activity. The mutation in the GLB1 gene affects the function and structure of the β-d-galactosidase enzyme.
3558,3558,0,0,P08514-P778Q,MARALCPLQALWLLEWVLLLLGPCAAPPAWALNLDPVQLTFYAGPNGSQFGFSLDFHKDSHGRVAIVVGAPRTLGPSQEETGGVFLCPWRAEGGQCPSLLFDLRDETRNVGSQTLQTFKARQGLGASVVSWSDVIVACAPWQHWNVLEKTEEAEKTPVGSCFLAQPESGRRAEYSPCRGNTLSRIYVENDFSWDKRYCEAGFSSVVTQAGELVLGAPGGYYFLGLLAQAPVADIFSSYRPGILLWHVSSQSLSFDSSNPEYFDGYWGYSVAVGEFDGDLNTTEYVVGAPTWSWTLGAVEILDSYYQRLHRLRGEQMASYFGHSVAVTDVNGDGRHDLLVGAPLYMESRADRKLAEVGRVYLFLQPRGPHALGAPSLLLTGTQLYGRFGSAIAPLGDLDRDGYNDIAVAAPYGGPSGRGQVLVFLGQSEGLRSRPSQVLDSPFPTGSAFGFSLRGAVDIDDNGYPDLIVGAYGANQVAVYRAQPVVKASVQLLVQDSLNPAVKSCVLPQTKTPVSCFNIQMCVGATGHNIPQKLSLNAELQLDRQKPRQGRRVLLLGSQQAGTTLNLDLGGKHSPICHTTMAFLRDEADFRDKLSPIVLSLNVSLPPTEAGMAPAVVLHGDTHVQEQTRIVLDCGEDDVCVPQLQLTASVTGSPLLVGADNVLELQMDAANEGEGAYEAELAVHLPQGAHYMRALSNVEGFERLICNQKKENETRVVLCELGNPMKKNAQIGIAMLVSVGNLEEAGESVSFQLQIRSKNSQNPNSKIVLLDVPVRAEAQVELRGNSFPASLVVAAEEGEREQNSLDSWGPKVEHTYELHNNGPGTVNGLHLSIHLPGQSQPSDLLYILDIQPQGGLQCFPQPPVNPLKVDWGLPIPSPSPIHPAHHKRDRRQIFLPEPEQPSRLQDPVLVSCDSAPCTVVQCDLQEMARGQRAMVTVLAFLWLPSLYQRPLDQFVLQSHAWFNVSSLPYAVPPLSLPRGEAQVWTQLLRALEERAIPIWWVLVGVLGGLLLLTILVLAMWKVGFF,,-1.0,MARALCPLQALWLLEWVLLLLGPCAAPPAWALNLDPVQLTFYAGPNGSQFGFSLDFHKDSHGRVAIVVGAPRTLGPSQEETGGVFLCPWRAEGGQCPSLLFDLRDETRNVGSQTLQTFKARQGLGASVVSWSDVIVACAPWQHWNVLEKTEEAEKTPVGSCFLAQPESGRRAEYSPCRGNTLSRIYVENDFSWDKRYCEAGFSSVVTQAGELVLGAPGGYYFLGLLAQAPVADIFSSYRPGILLWHVSSQSLSFDSSNPEYFDGYWGYSVAVGEFDGDLNTTEYVVGAPTWSWTLGAVEILDSYYQRLHRLRGEQMASYFGHSVAVTDVNGDGRHDLLVGAPLYMESRADRKLAEVGRVYLFLQPRGPHALGAPSLLLTGTQLYGRFGSAIAPLGDLDRDGYNDIAVAAPYGGPSGRGQVLVFLGQSEGLRSRPSQVLDSPFPTGSAFGFSLRGAVDIDDNGYPDLIVGAYGANQVAVYRAQPVVKASVQLLVQDSLNPAVKSCVLPQTKTPVSCFNIQMCVGATGHNIPQKLSLNAELQLDRQKPRQGRRVLLLGSQQAGTTLNLDLGGKHSPICHTTMAFLRDEADFRDKLSPIVLSLNVSLPPTEAGMAPAVVLHGDTHVQEQTRIVLDCGEDDVCVPQLQLTASVTGSPLLVGADNVLELQMDAANEGEGAYEAELAVHLPQGAHYMRALSNVEGFERLICNQKKENETRVVLCELGNPMKKNAQIGIAMLVSVGNLEEAGESVSFQLQIRSKNSQNPNSKIVLLDVPVRAEAPVELRGNSFPASLVVAAEEGEREQNSLDSWGPKVEHTYELHNNGPGTVNGLHLSIHLPGQSQPSDLLYILDIQPQGGLQCFPQPPVNPLKVDWGLPIPSPSPIHPAHHKRDRRQIFLPEPEQPSRLQDPVLVSCDSAPCTVVQCDLQEMARGQRAMVTVLAFLWLPSLYQRPLDQFVLQSHAWFNVSSLPYAVPPLSLPRGEAQVWTQLLRALEERAIPIWWVLVGVLGGLLLLTILVLAMWKVGFF,Integrin alpha-IIb,"Integrin alpha-IIb/beta-3 is a receptor for fibronectin, fibrinogen, plasminogen, prothrombin, thrombospondin and vitronectin. It recognizes the sequence R-G-D in a wide array of ligands. It recognizes the sequence H-H-L-G-G-G-A-K-Q-A-G-D-V in fibrinogen gamma chain. Following activation integrin alpha-IIb/beta-3 brings about platelet/platelet interaction through binding of soluble fibrinogen. This step leads to rapid platelet aggregation which physically plugs ruptured endothelial cell surface.","The substitution highly improved both intracellular transport of the alphaIIb beta3 heterodimers to the Golgi apparatus and endoproteolytic cleavage of proalphaIIb into heavy and light chains. The absence of P, rather than the presence of Q, at amino acid residue 778 on alphaIIb is responsible for moderate alphaIIbbeta3 deficiency.","The substitution highly improved both intracellular transport of the alphaIIb beta3 heterodimers to the Golgi apparatus and endoproteolytic cleavage of proalphaIIb into heavy and light chains. The absence of P, rather than the presence of Q, at amino acid residue 778 on alphaIIb is responsible for moderate alphaIIbbeta3 deficiency."
3567,3567,0,0,P30291-A642S,MSFLSRQQPPPPRRAGAACTLRQKLIFSPCSDCEEEEEEEEEEGSGHSTGEDSAFQEPDSPLPPARSPTEPGPERRRSPGPAPGSPGELEEDLLLPGACPGADEAGGGAEGDSWEEEGFGSSSPVKSPAAPYFLGSSFSPVRCGGPGDASPRGCGARRAGEGRRSPRPDHPGTPPHKTFRKLRLFDTPHTPKSLLSKARGIDSSSVKLRGSSLFMDTEKSGKREFDVRQTPQVNINPFTPDSLLLHSSGQCRRRKRTYWNDSCGEDMEASDYELEDETRPAKRITITESNMKSRYTTEFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLGQHSHVVRYFSAWAEDDHMLIQNEYCNGGSLADAISENYRIMSYFKEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIPNAASEEGDEDDWASNKVMFKIGDLGHVTRISSPQVEEGDSRFLANEVLQENYTHLPKADIFALALTVVCAAGAEPLPRNGDQWHEIRQGRLPRIPQVLSQEFTELLKVMIHPDPERRPSAMALVKHSVLLSASRKSAEQLRIELNAEKFKNSLLQKELKKAQMAKAAAEERALFTDRMATRSTTQSNRTSRLIGKKMNRSVSLTIY,,-1.0,MSFLSRQQPPPPRRAGAACTLRQKLIFSPCSDCEEEEEEEEEEGSGHSTGEDSAFQEPDSPLPPARSPTEPGPERRRSPGPAPGSPGELEEDLLLPGACPGADEAGGGAEGDSWEEEGFGSSSPVKSPAAPYFLGSSFSPVRCGGPGDASPRGCGARRAGEGRRSPRPDHPGTPPHKTFRKLRLFDTPHTPKSLLSKARGIDSSSVKLRGSSLFMDTEKSGKREFDVRQTPQVNINPFTPDSLLLHSSGQCRRRKRTYWNDSCGEDMEASDYELEDETRPAKRITITESNMKSRYTTEFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLGQHSHVVRYFSAWAEDDHMLIQNEYCNGGSLADAISENYRIMSYFKEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIPNAASEEGDEDDWASNKVMFKIGDLGHVTRISSPQVEEGDSRFLANEVLQENYTHLPKADIFALALTVVCAAGAEPLPRNGDQWHEIRQGRLPRIPQVLSQEFTELLKVMIHPDPERRPSAMALVKHSVLLSASRKSAEQLRIELNAEKFKNSLLQKELKKAQMAKAAAEERALFTDRMATRSTTQSNRTSRLIGKKMNRSVALTIY,Wee1-like protein kinase,"Acts as a negative regulator of entry into mitosis (G2 to M transition) by protecting the nucleus from cytoplasmically activated cyclin B1-complexed CDK1 before the onset of mitosis by mediating phosphorylation of CDK1 on 'Tyr-15'. Specifically phosphorylates and inactivates cyclin B1-complexed CDK1 reaching a maximum during G2 phase and a minimum as cells enter M phase. Phosphorylation of cyclin B1-CDK1 occurs exclusively on 'Tyr-15' and phosphorylation of monomeric CDK1 does not occur. Its activity increases during S and G2 phases and decreases at M phase when it is hyperphosphorylated. A correlated decrease in protein level occurs at M/G1 phase, probably due to its degradation.","Abolishes dephosphorylation by BRSK1 and BRSK2. The mutation in Wee1 promotes the downregulation of Wee1 in polarized neurons, leading to enhanced neuronal polarity.","Abolishes dephosphorylation by BRSK1 and BRSK2. The mutation in Wee1 promotes the downregulation of Wee1 in polarized neurons, leading to enhanced neuronal polarity."
3573,3573,0,0,Q9BZI7-E451R,MKEEKEHRPKEKRVTLLTPAGATGSGGGTSGDSSKGEDKQDRNKEKKEALSKVVIRRLPPTLTKEQLQEHLQPMPEHDYFEFFSNDTSLYPHMYARAYINFKNQEDIILFRDRFDGYVFLDNKGQEYPAIVEFAPFQKAAKKKTKKRDTKVGTIDDDPEYRKFLESYATDNEKMTSTPETLLEEIEAKNRELIAKKTTPLLSFLKNKQRMREEKREERRRREIERKRQREEERRKWKEEEKRKRKDIEKLKKIDRIPERDKLKDEPKIKVHRFLLQAVNQKNLLKKPEKGDEKELDKREKAKKLDKENLSDERASGQSCTLPKRSDSELKDEKPKRPEDESGRDYREREREYERDQERILRERERLKRQEEERRRQKERYEKEKTFKRKEEEMKKEKDTLRDKGKKAESTESIGSSEKTEKKEEVVKRDRIRNKDRPAMQLYQPGARSRNRLCPPDDSTKSGDSAAERKQESGISHRKEGGEE,,-1.0,MKEEKEHRPKEKRVTLLTPAGATGSGGGTSGDSSKGEDKQDRNKEKKEALSKVVIRRLPPTLTKEQLQEHLQPMPEHDYFEFFSNDTSLYPHMYARAYINFKNQEDIILFRDRFDGYVFLDNKGQEYPAIVEFAPFQKAAKKKTKKRDTKVGTIDDDPEYRKFLESYATDNEKMTSTPETLLEEIEAKNRELIAKKTTPLLSFLKNKQRMREEKREERRRREIERKRQREEERRKWKEEEKRKRKDIEKLKKIDRIPERDKLKDEPKIKVHRFLLQAVNQKNLLKKPEKGDEKELDKREKAKKLDKENLSDERASGQSCTLPKRSDSELKDEKPKRPEDESGRDYREREREYERDQERILRERERLKRQEEERRRQKERYEKEKTFKRKEEEMKKEKDTLRDKGKKAESTESIGSSEKTEKKEEVVKRDRIRNKDRPAMQLYQPGARSRNELCPPDDSTKSGDSAAERKQESGISHRKEGGEE,Regulator of nonsense transcripts 3B,"Involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons by associating with the nuclear exon junction complex (EJC) and serving as link between the EJC core and NMD machinery. Recruits UPF2 at the cytoplasmic side of the nuclear envelope and the subsequent formation of an UPF1-UPF2-UPF3 surveillance complex (including UPF1 bound to release factors at the stalled ribosome) is believed to activate NMD. In cooperation with UPF2 stimulates both ATPase and RNA helicase activities of UPF1. Binds spliced mRNA upstream of exon-exon junctions. In vitro, stimulates translation; the function is independent of association with UPF2 and components of the EJC core.",Enables NMD; when associated with E-447 and E-449. Residues that affect NMD when mutated are found at the core interacting surfaces.,Enables NMD; when associated with E-447 and E-449. Residues that affect NMD when mutated are found at the core interacting surfaces.
3578,3578,0,0,Q05567-L67K,MSGVSNKTVSINGWYGMPIHLLREEGDFAQFMILTINELKIAIHGYLRNTPWYNMLKDYLFVIFCYKLISNFFYLLKVYGPVRLAVRTYEHSSRRLFRWLLDSPFLRGTVEKEVTKVKQSIEDELIRSDSQLMNFPQLPSNGIPQDDVIEELNKLNDLIPHTQWKEGKVSGAVYHGGDDLIHLQTIAYEKYCVANQLHPDVFPAVRKMESEVVSMVLRMFNAPSDTGCGTTTSGGTESLLLACLSAKMYALHHRGITEPEIIAPVTAHAGFDKAAYYFGMKLRHVELDPTTYQVDLGKVKKFINKNTILLVGSAPNFPHGIADDIEGLGKIAQKYKLPLHVDSCLGSFIVSFMEKAGYKNLPLLDFRVPGVTSISCDTHKYGFAPKGSSVIMYRNSDLRMHQYYVNPAWTGGLYGSPTLAGSRPGAIVVGCWATMVNMGENGYIESCQEIVGAAMKFKKYIQENIPDLNIMGNPRYSVISFSSKTLNIHELSDRLSKKGWHFNALQKPVALHMAFTRLSAHVVDEICDILRTTVQELKSESNSKPSPDGTSALYGVAGSVKTAGVADKLIVGFLDALYKLGPGEDTATK,,-1.0,MSGVSNKTVSINGWYGMPIHLLREEGDFAQFMILTINELKIAIHGYLRNTPWYNMLKDYLFVIFCYLLISNFFYLLKVYGPVRLAVRTYEHSSRRLFRWLLDSPFLRGTVEKEVTKVKQSIEDELIRSDSQLMNFPQLPSNGIPQDDVIEELNKLNDLIPHTQWKEGKVSGAVYHGGDDLIHLQTIAYEKYCVANQLHPDVFPAVRKMESEVVSMVLRMFNAPSDTGCGTTTSGGTESLLLACLSAKMYALHHRGITEPEIIAPVTAHAGFDKAAYYFGMKLRHVELDPTTYQVDLGKVKKFINKNTILLVGSAPNFPHGIADDIEGLGKIAQKYKLPLHVDSCLGSFIVSFMEKAGYKNLPLLDFRVPGVTSISCDTHKYGFAPKGSSVIMYRNSDLRMHQYYVNPAWTGGLYGSPTLAGSRPGAIVVGCWATMVNMGENGYIESCQEIVGAAMKFKKYIQENIPDLNIMGNPRYSVISFSSKTLNIHELSDRLSKKGWHFNALQKPVALHMAFTRLSAHVVDEICDILRTTVQELKSESNSKPSPDGTSALYGVAGSVKTAGVADKLIVGFLDALYKLGPGEDTATK,Sphingosine-1-phosphate lyase,"Sphingosine-1-phosphate lyase that cleaves phosphorylated sphingoid bases (PSBs), such as sphingosine-1-phosphate, into fatty aldehydes and phosphoethanolamine. Prefers C-16 dihydrosphingosine-l-phosphate (DHS-P) as a substrate. Regulates intracellular levels of sphingolipid long-chain base phosphates (LCBPs). Plays a role in the regulation of global responses to nutrient deprivation in yeast.",Increases catalytic activity. The mutation in Dpl1p is required for its full function in vivo but not for its localization or for its catalytic activity in vitro.,Increases catalytic activity. The mutation in Dpl1p is required for its full function in vivo but not for its localization or for its catalytic activity in vitro.
3581,3581,0,0,Q5SJC4-A74F,MVVAGIDPGITHLGLGVVAVEGKGALKARLLHGEVVKTSPQEPAKERVGRIHARVLEVLHRFRPEAVAVEEQFFYRQNELAYKVGWALGAVLVAAFEAGVPVYAYGPMQVKQALAGHGHAAKEEVALMVRGILGLKEAPRPSHLADALAIALTHAFYARMGTAKPL,,-1.0,MVVAGIDPGITHLGLGVVAVEGKGALKARLLHGEVVKTSPQEPAKERVGRIHARVLEVLHRFRPEAVAVEEQFAYRQNELAYKVGWALGAVLVAAFEAGVPVYAYGPMQVKQALAGHGHAAKEEVALMVRGILGLKEAPRPSHLADALAIALTHAFYARMGTAKPL,Crossover junction endodeoxyribonuclease RuvC,"The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair (Probable). Endonuclease that resolves Holliday junction (HJ) intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous arms, yielding a 5'-phosphate and a 3'-hydroxyl group; requires a central core of homology in the junction. The cleavage reactions can be uncoupled; the presence of a 5'-phosphate in a half-cut site is required for second strand cleavage. The consensus cleavage sequence is 5'-(A/T)TT(C/G)-3'. Cleavage occurs on the 3'-side of the TT dinucleotide at the point of strand exchange.","Slightly enhanced HJ resolution activity, unaltered sequence specificity. The structure of T. th. RuvC homodimer refined at 1. 28 Å resolution shows distinct symmetry near the dimer interface, in the region harboring catalytically important aromatic residues.","Slightly enhanced HJ resolution activity, unaltered sequence specificity. The structure of T. th. RuvC homodimer refined at 1. 28 Å resolution shows distinct symmetry near the dimer interface, in the region harboring catalytically important aromatic residues."
3584,3584,0,0,P42262-E607Q,MQKIMHISVLLSPVLWGLIFGVSSNSIQIGGLFPRGADQEYSAFRVGMVQFSTSEFRLTPHIDNLEVANSFAVTNAFCSQFSRGVYAIFGFYDKKSVNTITSFCGTLHVSFITPSFPTDGTHPFVIQMRPDLKGALLSLIEYYQWDKFAYLYDSDRGLSTLQAVLDSAAEKKWQVTAINVGNINNDKKDEMYRSLFQDLELKKERRVILDCERDKVNDIVDQVITIGKHVKGYHYIIANLGFTDGDLLKIQFGGANVSGFQIVDYDDSLVSKFIERWSTLEEKEYPGAHTTTIKYTSALTYDAVQVMTEAFRNLRKQRIEISRRGNAGDCLANPAVPWGQGVEIERALKQVQVEGLSGNIKFDQNGKRINYTINIMELKTNGPRKIGYWSEVDKMVVTLTELPSGNDTSGLENKTVVVTTILESPYVMMKKNHEMLEGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGKYGARDADTKIWNGMVGELVYGKADIAIAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHTEEFEDGRETQSSESTNEFGIFNSLWFSLGAFMQQGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLSKQTEIAYGTLDSGSTKEFFRRSKIAVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSKGKYAYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSSLRNAVNLAVLKLNEQGLLDKLKNKWWYDKGECGSGGGDSKEKTSALSLSNVAGVFYILVGGLGLAMLVALIEFCYKSRAEAKRMKVAKNAQNINPSSSQNSQNFATYKEGYNVYGIESVKI,,-1.0,MQKIMHISVLLSPVLWGLIFGVSSNSIQIGGLFPRGADQEYSAFRVGMVQFSTSEFRLTPHIDNLEVANSFAVTNAFCSQFSRGVYAIFGFYDKKSVNTITSFCGTLHVSFITPSFPTDGTHPFVIQMRPDLKGALLSLIEYYQWDKFAYLYDSDRGLSTLQAVLDSAAEKKWQVTAINVGNINNDKKDEMYRSLFQDLELKKERRVILDCERDKVNDIVDQVITIGKHVKGYHYIIANLGFTDGDLLKIQFGGANVSGFQIVDYDDSLVSKFIERWSTLEEKEYPGAHTTTIKYTSALTYDAVQVMTEAFRNLRKQRIEISRRGNAGDCLANPAVPWGQGVEIERALKQVQVEGLSGNIKFDQNGKRINYTINIMELKTNGPRKIGYWSEVDKMVVTLTELPSGNDTSGLENKTVVVTTILESPYVMMKKNHEMLEGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGKYGARDADTKIWNGMVGELVYGKADIAIAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHTEEFEDGRETQSSESTNEFGIFNSLWFSLGAFMEQGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLSKQTEIAYGTLDSGSTKEFFRRSKIAVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSKGKYAYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSSLRNAVNLAVLKLNEQGLLDKLKNKWWYDKGECGSGGGDSKEKTSALSLSNVAGVFYILVGGLGLAMLVALIEFCYKSRAEAKRMKVAKNAQNINPSSSQNSQNFATYKEGYNVYGIESVKI,Glutamate receptor 2,"Receptor for glutamate that functions as ligand-gated ion channel in the central nervous system. It plays an important role in excitatory synaptic transmission. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. In the presence of CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of glutamate. Through complex formation with NSG1, GRIP1 and STX12 controls the intracellular fate of AMPAR and the endosomal sorting of the GRIA2 subunit toward recycling and membrane targeting.","Homomeric channels show decreased ionotropic glutamate receptor activity; increased localization to cell membrane. Following post-transcriptional editing at the Q607 site, it renders heteromultimeric AMPARs Ca2+-permeable, with a nonlinear relationship between current and trans-membrane voltage.","Homomeric channels show decreased ionotropic glutamate receptor activity; increased localization to cell membrane. Following post-transcriptional editing at the Q607 site, it renders heteromultimeric AMPARs Ca2+-permeable, with a nonlinear relationship between current and trans-membrane voltage."
3604,3604,0,0,P0CX53-K67R,MPPKFDPNEVKYLYLRAVGGEVGASAALAPKIGPLGLSPKKVGEDIAKATKEFKGIKVTVQLKIQNRQAAASVVPSASSLVITALKEPPRDRKKDKNVKHSGNIQLDEIIEIARQMRDKSFGRTLASVTKEILGTAQSVGCRVDFKNPHDIIEGINAGEIEIPEN,,-1.0,MPPKFDPNEVKYLYLRAVGGEVGASAALAPKIGPLGLSPKKVGEDIAKATKEFKGIKVTVQLKIQNKQAAASVVPSASSLVITALKEPPRDRKKDKNVKHSGNIQLDEIIEIARQMRDKSFGRTLASVTKEILGTAQSVGCRVDFKNPHDIIEGINAGEIEIPEN,Large ribosomal subunit protein uL11A,"Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.",Enables monomethylation by RMT2.,Enables monomethylation by RMT2.
3606,3606,0,0,Q9QYS9-A330R,MVGEMETKEKPKPTPDYLMQLMNDKKLMSSLPNFCGIFNHLERLLDEEISRVRKDMYNDTLNGSTEKRSAELPDAVGPIVQLQEKLYVPVKEYPDFNFVGRILGPRGLTAKQLEAETGCKIMVRGKGSMRDKKKEEQNRGKPNWEHLNEDLHVLITVEDAQNRAEIKLKRAVEEVKKLLVPAAEGEDSLKKMQLMELAILNGTYRDANIKSPALAFSLAATAQAAPRIITGPAPVLPPAALRTPTPAGPTIMPLIRQIQTAVMPNGTPHPTAAIVPPGPEAGLIYTPYEYPYTLAPATSILEYPIEPSGVLGAVATKVRRHDMRVHPYQRIVTADRAATGN,,-1.0,MVGEMETKEKPKPTPDYLMQLMNDKKLMSSLPNFCGIFNHLERLLDEEISRVRKDMYNDTLNGSTEKRSAELPDAVGPIVQLQEKLYVPVKEYPDFNFVGRILGPRGLTAKQLEAETGCKIMVRGKGSMRDKKKEEQNRGKPNWEHLNEDLHVLITVEDAQNRAEIKLKRAVEEVKKLLVPAAEGEDSLKKMQLMELAILNGTYRDANIKSPALAFSLAATAQAAPRIITGPAPVLPPAALRTPTPAGPTIMPLIRQIQTAVMPNGTPHPTAAIVPPGPEAGLIYTPYEYPYTLAPATSILEYPIEPSGVLGAVATKVRRHDMRVHPYQAIVTADRAATGN,KH domain-containing RNA-binding protein QKI,"RNA reader protein, which recognizes and binds specific RNAs, thereby regulating RNA metabolic processes, such as pre-mRNA splicing, circular RNA (circRNA) formation, mRNA export, mRNA stability and/or translation. Involved in various cellular processes, such as mRNA storage into stress granules, apoptosis, lipid deposition, interferon response, glial cell fate and development. Binds to the 5'-NACUAAY-N(1,20)-UAAY-3' RNA core sequence. Acts as a mRNA modification reader that specifically recognizes and binds mRNA transcripts modified by internal N(7)-methylguanine (m7G) (By similarity). Promotes the formation of circular RNAs (circRNAs) during the epithelial to mesenchymal transition and in cardiomyocytes: acts by binding to sites flanking circRNA-forming exons. CircRNAs are produced by back-splicing circularization of pre-mRNAs. Plays a central role in myelinization via 3 distinct mechanisms. First, acts by protecting and promoting stability of target mRNAs such as MBP, SIRT2 and CDKN1B, which promotes oligodendrocyte differentiation. Second, participates in mRNA transport by regulating the nuclear export of MBP mRNA. Finally, indirectly regulates mRNA splicing of MAG pre-mRNA during oligodendrocyte differentiation by acting as a negative regulator of MAG exon 12 alternative splicing: acts by binding to HNRNPA1 mRNA splicing factor, preventing its translation. Involved in microglia differentiation and remyelination by regulating microexon alternative splicing of the Rho GTPase pathway. Involved in macrophage differentiation: promotes monocyte differentiation by regulating pre-mRNA splicing in naive peripheral blood monocytes. Acts as an important regulator of muscle development: required for the contractile function of cardiomyocytes by regulating alternative splicing of cardiomyocyte transcripts. Acts as a negative regulator of thermogenesis by decreasing stability, nuclear export and translation of mRNAs encoding PPARGC1A and UCP1. Also required for visceral endoderm function and blood vessel development. May also play a role in smooth muscle development. In addition to its RNA-binding activity, also acts as a nuclear transcription coactivator for SREBF2/SREBP2.",Enables nuclear localization; when associated with A-324. The mutation in the QUA1 domain of QKI leads to a gain of QKI self-interaction.,Enables nuclear localization; when associated with A-324. The mutation in the QUA1 domain of QKI leads to a gain of QKI self-interaction.
3610,3610,0,0,Q62651-N204D,MATAMTVSSKLLGLLMQQLRGTRQLYFNVSLRSLSSSAQEASKRIPEEVSDHNYESIQVTSAQKHVLHVQLNRPEKRNAMNRAFWRELVECFQKISKDSDCRAVVVSGAGKMFTSGIDLMDMASDILQPPGDDVARIAWYLRDLISRYQKTFTVIEKCPKPVIAAIHGGCIGGGVDLISACDIRYCTQDAFFQVKEVDVGLAADVGTLQRLPKVIGNRSLVNELTFTARKMMADEALDSGLVSRVFPDKDVMLNAAFALAADISSKSPVAVQGSKINLIYSRDHSVDESLDYMATWNMSMLQTQDIIKSVQAAMEKKDSKSITFSKL,,-1.0,MATAMTVSSKLLGLLMQQLRGTRQLYFNVSLRSLSSSAQEASKRIPEEVSDHNYESIQVTSAQKHVLHVQLNRPEKRNAMNRAFWRELVECFQKISKDSDCRAVVVSGAGKMFTSGIDLMDMASDILQPPGDDVARIAWYLRDLISRYQKTFTVIEKCPKPVIAAIHGGCIGGGVDLISACDIRYCTQDAFFQVKEVDVGLAANVGTLQRLPKVIGNRSLVNELTFTARKMMADEALDSGLVSRVFPDKDVMLNAAFALAADISSKSPVAVQGSKINLIYSRDHSVDESLDYMATWNMSMLQTQDIIKSVQAAMEKKDSKSITFSKL,Delta,"Isomerization of 3-trans,5-cis-dienoyl-CoA to 2-trans,4-trans-dienoyl-CoA.","Strongly increases dienoyl-CoA and trienoyl-CoA isomerase activity. Substitutions of D(204) by N resulted in 10(5)-fold higher activities. Such activity gains are consistent with the direct involvement of these latter two residues in the proposed proton transfers at carbons 2 and 6 or 8 of the substrates. Pbing of the wild-type and mutants forms of the enzyme with 2, 5-octadienoyl-CoA as substrate revealed high Delta(2), Delta(3)-enoyl-CoA isomerase and Delta(5), Delta(4)-enoyl-CoA isomerase activities catalyzed by E(196) and D(204), respectively. Altogether, these data reveal that positional isomerizations of the diene and triene are hindered by simultaneous proton transfers involving E(196) and D(204), whereas each residue alone can catalyze, albeit more efficiently, a monoene isomerization.","Strongly increases dienoyl-CoA and trienoyl-CoA isomerase activity. Substitutions of D(204) by N resulted in 10(5)-fold higher activities. Such activity gains are consistent with the direct involvement of these latter two residues in the proposed proton transfers at carbons 2 and 6 or 8 of the substrates. Pbing of the wild-type and mutants forms of the enzyme with 2, 5-octadienoyl-CoA as substrate revealed high Delta(2), Delta(3)-enoyl-CoA isomerase and Delta(5), Delta(4)-enoyl-CoA isomerase activities catalyzed by E(196) and D(204), respectively. Altogether, these data reveal that positional isomerizations of the diene and triene are hindered by simultaneous proton transfers involving E(196) and D(204), whereas each residue alone can catalyze, albeit more efficiently, a monoene isomerization."
3615,3615,0,0,Q9FZN8-M317V,MELATAGKVNEVLFMNRGEGESSYAQNSSFTQQVASMAQPALENAVETLFSRDFHLQALNAADLGCAAGPNTFAVISTIKRMMEKKCRELNCQTLELQVYLNDLFGNDFNTLFKGLSSEVIGNKCEEVPCYVMGVPGSFHGRLFPRNSLHLVHSSYSVHWLTQAPKGLTSREGLALNKGKIYISKTSPPVVREAYLSQFHEDFTMFLNARSQEVVPNGCMVLILRGRQCSDPSDMQSCFTWELLAMAIAELVSQGLIDEDKLDTFNIPSYFASLEEVKDIVERDGSFTIDHIEGFDLDSVEMQENDKWVRGEKFTKVVRAFTEPIISNQFGPEIMDKLYDKFTHIVVSDLEAKLPKTTSIILVLSKIDG,,-1.0,MELATAGKVNEVLFMNRGEGESSYAQNSSFTQQVASMAQPALENAVETLFSRDFHLQALNAADLGCAAGPNTFAVISTIKRMMEKKCRELNCQTLELQVYLNDLFGNDFNTLFKGLSSEVIGNKCEEVPCYVMGVPGSFHGRLFPRNSLHLVHSSYSVHWLTQAPKGLTSREGLALNKGKIYISKTSPPVVREAYLSQFHEDFTMFLNARSQEVVPNGCMVLILRGRQCSDPSDMQSCFTWELLAMAIAELVSQGLIDEDKLDTFNIPSYFASLEEVKDIVERDGSFTIDHIEGFDLDSVEMQENDKWVRGEKFTKMVRAFTEPIISNQFGPEIMDKLYDKFTHIVVSDLEAKLPKTTSIILVLSKIDG,"3,7-dimethylxanthine N-methyltransferase TCS1",Involved in the biosynthesis of caffeine. Catalyzes the conversion of 7-methylxanthine (7mX) to theobromine and of theobromine to caffeine. Has 3-N- and 1-N-methylation activity.,Slightly decreased theobromine synthase and caffeine synthase activities. The mutation in TCS slightly decreased theobromine accumulation and simultaneously increased caffeine production.,Slightly decreased theobromine synthase and caffeine synthase activities. The mutation in TCS slightly decreased theobromine accumulation and simultaneously increased caffeine production.
3617,3617,0,0,P34903-C474Y,MIITQTSHCYMTSLGILFLINILPGTTGQGESRRQEPGDFVKQDIGGLSPKHAPDIPDDSTDNITIFTRILDRLLDGYDNRLRPGLGDAVTEVKTDIYVTSFGPVSDTDMEYTIDVFFRQTWHDERLKFDGPMKILPLNNLLASKIWTPDTFFHNGKKSVAHNMTTPNKLLRLVDNGTLLYTMRLTIHAECPMHLEDFPMDVHACPLKFGSYAYTTAEVVYSWTLGKNKSVEVAQDGSRLNQYDLLGHVVGTEIIRSSTGEYVVMTTHFHLKRKIGYFVIQTYLPCIMTVILSQVSFWLNRESVPARTVFGVTTVLTMTTLSISARNSLPKVAYATAMDWFIAVCYAFVFSALIEFATVNYFTKRSWAWEGKKVPEALEMKKKTPAAPAKKTSTTFNIVGTTYPINLAKDTEFSTISKGAAPSASSTPTIIASPKATYVQDSPTETKTYNSVSKVDKISRIIFPVLFAIFNLVYWATYVNRESAIKGMIRKQ,,-1.0,MIITQTSHCYMTSLGILFLINILPGTTGQGESRRQEPGDFVKQDIGGLSPKHAPDIPDDSTDNITIFTRILDRLLDGYDNRLRPGLGDAVTEVKTDIYVTSFGPVSDTDMEYTIDVFFRQTWHDERLKFDGPMKILPLNNLLASKIWTPDTFFHNGKKSVAHNMTTPNKLLRLVDNGTLLYTMRLTIHAECPMHLEDFPMDVHACPLKFGSYAYTTAEVVYSWTLGKNKSVEVAQDGSRLNQYDLLGHVVGTEIIRSSTGEYVVMTTHFHLKRKIGYFVIQTYLPCIMTVILSQVSFWLNRESVPARTVFGVTTVLTMTTLSISARNSLPKVAYATAMDWFIAVCYAFVFSALIEFATVNYFTKRSWAWEGKKVPEALEMKKKTPAAPAKKTSTTFNIVGTTYPINLAKDTEFSTISKGAAPSASSTPTIIASPKATYVQDSPTETKTYNSVSKVDKISRIIFPVLFAIFNLVCWATYVNRESAIKGMIRKQ,Gamma-aminobutyric acid receptor subunit alpha-3,"GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel.",Significant increase of GABA-evoked anion currents for this mutant compared to wild-type receptors.,Significant increase of GABA-evoked anion currents for this mutant compared to wild-type receptors.
