,Unnamed: 0.1,Unnamed: 0,entry,protein2,uniprot_description,rank,protein1,protein_name,function,GPT_description,all_description
0,0,1220,P69490-H130A,MNIRRKNRLWIACAVLAGLALTIGLVLYALRSNIDLFYTPGEILYGKRETQQMPEVGQRLRVGGMVMPGSVQRDPNSLKVTFTIYDAEGSVDVSYEGILPDLFREGQGVVVQGELEKGNHILAKEVLAKADENYTPPEVEKAMEANHRRPASVYKDPAS,Abolishes heme binding.,,MNIRRKNRLWIACAVLAGLALTIGLVLYALRSNIDLFYTPGEILYGKRETQQMPEVGQRLRVGGMVMPGSVQRDPNSLKVTFTIYDAEGSVDVSYEGILPDLFREGQGVVVQGELEKGNHILAKEVLAKHDENYTPPEVEKAMEANHRRPASVYKDPAS,Cytochrome c-type biogenesis protein CcmE,Heme chaperone required for the biogenesis of c-type cytochromes. Transiently binds heme delivered by CcmC and transfers the heme to apo-cytochromes in a process facilitated by CcmF and CcmH.,Mutation of H130 to alanine affected CcmE more than mutation of charged and polar residues. Our data suggest that heme is bound to a hydrophobic platform at the surface of the protein and then attached to H130 by a covalent bond.,Abolishes heme binding. Mutation of H130 to alanine affected CcmE more than mutation of charged and polar residues. Our data suggest that heme is bound to a hydrophobic platform at the surface of the protein and then attached to H130 by a covalent bond.
1,1,2340,P21926-C219A,MPVKGGTKCIKYLLFGFNFIFWLAGIAVLAIGLWLRFDSQTKSIFEQETNNNNSSFYTGVYILIGAGALMMLVGFLGCCGAVQESQCMLGLFFGFLLVIFAIEIAAAIWGYSHKDEVIKEVQEFYKDTYNKLKTKDEPQRETLKAIHYALNCCGLAGGVEQFISDICPKKDVLETFTVKSCPDAIKEVFDNKFHIIGAVGIGIAVVMIFGMIFSMILCAAIRRNREMV,Loss of palmitoylation; when associated with A-9; A-78; A-79; A-87 and A-218.,,MPVKGGTKCIKYLLFGFNFIFWLAGIAVLAIGLWLRFDSQTKSIFEQETNNNNSSFYTGVYILIGAGALMMLVGFLGCCGAVQESQCMLGLFFGFLLVIFAIEIAAAIWGYSHKDEVIKEVQEFYKDTYNKLKTKDEPQRETLKAIHYALNCCGLAGGVEQFISDICPKKDVLETFTVKSCPDAIKEVFDNKFHIIGAVGIGIAVVMIFGMIFSMILCCAIRRNREMV,CD9 antigen,"Integral membrane protein associated with integrins, which regulates different processes, such as sperm-egg fusion, platelet activation and aggregation, and cell adhesion. Present at the cell surface of oocytes and plays a key role in sperm-egg fusion, possibly by organizing multiprotein complexes and the morphology of the membrane required for the fusion. In myoblasts, associates with CD81 and PTGFRN and inhibits myotube fusion during muscle regeneration. In macrophages, associates with CD81 and beta-1 and beta-2 integrins, and prevents macrophage fusion into multinucleated giant cells specialized in ingesting complement-opsonized large particles. Also prevents the fusion between mononuclear cell progenitors into osteoclasts in charge of bone resorption. Acts as a receptor for PSG17. Involved in platelet activation and aggregation. Regulates paranodal junction formation. Involved in cell adhesion, cell motility and tumor metastasis.",,Loss of palmitoylation; when associated with A-9; A-78; A-79; A-87 and A-218.
2,2,2359,Q92504-S275A,MARGLGAPHWVAVGLLTWATLGLLVAGLGGHDDLHDDLQEDFHGHSHRHSHEDFHHGHSHAHGHGHTHESIWHGHTHDHDHGHSHEDLHHGHSHGYSHESLYHRGHGHDHEHSHGGYGESGAPGIKQDLDAVTLWAYALGATVLISAAPFFVLFLIPVESNSPRHRSLLQILLSFASGGLLGDAFLHLIPHALEPHSHHTLEQPGHGHSHSGQGPILSVGLWVLSGIVAFLVVEKFVRHVKGGHGHSHGHGHAHSHTRGSHGHGRQERSTKEKQASEEEEKETRGVQKRRGGSTVPKDGPVRPQNAEEEKRGLDLRVSGYLNLAADLAHNFTDGLAIGASFRGGRGLGILTTMTVLLHEVPHEVGDFAILVQSGCSKKQAMRLQLLTAVGALAGTACALLTEGGAVGSEIAGGAGPGWVLPFTAGGFIYVATVSVLPELLREASPLQSLLEVLGLLGGVIMMVLIAHLE,Loss of phosphorylation in response to Zn(2+) treatment and of cytosolic Zn(2+) release; when associated with A-276.,,MARGLGAPHWVAVGLLTWATLGLLVAGLGGHDDLHDDLQEDFHGHSHRHSHEDFHHGHSHAHGHGHTHESIWHGHTHDHDHGHSHEDLHHGHSHGYSHESLYHRGHGHDHEHSHGGYGESGAPGIKQDLDAVTLWAYALGATVLISAAPFFVLFLIPVESNSPRHRSLLQILLSFASGGLLGDAFLHLIPHALEPHSHHTLEQPGHGHSHSGQGPILSVGLWVLSGIVAFLVVEKFVRHVKGGHGHSHGHGHAHSHTRGSHGHGRQERSTKEKQSSEEEEKETRGVQKRRGGSTVPKDGPVRPQNAEEEKRGLDLRVSGYLNLAADLAHNFTDGLAIGASFRGGRGLGILTTMTVLLHEVPHEVGDFAILVQSGCSKKQAMRLQLLTAVGALAGTACALLTEGGAVGSEIAGGAGPGWVLPFTAGGFIYVATVSVLPELLREASPLQSLLEVLGLLGGVIMMVLIAHLE,Zinc transporter SLC39A7,"Transports Zn(2+) from the endoplasmic reticulum (ER)/Golgi apparatus to the cytosol, playing an essential role in the regulation of cytosolic zinc levels. Acts as gatekeeper of zinc release from intracellular stores, requiring post-translational activation by phosphorylation, resulting in activation of multiple downstream pathways leading to cell growth and proliferation. Has an essential role in B cell development and is required for proper B cell receptor signaling. Plays an important role in maintaining intestinal epithelial homeostasis and skin dermis development by regulating ER function. Controls cell signaling pathways involved in glucose metabolism in skeletal muscle. Has a protective role against ER stress in differents biological contexts. Mediates Zn(2+)-induced ferroptosis.","Phosphorylation of S275 in ZIP7 is associated with the gated release of Zn(2+) from intracellular stores, leading to activation of tyrosine kinases and the phosphorylation of AKT and extracellular signal-regulated kinases 1 and 2. The regulated release of zinc from intracellular stores is linked to phosphorylation of kinases involved in proliferative responses and cell migration. Phosphorylation on residue S275 is required for maximal ZIP7 activation.","Loss of phosphorylation in response to Zn(2+) treatment and of cytosolic Zn(2+) release; when associated with A-276. Phosphorylation of S275 in ZIP7 is associated with the gated release of Zn(2+) from intracellular stores, leading to activation of tyrosine kinases and the phosphorylation of AKT and extracellular signal-regulated kinases 1 and 2. The regulated release of zinc from intracellular stores is linked to phosphorylation of kinases involved in proliferative responses and cell migration. Phosphorylation on residue S275 is required for maximal ZIP7 activation."
3,3,3990,Q969S9-Y92S,MLTNLRIFAMSHQTIPSVYINNICCYKIRASLKRLKPHVPLGRNCSSLPGLIGNDIKSLHSIINPPIAKIRNIGIMAHIDAGKTTTTERILSYSGYTRSLGDVDDGDTVTDFMAQERERGITIQSAAVTFDWKGYRVNLIDTPGHVDFTLEVERCLRVLDGAVAVFDASAGVEAQTLTVWRQADKHNIPRICFLNKMDKTGASFKYAVESIREKLKAKPLLLQLPIGEAKTFKGVVDVVMKEKLLWNCNSNDGKDFERKPLLEMNDPELLKETTEARNALIEQVADLDDEFADLVLEEFSENFDLLPAEKLQTAIHRVTLAQTAVPVLCGSALKNKGIQPLLDAVTMYLPSPEERNYEFLQWYKDDLCALAFKVLHDKQRGPLVFMRIYSGTIKPQLAIHNINGNCTERISRLLLPFADQHVEIPSLTAGNIALTVGLKHTATGDTIVSSKSSALAAARRAEREGEKKHRQNNEAERLLLAGVEIPEPVFFCTIEPPSLSKQPDLEHALKCLQREDPSLKVRLDPDSGQTVLCGMGELHIEIIHDRIKREYGLETYLGPLQVAYRETILNSVRATDTLDRTLGDKRHLVTVEVEARPIETSSVMPVIEFEYAESINEGLLKVSQEAIENGIHSACLQGPLLGSPIQDVAITLHSLTIHPGTSTTMISACVSRCVQKALKKADKQVLEPLMNLEVTVARDYLSPVLADLAQRRGNIQEIQTRQDNKVVIGFVPLAEIMGYSTVLRTLTSGSATFALELSTYQAMNPQDQNTLLNRRSGLT,In COXPD39.,,MLTNLRIFAMSHQTIPSVYINNICCYKIRASLKRLKPHVPLGRNCSSLPGLIGNDIKSLHSIINPPIAKIRNIGIMAHIDAGKTTTTERILYYSGYTRSLGDVDDGDTVTDFMAQERERGITIQSAAVTFDWKGYRVNLIDTPGHVDFTLEVERCLRVLDGAVAVFDASAGVEAQTLTVWRQADKHNIPRICFLNKMDKTGASFKYAVESIREKLKAKPLLLQLPIGEAKTFKGVVDVVMKEKLLWNCNSNDGKDFERKPLLEMNDPELLKETTEARNALIEQVADLDDEFADLVLEEFSENFDLLPAEKLQTAIHRVTLAQTAVPVLCGSALKNKGIQPLLDAVTMYLPSPEERNYEFLQWYKDDLCALAFKVLHDKQRGPLVFMRIYSGTIKPQLAIHNINGNCTERISRLLLPFADQHVEIPSLTAGNIALTVGLKHTATGDTIVSSKSSALAAARRAEREGEKKHRQNNEAERLLLAGVEIPEPVFFCTIEPPSLSKQPDLEHALKCLQREDPSLKVRLDPDSGQTVLCGMGELHIEIIHDRIKREYGLETYLGPLQVAYRETILNSVRATDTLDRTLGDKRHLVTVEVEARPIETSSVMPVIEFEYAESINEGLLKVSQEAIENGIHSACLQGPLLGSPIQDVAITLHSLTIHPGTSTTMISACVSRCVQKALKKADKQVLEPLMNLEVTVARDYLSPVLADLAQRRGNIQEIQTRQDNKVVIGFVPLAEIMGYSTVLRTLTSGSATFALELSTYQAMNPQDQNTLLNRRSGLT,"Ribosome-releasing factor 2, mitochondrial",Mitochondrial GTPase that mediates the disassembly of ribosomes from messenger RNA at the termination of mitochondrial protein biosynthesis. Acts in collaboration with MRRF. GTP hydrolysis follows the ribosome disassembly and probably occurs on the ribosome large subunit. Not involved in the GTP-dependent ribosomal translocation step during translation elongation.,"The variant c. 275A>C results in the amino acid change p. () in the mtEFG2 protein. This variant causes defective mtEFG2 function, leading to clinical symptoms such as global developmental delay and abnormalities on cranial MRI.","In COXPD39. The variant c. 275A>C results in the amino acid change p. () in the mtEFG2 protein. This variant causes defective mtEFG2 function, leading to clinical symptoms such as global developmental delay and abnormalities on cranial MRI."