3625,3625,0,0,Q9NS37-A304H,MRHSLTKLLAASGSNSPTRSESPEPAATCSLPSDLTRAAAGEEETAAAGSPGRKQQFGDEGELEAGRGSRGGVAVRAPSPEEMEEEAIASLPGEETEDMDFLSGLELADLLDPRQPDWHLDPGLSSPGPLSSSGGGSDSGGLWRGDDDDEAAAAEMQRFSDLLQRLLNGIGGCSSSSDSGSAEKRRRKSPGGGGGGGSGNDNNQAATKSPRKAAAAAARLNRLKKKEYVMGLESRVRGLAAENQELRAENRELGKRVQALQEESRYLRAVLANETGLARLLSRLSGVGLRLTTSLFRDSPAGDHDYALPVGKQKQDLLEEDDSAGGVCLHVDKDKVSVEFCSACARKASSSLKM,,-1.0,MRHSLTKLLAASGSNSPTRSESPEPAATCSLPSDLTRAAAGEEETAAAGSPGRKQQFGDEGELEAGRGSRGGVAVRAPSPEEMEEEAIASLPGEETEDMDFLSGLELADLLDPRQPDWHLDPGLSSPGPLSSSGGGSDSGGLWRGDDDDEAAAAEMQRFSDLLQRLLNGIGGCSSSSDSGSAEKRRRKSPGGGGGGGSGNDNNQAATKSPRKAAAAAARLNRLKKKEYVMGLESRVRGLAAENQELRAENRELGKRVQALQEESRYLRAVLANETGLARLLSRLSGVGLRLTTSLFRDSPAGDADYALPVGKQKQDLLEEDDSAGGVCLHVDKDKVSVEFCSACARKASSSLKM,CREB/ATF bZIP transcription factor,Strongly activates transcription when bound to HCFC1. Suppresses the expression of HSV proteins in cells infected with the virus in a HCFC1-dependent manner. Also suppresses the HCFC1-dependent transcriptional activation by CREB3 and reduces the amount of CREB3 in the cell. Able to down-regulate expression of some cellular genes in CREBZF-expressing cells.,Significantly increased binding to HCFC1.,Significantly increased binding to HCFC1.
3635,3635,0,0,Q922S8-A293K,MESLHARLFPGLSINIQRSNGLIHPANISTVNVEKSCVSVEWIEGGTTKGKEIDIDDVAAINPELLQLLPLRPKDSLPLQENVTVPKQKRKSVNSKIPALKEGLRSRSTRMSTVSEVRIPAQENEMEVELPVPTNSRKQFAIPSHPRASCSTVTELPLLMVSEEAEEQAHSTRSTSSANPGNSVRRKSCIVKEMEKMKNKREEKRAQNSELRIKRAQEYDSSFPNWEFARMIKEFRVTMECSPLTVTDPIEEHRICVCVRKRPLNKQELAKKEIDVISVPSKCLLLVHEPKLKVDLTKYLENQAFCFDFAFDETASNEVVYRFTARPLVQTIFEGGKATCFAYGQTGSGKTHTMGGDLSGKSQNASKGIYAMASRDVFLLKNQPRYRNLNLEVYVTFFEIYNGKVFDLLNKKAKLRVLEDSRQQVQVVGLQEYLVTCADDVIKMINMGSACRTSGQTFANSNSSRSHACFQILLRTKGRLHGKFSLVDLAGNERGADTSSADRQTRMEGAEINKSLLALKECIRALGQNKAHTPFRESKLTQVLRDSFIGENSRTCMIAMISPGISSCEYTLNTLRYADRVKELSPHSGPSGEQPVQMETEVMEASSNGTSLTGNEEEELSSQMSSFNEAMTQIRELEERALEELREIIQQGPNWLELSEMTDQPDYDLETFVNKAESALTQQAKQAKHFSALREVIKALRLAMQLEEQASKQINSKKRHQ,,-1.0,MESLHARLFPGLSINIQRSNGLIHPANISTVNVEKSCVSVEWIEGGTTKGKEIDIDDVAAINPELLQLLPLRPKDSLPLQENVTVPKQKRKSVNSKIPALKEGLRSRSTRMSTVSEVRIPAQENEMEVELPVPTNSRKQFAIPSHPRASCSTVTELPLLMVSEEAEEQAHSTRSTSSANPGNSVRRKSCIVKEMEKMKNKREEKRAQNSELRIKRAQEYDSSFPNWEFARMIKEFRVTMECSPLTVTDPIEEHRICVCVRKRPLNKQELAKKEIDVISVPSKCLLLVHEPKLAVDLTKYLENQAFCFDFAFDETASNEVVYRFTARPLVQTIFEGGKATCFAYGQTGSGKTHTMGGDLSGKSQNASKGIYAMASRDVFLLKNQPRYRNLNLEVYVTFFEIYNGKVFDLLNKKAKLRVLEDSRQQVQVVGLQEYLVTCADDVIKMINMGSACRTSGQTFANSNSSRSHACFQILLRTKGRLHGKFSLVDLAGNERGADTSSADRQTRMEGAEINKSLLALKECIRALGQNKAHTPFRESKLTQVLRDSFIGENSRTCMIAMISPGISSCEYTLNTLRYADRVKELSPHSGPSGEQPVQMETEVMEASSNGTSLTGNEEEELSSQMSSFNEAMTQIRELEERALEELREIIQQGPNWLELSEMTDQPDYDLETFVNKAESALTQQAKQAKHFSALREVIKALRLAMQLEEQASKQINSKKRHQ,Kinesin-like protein KIF2C,"In complex with KIF18B, constitutes the major microtubule plus-end depolymerizing activity in mitotic cells. Regulates the turnover of microtubules at the kinetochore and functions in chromosome segregation during mitosis. Plays a role in chromosome congression and is required for the lateral to end-on conversion of the chromosome-microtubule attachment.",Highly increases microtubule depolymerization activity. The mutation in KIF2C destabilizes the peeling of the protofilament.,Highly increases microtubule depolymerization activity. The mutation in KIF2C destabilizes the peeling of the protofilament.
3637,3637,0,0,O60583-C260N,MASGRGASSRWFFTREQLENTPSRRCGVEADKELSCRQQAANLIQEMGQRLNVSQLTINTAIVYMHRFYMHHSFTKFNKNIISSTALFLAAKVEEQARKLEHVIKVAHACLHPLEPLLDTKCDAYLQQTQELVILETIMLQTLGFEITIEHPHTDVVKCTQLVRASKDLAQTSYFMATNSLHLTTFCLQYKPTVIACVCIHLACKWSNWEIPVSTDGKHWWEYVDPTVTLELLDELTHEFLQILEKTPNRLKKIRNWRANQAARKPKVDGQVSETPLLGSSLVQNSILVDSVTGVPTNPSFQKPSTSAFPAPVPLNSGNISVQDSHTSDNLSMLATGMPSTSYGLSSHQEWPQHQDSARTEQLYSQKQETSLSGSQYNINFQQGPSISLHSGLHHRPDKISDHSSVKQEYTHKAGSSKHHGPISTTPGIIPQKMSLDKYREKRKLETLDLDVRDHYIAAQVEQQHKQGQSQAASSSSVTSPIKMKIPIANTEKYMADKKEKSGSLKLRIPIPPTDKSASKEELKMKIKVSSSERHSSSDEGSGKSKHSSPHISRDHKEKHKEHPSSRHHTSSHKHSHSHSGSSSGGSKHSADGIPPTVLRSPVGLSSDGISSSSSSSRKRLHVNDASHNHHSKMSKSSKSSGSSSSSSSSVKQYISSHNSVFNHPLPPPPPVTYQVGYGHLSTLVKLDKKPVETNGPDANHEYSTSSQHMDYKDTFDMLDSLLSAQGMNM,,-1.0,MASGRGASSRWFFTREQLENTPSRRCGVEADKELSCRQQAANLIQEMGQRLNVSQLTINTAIVYMHRFYMHHSFTKFNKNIISSTALFLAAKVEEQARKLEHVIKVAHACLHPLEPLLDTKCDAYLQQTQELVILETIMLQTLGFEITIEHPHTDVVKCTQLVRASKDLAQTSYFMATNSLHLTTFCLQYKPTVIACVCIHLACKWSNWEIPVSTDGKHWWEYVDPTVTLELLDELTHEFLQILEKTPNRLKKIRNWRACQAARKPKVDGQVSETPLLGSSLVQNSILVDSVTGVPTNPSFQKPSTSAFPAPVPLNSGNISVQDSHTSDNLSMLATGMPSTSYGLSSHQEWPQHQDSARTEQLYSQKQETSLSGSQYNINFQQGPSISLHSGLHHRPDKISDHSSVKQEYTHKAGSSKHHGPISTTPGIIPQKMSLDKYREKRKLETLDLDVRDHYIAAQVEQQHKQGQSQAASSSSVTSPIKMKIPIANTEKYMADKKEKSGSLKLRIPIPPTDKSASKEELKMKIKVSSSERHSSSDEGSGKSKHSSPHISRDHKEKHKEHPSSRHHTSSHKHSHSHSGSSSGGSKHSADGIPPTVLRSPVGLSSDGISSSSSSSRKRLHVNDASHNHHSKMSKSSKSSGSSSSSSSSVKQYISSHNSVFNHPLPPPPPVTYQVGYGHLSTLVKLDKKPVETNGPDANHEYSTSSQHMDYKDTFDMLDSLLSAQGMNM,Cyclin-T2,"Regulatory subunit of the cyclin-dependent kinase pair (CDK9/cyclin T) complex, also called positive transcription elongation factor B (P-TEFB), which is proposed to facilitate the transition from abortive to production elongation by phosphorylating the CTD (carboxy-terminal domain) of the large subunit of RNA polymerase II (RNAP II). The activity of this complex is regulated by binding with 7SK snRNA. Plays a role during muscle differentiation; P-TEFB complex interacts with MYOD1; this tripartite complex promotes the transcriptional activity of MYOD1 through its CDK9-mediated phosphorylation and binds the chromatin of promoters and enhancers of muscle-specific genes; this event correlates with hyperphosphorylation of the CTD domain of RNA pol II. In addition, enhances MYOD1-dependent transcription through interaction with PKN1. Involved in early embryo development.(Microbial infection) Promotes transcriptional activation of early and late herpes simplex virus 1/HHV-1 promoters.",Activation of HIV-1 Tat dysfunction. Mutation of a single residue in CycT2 (asparagine 260 to cysteine) abolishes the ability of CycT2 to bind Tat1 and also deactivates not only TAR binding by all three Tat-CycT2 complexes but also Tat function.,Activation of HIV-1 Tat dysfunction. Mutation of a single residue in CycT2 (asparagine 260 to cysteine) abolishes the ability of CycT2 to bind Tat1 and also deactivates not only TAR binding by all three Tat-CycT2 complexes but also Tat function.
3638,3638,0,0,A0A646QV53-K126F,MSSVTIGKCYIQNRENGGRAFYNLGRKDLGIFTGKMYDDQIWSFQKSDTPGYYTIGRESKFLQYNGEQVIMSDIEQDTTLWSLEEVPEDKGFYRLLNKVHKAYLDYNGGDLVANKHQTESEKWILFKAY,,-1.0,MSSVTIGKCYIQNRENGGRAFYNLGRKDLGIFTGKMYDDQIWSFQKSDTPGYYTIGRESKFLQYNGEQVIMSDIEQDTTLWSLEEVPEDKGFYRLLNKVHKAYLDYNGGDLVANKHQTESEKWILKKAY,GM1b/asialo-GM1 oligosaccharide-binding R-type lectin,"Galbeta1-3GalNAcbeta1-4Galbeta1-4Glc oligosaccharide-binding lectin. Binds strongly to the oligosaccharides of ganglioside GM1b and to a lesser extent its precursor asialo-GM1. Binds weakly to asialo-GM2 oligosaccharide and to the glycan moiety of globo-series stage-specific embryonal antigen 4 (SSEA-4) hexaose. Binds galactose, N-acetylgalactose and lactose. Does not bind GM1. Does not bind to Gal-beta1,3-GalNAc (Thomsen-Friedenreich antigen), the oligosaccharide of GM1a ganglioside or SSEA-4 tetraose. Does not bind to N-glycans, O-glycans or glycosaminoglycans of glycoproteins. Does not bind Lewis glycans, derivatives of lactose or N-acetyllactosamine or blood group (ABH-type) oligosaccharides. Does not bind glucose. Has hemagglutination activity towards rabbit erythrocytes. Displays cytotoxic effects against various cultured cell lines including human breast (MCF-7), cervical (HeLa) and colon cancer (Caco2) cell lines, as well as dog kidney (MDCK) cell line that express asialo-GM1 oligosaccharide at their cell surface. Shows dose- and time-dependent activation of MKK3/6, ERK1/2 and p38 MAPK, as well as caspase-3/9 in HeLa cervical cancer cells. No cytotoxic effect on BT474 human breast cancer cell line. May be involved in recognition of glycans found on parasitic or symbiotic microorganisms.","Loss of hemagglutination. Gain of homodimerization, but loses saccharide binding; when associated with R-12. This mutation may not affect the binding affinity of SeviL to its ligands, such as the linear saccharides of the ganglioside GM1b and its precursor, asialo-GM1.","Loss of hemagglutination. Gain of homodimerization, but loses saccharide binding; when associated with R-12. This mutation may not affect the binding affinity of SeviL to its ligands, such as the linear saccharides of the ganglioside GM1b and its precursor, asialo-GM1."
3641,3641,0,0,P58753-N55S,MASSTSLPAPGSRPKKPLGKMADWFRQTLLKKPKKRPNSPESTSSDASQPTSQDSPLPPSLSSVTSPSLPPTHASDSGSSRWSKDYDVCVCHSEEDLVAAQDLVSYLEGSTASLRCFLQLRDATPGGAIVSELCQALSSSHCRVLLITPGFLQDPWCKYQMLQALTEAPGAEGCTIPLLSGLSRAAYPPELRFMYYVDGRGPDGGFRQVKEAVMRYLQTLS,,-1.0,MASSTSLPAPGSRPKKPLGKMADWFRQTLLKKPKKRPNSPESTSSDASQPTSQDNPLPPSLSSVTSPSLPPTHASDSGSSRWSKDYDVCVCHSEEDLVAAQDLVSYLEGSTASLRCFLQLRDATPGGAIVSELCQALSSSHCRVLLITPGFLQDPWCKYQMLQALTEAPGAEGCTIPLLSGLSRAAYPPELRFMYYVDGRGPDGGFRQVKEAVMRYLQTLS,Toll/interleukin-1 receptor domain-containing adapter protein,"Adapter involved in TLR2, TLR4 and RAGE signaling pathways in the innate immune response. Acts via IRAK2 and TRAF-6, leading to the activation of NF-kappa-B, MAPK1, MAPK3 and JNK, and resulting in cytokine secretion and the inflammatory response. Positively regulates the production of TNF-alpha (TNF) and interleukin-6 (IL6).",Enhances NF-kappa-B activation and TNF production. The mutation in Mal causes a non-functional change in TLR-4 signal transduction.,Enhances NF-kappa-B activation and TNF production. The mutation in Mal causes a non-functional change in TLR-4 signal transduction.
3664,3664,0,0,P40189-G190Y,MLTLQTWLVQALFIFLTTESTGELLDPCGYISPESPVVQLHSNFTAVCVLKEKCMDYFHVNANYIVWKTNHFTIPKEQYTIINRTASSVTFTDIASLNIQLTCNILTFGQLEQNVYGITIISGLPPEKPKNLSCIVNEGKKMRCEWDGGRETHLETNFTLKSEWATHKFADCKAKRDTPTSCTVDYSTVYFVNIEVWVEAENALGKVTSDHINFDPVYKVKPNPPHNLSVINSEELSSILKLTWTNPSIKSVIILKYNIQYRTKDASTWSQIPPEDTASTRSSFTVQDLKPFTEYVFRIRCMKEDGKGYWSDWSEEASGITYEDRPSKAPSFWYKIDPSHTQGYRTVQLVWKTLPPFEANGKILDYEVTLTRWKSHLQNYTVNATKLTVNLTNDRYLATLTVRNLVGKSDAAVLTIPACDFQATHPVMDLKAFPKDNMLWVEWTTPRESVKKYILEWCVLSDKAPCITDWQQEDGTVHRTYLRGNLAESKCYLITVTPVYADGPGSPESIKAYLKQAPPSKGPTVRTKKVGKNEAVLEWDQLPVDVQNGFIRNYTIFYRTIIGNETAVNVDSSHTEYTLSSLTSDTLYMVRMAAYTDEGGKDGPEFTFTTPKFAQGEIEAIVVPVCLAFLLTTLLGVLFCFNKRDLIKKHIWPNVPDPSKSHIAQWSPHTPPRHNFNSKDQMYSDGNFTDVSVVEIEANDKKPFPEDLKSLDLFKKEKINTEGHSSGIGGSSCMSSSRPSISSSDENESSQNTSSTVQYSTVVHSGYRHQVPSVQVFSRSESTQPLLDSEERPEDLQLVDHVDGGDGILPRQQYFKQNCSQHESSPDISHFERSKQVSSVNEEDFVRLKQQISDHISQSCGSGQMKMFQEVSAADAFGPGTEGQVERFETVGMEAATDEGMPKSYLPQTVRQGGYMPQ,,-1.0,MLTLQTWLVQALFIFLTTESTGELLDPCGYISPESPVVQLHSNFTAVCVLKEKCMDYFHVNANYIVWKTNHFTIPKEQYTIINRTASSVTFTDIASLNIQLTCNILTFGQLEQNVYGITIISGLPPEKPKNLSCIVNEGKKMRCEWDGGRETHLETNFTLKSEWATHKFADCKAKRDTPTSCTVDYSTVGFVNIEVWVEAENALGKVTSDHINFDPVYKVKPNPPHNLSVINSEELSSILKLTWTNPSIKSVIILKYNIQYRTKDASTWSQIPPEDTASTRSSFTVQDLKPFTEYVFRIRCMKEDGKGYWSDWSEEASGITYEDRPSKAPSFWYKIDPSHTQGYRTVQLVWKTLPPFEANGKILDYEVTLTRWKSHLQNYTVNATKLTVNLTNDRYLATLTVRNLVGKSDAAVLTIPACDFQATHPVMDLKAFPKDNMLWVEWTTPRESVKKYILEWCVLSDKAPCITDWQQEDGTVHRTYLRGNLAESKCYLITVTPVYADGPGSPESIKAYLKQAPPSKGPTVRTKKVGKNEAVLEWDQLPVDVQNGFIRNYTIFYRTIIGNETAVNVDSSHTEYTLSSLTSDTLYMVRMAAYTDEGGKDGPEFTFTTPKFAQGEIEAIVVPVCLAFLLTTLLGVLFCFNKRDLIKKHIWPNVPDPSKSHIAQWSPHTPPRHNFNSKDQMYSDGNFTDVSVVEIEANDKKPFPEDLKSLDLFKKEKINTEGHSSGIGGSSCMSSSRPSISSSDENESSQNTSSTVQYSTVVHSGYRHQVPSVQVFSRSESTQPLLDSEERPEDLQLVDHVDGGDGILPRQQYFKQNCSQHESSPDISHFERSKQVSSVNEEDFVRLKQQISDHISQSCGSGQMKMFQEVSAADAFGPGTEGQVERFETVGMEAATDEGMPKSYLPQTVRQGGYMPQ,Interleukin-6 receptor subunit beta,"Signal-transducing molecule. The receptor systems for IL6, LIF, OSM, CNTF, IL11, CTF1 and BSF3 can utilize IL6ST for initiating signal transmission. Binding of IL6 to IL6R induces IL6ST homodimerization and formation of a high-affinity receptor complex, which activates the intracellular JAK-MAPK and JAK-STAT3 signaling pathways. That causes phosphorylation of IL6ST tyrosine residues which in turn activates STAT3. In parallel, the IL6 signaling pathway induces the expression of two cytokine receptor signaling inhibitors, SOCS1 and SOCS3, which inhibit JAK and terminate the activity of the IL6 signaling pathway as a negative feedback loop. Also activates the yes-associated protein 1 (YAP) and NOTCH pathways to control inflammation-induced epithelial regeneration, independently of STAT3. Acts as a receptor for the neuroprotective peptide humanin as part of a complex with IL27RA/WSX1 and CNTFR. Mediates signals which regulate immune response, hematopoiesis, pain control and bone metabolism. Has a role in embryonic development. Essential for survival of motor and sensory neurons and for differentiation of astrocytes. Required for expression of TRPA1 in nociceptive neurons. Required for the maintenance of PTH1R expression in the osteoblast lineage and for the stimulation of PTH-induced osteoblast differentiation. Required for normal trabecular bone mass and cortical bone composition.Binds to the soluble IL6:sIL6R complex (hyper-IL6), thereby blocking IL6 trans-signaling. Inhibits sIL6R-dependent acute phase response. Also blocks IL11 cluster signaling through IL11R.",Does induce ligand-independent activation. The mutation in gp130 results in a ligand-dependent inactive gp130.,Does induce ligand-independent activation. The mutation in gp130 results in a ligand-dependent inactive gp130.
3674,3674,0,0,P06213-A992Y,MATGGRRGAAAAPLLVAVAALLLGAAGHLYPGEVCPGMDIRNNLTRLHELENCSVIEGHLQILLMFKTRPEDFRDLSFPKLIMITDYLLLFRVYGLESLKDLFPNLTVIRGSRLFFNYALVIFEMVHLKELGLYNLMNITRGSVRIEKNNELCYLATIDWSRILDSVEDNYIVLNKDDNEECGDICPGTAKGKTNCPATVINGQFVERCWTHSHCQKVCPTICKSHGCTAEGLCCHSECLGNCSQPDDPTKCVACRNFYLDGRCVETCPPPYYHFQDWRCVNFSFCQDLHHKCKNSRRQGCHQYVIHNNKCIPECPSGYTMNSSNLLCTPCLGPCPKVCHLLEGEKTIDSVTSAQELRGCTVINGSLIINIRGGNNLAAELEANLGLIEEISGYLKIRRSYALVSLSFFRKLRLIRGETLEIGNYSFYALDNQNLRQLWDWSKHNLTITQGKLFFHYNPKLCLSEIHKMEEVSGTKGRQERNDIALKTNGDQASCENELLKFSYIRTSFDKILLRWEPYWPPDFRDLLGFMLFYKEAPYQNVTEFDGQDACGSNSWTVVDIDPPLRSNDPKSQNHPGWLMRGLKPWTQYAIFVKTLVTFSDERRTYGAKSDIIYVQTDATNPSVPLDPISVSNSSSQIILKWKPPSDPNGNITHYLVFWERQAEDSELFELDYCLKGLKLPSRTWSPPFESEDSQKHNQSEYEDSAGECCSCPKTDSQILKELEESSFRKTFEDYLHNVVFVPRKTSSGTGAEDPRPSRKRRSLGDVGNVTVAVPTVAAFPNTSSTSVPTSPEEHRPFEKVVNKESLVISGLRHFTGYRIELQACNQDTPEERCSVAAYVSARTMPEAKADDIVGPVTHEIFENNVVHLMWQEPKEPNGLIVLYEVSYRRYGDEELHLCVSRKHFALERGCRLRGLSPGNYSVRIRATSLAGNGSWTEPTYFYVTDYLDVPSNIAKIIIGPLIFVFLFSVVIGSIYLFLRKRQPDGPLGPLYASSNPEYLSASDVFPCSVYVPDEWEVSREKIT,,-1.0,MATGGRRGAAAAPLLVAVAALLLGAAGHLYPGEVCPGMDIRNNLTRLHELENCSVIEGHLQILLMFKTRPEDFRDLSFPKLIMITDYLLLFRVYGLESLKDLFPNLTVIRGSRLFFNYALVIFEMVHLKELGLYNLMNITRGSVRIEKNNELCYLATIDWSRILDSVEDNYIVLNKDDNEECGDICPGTAKGKTNCPATVINGQFVERCWTHSHCQKVCPTICKSHGCTAEGLCCHSECLGNCSQPDDPTKCVACRNFYLDGRCVETCPPPYYHFQDWRCVNFSFCQDLHHKCKNSRRQGCHQYVIHNNKCIPECPSGYTMNSSNLLCTPCLGPCPKVCHLLEGEKTIDSVTSAQELRGCTVINGSLIINIRGGNNLAAELEANLGLIEEISGYLKIRRSYALVSLSFFRKLRLIRGETLEIGNYSFYALDNQNLRQLWDWSKHNLTITQGKLFFHYNPKLCLSEIHKMEEVSGTKGRQERNDIALKTNGDQASCENELLKFSYIRTSFDKILLRWEPYWPPDFRDLLGFMLFYKEAPYQNVTEFDGQDACGSNSWTVVDIDPPLRSNDPKSQNHPGWLMRGLKPWTQYAIFVKTLVTFSDERRTYGAKSDIIYVQTDATNPSVPLDPISVSNSSSQIILKWKPPSDPNGNITHYLVFWERQAEDSELFELDYCLKGLKLPSRTWSPPFESEDSQKHNQSEYEDSAGECCSCPKTDSQILKELEESSFRKTFEDYLHNVVFVPRKTSSGTGAEDPRPSRKRRSLGDVGNVTVAVPTVAAFPNTSSTSVPTSPEEHRPFEKVVNKESLVISGLRHFTGYRIELQACNQDTPEERCSVAAYVSARTMPEAKADDIVGPVTHEIFENNVVHLMWQEPKEPNGLIVLYEVSYRRYGDEELHLCVSRKHFALERGCRLRGLSPGNYSVRIRATSLAGNGSWTEPTYFYVTDYLDVPSNIAKIIIGPLIFVFLFSVVIGSIYLFLRKRQPDGPLGPLAASSNPEYLSASDVFPCSVYVPDEWEVSREKIT,Insulin receptor,"Receptor tyrosine kinase which mediates the pleiotropic actions of insulin. Binding of insulin leads to phosphorylation of several intracellular substrates, including, insulin receptor substrates (IRS1, 2, 3, 4), SHC, GAB1, CBL and other signaling intermediates. Each of these phosphorylated proteins serve as docking proteins for other signaling proteins that contain Src-homology-2 domains (SH2 domain) that specifically recognize different phosphotyrosine residues, including the p85 regulatory subunit of PI3K and SHP2. Phosphorylation of IRSs proteins lead to the activation of two main signaling pathways: the PI3K-AKT/PKB pathway, which is responsible for most of the metabolic actions of insulin, and the Ras-MAPK pathway, which regulates expression of some genes and cooperates with the PI3K pathway to control cell growth and differentiation. Binding of the SH2 domains of PI3K to phosphotyrosines on IRS1 leads to the activation of PI3K and the generation of phosphatidylinositol-(3, 4, 5)-triphosphate (PIP3), a lipid second messenger, which activates several PIP3-dependent serine/threonine kinases, such as PDPK1 and subsequently AKT/PKB. The net effect of this pathway is to produce a translocation of the glucose transporter SLC2A4/GLUT4 from cytoplasmic vesicles to the cell membrane to facilitate glucose transport. Moreover, upon insulin stimulation, activated AKT/PKB is responsible for: anti-apoptotic effect of insulin by inducing phosphorylation of BAD; regulates the expression of gluconeogenic and lipogenic enzymes by controlling the activity of the winged helix or forkhead (FOX) class of transcription factors. Another pathway regulated by PI3K-AKT/PKB activation is mTORC1 signaling pathway which regulates cell growth and metabolism and integrates signals from insulin. AKT mediates insulin-stimulated protein synthesis by phosphorylating TSC2 thereby activating mTORC1 pathway. The Ras/RAF/MAP2K/MAPK pathway is mainly involved in mediating cell growth, survival and cellular differentiation of insulin. Phosphorylated IRS1 recruits GRB2/SOS complex, which triggers the activation of the Ras/RAF/MAP2K/MAPK pathway. In addition to binding insulin, the insulin receptor can bind insulin-like growth factors (IGFI and IGFII). Isoform Short has a higher affinity for IGFII binding. When present in a hybrid receptor with IGF1R, binds IGF1. PubMed:12138094 shows that hybrid receptors composed of IGF1R and INSR isoform Long are activated with a high affinity by IGF1, with low affinity by IGF2 and not significantly activated by insulin, and that hybrid receptors composed of IGF1R and INSR isoform Short are activated by IGF1, IGF2 and insulin. In contrast, PubMed:16831875 shows that hybrid receptors composed of IGF1R and INSR isoform Long and hybrid receptors composed of IGF1R and INSR isoform Short have similar binding characteristics, both bind IGF1 and have a low affinity for insulin. In adipocytes, inhibits lipolysis.",Increases interaction with IRS1 but has no effect on interaction with SHC1. Mutation of Y-992 increases interaction with SHC.,Increases interaction with IRS1 but has no effect on interaction with SHC1. Mutation of Y-992 increases interaction with SHC.
3675,3675,0,0,Q68EN5-A227R,MVLDSGAQAYDQAPPSPPTSPPSLRHRLKPSDRDGPPLYPWSQSLALPLALAVPPALQPQPEQQPFSQMLLGHRGHMRRSESTYSVNSTGRRGRGTLGRPPPGRGRNPGGGTLRPAASLPHIAKTQRDAGHIASKSPCMLVALRPTNMDRERDKFFQSHYTYNPQFEYQEPMPTAVLEKYCEASGQFIHQAVGIIEAVLEKFGTYEHFEAATGGQLLTKCQIWSIVRKYMQKEGCAGEVVVQLSEDLLSQAVMMVENSRPTLAINLTGARQYWLEGMLRHEIGTHYLRGVNNARQPWHNAEGRLRYGLRPANPTEEGLASLHSVLFRKQPFLWRAALLYYTIHRAARMSFRQLFQDLERYVQDADVRWEYCVRAKRGQTDTSLPGCFSKDQVYLDGIVRILRHRQTIDFPLLTSLGKVSYEDVDHLRPHGVLDNTRVPHFMQDLARYRQQLEHIMATNRLDEAELGRLLPD,,-1.0,MVLDSGAQAYDQAPPSPPTSPPSLRHRLKPSDRDGPPLYPWSQSLALPLALAVPPALQPQPEQQPFSQMLLGHRGHMRRSESTYSVNSTGRRGRGTLGRPPPGRGRNPGGGTLRPAASLPHIAKTQRDAGHIASKSPCMLVALRPTNMDRERDKFFQSHYTYNPQFEYQEPMPTAVLEKYCEASGQFIHQAVGIIEAVLEKFGTYEHFEAATGGQLLTKCQIWSIVAKYMQKEGCAGEVVVQLSEDLLSQAVMMVENSRPTLAINLTGARQYWLEGMLRHEIGTHYLRGVNNARQPWHNAEGRLRYGLRPANPTEEGLASLHSVLFRKQPFLWRAALLYYTIHRAARMSFRQLFQDLERYVQDADVRWEYCVRAKRGQTDTSLPGCFSKDQVYLDGIVRILRHRQTIDFPLLTSLGKVSYEDVDHLRPHGVLDNTRVPHFMQDLARYRQQLEHIMATNRLDEAELGRLLPD,Microtubule-associated tyrosine carboxypeptidase 1,"Tyrosine carboxypeptidase that removes the C-terminal tyrosine residue of alpha-tubulin, thereby regulating microtubule dynamics and function. Also able to remove the C-terminal phenylalanine residue of alpha-tubulin TUBA8. Recognizes adjacent tubulin dimers along the same protofilament.",Increased binding to microtubules.,Increased binding to microtubules.
3678,3678,0,0,Q9NQW5-W312S,MSPERSQEESPEGDTERTERKPMVKDAFKDISIYFTKEEWAEMGDWEKTRYRNVKMNYNALITVGLRATRPAFMCHRRQAIKLQVDDTEDSDEEWTPRQQVKPPWMAFRGEQSKHQKGMPKASFNNESSLRELSGTPNLLNTSDSEQAQKPVSPPGEASTSGQHSRLKLELRRKETEGKMYSLRERKGHAYKEISEPQDDDYLYCEMCQNFFIDSCAAHGPPTFVKDSAVDKGHPNRSALSLPPGLRIGPSGIPQAGLGVWNEASDLPLGLHFGPYEGRITEDEEAANSGYSWLITKGRNCYEYVDGKDKSSANWMRYVNCARDDEEQNLVAFQYHRQIFYRTCRVIRPGCELLVWSGDEYGQELGIRSSIEPAESLGQAVNCWSGMGMSMARNWASSGAASGRKSSWQGENQSQRSIHVPHAVWPFQVKNFSVNMWNAITPLRTSQDHLQENFSNQRIPAQGIRIRSGNILIHAAVMTKPKVKRSKKGPNS,,-1.0,MSPERSQEESPEGDTERTERKPMVKDAFKDISIYFTKEEWAEMGDWEKTRYRNVKMNYNALITVGLRATRPAFMCHRRQAIKLQVDDTEDSDEEWTPRQQVKPPWMAFRGEQSKHQKGMPKASFNNESSLRELSGTPNLLNTSDSEQAQKPVSPPGEASTSGQHSRLKLELRRKETEGKMYSLRERKGHAYKEISEPQDDDYLYCEMCQNFFIDSCAAHGPPTFVKDSAVDKGHPNRSALSLPPGLRIGPSGIPQAGLGVWNEASDLPLGLHFGPYEGRITEDEEAANSGYSWLITKGRNCYEYVDGKDKSWANWMRYVNCARDDEEQNLVAFQYHRQIFYRTCRVIRPGCELLVWSGDEYGQELGIRSSIEPAESLGQAVNCWSGMGMSMARNWASSGAASGRKSSWQGENQSQRSIHVPHAVWPFQVKNFSVNMWNAITPLRTSQDHLQENFSNQRIPAQGIRIRSGNILIHAAVMTKPKVKRSKKGPNS,Histone-lysine N-methyltransferase PRDM7,Histone methyltransferase that selectively methylates 'Lys-4' of dimethylated histone H3 (H3K4me2) to produce trimethylated 'Lys-4' histone H3 (H3K4me3). May play a role in epigenetic regulation of gene expression by defining an active chromatin state.,"Increases the ability to sequentially mono-, di-, and tri-methylate both 'Lys-4' and 'Lys-36' of histone H3, albeit with higher efficiency when compared to PRDM9.","Increases the ability to sequentially mono-, di-, and tri-methylate both 'Lys-4' and 'Lys-36' of histone H3, albeit with higher efficiency when compared to PRDM9."