4,4,4985,P51843-L278P,MAGENHQWQGSILYNMLMSAKQTRAAPEAPETRLVDQCWGCSCGDEPGVGREGLLGGRNVALLYRCCFCGKDHPRQGSILYSMLTSAKQTYAAPKAPEATLGPCWGCSCGSDPGVGRAGLPGGRPVALLYRCCFCGEDHPRQGSILYSLLTSSKQTHVAPAAPEARPGGAWWDRSYFAQRPGGKEALPGGRATALLYRCCFCGEDHPQQGSTLYCVPTSTNQAQAAPEERPRAPWWDTSSGALRPVALKSPQVVCEAASAGLLKTLRFVKYLPCFQVPPLDQQLVLVRNCWASLLMLELAQDRLQFETVEVSEPSMLQKILTTRRRETGGNEPLPVPTLQHHLAPPAEARKVPSASQVQAIKCFLSKCWSLNISTKEYAYLKGTVLFNPDVPGLQCVKYIQGLQWGTQQILSEHTRMTHQGPHDRFIELNSTLFLLRFINANVIAELFFRPIIGTVSMDDMMLEMLCTKI,In AHC.,,MAGENHQWQGSILYNMLMSAKQTRAAPEAPETRLVDQCWGCSCGDEPGVGREGLLGGRNVALLYRCCFCGKDHPRQGSILYSMLTSAKQTYAAPKAPEATLGPCWGCSCGSDPGVGRAGLPGGRPVALLYRCCFCGEDHPRQGSILYSLLTSSKQTHVAPAAPEARPGGAWWDRSYFAQRPGGKEALPGGRATALLYRCCFCGEDHPQQGSTLYCVPTSTNQAQAAPEERPRAPWWDTSSGALRPVALKSPQVVCEAASAGLLKTLRFVKYLPCFQVLPLDQQLVLVRNCWASLLMLELAQDRLQFETVEVSEPSMLQKILTTRRRETGGNEPLPVPTLQHHLAPPAEARKVPSASQVQAIKCFLSKCWSLNISTKEYAYLKGTVLFNPDVPGLQCVKYIQGLQWGTQQILSEHTRMTHQGPHDRFIELNSTLFLLRFINANVIAELFFRPIIGTVSMDDMMLEMLCTKI,Nuclear receptor subfamily 0 group B member 1,Orphan nuclear receptor. Component of a cascade required for the development of the hypothalamic-pituitary-adrenal-gonadal axis. Acts as a coregulatory protein that inhibits the transcriptional activity of other nuclear receptors through heterodimeric interactions. May also have a role in the development of the embryo and in the maintenance of embryonic stem cell pluripotency.,The mutation in the DAX1 gene leads to X-linked adrenal hypoplasia congenita (AHC) and hypogonadotrophic hypogonadism (HHG).,In AHC. The mutation in the DAX1 gene leads to X-linked adrenal hypoplasia congenita (AHC) and hypogonadotrophic hypogonadism (HHG).
5,5,7593,O00899-K474R,MEGLEIEDEDVILLDEDDDSSSSSTVNNSSSNIKNNGNTNNNIGNDDSNKVTLMTSLREKGWGSGMLVDKEKNQYGTIKSYKDDKSSPWFEERQVIATLYKARVLLHEMIYTKMNQERLLSGNLCVGEIQSLLNTQKEDVETDWIAEIQELKRNMVAEIRRNHLLERDVNKLDKRIALLIKHRSNIKDLLLEQNKGKKDKKKKGDDKAEYITLDQKQLESYQNLFYLLQTEPHYLAKLVTLIQADQMEDFLDTVFLTLFGDDFSPREEFLILSLFRLAIGQEMSRIKSAGDLLAVESVVPKMIITYTRRKQGHEFLKQIIAPILENNVVNAPDLNLELNAVQVYQNMISEQEIQTGAKSTLNRGLAEDQIIQLKEVQSILEPRVEKCIQICERFFTGIIQSLNRLPYGIRWICKQIQSIAQKNFDSKPDEIAKVIGYFVYYRFINLAIVTPDAFEILDKELSITSRKNLVNIARVLQNLFTLKTFQNQGSERWMQPLNKWILSKTSIVRQYLEDLIQVTDPSEYLRVDKYNELTLKLNPVVVISLGEISQTHRLLIANLAALKMKEKEDPLELILKALPAPLEVVDENDREIQLTLINRFKENIEKEISISASLLAETKELVISVLRSIPIQQKQQQQQHDDEKRDDLISILQNAIKHGKETNNPQLSSNAEKIINNLKKMEAEGSIQSENNQYEGFIKVIALEVINRQEIREQQRKERMRLTIALRDLRKHQSYLNDQIQHYTSYLKDVLLHYGPKDKKKSTKPMKISFKELTKKGVIVESDIPKLSHGSTSFYISSDAPGIFDIEARIGVASVGTLSLSLDDLLDKSSAGIPYLKLENIVLDVNMTLHLLNRHFLKNI,Able to complement a gapA null mutant.,,MEGLEIEDEDVILLDEDDDSSSSSTVNNSSSNIKNNGNTNNNIGNDDSNKVTLMTSLREKGWGSGMLVDKEKNQYGTIKSYKDDKSSPWFEERQVIATLYKARVLLHEMIYTKMNQERLLSGNLCVGEIQSLLNTQKEDVETDWIAEIQELKRNMVAEIRRNHLLERDVNKLDKRIALLIKHRSNIKDLLLEQNKGKKDKKKKGDDKAEYITLDQKQLESYQNLFYLLQTEPHYLAKLVTLIQADQMEDFLDTVFLTLFGDDFSPREEFLILSLFRLAIGQEMSRIKSAGDLLAVESVVPKMIITYTRRKQGHEFLKQIIAPILENNVVNAPDLNLELNAVQVYQNMISEQEIQTGAKSTLNRGLAEDQIIQLKEVQSILEPRVEKCIQICERFFTGIIQSLNRLPYGIRWICKQIQSIAQKNFDSKPDEIAKVIGYFVYYRFINLAIVTPDAFEILDKELSITSRKNLVNIAKVLQNLFTLKTFQNQGSERWMQPLNKWILSKTSIVRQYLEDLIQVTDPSEYLRVDKYNELTLKLNPVVVISLGEISQTHRLLIANLAALKMKEKEDPLELILKALPAPLEVVDENDREIQLTLINRFKENIEKEISISASLLAETKELVISVLRSIPIQQKQQQQQHDDEKRDDLISILQNAIKHGKETNNPQLSSNAEKIINNLKKMEAEGSIQSENNQYEGFIKVIALEVINRQEIREQQRKERMRLTIALRDLRKHQSYLNDQIQHYTSYLKDVLLHYGPKDKKKSTKPMKISFKELTKKGVIVESDIPKLSHGSTSFYISSDAPGIFDIEARIGVASVGTLSLSLDDLLDKSSAGIPYLKLENIVLDVNMTLHLLNRHFLKNI,Ras GTPase-activating-like protein gapA,Part of signaling pathway that is required for completion of cytokinesis. gapA and rgaA control cortexillin localization to the cleavage furrow and hence may be involved in cleavage of the midbody in the final stage of cytokinesis by regulating the actin cytoskeleton. Forms a complex by linking activated rac1A to ctxA in the absence of rgaA. Assembly of this complex is necessary for the recruitment of cortexillin to the midzone of the dividing cell.,Positively charged side chain K474 of GAPA is essential for interaction with small GTPases in cytokinesis.,Able to complement a gapA null mutant. Positively charged side chain K474 of GAPA is essential for interaction with small GTPases in cytokinesis.
6,6,7900,Q7G065-A171I,MQFMMPLDTNACAQPMRRAGEGAGTERLMERLNIGGMTQEKALRKRCFGDGVTGTARCVFTSDADRDTPHLRTQSSRKNYADASHVSAVILGGGTGVQLFPLTSTRATPAVPVGGCYRLIDIPMSNCFNSGINKIFVMTQFNSASLNRHIHHTYLGGGINFTDGSVQVLAITQMPDEPAGWFQGTADAIRKFMWILEDHYNQNNIEHVVILCGDQLYRMNYMELVQKHVDDNADITISCAPIDGSRASDYGLVKFDDSGRVIQFLEKPEGADLESMKVDTSFLSYAIDDKQKYPYIASMGIYVLKKDVLLDILKSKYAHLQDFGSEILPRAVLEHNVKACVFTEYWEDIGTIKSFFDANLALTEQPPKFEFYDPKTPFFTSPRYLPPARLEKCKIKDAIISDGCSFSECTIEHSVIGISSRVSIGCELKDTMMMGADQYETEEETSKLLFEGKVPIGIGENTKIRNCIIDMNARIGRNVIIANTQGVQESDHPEEGYYIRSGIVVILKNATIKDGTVI,Reduces activity more than 3-fold.,,MQFMMPLDTNACAQPMRRAGEGAGTERLMERLNIGGMTQEKALRKRCFGDGVTGTARCVFTSDADRDTPHLRTQSSRKNYADASHVSAVILGGGTGVQLFPLTSTRATPAVPVGGCYRLIDIPMSNCFNSGINKIFVMTQFNSASLNRHIHHTYLGGGINFTDGSVQVLAATQMPDEPAGWFQGTADAIRKFMWILEDHYNQNNIEHVVILCGDQLYRMNYMELVQKHVDDNADITISCAPIDGSRASDYGLVKFDDSGRVIQFLEKPEGADLESMKVDTSFLSYAIDDKQKYPYIASMGIYVLKKDVLLDILKSKYAHLQDFGSEILPRAVLEHNVKACVFTEYWEDIGTIKSFFDANLALTEQPPKFEFYDPKTPFFTSPRYLPPARLEKCKIKDAIISDGCSFSECTIEHSVIGISSRVSIGCELKDTMMMGADQYETEEETSKLLFEGKVPIGIGENTKIRNCIIDMNARIGRNVIIANTQGVQESDHPEEGYYIRSGIVVILKNATIKDGTVI,"Glucose-1-phosphate adenylyltransferase large subunit 2, cytosolic","Involved in synthesis of starch. Catalyzes the synthesis of ADP-glucose, a molecule that serves as an activated glycosyl donor for alpha-1,4-glucan synthesis. Essential for starch synthesis in seed endosperm (PubMed:17406793, Ref.13, PubMed:24747952, PubMed:27957808). Is essential for both catalytic and allosteric regulatory properties of the cytosolic heterotetramer enzyme.",Seeds from the missense mutant containing were severely shriveled and had seed weight and starch content comparable with the shriveled seeds from OsAGPL2 null mutants. The catalytic and allosteric regulatory properties of the mutant enzyme were significantly impaired. The mutant enzyme had lower specific (catalytic) activity and affinity for the activator 3-phosphoglycerate (3-PGA). The mutant enzyme also showed more sensitivity to inhibition by the inhibitor inorganic phosphate (Pi) than the wild-type AGPase.,Reduces activity more than 3-fold. Seeds from the missense mutant containing were severely shriveled and had seed weight and starch content comparable with the shriveled seeds from OsAGPL2 null mutants. The catalytic and allosteric regulatory properties of the mutant enzyme were significantly impaired. The mutant enzyme had lower specific (catalytic) activity and affinity for the activator 3-phosphoglycerate (3-PGA). The mutant enzyme also showed more sensitivity to inhibition by the inhibitor inorganic phosphate (Pi) than the wild-type AGPase.