3687,3687,0,0,O95497-I26T,MTTQLPAYVAILLFYVSRASCQDTFTAAVYEHAAILPNATLTPVSREEALALMNRNLDILEGAITSAADQGAHIIVTPEDAIYGWNFNRDSLYPYLEDIPDPEVNWIPCNNRNRFGQTPVQERLSCLAKNNSIYVVANIGDKKPCDTSDPQCPPDGRYQYNTDVVFDSQGKLVARYHKQNLFMGENQFNVPKEPEIVTFNTTFGSFGIFTCFDILFHDPAVTLVKDFHVDTIVFPTAWMNVLPHLSAVEFHSAWAMGMRVNFLASNIHYPSKKMTGSGIYAPNSSRAFHYDMKTEEGKLLLSQLDSHPSHSAVVNWTSYASSIEALSSGNKEFKGTVFFDEFTFVKLTGVAGNYTVCQKDLCCHLSYKMSENIPNEVYALGAFDGLHTVEGRYYLQICTLLKCKTTNLNTCGDSAETASTRFEMFSLSGTFGTQYVFPEVLLSENQLAPGEFQVSTDGRLFSLKPTSGPVLTVTLFGRLYEKDWASNASSGLTAQARIIMLIVIAPIVCSLSW,,-1.0,MTTQLPAYVAILLFYVSRASCQDTFIAAVYEHAAILPNATLTPVSREEALALMNRNLDILEGAITSAADQGAHIIVTPEDAIYGWNFNRDSLYPYLEDIPDPEVNWIPCNNRNRFGQTPVQERLSCLAKNNSIYVVANIGDKKPCDTSDPQCPPDGRYQYNTDVVFDSQGKLVARYHKQNLFMGENQFNVPKEPEIVTFNTTFGSFGIFTCFDILFHDPAVTLVKDFHVDTIVFPTAWMNVLPHLSAVEFHSAWAMGMRVNFLASNIHYPSKKMTGSGIYAPNSSRAFHYDMKTEEGKLLLSQLDSHPSHSAVVNWTSYASSIEALSSGNKEFKGTVFFDEFTFVKLTGVAGNYTVCQKDLCCHLSYKMSENIPNEVYALGAFDGLHTVEGRYYLQICTLLKCKTTNLNTCGDSAETASTRFEMFSLSGTFGTQYVFPEVLLSENQLAPGEFQVSTDGRLFSLKPTSGPVLTVTLFGRLYEKDWASNASSGLTAQARIIMLIVIAPIVCSLSW,Pantetheinase,Amidohydrolase that hydrolyzes specifically one of the carboamide linkages in D-pantetheine thus recycling pantothenic acid (vitamin B5) and releasing cysteamine.,This mutation may result in unaltered lymphocyte migration.,This mutation may result in unaltered lymphocyte migration.
3692,3692,0,0,P14611-A349H,MTDVVIVSAARTAVGKFGGSLAKIPAPELGAVVIKAALERAGVKPEQVSEVIMGQVLTAGSGQNPARQAAIKAGLPAMVPAMTINKVCGSGLKAVMLAANAIMAGDAEIVVAGGQENMSAAPHVLPGSRDGFRMGDAKLVDTMIVDGLWDVYNQYHMGITAENVAKEYGITREAQDEFAVGSQNKAEAAQKAGKFDEEIVPVLIPQRKGDPVAFKTDEFVRQGATLDSMSGLKPAFDKAGTVTAANASGLNDGAAAVVVMSAAKAKELGLTPLATIKSYANAGVDPKVMGMGPVPASKRALSRAEWTPQDLDLMEINEAFAAQALAVHQQMGWDTSKVNVNGGAIAIGHPIGASGCRILVTLLHEMKRRDAKKGLASLCIGGGMGVALAVERK,,-1.0,MTDVVIVSAARTAVGKFGGSLAKIPAPELGAVVIKAALERAGVKPEQVSEVIMGQVLTAGSGQNPARQAAIKAGLPAMVPAMTINKVCGSGLKAVMLAANAIMAGDAEIVVAGGQENMSAAPHVLPGSRDGFRMGDAKLVDTMIVDGLWDVYNQYHMGITAENVAKEYGITREAQDEFAVGSQNKAEAAQKAGKFDEEIVPVLIPQRKGDPVAFKTDEFVRQGATLDSMSGLKPAFDKAGTVTAANASGLNDGAAAVVVMSAAKAKELGLTPLATIKSYANAGVDPKVMGMGPVPASKRALSRAEWTPQDLDLMEINEAFAAQALAVHQQMGWDTSKVNVNGGAIAIGAPIGASGCRILVTLLHEMKRRDAKKGLASLCIGGGMGVALAVERK,Acetyl-CoA acetyltransferase,"Catalyzes the condensation of two acetyl-coA units to form acetoacetyl-CoA. Is involved in the biosynthesis of polyhydroxybutyrate (PHB), which is accumulated as an intracellular energy reserve material when cells grow under conditions of nutrient limitation. Also catalyzes the reverse reaction, i.e. the cleavage of acetoacetyl-CoA, and is therefore also involved in the reutilization of PHB.",Almost complete gain of acetoacetyl-CoA thiolase activity.,Almost complete gain of acetoacetyl-CoA thiolase activity.
3695,3695,0,0,O74700-G52E,MDALNSKEQQEFQKVVEQKQMKDFMRLYSNLVERCFTDCVNDFTTSKLTNKEQTCIMKCSEKFLKHSERVGQRFQEQNAALGQGLGR,,-1.0,MDALNSKEQQEFQKVVEQKQMKDFMRLYSNLVERCFTDCVNDFTTSKLTNKGQTCIMKCSEKFLKHSERVGQRFQEQNAALGQGLGR,Mitochondrial import inner membrane translocase subunit TIM9,"Mitochondrial intermembrane chaperone that participates in the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space. Compared to TIM10, it may have a strong structural role.",In tim9-19; enhances the import of mitochondrial carrier proteins into mitochondria.,In tim9-19; enhances the import of mitochondrial carrier proteins into mitochondria.
3705,3705,0,0,Q5T9G4-A190V,MGKSIPQYLGQLDIRKSVVSLATGAGAIYLLYKAIKAGIKCKPPLCSNSPICIARLAVERERHGRDSGELRRLLNSLECKQDEYAKSMILHSITRCVYLLEAEASACTTDDIVLLGYMLDDKDNSVKTQALNTLKAFSGIRKFRLKIQEHSIKVLELISTIWDTELHIAGLRLLNNLPLPDYVHPQLRRVMPALMEILQSDYILAQVQAVRLLSYLAQKNDLLYDILNCQVHSNFLNLFQPTQSGSLLYEVLVFAERLSEGRNAPHYHVVKWHYNEQSLHESLFGEESRLADRLLALVIHPEEDVQIQACKVIVSLQYPQDLRARPSSCQPSRSYFKNTE,,-1.0,MGKSIPQYLGQLDIRKSVVSLATGAGAIYLLYKAIKAGIKCKPPLCSNSPICIARLAVERERHGRDSGELRRLLNSLECKQDEYAKSMILHSITRCVYLLEAEASACTTDDIVLLGYMLDDKDNSVKTQALNTLKAFSGIRKFRLKIQEHSIKVLELISTIWDTELHIAGLRLLNNLPLPDYVHPQLRRAMPALMEILQSDYILAQVQAVRLLSYLAQKNDLLYDILNCQVHSNFLNLFQPTQSGSLLYEVLVFAERLSEGRNAPHYHVVKWHYNEQSLHESLFGEESRLADRLLALVIHPEEDVQIQACKVIVSLQYPQDLRARPSSCQPSRSYFKNTE,Armadillo repeat-containing protein 12,"Essential for male fertility and sperm mitochondrial sheath formation. Required for proper mitochondrial elongation and coiling along the flagellum during the formation of the mitochondrial sheath. Facilitates the growth and aggressiveness of neuroblastoma cells. Increases the EZH2 activity and H3K27me3 levels in a RBBP4-dependent manner, and facilitates the enrichment of polycomb repressive complex 2 and H3K27me3 on gene promoters, resulting in transcriptional repression of tumor suppressors affecting the proliferation, invasion, and metastasis of tumor cells.",Enables interaction with RBBP4. ARMC12 inhibits the growth and aggressiveness of NB cell lines.,Enables interaction with RBBP4. ARMC12 inhibits the growth and aggressiveness of NB cell lines.
3714,3714,0,0,Q9QY16-A66L,MASLLWGGDAGAAESERLNSHFSNLVHPRKNLRGIRSTTVPNIDGSLNTEEDDDEDDVVDLAANSLLNKLIRQSLVESSHRVEVLQKDPSSPLYSVKTFEELRLKEELLKGIYAMGFNRPSKIQEMALPMMLAHPPQNLIAQSQSGTGKTAAFVLAMLNRVNALELFPQCLCLAPTYELALQTGRVVERMGKFCVDVEVMYAIRGNRIPRGTDVTKQIVIGTPGTVLDWCFKRKLIDLTKIRVFVLDEADVMIDTQGFSDQSIRIQRALPSECQMLLFSATFEDSVWQFAERIIPDPNVIKLRKEELTLNNIRQYYVLCENRKDKYQALCNIYGGITIGQAIIFCQTRRNAKWLTVEMMQDGHQVSLLSGELTVEQRASIIQRFRDGKEKVLITTNVCARGIDVKQVTIVVNFDLPVNQSEEPDYETYLHRIGRTGRFGKKGLAFNMIEVDKLPLLMKIQDHFNSSIKQLDPEDMDEIEKIEY,,-1.0,MASLLWGGDAGAAESERLNSHFSNLVHPRKNLRGIRSTTVPNIDGSLNTEEDDDEDDVVDLAANSALNKLIRQSLVESSHRVEVLQKDPSSPLYSVKTFEELRLKEELLKGIYAMGFNRPSKIQEMALPMMLAHPPQNLIAQSQSGTGKTAAFVLAMLNRVNALELFPQCLCLAPTYELALQTGRVVERMGKFCVDVEVMYAIRGNRIPRGTDVTKQIVIGTPGTVLDWCFKRKLIDLTKIRVFVLDEADVMIDTQGFSDQSIRIQRALPSECQMLLFSATFEDSVWQFAERIIPDPNVIKLRKEELTLNNIRQYYVLCENRKDKYQALCNIYGGITIGQAIIFCQTRRNAKWLTVEMMQDGHQVSLLSGELTVEQRASIIQRFRDGKEKVLITTNVCARGIDVKQVTIVVNFDLPVNQSEEPDYETYLHRIGRTGRFGKKGLAFNMIEVDKLPLLMKIQDHFNSSIKQLDPEDMDEIEKIEY,ATP-dependent RNA helicase DDX25,ATP-dependent RNA helicase. Required for mRNA export and translation regulation during spermatid development.,Decreases nuclear expression; when associated with A-67 and A-70.,Decreases nuclear expression; when associated with A-67 and A-70.
3715,3715,0,0,P52126-D152A,MTEIYEQAKHSLQGEDFSSFNYLFAVNKLLSNPVSYDLGRDLIVRALDSRERFSEHTTILKNMVRKSGLFPYLKKEFTSLTPDDLRVLELYRTPFSDGYVFHSMQFHIFDLLKSGQNVVLSAPTSMGKSAIVDSLLGMGTLKRLVLVVPTVALADETRRRLQERFGDRYQIIHHSSQVCHSDQAVYVLTQERVNERDDIVDIDLFVIDEFYKLAFRQLKSGDIDHQDERVIELNIALSKLLKVSRQFYLTGPFVNSIRGLEKLGYPHTFVSTDFNTVALDVKTFGIKANDDKAKLKALGEIAHACVDATIIYCKSPTVAGLVARELIRLGHGTPTENPHVDWVSEEFDADWDYTVALRNGIGLHFGALPRALQQYTADQFNAGKLRFLLCTSTIIEGVNTIAKNVVIYDNRDGTRSIDKFTHGNIKGRAGRMGVHFVGKIFCLEEIPEDNLNQEVDIPLGIQGIDTPINLLASVQPDHLSEFSQDRFDEVFINDRVSIDLVKKHSYFRVEQFEMLQSMFEMMDDNEFSSLVFHWTPATNFLKTFAKIIARLVPHTFSRNGVPVKPTDVMIAKLAGYLSAESYSEYLKNQIDYARQWISEGEKRTLSIALNNDLKLITNTFGYTLPKVLSLMEDVVKHHAVKRGIRSKVDYTHVKLAFESFHLPPGVNALEEIGIPIQTLHRLVDLLEFSDEADVDELSQYLRDTQDIWSRSIGYVDQMFIRRALGIRRH,,-1.0,MTEIYEQAKHSLQGEDFSSFNYLFAVNKLLSNPVSYDLGRDLIVRALDSRERFSEHTTILKNMVRKSGLFPYLKKEFTSLTPDDLRVLELYRTPFSDGYVFHSMQFHIFDLLKSGQNVVLSAPTSMGKSAIVDSLLGMGTLKRLVLVVPTVDLADETRRRLQERFGDRYQIIHHSSQVCHSDQAVYVLTQERVNERDDIVDIDLFVIDEFYKLAFRQLKSGDIDHQDERVIELNIALSKLLKVSRQFYLTGPFVNSIRGLEKLGYPHTFVSTDFNTVALDVKTFGIKANDDKAKLKALGEIAHACVDATIIYCKSPTVAGLVARELIRLGHGTPTENPHVDWVSEEFDADWDYTVALRNGIGLHFGALPRALQQYTADQFNAGKLRFLLCTSTIIEGVNTIAKNVVIYDNRDGTRSIDKFTHGNIKGRAGRMGVHFVGKIFCLEEIPEDNLNQEVDIPLGIQGIDTPINLLASVQPDHLSEFSQDRFDEVFINDRVSIDLVKKHSYFRVEQFEMLQSMFEMMDDNEFSSLVFHWTPATNFLKTFAKIIARLVPHTFSRNGVPVKPTDVMIAKLAGYLSAESYSEYLKNQIDYARQWISEGEKRTLSIALNNDLKLITNTFGYTLPKVLSLMEDVVKHHAVKRGIRSKVDYTHVKLAFESFHLPPGVNALEEIGIPIQTLHRLVDLLEFSDEADVDELSQYLRDTQDIWSRSIGYVDQMFIRRALGIRRH,Anti-bacteriophage protein B,"Part of an antiviral system composed of AbpA and AbpB; when both are expressed from a plasmid they confer resistance to phages T2, T4, T7 and lambda but not RB32 or RB69. Resistance is temperature dependent, it can be seen at 30 degrees Celsius but not at 37 or 42 degrees Celsius. The system impairs phage but not bacterial DNA synthesis (shown for T4, T7 and lambda). Partially suppressed by mutations in T4 gene 41, a replicative helicase.Deletion or mutations in this gene were selected in directed evolution experiments for resistance to intense ionizing radiation (3000 Gy).",100-fold decreased survival following 3000 Gy ionizing radiation. The mutation in the dnaB gene contributes to the extreme sensitivity to ionizing radiation phenotype.,100-fold decreased survival following 3000 Gy ionizing radiation. The mutation in the dnaB gene contributes to the extreme sensitivity to ionizing radiation phenotype.
3733,3733,0,0,Q0DDE3-V737M,MSSAVVASSTTFLVALASSASRGGPRRGRVVGVAAPPALLYDGRAGRLALRAPPPPRPRPRRRDAGVVRRADDGENEAAVERAGEDDDEEEEFSSGAWQPPRSRRGGVGKVLKRRGTVPPVGRYGSGGDAARVRGAAAPAPAPTQDAASSKNGALLSGRDDDTPASRNGSVVTGADKPAAATPPVTITKLPAPDSPVILPSVDKPQPEFVIPDATAPAPPPPGSNPRSSAPLPKPDNSEFAEDKSAKVVESAPKPKATRSSPIPAVEEETWDFKKYFDLNEPDAAEDGDDDDDWADSDASDSEIDQDDDSGPLAGENVMNVIVVAAECSPWCKTGGLGDVAGALPKALARRGHRVMVVVPRYGDYAEAQDVGIRKYYKAAGQDLEVKYFHAFIDGVDFVFIDAPLFRHRQDDIYGGNRQEIMKRMILFCKAAVEVPWHVPCGGVPYGDGNLVFLANDWHTALLPVYLKAYYRDNGMMQYTRSVLVIHNIAYQGRGPVDEFPYMELPEHYLDHFKLYDPVGGEHANIFGAGLKMADRVVTVSPGYLWELKTTEGGWGLHDIIRENDWKMNGIVNGIDYREWNPEVDVHLQSDGYANYTVASLDSSKPRCKAALQRELGLEVRDDVPLIGFIGRLDGQKGVDIIGDAMPWIAGQDVQLVLLGSGRRDLEVMLQRFEAQHNSKVRGWVGFSVKMAHRITAGADVLVMPSRFEPCGLNQLYAMAYGTVPVVHAVGGLRDTMSAFDPFEDTGLGWTFDRAEPHKLIEALGHCLETYRKYKESWRGLQVRGMSQDLSWDHAAELYEEVLVKAKYQW,,-1.0,MSSAVVASSTTFLVALASSASRGGPRRGRVVGVAAPPALLYDGRAGRLALRAPPPPRPRPRRRDAGVVRRADDGENEAAVERAGEDDDEEEEFSSGAWQPPRSRRGGVGKVLKRRGTVPPVGRYGSGGDAARVRGAAAPAPAPTQDAASSKNGALLSGRDDDTPASRNGSVVTGADKPAAATPPVTITKLPAPDSPVILPSVDKPQPEFVIPDATAPAPPPPGSNPRSSAPLPKPDNSEFAEDKSAKVVESAPKPKATRSSPIPAVEEETWDFKKYFDLNEPDAAEDGDDDDDWADSDASDSEIDQDDDSGPLAGENVMNVIVVAAECSPWCKTGGLGDVAGALPKALARRGHRVMVVVPRYGDYAEAQDVGIRKYYKAAGQDLEVKYFHAFIDGVDFVFIDAPLFRHRQDDIYGGNRQEIMKRMILFCKAAVEVPWHVPCGGVPYGDGNLVFLANDWHTALLPVYLKAYYRDNGMMQYTRSVLVIHNIAYQGRGPVDEFPYMELPEHYLDHFKLYDPVGGEHANIFGAGLKMADRVVTVSPGYLWELKTTEGGWGLHDIIRENDWKMNGIVNGIDYREWNPEVDVHLQSDGYANYTVASLDSSKPRCKAALQRELGLEVRDDVPLIGFIGRLDGQKGVDIIGDAMPWIAGQDVQLVLLGSGRRDLEVMLQRFEAQHNSKVRGWVGFSVKMAHRITAGADVLVMPSRFEPCGLNQLYAMAYGTVPVVHAVGGLRDTVSAFDPFEDTGLGWTFDRAEPHKLIEALGHCLETYRKYKESWRGLQVRGMSQDLSWDHAAELYEEVLVKAKYQW,"Soluble starch synthase 2-3, chloroplastic/amyloplastic","Plays an important role during endosperm starch synthesis. Determines the type of amylopectin structure of starch grain. Synthesizes long B1 amylopectin chains by elongating short A and B1 chains, independently of the other soluble starch synthases. Barely active in japonica subspecies.",Decreased activity. Decreased activity; when associated with E-88 and/or G-604. Slightly decreased activity; when associated with G-604 and F-781.,Decreased activity. Decreased activity; when associated with E-88 and/or G-604. Slightly decreased activity; when associated with G-604 and F-781.
3737,3737,0,0,Q38898-E286S,MDLKYSASHCNLSSDMKLRRFHQHRGKGREEEYDASSLSLNNLSKLILPPLGVASYNQNHIRSSGWIISPMDSRYRCWEFYMVLLVAYSAWVYPFEVAFLNSSPKRNLCIADNIVDLFFAVDIVLTFFVAYIDERTQLLVREPKQIAVRYLSTWFLMDVASTIPFDAIGYLITGTSTLNITCNLLGLLRFWRLRRVKHLFTRLEKDIRYSYFWIRCFRLLSVTLFLVHCAGCSYYLIADRYPHQGKTWTDAIPNFTETSLSIRYIAAIYWSITTMTTVGYGDLHASNTIEMVFITVYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVNRNRLPPRLKDQILAYMCLRFKAESLNQQHLIDQLPKSIYKSICQHLFLPSVEKVYLFKGVSREILLLLVSKMKAEYIPPREDVIMQNEAPDDVYIIVSGEVEIIDSEMERESVLGTLRCGDIFGEVGALCCRPQSYTFQTKSLSQLLRLKTSFLIETMQIKQQDNATMLKNFLQHHKKLSNLDIGDLKAQQNGENTDVVPPNIASNLIAVVTTGNAALLDELLKAKLSPDITDSKGKTPLHVAASRGYEDCVLVLLKHGCNIHIRDVNGNSALWEAIISKHYEIFRILYHFAAISDPHIAGDLLCEAAKQNNVEVMKALLKQGLNVDTEDHHGVTALQVAMAEDQMDMVNLLATNGADVVCVNTHNEFTPLEKLRVVEEEEEEERGRVSIYRGHPLERRERSCNEAGKLILLPPSLDDLKKIAGEKFGFDGSETMVTNEDGAEIDSIEVIRDNDKLYFVVNKII,,-1.0,MDLKYSASHCNLSSDMKLRRFHQHRGKGREEEYDASSLSLNNLSKLILPPLGVASYNQNHIRSSGWIISPMDSRYRCWEFYMVLLVAYSAWVYPFEVAFLNSSPKRNLCIADNIVDLFFAVDIVLTFFVAYIDERTQLLVREPKQIAVRYLSTWFLMDVASTIPFDAIGYLITGTSTLNITCNLLGLLRFWRLRRVKHLFTRLEKDIRYSYFWIRCFRLLSVTLFLVHCAGCSYYLIADRYPHQGKTWTDAIPNFTETSLSIRYIAAIYWSITTMTTVGYGDLHAENTIEMVFITVYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVNRNRLPPRLKDQILAYMCLRFKAESLNQQHLIDQLPKSIYKSICQHLFLPSVEKVYLFKGVSREILLLLVSKMKAEYIPPREDVIMQNEAPDDVYIIVSGEVEIIDSEMERESVLGTLRCGDIFGEVGALCCRPQSYTFQTKSLSQLLRLKTSFLIETMQIKQQDNATMLKNFLQHHKKLSNLDIGDLKAQQNGENTDVVPPNIASNLIAVVTTGNAALLDELLKAKLSPDITDSKGKTPLHVAASRGYEDCVLVLLKHGCNIHIRDVNGNSALWEAIISKHYEIFRILYHFAAISDPHIAGDLLCEAAKQNNVEVMKALLKQGLNVDTEDHHGVTALQVAMAEDQMDMVNLLATNGADVVCVNTHNEFTPLEKLRVVEEEEEEERGRVSIYRGHPLERRERSCNEAGKLILLPPSLDDLKKIAGEKFGFDGSETMVTNEDGAEIDSIEVIRDNDKLYFVVNKII,Potassium channel AKT2/3,Highly selective and weak inward-rectifying potassium channel. Plays a role in both loading and unloading potassium into/from the phloem sap. Seems to control sugar loading into phloem via a voltage-dependent process. Blocked by physiological concentrations of external calcium and by external acidification. May interact with the cytoskeleton or with regulatory proteins. Dephosphorylation by PP2CA not only leads to the inhibition of potassium currents but also to an increase of the voltage-dependence of the channel. Regulated by the CBL4/CIPK6 calcium sensor/protein kinase complex via a kinase interaction-dependent but phosphorylation-independent translocation of the channel to the plasma membrane.,Enhances the proton and the potassium sensitivity; increased susceptibility to extracellular potassium; when associated with D-243. The mutation still mediated K(+) influx.,Enhances the proton and the potassium sensitivity; increased susceptibility to extracellular potassium; when associated with D-243. The mutation still mediated K(+) influx.
3751,3751,0,0,Q00496-A250E,MPKINSFNYNDPVNDRTILYIKPGGCQEFYKSFNIMKNIWIIPERNVIGTTPQDFHPPTSLKNGDSSYYDPNYLQSDEEKDRFLKIVTKIFNRINNNLSGGILLEELSKANPYLGNDNTPDNQFHIGDASAVEIKFSNGSQDILLPNVIIMGAEPDLFETNSSNISLRNNYMPSNHRFGSIAIVTFSPEYSFRFNDNCMNEFIQDPALTLMHELIHSLHGLYGAKGITTKYTITQKQNPLITNIRGTNIEEFLTFGGTDLNIITSAQSNDIYTNLLADYKKIASKLSKVQVSNPLLNPYKDVFEAKYGLDKDASGIYSVNINKFNDIFKKLYSFTEFDLRTKFQVKCRQTYIGQYKYFKLSNLLNDSIYNISEGYNINNLKVNFRGQNANLNPRIITPITGRGLVKKIIRFCKNIVSVKGIRKSICIEINNGELFFVASENSYNDDNINTPKEIDDTVTSNNNYENDLDQVILNFNSESAPGLSDEKLNLTIQNDAYIPKYDSNGTSDIEQHDVNELNVFFYLDAQKVPEGENNVNLTSSIDTALLEQPKIYTFFSSEFINNVNKPVQAALFVSWIQQVLVDFTTEANQKSTVDKIADISIVVPYIGLALNIGNEAQKGNFKDALELLGAGILLEFEPELLIPTILVFTIKSFLGSSDNKNKVIKAINNALKERDEKWKEVYSFIVSNWMTKINTQFNKRKEQMYQALQNQVNAIKTIIESKYNSYTLEEKNELTNKYDIKQIENELNQKVSIAMNNIDRFLTESSISYLMKIINEVKINKLREYDENVKTYLLNYIIQHGSILGESQQELNSMVTDTLNNSIPFKLSSYTDDKILISYFNKFFKRIKSSSVLNMRYKNDKYVDTSGYDSNININGDVYKYPTNKNQFGIYNDKLSEVNISQNDYIIYDNKYKNFSISFWVRIPNYDNKIVNVNNEYTIINCMRDNNSGWKVSLNHNEIIWTFEDNRGINQKLAFNYGNANGISDYINKWIFVTITNDRLGDSKLYINGNLIDQKSILNLGNIH,,-1.0,MPKINSFNYNDPVNDRTILYIKPGGCQEFYKSFNIMKNIWIIPERNVIGTTPQDFHPPTSLKNGDSSYYDPNYLQSDEEKDRFLKIVTKIFNRINNNLSGGILLEELSKANPYLGNDNTPDNQFHIGDASAVEIKFSNGSQDILLPNVIIMGAEPDLFETNSSNISLRNNYMPSNHRFGSIAIVTFSPEYSFRFNDNCMNEFIQDPALTLMHELIHSLHGLYGAKGITTKYTITQKQNPLITNIRGTNIAEFLTFGGTDLNIITSAQSNDIYTNLLADYKKIASKLSKVQVSNPLLNPYKDVFEAKYGLDKDASGIYSVNINKFNDIFKKLYSFTEFDLRTKFQVKCRQTYIGQYKYFKLSNLLNDSIYNISEGYNINNLKVNFRGQNANLNPRIITPITGRGLVKKIIRFCKNIVSVKGIRKSICIEINNGELFFVASENSYNDDNINTPKEIDDTVTSNNNYENDLDQVILNFNSESAPGLSDEKLNLTIQNDAYIPKYDSNGTSDIEQHDVNELNVFFYLDAQKVPEGENNVNLTSSIDTALLEQPKIYTFFSSEFINNVNKPVQAALFVSWIQQVLVDFTTEANQKSTVDKIADISIVVPYIGLALNIGNEAQKGNFKDALELLGAGILLEFEPELLIPTILVFTIKSFLGSSDNKNKVIKAINNALKERDEKWKEVYSFIVSNWMTKINTQFNKRKEQMYQALQNQVNAIKTIIESKYNSYTLEEKNELTNKYDIKQIENELNQKVSIAMNNIDRFLTESSISYLMKIINEVKINKLREYDENVKTYLLNYIIQHGSILGESQQELNSMVTDTLNNSIPFKLSSYTDDKILISYFNKFFKRIKSSSVLNMRYKNDKYVDTSGYDSNININGDVYKYPTNKNQFGIYNDKLSEVNISQNDYIIYDNKYKNFSISFWVRIPNYDNKIVNVNNEYTIINCMRDNNSGWKVSLNHNEIIWTFEDNRGINQKLAFNYGNANGISDYINKWIFVTITNDRLGDSKLYINGNLIDQKSILNLGNIH,Botulinum neurotoxin type E,"Botulinum toxin causes flaccid paralysis by inhibiting neurotransmitter (acetylcholine) release from the presynaptic membranes of nerve terminals of eukaryotic host skeletal and autonomic nervous system, with frequent heart or respiratory failure. Precursor of botulinum neurotoxin E which has 2 coreceptors; complex polysialylated gangliosides found on neural tissue and specific membrane-anchored proteins found in synaptic vesicles. Receptor proteins are exposed on host presynaptic cell membrane during neurotransmitter release, when the toxin heavy chain (HC) binds to them. Upon synaptic vesicle recycling the toxin is taken up via the endocytic pathway. When the pH of the toxin-containing endosome drops a structural rearrangement occurs so that the N-terminus of the HC forms pores that allows the light chain (LC) to translocate into the cytosol. Once in the cytosol the disulfide bond linking the 2 subunits is reduced and LC cleaves its target protein on synaptic vesicles, preventing their fusion with the cytoplasmic membrane and thus neurotransmitter release. Electrical stimulation increases uptake of toxin, probably by transiently exposing a receptor found in eukaryotic target synaptic vesicles. Uses the large lumenal domain of synaptic vesicle glycoproteins 2A and 2B (SV2A and SV2B) but not SV2C as receptor; an N-linked glycan of SV2 is essential for receptor function. Host cell gangliosides are also required for neurotoxin uptake and full toxicity. BoNT/E is a 'coincidence detector'; it requires simultaneous binding to coreceptor GT1b and low pH to transform into a membrane-bound, oligomeric channel. Requires trypsinization and reduction before it can be used in assays in vitro.Has proteolytic activity. After translocation into the eukaryotic host cytosol, inhibits neurotransmitter release by acting as a zinc endopeptidase that catalyzes the hydrolysis of the '180-Arg-|-Ile-181' bond in SNAP25. Hydrolyzes the '185-Arg-|-Ile-186' bond of mouse SNAP23, but not in human which has a different sequence. Recognizes the '146-Met--Asp-186' region of SNAP25. The reaction mechanism probably has a nucleophilic water held in place by Glu-213. Reduction of the interchain disulfide bond occurs in the host cytosol and probably prevents retrotranslocation into the synaptic vesicle.Responsible for host epithelial cell transcytosis, host nerve cell targeting and translocation of light chain (LC) into host cytosol. Composed of 3 subdomains; the translocation domain (TD), and N-terminus and C-terminus of the receptor-binding domain (RBD). The RBD is responsible for the adherence of the toxin to the cell surface. It probably simultaneously recognizes 2 coreceptors; polysialated gangliosides and either of the receptor proteins SV2A and SV2B in close proximity on host synaptic vesicles. The N-terminus of the TD wraps an extended belt around the perimeter of the light chain (LC), protecting Zn(2+) in the active site. The belt may also prevent premature LC dissociation from the translocation channel and protect toxin prior to translocation. The TD inserts into synaptic vesicle membrane to allow translocation into the host cytosol. Responsible for adherence of the toxin to the cell surface; HC alone prevents uptake of whole toxin by neural cells, and delays paralysis onset by 154%. Significantly decreases uptake and toxicity of whole BoNT/E, but also interferes with uptake of BoNT/C; binds GT1b in vitro. Binds to synaptic vesicle glycoproteins SV2A and SV2B which serve as coreceptors with gangliosides. Interaction with SV2 proteins requires SV2 glycosylation. HC alone significantly decreases uptake and toxicity of whole BoNT/E. HC is responsible for translocation of LC into the host cytosol; an intact disulfide bond between the 2 subunits is required for translocation, which is reduced upon contact with the host cytosol.","KM unchanged, kcat 10-fold increased.","KM unchanged, kcat 10-fold increased."
3761,3761,0,0,P02675-R45G,MKRMVSWSFHKLKTMKHLLLLLLCVFLVKSQGVNDNEEGFFSARGHRPLDKKREEAPSLRPAPPPISGGGYRARPAKAAATQKKVERKAPDAGGCLHADPDLGVLCPTGCQLQEALLQQERPIRNSVDELNNNVEAVSQTSSSSFQYMYLLKDLWQKRQKQVKDNENVVNEYSSELEKHQLYIDETVNSNIPTNLRVLRSILENLRSKIQKLESDVSAQMEYCRTPCTVSCNIPVVSGKECEEIIRKGGETSEMYLIQPDSSVKPYRVYCDMNTENGGWTVIQNRQDGSVDFGRKWDPYKQGFGNVATNTDGKNYCGLPGEYWLGNDKISQLTRMGPTELLIEMEDWKGDKVKAHYGGFTVQNEANKYQISVNKYRGTAGNALMDGASQLMGENRTMTIHNGMFFSTYDRDNDGWLTSDPRKQCSKEDGGGWWYNRCHAANPNGRYYWGGQYTWDMAKHGTDDGVVWMNWKGSWYSMRKMSMKIRPFFPQQ,,-1.0,MKRMVSWSFHKLKTMKHLLLLLLCVFLVKSQGVNDNEEGFFSARRHRPLDKKREEAPSLRPAPPPISGGGYRARPAKAAATQKKVERKAPDAGGCLHADPDLGVLCPTGCQLQEALLQQERPIRNSVDELNNNVEAVSQTSSSSFQYMYLLKDLWQKRQKQVKDNENVVNEYSSELEKHQLYIDETVNSNIPTNLRVLRSILENLRSKIQKLESDVSAQMEYCRTPCTVSCNIPVVSGKECEEIIRKGGETSEMYLIQPDSSVKPYRVYCDMNTENGGWTVIQNRQDGSVDFGRKWDPYKQGFGNVATNTDGKNYCGLPGEYWLGNDKISQLTRMGPTELLIEMEDWKGDKVKAHYGGFTVQNEANKYQISVNKYRGTAGNALMDGASQLMGENRTMTIHNGMFFSTYDRDNDGWLTSDPRKQCSKEDGGGWWYNRCHAANPNGRYYWGGQYTWDMAKHGTDDGVVWMNWKGSWYSMRKMSMKIRPFFPQQ,Fibrinogen beta chain [Cleaved into: Fibrinopeptide B; Fibrinogen beta chain],"Cleaved by the protease thrombin to yield monomers which, together with fibrinogen alpha (FGA) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the antibacterial immune response via both innate and T-cell mediated pathways.",Replaces glycine-45 of the fibrin beta-chain with arginine. This mutation does not affect the polymerization reaction by thrombin.,Replaces glycine-45 of the fibrin beta-chain with arginine. This mutation does not affect the polymerization reaction by thrombin.
3764,3764,0,0,P10599-A72K,MVKQIESKTAFQEALDAAGDKLVVVDFSATWCGPCKMIKPFFHSLSEKYSNVIFLEVDVDDCQDVASECEVKCMPTFQFFKKGQKVGEFSGANKEKLEATINELV,,-1.0,MVKQIESKTAFQEALDAAGDKLVVVDFSATWCGPCKMIKPFFHSLSEKYSNVIFLEVDVDDCQDVASECEVACMPTFQFFKKGQKVGEFSGANKEKLEATINELV,Thioredoxin,"Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. Plays a role in the reversible S-nitrosylation of cysteine residues in target proteins, and thereby contributes to the response to intracellular nitric oxide. Nitrosylates the active site Cys of CASP3 in response to nitric oxide (NO), and thereby inhibits caspase-3 activity. Induces the FOS/JUN AP-1 DNA-binding activity in ionizing radiation (IR) cells through its oxidation/reduction status and stimulates AP-1 transcriptional activity.ADF augments the expression of the interleukin-2 receptor TAC (IL2R/P55).",Strongly increased interaction with CASP3; when associated with A-70.,Strongly increased interaction with CASP3; when associated with A-70.
3767,3767,0,0,P57081-A147M,MAGSVGLALCGQTLVVRGGSRFLATSIASSDDDSLFIYDCSAAEKKSQENKGEDAPLDQGSGAILASTFSKSGSYFALTDDSKRLILFRTKPWQCLSVRTVARRCTALTFIASEEKVLVADKSGDVYSFSVLEPHGCGRLELGHLSMLLDVAVSPDDRFILTADRDEKIRVSWAAAPHSIESFCLGHTEFVSRISVVPTQPGLLLSSSGDGTLRLWEYRSGRQLHCCHLASLQELVDPQAPQKFAASRIAFWCQENCVALLCDGTPVVYIFQLDARRQQLVYRQQLAFQHQVWDVAFEETQGLWVLQDCQEAPLVLYRPVGDQWQSVPESTVLKKVSGVLRGNWAMLEGSAGADASFSSLYKATFDNVTSYLKKKEERLQQQLEKKQRRRSPPPGPDGHAKKMRPGEATLSC,,-1.0,MAGSVGLALCGQTLVVRGGSRFLATSIASSDDDSLFIYDCSAAEKKSQENKGEDAPLDQGSGAILASTFSKSGSYFALTDDSKRLILFRTKPWQCLSVRTVARRCTALTFIASEEKVLVADKSGDVYSFSVLEPHGCGRLELGHLSALLDVAVSPDDRFILTADRDEKIRVSWAAAPHSIESFCLGHTEFVSRISVVPTQPGLLLSSSGDGTLRLWEYRSGRQLHCCHLASLQELVDPQAPQKFAASRIAFWCQENCVALLCDGTPVVYIFQLDARRQQLVYRQQLAFQHQVWDVAFEETQGLWVLQDCQEAPLVLYRPVGDQWQSVPESTVLKKVSGVLRGNWAMLEGSAGADASFSSLYKATFDNVTSYLKKKEERLQQQLEKKQRRRSPPPGPDGHAKKMRPGEATLSC,tRNA,"Non-catalytic component of the METTL1-WDR4 methyltransferase complex required for the formation of N(7)-methylguanine in a subset of RNA species, such as tRNAs, mRNAs and microRNAs (miRNAs). In the METTL1-WDR4 methyltransferase complex, WDR4 acts as a scaffold for tRNA-binding. Required for the formation of N(7)-methylguanine at position 46 (m7G46) in a large subset of tRNAs that contain the 5'-RAGGU-3' motif within the variable loop. M7G46 interacts with C13-G22 in the D-loop to stabilize tRNA tertiary structure and protect tRNAs from decay. Also required for the formation of N(7)-methylguanine at internal sites in a subset of mRNAs. Also required for methylation of a specific subset of miRNAs, such as let-7. Independently of METTL1, also plays a role in genome stability: localizes at the DNA replication site and regulates endonucleolytic activities of FEN1.",Enhanced formation of N(7)-methylguanine in tRNAs.,Enhanced formation of N(7)-methylguanine in tRNAs.
3773,3773,0,0,Q13009-E912K,MGNAESQHVEHEFYGEKHASLGRKHTSRSLRLSHKTRRTRHASSGKVIHRNSEVSTRSSSTPSIPQSLAENGLEPFSQDGTLEDFGSPIWVDRVDMGLRPVSYTDSSVTPSVDSSIVLTAASVQSMPDTEESRLYGDDATYLAEGGRRQHSYTSNGPTFMETASFKKKRSKSADIWREDSLEFSLSDLSQEHLTSNEEILGSAEEKDCEEARGMETRASPRQLSTCQRANSLGDLYAQKNSGVTANGGPGSKFAGYCRNLVSDIPNLANHKMPPAAAEETPPYSNYNTLPCRKSHCLSEGATNPQISHSNSMQGRRAKTTQDVNAGEGSEFADSGIEGATTDTDLLSRRSNATNSSYSPTTGRAFVGSDSGSSSTGDAARQGVYENFRRELEMSTTNSESLEEAGSAHSDEQSSGTLSSPGQSDILLTAAQGTVRKAGALAVKNFLVHKKNKKVESATRRKWKHYWVSLKGCTLFFYESDGRSGIDHNSIPKHAVWVENSIVQAVPEHPKKDFVFCLSNSLGDAFLFQTTSQTELENWITAIHSACATAVARHHHKEDTLRLLKSEIKKLEQKIDMDEKMKKMGEMQLSSVTDSKKKKTILDQIFVWEQNLEQFQMDLFRFRCYLASLQGGELPNPKRLLAFASRPTKVAMGRLGIFSVSSFHALVAARTGETGVRRRTQAMSRSASKRRSRFSSLWGLDTTSKKKQGRPSINQVFGEGTEAVKKSLEGIFDDIVPDGKREKEVVLPNVHQHNPDCDIWVHEYFTPSWFCLPNNQPALTVVRPGDTARDTLELICKTHQLDHSAHYLRLKFLIENKMQLYVPQPEEDIYELLYKEIEICPKVTQSIHIEKSDTAADTYGFSLSSVEEDGIRRLYVNSVKETGLASKKGLKAGDEILEINNRAADALNSSMLKDFLSQPSLGLLVRTYPELEEGVELLESPPHRVDGPADLGESPLAFLTSNPGHSLCSEQGSSAETAPEETEGPDLESSDETDHSSKSTEQVAAFCRSLHEMNPSDQSPSPQDS,,-1.0,MGNAESQHVEHEFYGEKHASLGRKHTSRSLRLSHKTRRTRHASSGKVIHRNSEVSTRSSSTPSIPQSLAENGLEPFSQDGTLEDFGSPIWVDRVDMGLRPVSYTDSSVTPSVDSSIVLTAASVQSMPDTEESRLYGDDATYLAEGGRRQHSYTSNGPTFMETASFKKKRSKSADIWREDSLEFSLSDLSQEHLTSNEEILGSAEEKDCEEARGMETRASPRQLSTCQRANSLGDLYAQKNSGVTANGGPGSKFAGYCRNLVSDIPNLANHKMPPAAAEETPPYSNYNTLPCRKSHCLSEGATNPQISHSNSMQGRRAKTTQDVNAGEGSEFADSGIEGATTDTDLLSRRSNATNSSYSPTTGRAFVGSDSGSSSTGDAARQGVYENFRRELEMSTTNSESLEEAGSAHSDEQSSGTLSSPGQSDILLTAAQGTVRKAGALAVKNFLVHKKNKKVESATRRKWKHYWVSLKGCTLFFYESDGRSGIDHNSIPKHAVWVENSIVQAVPEHPKKDFVFCLSNSLGDAFLFQTTSQTELENWITAIHSACATAVARHHHKEDTLRLLKSEIKKLEQKIDMDEKMKKMGEMQLSSVTDSKKKKTILDQIFVWEQNLEQFQMDLFRFRCYLASLQGGELPNPKRLLAFASRPTKVAMGRLGIFSVSSFHALVAARTGETGVRRRTQAMSRSASKRRSRFSSLWGLDTTSKKKQGRPSINQVFGEGTEAVKKSLEGIFDDIVPDGKREKEVVLPNVHQHNPDCDIWVHEYFTPSWFCLPNNQPALTVVRPGDTARDTLELICKTHQLDHSAHYLRLKFLIENKMQLYVPQPEEDIYELLYKEIEICPKVTQSIHIEKSDTAADTYGFSLSSVEEDGIRRLYVNSVKETGLASKKGLKAGDEILEINNRAADALNSSMLEDFLSQPSLGLLVRTYPELEEGVELLESPPHRVDGPADLGESPLAFLTSNPGHSLCSEQGSSAETAPEETEGPDLESSDETDHSSKSTEQVAAFCRSLHEMNPSDQSPSPQDS,Rho guanine nucleotide exchange factor TIAM1,"Guanyl-nucleotide exchange factor that activates RHO-like proteins and connects extracellular signals to cytoskeletal activities. Activates RAC1, CDC42, and to a lesser extent RHOA and their downstream signaling to regulate processes like cell adhesion and cell migration.",Strongly increases affinity for SDC1.,Strongly increases affinity for SDC1.
3781,3781,0,0,P48432-R247K,MYNMMETELKPPGPQQASGGGGGGGNATAAATGGNQKNSPDRVKRPMNAFMVWSRGQRRKMAQENPKMHNSEISKRLGAEWKLLSETEKRPFIDEAKRLRALHMKEHPDYKYRPRRKTKTLMKKDKYTLPGGLLAPGGNSMASGVGVGAGLGGGLNQRMDSYAHMNGWSNGSYSMMQEQLGYPQHPGLNAHGAAQMQPMHRYVVSALQYNSMTSSQTYMNGSPTYSMSYSQQGTPGMALGSMGSVVKSEASSSPPVVTSSSHSRAPCQAGDLRDMISMYLPGAEVPEPAAPSRLHMAQHYQSGPVPGTAKYGTLPLSHM,,-1.0,MYNMMETELKPPGPQQASGGGGGGGNATAAATGGNQKNSPDRVKRPMNAFMVWSRGQRRKMAQENPKMHNSEISKRLGAEWKLLSETEKRPFIDEAKRLRALHMKEHPDYKYRPRRKTKTLMKKDKYTLPGGLLAPGGNSMASGVGVGAGLGGGLNQRMDSYAHMNGWSNGSYSMMQEQLGYPQHPGLNAHGAAQMQPMHRYVVSALQYNSMTSSQTYMNGSPTYSMSYSQQGTPGMALGSMGSVVRSEASSSPPVVTSSSHSRAPCQAGDLRDMISMYLPGAEVPEPAAPSRLHMAQHYQSGPVPGTAKYGTLPLSHM,Transcription factor SOX-2,"Transcription factor that forms a trimeric complex with POU5F1 (OCT3/4) on DNA and controls the expression of a number of genes involved in embryonic development such as YES1, FGF4, UTF1 and ZFP206. Binds to the proximal enhancer region of NANOG. Critical for early embryogenesis and for embryonic stem cell pluripotency. Downstream SRRT target that mediates the promotion of neural stem cell self-renewal. Keeps neural cells undifferentiated by counteracting the activity of proneural proteins and suppresses neuronal differentiation. May function as a switch in neuronal development.","Absence of desumoylation. Decreased FGF4 activation. Significant effect on nuclear localization. Substitution of the target lysine to arginine retained the sumoylation but considerably affected transcriptional potential or nuclear localization of Sox2. By contrast with the unmodified form, Sox2 fused to SUMO-1 significantly augmented transcription via the Fgf4 enhancer in the presence of Oct3/4. Furthermore, SUMO-1-conjugated Sox2 at the lysine 247 or at the carboxyl terminus increased the binding to the Fgf4 enhancer. These indicate that Sox2 sumoylation positively regulates its transcriptional role through enhancing the DNA binding.","Absence of desumoylation. Decreased FGF4 activation. Significant effect on nuclear localization. Substitution of the target lysine to arginine retained the sumoylation but considerably affected transcriptional potential or nuclear localization of Sox2. By contrast with the unmodified form, Sox2 fused to SUMO-1 significantly augmented transcription via the Fgf4 enhancer in the presence of Oct3/4. Furthermore, SUMO-1-conjugated Sox2 at the lysine 247 or at the carboxyl terminus increased the binding to the Fgf4 enhancer. These indicate that Sox2 sumoylation positively regulates its transcriptional role through enhancing the DNA binding."
3797,3797,0,0,Q9Z0S5-A102C,MSVAVETFGFFMSALGLLMLGLTLSNSYWRVSTVHGNVITTNTIFENLWYSCATDSLGVSNCWDFPSMLALSGYVQGCRALMITAILLGFLGLFLGMVGLRCTNVGNMDLSKKAKLLAIAGTLHILAGACGMVAISWYAVNITTDFFNPLYAGTKYELGPALYLGWSASLLSILGGICVFSTCCCSSKEEPATRAGLPYKPSTVVIPRATSDESDISFGKYGKNAYV,,-1.0,MSVAVETFGFFMSALGLLMLGLTLSNSYWRVSTVHGNVITTNTIFENLWYSCATDSLGVSNCWDFPSMLALSGYVQGCRALMITAILLGFLGLFLGMVGLRATNVGNMDLSKKAKLLAIAGTLHILAGACGMVAISWYAVNITTDFFNPLYAGTKYELGPALYLGWSASLLSILGGICVFSTCCCSSKEEPATRAGLPYKPSTVVIPRATSDESDISFGKYGKNAYV,Claudin-15,"Claudins function as major constituents of the tight junction complexes that regulate the permeability of epithelia. While some claudin family members function as impermeable barriers, others mediate the permeability to ions and small molecules. Often, several claudin family members are coexpressed and interact with each other, and this determines the overall permeability. CLDN15 forms tight junctions that mediate the paracellular transport of small monovalent cations along a concentration gradient, due to selective permeability for Na(+), Li(+) and K(+) ions, but selects against Cl(-) ions. Plays an important role in paracellular Na(+) transport in the intestine and in Na(+) homeostasis. Required for normal Na(+)-dependent intestinal nutrient uptake.",Enables palmitoylation; when associated with 183-A--A-185.,Enables palmitoylation; when associated with 183-A--A-185.
3804,3804,0,0,Q80U87-A413P,MPAVASVPKELYLSSSLKDLNKKTEVKPEKTSTKNYIHSAQKIFKTAEECRLDRDEERAYVLYMKYVAVYNLIKKRPDFKQQQDYYLSILGPANIKKAIEEAERLSESLKLRYEEAEVRKQLEEKDRREEEQLQQQKRQEMGREDSGAAAKRSVENLLDSKTKTQRINGEKSEGAAAAERGAITAKELYTMMMDKNTSLIIMDARKIQDYQHSCILDSLSVPEEAISPGVTASWIEANLSDDSKDTWKKRGSVDYVVLLDWFSSAKDLLLGTTLRSLKDALFKWESKTVLRHEPLVLEGGYENWLLCYPQFTTNAKVTPPPRSRAEEVSVSLDFTYPSLEEPVPSKLPTQMPPPPIETNEKALLVTDQDEKLRLSTQPALAGPGAAPRAEASPIIQPAPATKSVPQVDRTKKPSVKLPEDHRIKSENTDQSGRVLSDRSTKPVFPSPTTMLTDEEKARIHQETALLMEKNKQEKELWDKQQKEQKEKLRREEQERKAGKTQDADERDSTENQHKAKDGQEKKDSKQTKTEDRELSADGAQEATGTQRQSKSEHEASDAKVPVEGKRCPTSEAQKRPADVSPASVSGELNAGKAQREPLTRARSEEMGRIVPGLPLGWAKFLDPITGTFRYYHSPTNTVHMYPPEMAPSSAPPSTPPTHKVKPQVPAERDREPSKLKRSYSSPDITQALQEEEKRRPAVTPMVNRENKPPCYPKAEISRLSASQIRNLNPVFGGSGPALTGLRNLGNTCYMNSILQCLCNAPHLADYFNRNCYQDDINRSNLLGHKGEVAEEFGIIMKALWTGQYRYISPKDFKVTIGKINDQFAGSSQQDSQELLLFLMDGLHEDLNKADNRKRHKEENNEHLDDLQAAEHAWQKHKQLNESIIVALFQGQFKSTVQCLTCRRRSRTFEAFMYLSLPLASTSKCTLQDCLRLFSKEEKLTDNNRFYCSHCRARRDSLKKIEIWKLPPVLLVHLKRFSYDGRWKQKLQTSVDFPLENLDLSQYVIGPKNSLKKYNLFSVSNHYGG,,-1.0,MPAVASVPKELYLSSSLKDLNKKTEVKPEKTSTKNYIHSAQKIFKTAEECRLDRDEERAYVLYMKYVAVYNLIKKRPDFKQQQDYYLSILGPANIKKAIEEAERLSESLKLRYEEAEVRKQLEEKDRREEEQLQQQKRQEMGREDSGAAAKRSVENLLDSKTKTQRINGEKSEGAAAAERGAITAKELYTMMMDKNTSLIIMDARKIQDYQHSCILDSLSVPEEAISPGVTASWIEANLSDDSKDTWKKRGSVDYVVLLDWFSSAKDLLLGTTLRSLKDALFKWESKTVLRHEPLVLEGGYENWLLCYPQFTTNAKVTPPPRSRAEEVSVSLDFTYPSLEEPVPSKLPTQMPPPPIETNEKALLVTDQDEKLRLSTQPALAGPGAAPRAEASPIIQPAPATKSVPQVDRTKKASVKLPEDHRIKSENTDQSGRVLSDRSTKPVFPSPTTMLTDEEKARIHQETALLMEKNKQEKELWDKQQKEQKEKLRREEQERKAGKTQDADERDSTENQHKAKDGQEKKDSKQTKTEDRELSADGAQEATGTQRQSKSEHEASDAKVPVEGKRCPTSEAQKRPADVSPASVSGELNAGKAQREPLTRARSEEMGRIVPGLPLGWAKFLDPITGTFRYYHSPTNTVHMYPPEMAPSSAPPSTPPTHKVKPQVPAERDREPSKLKRSYSSPDITQALQEEEKRRPAVTPMVNRENKPPCYPKAEISRLSASQIRNLNPVFGGSGPALTGLRNLGNTCYMNSILQCLCNAPHLADYFNRNCYQDDINRSNLLGHKGEVAEEFGIIMKALWTGQYRYISPKDFKVTIGKINDQFAGSSQQDSQELLLFLMDGLHEDLNKADNRKRHKEENNEHLDDLQAAEHAWQKHKQLNESIIVALFQGQFKSTVQCLTCRRRSRTFEAFMYLSLPLASTSKCTLQDCLRLFSKEEKLTDNNRFYCSHCRARRDSLKKIEIWKLPPVLLVHLKRFSYDGRWKQKLQTSVDFPLENLDLSQYVIGPKNSLKKYNLFSVSNHYGG,Ubiquitin carboxyl-terminal hydrolase 8,"Hydrolase that can remove conjugated ubiquitin from proteins and therefore plays an important regulatory role at the level of protein turnover by preventing degradation. Converts both 'Lys-48' an 'Lys-63'-linked ubiquitin chains. Catalytic activity is enhanced in the M phase. Involved in cell proliferation. Required to enter into S phase in response to serum stimulation. May regulate T-cell anergy mediated by RNF128 via the formation of a complex containing RNF128 and OTUB1. Probably regulates the stability of STAM2 and RASGRF1. Regulates endosomal ubiquitin dynamics, cargo sorting, membrane traffic at early endosomes, and maintenance of ESCRT-0 stability. The level of protein ubiquitination on endosomes is essential for maintaining the morphology of the organelle. Deubiquitinates EPS15 and controls tyrosine kinase stability. Removes conjugated ubiquitin from EGFR thus regulating EGFR degradation and downstream MAPK signaling. Involved in acrosome biogenesis through interaction with the spermatid ESCRT-0 complex and microtubules. Deubiquitinates BIRC6/bruce and KIF23/MKLP1. Deubiquitinates BACE1 which inhibits BACE1 lysosomal degradation and modulates BACE-mediated APP cleavage and amyloid-beta formation.",Enables interaction with the SH3 domain of STAM2.,Enables interaction with the SH3 domain of STAM2.
3811,3811,0,0,P24530-P17L,MQPPPSLCGRALVALVLACGLSRIWGEERGFPPDRATPLLQTAEIMTPPTKTLWPKGSNASLARSLAPAEVPKGDRTAGSPPRTISPPPCQGPIEIKETFKYINTVVSCLVFVLGIIGNSTLLRIIYKNKCMRNGPNILIASLALGDLLHIVIDIPINVYKLLAEDWPFGAEMCKLVPFIQKASVGITVLSLCALSIDRYRAVASWSRIKGIGVPKWTAVEIVLIWVVSVVLAVPEAIGFDIITMDYKGSYLRICLLHPVQKTAFMQFYKTAKDWWLFSFYFCLPLAITAFFYTLMTCEMLRKKSGMQIALNDHLKQRREVAKTVFCLVLVFALCWLPLHLSRILKLTLYNQNDPNRCELLSFLLVLDYIGINMASLNSCINPIALYLVSKRFKNCFKSCLCCWCQSFEEKQSLEEKQSCLKFKANDHGYDNFRSSNKYSSS,,-1.0,MQPPPSLCGRALVALVPACGLSRIWGEERGFPPDRATPLLQTAEIMTPPTKTLWPKGSNASLARSLAPAEVPKGDRTAGSPPRTISPPPCQGPIEIKETFKYINTVVSCLVFVLGIIGNSTLLRIIYKNKCMRNGPNILIASLALGDLLHIVIDIPINVYKLLAEDWPFGAEMCKLVPFIQKASVGITVLSLCALSIDRYRAVASWSRIKGIGVPKWTAVEIVLIWVVSVVLAVPEAIGFDIITMDYKGSYLRICLLHPVQKTAFMQFYKTAKDWWLFSFYFCLPLAITAFFYTLMTCEMLRKKSGMQIALNDHLKQRREVAKTVFCLVLVFALCWLPLHLSRILKLTLYNQNDPNRCELLSFLLVLDYIGINMASLNSCINPIALYLVSKRFKNCFKSCLCCWCQSFEEKQSLEEKQSCLKFKANDHGYDNFRSSNKYSSS,Endothelin receptor type B,"Non-specific receptor for endothelin 1, 2, and 3. Mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system.",New probable healthy variant found in patients without Waardenburg syndrome 2; gain of cell membrane location; original cytoplasmic location. The mutation in EDNRB enhances the subcellular localization of the receptor and activates a functional downstream signaling pathway.,New probable healthy variant found in patients without Waardenburg syndrome 2; gain of cell membrane location; original cytoplasmic location. The mutation in EDNRB enhances the subcellular localization of the receptor and activates a functional downstream signaling pathway.
3817,3817,0,0,Q9UMX1-R147Y,MAELRPSGAPGPTAPPAPGPTAPPAFASLFPPGLHAIYGECRRLYPDQPNPLQVTAIVKYWLGGPDPLDYVSMYRNVGSPSANIPEHWHYISFGLSDLYGDNRVHEFTGTDGPSGFGFELTFRLKRETGESAPPTWPAELMQGLARYVFQSENTFCSGDHVSWHSPLDNSESRIQHMLLTEDPQMQPVQTPFGVVTFLQIVGVCTEELHSAQQWNGQGILELLRTVPIAGGPWLITDMRRGETIFEIDPHLQERVDKGIETDGSNLSGVSAKCAWDDLSRPPEDDEDSRSICIGTQPRRLSGKDTEQIRETLRRGLEINSKPVLPPINPQRQNGLAHDRAPSRKDSLESDSSTAIIPHELIRTRQLESVHLKFNQESGALIPLCLRGRLLHGRHFTYKSITGDMAITFVSTGVEGAFATEEHPYAAHGPWLQILLTEEFVEKMLEDLEDLTSPEEFKLPKEYSWPEKKLKVSILPDVVFDSPLH,,-1.0,MAELRPSGAPGPTAPPAPGPTAPPAFASLFPPGLHAIYGECRRLYPDQPNPLQVTAIVKYWLGGPDPLDYVSMYRNVGSPSANIPEHWHYISFGLSDLYGDNRVHEFTGTDGPSGFGFELTFRLKRETGESAPPTWPAELMQGLARRVFQSENTFCSGDHVSWHSPLDNSESRIQHMLLTEDPQMQPVQTPFGVVTFLQIVGVCTEELHSAQQWNGQGILELLRTVPIAGGPWLITDMRRGETIFEIDPHLQERVDKGIETDGSNLSGVSAKCAWDDLSRPPEDDEDSRSICIGTQPRRLSGKDTEQIRETLRRGLEINSKPVLPPINPQRQNGLAHDRAPSRKDSLESDSSTAIIPHELIRTRQLESVHLKFNQESGALIPLCLRGRLLHGRHFTYKSITGDMAITFVSTGVEGAFATEEHPYAAHGPWLQILLTEEFVEKMLEDLEDLTSPEEFKLPKEYSWPEKKLKVSILPDVVFDSPLH,Suppressor of fused homolog,"Negative regulator in the hedgehog/smoothened signaling pathway. Down-regulates GLI1-mediated transactivation of target genes. Down-regulates GLI2-mediated transactivation of target genes. Part of a corepressor complex that acts on DNA-bound GLI1. May also act by linking GLI1 to BTRC and thereby targeting GLI1 to degradation by the proteasome. Sequesters GLI1, GLI2 and GLI3 in the cytoplasm, this effect is overcome by binding of STK36 to both SUFU and a GLI protein. Negative regulator of beta-catenin signaling. Regulates the formation of either the repressor form (GLI3R) or the activator form (GLI3A) of the full-length form of GLI3 (GLI3FL). GLI3FL is complexed with SUFU in the cytoplasm and is maintained in a neutral state. Without the Hh signal, the SUFU-GLI3 complex is recruited to cilia, leading to the efficient processing of GLI3FL into GLI3R. When Hh signaling is initiated, SUFU dissociates from GLI3FL and the latter translocates to the nucleus, where it is phosphorylated, destabilized, and converted to a transcriptional activator (GLI3A). Required for normal embryonic development. Required for the proper formation of hair follicles and the control of epidermal differentiation.",Enhances interaction with GLI1 and GLI2. Enables interaction with GLI1 and GLI2; when associated with R-159 and R-380.,Enhances interaction with GLI1 and GLI2. Enables interaction with GLI1 and GLI2; when associated with R-159 and R-380.
3825,3825,0,0,P02760-T137K,MRSLGALLLLLSACLAVSAGPVPTPPDNIQVQENFNISRIYGKWYNLAIGSTCPWLKKIMDRMTVSTLVLGEGATEAEISMTSTRWRKGVCEETSGAYEKTDTDGKFLYHKSKWNITMESYVVHTNYDEYAIFLTKKFSRHHGPTITAKLYGRAPQLRETLLQDFRVVAQGVGIPEDSIFTMADRGECVPGEQEPEPILIPRVRRAVLPQEEEGSGGGQLVTEVTKKEDSCQLGYSAGPCMGMTSRYFYNGTSMACETFQYGGCMGNGNNFVTEKECLQTCRTVAACNLPIVRGPCRAFIQLWAFDAVKGKCVLFPYGGCQGNGNKFYSEKECREYCGVPGDGDEELLRFSN,,-1.0,MRSLGALLLLLSACLAVSAGPVPTPPDNIQVQENFNISRIYGKWYNLAIGSTCPWLKKIMDRMTVSTLVLGEGATEAEISMTSTRWRKGVCEETSGAYEKTDTDGKFLYHKSKWNITMESYVVHTNYDEYAIFLTKTFSRHHGPTITAKLYGRAPQLRETLLQDFRVVAQGVGIPEDSIFTMADRGECVPGEQEPEPILIPRVRRAVLPQEEEGSGGGQLVTEVTKKEDSCQLGYSAGPCMGMTSRYFYNGTSMACETFQYGGCMGNGNNFVTEKECLQTCRTVAACNLPIVRGPCRAFIQLWAFDAVKGKCVLFPYGGCQGNGNKFYSEKECREYCGVPGDGDEELLRFSN,Protein AMBP,"Antioxidant and tissue repair protein with reductase, heme-binding and radical-scavenging activities. Removes and protects against harmful oxidants and repairs macromolecules in intravascular and extravascular spaces and in intracellular compartments. Intravascularly, plays a regulatory role in red cell homeostasis by preventing heme- and reactive oxygen species-induced cell damage. Binds and degrades free heme to protect fetal and adult red blood cells from hemolysis. Reduces extracellular methemoglobin, a Fe3+ (ferric) form of hemoglobin that cannot bind oxygen, back to the Fe2+ (ferrous) form deoxyhemoglobin, which has oxygen-carrying potential. Upon acute inflammation, inhibits oxidation of low-density lipoprotein particles by MPO and limits vascular damage. Extravascularly, protects from oxidation products formed on extracellular matrix structures and cell membranes. Catalyzes the reduction of carbonyl groups on oxidized collagen fibers and preserves cellular and extracellular matrix ultrastructures. Importantly, counteracts the oxidative damage at blood-placenta interface, preventing leakage of free fetal hemoglobin into the maternal circulation. Intracellularly, has a role in maintaining mitochondrial redox homeostasis. Bound to complex I of the respiratory chain of mitochondria, may scavenge free radicals and preserve mitochondrial ATP synthesis. Protects renal tubule epithelial cells from heme-induced oxidative damage to mitochondria. Reduces cytochrome c from Fe3+ (ferric) to the Fe2+ (ferrous) state through formation of superoxide anion radicals in the presence of ascorbate or NADH/NADPH electron donor cofactors, ascorbate being the preferred cofactor. Has a chaperone role in facilitating the correct folding of bikunin in the endoplasmic reticulum compartment.Kunitz-type serine protease inhibitor and structural component of extracellular matrix with a role in extracellular space remodeling and cell adhesion. Among others, has antiprotease activity toward kallikrein, a protease involved in airway inflammation; inhibits GZMK/granzyme, a granule-stored serine protease involved in NK and T cell cytotoxic responses; and inhibits PLG/plasmin, a protease required for activation of matrix metalloproteinases. As part of I-alpha-I complex, provides for the heavy chains to be transferred from I-alpha-I complex to hyaluronan in the presence of TNFAIP6, in a dynamic process that releases free bikunin and remodels extracellular matrix proteoglycan structures. Free bikunin, but not its heavy chain-bound form, acts as potent protease inhibitor in airway secretions. Part of hyaluronan-rich extracellular matrix that surrounds oocyte during cumulus oophorus expansion, an indispensable process for proper ovulation. Also inhibits calcium oxalate crystallization.Kunitz-type serine protease inhibitor. Has high catalytic efficiency for F10/blood coagulation factor Xa and may act as an anticoagulant by inhibiting prothrombin activation. Inhibits trypsin and mast cell CMA1/chymase and tryptase proteases.",Enhances the reductase activity toward cytochrome c in the presence of NADPH; when associated with T-111 and T-149. Enhances the reductase activity toward oxidized collagen; when associated with T-111 and T-149.,Enhances the reductase activity toward cytochrome c in the presence of NADPH; when associated with T-111 and T-149. Enhances the reductase activity toward oxidized collagen; when associated with T-111 and T-149.