7,7,8358,Q9ULZ3-E19A,MGRARDAILDALENLTAEALKKFKLKLLSVPLREGYGRIPRGALLSMDALDLTDKLVSFYLETYGAELTANVLRDMGLQEMAGQLQAATHQGSGAAPAGIQAPPQSAAKPGLHFIDQHRAALIARVTNVEWLLDALYGKVLTDEQYQAVRAEPTNPSKMRKLFSFTPAWNWTCKDLLLQALRESQSYLVEDLERS,Abolishes homooligomerization.,,MGRARDAILDALENLTAEELKKFKLKLLSVPLREGYGRIPRGALLSMDALDLTDKLVSFYLETYGAELTANVLRDMGLQEMAGQLQAATHQGSGAAPAGIQAPPQSAAKPGLHFIDQHRAALIARVTNVEWLLDALYGKVLTDEQYQAVRAEPTNPSKMRKLFSFTPAWNWTCKDLLLQALRESQSYLVEDLERS,Apoptosis-associated speck-like protein containing a CARD,"Functions as key mediator in apoptosis and inflammation. Promotes caspase-mediated apoptosis involving predominantly caspase-8 and also caspase-9 in a probable cell type-specific manner. Involved in activation of the mitochondrial apoptotic pathway, promotes caspase-8-dependent proteolytic maturation of BID independently of FADD in certain cell types and also mediates mitochondrial translocation of BAX and activates BAX-dependent apoptosis coupled to activation of caspase-9, -2 and -3. Involved in innate immune response by acting as an integral adapter in the assembly of various inflammasomes (NLRP1, NLRP2, NLRP3, NLRP6, AIM2 and probably IFI16) which recruit and activate caspase-1 leading to processing and secretion of pro-inflammatory cytokines. Caspase-1-dependent inflammation leads to macrophage pyroptosis, a form of cell death. The function as activating adapter in different types of inflammasomes is mediated by the pyrin and CARD domains and their homotypic interactions. Clustered PYCARD nucleates the formation of caspase-1 filaments through the interaction of their respective CARD domains, acting as a platform for of caspase-1 polymerization. In the NLRP1 and NLRC4 inflammasomes seems not be required but facilitates the processing of procaspase-1. In cooperation with NOD2 involved in an inflammasome activated by bacterial muramyl dipeptide leading to caspase-1 activation. May be involved in RIGI-triggered pro-inflammatory responses and inflammasome activation. In collaboration with AIM2 which detects cytosolic double-stranded DNA may also be involved in a caspase-1-independent cell death that involves caspase-8. In adaptive immunity may be involved in maturation of dendritic cells to stimulate T-cell immunity and in cytoskeletal rearrangements coupled to chemotaxis and antigen uptake may be involved in post-transcriptional regulation of the guanine nucleotide exchange factor DOCK2; the latter function is proposed to involve the nuclear form. Also involved in transcriptional activation of cytokines and chemokines independent of the inflammasome; this function may involve AP-1, NF-kappa-B, MAPK and caspase-8 signaling pathways. For regulation of NF-kappa-B activating and inhibiting functions have been reported. Modulates NF-kappa-B induction at the level of the IKK complex by inhibiting kinase activity of CHUK and IKBK. Proposed to compete with RIPK2 for association with CASP1 thereby down-regulating CASP1-mediated RIPK2-dependent NF-kappa-B activation and activating interleukin-1 beta processing. Modulates host resistance to DNA virus infection, probably by inducing the cleavage of and inactivating CGAS in presence of cytoplasmic double-stranded DNA.May have a regulating effect on the function as inflammasome adapter.Seems to inhibit inflammasome-mediated maturation of interleukin-1 beta.",Mutation of E19 to A in ASC protein leads to loss of filament formation.,Abolishes homooligomerization. Mutation of E19 to A in ASC protein leads to loss of filament formation.
8,8,8493,A0A0H2URG7-R103A,MTIYNINLGIGWASSGVEYAQAYRAGVFRKLNLSSKFIFTDMILADNIQHLTANIGFDDNQVIWLYNHFTDIKIAPTSVTVDDVLAYFGGEESHREKNGKVLAVFFFDQDKFVTCYLVDENKDLVQHAEYVFKGNLIRKDYFSYTRYCSEYFAPKDNVAVLYQRTFYNEDGTPVYDILMNQGKEEVYHFKDKIFYGKQAFVRAFMKSLNLNKSDLVILDRETGIGQVVFEEAQTAHLAVVVHAEHYSENATNEDYILWNNYYDYQFTNADKVDFFIVSTDRQNEVLQEQFAKYTQHQPKIVTIPVGSIDSLTDSSQGRKPFSLITASRLAKEKHIDWLVKAVIEAHKELPELTFDIYGSGGEDSLLREIIANHQAEDYIQLKGHAELSQIYSQYEVYLTASTSEGFGLTLMEAIGSGLPLIGFDVPYGNQTFIEDGQNGYLIPSSSDHVEDQIKQAYAAKICQLYQENRLEAMRAYSYQIAEGFLTKEILEKWKKTVEEVLHD,"Decreased N-acetylglucosaminyl transferase activity, decreased binding of PsrP.",,MTIYNINLGIGWASSGVEYAQAYRAGVFRKLNLSSKFIFTDMILADNIQHLTANIGFDDNQVIWLYNHFTDIKIAPTSVTVDDVLAYFGGEESHREKNGKVLRVFFFDQDKFVTCYLVDENKDLVQHAEYVFKGNLIRKDYFSYTRYCSEYFAPKDNVAVLYQRTFYNEDGTPVYDILMNQGKEEVYHFKDKIFYGKQAFVRAFMKSLNLNKSDLVILDRETGIGQVVFEEAQTAHLAVVVHAEHYSENATNEDYILWNNYYDYQFTNADKVDFFIVSTDRQNEVLQEQFAKYTQHQPKIVTIPVGSIDSLTDSSQGRKPFSLITASRLAKEKHIDWLVKAVIEAHKELPELTFDIYGSGGEDSLLREIIANHQAEDYIQLKGHAELSQIYSQYEVYLTASTSEGFGLTLMEAIGSGLPLIGFDVPYGNQTFIEDGQNGYLIPSSSDHVEDQIKQAYAAKICQLYQENRLEAMRAYSYQIAEGFLTKEILEKWKKTVEEVLHD,UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase GtfA subunit,Required for the polymorphic O-glycosylation of serine-rich repeat protein PsrP. Catalyzes the first step in glycosylation by transferring N-acetylglucosamine from UDP-GlcNAc to serine residues in PsrP. Part of the accessory SecA2/SecY2 system specifically required to export serine-rich repeat cell wall proteins encoded upstream in the same operon (Probable). The GtfA-GtfB complex adds GlcNAc from UDP-GlcNAc to PsrP (experimentally characterized with truncated PsrP-SSR1 constructs); this subunit alone has weak N-acetylglucosaminyl transferase activity that is 10-fold stimulated by GtfB. The complex requires at least a 25 residue-long peptide for activity; the in vitro assay has only been seen to glycosylate Ser residues. The alpha linkage was shown in L.reuteri.,,"Decreased N-acetylglucosaminyl transferase activity, decreased binding of PsrP."
9,9,8708,P16522-S93F,MNDDSQDKIIHDIRIQLRKAATELSRWKLYGSSKWAAEALAGLAEAIDVDQTHSLADESPLRNKQGVPKQMFEIPQNGFGLSETEYDLYLLGFTLFDAKEFDRCVFFLKDVTNPYLKFLKLYSKFLSWDKKSQESMENILTTGKFTDEMYRANKDGDGSGNEDINQSGHQRANLKMVSNEHESQSNISSILKEINTFLESYEIKIDDDEADLGLALLYYLRGVILKQEKNISKAMSSFLKSLSCYSFNWSCWLELMDCLQKVDDALLLNNYLYQNFQFKFSENLGSQRTIEFNIMIKFFKLKVFEELNGQLEDYFEDLEFLLQVFPNFTFLKAYNATISYNNLDYVTAESRFDDIVKQDPYRLNDLETYSNILYVMQKNSKLAYLAQFVSQIDRFRPETCCIIANYYSARQEHEKSIMYFRRALTLDKKTTNAWTLMGHEFVELSNSHAAIECYRRAVDICPRDFKAWFGLGQAYALLDMHLYSLYYFQKACTLKPWDRRIWQVLGECYSKTGNKVEAIKCYKRSIKASQTVDQNTSIYYRLAQLYEELEDLQECKKFMMKCVDVEELLEGIVTDETVKARLWLAIFEIKAGNYQLAYDYAMGVSSGTSQEIEEARMLARECRRHM,In CDC23-52; G2/M cell cycle arrest at 37 degrees Celsius.,,MNDDSQDKIIHDIRIQLRKAATELSRWKLYGSSKWAAEALAGLAEAIDVDQTHSLADESPLRNKQGVPKQMFEIPQNGFGLSETEYDLYLLGSTLFDAKEFDRCVFFLKDVTNPYLKFLKLYSKFLSWDKKSQESMENILTTGKFTDEMYRANKDGDGSGNEDINQSGHQRANLKMVSNEHESQSNISSILKEINTFLESYEIKIDDDEADLGLALLYYLRGVILKQEKNISKAMSSFLKSLSCYSFNWSCWLELMDCLQKVDDALLLNNYLYQNFQFKFSENLGSQRTIEFNIMIKFFKLKVFEELNGQLEDYFEDLEFLLQVFPNFTFLKAYNATISYNNLDYVTAESRFDDIVKQDPYRLNDLETYSNILYVMQKNSKLAYLAQFVSQIDRFRPETCCIIANYYSARQEHEKSIMYFRRALTLDKKTTNAWTLMGHEFVELSNSHAAIECYRRAVDICPRDFKAWFGLGQAYALLDMHLYSLYYFQKACTLKPWDRRIWQVLGECYSKTGNKVEAIKCYKRSIKASQTVDQNTSIYYRLAQLYEELEDLQECKKFMMKCVDVEELLEGIVTDETVKARLWLAIFEIKAGNYQLAYDYAMGVSSGTSQEIEEARMLARECRRHM,Anaphase-promoting complex subunit CDC23,"Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. In early mitosis, the APC/C is activated by CDC20 and targets securin PDS1, the B-type cyclin CLB5, and other anaphase inhibitory proteins for proteolysis, thereby triggering the separation of sister chromatids at the metaphase-to-anaphase transition. In late mitosis and in G1, degradation of CLB5 allows activation of the APC/C by CDH1, which is needed to destroy CDC20 and the B-type cyclin CLB2 to allow exit from mitosis and creating the low CDK state necessary for cytokinesis and for reforming prereplicative complexes in G1 prior to another round of replication.",The mutation in the CDC23 gene causes a single amino acid change in the protein. This mutation is found within a mutable domain of CDC23 and may affect its function or stability.,In CDC23-52; G2/M cell cycle arrest at 37 degrees Celsius. The mutation in the CDC23 gene causes a single amino acid change in the protein. This mutation is found within a mutable domain of CDC23 and may affect its function or stability.
10,10,9004,P51843-V385G,MAGENHQWQGSILYNMLMSAKQTRAAPEAPETRLVDQCWGCSCGDEPGVGREGLLGGRNVALLYRCCFCGKDHPRQGSILYSMLTSAKQTYAAPKAPEATLGPCWGCSCGSDPGVGRAGLPGGRPVALLYRCCFCGEDHPRQGSILYSLLTSSKQTHVAPAAPEARPGGAWWDRSYFAQRPGGKEALPGGRATALLYRCCFCGEDHPQQGSTLYCVPTSTNQAQAAPEERPRAPWWDTSSGALRPVALKSPQVVCEAASAGLLKTLRFVKYLPCFQVLPLDQQLVLVRNCWASLLMLELAQDRLQFETVEVSEPSMLQKILTTRRRETGGNEPLPVPTLQHHLAPPAEARKVPSASQVQAIKCFLSKCWSLNISTKEYAYLKGTGLFNPDVPGLQCVKYIQGLQWGTQQILSEHTRMTHQGPHDRFIELNSTLFLLRFINANVIAELFFRPIIGTVSMDDMMLEMLCTKI,In AHC.,,MAGENHQWQGSILYNMLMSAKQTRAAPEAPETRLVDQCWGCSCGDEPGVGREGLLGGRNVALLYRCCFCGKDHPRQGSILYSMLTSAKQTYAAPKAPEATLGPCWGCSCGSDPGVGRAGLPGGRPVALLYRCCFCGEDHPRQGSILYSLLTSSKQTHVAPAAPEARPGGAWWDRSYFAQRPGGKEALPGGRATALLYRCCFCGEDHPQQGSTLYCVPTSTNQAQAAPEERPRAPWWDTSSGALRPVALKSPQVVCEAASAGLLKTLRFVKYLPCFQVLPLDQQLVLVRNCWASLLMLELAQDRLQFETVEVSEPSMLQKILTTRRRETGGNEPLPVPTLQHHLAPPAEARKVPSASQVQAIKCFLSKCWSLNISTKEYAYLKGTVLFNPDVPGLQCVKYIQGLQWGTQQILSEHTRMTHQGPHDRFIELNSTLFLLRFINANVIAELFFRPIIGTVSMDDMMLEMLCTKI,Nuclear receptor subfamily 0 group B member 1,Orphan nuclear receptor. Component of a cascade required for the development of the hypothalamic-pituitary-adrenal-gonadal axis. Acts as a coregulatory protein that inhibits the transcriptional activity of other nuclear receptors through heterodimeric interactions. May also have a role in the development of the embryo and in the maintenance of embryonic stem cell pluripotency.,The mutation in the DAX1 protein is mentioned in the document. It is located in the conserved hydrophobic core of the putative ligand-binding domain (LBD) of DAX1. This mutation does not affect residues expected to interact directly with a ligand. The functional changes caused by this mutation are not specified in the document.,In AHC. The mutation in the DAX1 protein is mentioned in the document. It is located in the conserved hydrophobic core of the putative ligand-binding domain (LBD) of DAX1. This mutation does not affect residues expected to interact directly with a ligand. The functional changes caused by this mutation are not specified in the document.