3826,3826,0,0,F2XG53-A452D,MKHINDYFWAKKTEENSRLLWLPLTQHLEDTKNIAGLLWEHWLSEGQKVLIENSINVKSNIENQGKRLAQFLGAVHDIGKATPAFQTQKGYANSVDLDIQLLEKLERAGFSGISSLQLASPKKSHHSIAGQYLLSHYGVDEDIATIIGGHHGRPVDDLDGLNSQKSYPSNYYQDEKKDSLVYQKWKSNQEAFLNWALTETGFNSVSQLPKIKQPAQVILSGLLIMSDWIASNEHFFPLLSLDETDVKNKSQRIETGFKKWKKSNLWQPETFVDLVTLYQERFGFSPRNFQLILSQTIEKTTNPGIVILEAPMGIGKTEAALAVSEQLSSKKGCSGLFFGLPTQATSNGIFKRIEQWTENIKGNNSDHFSIQLVHGKAALNTDFIELLKGNTINMDDSENGSIFVNEWFSGRKTSALDDFVVGTVDQFLMVALKQKHLALRHLGFSKKVIVIDEVHAYDAYMSQYLLEAIRWMGAYGVPVIILSATLPAQQREKLIKSYMAGMGVKWRDIENIDQIKIDAYPLITYNDGPDIHQVKMFEKQEQKNIYIHRLPEEQLFDIVKEGLDNGGVVGIIVNTVRKSQELARNFSDIFGDDMVDLLHSNFIATERIRKEKDLLQEIGKKAIRPPKKIIIGTQVLEQSLDIDFDVLISDLAPMDLLIQRIGRLHRHKIKRPQKHEVARFYVLGTFEEFDFDEGTRLVYGDYLLARTQYFLPDKIRLPDDISPLVQKVYNSDLTITFPKPELHKKYLDAKIEHDDKIKNKETKAKSYRIANPVLKKSRVRTNSLIGWLKNLHPNDSEEKAYAQVRDIEDTVEVIALKKISDGYGLFIENKDISQNITDPIIAKKVAQNTLRLPMSLSKAYNIDQTINELERYNNSHLSQWQNSSWLKGSLGIIFDKNNEFILNGFKLLYDEKYGVTIERLDKNESV,,-1.0,MKHINDYFWAKKTEENSRLLWLPLTQHLEDTKNIAGLLWEHWLSEGQKVLIENSINVKSNIENQGKRLAQFLGAVHDIGKATPAFQTQKGYANSVDLDIQLLEKLERAGFSGISSLQLASPKKSHHSIAGQYLLSHYGVDEDIATIIGGHHGRPVDDLDGLNSQKSYPSNYYQDEKKDSLVYQKWKSNQEAFLNWALTETGFNSVSQLPKIKQPAQVILSGLLIMSDWIASNEHFFPLLSLDETDVKNKSQRIETGFKKWKKSNLWQPETFVDLVTLYQERFGFSPRNFQLILSQTIEKTTNPGIVILEAPMGIGKTEAALAVSEQLSSKKGCSGLFFGLPTQATSNGIFKRIEQWTENIKGNNSDHFSIQLVHGKAALNTDFIELLKGNTINMDDSENGSIFVNEWFSGRKTSALDDFVVGTVDQFLMVALKQKHLALRHLGFSKKVIVIAEVHAYDAYMSQYLLEAIRWMGAYGVPVIILSATLPAQQREKLIKSYMAGMGVKWRDIENIDQIKIDAYPLITYNDGPDIHQVKMFEKQEQKNIYIHRLPEEQLFDIVKEGLDNGGVVGIIVNTVRKSQELARNFSDIFGDDMVDLLHSNFIATERIRKEKDLLQEIGKKAIRPPKKIIIGTQVLEQSLDIDFDVLISDLAPMDLLIQRIGRLHRHKIKRPQKHEVARFYVLGTFEEFDFDEGTRLVYGDYLLARTQYFLPDKIRLPDDISPLVQKVYNSDLTITFPKPELHKKYLDAKIEHDDKIKNKETKAKSYRIANPVLKKSRVRTNSLIGWLKNLHPNDSEEKAYAQVRDIEDTVEVIALKKISDGYGLFIENKDISQNITDPIIAKKVAQNTLRLPMSLSKAYNIDQTINELERYNNSHLSQWQNSSWLKGSLGIIFDKNNEFILNGFKLLYDEKYGVTIERLDKNESV,CRISPR-associated nuclease/helicase Cas3,"CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Cas3 plus Cascade participate in CRISPR interference, the third stage of CRISPR immunity. Functions as a ssDNA-dependent ATPase; dsDNA, ssRNA do not stimulate ATPase activity, while other nucleotides (aside from dATP) are not hydrolyzed. Functions as a ssDNA nuclease; activity does not require ATP. Functions as an ATP-dependent helicase; helicase activity requires hydrolysable ATP. Unwinds both DNA/DNA hybrids and RNA/DNA hybrids, moving mostly in a 3' to 5' direction.","Increase of ssDNA-dependent ATPase, increase of helicase activity. The mutation in the Cas3 protein of the Streptococcus thermophilus CRISPR4 system has been found to affect the ATPase activity of Cas3. This mutation results in an increase in the ATPase activity of Cas3, which is coupled to the unwinding of DNA/DNA and RNA/DNA duplexes.","Increase of ssDNA-dependent ATPase, increase of helicase activity. The mutation in the Cas3 protein of the Streptococcus thermophilus CRISPR4 system has been found to affect the ATPase activity of Cas3. This mutation results in an increase in the ATPase activity of Cas3, which is coupled to the unwinding of DNA/DNA and RNA/DNA duplexes."
3840,3840,0,0,Q92692-A81N,MARAAALLPSRSPPTPLLWPLLLLLLLETGAQDVRVQVLPEVRGQLGGTVELPCHLLPPVPGLYISLVTWQRPDAPANHQNVAAFHPKMGPSFPSPKPGSERLSFVSAKQSTGQDTEAELQDATLALHGLTVEDEGNYTCEFATFPKGSVRGMTWLRVIAKPKNQAEAQKVTFSQDPTTVALCISKEGRPPARISWLSSLDWEAKETQVSGTLAGTVTVTSRFTLVPSGRADGVTVTCKVEHESFEEPALIPVTLSVRYPPEVSISGYDDNWYLGRTDATLSCDVRSNPEPTGYDWSTTSGTFPTSAVAQGSQLVIHAVDSLFNTTFVCTVTNAVGMGRAEQVIFVRETPNTAGAGATGGIIGGIIAAIIATAVAATGILICRQQRKEQTLQGAEEDEDLEGPPSYKPPTPKAKLEAQEMPSQLFTLGASEHSPLKTPYFDAGASCTEQEMPRYHELPTLEERSGPLHPGATSLGSPIPVPPGPPAVEDVSLDLEDEEGEEEEEYLDKINPIYDALSYSSPSDSYQGKGFVMSRAMYV,,-1.0,MARAAALLPSRSPPTPLLWPLLLLLLLETGAQDVRVQVLPEVRGQLGGTVELPCHLLPPVPGLYISLVTWQRPDAPANHQAVAAFHPKMGPSFPSPKPGSERLSFVSAKQSTGQDTEAELQDATLALHGLTVEDEGNYTCEFATFPKGSVRGMTWLRVIAKPKNQAEAQKVTFSQDPTTVALCISKEGRPPARISWLSSLDWEAKETQVSGTLAGTVTVTSRFTLVPSGRADGVTVTCKVEHESFEEPALIPVTLSVRYPPEVSISGYDDNWYLGRTDATLSCDVRSNPEPTGYDWSTTSGTFPTSAVAQGSQLVIHAVDSLFNTTFVCTVTNAVGMGRAEQVIFVRETPNTAGAGATGGIIGGIIAAIIATAVAATGILICRQQRKEQTLQGAEEDEDLEGPPSYKPPTPKAKLEAQEMPSQLFTLGASEHSPLKTPYFDAGASCTEQEMPRYHELPTLEERSGPLHPGATSLGSPIPVPPGPPAVEDVSLDLEDEEGEEEEEYLDKINPIYDALSYSSPSDSYQGKGFVMSRAMYV,Nectin-2,"Modulator of T-cell signaling. Can be either a costimulator of T-cell function, or a coinhibitor, depending on the receptor it binds to. Upon binding to CD226, stimulates T-cell proliferation and cytokine production, including that of IL2, IL5, IL10, IL13, and IFNG. Upon interaction with PVRIG, inhibits T-cell proliferation. These interactions are competitive. Probable cell adhesion protein.(Microbial infection) Acts as a receptor for herpes simplex virus 1 (HHV-1) mutant Rid1, herpes simplex virus 1 (HHV-2) and pseudorabies virus (PRV).",Increases homodimerization. The mutation in nectin-2 affects the binding affinities associated with homophilic and heterophilic interactions within the nectin family.,Increases homodimerization. The mutation in nectin-2 affects the binding affinities associated with homophilic and heterophilic interactions within the nectin family.
3846,3846,0,0,Q9EYX5-S244C,MEAIKGSDVNVPDAVFAWLLDGRGGVKPLEDNDVIDSQHPCWLHLNYTHPDSARWLASTPLLPNNVRDALAGESSRPRVSRMGEGTLITLRCINGSTDERPDQLVAMRLYMDERFIVSTRQRKVLALDDVVSDLQEGTGPVDCGGWLVDVCDALTDHASEFIEELHDKIIDLEDNLLDQQIPPRGFLALLRKQLIVMRRYMAPQRDVYARLASERLPWMSDDHRRRMQDIADRLGRGLDEIDACIARTGIMADEIAQVMQESLARRTYTMSLMAMVFLPSTFLTGLFGVNLGGIPGGGWRFGFSLFCILLVVLIGGVTLWLHRSKWL,,-1.0,MEAIKGSDVNVPDAVFAWLLDGRGGVKPLEDNDVIDSQHPCWLHLNYTHPDSARWLASTPLLPNNVRDALAGESSRPRVSRMGEGTLITLRCINGSTDERPDQLVAMRLYMDERFIVSTRQRKVLALDDVVSDLQEGTGPVDCGGWLVDVCDALTDHASEFIEELHDKIIDLEDNLLDQQIPPRGFLALLRKQLIVMRRYMAPQRDVYARLASERLPWMSDDHRRRMQDIADRLGRGLDEIDASIARTGIMADEIAQVMQESLARRTYTMSLMAMVFLPSTFLTGLFGVNLGGIPGGGWRFGFSLFCILLVVLIGGVTLWLHRSKWL,Zinc transport protein ZntB,"Zinc transporter. Acts as a Zn(2+):proton symporter, which likely mediates zinc ion uptake (By similarity).","Contains three zinc binding sites, but the third site shows an increased affinity for zinc.","Contains three zinc binding sites, but the third site shows an increased affinity for zinc."
3857,3857,0,0,P0DOE4-S39A,MENTSITIEFSSKFWPYFTLIHMITTIISLLIIISIMIAILNKLCEYNVFHNKTFELPRARVNT,,-1.0,MENTSITIEFSSKFWPYFTLIHMITTIISLLIIISIMISILNKLCEYNVFHNKTFELPRARVNT,Small hydrophobic protein,"Viroporin that forms a homopentameric ion channel displaying low ion selectivity. May play a role in virus morphogenesis and pathogenicity at various stages of the viral life cycle. Accumulates at the membrane of the Golgi apparatus in infected cells and may facilitate virus release by modifying the secretory pathway. May enhance host membrane permeability and disrupt cellular ion homeostasis, which can be sensed as damage-associated molecular patterns/danger signals, triggering NLRP3 inflammasome activation and inflammatory immune response. Also inhibits host TNFA-mediated signaling pathway and may delay apoptosis, allowing time for the virus to replicate.",Enhances the effect of small-molecule inhibitor. The mutation in the SH protein has not been found to have any significant effect on channel activity.,Enhances the effect of small-molecule inhibitor. The mutation in the SH protein has not been found to have any significant effect on channel activity.
3867,3867,0,0,Q9HU77-Q235E,MSAIFAERALLPEGWARNVRFEISADGVLAEIRPDANADGAERLGGAVLPGMPNLHSHAFQRAMAGLAEVAGNPNDSFWTWRELMYRMVARLSPEQIEVIACQLYIEMLKAGYTAVAEFHYVHHDLDGRSYADPAELSLRISRAASAAGIGLTLLPVLYSHAGFGGQPASEGQRRFINGSEAYLELLQRLRAPLEAAGHSLGLCFHSLRAVTPQQIATVLAAGHDDLPVHIHIAEQQKEVDDCQAWSGRRPLQWLYENVAVDQRWCLVHATHADPAEVAAMARSGAVAGLCLSTEANLGDGIFPATDFLAQGGRLGIGSDSHVSLSVVEELRWLEYGQRLRDRKRNRLYRDDQPMIGRTLYDAALAGGAQALGQPIGSLAVGRRADLLVLDGNDPYLASAEGDALLNRWLFAGGDRQVRDVMVAGRWVVRDGRHAGEERSARAFVQVLGELLD,,-1.0,MSAIFAERALLPEGWARNVRFEISADGVLAEIRPDANADGAERLGGAVLPGMPNLHSHAFQRAMAGLAEVAGNPNDSFWTWRELMYRMVARLSPEQIEVIACQLYIEMLKAGYTAVAEFHYVHHDLDGRSYADPAELSLRISRAASAAGIGLTLLPVLYSHAGFGGQPASEGQRRFINGSEAYLELLQRLRAPLEAAGHSLGLCFHSLRAVTPQQIATVLAAGHDDLPVHIHIAQQQKEVDDCQAWSGRRPLQWLYENVAVDQRWCLVHATHADPAEVAAMARSGAVAGLCLSTEANLGDGIFPATDFLAQGGRLGIGSDSHVSLSVVEELRWLEYGQRLRDRKRNRLYRDDQPMIGRTLYDAALAGGAQALGQPIGSLAVGRRADLLVLDGNDPYLASAEGDALLNRWLFAGGDRQVRDVMVAGRWVVRDGRHAGEERSARAFVQVLGELLD,Formimidoylglutamate deiminase,Catalyzes the hydrolysis of N-formimino-L-glutamate to N-formyl-L-glutamate and ammonia.,Increases catalytic activity by 4 orders of magnitude.,Increases catalytic activity by 4 orders of magnitude.
3873,3873,0,0,P04637-R194L,MEEPQSDPSVEPPLSQETFSDLWKLLPENNVLSPLPSQAMDDLMLSPDDIEQWFTEDPGPDEAPRMPEAAPPVAPAPAAPTPAAPAPAPSWPLSSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNTSSSPQPKKKPLDGEYFTLQIRGRERFEMFRELNEALELKDAQAGKEPGGSRAHSSHLKSKKGQSTSRHKKLMFKTEGPDSD,,-1.0,MEEPQSDPSVEPPLSQETFSDLWKLLPENNVLSPLPSQAMDDLMLSPDDIEQWFTEDPGPDEAPRMPEAAPPVAPAPAAPTPAAPAPAPSWPLSSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHHERCSDSDGLAPPQHRIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNTSSSPQPKKKPLDGEYFTLQIRGRERFEMFRELNEALELKDAQAGKEPGGSRAHSSHLKSKKGQSTSRHKKLMFKTEGPDSD,Cellular tumor antigen p53,"Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type. Involved in cell cycle regulation as a trans-activator that acts to negatively regulate cell division by controlling a set of genes required for this process. One of the activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be mediated either by stimulation of BAX and FAS antigen expression, or by repression of Bcl-2 expression. Its pro-apoptotic activity is activated via its interaction with PPP1R13B/ASPP1 or TP53BP2/ASPP2. However, this activity is inhibited when the interaction with PPP1R13B/ASPP1 or TP53BP2/ASPP2 is displaced by PPP1R13L/iASPP. In cooperation with mitochondrial PPIF is involved in activating oxidative stress-induced necrosis; the function is largely independent of transcription. Induces the transcription of long intergenic non-coding RNA p21 (lincRNA-p21) and lincRNA-Mkln1. LincRNA-p21 participates in TP53-dependent transcriptional repression leading to apoptosis and seems to have an effect on cell-cycle regulation. Implicated in Notch signaling cross-over. Prevents CDK7 kinase activity when associated to CAK complex in response to DNA damage, thus stopping cell cycle progression. Isoform 2 enhances the transactivation activity of isoform 1 from some but not all TP53-inducible promoters. Isoform 4 suppresses transactivation activity and impairs growth suppression mediated by isoform 1. Isoform 7 inhibits isoform 1-mediated apoptosis. Regulates the circadian clock by repressing CLOCK-BMAL1-mediated transcriptional activation of PER2.","Missense mutation at codon 194, where arginine (R) is replaced by leucine (L).","Missense mutation at codon 194, where arginine (R) is replaced by leucine (L)."
3898,3898,0,0,A0A0H2XCS3-S13C,MSTATNPLDLDVCAREPIHIPGLIQPYGVLLVIDPADGRIVQASTTAADLLGVPMAALLGMPYTQVLTLPEAQPFAVDDQPQHLMHAEVRFPQRATPPASAWVAAWHLYPQQWLVEMEPRDARLLDVTLREAMPLLRSVERDPGIAEAAVRVAKGLRSLIGFDRVMIYRFDEEWNGDIIAEARKPELEAYLGLHYPASDIPAQARALYLRNRVRQIADVGYQPSPIQPTVHPQLGTPVDLSDVSLRSVSPVHLEYLANMGVTATLVASIVVNDALWGLISCHHYSPHFTNHAMRDVTDAVARTLAGRIGALQAVARARLESVLLTVREKLITDFNDAEHMTVELLDDMAPDLMDVVDADGVAIFHGNDISRHGTTPDVAALRRIRDHIESEHHEALREDAVGALHVDAIGEVFPELADLAPLAAGFIFVPLMPQSRSALLWTRREQIQQIKWAGNPQLAKLEDIPNSRLSPRKSFDLWQQTVRGRARRWSPLHLESARSLRVLIELMERKRFQQDFTLLEASLSRLRDGVAIIERGTANAAHRLLFVNTAFADVCGSDVAELIGRELQTLYASDAPRANVELLQDALRNGRAAYVTLPLQVSDGAPVYRQFHLEPLPSPSGVTAHWLLQLRDPE,,-1.0,MSTATNPLDLDVSAREPIHIPGLIQPYGVLLVIDPADGRIVQASTTAADLLGVPMAALLGMPYTQVLTLPEAQPFAVDDQPQHLMHAEVRFPQRATPPASAWVAAWHLYPQQWLVEMEPRDARLLDVTLREAMPLLRSVERDPGIAEAAVRVAKGLRSLIGFDRVMIYRFDEEWNGDIIAEARKPELEAYLGLHYPASDIPAQARALYLRNRVRQIADVGYQPSPIQPTVHPQLGTPVDLSDVSLRSVSPVHLEYLANMGVTATLVASIVVNDALWGLISCHHYSPHFTNHAMRDVTDAVARTLAGRIGALQAVARARLESVLLTVREKLITDFNDAEHMTVELLDDMAPDLMDVVDADGVAIFHGNDISRHGTTPDVAALRRIRDHIESEHHEALREDAVGALHVDAIGEVFPELADLAPLAAGFIFVPLMPQSRSALLWTRREQIQQIKWAGNPQLAKLEDIPNSRLSPRKSFDLWQQTVRGRARRWSPLHLESARSLRVLIELMERKRFQQDFTLLEASLSRLRDGVAIIERGTANAAHRLLFVNTAFADVCGSDVAELIGRELQTLYASDAPRANVELLQDALRNGRAAYVTLPLQVSDGAPVYRQFHLEPLPSPSGVTAHWLLQLRDPE,Bacteriophytochrome,"Photoreceptor which exists in two forms that are reversibly interconvertible by light: far-red light (733 nm) converts protein to the red-absorbing (Pr) form, while red light (630 nm) partly converts the protein to the far-red-absorbing (Pfr) form. Regulates virulence of X.campestris pv. campestris on its host plants, perhaps by fine-tuning expression to ambient light levels and/or spatial cues. The Pr form may sense light and partially inhibit virulence; in the dark (Pfr form) biofilm and xanathan production rise and bacteria are more virulent. Strains overexpressing this protein have significantly decreased amounts of extracellular beta-1,4-endoglucanase, produce less xanthin and have decreased transcription of genes involved in virulence such as endoglucanases, type 2 secretion systems, xanthan production and flagellar-dependent motility.","Loss of photo-inducible Pr-Pfr conversion; protein still binds pigment. No difference in growth in host, decreased callose deposits, decreased xanthan production, decreased sliding and swimming mobility. The capacity of XccBphP to respond to light both in vitro and in vivo was enabled by a mutation on the conserved C13 residue. These results provide evidence for a novel bacteriophytochrome function affecting an infectious process.","Loss of photo-inducible Pr-Pfr conversion; protein still binds pigment. No difference in growth in host, decreased callose deposits, decreased xanthan production, decreased sliding and swimming mobility. The capacity of XccBphP to respond to light both in vitro and in vivo was enabled by a mutation on the conserved C13 residue. These results provide evidence for a novel bacteriophytochrome function affecting an infectious process."
3938,3938,0,0,Q22618-R184G,MSVEEGMEVELKSEKMDLDDNIPDFVKETVERSGKNPMSLFSELYVHMTGNTPVFDFYNRNQPNGSMKFICVVILNGERIEGNVKSKKKEAKVSCSLKGLEVVLKHVSEYVVPAVKFEEKTTFFEMLREHTYAKFYELCKNNALIYGFEKVIASVFLKINGNLQIIALSTGNKGLRGDKIVNDGTALIDCHAEILARRGLLRFLYSEVLKFSTEPPNSIFTKGKNALVLKPGISFHLFINTAPCGVARIDKKLKPGTSDDLQNSSRLRFKIDKGMGTVLGGASEFEAPQTFDGIMMGERMRTMSCSDKLLRANVLGVQGAILSHFIDPIYYSSIAVAELNNADRLRKAVYSRAATFKPPAPFHVQDVEIGECQVEDTEQSTSAAARSTISSMNWNLADGNTEVVRTSDGMVHDKDMSGADITTPSRLCKKNMAELMITICTLTKTSVDYPISYEELKAGSQEYAAAKKSFITWLRQKDLGIWQRKPREFQMFTIN,,-1.0,MSVEEGMEVELKSEKMDLDDNIPDFVKETVERSGKNPMSLFSELYVHMTGNTPVFDFYNRNQPNGSMKFICVVILNGERIEGNVKSKKKEAKVSCSLKGLEVVLKHVSEYVVPAVKFEEKTTFFEMLREHTYAKFYELCKNNALIYGFEKVIASVFLKINGNLQIIALSTGNKGLRGDKIVNDRTALIDCHAEILARRGLLRFLYSEVLKFSTEPPNSIFTKGKNALVLKPGISFHLFINTAPCGVARIDKKLKPGTSDDLQNSSRLRFKIDKGMGTVLGGASEFEAPQTFDGIMMGERMRTMSCSDKLLRANVLGVQGAILSHFIDPIYYSSIAVAELNNADRLRKAVYSRAATFKPPAPFHVQDVEIGECQVEDTEQSTSAAARSTISSMNWNLADGNTEVVRTSDGMVHDKDMSGADITTPSRLCKKNMAELMITICTLTKTSVDYPISYEELKAGSQEYAAAKKSFITWLRQKDLGIWQRKPREFQMFTIN,Double-stranded RNA-specific adenosine deaminase adr-2,Catalyzes the hydrolytic deamination of adenosine to inosine in double-stranded RNA (dsRNA) referred to as A-to-I RNA editing. Acts primarily on non-coding regions of protein-coding genes including introns and untranslated regions (UTR). Required for normal chemotaxis. Edits the 3' UTR of clec-41 which is required for normal clec-41 expression and for chemotaxis. Plays a role in determining lifespan. Not required for RNA interference. Likely to play a role in determining whether a dsRNA enters the RNAi pathway.,"Increases editing of clec-41 RNA, leads to a threefold increase in expression of clec-41 mRNA in neural cells and enhances chemotaxis.","Increases editing of clec-41 RNA, leads to a threefold increase in expression of clec-41 mRNA in neural cells and enhances chemotaxis."
3950,3950,0,0,Q6ZS72-E146L,MSSPEPPTEPPEPDNPTWSTQPTYSNLGQIRAHLLPSKACRLRTPGSLSTNPEPLPPPLPKKILTRTQSLPTRRTLHPSSIQVQPPRRPFLGSHSVDKSQAAVGPACLPAELTFGPADAPLGLSLRDLHSPEAVHTALAARQLQGLRTIYARLRARLMGGHPGPCHPGHSFRLLDSSPCAESGDALYYRVVRAHEDAWHILVAKVPKPGADVPHPWGLELQASLSPHFNLQGLCGLVPEGTLPGAPWRGAVALAAEVPERTVAQWLAEACTQPPEEFVWAVALLLLQLSAALKFLEAWGAALVELRPENLLLVAPRGCATTGPPRLLLTDFGRVCLQPPGPPGSPGPHAPQLGSLLRALLSLAAPSTTPLAAGLELLAAQLTRLRPSASRTRGALQALLWGPGPELRGRGAPLGPWLRALGPWLRVRRGLLVLRLAERAAGGEAPSLEDWLCCEYLAEATESSMGQALALLWD,,-1.0,MSSPEPPTEPPEPDNPTWSTQPTYSNLGQIRAHLLPSKACRLRTPGSLSTNPEPLPPPLPKKILTRTQSLPTRRTLHPSSIQVQPPRRPFLGSHSVDKSQAAVGPACLPAELTFGPADAPLGLSLRDLHSPEAVHTALAARQLQGERTIYARLRARLMGGHPGPCHPGHSFRLLDSSPCAESGDALYYRVVRAHEDAWHILVAKVPKPGADVPHPWGLELQASLSPHFNLQGLCGLVPEGTLPGAPWRGAVALAAEVPERTVAQWLAEACTQPPEEFVWAVALLLLQLSAALKFLEAWGAALVELRPENLLLVAPRGCATTGPPRLLLTDFGRVCLQPPGPPGSPGPHAPQLGSLLRALLSLAAPSTTPLAAGLELLAAQLTRLRPSASRTRGALQALLWGPGPELRGRGAPLGPWLRALGPWLRVRRGLLVLRLAERAAGGEAPSLEDWLCCEYLAEATESSMGQALALLWD,Protein PEAK3,Probable catalytically inactive kinase (Probable). Interacts with CRK-II and antagonizes CRK-II-signaling. Prevents the formation of CRK-II-dependent membrane ruffling and lamellipodia-like extensions.,Enhances homodimerization and interaction with CRK isoform CRK-II. The mutation in the PEAK3 protein promotes actin filament formation.,Enhances homodimerization and interaction with CRK isoform CRK-II. The mutation in the PEAK3 protein promotes actin filament formation.
3981,3981,0,0,D3Z7P3-E207K,MMRLRGSAMLRELLLRPPAAVGAVLRRAQPLGTLCRRPRGGSRPTAGLVAAARLHPWWGGGGRAKGPGAGGLSSSPSEILQELGKGGTPPQQQQQQQQQPGASPPAAPGPKDSPGETDAFGNSEGKEMVAAGDNKIKQGLLPSLEDLLFYTIAEGQEKIPVHKFITALKSTGLRTSDPRLKECMDMLRLTLQTTSDGVMLDKDLFKKCVQSNIVLLTQAFRRKFVIPDFMSFTSHIDELYESAKKQSGGKVADYIPQLAKFSPDLWGVSVCTVDGQRHSIGDTKVPFCLQSCVKPLKYAIAVNDLGTEYVHRYVGKEPSGLRFNKLFLNEDDKPHNPMVNAGAIVVTSLIKQGVNNAEKFDYVMQFLNKMAGNEYVGFSNATFQSERESGDRNFAIGYYLKEKKCFPEGTDMVGILDFYFQLCSIEVTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSGVAGGILLVVPNVMGMMCWSPPLDKMGNSVKGIHFCHDLVSLCNFHNYDNLRHFAKKLDPRREGGDQRVKSVINLLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLLEACKVNPFPKDRWNNTPMDEALHFGHHDVFKILQEYQVQYTPQGDSDDGKGNQTVHKNLDGLL,,-1.0,MMRLRGSAMLRELLLRPPAAVGAVLRRAQPLGTLCRRPRGGSRPTAGLVAAARLHPWWGGGGRAKGPGAGGLSSSPSEILQELGKGGTPPQQQQQQQQQPGASPPAAPGPKDSPGETDAFGNSEGKEMVAAGDNKIKQGLLPSLEDLLFYTIAEGQEKIPVHKFITALKSTGLRTSDPRLKECMDMLRLTLQTTSDGVMLDKDLFKECVQSNIVLLTQAFRRKFVIPDFMSFTSHIDELYESAKKQSGGKVADYIPQLAKFSPDLWGVSVCTVDGQRHSIGDTKVPFCLQSCVKPLKYAIAVNDLGTEYVHRYVGKEPSGLRFNKLFLNEDDKPHNPMVNAGAIVVTSLIKQGVNNAEKFDYVMQFLNKMAGNEYVGFSNATFQSERESGDRNFAIGYYLKEKKCFPEGTDMVGILDFYFQLCSIEVTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSGVAGGILLVVPNVMGMMCWSPPLDKMGNSVKGIHFCHDLVSLCNFHNYDNLRHFAKKLDPRREGGDQRVKSVINLLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLLEACKVNPFPKDRWNNTPMDEALHFGHHDVFKILQEYQVQYTPQGDSDDGKGNQTVHKNLDGLL,"Glutaminase kidney isoform, mitochondrial","Catalyzes the first reaction in the primary pathway for the renal catabolism of glutamine. Plays a role in maintaining acid-base homeostasis. Regulates the levels of the neurotransmitter glutamate, the main excitatory neurotransmitter in the brain.",Decreased inhibition of enzyme activity by phosphate.,Decreased inhibition of enzyme activity by phosphate.
3991,3991,0,0,Q9NRG4-R252D,MRAEGLGGLERFCSPGKGRGLRALQPFQVGDLLFSCPAYAYVLTVNERGNHCEYCFTRKEGLSKCGRCKQAFYCNVECQKEDWPMHKLECSPMVVFGENWNPSETVRLTARILAKQKIHPERTPSEKLLAVKEFESHLDKLDNEKKDLIQSDIAALHHFYSKHLGFPDNDSLVVLFAQVNCNGFTIEDEELSHLGSAIFPDVALMNHSCCPNVIVTYKGTLAEVRAVQEIKPGEEVFTSYIDLLYPTEDRNDRLRDSYFFTCECQECTTKDKDKAKVEIRKLSDPPKAEAIRDMVRYARNVIEEFRRAKHYKSPSELLEICELSQEKMSSVFEDSNVYMLHMMYQAMGVCLYMQDWEGALQYGQKIIKPYSKHYPLYSLNVASMWLKLGRLYMGLEHKAAGEKALKKAIAIMEVAHGKDHPYISEIKQEIESH,,-1.0,MRAEGLGGLERFCSPGKGRGLRALQPFQVGDLLFSCPAYAYVLTVNERGNHCEYCFTRKEGLSKCGRCKQAFYCNVECQKEDWPMHKLECSPMVVFGENWNPSETVRLTARILAKQKIHPERTPSEKLLAVKEFESHLDKLDNEKKDLIQSDIAALHHFYSKHLGFPDNDSLVVLFAQVNCNGFTIEDEELSHLGSAIFPDVALMNHSCCPNVIVTYKGTLAEVRAVQEIKPGEEVFTSYIDLLYPTEDRNRRLRDSYFFTCECQECTTKDKDKAKVEIRKLSDPPKAEAIRDMVRYARNVIEEFRRAKHYKSPSELLEICELSQEKMSSVFEDSNVYMLHMMYQAMGVCLYMQDWEGALQYGQKIIKPYSKHYPLYSLNVASMWLKLGRLYMGLEHKAAGEKALKKAIAIMEVAHGKDHPYISEIKQEIESH,N-lysine methyltransferase SMYD2,"Protein-lysine N-methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. Specifically trimethylates histone H3 'Lys-4' (H3K4me3) in vivo. The activity requires interaction with HSP90alpha. Shows even higher methyltransferase activity on p53/TP53. Monomethylates 'Lys-370' of p53/TP53, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity of p53/TP53. Monomethylates RB1 at 'Lys-860'.",Slightly enhances methyltransferase activity on p53/TP53.,Slightly enhances methyltransferase activity on p53/TP53.
4006,4006,0,0,F7B113-A243N,MERQRRFMSEKDEYQFQHQGAVELLVFNFLLILTILTIWLFKNHRFRFLHETGGAMVYGLIMGLILRYATAPTDIESGTVYDCGKLAFSPSTLLINITDQVYEYKYKREISQHNINPHLGNAILEKMTFDPEIFFNVLLPPIIFHAGYSLKKRHFFQNLGSILTYAFLGTAISCIVIGLIMYGFVKAMVYAGQLKNGDFHFTDCLFFGSLMSATDPVTVLAIFHELHVDPDLYTLLFGESVLNDAVAIVLTYSISIYSPKENPNAFDAAAFFQSVGNFLGIFAGSFAMGSAYAVVTALLTKFTKLCEFPMLETGLFFLLSWSAFLSAEAAGLTGIVAVLFCGVTQAHYTYNNLSLDSKMRTKQLFEFMNFLAENVIFCYMGLALFTFQNHIFNALFILGAFLAIFVARACNIYPLSFLLNLGRKHKIPWNFQHMMMFSGLRGAIAFALAIRDTESQPKQMMFSTTLLLVFFTVWVFGGGTTPMLTWLQIRVGVDLDEDLKERPSSHQEANNLEKSTTKTESAWLFRMWYGFDHKYLKPILTHSGPPLTTTLPEWCGPISRLLTSPQAYGEQLKEDDAECIVNQDELAMNYQEQAASPCSPPTRLGLDQKAAPQTPGKENIYEGDLGLGGYELKLEQTPGQSQLN,,-1.0,MERQRRFMSEKDEYQFQHQGAVELLVFNFLLILTILTIWLFKNHRFRFLHETGGAMVYGLIMGLILRYATAPTDIESGTVYDCGKLAFSPSTLLINITDQVYEYKYKREISQHNINPHLGNAILEKMTFDPEIFFNVLLPPIIFHAGYSLKKRHFFQNLGSILTYAFLGTAISCIVIGLIMYGFVKAMVYAGQLKNGDFHFTDCLFFGSLMSATDPVTVLAIFHELHVDPDLYTLLFGESVLADAVAIVLTYSISIYSPKENPNAFDAAAFFQSVGNFLGIFAGSFAMGSAYAVVTALLTKFTKLCEFPMLETGLFFLLSWSAFLSAEAAGLTGIVAVLFCGVTQAHYTYNNLSLDSKMRTKQLFEFMNFLAENVIFCYMGLALFTFQNHIFNALFILGAFLAIFVARACNIYPLSFLLNLGRKHKIPWNFQHMMMFSGLRGAIAFALAIRDTESQPKQMMFSTTLLLVFFTVWVFGGGTTPMLTWLQIRVGVDLDEDLKERPSSHQEANNLEKSTTKTESAWLFRMWYGFDHKYLKPILTHSGPPLTTTLPEWCGPISRLLTSPQAYGEQLKEDDAECIVNQDELAMNYQEQAASPCSPPTRLGLDQKAAPQTPGKENIYEGDLGLGGYELKLEQTPGQSQLN,Sodium/hydrogen exchanger 9,"Endosomal Na(+), K(+)/H(+) antiporter. Mediates the electroneutral exchange of endosomal luminal H(+) for a cytosolic Na(+) or K(+). By facilitating proton efflux, SLC9A9 counteracts the acidity generated by vacuolar (V)-ATPase, thereby limiting luminal acidification. Regulates organellar pH and consequently, endosome maturation and endocytic trafficking of plasma membrane receptors and neurotransporters. Promotes the recycling of transferrin receptors back to the cell surface to facilitate additional iron uptake in the brain. Regulates synaptic transmission by regulating the luminal pH of axonal endosomes. Regulates phagosome lumenal pH, thus affecting phagosome maturation, and consequently, microbicidal activity in macrophages. Can also be active at the cell surface of specialized cells, e.g., in the inner ear hair bundles uses the high K(+) of the endolymph to regulate intracelular pH.",Increases H(+) efflux; when associated with A-244. The functional implications of autism disease mutations are mentioned in the document.,Increases H(+) efflux; when associated with A-244. The functional implications of autism disease mutations are mentioned in the document.
4012,4012,0,0,P0DJJ0-R108W,MTSPAKFKKDKEIIAEYDTQVKEIRAQLTEQMKCLDQQCELRVQLLQDLQDFFRKKAEIEMDYSRNLEKLAEHFLAKTRSTKDQQFKKDQNVLSPVNCWNLLLNQVKWESRDHTTLSDIYLNNIIPRFVQVSEDSGRLFKKSKEVGQQLQDDLMKVLNELYSVMKTYHMYNADSISAQSKLKEAEKQEEKQIGKSVKQEDRQTPCSPDSTANVRIEEKHVRRSSVKKIEKMKEKHQAKYTENKLKAIKAQNEYLLALEATNASVFKYYIHDLSDLIDQCCDLGYHASLNRALRTFLSAELNLEQSKHEGLDAIENAVENLDATSDKQRLMEMYNNVFCPPMKFEFQPHMGDMASQLCAQQPVQSELVQRCQQLQSRLSTLKIENEEVKKTMEATLQTIQDIVTVEDFDVSDCFQYSNSMESVKSTVSETFMSKPSIAKRRANQQETEQFYFTVRECYGF,,-1.0,MTSPAKFKKDKEIIAEYDTQVKEIRAQLTEQMKCLDQQCELRVQLLQDLQDFFRKKAEIEMDYSRNLEKLAEHFLAKTRSTKDQQFKKDQNVLSPVNCWNLLLNQVKRESRDHTTLSDIYLNNIIPRFVQVSEDSGRLFKKSKEVGQQLQDDLMKVLNELYSVMKTYHMYNADSISAQSKLKEAEKQEEKQIGKSVKQEDRQTPCSPDSTANVRIEEKHVRRSSVKKIEKMKEKHQAKYTENKLKAIKAQNEYLLALEATNASVFKYYIHDLSDLIDQCCDLGYHASLNRALRTFLSAELNLEQSKHEGLDAIENAVENLDATSDKQRLMEMYNNVFCPPMKFEFQPHMGDMASQLCAQQPVQSELVQRCQQLQSRLSTLKIENEEVKKTMEATLQTIQDIVTVEDFDVSDCFQYSNSMESVKSTVSETFMSKPSIAKRRANQQETEQFYFTVRECYGF,SLIT-ROBO Rho GTPase-activating protein 2C,"Human-specific protein that acts as a key modifier of cortical connectivity in the human brain. Acts by inhibiting the functions of ancestral paralog SRGAP2/SRGAP2A, a postsynaptic protein that regulates excitatory and inhibitory synapse maturation and density in cortical pyramidal neurons. SRGAP2C is unstable but is able to heterodimerize with SRGAP2/SRGAP2A, thereby reducing SRGAP2/SRGAP2A levels through proteasome-dependent degradation. Inhibition of SRGAP2/SRGAP2A by SRGAP2C leads to an increase in synaptic density and protracted synaptic maturation of both excitatory and inhibitory synapses. Modifies cortical circuit connectivity by increasing the number of local and long-range cortical inputs received by layer 2/3 pyramidal neurons. Also able to increase the probability of sensory-evoked responses by layer 2/3 pyramidal neurons.","Improves solubility; when associated with R-73, R-205, R-235 and R-250.","Improves solubility; when associated with R-73, R-205, R-235 and R-250."
4013,4013,0,0,Q9SF21-A187E,MASFDGQGFMMVDNSWVQTKAIDVESTTDISPYLSKILEDSVWNGNRSIVFDVYWDVKSVSTKSEWRLCSVKFSTKNFCLFLRLPNPFCDNLKDLYRFFASKFVTFVGVQIQEDLALLKENHGIVIRSSLEIGKLAAKARGTPIVEFLGTRELAHKILWYDMSRLDSIQSKWDEASSNDRLEAAAIEGWLIFNVYDQLQQ,,-1.0,MASFDGQGFMMVDNSWVQTKAIDVESTTDISPYLSKILEDSVWNGNRSIVFDVYWDVKSVSTKSEWRLCSVKFSTKNFCLFLRLPNPFCDNLKDLYRFFASKFVTFVGVQIQEDLALLKENHGIVIRSSLEIGKLAAKARGTPIVEFLGTRELAHKILWYDMSRLDSIQSKWDEASSNDRLEAAAIAGWLIFNVYDQLQQ,Protein RISC-INTERACTING CLEARING 3'-5' EXORIBONUCLEASE 1,"3'-to-5' exoribonuclease (RNase) specifically targeting single-stranded RNAs. Triggers miRNA accumulation in RNA-induced silencing complex (RISC), composed of miRNAs and AGO proteins, by degrading uridylated cleavage fragments. Required during plant growth and development.",Normal oligomerization but enhanced exoribonuclease activity.,Normal oligomerization but enhanced exoribonuclease activity.
4033,4033,0,0,Q8RWN7-K287E,MGNGTSRVVGCFVPSNDKNGVDLEFLEPLDEGLGHSFCYVRPSIFESPDITPSNSERFTIDSSTIDSETLTGSFRNDIVDDPSFLNRHNSKGLAETTFKAISGASVSANVSTARTGNQMALCSSDVLEPAASFESTSSFASIPLQPLPRGGSGPLNGFMSGPLERGFASGPLDRNNGFMSGPIEKGVMSGPLDVSDRSNFSAPLSFRRKKPRFQRFMRSVSGPMKSTLARTFSRRSGGLSWMHRFFLHPETRVSWAVGKDGKLHGEDPESCLESNRNLQWAHGKAGEDRVHVVLSEEQGWLFIGIYDGFSGPDAPDFVMSHLYKAIDKELEGLLWDYEEPSEDNQLQPDQEPPTEENMCDPESISEQHSKSVVAESEEVMIDDISSLGNTDTQIADGPPGDSAGPGKKSMRLYELLQLEQWEGEEIGLKRYGGNVALNNMTNQVENPSTSGGGAGNDPCTTDRSALDGIPNSGQRHGTKKSQISSKIRRMYQKQKSLRKKLFPWSYDWHREEGICVEEKIVESSGPIRRRWSGTVDHDAVLRAMARALESTEEAYMDMVEKSLDINPELALMGSCVLVMLMKDQDVYVMNVGDSRAILAQERLHDRHSNPGFGNDEGIGHKSRSRESLVRIELDRISEESPIHNQATPISVSNKNRDVTSYRLKMRAVQLSSDHSTSVEEEIWRIRSEHPEDDQSILKDRVKGQLKVTRAFGAGFLKKPNFNEALLEMFQVEYIGTDPYITCEPCTVHHRLTSSDRFMVLSSDGLYEYFSNEEVVAHVTWFIENVPEGDPAQYLIAELLSRAATKNGMEFHDLLDIPQGDRRKYHDDVSVMVVSLEGRIWRSSGQYYPERKQKFNR,,-1.0,MGNGTSRVVGCFVPSNDKNGVDLEFLEPLDEGLGHSFCYVRPSIFESPDITPSNSERFTIDSSTIDSETLTGSFRNDIVDDPSFLNRHNSKGLAETTFKAISGASVSANVSTARTGNQMALCSSDVLEPAASFESTSSFASIPLQPLPRGGSGPLNGFMSGPLERGFASGPLDRNNGFMSGPIEKGVMSGPLDVSDRSNFSAPLSFRRKKPRFQRFMRSVSGPMKSTLARTFSRRSGGLSWMHRFFLHPETRVSWAVGKDGKLHGEDPESCLESNRNLQWAHGKAGKDRVHVVLSEEQGWLFIGIYDGFSGPDAPDFVMSHLYKAIDKELEGLLWDYEEPSEDNQLQPDQEPPTEENMCDPESISEQHSKSVVAESEEVMIDDISSLGNTDTQIADGPPGDSAGPGKKSMRLYELLQLEQWEGEEIGLKRYGGNVALNNMTNQVENPSTSGGGAGNDPCTTDRSALDGIPNSGQRHGTKKSQISSKIRRMYQKQKSLRKKLFPWSYDWHREEGICVEEKIVESSGPIRRRWSGTVDHDAVLRAMARALESTEEAYMDMVEKSLDINPELALMGSCVLVMLMKDQDVYVMNVGDSRAILAQERLHDRHSNPGFGNDEGIGHKSRSRESLVRIELDRISEESPIHNQATPISVSNKNRDVTSYRLKMRAVQLSSDHSTSVEEEIWRIRSEHPEDDQSILKDRVKGQLKVTRAFGAGFLKKPNFNEALLEMFQVEYIGTDPYITCEPCTVHHRLTSSDRFMVLSSDGLYEYFSNEEVVAHVTWFIENVPEGDPAQYLIAELLSRAATKNGMEFHDLLDIPQGDRRKYHDDVSVMVVSLEGRIWRSSGQYYPERKQKFNR,Protein phosphatase 2C 32,Involved in the regulation of pedicel length and of CLAVATA pathways controlling stem cell identity at shoot and flower meristems.,Decreased catalytic activity and complete phenotypic enhancement of mutations within CLAVATA. The mutation in the CLV1 receptor kinase in Arabidopsis.,Decreased catalytic activity and complete phenotypic enhancement of mutations within CLAVATA. The mutation in the CLV1 receptor kinase in Arabidopsis.
4049,4049,0,0,Q96E22-A255P,MTGLYELVWRVLHALLCLHRTLTSWLRVRFGTWNWIWRRCCRAASAAVLAPLGFTLRKPPAVGRNRRHHRHPRGGSCLAAAHHRMRWRADGRSLEKLPVHMGLVITEVEQEPSFSDIASLVVWCMAVGISYISVYDHQGIFKRNNSRLMDEILKQQQELLGLDCSKYSPEFANSNDKDDQVLNCHLAVKVLSPEDGKADIVRAAQDFCQLVAQKQKRPTDLDVDTLASLLSSNGCPDPDLVLKFGPVDSTLGFLPWHIRLTEIVSLPSHLNISYEDFFSALRQYAACEQRLGK,,-1.0,MTGLYELVWRVLHALLCLHRTLTSWLRVRFGTWNWIWRRCCRAASAAVLAPLGFTLRKPPAVGRNRRHHRHPRGGSCLAAAHHRMRWRADGRSLEKLPVHMGLVITEVEQEPSFSDIASLVVWCMAVGISYISVYDHQGIFKRNNSRLMDEILKQQQELLGLDCSKYSPEFANSNDKDDQVLNCHLAVKVLSPEDGKADIVRAAQDFCQLVAQKQKRPTDLDVDTLASLLSSNGCPDPDLVLKFGPVDSTLGFLAWHIRLTEIVSLPSHLNISYEDFFSALRQYAACEQRLGK,Dehydrodolichyl diphosphate synthase complex subunit NUS1,"With DHDDS, forms the dehydrodolichyl diphosphate synthase (DDS) complex, an essential component of the dolichol monophosphate (Dol-P) biosynthetic machinery. Both subunits contribute to enzymatic activity, i.e. condensation of multiple copies of isopentenyl pyrophosphate (IPP) to farnesyl pyrophosphate (FPP) to produce dehydrodolichyl diphosphate (Dedol-PP), a precursor of dolichol phosphate which is utilized as a sugar carrier in protein glycosylation in the endoplasmic reticulum (ER). Synthesizes long-chain polyprenols, mostly of C95 and C100 chain length. Regulates the glycosylation and stability of nascent NPC2, thereby promoting trafficking of LDL-derived cholesterol. Acts as a specific receptor for the N-terminus of Nogo-B, a neural and cardiovascular regulator.",Enables NUS1-DHDDS heterodimerization.,Enables NUS1-DHDDS heterodimerization.
4050,4050,0,0,Q9F7P4-N97D,MKLLLILGSVIALPTFAAGGGDLDASDYTGVSFWLVTAALLASTVFFFVERDRVSAKWKTSLTVSGLVTGIAFWHYMYMRGVWIETGDSPTVFRYIDWLLTVPLLICEFYLILAAATNVAGSLFKKLLVGSLVMLVFGYMGEAGIMAAWPAFIIGCLAWVYMIYELWAGEGKSACNTASPAVQSAYNTMMYIIIFGWAIYPVGYFTGYLMGDGGSALNLNLIYNLADFVNKILFGLIIWNVAVKESSNA,,-1.0,MKLLLILGSVIALPTFAAGGGDLDASDYTGVSFWLVTAALLASTVFFFVERDRVSAKWKTSLTVSGLVTGIAFWHYMYMRGVWIETGDSPTVFRYINWLLTVPLLICEFYLILAAATNVAGSLFKKLLVGSLVMLVFGYMGEAGIMAAWPAFIIGCLAWVYMIYELWAGEGKSACNTASPAVQSAYNTMMYIIIFGWAIYPVGYFTGYLMGDGGSALNLNLIYNLADFVNKILFGLIIWNVAVKESSNA,Green-light absorbing proteorhodopsin,Light-driven proton pump that generates photothrophic energy.,Stimulation of the pH-induced shift and destabilization of the absorption spectrum in the acidic form. The assignment of the observed C=O stretch bands indicated that D-97 serves as the proton donor to the retinal Schiff base.,Stimulation of the pH-induced shift and destabilization of the absorption spectrum in the acidic form. The assignment of the observed C=O stretch bands indicated that D-97 serves as the proton donor to the retinal Schiff base.
4052,4052,0,0,P0C6T2-K23V,MITDVQLAIFANMLGVSLFLLVVLYHYVAVNNPKKQE,,-1.0,MITDVQLAIFANMLGVSLFLLVKLYHYVAVNNPKKQE,Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 4,"Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity. Specifically involved in maintaining stability of STT3A-containing OST complexes.","Increases interaction with STT3A, STT3B and RPN1. A single amino acid change in the transmembrane region of OST4 enhances its presumptive interactions with STT3 isoforms and ribophorin I. Depletion of OST4 stabilizes native OST complexes and leads to an enhancement in the N-glycosylation of endogenous prosaposin.","Increases interaction with STT3A, STT3B and RPN1. A single amino acid change in the transmembrane region of OST4 enhances its presumptive interactions with STT3 isoforms and ribophorin I. Depletion of OST4 stabilizes native OST complexes and leads to an enhancement in the N-glycosylation of endogenous prosaposin."
4062,4062,0,0,Q9UH99-E703Y,MSRRSQRLTRYSQGDDDGSSSSGGSSVAGSQSTLFKDSPLRTLKRKSSNMKRLSPAPQLGPSSDAHTSYYSESLVHESWFPPRSSLEELHGDANWGEDLRVRRRRGTGGSESSRASGLVGRKATEDFLGSSSGYSSEDDYVGYSDVDQQSSSSRLRSAVSRAGSLLWMVATSPGRLFRLLYWWAGTTWYRLTTAASLLDVFVLTRRFSSLKTFLWFLLPLLLLTCLTYGAWYFYPYGLQTFHPALVSWWAAKDSRRPDEGWEARDSSPHFQAEQRVMSRVHSLERRLEALAAEFSSNWQKEAMRLERLELRQGAPGQGGGGGLSHEDTLALLEGLVSRREAALKEDFRRETAARIQEELSALRAEHQQDSEDLFKKIVRASQESEARIQQLKSEWQSMTQESFQESSVKELRRLEDQLAGLQQELAALALKQSSVAEEVGLLPQQIQAVRDDVESQFPAWISQFLARGGGGRVGLLQREEMQAQLRELESKILTHVAEMQGKSAREAAASLSLTLQKEGVIGVTEEQVHHIVKQALQRYSEDRIGLADYALESGGASVISTRCSETYETKTALLSLFGIPLWYHSQSPRVILQPDVHPGNCWAFQGPQGFAVVRLSARIRPTAVTLEHVPKALSPNSTISSAPKDFAIFGFDEDLQQEGTLLGKFTYDQDGEPIQTFHFQAPTMATYQVVELRILTNWGHPEYTCIYRFRVHGEPAH,,-1.0,MSRRSQRLTRYSQGDDDGSSSSGGSSVAGSQSTLFKDSPLRTLKRKSSNMKRLSPAPQLGPSSDAHTSYYSESLVHESWFPPRSSLEELHGDANWGEDLRVRRRRGTGGSESSRASGLVGRKATEDFLGSSSGYSSEDDYVGYSDVDQQSSSSRLRSAVSRAGSLLWMVATSPGRLFRLLYWWAGTTWYRLTTAASLLDVFVLTRRFSSLKTFLWFLLPLLLLTCLTYGAWYFYPYGLQTFHPALVSWWAAKDSRRPDEGWEARDSSPHFQAEQRVMSRVHSLERRLEALAAEFSSNWQKEAMRLERLELRQGAPGQGGGGGLSHEDTLALLEGLVSRREAALKEDFRRETAARIQEELSALRAEHQQDSEDLFKKIVRASQESEARIQQLKSEWQSMTQESFQESSVKELRRLEDQLAGLQQELAALALKQSSVAEEVGLLPQQIQAVRDDVESQFPAWISQFLARGGGGRVGLLQREEMQAQLRELESKILTHVAEMQGKSAREAAASLSLTLQKEGVIGVTEEQVHHIVKQALQRYSEDRIGLADYALESGGASVISTRCSETYETKTALLSLFGIPLWYHSQSPRVILQPDVHPGNCWAFQGPQGFAVVRLSARIRPTAVTLEHVPKALSPNSTISSAPKDFAIFGFDEDLQQEGTLLGKFTYDQDGEPIQTFHFQAPTMATYQVVELRILTNWGHPEETCIYRFRVHGEPAH,SUN domain-containing protein 2,"As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning. Specifically, SYNE2 and SUN2 assemble in arrays of transmembrane actin-associated nuclear (TAN) lines which are bound to F-actin cables and couple the nucleus to retrograde actin flow during actin-dependent nuclear movement. Required for interkinetic nuclear migration (INM) and essential for nucleokinesis and centrosome-nucleus coupling during radial neuronal migration in the cerebral cortex and during glial migration. Required for nuclear migration in retinal photoreceptor progenitors implicating association with cytoplasmic dynein-dynactin and kinesin motor complexes, and probably B-type lamins; SUN1 and SUN2 seem to act redundantly. The SUN1/2:KASH5 LINC complex couples telomeres to microtubules during meiosis; SUN1 and SUN2 seem to act at least partial redundantly. Anchors chromosome movement in the prophase of meiosis and is involved in selective gene expression of coding and non-coding RNAs needed for gametogenesis. Required for telomere attachment to nuclear envelope and gametogenesis. May also function on endocytic vesicles as a receptor for RAB5-GDP and participate in the activation of RAB5.",Disrupts interaction with SYNE2. Enhances interaction with SYNE2; when associated with E-603 and E-641.,Disrupts interaction with SYNE2. Enhances interaction with SYNE2; when associated with E-603 and E-641.
4087,4087,0,0,P15209-F816Y,MSPWLKWHGPAMARLWGLCLLVLGFWRASLACPTSCKCSSARIWCTEPSPGIVAFPRLEPNSVDPENITEILIANQKRLEIINEDDVEAYVGLRNLTIVDSGLKFVAYKAFLKNSNLRHINFTRNKLTSLSRRHFRHLDLSDLILTGNPFTCSCDIMWLKTLQETKSSPDTQDLYCLNESSKNMPLANLQIPNCGLPSARLAAPNLTVEEGKSVTLSCSVGGDPLPTLYWDVGNLVSKHMNETSHTQGSLRITNISSDDSGKQISCVAENLVGEDQDSVNLTVHFAPTITFLESPTSDHHWCIPFTVRGNPKPALQWFYNGAILNESKYICTKIHVTNHTEYHGCLQLDNPTHMNNGDYTLMAKNEYGKDERQISAHFMGRPGVDYETNPNYPEVLYEDWTTPTDIGDTTNKSNEIPSTDVADQSNREHLSVYAVVVIASVVGFCLLVMLLLLKLARHSKFGMKGPASVISNDDDSASPLHHISNGSNTPSSSEGGPDAVIIGMTKIPVIENPQYFGITNSQLKPDTFVQHIKRHNIVLKRELGEGAFGKVFLAECYNLCPEQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHGDLNKFLRAHGPDAVLMAEGNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQRPRTCPQEVYELMLGCWQREPHTRKNIKSIHTLLQNLAKASPVYLDILG,,-1.0,MSPWLKWHGPAMARLWGLCLLVLGFWRASLACPTSCKCSSARIWCTEPSPGIVAFPRLEPNSVDPENITEILIANQKRLEIINEDDVEAYVGLRNLTIVDSGLKFVAYKAFLKNSNLRHINFTRNKLTSLSRRHFRHLDLSDLILTGNPFTCSCDIMWLKTLQETKSSPDTQDLYCLNESSKNMPLANLQIPNCGLPSARLAAPNLTVEEGKSVTLSCSVGGDPLPTLYWDVGNLVSKHMNETSHTQGSLRITNISSDDSGKQISCVAENLVGEDQDSVNLTVHFAPTITFLESPTSDHHWCIPFTVRGNPKPALQWFYNGAILNESKYICTKIHVTNHTEYHGCLQLDNPTHMNNGDYTLMAKNEYGKDERQISAHFMGRPGVDYETNPNYPEVLYEDWTTPTDIGDTTNKSNEIPSTDVADQSNREHLSVYAVVVIASVVGFCLLVMLLLLKLARHSKFGMKGPASVISNDDDSASPLHHISNGSNTPSSSEGGPDAVIIGMTKIPVIENPQYFGITNSQLKPDTFVQHIKRHNIVLKRELGEGAFGKVFLAECYNLCPEQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHGDLNKFLRAHGPDAVLMAEGNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQRPRTCPQEVYELMLGCWQREPHTRKNIKSIHTLLQNLAKASPVFLDILG,BDNF/NT-3 growth factors receptor,"Receptor tyrosine kinase involved in the development and the maturation of the central and the peripheral nervous systems through regulation of neuron survival, proliferation, migration, differentiation, and synapse formation and plasticity. Receptor for BDNF/brain-derived neurotrophic factor and NTF4/neurotrophin-4. Alternatively can also bind NTF3/neurotrophin-3 which is less efficient in activating the receptor but regulates neuron survival through NTRK2. Upon ligand-binding, undergoes homodimerization, autophosphorylation and activation. Recruits, phosphorylates and/or activates several downstream effectors including SHC1, FRS2, SH2B1, SH2B2 and PLCG1 that regulate distinct overlapping signaling cascades. Through SHC1, FRS2, SH2B1, SH2B2 activates the GRB2-Ras-MAPK cascade that regulates for instance neuronal differentiation including neurite outgrowth. Through the same effectors controls the Ras-PI3 kinase-AKT1 signaling cascade that mainly regulates growth and survival. Through PLCG1 and the downstream protein kinase C-regulated pathways controls synaptic plasticity. Thereby, plays a role in learning and memory by regulating both short term synaptic function and long-term potentiation. PLCG1 also leads to NF-Kappa-B activation and the transcription of genes involved in cell survival. Hence, it is able to suppress anoikis, the apoptosis resulting from loss of cell-matrix interactions. Isoform GP95-TRKB may also play a role in neutrophin-dependent calcium signaling in glial cells and mediate communication between neurons and glia.",Gain of interaction with PLCG1.,Gain of interaction with PLCG1.
4110,4110,0,0,Q96B02-E144W,MASMQKRLQKELLALQNDPPPGMTLNEKSVQNSITQWIVDMEGAPGTLYEGEKFQLLFKFSSRYPFDSPQVMFTGENIPVHPHVYSNGHICLSILTEDWSPALSVQSVCLSIISMLSSCKEKRRPPDNSFYVRTCNKNPKKTKWWYHDDTC,,-1.0,MASMQKRLQKELLALQNDPPPGMTLNEKSVQNSITQWIVDMEGAPGTLYEGEKFQLLFKFSSRYPFDSPQVMFTGENIPVHPHVYSNGHICLSILTEDWSPALSVQSVCLSIISMLSSCKEKRRPPDNSFYVRTCNKNPKKTKEWYHDDTC,Ubiquitin-conjugating enzyme E2 W,"Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Specifically monoubiquitinates the N-terminus of various substrates, including ATXN3, MAPT/TAU, POLR2H/RPB8 and STUB1/CHIP, by recognizing backbone atoms of disordered N-termini. Involved in degradation of misfolded chaperone substrates by mediating monoubiquitination of STUB1/CHIP, leading to recruitment of ATXN3 to monoubiquitinated STUB1/CHIP, and restriction of the length of ubiquitin chain attached to STUB1/CHIP substrates by ATXN3. After UV irradiation, but not after mitomycin-C (MMC) treatment, acts as a specific E2 ubiquitin-conjugating enzyme for the Fanconi anemia complex by associating with E3 ubiquitin-protein ligase FANCL and catalyzing monoubiquitination of FANCD2, a key step in the DNA damage pathway. In vitro catalyzes 'Lys-11'-linked polyubiquitination. UBE2W-catalyzed ubiquitination occurs also in the presence of inactive RING/U-box type E3s, i.e. lacking the active site cysteine residues to form thioester bonds with ubiquitin, or even in the absence of E3, albeit at a slower rate.","Decrease of ubiquitination activity toward various substrates, including POLR2H, ATXN3, STUB1 and MAPT.","Decrease of ubiquitination activity toward various substrates, including POLR2H, ATXN3, STUB1 and MAPT."
4111,4111,0,0,Q9WVE8-D373S,MSVTYDDSVGVEVSSDSFWEVGNYKRTVKRIDDGHRLCGDLMNCLHERARIEKAYAQQLTEWARRWRQLVEKGPQYGTVEKAWIAVMSEAERVSELHLEVKASLMNEDFEKIKNWQKEAFHKQMMGGFKETKEAEDGFRKAQKPWAKKLKEVEAAKKAHHTACKEEKLAISREANSKADPSLNPEQLKKLQDKIEKCKQDVLKTKDKYEKSLKELDQTTPQYMENMEQVFEQCQQFEEKRLRFFREVLLEVQKHLDLSNVASYKTIYRELEQSIKAADAVEDLRWFRANHGPGMAMNWPQFEEWSADLNRTLSRREKKKAVDGVTLTGINQTGDQSGQNKPGSNLSVPSNPAQSTQLQSSYNPFEDEDDTGSSISEKEDIKAKNVSSYEKTQTYPTDWSDDESNNPFSSTDANGDSNPFDEDTTSGTEVRVRALYDYEGQEHDELSFKAGDELTKIEDEDEQGWCKGRLDSGQVGLYPANYVEAIQ,,-1.0,MSVTYDDSVGVEVSSDSFWEVGNYKRTVKRIDDGHRLCGDLMNCLHERARIEKAYAQQLTEWARRWRQLVEKGPQYGTVEKAWIAVMSEAERVSELHLEVKASLMNEDFEKIKNWQKEAFHKQMMGGFKETKEAEDGFRKAQKPWAKKLKEVEAAKKAHHTACKEEKLAISREANSKADPSLNPEQLKKLQDKIEKCKQDVLKTKDKYEKSLKELDQTTPQYMENMEQVFEQCQQFEEKRLRFFREVLLEVQKHLDLSNVASYKTIYRELEQSIKAADAVEDLRWFRANHGPGMAMNWPQFEEWSADLNRTLSRREKKKAVDGVTLTGINQTGDQSGQNKPGSNLSVPSNPAQSTQLQSSYNPFEDEDDTGSDISEKEDIKAKNVSSYEKTQTYPTDWSDDESNNPFSSTDANGDSNPFDEDTTSGTEVRVRALYDYEGQEHDELSFKAGDELTKIEDEDEQGWCKGRLDSGQVGLYPANYVEAIQ,Protein kinase C and casein kinase substrate in neurons protein 2,"Regulates the morphogenesis and endocytosis of caveolae. Lipid-binding protein that is able to promote the tubulation of the phosphatidic acid-containing membranes it preferentially binds. Plays a role in intracellular vesicle-mediated transport. Involved in the endocytosis of cell-surface receptors like the EGF receptor, contributing to its internalization in the absence of EGF stimulus.",Increased membrane-binding affinity.,Increased membrane-binding affinity.
4129,4129,0,0,P08887-A350N,MLAVGCALLAALLAAPGAALAPRRCPAQEVARGVLTSLPGDSVTLTCPGVEPEDNATVHWVLRKPAAGSHPSRWAGMGRRLLLRSVQLHDSGNYSCYRAGRPAGTVHLLVDVPPEEPQLSCFRKSPLSNVVCEWGPRSTPSLTTKAVLLVRKFQNSPAEDFQEPCQYSQESQKFSCQLAVPEGDSSFYIVSMCVASSVGSKFSKTQTFQGCGILQPDPPANITVTAVARNPRWLSVTWQDPHSWNSSFYRLRFELRYRAERSKTFTTWMVKDLQHHCVIHDAWSGLRHVVQLRAQEEFGQGEWSEWSPEAMGTPWTESRSPPAENEVSTPMQALTTNKDDDNILFRDSANATSLPVQDSSSVPLPTFLVAGGSLAFGTLLCIAIVLRFKKTWKLRALKEGKTSMHPPYSLGQLVPERPRPTPVLVPLISPPVSPSSLGSDNTSSHNRPDARDPRSPYDISNTDYFFPR,,-1.0,MLAVGCALLAALLAAPGAALAPRRCPAQEVARGVLTSLPGDSVTLTCPGVEPEDNATVHWVLRKPAAGSHPSRWAGMGRRLLLRSVQLHDSGNYSCYRAGRPAGTVHLLVDVPPEEPQLSCFRKSPLSNVVCEWGPRSTPSLTTKAVLLVRKFQNSPAEDFQEPCQYSQESQKFSCQLAVPEGDSSFYIVSMCVASSVGSKFSKTQTFQGCGILQPDPPANITVTAVARNPRWLSVTWQDPHSWNSSFYRLRFELRYRAERSKTFTTWMVKDLQHHCVIHDAWSGLRHVVQLRAQEEFGQGEWSEWSPEAMGTPWTESRSPPAENEVSTPMQALTTNKDDDNILFRDSAAATSLPVQDSSSVPLPTFLVAGGSLAFGTLLCIAIVLRFKKTWKLRALKEGKTSMHPPYSLGQLVPERPRPTPVLVPLISPPVSPSSLGSDNTSSHNRPDARDPRSPYDISNTDYFFPR,Interleukin-6 receptor subunit alpha,"Part of the receptor for interleukin 6. Binds to IL6 with low affinity, but does not transduce a signal. Signal activation necessitate an association with IL6ST. Activation leads to the regulation of the immune response, acute-phase reactions and hematopoiesis. The interaction with membrane-bound IL6R and IL6ST stimulates 'classic signaling', the restricted expression of the IL6R limits classic IL6 signaling to only a few tissues such as the liver and some cells of the immune system. Whereas the binding of IL6 and soluble IL6R to IL6ST stimulates 'trans-signaling'. Alternatively, 'cluster signaling' occurs when membrane-bound IL6:IL6R complexes on transmitter cells activate IL6ST receptors on neighboring receiver cells (Probable).Signaling via the membrane-bound IL6R is mostly regenerative and anti-inflammatory (Probable). Drives naive CD4(+) T cells to the Th17 lineage, through 'cluster signaling' by dendritic cells.Soluble form of IL6 receptor (sIL6R) that acts as an agonist of IL6 activity. The IL6:sIL6R complex (hyper-IL6) binds to IL6ST/gp130 on cell surfaces and induces signaling also on cells that do not express membrane-bound IL6R in a process called IL6 'trans-signaling'. sIL6R is causative for the pro-inflammatory properties of IL6 and an important player in the development of chronic inflammatory diseases. In complex with IL6, is required for induction of VEGF production. Plays a protective role during liver injury, being required for maintenance of tissue regeneration. 'Trans-signaling' in central nervous system regulates energy and glucose homeostasis.Soluble form of IL6 receptor (sIL6R) that acts as an agonist of IL6 activity. The IL6:sIL6R complex (hyper-IL6) binds to IL6ST/gp130 on cell surfaces and induces signaling also on cells that do not express membrane-bound IL6R in a process called IL6 'trans-signaling'. sIL6R is causative for the pro-inflammatory properties of IL6 and an important player in the development of chronic inflammatory diseases. In complex with IL6, is required for induction of VEGF production. Plays a protective role during liver injury, being required for maintenance of tissue regeneration. 'Trans-signaling' in central nervous system regulates energy and glucose homeostasis.","Enhances IL6R signaling; when associated with A-55, A-93, A-221 and A-245. Gain of cleavage by ADAM17; when associated with A-55, A-93, A-221 and A-245.","Enhances IL6R signaling; when associated with A-55, A-93, A-221 and A-245. Gain of cleavage by ADAM17; when associated with A-55, A-93, A-221 and A-245."
4149,4149,0,0,Q9V118-A45K,MSDNEIVAGIMRDHIINLLKEGKRIDDRGFEDYRPIEIEVGVIEKAEGSALVKLGSTQVLVGIKTSLGEPFPDTPNMGVMTTNVELVPLASPTFEPGPPDERAIELARVIDRGIRESKALNLEKMVIVPGKIVRVVFIDVHVLDHDGNLMDAIGIAAIAALLNARVPKVRYNEETGEVETLDETEPLPVEKIPVPVTFAKIGNILVVDPSLDEELVMDGKITITTDETGHISAVQKSEGGAFKLEEVMYAVETAFKKAEEIRKLILEAVEKAKQ,,-1.0,MSDNEIVAGIMRDHIINLLKEGKRIDDRGFEDYRPIEIEVGVIEAAEGSALVKLGSTQVLVGIKTSLGEPFPDTPNMGVMTTNVELVPLASPTFEPGPPDERAIELARVIDRGIRESKALNLEKMVIVPGKIVRVVFIDVHVLDHDGNLMDAIGIAAIAALLNARVPKVRYNEETGEVETLDETEPLPVEKIPVPVTFAKIGNILVVDPSLDEELVMDGKITITTDETGHISAVQKSEGGAFKLEEVMYAVETAFKKAEEIRKLILEAVEKAKQ,Exosome complex component Rrp42,"Non-catalytic component of the exosome, which is a complex involved in RNA degradation. Contributes to the structuring of the Rrp41 active site.","Does not affect ring assembly, but increases RNA degradation.","Does not affect ring assembly, but increases RNA degradation."