11,11,12502,Q9JJS6-H49A,MEIIFGQNKKEQLEPVQAKVTGSIPAWLQGTLLRNGPGMHTVGESKYNAWFDGLALLHSFSIRDGEVFYRSKYLQSDTYIANIEANRIVVSEFGTMAYPDPCKNIFSKAFSYLSHTIPDFTDNCLINIMKCGEDFYATTETNYIRKIDPQTLETLEKVDYRKYVAVNLATSHPHYDEAGNVLNMGTSVVDKGRTKYVIFKIPATVPDSKKKGKSPVKHAEVFCSISSRSLLSPSYYHSFGVTENYVVFLEQPFKLDILKMATAYMRGVSWASCMSFDREDKTYIHIIDQRTRKPVPTKFYTDPMVVFHHVNAYEEDGCVLFDVIAYEDSSLYQLFYLANLNKDFEEKSRLTSVPTLRRFAVPLHVDKDAEVGSNLVKVSSTTATALKEKDGHVYCQPEVLYEGLELPRINYAYNGKPYRYIFAAEVQWSPVPTKILKYDILTKSSLKWSEESCWPAEPLFVPTPGAKDEDDGVILSAIVSTDPQKLPFLLILDAKSFTELARASVDADMHLDLHGLFIPDADWNAVKQTPAETQEVENSDHPTDPTAPELSHSENDFTAGHGGSSL,"No significant effect on beta-carotene 15,15'-monooxygenase activity. Decreased stability.",,MEIIFGQNKKEQLEPVQAKVTGSIPAWLQGTLLRNGPGMHTVGESKYNHWFDGLALLHSFSIRDGEVFYRSKYLQSDTYIANIEANRIVVSEFGTMAYPDPCKNIFSKAFSYLSHTIPDFTDNCLINIMKCGEDFYATTETNYIRKIDPQTLETLEKVDYRKYVAVNLATSHPHYDEAGNVLNMGTSVVDKGRTKYVIFKIPATVPDSKKKGKSPVKHAEVFCSISSRSLLSPSYYHSFGVTENYVVFLEQPFKLDILKMATAYMRGVSWASCMSFDREDKTYIHIIDQRTRKPVPTKFYTDPMVVFHHVNAYEEDGCVLFDVIAYEDSSLYQLFYLANLNKDFEEKSRLTSVPTLRRFAVPLHVDKDAEVGSNLVKVSSTTATALKEKDGHVYCQPEVLYEGLELPRINYAYNGKPYRYIFAAEVQWSPVPTKILKYDILTKSSLKWSEESCWPAEPLFVPTPGAKDEDDGVILSAIVSTDPQKLPFLLILDAKSFTELARASVDADMHLDLHGLFIPDADWNAVKQTPAETQEVENSDHPTDPTAPELSHSENDFTAGHGGSSL,"Beta,beta-carotene 15,15'-dioxygenase",Symmetrically cleaves beta-carotene into two molecules of retinal using a dioxygenase mechanism.,,"No significant effect on beta-carotene 15,15'-monooxygenase activity. Decreased stability."
12,12,12718,O14746-S457A,MPRAPRCRAVRSLLRSHYREVLPLATFVRRLGPQGWRLVQRGDPAAFRALVAQCLVCVPWDARPPPAAPSFRQVSCLKELVARVLQRLCERGAKNVLAFGFALLDGARGGPPEAFTTSVRSYLPNTVTDALRGSGAWGLLLRRVGDDVLVHLLARCALFVLVAPSCAYQVCGPPLYQLGAATQARPPPHASGPRRRLGCERAWNHSVREAGVPLGLPAPGARRRGGSASRSLPLPKRPRRGAAPEPERTPVGQGSWAHPGRTRGPSDRGFCVVSPARPAEEATSLEGALSGTRHSHPSVGRQHHAGPPSTSRPPRPWDTPCPPVYAETKHFLYSSGDKEQLRPSFLLSSLRPSLTGARRLVETIFLGSRPWMPGTPRRLPRLPQRYWQMRPLFLELLGNHAQCPYGVLLKTHCPLRAAVTPAAGVCAREKPQGSVAAPEEEDTDPRRLVQLLRQHSAPWQVYGFVRACLRRLVPPGLWGSRHNERRFLRNTKKFISLGKHAKLSLQELTWKMSVRDCAWLRRSPGVGCVPAAEHRLREEILAKFLHWLMSVYVVELLRSFFYVTETTFQKNRLFFYRKSVWSKLQSIGIRQHLKRVQLRELSEAEVRQHREARPALLTSRLRFIPKPDGLRPIVNMDYVVGARTFRREKRAERLTSRVKALFSVLNYERARRPGLLGASVLGLDDIHRAWRTFVLRVRAQDPPPELYFVKVDVTGAYDTIPQDRLTEVIASIIKPQNTYCVRRYAVVQKAAHGHVRKAFKSHVSTLTDLQPYMRQFVAHLQETSPLRDAVVIEQSSSLNEASSGLFDVFLRFMCHHAVRIRGKSYVQCQGIPQGSILSTLLCSLCYGDMENKLFAGIRRDGLLLRLVDDFLLVTPHLTHAKTFLRTLVRGVPEYGCVVNLRKTVVNFPVEDEALGGTAFVQMPAHGLFPWCGLLLDTRTLEVQSDYSSYARTSIRASLTFNRGFKAGRNMRRKLFGVLRLKCHSLFLDLQVNSLQTVCTNIYKILLLQAYRFHACVLQLPFHQQ,Abolishes phosphorylation by DYRK2.,,MPRAPRCRAVRSLLRSHYREVLPLATFVRRLGPQGWRLVQRGDPAAFRALVAQCLVCVPWDARPPPAAPSFRQVSCLKELVARVLQRLCERGAKNVLAFGFALLDGARGGPPEAFTTSVRSYLPNTVTDALRGSGAWGLLLRRVGDDVLVHLLARCALFVLVAPSCAYQVCGPPLYQLGAATQARPPPHASGPRRRLGCERAWNHSVREAGVPLGLPAPGARRRGGSASRSLPLPKRPRRGAAPEPERTPVGQGSWAHPGRTRGPSDRGFCVVSPARPAEEATSLEGALSGTRHSHPSVGRQHHAGPPSTSRPPRPWDTPCPPVYAETKHFLYSSGDKEQLRPSFLLSSLRPSLTGARRLVETIFLGSRPWMPGTPRRLPRLPQRYWQMRPLFLELLGNHAQCPYGVLLKTHCPLRAAVTPAAGVCAREKPQGSVAAPEEEDTDPRRLVQLLRQHSSPWQVYGFVRACLRRLVPPGLWGSRHNERRFLRNTKKFISLGKHAKLSLQELTWKMSVRDCAWLRRSPGVGCVPAAEHRLREEILAKFLHWLMSVYVVELLRSFFYVTETTFQKNRLFFYRKSVWSKLQSIGIRQHLKRVQLRELSEAEVRQHREARPALLTSRLRFIPKPDGLRPIVNMDYVVGARTFRREKRAERLTSRVKALFSVLNYERARRPGLLGASVLGLDDIHRAWRTFVLRVRAQDPPPELYFVKVDVTGAYDTIPQDRLTEVIASIIKPQNTYCVRRYAVVQKAAHGHVRKAFKSHVSTLTDLQPYMRQFVAHLQETSPLRDAVVIEQSSSLNEASSGLFDVFLRFMCHHAVRIRGKSYVQCQGIPQGSILSTLLCSLCYGDMENKLFAGIRRDGLLLRLVDDFLLVTPHLTHAKTFLRTLVRGVPEYGCVVNLRKTVVNFPVEDEALGGTAFVQMPAHGLFPWCGLLLDTRTLEVQSDYSSYARTSIRASLTFNRGFKAGRNMRRKLFGVLRLKCHSLFLDLQVNSLQTVCTNIYKILLLQAYRFHACVLQLPFHQQ,Telomerase reverse transcriptase,"Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. Active in progenitor and cancer cells. Inactive, or very low activity, in normal somatic cells. Catalytic component of the teleromerase holoenzyme complex whose main activity is the elongation of telomeres by acting as a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme. Catalyzes the RNA-dependent extension of 3'-chromosomal termini with the 6-nucleotide telomeric repeat unit, 5'-TTAGGG-3'. The catalytic cycle involves primer binding, primer extension and release of product once the template boundary has been reached or nascent product translocation followed by further extension. More active on substrates containing 2 or 3 telomeric repeats. Telomerase activity is regulated by a number of factors including telomerase complex-associated proteins, chaperones and polypeptide modifiers. Modulates Wnt signaling. Plays important roles in aging and antiapoptosis.",,Abolishes phosphorylation by DYRK2.
13,13,12727,A0A0H2URG7-K333A,MTIYNINLGIGWASSGVEYAQAYRAGVFRKLNLSSKFIFTDMILADNIQHLTANIGFDDNQVIWLYNHFTDIKIAPTSVTVDDVLAYFGGEESHREKNGKVLRVFFFDQDKFVTCYLVDENKDLVQHAEYVFKGNLIRKDYFSYTRYCSEYFAPKDNVAVLYQRTFYNEDGTPVYDILMNQGKEEVYHFKDKIFYGKQAFVRAFMKSLNLNKSDLVILDRETGIGQVVFEEAQTAHLAVVVHAEHYSENATNEDYILWNNYYDYQFTNADKVDFFIVSTDRQNEVLQEQFAKYTQHQPKIVTIPVGSIDSLTDSSQGRKPFSLITASRLAKEAHIDWLVKAVIEAHKELPELTFDIYGSGGEDSLLREIIANHQAEDYIQLKGHAELSQIYSQYEVYLTASTSEGFGLTLMEAIGSGLPLIGFDVPYGNQTFIEDGQNGYLIPSSSDHVEDQIKQAYAAKICQLYQENRLEAMRAYSYQIAEGFLTKEILEKWKKTVEEVLHD,Loss of N-acetylglucosaminyl transferase activity.,,MTIYNINLGIGWASSGVEYAQAYRAGVFRKLNLSSKFIFTDMILADNIQHLTANIGFDDNQVIWLYNHFTDIKIAPTSVTVDDVLAYFGGEESHREKNGKVLRVFFFDQDKFVTCYLVDENKDLVQHAEYVFKGNLIRKDYFSYTRYCSEYFAPKDNVAVLYQRTFYNEDGTPVYDILMNQGKEEVYHFKDKIFYGKQAFVRAFMKSLNLNKSDLVILDRETGIGQVVFEEAQTAHLAVVVHAEHYSENATNEDYILWNNYYDYQFTNADKVDFFIVSTDRQNEVLQEQFAKYTQHQPKIVTIPVGSIDSLTDSSQGRKPFSLITASRLAKEKHIDWLVKAVIEAHKELPELTFDIYGSGGEDSLLREIIANHQAEDYIQLKGHAELSQIYSQYEVYLTASTSEGFGLTLMEAIGSGLPLIGFDVPYGNQTFIEDGQNGYLIPSSSDHVEDQIKQAYAAKICQLYQENRLEAMRAYSYQIAEGFLTKEILEKWKKTVEEVLHD,UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase GtfA subunit,Required for the polymorphic O-glycosylation of serine-rich repeat protein PsrP. Catalyzes the first step in glycosylation by transferring N-acetylglucosamine from UDP-GlcNAc to serine residues in PsrP. Part of the accessory SecA2/SecY2 system specifically required to export serine-rich repeat cell wall proteins encoded upstream in the same operon (Probable). The GtfA-GtfB complex adds GlcNAc from UDP-GlcNAc to PsrP (experimentally characterized with truncated PsrP-SSR1 constructs); this subunit alone has weak N-acetylglucosaminyl transferase activity that is 10-fold stimulated by GtfB. The complex requires at least a 25 residue-long peptide for activity; the in vitro assay has only been seen to glycosylate Ser residues. The alpha linkage was shown in L.reuteri.,,Loss of N-acetylglucosaminyl transferase activity.