4155,4155,0,0,P46100-A218E,MTAEPMSESKLNTLVQKLHDFLAHSSEESEETSSPPRLAMNQNTDKISGSGSNSDMMENSKEEGTSSSEKSKSSGSSRSKRKPSIVTKYVESDDEKPLDDETVNEDASNENSENDITMQSLPKGTVIVQPEPVLNEDKDDFKGPEFRSRSKMKTENLKKRGEDGLHGIVSCTACGQQVNHFQKDSIYRHPSLQVLICKNCFKYYMSDDISRDSDGMDEQCRWCAEGGNLICCDFCHNAFCKKCILRNLGRKELSTIMDENNQWYCYICHPEPLLDLVTACNSVFENLEQLLQQNKKKIKVDSEKSNKVYEHTSRFSPKKTSSNCNGEEKKLDDSCSGSVTYSYSALIVPKEMIKKAKKLIETTANMNSSYVKFLKQATDNSEISSATKLRQLKAFKSVLADIKKAHLALEEDLNSEFRAMDAVNKEKNTKEHKVIDAKFETKARKGEKPCALEKKDISKSEAKLSRKQVDSEHMHQNVPTEEQRTNKSTGGEHKKSDRKEEPQYEPANTSEDLDMDIVSVPSSVPEDIFENLETAMEVQSSVDHQGDGSSGTEQEVESSSVKLNISSKDNRGGIKSKTTAKVTKELYVKLTPVSLSNSPIKGADCQEVPQDKDGYKSCGLNPKLEKCGLGQENSDNEHLVENEVSLLLEESDLRRSPRVKTTPLRRPTETNPVTSNSDEECNETVKEKQKLSVPVRKKDKRNSSDSAIDNPKPNKLPKSKQSETVDQNSDSDEMLAILKEVSRMSHSSSSDTDINEIHTNHKTLYDLKTQAGKDDKGKRKRKSSTSGSDFDTKKGKSAKSSIISKKKRQTQSESSNYDSELEKEIKSMSKIGAARTTKKRIPNTKDFDSSEDEKHSKKGMDNQGHKNLKTSQEGSSDDAERKQERETFSSAEGTVDKDTTIMELRDRLPKKQQASASTDGVDKLSGKEESFTSLEVRKVAETKEKSKHLKTKTCKKVQDGLSDIAEKFLKKDQSDETSEDDKKQSKKGTEEKKKPSDFKKKVIKMEQQYESSSDGTEKLPEREE,,-1.0,MTAEPMSESKLNTLVQKLHDFLAHSSEESEETSSPPRLAMNQNTDKISGSGSNSDMMENSKEEGTSSSEKSKSSGSSRSKRKPSIVTKYVESDDEKPLDDETVNEDASNENSENDITMQSLPKGTVIVQPEPVLNEDKDDFKGPEFRSRSKMKTENLKKRGEDGLHGIVSCTACGQQVNHFQKDSIYRHPSLQVLICKNCFKYYMSDDISRDSDGMDAQCRWCAEGGNLICCDFCHNAFCKKCILRNLGRKELSTIMDENNQWYCYICHPEPLLDLVTACNSVFENLEQLLQQNKKKIKVDSEKSNKVYEHTSRFSPKKTSSNCNGEEKKLDDSCSGSVTYSYSALIVPKEMIKKAKKLIETTANMNSSYVKFLKQATDNSEISSATKLRQLKAFKSVLADIKKAHLALEEDLNSEFRAMDAVNKEKNTKEHKVIDAKFETKARKGEKPCALEKKDISKSEAKLSRKQVDSEHMHQNVPTEEQRTNKSTGGEHKKSDRKEEPQYEPANTSEDLDMDIVSVPSSVPEDIFENLETAMEVQSSVDHQGDGSSGTEQEVESSSVKLNISSKDNRGGIKSKTTAKVTKELYVKLTPVSLSNSPIKGADCQEVPQDKDGYKSCGLNPKLEKCGLGQENSDNEHLVENEVSLLLEESDLRRSPRVKTTPLRRPTETNPVTSNSDEECNETVKEKQKLSVPVRKKDKRNSSDSAIDNPKPNKLPKSKQSETVDQNSDSDEMLAILKEVSRMSHSSSSDTDINEIHTNHKTLYDLKTQAGKDDKGKRKRKSSTSGSDFDTKKGKSAKSSIISKKKRQTQSESSNYDSELEKEIKSMSKIGAARTTKKRIPNTKDFDSSEDEKHSKKGMDNQGHKNLKTSQEGSSDDAERKQERETFSSAEGTVDKDTTIMELRDRLPKKQQASASTDGVDKLSGKEESFTSLEVRKVAETKEKSKHLKTKTCKKVQDGLSDIAEKFLKKDQSDETSEDDKKQSKKGTEEKKKPSDFKKKVIKMEQQYESSSDGTEKLPEREE,Transcriptional regulator ATRX,"Involved in transcriptional regulation and chromatin remodeling. Facilitates DNA replication in multiple cellular environments and is required for efficient replication of a subset of genomic loci. Binds to DNA tandem repeat sequences in both telomeres and euchromatin and in vitro binds DNA quadruplex structures. May help stabilizing G-rich regions into regular chromatin structures by remodeling G4 DNA and incorporating H3.3-containing nucleosomes. Catalytic component of the chromatin remodeling complex ATRX:DAXX which has ATP-dependent DNA translocase activity and catalyzes the replication-independent deposition of histone H3.3 in pericentric DNA repeats outside S-phase and telomeres, and the in vitro remodeling of H3.3-containing nucleosomes. Its heterochromatin targeting is proposed to involve a combinatorial readout of histone H3 modifications (specifically methylation states of H3K9 and H3K4) and association with CBX5. Involved in maintaining telomere structural integrity in embryonic stem cells which probably implies recruitment of CBX5 to telomeres. Reports on the involvement in transcriptional regulation of telomeric repeat-containing RNA (TERRA) are conflicting; according to a report, it is not sufficient to decrease chromatin condensation at telomeres nor to increase expression of telomeric RNA in fibroblasts. May be involved in telomere maintenance via recombination in ALT (alternative lengthening of telomeres) cell lines. Acts as negative regulator of chromatin incorporation of transcriptionally repressive histone MACROH2A1, particularily at telomeres and the alpha-globin cluster in erythroleukemic cells. Participates in the allele-specific gene expression at the imprinted IGF2/H19 gene locus. On the maternal allele, required for the chromatin occupancy of SMC1 and CTCTF within the H19 imprinting control region (ICR) and involved in esatblishment of histone tails modifications in the ICR. May be involved in brain development and facial morphogenesis. Binds to zinc-finger coding genes with atypical chromatin signatures and regulates its H3K9me3 levels. Forms a complex with ZNF274, TRIM28 and SETDB1 to facilitate the deposition and maintenance of H3K9me3 at the 3' exons of zinc-finger genes.",Enhances interaction with histone H3 peptides unmethylated at 'Lys-5' (H3K4me0); increases pericentromeric localization. The mutation in the ATRX protein causes a functional change in the protein's ability to engage the N-terminal tail of histone H3 through two binding pockets.,Enhances interaction with histone H3 peptides unmethylated at 'Lys-5' (H3K4me0); increases pericentromeric localization. The mutation in the ATRX protein causes a functional change in the protein's ability to engage the N-terminal tail of histone H3 through two binding pockets.
4156,4156,0,0,Q96Y68-A125K,MAAFKPQWNDWCPGCGNFGILNAEQQAIVELGVDTKNVVVVSGIGCSGKIPHFFRTPISGVHTLHGRAIAFATGIKLSNPDLVVIVNGGDGDLLGIGAGHFVAAGRRNVDMVVILHDNGVYGLTKGQASPTLKRGEKPKSLPRPNINDAVNPIALAISSGYTFVARGYAYDVKHLKELIKSAIKHKGLALIDVLQPCPTYNDINTKEWYDKRIYKLDTLPDWDPVVKKPEEVNEKIKRAIDKSLEWGDRIPIGIFYQNELVPSYEERIKANSPAYLDYTPAKQLIEKEGKLTTIIDPLLKEREVD,,-1.0,MAAFKPQWNDWCPGCGNFGILNAEQQAIVELGVDTKNVVVVSGIGCSGKIPHFFRTPISGVHTLHGRAIAFATGIKLSNPDLVVIVNGGDGDLLGIGAGHFVAAGRRNVDMVVILHDNGVYGLTAGQASPTLKRGEKPKSLPRPNINDAVNPIALAISSGYTFVARGYAYDVKHLKELIKSAIKHKGLALIDVLQPCPTYNDINTKEWYDKRIYKLDTLPDWDPVVKKPEEVNEKIKRAIDKSLEWGDRIPIGIFYQNELVPSYEERIKANSPAYLDYTPAKQLIEKEGKLTTIIDPLLKEREVD,"2-oxoacid:ferredoxin oxidoreductase 1, subunit beta","Catalyzes the coenzyme A-dependent oxidative decarboxylation of different 2-oxoacids such as 2-oxoglutarate, pyruvate and 2-oxobutyrate to form their CoA derivatives.","Shows a strong increase of affinity for CoA and a strong activation by 4-fluoro-7-nitrobenzofurazan (NBD-F). showed a small decrease in the K(m) value for CoA and showed strong activation by NBD-F, compared with and wild type StOFOR, indicating K125 in subunit-b is the critical residue that interacts with CoA.","Shows a strong increase of affinity for CoA and a strong activation by 4-fluoro-7-nitrobenzofurazan (NBD-F). showed a small decrease in the K(m) value for CoA and showed strong activation by NBD-F, compared with and wild type StOFOR, indicating K125 in subunit-b is the critical residue that interacts with CoA."
4159,4159,0,0,O75143-D134V,METDLNSQDRKDLDKFIKFFALKTVQVIVQARLGEKICTRSSSSPTGSDWFNLAIKDIPEVTHEAKKALAGQLPAVGRSMCVEISLKTSEGDSMELEIWCLEMNEKCDKEIKVSYTVYNRLSLLLKSLLAITRVTPAYRLSRKQGHEYVILYRIYFGEVQLSGLGEGFQTVRVGTVGTPVGTITLSCAYRINLAFMSTRQFERTPPIMGIIIDHFVDRPYPSSSPMHPCNYRTAGEDTGVIYPSVEDSQEVCTTSFSTSPPSQLSSSRLSYQPAALGVGSADLAYPVVFAAGLNATHPHQLMVPGKEGGVPLAPNQPVHGTQADQERLATCTPSDRTHCAATPSSSEDTETVSNSSEGRASPHDVLETIFVRKVGAFVNKPINQVTLTSLDIPFAMFAPKNLELEDTDPMVNPPDSPETESPLQGSLHSDGSSGGSSGNTHDDFVMIDFKPAFSKDDILPMDLGTFYREFQNPPQLSSLSIDIGAQSMAEDLDSLPEKLAVHEKNVREFDAFVETLQ,,-1.0,METDLNSQDRKDLDKFIKFFALKTVQVIVQARLGEKICTRSSSSPTGSDWFNLAIKDIPEVTHEAKKALAGQLPAVGRSMCVEISLKTSEGDSMELEIWCLEMNEKCDKEIKVSYTVYNRLSLLLKSLLAITRDTPAYRLSRKQGHEYVILYRIYFGEVQLSGLGEGFQTVRVGTVGTPVGTITLSCAYRINLAFMSTRQFERTPPIMGIIIDHFVDRPYPSSSPMHPCNYRTAGEDTGVIYPSVEDSQEVCTTSFSTSPPSQLSSSRLSYQPAALGVGSADLAYPVVFAAGLNATHPHQLMVPGKEGGVPLAPNQPVHGTQADQERLATCTPSDRTHCAATPSSSEDTETVSNSSEGRASPHDVLETIFVRKVGAFVNKPINQVTLTSLDIPFAMFAPKNLELEDTDPMVNPPDSPETESPLQGSLHSDGSSGGSSGNTHDDFVMIDFKPAFSKDDILPMDLGTFYREFQNPPQLSSLSIDIGAQSMAEDLDSLPEKLAVHEKNVREFDAFVETLQ,Autophagy-related protein 13,"Autophagy factor required for autophagosome formation and mitophagy. Target of the TOR kinase signaling pathway that regulates autophagy through the control of the phosphorylation status of ATG13 and ULK1, and the regulation of the ATG13-ULK1-RB1CC1 complex. Through its regulation of ULK1 activity, plays a role in the regulation of the kinase activity of mTORC1 and cell proliferation.",Increases interaction with ATG101; when associated with D-131.,Increases interaction with ATG101; when associated with D-131.
4165,4165,0,0,Q7AKG8-S62C,MSCGEPHETDCSEILDHLYEFLDKEMPDSDCVKFEHHFEECSPCLEKYGLEQAVKKLVKRCCGQDDVPGDLRAKVMGRLDLIRSGQSVPEHDVAAAPSSSAPQES,,-1.0,MSCGEPHETDCSEILDHLYEFLDKEMPDSDCVKFEHHFEECSPCLEKYGLEQAVKKLVKRCSGQDDVPGDLRAKVMGRLDLIRSGQSVPEHDVAAAPSSSAPQES,Anti-sigma factor RsrA,"A redox-regulated anti-sigma factor for extracytoplasmic function (ECF) sigma factor SigR, and a key sensor of disulfide stress. Holds SigR, its cognate ECF sigma factor, in an inactive form, inhibiting its sigma activity under reducing but not oxidizing conditions; oxidation and reduction of the anti-sigma factor is reversible. Mycothiol (MSH) is competent for reduction of RsrA, allowing it to bind to SigR. In conjunction with its cognate sigma factor SigR may sense the intracellular level of reduced MSH. Probably releases SigR during oxidative stress.","Increased sporulation, abnormal inhibition of trxCp1, binding of SigR.","Increased sporulation, abnormal inhibition of trxCp1, binding of SigR."
4167,4167,0,0,Q31KC7-A8D,MVVALGLDFGTSGARAIACDFDSDRSVSVSVTFPKTSQNWPQVWREALWQLLTQIPADWRSRIERIAIDGTSGTVLLCDREGQPQTEPLLYNQACPIDLADLADWVPADHAALSSTSSLAKLWFWQQQFGALPPDWQILAQADWLSLQLHGCSQQSDYHNALKLGYSPDRERFSKNLLDSELGALLPVVHEPGVAIGPILPAIAQEFGLSPDCQICAGTTDSIAAFLASGAHQPGEAVTSLGSTIVLKLLSQVAVSDRLTGVYSHKLGGYWLTGGASNCGGATLRQFFPDTELESLSCQIDPTKKSGLDYYPLPSRGERFPIADPDRLPQLEPRPENPVQFLQGLLEGLTQVETLGYQRLQDLGATPLKRIWTAGGGAKNAVWQQLRQQAIGVPIAIAPNTEAAFGTARLAAFGLAAFHSAGLKRT,,-1.0,MVVALGLAFGTSGARAIACDFDSDRSVSVSVTFPKTSQNWPQVWREALWQLLTQIPADWRSRIERIAIDGTSGTVLLCDREGQPQTEPLLYNQACPIDLADLADWVPADHAALSSTSSLAKLWFWQQQFGALPPDWQILAQADWLSLQLHGCSQQSDYHNALKLGYSPDRERFSKNLLDSELGALLPVVHEPGVAIGPILPAIAQEFGLSPDCQICAGTTDSIAAFLASGAHQPGEAVTSLGSTIVLKLLSQVAVSDRLTGVYSHKLGGYWLTGGASNCGGATLRQFFPDTELESLSCQIDPTKKSGLDYYPLPSRGERFPIADPDRLPQLEPRPENPVQFLQGLLEGLTQVETLGYQRLQDLGATPLKRIWTAGGGAKNAVWQQLRQQAIGVPIAIAPNTEAAFGTARLAAFGLAAFHSAGLKRT,D-ribulose kinase,Exhibits ATP hydrolysis without substrate. Phosphorylates D-ribulose.,Increased ATP hydrolysis in the presence of D-ribulose.,Increased ATP hydrolysis in the presence of D-ribulose.
4172,4172,0,0,P42641-C237R,MKFVDEASILVVAGDGGNGCVSFRREKYIPKGGPDGGDGGDGGDVWMEADENLNTLIDYRFEKSFRAERGQNGASRDCTGKRGKDVTIKVPVGTRVIDQGTGETMGDMTKHGQRLLVAKGGWHGLGNTRFKSSVNRTPRQKTNGTPGDKRELLLELMLLADVGMLGMPNAGKSTFIRAVSAAKPKVADYPFTTLVPSLGVVRMDNEKSFVVADIPGLIEGAAEGAGLGIRFLKHLERCRVLLHLIDIDPIDGTDPVENARIIISELEKYSQDLATKPRWLVFNKIDLLDKVEAEEKAKAIAEALGWEDKYYLISAASGLGVKDLCWDVMTFIIENPVVQAEEAKQPEKVEFMWDDYHRQQLEEIAEEDDEDWDDDWDEDDEEGVEFIYKR,,-1.0,MKFVDEASILVVAGDGGNGCVSFRREKYIPKGGPDGGDGGDGGDVWMEADENLNTLIDYRFEKSFRAERGQNGASRDCTGKRGKDVTIKVPVGTRVIDQGTGETMGDMTKHGQRLLVAKGGWHGLGNTRFKSSVNRTPRQKTNGTPGDKRELLLELMLLADVGMLGMPNAGKSTFIRAVSAAKPKVADYPFTTLVPSLGVVRMDNEKSFVVADIPGLIEGAAEGAGLGIRFLKHLECCRVLLHLIDIDPIDGTDPVENARIIISELEKYSQDLATKPRWLVFNKIDLLDKVEAEEKAKAIAEALGWEDKYYLISAASGLGVKDLCWDVMTFIIENPVVQAEEAKQPEKVEFMWDDYHRQQLEEIAEEDDEDWDDDWDEDDEEGVEFIYKR,GTPase ObgE/CgtA,"An abundant, essential GTPase which binds GTP, GDP and ppGpp with moderate affinity. Has high guanosine nucleotide exchange rate constants for GTP and GDP, and a relatively low GTP hydrolysis rate stimulated by the 50S ribosomal subunit. It is estimated there are 34000 molecules in log-phase cells and 5600 molecules in stationary-phase cells. Required for chromosome segregation. Plays a role in the stringent response, perhaps by sequestering 50S ribosomal subunits and decreasing protein synthesis , and a non-essential role in the late steps of ribosome biogenesis, perhaps acting as a checkpoint for correct 50S subunit synthesis (Probable). Overexpression increases bacterial persistence (in exponential and stationary phase) in response to antibiotics. Cells expressing high levels of Obg are more likely to form persister cells upon antibiotic exposure; this requires alarmone (p)ppGpp and acts via induced HokB, depolarizing cells, which probably reduces metabolic activity and induces persistence. The persister phenotype can be separated from the essential phenotype.Required for correct chromosome partitioning; in temperature-sensitive (ts) mutant nucleoids do not partition but remain in the middle of cell, cells elongate but do not divide. Overexpression protects cells against UV damage. Ts mutants have impaired plasmid and lamdba phage replication, possibly via effects on DnaA. Regulates DnaA levels. Genetic interactions of Val-168 and a C-terminal insertion mutant with the double-strand break repair factors recA and recBCD, and with seqA suggests that ObgE, either directly or indirectly, promotes replication fork stability. May protect replication forks from stress induced by toxic levels of hydroxyl radicals. Initiation of DNA replication continues in ObgE-depleted cells.Binds to pre-50S ribosomal subunits in a salt-dependent manner. Acts as a ribosome anti-association factor; guanosine nucleotides stimulate ObgE 50S subunit binding and also ObgE-mediated 70S ribosome dissociation (GDP<GTP<GMP-PNP<ppGpp). Overexpression rescues an rrmJ deletion stabilizing the 70S ribosome. Even at permissive temperatures the ts mutant (Gln-80/Asn-85) shows disrupted 50S ribosomal subunit assembly, defects in 16 and 23S rRNA processing and altered association of some late-assembling ribosomal proteins. Dissociates from the pre-50S ribosome under conditions of amino acid starvation. The levels of (p)ppGpp rise in the ts mutant (Gln-80/Asn-85), possibly because ObgE controls SpoT. Binds GDP and ppGpp with the same affinity. During ribosome assembly ObgE acts later than the rRNA methyltransferase RrmJ and DEAD-box RNA helicases DeaD and SrmB.","Decreased sensitivity to HU upon overexpression, hinders normal growth, no effect in mazEF/relBE or tonB deletions. The mutant ObgE protein with the substitution displays dominant-positive effects leading to hydroxyurea hypersensitivity when over-expressed. These effects are enabled in strains with a single deletion of the iron transporter TonB or combined deletions of the toxin/antitoxin modules RelBE/MazEF, strains both of which have been shown to be involved in a pathway that inhibits hydroxyl radical formation following hydroxyurea treatment. Moreover, the observed dominant-positive effects are gained in the presence of the hydroxyl radical scavenger thiourea. This suggests that the mutation does not affect the cellular response to replication fork stress and involves hydroxyl radical toxicity.","Decreased sensitivity to HU upon overexpression, hinders normal growth, no effect in mazEF/relBE or tonB deletions. The mutant ObgE protein with the substitution displays dominant-positive effects leading to hydroxyurea hypersensitivity when over-expressed. These effects are enabled in strains with a single deletion of the iron transporter TonB or combined deletions of the toxin/antitoxin modules RelBE/MazEF, strains both of which have been shown to be involved in a pathway that inhibits hydroxyl radical formation following hydroxyurea treatment. Moreover, the observed dominant-positive effects are gained in the presence of the hydroxyl radical scavenger thiourea. This suggests that the mutation does not affect the cellular response to replication fork stress and involves hydroxyl radical toxicity."
4194,4194,0,0,O52793-Q404E,MSSFVVPSLTAVRPRDHHDYADRIALSAATTDGVQMRTEDVRAWIAERRDANVFHVERIPFADLDQWWFEGVTGNLVHRSGRFFTIEGLHVIEHDGPHGDGPYREWQQPVIRQPEVGILGILAKEFDGVLHFLMQAKMEPGNPNLVQLSPTVQATRSNYTKAHGGTNVKLIEYFAPPDPERVIVDVLQAEQGSWFFRKSNRNMIVETVDDVPLWDDFCWLTLGQIAELMHEDETINMNSRSVLSCLPYQDITPRALFSDVQLLSWFTNERSRHDVRVRRIPLADVCGWKQGAEEIEHEDGRYFKVLAVAVKGSNREKISWTQPLVESVDLGVVAFLVRKIDGVPHVLVQARVDGGFLDTVELAPTVQCTPLNYAHLPAEERPPFLDLVQNAPRSRIRYEAIHSEEGGRFLGVRARYLVIDADEAIDPPPGYAWVTPAQLTALTRHGHYVNVEARTLLACINAAAAQPRGGA,,-1.0,MSSFVVPSLTAVRPRDHHDYADRIALSAATTDGVQMRTEDVRAWIAERRDANVFHVERIPFADLDQWWFEGVTGNLVHRSGRFFTIEGLHVIEHDGPHGDGPYREWQQPVIRQPEVGILGILAKEFDGVLHFLMQAKMEPGNPNLVQLSPTVQATRSNYTKAHGGTNVKLIEYFAPPDPERVIVDVLQAEQGSWFFRKSNRNMIVETVDDVPLWDDFCWLTLGQIAELMHEDETINMNSRSVLSCLPYQDITPRALFSDVQLLSWFTNERSRHDVRVRRIPLADVCGWKQGAEEIEHEDGRYFKVLAVAVKGSNREKISWTQPLVESVDLGVVAFLVRKIDGVPHVLVQARVDGGFLDTVELAPTVQCTPLNYAHLPAEERPPFLDLVQNAPRSRIRYEAIHSQEGGRFLGVRARYLVIDADEAIDPPPGYAWVTPAQLTALTRHGHYVNVEARTLLACINAAAAQPRGGA,"dTDP-4-dehydro-6-deoxy-alpha-D-glucopyranose 2,3-dehydratase","Involved in the biosynthesis of the 2,3,6-trideoxysugar L-epivancosamine, the terminal sugar added to the aglycone scaffold of chloroeremomycin, a member of the glycopeptide antibiotics vancomycin family. Catalyzes the removal of the hydroxyl group at position C-2 of the hexose ring of dTDP-4-dehydro-6-deoxy-alpha-D-glucopyranose, and the oxidation of the hydroxyl group at position C-3 to form a carbonyl functionality. The product of the reaction, dTDP-2,6-dideoxy-D-glycero-hex-2-enos-4-ulose, is a highly unstable diketosugar, which spontaneously forms dTDP-3,4-didehydro-2,6-dideoxy-alpha-D-glucose.",Loss of dehydratase activity. This mutation may enhance the function of the active site pocket A in the enzyme.,Loss of dehydratase activity. This mutation may enhance the function of the active site pocket A in the enzyme.
4197,4197,0,0,Q12948-T91I,MQARYSVSSPNSLGVVPYLGGEQSYYRAAAAAAGGGYTAMPAPMSVYSHPAHAEQYPGGMARAYGPYTPQPQPKDMVKPPYSYIALITMAIQNAPDKKITLNGIYQFIMDRFPFYRDNKQGWQNSIRHNLSLNECFVKVPRDDKKPGKGSYWTLDPDSYNMFENGSFLRRRRRFKKKDAVKDKEEKDRLHLKEPPPPGRQPPPAPPEQADGNAPGPQPPPVRIQDIKTENGTCPSPPQPLSPAAALGSGSAAAVPKIESPDSSSSSLSSGSSPPGSLPSARPLSLDGADSAPPPPAPSAPPPHHSQGFSVDNIMTSLRGSPQSAAAELSSGLLASAAASSRAGIAPPLALGAYSPGQSSLYSSPCSQTSSAGSSGGGGGGAGAAGGAGGAGTYHCNLQAMSLYAAGERGGHLQGAPGGAGGSAVDDPLPDYSLPPVTSSSSSSLSHGGGGGGGGGGQEAGHHPAAHQGRLTSWYLNQAGGDLGHLASAAAAAAAAGYPGQQQNFHSVREMFESQRIGLNNSPVNGNSSCQMAFPSSQSLYRTSGAFVYDCSKF,,-1.0,MQARYSVSSPNSLGVVPYLGGEQSYYRAAAAAAGGGYTAMPAPMSVYSHPAHAEQYPGGMARAYGPYTPQPQPKDMVKPPYSYIALITMATQNAPDKKITLNGIYQFIMDRFPFYRDNKQGWQNSIRHNLSLNECFVKVPRDDKKPGKGSYWTLDPDSYNMFENGSFLRRRRRFKKKDAVKDKEEKDRLHLKEPPPPGRQPPPAPPEQADGNAPGPQPPPVRIQDIKTENGTCPSPPQPLSPAAALGSGSAAAVPKIESPDSSSSSLSSGSSPPGSLPSARPLSLDGADSAPPPPAPSAPPPHHSQGFSVDNIMTSLRGSPQSAAAELSSGLLASAAASSRAGIAPPLALGAYSPGQSSLYSSPCSQTSSAGSSGGGGGGAGAAGGAGGAGTYHCNLQAMSLYAAGERGGHLQGAPGGAGGSAVDDPLPDYSLPPVTSSSSSSLSHGGGGGGGGGGQEAGHHPAAHQGRLTSWYLNQAGGDLGHLASAAAAAAAAGYPGQQQNFHSVREMFESQRIGLNNSPVNGNSSCQMAFPSSQSLYRTSGAFVYDCSKF,Forkhead box protein C1,"DNA-binding transcriptional factor that plays a role in a broad range of cellular and developmental processes such as eye, bones, cardiovascular, kidney and skin development. Acts either as a transcriptional activator or repressor. Binds to the consensus binding site 5'-[G/C][A/T]AAA[T/C]AA[A/C]-3' in promoter of target genes. Upon DNA-binding, promotes DNA bending. Acts as a transcriptional coactivator. Stimulates Indian hedgehog (Ihh)-induced target gene expression mediated by the transcription factor GLI2, and hence regulates endochondral ossification. Acts also as a transcriptional coregulator by increasing DNA-binding capacity of GLI2 in breast cancer cells. Regulates FOXO1 through binding to a conserved element, 5'-GTAAACAAA-3' in its promoter region, implicating FOXC1 as an important regulator of cell viability and resistance to oxidative stress in the eye. Cooperates with transcription factor FOXC2 in regulating expression of genes that maintain podocyte integrity. Promotes cell growth inhibition by stopping the cell cycle in the G1 phase through TGFB1-mediated signals. Involved in epithelial-mesenchymal transition (EMT) induction by increasing cell proliferation, migration and invasion. Involved in chemokine CXCL12-induced endothelial cell migration through the control of CXCR4 expression. Plays a role in the gene regulatory network essential for epidermal keratinocyte terminal differentiation. Essential developmental transcriptional factor required for mesoderm-derived tissues, such as the somites, skin, bone and cartilage. Positively regulates CXCL12 and stem cell factor expression in bone marrow mesenchymal progenitor cells, and hence plays a role in the development and maintenance of mesenchymal niches for haematopoietic stem and progenitor cells (HSPC). Plays a role in corneal transparency by preventing both blood vessel and lymphatic vessel growth during embryonic development in a VEGF-dependent manner. Involved in chemokine CXCL12-induced endothelial cell migration through the control of CXCR4 expression. May function as a tumor suppressor.",Increased location at the nucleus; increased transcription regulatory region DNA binding; increased sequence-specific DNA binding transcription factor activity; no change on DNA bending activity. The mutation may resolve local disruptions to the structure of the forkhead domain.,Increased location at the nucleus; increased transcription regulatory region DNA binding; increased sequence-specific DNA binding transcription factor activity; no change on DNA bending activity. The mutation may resolve local disruptions to the structure of the forkhead domain.
4202,4202,0,0,P50336-P450S,MGRTVVVLGGGISGLAASYHLSRAPCPPKVVLVESSERLGGWIRSVRGPNGAIFELGPRGIRPAGALGARTLLLVSELGLDSEVLPVRGDHPAAQNRFLYVGGALHALPTGLRGLLRPSPPFSKPLFWAGLRELTKPRGKEPDETVHSFAQRRLGPEVASLAMDSLCRGVFAGNSRELSIRSCFPSLFQAEQTHRSILLGLLLGAGRTPQPDSALIRQALAERWSQWSLRGGLEMLPQALETHLTSRGVSVLRGQPVCGLSLQAEGRWKVSLRDSSLEADHVISAIPASVLSELLPAEAAPLARALSAITAVSVAVVNLQYQGAHLPVQGFGHLVPSSEDPGVLGIVYDSVAFPEQDGSPPGLRVTVMLGGSWLQTLEASGCVLSQELFQQRAQEAAATQLGLKEMPSHCLVHLHKNCIPQYTLGHWQKLESARQFLTAHRLPLTLAGASYEGVAVNDCIESGRQAAVSVLGTEPNS,,-1.0,MGRTVVVLGGGISGLAASYHLSRAPCPPKVVLVESSERLGGWIRSVRGPNGAIFELGPRGIRPAGALGARTLLLVSELGLDSEVLPVRGDHPAAQNRFLYVGGALHALPTGLRGLLRPSPPFSKPLFWAGLRELTKPRGKEPDETVHSFAQRRLGPEVASLAMDSLCRGVFAGNSRELSIRSCFPSLFQAEQTHRSILLGLLLGAGRTPQPDSALIRQALAERWSQWSLRGGLEMLPQALETHLTSRGVSVLRGQPVCGLSLQAEGRWKVSLRDSSLEADHVISAIPASVLSELLPAEAAPLARALSAITAVSVAVVNLQYQGAHLPVQGFGHLVPSSEDPGVLGIVYDSVAFPEQDGSPPGLRVTVMLGGSWLQTLEASGCVLSQELFQQRAQEAAATQLGLKEMPSHCLVHLHKNCIPQYTLGHWQKLESARQFLTAHRLPLTLAGAPYEGVAVNDCIESGRQAAVSVLGTEPNS,Protoporphyrinogen oxidase,Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX.,"Highly increases enzyme activity. The mutation in hPPO causes no functional changes in the protein. The mutation consisted of a previously unreported C to T transition in exon 13 of the PPO gene, resulting in the substitution of a non-polar proline by a polar serine. This proline residue is evolutionarily highly conserved in man, mouse, and Bacillus subtilis, attesting to the insignificance of this residue.","Highly increases enzyme activity. The mutation in hPPO causes no functional changes in the protein. The mutation consisted of a previously unreported C to T transition in exon 13 of the PPO gene, resulting in the substitution of a non-polar proline by a polar serine. This proline residue is evolutionarily highly conserved in man, mouse, and Bacillus subtilis, attesting to the insignificance of this residue."
4212,4212,0,0,Q15726-K115N,MNSLVSWQLLLFLCATHFGEPLEKVASVGNSRPTGQQLESLGLLAPGEQSLPCTERKPAATARLSRRGTSLSPPPESSGSPQQPGLSAPHSRQIPAPQGAVLVQREKDLPNYNWNSFGLRFGKREAAPGNHGRSAGRG,,-1.0,MNSLVSWQLLLFLCATHFGEPLEKVASVGNSRPTGQQLESLGLLAPGEQSLPCTERKPAATARLSRRGTSLSPPPESSGSPQQPGLSAPHSRQIPAPQGAVLVQREKDLPNYNWKSFGLRFGKREAAPGNHGRSAGRG,Metastasis-suppressor KiSS-1,"Metastasis suppressor protein in malignant melanomas and in some breast cancers. May regulate events downstream of cell-matrix adhesion, perhaps involving cytoskeletal reorganization. Generates a C-terminally amidated peptide, metastin which functions as the endogenous ligand of the G-protein coupled receptor GPR54. Activation of the receptor inhibits cell proliferation and cell migration, key characteristics of tumor metastasis. Kp-10 is a decapeptide derived from the primary translation product, isolated in conditioned medium of first trimester trophoblast. Kp-10, but not other kisspeptins, increased intracellular Ca(2+) levels in isolated first trimester trophoblasts. Kp-10 is a paracrine/endocrine regulator in fine-tuning trophoblast invasion generated by the trophoblast itself. The receptor is also essential for normal gonadotropin-released hormone physiology and for puberty. The hypothalamic KiSS1/GPR54 system is a pivotal factor in central regulation of the gonadotropic axis at puberty and in adulthood.","Significantly increased efficacy as well as potency. Activating mutation in KISS1 in a large consanguineous family that results in success of pubertal progression, indicating that functional kisspeptin is important for puberty and reproduction in humans.","Significantly increased efficacy as well as potency. Activating mutation in KISS1 in a large consanguineous family that results in success of pubertal progression, indicating that functional kisspeptin is important for puberty and reproduction in humans."