14,14,13610,Q1PEI6-M377V,MEFSCVHFLQNKTILVTGATGFLAKVFVEKILRVQPNVNKLYLVVRASDNEAATKRLRTEAFEKDLFKVLRDNLGDEKLNTLLSEKVVPVAGDIAMDHLGMKDSNLRERMQKEIDIVVNVAATTNFDERYDIGLGINTFGALNVLNFAKKCVKAQLLLHVSTAYVCGEKPGLLPEKPFVMEEICNENGLQLDINLERELMKQRLKELNEQGCSEEGTTFYMKELGMERAKLHGWPNTYVFTKSMGEMLLGNHKENLPLVIIRPTMITSTLFEPFPGWIEGLRTVDSVIIAYGKGVLKCFLVDVNSVCDMIPADMVANAMIAAAATHAGGSKVHMVYQVGSSHQNPIIYGEIREILFCYFTKNSLRSRNGSMITVSKVKLIPTLALFSLYMTIRYKLPVQLLKLVDIIYPSREGDEYKNKNRKIDMVMRLVKLYEPYVLFKGIFDDRNTKNLCAKQKEEDNRNSENFMFDFDPKIIKWKDYLINVHIPGLITHVLKK,Catalyzes the formation of C18:0 fatty alcohol instead of C16:0; when associated with T-347 and A-355.,,MEFSCVHFLQNKTILVTGATGFLAKVFVEKILRVQPNVNKLYLVVRASDNEAATKRLRTEAFEKDLFKVLRDNLGDEKLNTLLSEKVVPVAGDIAMDHLGMKDSNLRERMQKEIDIVVNVAATTNFDERYDIGLGINTFGALNVLNFAKKCVKAQLLLHVSTAYVCGEKPGLLPEKPFVMEEICNENGLQLDINLERELMKQRLKELNEQGCSEEGTTFYMKELGMERAKLHGWPNTYVFTKSMGEMLLGNHKENLPLVIIRPTMITSTLFEPFPGWIEGLRTVDSVIIAYGKGVLKCFLVDVNSVCDMIPADMVANAMIAAAATHAGGSKVHMVYQVGSSHQNPIIYGEIREILFCYFTKNSLRSRNGSMITVSKMKLIPTLALFSLYMTIRYKLPVQLLKLVDIIYPSREGDEYKNKNRKIDMVMRLVKLYEPYVLFKGIFDDRNTKNLCAKQKEEDNRNSENFMFDFDPKIIKWKDYLINVHIPGLITHVLKK,Fatty acyl-CoA reductase 8,Catalyzes the reduction of fatty acyl-CoA to fatty alcohols. Catalyzes specifically the formation of C16:0 fatty alcohol.,converting its specificity from 16:0-CoA to 18:0-CoA.,Catalyzes the formation of C18:0 fatty alcohol instead of C16:0; when associated with T-347 and A-355. converting its specificity from 16:0-CoA to 18:0-CoA.
15,15,13983,Q8IB06-I57H,MGSCYSRKNKVSTISLDEEEKKKEKKKKKKIYILNGASGSGKDTQCRLLEKKYNYKHICISKLLKEYKEEYNKENVLNEEENYFDEIEKCMIDGSLVNDQIVIEIFHKQLNKYINDDKYNGIIINGFPRNYEQALLIIQNNISITKFINIQVGKDTLWTRINNRIIDPITNISYNENIIQIIKKKREGQELSDKEQKQLIIDNHLYNNLSNDILERLTKRKDDEEQVFNKRFQLYIESEQKINSLFKNICKNVDGEKSINDIFDQICSIIDDNPN,Loss of catalytic activity.,,MGSCYSRKNKVSTISLDEEEKKKEKKKKKKIYILNGASGSGKDTQCRLLEKKYNYKIICISKLLKEYKEEYNKENVLNEEENYFDEIEKCMIDGSLVNDQIVIEIFHKQLNKYINDDKYNGIIINGFPRNYEQALLIIQNNISITKFINIQVGKDTLWTRINNRIIDPITNISYNENIIQIIKKKREGQELSDKEQKQLIIDNHLYNNLSNDILERLTKRKDDEEQVFNKRFQLYIESEQKINSLFKNICKNVDGEKSINDIFDQICSIIDDNPN,Adenylate kinase 2,"Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Has very low activity with CTP, GTP, ITP and UTP and no activity with GMP, UMP or IMP in vitro.",,Loss of catalytic activity.
16,16,14153,Q9HSF6-H40A,MPVVECDIQTARAALADAGASFSDGNSEHELWHADLGDAAAVAYADKLVVQGGSPTDITAVVQPDRGGRVHAYFDGASRGNPGPAAVGWVLVSGDGGIVAEGGDTIGRATNNQAEYDALIAALEAAADFGFDDIELRGDSQLVEKQLTGAWDTNDPDLRRKRVRARELLTGFDDWSITHVPRATNERADALANEALDDA,No loss of RNase H activity.,,MPVVECDIQTARAALADAGASFSDGNSEHELWHADLGDAHAVAYADKLVVQGGSPTDITAVVQPDRGGRVHAYFDGASRGNPGPAAVGWVLVSGDGGIVAEGGDTIGRATNNQAEYDALIAALEAAADFGFDDIELRGDSQLVEKQLTGAWDTNDPDLRRKRVRARELLTGFDDWSITHVPRATNERADALANEALDDA,Ribonuclease HI,Nuclease that specifically degrades the RNA of RNA-DNA hybrids; seems to act exonucleolytically on RNA/DNA hybrids. Endonucleolytically removes RNA primers from the Okazaki fragments of lagging strand synthesis on its own. Complements the temperature-sensitive phenotype of an E.coli double rnhA/rnhB (RNase H) disruption mutant.,,No loss of RNase H activity.
17,17,14855,Q9AQS0-R612A,MLSGILIAALLMTLWGGWQPDIAHASDEFDALRIKWATLLTGGPALDPADSDIAARTDKLAQDANDYWEDMDLSSSRTYIWYALRGNGTSDNVNAVYERLRTMALAATTVGSSLYGNADLKEDILDALDWLYVNSYNSTRSRSAYNWWHWQLGIPMSLNDIAVLLYDDISAARMATYMDTIDYFTPSIGLTGANRAWQAIVVGVRAVIVKDAVKLAAARNGLSGTGIFPYATGGDGFYADGSFVQHTTFAYTGGYGSSVLETTANLMYLLSGSTWSVSDPNQSNVWQWIYEAYRPLLYKGAMMDMVRGREISRSYAQDHAVGHGIVASIVRLAQFAPAPHAAAFKQIAKRVIQEDTFSSFYGDVSTDTIRLAKAIVDDPSIAPAAAPNLYKQYAAMDRAVLQRPGFALGLALYSTRISSYESINSENGRGWYTGAGATYLYNQDLAQYSEDYWPTVDAYRIPGTTVASGTPIASGTGTSSWTGGVSLAGQYGASGMDLSYGAYNLSARKSWFMFDDEIVALGSGISSTAGIPIETVVDNRKLNGAGDNAWTANGAALSTGLGVAQTLTGVNWVHLAGNTADGSDIGYYFPGGATLQTKREARTGTWKQINNAPATPSTAVTRNYETMWIDHGTNPSGASYGYVLLPNKTSAQVGAYAADPAIEIVVNTSGVQSVKEKTLGLVGANFWTDTTQTADLITSNKKASVMTREIADERLEASVSDPTQANNGTIAIELARSAEGYSADPGITVTQLAPTIKFTVNVNGAKGKSFHASFQLGEDTSGPVDPGEPELPSVIVDNADSAGVTRTGTWKTASTQTDRYGANYLHDDNAGKGTKSVTFTPNLPIAGSYEVYLMWPAHFNREDAVQVDVGHASGTTRTAVDQRSGGGVWHSIGTYEFLAGSGGSVTIRNDALGSPDGYVVADAVKFVAVG,Increased catalysis rate but decreased affinity with substrate.,,MLSGILIAALLMTLWGGWQPDIAHASDEFDALRIKWATLLTGGPALDPADSDIAARTDKLAQDANDYWEDMDLSSSRTYIWYALRGNGTSDNVNAVYERLRTMALAATTVGSSLYGNADLKEDILDALDWLYVNSYNSTRSRSAYNWWHWQLGIPMSLNDIAVLLYDDISAARMATYMDTIDYFTPSIGLTGANRAWQAIVVGVRAVIVKDAVKLAAARNGLSGTGIFPYATGGDGFYADGSFVQHTTFAYTGGYGSSVLETTANLMYLLSGSTWSVSDPNQSNVWQWIYEAYRPLLYKGAMMDMVRGREISRSYAQDHAVGHGIVASIVRLAQFAPAPHAAAFKQIAKRVIQEDTFSSFYGDVSTDTIRLAKAIVDDPSIAPAAAPNLYKQYAAMDRAVLQRPGFALGLALYSTRISSYESINSENGRGWYTGAGATYLYNQDLAQYSEDYWPTVDAYRIPGTTVASGTPIASGTGTSSWTGGVSLAGQYGASGMDLSYGAYNLSARKSWFMFDDEIVALGSGISSTAGIPIETVVDNRKLNGAGDNAWTANGAALSTGLGVAQTLTGVNWVHLAGNTADGSDIGYYFPGGATLQTKREARTGTWKQINNRPATPSTAVTRNYETMWIDHGTNPSGASYGYVLLPNKTSAQVGAYAADPAIEIVVNTSGVQSVKEKTLGLVGANFWTDTTQTADLITSNKKASVMTREIADERLEASVSDPTQANNGTIAIELARSAEGYSADPGITVTQLAPTIKFTVNVNGAKGKSFHASFQLGEDTSGPVDPGEPELPSVIVDNADSAGVTRTGTWKTASTQTDRYGANYLHDDNAGKGTKSVTFTPNLPIAGSYEVYLMWPAHFNREDAVQVDVGHASGTTRTAVDQRSGGGVWHSIGTYEFLAGSGGSVTIRNDALGSPDGYVVADAVKFVAVG,Xanthan lyase,"Plays a role in xanthan depolymerization pathway by cleaving the linkage between the terminal mannosyl and glucuronyl residues of the side chain of xanthan to liberate pyruvylated mannose. Is highly specific for pyruvylated side-chains of xanthan and is not effective with hyaluronate, chondroitin A, gellan, heparin or pectin.",Site-directed mutagenesis of the two residues demonstrated that R612 is a key residue in recognizing pyruvated mannose.,Increased catalysis rate but decreased affinity with substrate. Site-directed mutagenesis of the two residues demonstrated that R612 is a key residue in recognizing pyruvated mannose.
18,18,16755,Q31125-H75A,MTMGLRAPHWVAVGLLTWAALGLLVAGHEGHGDLHKDVEEDFHGHSHGHSHEDFHHGHSHGHSHEDFHHGHGHTAESIWHGHAHSHDHGHSREELHHGHSHGHSHDSLHHGGHGHAHREHSHGTSREAGAPGIKHHLDTVTLWAYALGATVLISAAPFFVLFLIPVESNSPRHRSLLQILLSFASGGLLGDAFLHLIPHALEPHSHHAPEQPGHGHSHSGQGPILSVGLWVLSGIVAFLVVEKFVRHVKGGHGHSHGHGDRHAHGDSHTHGDRHECSSKEKPSTEEEKEVGGLRKRRGGNTGPRDGPVKPQSPEEEKAGSDLRVSGYLNLAADLAHNFTDGLAIGASFRGGRGLGILTTMTVLLHEVPHEVGDFAILVQSGCSKKQAMRLQLVTAIGALAGTACALLTEGGAVDSDVAGGAGPGWVLPFTAGGFIYVATVSVLPELLREASPLQSLLEVLGLLGGVAMMVLIAHLE,Abolished METTL9-mediated methylation.,,MTMGLRAPHWVAVGLLTWAALGLLVAGHEGHGDLHKDVEEDFHGHSHGHSHEDFHHGHSHGHSHEDFHHGHGHTHESIWHGHAHSHDHGHSREELHHGHSHGHSHDSLHHGGHGHAHREHSHGTSREAGAPGIKHHLDTVTLWAYALGATVLISAAPFFVLFLIPVESNSPRHRSLLQILLSFASGGLLGDAFLHLIPHALEPHSHHAPEQPGHGHSHSGQGPILSVGLWVLSGIVAFLVVEKFVRHVKGGHGHSHGHGDRHAHGDSHTHGDRHECSSKEKPSTEEEKEVGGLRKRRGGNTGPRDGPVKPQSPEEEKAGSDLRVSGYLNLAADLAHNFTDGLAIGASFRGGRGLGILTTMTVLLHEVPHEVGDFAILVQSGCSKKQAMRLQLVTAIGALAGTACALLTEGGAVDSDVAGGAGPGWVLPFTAGGFIYVATVSVLPELLREASPLQSLLEVLGLLGGVAMMVLIAHLE,Zinc transporter SLC39A7,"Transports Zn(2+) from the endoplasmic reticulum (ER)/Golgi apparatus to the cytosol, playing an essential role in the regulation of cytosolic zinc levels. Acts as gatekeeper of zinc release from intracellular stores, requiring post-translational activation by phosphorylation, resulting in activation of multiple downstream pathways leading to cell growth and proliferation. Has an essential role in B cell development and is required for proper B cell receptor signaling. Plays an important role in maintaining intestinal epithelial homeostasis and skin dermis development by regulating ER function. Controls cell signaling pathways involved in glucose metabolism in skeletal muscle. Has a protective role against ER stress in differents biological contexts. Mediates Zn(2+)-induced ferroptosis.",,Abolished METTL9-mediated methylation.
19,19,17150,Q7G065-T139V,MQFMMPLDTNACAQPMRRAGEGAGTERLMERLNIGGMTQEKALRKRCFGDGVTGTARCVFTSDADRDTPHLRTQSSRKNYADASHVSAVILGGGTGVQLFPLTSTRATPAVPVGGCYRLIDIPMSNCFNSGINKIFVMVQFNSASLNRHIHHTYLGGGINFTDGSVQVLAATQMPDEPAGWFQGTADAIRKFMWILEDHYNQNNIEHVVILCGDQLYRMNYMELVQKHVDDNADITISCAPIDGSRASDYGLVKFDDSGRVIQFLEKPEGADLESMKVDTSFLSYAIDDKQKYPYIASMGIYVLKKDVLLDILKSKYAHLQDFGSEILPRAVLEHNVKACVFTEYWEDIGTIKSFFDANLALTEQPPKFEFYDPKTPFFTSPRYLPPARLEKCKIKDAIISDGCSFSECTIEHSVIGISSRVSIGCELKDTMMMGADQYETEEETSKLLFEGKVPIGIGENTKIRNCIIDMNARIGRNVIIANTQGVQESDHPEEGYYIRSGIVVILKNATIKDGTVI,Reduces activity more than 3-fold.,,MQFMMPLDTNACAQPMRRAGEGAGTERLMERLNIGGMTQEKALRKRCFGDGVTGTARCVFTSDADRDTPHLRTQSSRKNYADASHVSAVILGGGTGVQLFPLTSTRATPAVPVGGCYRLIDIPMSNCFNSGINKIFVMTQFNSASLNRHIHHTYLGGGINFTDGSVQVLAATQMPDEPAGWFQGTADAIRKFMWILEDHYNQNNIEHVVILCGDQLYRMNYMELVQKHVDDNADITISCAPIDGSRASDYGLVKFDDSGRVIQFLEKPEGADLESMKVDTSFLSYAIDDKQKYPYIASMGIYVLKKDVLLDILKSKYAHLQDFGSEILPRAVLEHNVKACVFTEYWEDIGTIKSFFDANLALTEQPPKFEFYDPKTPFFTSPRYLPPARLEKCKIKDAIISDGCSFSECTIEHSVIGISSRVSIGCELKDTMMMGADQYETEEETSKLLFEGKVPIGIGENTKIRNCIIDMNARIGRNVIIANTQGVQESDHPEEGYYIRSGIVVILKNATIKDGTVI,"Glucose-1-phosphate adenylyltransferase large subunit 2, cytosolic","Involved in synthesis of starch. Catalyzes the synthesis of ADP-glucose, a molecule that serves as an activated glycosyl donor for alpha-1,4-glucan synthesis. Essential for starch synthesis in seed endosperm (PubMed:17406793, Ref.13, PubMed:24747952, PubMed:27957808). Is essential for both catalytic and allosteric regulatory properties of the cytosolic heterotetramer enzyme.",Seeds from the missense mutant containing were severely shriveled and had seed weight and starch content comparable with the shriveled seeds from OsAGPL2 null mutants. The catalytic and allosteric regulatory properties of the mutant enzyme were significantly impaired. The mutant enzyme had lower specific (catalytic) activity and affinity for the activator 3-phosphoglycerate (3-PGA). The mutant enzyme also showed more sensitivity to inhibition by the inhibitor inorganic phosphate (Pi) than the wild-type AGPase.,Reduces activity more than 3-fold. Seeds from the missense mutant containing were severely shriveled and had seed weight and starch content comparable with the shriveled seeds from OsAGPL2 null mutants. The catalytic and allosteric regulatory properties of the mutant enzyme were significantly impaired. The mutant enzyme had lower specific (catalytic) activity and affinity for the activator 3-phosphoglycerate (3-PGA). The mutant enzyme also showed more sensitivity to inhibition by the inhibitor inorganic phosphate (Pi) than the wild-type AGPase.
20,20,17910,B9EJA2-P540A,MATDSASCEPDLSRTPGDTEGATAEAAKKEFDVDTLSKSELRMLLSVMEGELEARDLVIEALRARRKEVFIQERYGRFNLNDPFLALQRDYEAGPGDKEKPVCTNPLSILEAVMAHCRKMQERMSAQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKNKHVVLMLVKECKQLSGKVVEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEIDKMKKMMEQMKKGSDGKPGLSLPRKTKDKRLASISVATEGPVTRSVACQTDVVTESTDPVKKLPLTVPIKPSTGSPLVPTNTKGNVGPSALLIRPGIDRQSSHSDLGPSPPTALPSSANRIEENGPSTGNAPDLSNSTPSTPSSTAPAAAQTPGTAPQNHSQAPTVHSLHSPCANTHPGLNPRIQAARFRFQGNANDPDQNGNNTQSPPSRDVSPTSRDNLVAKQLARNTVTQALSRFTSPQAGASSRLGVSPGGDAGTCPPVGRTGLKTPGAARVDRGNPAPIPPKKPGLSQTPSPPHPQLRASNAGAKVDNKIVASPPSTLPQGTKVVNEENVPKSSSPQLPPKPSIDLTVAPAGCPVSALATSQVGAWPAGTPGLNQPACSDSSLVIPATVAFCSSINPVSASSRSPGASDSLLVAASGWSPSLTPLLMSGGPAPLAGRPTLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFECIELLTAYNANINHSAAGGQTPLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVDSLKLLMYHRVRAHGNSLSSEEPKSGLFSLNGGESPTGPSKPVVPADLINHADKEGWTAAHIAASKGFKNCLEVLCRHGGLEPERRDKCNRTVHDVATDDCKHLLENLNALKIPLRISVGEIQPSNDVSDDFECEHTICTLNIRKQTSWEDFSKAVSQALTNHFQAISSDGWWSLEDG,Almost complete loss of CTTN-binding and loss of regulation of spine density; when associated with A-543.,,MATDSASCEPDLSRTPGDTEGATAEAAKKEFDVDTLSKSELRMLLSVMEGELEARDLVIEALRARRKEVFIQERYGRFNLNDPFLALQRDYEAGPGDKEKPVCTNPLSILEAVMAHCRKMQERMSAQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKNKHVVLMLVKECKQLSGKVVEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEIDKMKKMMEQMKKGSDGKPGLSLPRKTKDKRLASISVATEGPVTRSVACQTDVVTESTDPVKKLPLTVPIKPSTGSPLVPTNTKGNVGPSALLIRPGIDRQSSHSDLGPSPPTALPSSANRIEENGPSTGNAPDLSNSTPSTPSSTAPAAAQTPGTAPQNHSQAPTVHSLHSPCANTHPGLNPRIQAARFRFQGNANDPDQNGNNTQSPPSRDVSPTSRDNLVAKQLARNTVTQALSRFTSPQAGASSRLGVSPGGDAGTCPPVGRTGLKTPGAARVDRGNPPPIPPKKPGLSQTPSPPHPQLRASNAGAKVDNKIVASPPSTLPQGTKVVNEENVPKSSSPQLPPKPSIDLTVAPAGCPVSALATSQVGAWPAGTPGLNQPACSDSSLVIPATVAFCSSINPVSASSRSPGASDSLLVAASGWSPSLTPLLMSGGPAPLAGRPTLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFECIELLTAYNANINHSAAGGQTPLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVDSLKLLMYHRVRAHGNSLSSEEPKSGLFSLNGGESPTGPSKPVVPADLINHADKEGWTAAHIAASKGFKNCLEVLCRHGGLEPERRDKCNRTVHDVATDDCKHLLENLNALKIPLRISVGEIQPSNDVSDDFECEHTICTLNIRKQTSWEDFSKAVSQALTNHFQAISSDGWWSLEDG,Cortactin-binding protein 2,"Regulates the dendritic spine distribution of CTTN/cortactin in hippocampal neurons, and thus controls dendritic spinogenesis and dendritic spine maintenance.",,Almost complete loss of CTTN-binding and loss of regulation of spine density; when associated with A-543.
21,21,19813,O15393-V160M,MALNSGSPPAIGPYYENHGYQPENPYPAQPTVVPTVYEVHPAQYYPSPVPQYAPRVLTQASNPVVCTQPKSPSGTVCTSKTKKALCITLTLGTFLVGAALAAGLLWKFMGSKCSNSGIECDSSGTCINPSNWCDGVSHCPGGEDENRCVRLYGPNFILQMYSSQRKSWHPVCQDDWNENYGRAACRDMGYKNNFYSSQGIVDDSGSTSFMKLNTSAGNVDIYKKLYHSDACSSKAVVSLRCIACGVNLNSSRQSRIVGGESALPGAWPWQVSLHVQNVHVCGGSIITPEWIVTAAHCVEKPLNNPWHWTAFAGILRQSFMFYGAGYQVEKVISHPNYDSKTKNNDIALMKLQKPLTFNDLVKPVCLPNPGMMLQPEQLCWISGWGATEEKGKTSEVLNAAKVLLIETQRCNSRYVYDNLITPAMICAGFLQGNVDSCQGDSGGPLVTSKNNIWWLIGDTSWGSGCAKAYRPGVYGNVMVFTDWIYRQMRADG,,,MALNSGSPPAIGPYYENHGYQPENPYPAQPTVVPTVYEVHPAQYYPSPVPQYAPRVLTQASNPVVCTQPKSPSGTVCTSKTKKALCITLTLGTFLVGAALAAGLLWKFMGSKCSNSGIECDSSGTCINPSNWCDGVSHCPGGEDENRCVRLYGPNFILQVYSSQRKSWHPVCQDDWNENYGRAACRDMGYKNNFYSSQGIVDDSGSTSFMKLNTSAGNVDIYKKLYHSDACSSKAVVSLRCIACGVNLNSSRQSRIVGGESALPGAWPWQVSLHVQNVHVCGGSIITPEWIVTAAHCVEKPLNNPWHWTAFAGILRQSFMFYGAGYQVEKVISHPNYDSKTKNNDIALMKLQKPLTFNDLVKPVCLPNPGMMLQPEQLCWISGWGATEEKGKTSEVLNAAKVLLIETQRCNSRYVYDNLITPAMICAGFLQGNVDSCQGDSGGPLVTSKNNIWWLIGDTSWGSGCAKAYRPGVYGNVMVFTDWIYRQMRADG,Transmembrane protease serine 2,"Plasma membrane-anchored serine protease that cleaves at arginine residues. Participates in proteolytic cascades of relevance for the normal physiologic function of the prostate. Androgen-induced TMPRSS2 activates several substrates that include pro-hepatocyte growth factor/HGF, the protease activated receptor-2/F2RL1 or matriptase/ST14 leading to extracellular matrix disruption and metastasis of prostate cancer cells. In addition, activates trigeminal neurons and contribute to both spontaneous pain and mechanical allodynia.(Microbial infection) Facilitates human coronaviruses SARS-CoV and SARS-CoV-2 infections via two independent mechanisms, proteolytic cleavage of ACE2 receptor which promotes viral uptake, and cleavage of coronavirus spike glycoproteins which activates the glycoprotein for host cell entry. The cleavage of SARS-COV2 spike glycoprotein occurs between the S2 and S2' site. Upon SARS-CoV-2 infection, increases syncytia formation by accelerating the fusion process. Proteolytically cleaves and activates the spike glycoproteins of human coronavirus 229E (HCoV-229E) and human coronavirus EMC (HCoV-EMC) and the fusion glycoproteins F0 of Sendai virus (SeV), human metapneumovirus (HMPV), human parainfluenza 1, 2, 3, 4a and 4b viruses (HPIV). Essential for spread and pathogenesis of influenza A virus (strains H1N1, H3N2 and H7N9); involved in proteolytic cleavage and activation of hemagglutinin (HA) protein which is essential for viral infectivity.","This mutation may affect the function of the TMPRSS2 protein, although the specific functional changes are not mentioned in the document.","This mutation may affect the function of the TMPRSS2 protein, although the specific functional changes are not mentioned in the document."