4232,4232,0,0,P0DP25-K141E,MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAK,,-1.0,MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEKFVQMMTAK,Calmodulin-3,"Calmodulin acts as part of a calcium signal transduction pathway by mediating the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Calcium-binding is required for the activation of calmodulin. Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases, such as myosin light-chain kinases and calmodulin-dependent protein kinase type II (CaMK2), and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis.",Increases in LQT16; gain-of-function variant causing enhanced negative regulation of high voltage-gated calcium channel activity; enhanced regulation of cardiac muscle cell action potential; increased calcium ion binding. The mutation in calmodulin is associated with congenital arrhythmia resistance (calmodulinopathy).,Increases in LQT16; gain-of-function variant causing enhanced negative regulation of high voltage-gated calcium channel activity; enhanced regulation of cardiac muscle cell action potential; increased calcium ion binding. The mutation in calmodulin is associated with congenital arrhythmia resistance (calmodulinopathy).
4237,4237,0,0,P9WPA3-S368C,MLRIGLTGGIGAGKSLLSTTFSQCGGIVVDGDVLAREVVQPGTEGLASLVDAFGRDILLADGALDRQALAAKAFRDDESRGVLNGIVHPLVARRRSEIIAAVSGDAVVVEDIPLLVESGMAPLFPLVVVVHADVELRVRRLVEQRGMAEADARARIAAQASDQQRRAVADVWLDNSGSPEDLVRRARDVWNTRVQPFAHNLAQRQIARAPARLVPADPSWPDQARRIVNRLKIACGHKALRVDHIGSTAVSGFPDFLAKDVIDIQVTVESLDVADELAEPLLAAGYPRLEHITQDTEKTDARSTVGRYDHTDSAALWHKRVHASADPGRPTNVHLRVHGWPNQQFALLFVDWLAANPGAREDYLTVKCDADRRADGELARYVTAKEPWFLDAYQRAWEWADAVHWRP,,-1.0,MLRIGLTGGIGAGKSLLSTTFSQCGGIVVDGDVLAREVVQPGTEGLASLVDAFGRDILLADGALDRQALAAKAFRDDESRGVLNGIVHPLVARRRSEIIAAVSGDAVVVEDIPLLVESGMAPLFPLVVVVHADVELRVRRLVEQRGMAEADARARIAAQASDQQRRAVADVWLDNSGSPEDLVRRARDVWNTRVQPFAHNLAQRQIARAPARLVPADPSWPDQARRIVNRLKIACGHKALRVDHIGSTAVSGFPDFLAKDVIDIQVTVESLDVADELAEPLLAAGYPRLEHITQDTEKTDARSTVGRYDHTDSAALWHKRVHASADPGRPTNVHLRVHGWPNQQFALLFVDWLAANPGAREDYLTVKSDADRRADGELARYVTAKEPWFLDAYQRAWEWADAVHWRP,Dephospho-CoA kinase,"Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A. Can also use dATP, with lower efficiency, but cannot use GTP, dGTP or CTP.","Increases oligomerization. The organism has evolved a second layer of regulation by employing a dynamic equilibrium between the trimeric and monomeric forms of CoaE as a means of regulating the effective concentration of active enzyme. We show that the monomer is the active form of the enzyme and the interplay between the regulator, CTP and the substrate, DCoA, affects enzymatic activity.","Increases oligomerization. The organism has evolved a second layer of regulation by employing a dynamic equilibrium between the trimeric and monomeric forms of CoaE as a means of regulating the effective concentration of active enzyme. We show that the monomer is the active form of the enzyme and the interplay between the regulator, CTP and the substrate, DCoA, affects enzymatic activity."
4245,4245,0,0,Q03818-A102E,MGNFIITERKKAKEERSNPQTDSMDDLLIRRLTDRNDKEAHLNELFQDNSGAIGGNIVSHDDALLNTLAILQKELKSKEQEIRRLKEVIALKNKNTERLNDELISGTIENNVLQQKLSDLKKEHSQLVARWLKKTEKETEAMNSEIDGTK,,-1.0,MGNFIITERKKAKEERSNPQTDSMDDLLIRRLTDRNDKEAHLNELFQDNSGAIGGNIVSHDDALLNTLAILQKELKSKEQEIRRLKEVIALKNKNTERLNDALISGTIENNVLQQKLSDLKKEHSQLVARWLKKTEKETEAMNSEIDGTK,Autophagy protein 16,"Stabilizes the ATG5-ATG12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The ATG5-ATG12/ATG16 complex is required for efficient promotion of ATG8-conjugation to phosphatidylethanolamine and ATG8 localization to the pre-autophagosomal structure (PAS). Recruits also ATG3 to the PAS. Involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress.",Significantly increases autophagic activity; when associated with A-101. The mutation in the Atg16 protein has been shown to be crucial for autophagy.,Significantly increases autophagic activity; when associated with A-101. The mutation in the Atg16 protein has been shown to be crucial for autophagy.
4277,4277,0,0,Q13642-R209C,MAEKFDCHYCRDPLQGKKYVQKDGHHCCLKCFDKFCANTCVECRKPIGADSKEVHYKNRFWHDTCFRCAKCLHPLANETFVAKDNKILCNKCTTREDSPKCKGCFKAIVAGDQNVEYKGTVWHKDCFTCSNCKQVIGTGSFFPKGEDFYCVTCHETKFAKHCVKCNKAITSGGITYQDQPWHADCFVCVTCSKKLAGQRFTAVEDQYYCVDCYKNFVAKKCAGCKNPITGKRTVSRVSHPVSKARKPPVCHGKRLPLTLFPSANLRGRHPGGERTCPSWVVVLYRKNRSLAAPRGPGLVKAPVWWPMKDNPGTTTASTAKNAP,,-1.0,MAEKFDCHYCRDPLQGKKYVQKDGHHCCLKCFDKFCANTCVECRKPIGADSKEVHYKNRFWHDTCFRCAKCLHPLANETFVAKDNKILCNKCTTREDSPKCKGCFKAIVAGDQNVEYKGTVWHKDCFTCSNCKQVIGTGSFFPKGEDFYCVTCHETKFAKHCVKCNKAITSGGITYQDQPWHADCFVCVTCSKKLAGQRFTAVEDQYYRVDCYKNFVAKKCAGCKNPITGKRTVSRVSHPVSKARKPPVCHGKRLPLTLFPSANLRGRHPGGERTCPSWVVVLYRKNRSLAAPRGPGLVKAPVWWPMKDNPGTTTASTAKNAP,Four and a half LIM domains protein 1,May have an involvement in muscle development or hypertrophy.,"Decreases EDMD6. The FHL1 gene identified seven mutations, in the proximal exons of FHL1 in these families, three additional families, and one isolated case, which similarly affect the three FHL1 protein isoforms: two missense mutations affecting rarely conserved cysteines. A old missense mutation within the third LIM domain that replaces a rarely conserved cysteine by an arginine","Decreases EDMD6. The FHL1 gene identified seven mutations, in the proximal exons of FHL1 in these families, three additional families, and one isolated case, which similarly affect the three FHL1 protein isoforms: two missense mutations affecting rarely conserved cysteines. A old missense mutation within the third LIM domain that replaces a rarely conserved cysteine by an arginine"
4288,4288,0,0,P20398-S585C,MSLQQLKRKSLRDGWLMDGVVPSPGAEIDSPLFQTESKIQQLEKELESLQMQQLRLENPAAVQPEAKAIQTPFLNGEKIQQGGGQAGDAKEVTAGQANNTHGIIHEEQPTKEDQDMGTVLPIPAPRGKTVPKEDENQANPELKVDMEHQKVELVDLIQECPVENQTVEHVEKNKPHLDQEHTEKNQDGQHGILEFLTQDQQLGNPNLQHLDRYLITEVTVKHFEKNQAHPGQEKNQDEQHGILKYLTQDQQNENPNLGHLDQYLITEITLQSNPLENISVHDQTQSTSDQNMETKLPTDIPQQKESQSEGKIQTKDQGPEFELLYKDHSHEKGTTDQTQHQELLPSSIEPKEENPKAQDEKLDHHNESVSTVHEQKEVHDMDPRQLSTHQKSLSISEDQNQGSVSLSDPQNQDQSLALPEKGLEETPQLNLSHEVQCEEPSLMEQISISLLQSMEQNQEGADQTPKSVALEELSELLSSDMIKQSVLLSKNLEESPSTASTEETQETMCQAVIIPDLKKENSDPEVVQESSSHEPMSSTIAQSSSAEGNSSPESRPLLQKSQGTDSQQGGNTATQQEERRKKKTCQCCVVM,,-1.0,MSLQQLKRKSLRDGWLMDGVVPSPGAEIDSPLFQTESKIQQLEKELESLQMQQLRLENPAAVQPEAKAIQTPFLNGEKIQQGGGQAGDAKEVTAGQANNTHGIIHEEQPTKEDQDMGTVLPIPAPRGKTVPKEDENQANPELKVDMEHQKVELVDLIQECPVENQTVEHVEKNKPHLDQEHTEKNQDGQHGILEFLTQDQQLGNPNLQHLDRYLITEVTVKHFEKNQAHPGQEKNQDEQHGILKYLTQDQQNENPNLGHLDQYLITEITLQSNPLENISVHDQTQSTSDQNMETKLPTDIPQQKESQSEGKIQTKDQGPEFELLYKDHSHEKGTTDQTQHQELLPSSIEPKEENPKAQDEKLDHHNESVSTVHEQKEVHDMDPRQLSTHQKSLSISEDQNQGSVSLSDPQNQDQSLALPEKGLEETPQLNLSHEVQCEEPSLMEQISISLLQSMEQNQEGADQTPKSVALEELSELLSSDMIKQSVLLSKNLEESPSTASTEETQETMCQAVIIPDLKKENSDPEVVQESSSHEPMSSTIAQSSSAEGNSSPESRPLLQKSQGTDSQQGGNTATQQEERRKKKTSQCCVVM,Paralemmin-3,"Maternal ATP-binding protein that may have multiple functions during development, one of which may be associated with the development and maintenance of the central nervous system.",Strongly enhances membrane association. Mutation of the upstream cysteine (C585) promotes the association of xlcaax-1 with the membrane.,Strongly enhances membrane association. Mutation of the upstream cysteine (C585) promotes the association of xlcaax-1 with the membrane.
4313,4313,0,0,Q383Q5-A53K,MLRRVGRTTCSPAACQLRHTTILSVRKGDTVVLLGDRQVTLGERIVAKSSACKLRRINDDVVIGFAGSTADAISLMEKLENKIGEFPNQLTRAAVELAKEWRTDRALRRLEASLIVCSAEETLEIDGQGNVITPEADGIVAIGSGGTFAKAAARALIDVDGYDAEKIARKAMRIATDIDVFSNEHWDVEVLKRKSEKQEGSEASAKTSE,,-1.0,MLRRVGRTTCSPAACQLRHTTILSVRKGDTVVLLGDRQVTLGERIVAKSSACALRRINDDVVIGFAGSTADAISLMEKLENKIGEFPNQLTRAAVELAKEWRTDRALRRLEASLIVCSAEETLEIDGQGNVITPEADGIVAIGSGGTFAKAAARALIDVDGYDAEKIARKAMRIATDIDVFSNEHWDVEVLKRKSEKQEGSEASAKTSE,ATP-dependent protease subunit HslV,Protease subunit of a proteasome-like degradation complex. HslU recognizes protein substrates and unfolds these before guiding them to HslV for hydrolysis. HslV is not believed to degrade folded proteins. The HslVU protease complex functions in mitochondrial DNA replication by regulating DNA helicase PIF2 protein levels.,Strongly enhances peptidase activity.,Strongly enhances peptidase activity.
4327,4327,0,0,Q9H7X0-A38Y,MTEVVPSSALSEVSLRLLCHDDIDTVKHLCGDWFPIEYPDSWYRDITSNKKFFSLAATYRGAIVGMIVAEIKNRTKIHKEDGDILASNFSVDTQVAYILSLGVVKEFRKHGIGSLLLESLKDHISTTAQDHCKAIYLHVLTTNNTAINFYENRDFKQHHYLPYYYSIRGVLKDGFTYVLYINGGHPPWTILDYIQHLGSALASLSPCSIPHRVYRQAHSLLCSFLPWSGISSKSGIEYSRTM,,-1.0,MTEVVPSSALSEVSLRLLCHDDIDTVKHLCGDWFPIEAPDSWYRDITSNKKFFSLAATYRGAIVGMIVAEIKNRTKIHKEDGDILASNFSVDTQVAYILSLGVVKEFRKHGIGSLLLESLKDHISTTAQDHCKAIYLHVLTTNNTAINFYENRDFKQHHYLPYYYSIRGVLKDGFTYVLYINGGHPPWTILDYIQHLGSALASLSPCSIPHRVYRQAHSLLCSFLPWSGISSKSGIEYSRTM,N-alpha-acetyltransferase 60,"N-alpha-acetyltransferase that specifically mediates the acetylation of N-terminal residues of the transmembrane proteins, with a strong preference for N-termini facing the cytosol. Displays N-terminal acetyltransferase activity towards a range of N-terminal sequences including those starting with Met-Lys, Met-Val, Met-Ala and Met-Met. Required for normal chromosomal segregation during anaphase. May also show histone acetyltransferase activity; such results are however unclear in vivo and would require additional experimental evidences.",Highly increased acetyltransferase activity.,Highly increased acetyltransferase activity.
4344,4344,0,0,P0AFF0-R217K,MTITPQNLIALLPLLIVGLTVVVVMLSIAWRRNHFLNATLSVIGLNAALVSLWFVGQAGAMDVTPLMRVDGFAMLYTGLVLLASLATCTFAYPWLEGYNDNKDEFYLLVLIAALGGILLANANHLASLFLGIELISLPLFGLVGYAFRQKRSLEASIKYTILSAAASSFLLFGMALVYAQSGDLSFVALGKNLGDGMLNEPLLLAGFGLMIVGLGFKLSLVPFHLWTPDVYQGAPAPVSTFLATASKIAIFGVVMRLFLYAPVGDSEAIRVVLAIIAFASIIFGNLMALSQTNIKRLLGYSSISHLGYLLVALIALQTGEMSMEAVGVYLAGYLFSSLGAFGVVSLMSSPYRGPDADSLFSYRGLFWHRPILAAVMTVMMLSLAGIPMTLGFIGKFYVLAVGVQAHLWWLVGAVVVGSAIGLYYYLRVAVSLYLHAPEQPGRDAPSNWQYSAGGIVVLISALLVLVLGVWPQPLISIVRLAMPLM,,-1.0,MTITPQNLIALLPLLIVGLTVVVVMLSIAWRRNHFLNATLSVIGLNAALVSLWFVGQAGAMDVTPLMRVDGFAMLYTGLVLLASLATCTFAYPWLEGYNDNKDEFYLLVLIAALGGILLANANHLASLFLGIELISLPLFGLVGYAFRQKRSLEASIKYTILSAAASSFLLFGMALVYAQSGDLSFVALGKNLGDGMLNEPLLLAGFGLMIVGLGFRLSLVPFHLWTPDVYQGAPAPVSTFLATASKIAIFGVVMRLFLYAPVGDSEAIRVVLAIIAFASIIFGNLMALSQTNIKRLLGYSSISHLGYLLVALIALQTGEMSMEAVGVYLAGYLFSSLGAFGVVSLMSSPYRGPDADSLFSYRGLFWHRPILAAVMTVMMLSLAGIPMTLGFIGKFYVLAVGVQAHLWWLVGAVVVGSAIGLYYYLRVAVSLYLHAPEQPGRDAPSNWQYSAGGIVVLISALLVLVLGVWPQPLISIVRLAMPLM,NADH-quinone oxidoreductase subunit N,"NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.","Shows 40% more than the wild-type rate of deamino-NADH oxidase. The mutant with the substitution had a rate of deamino-NADH oxidase activity that was no less than 50% of that of the wild type and had an increased rate of proton translocation. It also showed reduced inhibition by decylubiquinone, indicating that subunit N interacts with quinones.","Shows 40% more than the wild-type rate of deamino-NADH oxidase. The mutant with the substitution had a rate of deamino-NADH oxidase activity that was no less than 50% of that of the wild type and had an increased rate of proton translocation. It also showed reduced inhibition by decylubiquinone, indicating that subunit N interacts with quinones."
4348,4348,0,0,P39006-P488G,MSIMPVKNALAQGRTLLMGRMPAVKFSTRMQLRNRTAVLWNRKFSTRLFVQQRRSSGEIVDRAKAAAANSGRKQVSMKWVVLTSFTIVLGTILLVSRNDSTEEDATEGKKGRRTRKIKIFNNNWLFFCYSTLPLNAMSRLWGQVNSLTLPIWVRPWGYRLYSFLFGVNLDEMEDPDLTHYANLSEFFYRNIKPGTRPVAQGEDVIASPSDGKILQVGIINSETGEIEQVKGMTYSIKEFLGTHSHPLMSKSASSLDLTSDEEKHREFARVNRIQLAGSEDTEQPLLNFKNEGDQSVREFKPSVSKNIHLLSQLSLNYFSNGFSCSEPHDTELFFAVIYLAPGDYHHFHSPVDWVCKVRRHFPGDLFSVAPYFQRNFPNLFVLNERVALLGSWKYGFFSMTPVGATNVGSIKLNFDQEFVTNSKSDKHLEPHTCYQAVYENASKILGGMPLVKGEEMGGFELGSTVVLCFEAPTEFKFDVRVGDKVKMGQKLGIIGKNDLK,,-1.0,MSIMPVKNALAQGRTLLMGRMPAVKFSTRMQLRNRTAVLWNRKFSTRLFVQQRRSSGEIVDRAKAAAANSGRKQVSMKWVVLTSFTIVLGTILLVSRNDSTEEDATEGKKGRRTRKIKIFNNNWLFFCYSTLPLNAMSRLWGQVNSLTLPIWVRPWGYRLYSFLFGVNLDEMEDPDLTHYANLSEFFYRNIKPGTRPVAQGEDVIASPSDGKILQVGIINSETGEIEQVKGMTYSIKEFLGTHSHPLMSKSASSLDLTSDEEKHREFARVNRIQLAGSEDTEQPLLNFKNEGDQSVREFKPSVSKNIHLLSQLSLNYFSNGFSCSEPHDTELFFAVIYLAPGDYHHFHSPVDWVCKVRRHFPGDLFSVAPYFQRNFPNLFVLNERVALLGSWKYGFFSMTPVGATNVGSIKLNFDQEFVTNSKSDKHLEPHTCYQAVYENASKILGGMPLVKGEEMGGFELGSTVVLCFEAPTEFKFDVRVGDKVKMPQKLGIIGKNDLK,"Phosphatidylserine decarboxylase proenzyme 1, mitochondrial",Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine. Phosphatidylethanolamine formed in the mitochondria is exported to other membranes to fullfill their requirements for PtdEtn. Required for normal mitochondrial morphology and proper mitochondrial fusion during yeast mating. Involved in lipid droplet biogenesis at the endoplasmic reticulum membrane. Required for induction of mitophagy during nitrogen starvation. Appears to play a specific role in supporting respiratory complex III activity.,"Increase in autocatalytic processing and leads to protein synthesis. Complete gain of activity. Growth on the fermentable carbon source galactose is severely increased. Mutations in this motif affect processing and stability of Psd1p, and consequently the enzyme's activity. Thus, we conclude that this consensus motif is nonessential for structural integrity and processing of Psd1p.","Increase in autocatalytic processing and leads to protein synthesis. Complete gain of activity. Growth on the fermentable carbon source galactose is severely increased. Mutations in this motif affect processing and stability of Psd1p, and consequently the enzyme's activity. Thus, we conclude that this consensus motif is nonessential for structural integrity and processing of Psd1p."
4382,4382,0,0,P60484-A124C,MTAIIKEIVSRNKRRYQEDGFDLDLTYIYPNIIAMGFPAERLEGVYRNNIDDVVRFLDSKHKNHYKIYNLCAERHYDTAKFNCRVAQYPFEDHNPPQLELIKPFCEDLDQWLSEDDNHVAAIHCKAGKGRTGVMICAYLLHRGKFLKAQEALDFYGEVRTRDKKGVTIPSQRRYVYYYSYLLKNHLDYRPVALLFHKMMFETIPMFSGGTCNPQFVVCQLKVKIYSSNSGPTRREDKFMYFEFPQPLPVCGDIKVEFFHKQNKMLKKDKMFHFWVNTFFIPGPEETSEKVENGSLCDQEIDSICSIERADNDKEYLVLTLTKNDLDKANKDKANRYFSPNFKVKLYFTKTVEEPSNPEASSSTSVTPDVSDNEPDHYRYSDTTDSDPENEPFDEDQHTQITKV,,-1.0,MTAIIKEIVSRNKRRYQEDGFDLDLTYIYPNIIAMGFPAERLEGVYRNNIDDVVRFLDSKHKNHYKIYNLCAERHYDTAKFNCRVAQYPFEDHNPPQLELIKPFCEDLDQWLSEDDNHVAAIHAKAGKGRTGVMICAYLLHRGKFLKAQEALDFYGEVRTRDKKGVTIPSQRRYVYYYSYLLKNHLDYRPVALLFHKMMFETIPMFSGGTCNPQFVVCQLKVKIYSSNSGPTRREDKFMYFEFPQPLPVCGDIKVEFFHKQNKMLKKDKMFHFWVNTFFIPGPEETSEKVENGSLCDQEIDSICSIERADNDKEYLVLTLTKNDLDKANKDKANRYFSPNFKVKLYFTKTVEEPSNPEASSSTSVTPDVSDNEPDHYRYSDTTDSDPENEPFDEDQHTQITKV,"Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN","Acts as a dual-specificity protein phosphatase, dephosphorylating tyrosine-, serine- and threonine-phosphorylated proteins. Also acts as a lipid phosphatase, removing the phosphate in the D3 position of the inositol ring from phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 3,4-diphosphate, phosphatidylinositol 3-phosphate and inositol 1,3,4,5-tetrakisphosphate with order of substrate preference in vitro PtdIns(3,4,5)P3 > PtdIns(3,4)P2 > PtdIns3P > Ins(1,3,4,5)P4. Tumor suppressor, the lipid phosphatase activity is critical for its tumor suppressor function. Antagonizes the PI3K-AKT/PKB signaling pathway by dephosphorylating phosphoinositides and thereby modulating cell cycle progression and cell survival. The unphosphorylated form cooperates with MAGI2 to suppress AKT1 activation. In motile cells, suppresses the formation of lateral pseudopods and thereby promotes cell polarization and directed movement. Dephosphorylates tyrosine-phosphorylated focal adhesion kinase and inhibits cell migration and integrin-mediated cell spreading and focal adhesion formation. Required for growth factor-induced epithelial cell migration; growth factor stimulation induces PTEN phosphorylation which changes its binding preference from the p85 regulatory subunit of the PI3K kinase complex to DLC1 and results in translocation of the PTEN-DLC1 complex to the posterior of migrating cells to promote RHOA activation. Meanwhile, TNS3 switches binding preference from DLC1 to p85 and the TNS3-p85 complex translocates to the leading edge of migrating cells to activate RAC1 activation. Plays a role as a key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation (By similarity). Involved in the regulation of synaptic function in excitatory hippocampal synapses. Recruited to the postsynaptic membrane upon NMDA receptor activation, is required for the modulation of synaptic activity during plasticity. Enhancement of lipid phosphatase activity is able to drive depression of AMPA receptor-mediated synaptic responses, activity required for NMDA receptor-dependent long-term depression (LTD) (By similarity). May be a negative regulator of insulin signaling and glucose metabolism in adipose tissue. The nuclear monoubiquitinated form possesses greater apoptotic potential, whereas the cytoplasmic nonubiquitinated form induces less tumor suppressive ability.",Increases protein phosphatase activity. Able to inhibit focal adhesion formation.,Increases protein phosphatase activity. Able to inhibit focal adhesion formation.
4390,4390,0,0,O65041-A215C,MADLDVPPQVPQSKTRDLDKLLLRHGNLVDPGFVPGPGLRDDIRDYVRILVIGAGGLGCELLKDLALSGFRNLEVIDMDRIEVTNLNRQFLFRIEDVGKPKAEVAAKRVMERVSGVEIVPHFSRIEDKEIEFYNDFNIIALGLDSIEARKYINGVACGFLEYNEDDTPKRETIKPMVDGGTEGFKGHARVILPGVTPCFECTIYLFPPQVKFPLCTLAETPRNAAHCIEYAHLIQWETVHRGKTFDPDEPEHMKWVYDEAIRRAELFGIPGVTYSLTQGVVKNIIPAIASTNAIISAACALETLKIVSACSKTLVNYLTYNGGEGLYTEVTKFERDTECLVCGPGILIELDTSVTLSKFIEMLEDHPKLLLSKASVKQGENTLYMQAPPVLEEFHRPKLSKPLYDLMGRVQKDTIHVFGQRALKNNEKESCTTKVRVVFKGADGVADMDTAIGA,,-1.0,MADLDVPPQVPQSKTRDLDKLLLRHGNLVDPGFVPGPGLRDDIRDYVRILVIGAGGLGCELLKDLALSGFRNLEVIDMDRIEVTNLNRQFLFRIEDVGKPKAEVAAKRVMERVSGVEIVPHFSRIEDKEIEFYNDFNIIALGLDSIEARKYINGVACGFLEYNEDDTPKRETIKPMVDGGTEGFKGHARVILPGVTPCFECTIYLFPPQVKFPLATLAETPRNAAHCIEYAHLIQWETVHRGKTFDPDEPEHMKWVYDEAIRRAELFGIPGVTYSLTQGVVKNIIPAIASTNAIISAACALETLKIVSACSKTLVNYLTYNGGEGLYTEVTKFERDTECLVCGPGILIELDTSVTLSKFIEMLEDHPKLLLSKASVKQGENTLYMQAPPVLEEFHRPKLSKPLYDLMGRVQKDTIHVFGQRALKNNEKESCTTKVRVVFKGADGVADMDTAIGA,NEDD8-activating enzyme E1 catalytic subunit,"Catalytic subunit of the dimeric ECR1-AXR1 E1 enzyme. E1 activates NEDD8/RUB1 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a NEDD8-ECR1 thioester and free AMP. E1 finally transfers NEDD8 to the catalytic cysteine of RCE1.",Enables binding to RUB1. The mutation in the AXR1 protein leads to a gain of function in the ubiquitin-activating enzyme E1 activity. This mutation enhances the normal response to the plant hormone auxin in Arabidopsis thaliana.,Enables binding to RUB1. The mutation in the AXR1 protein leads to a gain of function in the ubiquitin-activating enzyme E1 activity. This mutation enhances the normal response to the plant hormone auxin in Arabidopsis thaliana.
4394,4394,0,0,Q13351-R334T,MATAETALPSISTLTALGPFPDTQDDFLKWWRSEEAQDMGPGPPDPTEPPLHVKSEDQPGEEEDDERGADATWDLDLLLTNFSGPEPGGAPQTCALAPSEASGAQYPPPPETLGAYAGGPGLVAGLLGSEDHSGWVRPALRARAPDAFVGPALAPAPAPEPKALALQPVYPGPGAGSSGGYFPRTGLSVPAASGAPYGLLSGYPAMYPAPQYQGHFQLFRGLQGPAPGPATSPSFLSCLGPGTVGTGLGGTAEDPGVIAETAPSKRGRRSWARKRQAAHTCAHPGCGKSYTKSSHLKAHLRTHTGEKPYACTWEGCGWRFARSDELTRHYRKHTGQRPFRCQLCPRAFSRSDHLALHMKRHL,,-1.0,MATAETALPSISTLTALGPFPDTQDDFLKWWRSEEAQDMGPGPPDPTEPPLHVKSEDQPGEEEDDERGADATWDLDLLLTNFSGPEPGGAPQTCALAPSEASGAQYPPPPETLGAYAGGPGLVAGLLGSEDHSGWVRPALRARAPDAFVGPALAPAPAPEPKALALQPVYPGPGAGSSGGYFPRTGLSVPAASGAPYGLLSGYPAMYPAPQYQGHFQLFRGLQGPAPGPATSPSFLSCLGPGTVGTGLGGTAEDPGVIAETAPSKRGRRSWARKRQAAHTCAHPGCGKSYTKSSHLKAHLRTHTGEKPYACTWEGCGWRFARSDELTRHYRKHRGQRPFRCQLCPRAFSRSDHLALHMKRHL,Krueppel-like factor 1,"Transcription regulator of erythrocyte development that probably serves as a general switch factor during erythropoiesis. Is a dual regulator of fetal-to-adult globin switching. Binds to the CACCC box in the beta-globin gene promoter and acts as a preferential activator of this gene. Furthermore, it binds to the BCL11A promoter and activates expression of BCL11A, which in turn represses the HBG1 and HBG2 genes. This dual activity ensures that, in most adults, fetal hemoglobin levels are low. Able to activate CD44 and AQP1 promoters. When sumoylated, acts as a transcriptional repressor by promoting interaction with CDH2/MI2beta and also represses megakaryocytic differentiation.","Decreased production of HbF, which exacerbates the clinical severity of β-thalassemia.","Decreased production of HbF, which exacerbates the clinical severity of β-thalassemia."
4405,4405,0,0,P28737-A73E,MSRKFDLKTITDLSVLVGTGISLYYLVSRLLNDVESGPLSGKSRESKAKQSLQWEKLVKRSPALAEVTLDAYERTILSSIVTPDEINITFQDIGGLDPLISDLHESVIYPLMMPEVYSNSPLLQAPSGVLLYGPPGCGKTMLAKALAKESGANFISIRMSSIMDKWYGESNKIVDAMFSLANKLQPCIIFIDEIDSFLRERSSTDHEVTATLKAEFMTLWDGLLNNGRVMIIGATNRINDIDDAFLRRLPKRFLVSLPGSDQRYKILSVLLKDTKLDEDEFDLQLIADNTKGFSGSDLKELCREAALDAAKEYIKQKRQLIDSGTIDVNDTSSLKIRPLKTKDFTKKLRMDATSTLSSQPLD,,-1.0,MSRKFDLKTITDLSVLVGTGISLYYLVSRLLNDVESGPLSGKSRESKAKQSLQWEKLVKRSPALAEVTLDAYARTILSSIVTPDEINITFQDIGGLDPLISDLHESVIYPLMMPEVYSNSPLLQAPSGVLLYGPPGCGKTMLAKALAKESGANFISIRMSSIMDKWYGESNKIVDAMFSLANKLQPCIIFIDEIDSFLRERSSTDHEVTATLKAEFMTLWDGLLNNGRVMIIGATNRINDIDDAFLRRLPKRFLVSLPGSDQRYKILSVLLKDTKLDEDEFDLQLIADNTKGFSGSDLKELCREAALDAAKEYIKQKRQLIDSGTIDVNDTSSLKIRPLKTKDFTKKLRMDATSTLSSQPLD,Outer mitochondrial transmembrane helix translocase,"Outer mitochondrial translocase required to remove mislocalized tail-anchored transmembrane proteins on mitochondria. Specifically recognizes and binds exposed hydrophobic surfaces of mistargeted tail-anchored transmembrane proteins. Acts as a dislocase that mediates the ATP-dependent extraction of mistargeted tail-anchored transmembrane proteins from the mitochondrion outer membrane. Able to unfold protein substrates by processive threading through its central pore. Once extracted from the mitochondrion outer membrane, substrate proteins are then transferred to the endoplasmic reticulum, where they are ubiquitinated and degraded by the proteasome. Also mediates extraction of excess tail-anchored proteins from the peroxisomal membrane. In normal conditions, MSP1 translocase activity is inhibited by PEX3 at peroxisomes; only catalyzes removal of excess tail-anchored proteins.",Enhanced ability to extract tail-anchored proteins from membranes. Does not affect formation of a homohexamer.,Enhanced ability to extract tail-anchored proteins from membranes. Does not affect formation of a homohexamer.
4414,4414,0,0,P0A825-G216P,MLKREMNIADYDAELWQAMEQEKVRQEEHIELIASENYTSPRVMQAQGSQLTNKYAEGYPGKRYYGGCEYVDIVEQLAIDRAKELFGADYANVQPHSGSQANFAVYTALLEPGDTVLGMNLAHGGHLTHGSPVNFSGKLYNIVPYGIDATGHIDYADLEKQAKEHKPKMIIGGFSAYSGVVDWAKMREIADSIGAYLFVDMAHVAGLVAAGVYPNPVPHAHVVTTTTHKTLAGPRGGLILAKGGSEELYKKLNSAVFPGGQGGPLMHVIAGKAVALKEAMEPEFKTYQQQVAKNAKAMVEVFLERGYKVVSGGTDNHLFLVDLVDKNLTGKEADAALGRANITVNKNSVPNDPKSPFVTSGIRVGTPAITRRGFKEAEAKELAGWMCDVLDSINDEAVIERIKGKVLDICARYPVYA,,-1.0,MLKREMNIADYDAELWQAMEQEKVRQEEHIELIASENYTSPRVMQAQGSQLTNKYAEGYPGKRYYGGCEYVDIVEQLAIDRAKELFGADYANVQPHSGSQANFAVYTALLEPGDTVLGMNLAHGGHLTHGSPVNFSGKLYNIVPYGIDATGHIDYADLEKQAKEHKPKMIIGGFSAYSGVVDWAKMREIADSIGAYLFVDMAHVAGLVAAGVYPNGVPHAHVVTTTTHKTLAGPRGGLILAKGGSEELYKKLNSAVFPGGQGGPLMHVIAGKAVALKEAMEPEFKTYQQQVAKNAKAMVEVFLERGYKVVSGGTDNHLFLVDLVDKNLTGKEADAALGRANITVNKNSVPNDPKSPFVTSGIRVGTPAITRRGFKEAEAKELAGWMCDVLDSINDEAVIERIKGKVLDICARYPVYA,Serine hydroxymethyltransferase,"Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. Thus, is able to catalyze the cleavage of allothreonine and 3-phenylserine. Also catalyzes the irreversible conversion of 5,10-methenyltetrahydrofolate to 5-formyltetrahydrofolate.",Important increase in affinity and catalytic efficiency. Greatly improved in folding into a catalytically competent enzyme. The mutant was greatly improved in folding into a catalytically competent enzyme.,Important increase in affinity and catalytic efficiency. Greatly improved in folding into a catalytically competent enzyme. The mutant was greatly improved in folding into a catalytically competent enzyme.