22,22,20472,P25522-N226A,MSDNDTIVAQATPPGRGGVGILRISGFKAREVAETVLGKLPKPRYADYLPFKDADGSVLDQGIALWFPGPNSFTGEDVLELQGHGGPVILDLLLKRILTIPGLRIARPGEFSERAFLNDKLDLAQAEAIADLIDASSEQAARSALNSLQGAFSARVNHLVEALTHLRIYVEAAIDFPDEEIDFLSDGKIEAQLNDVIADLDAVRAEARQGSLLREGMKVVIAGRPAAGKSSLLNALAGREAAIVTDIAGTTRDVLREHIHIDGMPLHIIDTAGLREASDEVERIGIERAWQEIEQADRVLFMVDGTTTDAVDPAEIWPEFIARLPAKLPITVVRNKADITGETLGMSEVNGHALIRLSARTGEGVDVLRNHLKQSMGFDTNMEGGFLARRRHLQALEQAAEHLQQGKAQLLGAWAGELLAEELRLAQQNLSEITGEFTSDDLLGRIFSSFCIGK,100-fold decrease in GTPase activity. 5-fold decrease of affinity for GTP.,,MSDNDTIVAQATPPGRGGVGILRISGFKAREVAETVLGKLPKPRYADYLPFKDADGSVLDQGIALWFPGPNSFTGEDVLELQGHGGPVILDLLLKRILTIPGLRIARPGEFSERAFLNDKLDLAQAEAIADLIDASSEQAARSALNSLQGAFSARVNHLVEALTHLRIYVEAAIDFPDEEIDFLSDGKIEAQLNDVIADLDAVRAEARQGSLLREGMKVVIAGRPNAGKSSLLNALAGREAAIVTDIAGTTRDVLREHIHIDGMPLHIIDTAGLREASDEVERIGIERAWQEIEQADRVLFMVDGTTTDAVDPAEIWPEFIARLPAKLPITVVRNKADITGETLGMSEVNGHALIRLSARTGEGVDVLRNHLKQSMGFDTNMEGGFLARRRHLQALEQAAEHLQQGKAQLLGAWAGELLAEELRLAQQNLSEITGEFTSDDLLGRIFSSFCIGK,tRNA modification GTPase MnmE,"Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.",,100-fold decrease in GTPase activity. 5-fold decrease of affinity for GTP.
23,23,21132,Q9ULZ3-L12A,MGRARDAILDAAENLTAEELKKFKLKLLSVPLREGYGRIPRGALLSMDALDLTDKLVSFYLETYGAELTANVLRDMGLQEMAGQLQAATHQGSGAAPAGIQAPPQSAAKPGLHFIDQHRAALIARVTNVEWLLDALYGKVLTDEQYQAVRAEPTNPSKMRKLFSFTPAWNWTCKDLLLQALRESQSYLVEDLERS,Abolishes homooligomerization.,,MGRARDAILDALENLTAEELKKFKLKLLSVPLREGYGRIPRGALLSMDALDLTDKLVSFYLETYGAELTANVLRDMGLQEMAGQLQAATHQGSGAAPAGIQAPPQSAAKPGLHFIDQHRAALIARVTNVEWLLDALYGKVLTDEQYQAVRAEPTNPSKMRKLFSFTPAWNWTCKDLLLQALRESQSYLVEDLERS,Apoptosis-associated speck-like protein containing a CARD,"Functions as key mediator in apoptosis and inflammation. Promotes caspase-mediated apoptosis involving predominantly caspase-8 and also caspase-9 in a probable cell type-specific manner. Involved in activation of the mitochondrial apoptotic pathway, promotes caspase-8-dependent proteolytic maturation of BID independently of FADD in certain cell types and also mediates mitochondrial translocation of BAX and activates BAX-dependent apoptosis coupled to activation of caspase-9, -2 and -3. Involved in innate immune response by acting as an integral adapter in the assembly of various inflammasomes (NLRP1, NLRP2, NLRP3, NLRP6, AIM2 and probably IFI16) which recruit and activate caspase-1 leading to processing and secretion of pro-inflammatory cytokines. Caspase-1-dependent inflammation leads to macrophage pyroptosis, a form of cell death. The function as activating adapter in different types of inflammasomes is mediated by the pyrin and CARD domains and their homotypic interactions. Clustered PYCARD nucleates the formation of caspase-1 filaments through the interaction of their respective CARD domains, acting as a platform for of caspase-1 polymerization. In the NLRP1 and NLRC4 inflammasomes seems not be required but facilitates the processing of procaspase-1. In cooperation with NOD2 involved in an inflammasome activated by bacterial muramyl dipeptide leading to caspase-1 activation. May be involved in RIGI-triggered pro-inflammatory responses and inflammasome activation. In collaboration with AIM2 which detects cytosolic double-stranded DNA may also be involved in a caspase-1-independent cell death that involves caspase-8. In adaptive immunity may be involved in maturation of dendritic cells to stimulate T-cell immunity and in cytoskeletal rearrangements coupled to chemotaxis and antigen uptake may be involved in post-transcriptional regulation of the guanine nucleotide exchange factor DOCK2; the latter function is proposed to involve the nuclear form. Also involved in transcriptional activation of cytokines and chemokines independent of the inflammasome; this function may involve AP-1, NF-kappa-B, MAPK and caspase-8 signaling pathways. For regulation of NF-kappa-B activating and inhibiting functions have been reported. Modulates NF-kappa-B induction at the level of the IKK complex by inhibiting kinase activity of CHUK and IKBK. Proposed to compete with RIPK2 for association with CASP1 thereby down-regulating CASP1-mediated RIPK2-dependent NF-kappa-B activation and activating interleukin-1 beta processing. Modulates host resistance to DNA virus infection, probably by inducing the cleavage of and inactivating CGAS in presence of cytoplasmic double-stranded DNA.May have a regulating effect on the function as inflammasome adapter.Seems to inhibit inflammasome-mediated maturation of interleukin-1 beta.",The mutation in ASC induces both apoptosis and NF-kappa B activation. Mutation of L12 to A in ASC protein leads to loss of filament formation.,Abolishes homooligomerization. The mutation in ASC induces both apoptosis and NF-kappa B activation. Mutation of L12 to A in ASC protein leads to loss of filament formation.
24,24,21334,Q0IGK1-D429A,MVPPIIYKYKRRKDRRLGRDDDSSVMMTRRRPDSDFIEVSDENRSFALFKEDDEKNRDLGLVDDGSTNLVLQCHDDGCSLEKDNSNSLDDLFSGFVYKGVRRRKRDDFGSITTSNLVSPQIADDDDDSVSDSHIERQECSEFHVEVRRVSPYFQGSTVSQQSKEGCDSDSVCSKEGCSKVQAKVPRVSPYFQASTISQCDSDIVSSSQSGRNYRKGSSKRQVKVRRVSPYFQESTVSEQPNQAPKGLRNYFKVVKVSRYFHADGIQVNESQKEKSRNVRKTPIVSPVLSLSQKTDDVYLRKTPDNTWVPPRSPCNLLQEDHWHDPWRVLVICMLLNKTSGAQTRGVISDLFGLCTDAKTATEVKEEEIENLIKPLGLQKKRTKMIQRLSLEYLQESWTHVTQLHGVGKYAADAYAIFCNGNWDRVKPNAHMLNYYWDYLRIRYKL,Reduces activity 160-fold.,,MVPPIIYKYKRRKDRRLGRDDDSSVMMTRRRPDSDFIEVSDENRSFALFKEDDEKNRDLGLVDDGSTNLVLQCHDDGCSLEKDNSNSLDDLFSGFVYKGVRRRKRDDFGSITTSNLVSPQIADDDDDSVSDSHIERQECSEFHVEVRRVSPYFQGSTVSQQSKEGCDSDSVCSKEGCSKVQAKVPRVSPYFQASTISQCDSDIVSSSQSGRNYRKGSSKRQVKVRRVSPYFQESTVSEQPNQAPKGLRNYFKVVKVSRYFHADGIQVNESQKEKSRNVRKTPIVSPVLSLSQKTDDVYLRKTPDNTWVPPRSPCNLLQEDHWHDPWRVLVICMLLNKTSGAQTRGVISDLFGLCTDAKTATEVKEEEIENLIKPLGLQKKRTKMIQRLSLEYLQESWTHVTQLHGVGKYAADAYAIFCNGNWDRVKPNDHMLNYYWDYLRIRYKL,Methyl-CpG-binding domain protein 4-like protein,"Monofunctional DNA glycosylase targeting U:G and T:G mispairs. Excises uracil derivatives and exhibits a preference for a CpG sequence context, irrespective of the methylation status of the complementary strand. The activity follows a biphasic kinetics, with an initial burst of product accumulation followed by a slower phase. Specifically binds its reaction product. Triggers the base excision repair (BER) pathway.","The enzyme binds to the abasic site product generated after excision, which decreases its catalytic turnover in vitro.","Reduces activity 160-fold. The enzyme binds to the abasic site product generated after excision, which decreases its catalytic turnover in vitro."
25,25,21563,P15917-H75A,MNIKKEFIKVISMSCLVTAITLSGPVFIPLVQGAGGHGDVGMHVKEKEKNKDENKRKDEERNKTQEEHLKEIMKAIVKIEVKGEEAVKKEAAEKLLEKVPSDVLEMYKAIGGKIYIVDGDITKHISLEALSEDKKKIKDIYGKDALLHEHYVYAKEGYEPVLVIQSSEDYVENTEKALNVYYEIGKILSRDILSKINQPYQKFLDVLNTIKNASDSDGQDLLFTNQLKEHPTDFSVEFLEQNSNEVQEVFAKAFAYYIEPQHRDVLQLYAPEAFNYMDKFNEQEINLSLEELKDQRMLARYEKWEKIKQHYQHWSDSLSEEGRGLLKKLQIPIEPKKDDIIHSLSQEEKELLKRIQIDSSDFLSTEEKEFLKKLQIDIRDSLSEEEKELLNRIQVDSSNPLSEKEKEFLKKLKLDIQPYDINQRLQDTGGLIDSPSINLDVRKQYKRDIQNIDALLHQSIGSTLYNKIYLYENMNINNLTATLGADLVDSTDNTKINRGIFNEFKKNFKYSISSNYMIVDINERPALDNERLKWRIQLSPDTRAGYLENGKLILQRNIGLEIKDVQIIKQSEKEYIRIDAKVVPKSKIDTKIQEAQLNINQEWNKALGLPKYTKLITFNVHNRYASNIVESAYLILNEWKNNIQSDLIKKVTNYLVDGNGRFVFTDITLPNIAEQYTHQDEIYEQVHSKGLYVPESRSILLHGPSKGVELRNDSEGFIHEFGHAVDDYAGYLLDKNQSDLVTNSKKFIDIFKEEGSNLTSYGRTNEAEFFAEAFRLMHSTDHAERLKVQKNAPKTFQFINDQIKFIINS,Impaired translocation into host cytoplasm.,,MNIKKEFIKVISMSCLVTAITLSGPVFIPLVQGAGGHGDVGMHVKEKEKNKDENKRKDEERNKTQEEHLKEIMKHIVKIEVKGEEAVKKEAAEKLLEKVPSDVLEMYKAIGGKIYIVDGDITKHISLEALSEDKKKIKDIYGKDALLHEHYVYAKEGYEPVLVIQSSEDYVENTEKALNVYYEIGKILSRDILSKINQPYQKFLDVLNTIKNASDSDGQDLLFTNQLKEHPTDFSVEFLEQNSNEVQEVFAKAFAYYIEPQHRDVLQLYAPEAFNYMDKFNEQEINLSLEELKDQRMLARYEKWEKIKQHYQHWSDSLSEEGRGLLKKLQIPIEPKKDDIIHSLSQEEKELLKRIQIDSSDFLSTEEKEFLKKLQIDIRDSLSEEEKELLNRIQVDSSNPLSEKEKEFLKKLKLDIQPYDINQRLQDTGGLIDSPSINLDVRKQYKRDIQNIDALLHQSIGSTLYNKIYLYENMNINNLTATLGADLVDSTDNTKINRGIFNEFKKNFKYSISSNYMIVDINERPALDNERLKWRIQLSPDTRAGYLENGKLILQRNIGLEIKDVQIIKQSEKEYIRIDAKVVPKSKIDTKIQEAQLNINQEWNKALGLPKYTKLITFNVHNRYASNIVESAYLILNEWKNNIQSDLIKKVTNYLVDGNGRFVFTDITLPNIAEQYTHQDEIYEQVHSKGLYVPESRSILLHGPSKGVELRNDSEGFIHEFGHAVDDYAGYLLDKNQSDLVTNSKKFIDIFKEEGSNLTSYGRTNEAEFFAEAFRLMHSTDHAERLKVQKNAPKTFQFINDQIKFIINS,Lethal factor,"Lethal factor (LF), which constitutes one of the three proteins composing the anthrax toxin, is able to trigger rapid cell death in macrophages. Acts as a protease that cleaves the N-terminal of most dual specificity mitogen-activated protein kinase kinases (MAPKKs or MAP2Ks) (except for MAP2K5): cleavage invariably occurs within the N-terminal proline-rich region preceding the kinase domain, thus disrupting a sequence involved in directing specific protein-protein interactions necessary for the assembly of signaling complexes. Also cleaves mouse Nlrp1b: host Nlrp1b cleavage promotes ubiquitination and degradation of the N-terminal part of Nlrp1b by the proteasome, thereby releasing the cleaved C-terminal part of Nlrp1b, which polymerizes and forms the Nlrp1b inflammasome followed by host cell pyroptosis. Able to cleave mouse Nlrp1b alleles 1 and 5, while it is not able to cleave Nlrp1b alleles 2, 3 and 4. In contrast, does not cleave NLRP1 human ortholog. LF is not toxic by itself and only acts as a lethal factor when associated with protective antigen (PA) to form the lethal toxin (LeTx): PA is required for LF translocation into the host cytosol.",,Impaired translocation into host cytoplasm.
26,26,22948,Q9JJS6-E457A,MEIIFGQNKKEQLEPVQAKVTGSIPAWLQGTLLRNGPGMHTVGESKYNHWFDGLALLHSFSIRDGEVFYRSKYLQSDTYIANIEANRIVVSEFGTMAYPDPCKNIFSKAFSYLSHTIPDFTDNCLINIMKCGEDFYATTETNYIRKIDPQTLETLEKVDYRKYVAVNLATSHPHYDEAGNVLNMGTSVVDKGRTKYVIFKIPATVPDSKKKGKSPVKHAEVFCSISSRSLLSPSYYHSFGVTENYVVFLEQPFKLDILKMATAYMRGVSWASCMSFDREDKTYIHIIDQRTRKPVPTKFYTDPMVVFHHVNAYEEDGCVLFDVIAYEDSSLYQLFYLANLNKDFEEKSRLTSVPTLRRFAVPLHVDKDAEVGSNLVKVSSTTATALKEKDGHVYCQPEVLYEGLELPRINYAYNGKPYRYIFAAEVQWSPVPTKILKYDILTKSSLKWSEESCWPAAPLFVPTPGAKDEDDGVILSAIVSTDPQKLPFLLILDAKSFTELARASVDADMHLDLHGLFIPDADWNAVKQTPAETQEVENSDHPTDPTAPELSHSENDFTAGHGGSSL,"Decreased beta-carotene 15,15'-monooxygenase activity.",,MEIIFGQNKKEQLEPVQAKVTGSIPAWLQGTLLRNGPGMHTVGESKYNHWFDGLALLHSFSIRDGEVFYRSKYLQSDTYIANIEANRIVVSEFGTMAYPDPCKNIFSKAFSYLSHTIPDFTDNCLINIMKCGEDFYATTETNYIRKIDPQTLETLEKVDYRKYVAVNLATSHPHYDEAGNVLNMGTSVVDKGRTKYVIFKIPATVPDSKKKGKSPVKHAEVFCSISSRSLLSPSYYHSFGVTENYVVFLEQPFKLDILKMATAYMRGVSWASCMSFDREDKTYIHIIDQRTRKPVPTKFYTDPMVVFHHVNAYEEDGCVLFDVIAYEDSSLYQLFYLANLNKDFEEKSRLTSVPTLRRFAVPLHVDKDAEVGSNLVKVSSTTATALKEKDGHVYCQPEVLYEGLELPRINYAYNGKPYRYIFAAEVQWSPVPTKILKYDILTKSSLKWSEESCWPAEPLFVPTPGAKDEDDGVILSAIVSTDPQKLPFLLILDAKSFTELARASVDADMHLDLHGLFIPDADWNAVKQTPAETQEVENSDHPTDPTAPELSHSENDFTAGHGGSSL,"Beta,beta-carotene 15,15'-dioxygenase",Symmetrically cleaves beta-carotene into two molecules of retinal using a dioxygenase mechanism.,Mutation of E457 caused total loss of activity.,"Decreased beta-carotene 15,15'-monooxygenase activity. Mutation of E457 caused total loss of activity."
27,27,23871,Q31125-H204A,MTMGLRAPHWVAVGLLTWAALGLLVAGHEGHGDLHKDVEEDFHGHSHGHSHEDFHHGHSHGHSHEDFHHGHGHTHESIWHGHAHSHDHGHSREELHHGHSHGHSHDSLHHGGHGHAHREHSHGTSREAGAPGIKHHLDTVTLWAYALGATVLISAAPFFVLFLIPVESNSPRHRSLLQILLSFASGGLLGDAFLHLIPHALEPASHHAPEQPGHGHSHSGQGPILSVGLWVLSGIVAFLVVEKFVRHVKGGHGHSHGHGDRHAHGDSHTHGDRHECSSKEKPSTEEEKEVGGLRKRRGGNTGPRDGPVKPQSPEEEKAGSDLRVSGYLNLAADLAHNFTDGLAIGASFRGGRGLGILTTMTVLLHEVPHEVGDFAILVQSGCSKKQAMRLQLVTAIGALAGTACALLTEGGAVDSDVAGGAGPGWVLPFTAGGFIYVATVSVLPELLREASPLQSLLEVLGLLGGVAMMVLIAHLE,Decreased METTL9-mediated methylation; when associated with A-216.,,MTMGLRAPHWVAVGLLTWAALGLLVAGHEGHGDLHKDVEEDFHGHSHGHSHEDFHHGHSHGHSHEDFHHGHGHTHESIWHGHAHSHDHGHSREELHHGHSHGHSHDSLHHGGHGHAHREHSHGTSREAGAPGIKHHLDTVTLWAYALGATVLISAAPFFVLFLIPVESNSPRHRSLLQILLSFASGGLLGDAFLHLIPHALEPHSHHAPEQPGHGHSHSGQGPILSVGLWVLSGIVAFLVVEKFVRHVKGGHGHSHGHGDRHAHGDSHTHGDRHECSSKEKPSTEEEKEVGGLRKRRGGNTGPRDGPVKPQSPEEEKAGSDLRVSGYLNLAADLAHNFTDGLAIGASFRGGRGLGILTTMTVLLHEVPHEVGDFAILVQSGCSKKQAMRLQLVTAIGALAGTACALLTEGGAVDSDVAGGAGPGWVLPFTAGGFIYVATVSVLPELLREASPLQSLLEVLGLLGGVAMMVLIAHLE,Zinc transporter SLC39A7,"Transports Zn(2+) from the endoplasmic reticulum (ER)/Golgi apparatus to the cytosol, playing an essential role in the regulation of cytosolic zinc levels. Acts as gatekeeper of zinc release from intracellular stores, requiring post-translational activation by phosphorylation, resulting in activation of multiple downstream pathways leading to cell growth and proliferation. Has an essential role in B cell development and is required for proper B cell receptor signaling. Plays an important role in maintaining intestinal epithelial homeostasis and skin dermis development by regulating ER function. Controls cell signaling pathways involved in glucose metabolism in skeletal muscle. Has a protective role against ER stress in differents biological contexts. Mediates Zn(2+)-induced ferroptosis.",,Decreased METTL9-mediated methylation; when associated with A-216.
28,28,24074,Q68CZ1-A695P,MSGPTDETAGDLPVKDTGLNLFGMGGLQETSTTRTMKSRQAVSRVSREELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIRLVNDKKRYERVGGGPKRLGRDVEMEEMIEQLQEKVHELEKQNETLKNRLISAKQQLQTQGYRQTPYNNVQSRINTGRRKANENAGLQECPRKGIKFQDADVAETPHPMFTKYGNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIELSLLQLREQQATDQRSNIRDNVEMIKLHKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQLHSMKFSERRIEELQDRINDLEKERELLKENYDKLYDSAFSAAHEEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQQLDELKKRIKLYNQENDINADELSEALLLIKAQKEQKNGDLSFLVKVDSEINKDLERSMRELQATHAETVQELEKTRNMLIMQHKINKDYQMEVEAVTRKMENLQQDYELKVEQYVHLLDIRAARIHKLEAQLKDIAYGTKQYKFKPEIMPDDSVDEFDETIHLERGENLFEIHINKVTFSSEVLQASGDKEPVTFCTYAFYDFELQTTPVVRGLHPEYNFTSQYLVHVNDLFLQYIQKNTITLEVHQAYSTEYETIAPCQLKFHEILEKSGRIFCTASLIGTKGDIPNFGTVEYWFRLRVPMDQAIRLYRERAKALGYITSNFKGPEHMQSLSQQAPKTAQLSSTDSTDGNLNELHITIRCCNHLQSRASHLQPHPYVVYKFFDFADHDTAIIPSSNDPQFDDHMYFPVPMNMDLDRYLKSESLSFYVFDDSDTQENIYIGKVNVPLISLAHDRCISGIFELTDHQKHPAGTIHVILKWKFAYLPPSGSITTEDLGNFIRSEEPEVVQRLPPASSVSTLVLAPRPKPRQRLTPVDKKVSFVDIMPHQSDETSPPPEDRKEISPEVEHIPEIEINMLTVPHVPKVSQE,In JBTS7; seems not to affect interaction with NPHP4.,,MSGPTDETAGDLPVKDTGLNLFGMGGLQETSTTRTMKSRQAVSRVSREELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIRLVNDKKRYERVGGGPKRLGRDVEMEEMIEQLQEKVHELEKQNETLKNRLISAKQQLQTQGYRQTPYNNVQSRINTGRRKANENAGLQECPRKGIKFQDADVAETPHPMFTKYGNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIELSLLQLREQQATDQRSNIRDNVEMIKLHKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQLHSMKFSERRIEELQDRINDLEKERELLKENYDKLYDSAFSAAHEEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQQLDELKKRIKLYNQENDINADELSEALLLIKAQKEQKNGDLSFLVKVDSEINKDLERSMRELQATHAETVQELEKTRNMLIMQHKINKDYQMEVEAVTRKMENLQQDYELKVEQYVHLLDIRAARIHKLEAQLKDIAYGTKQYKFKPEIMPDDSVDEFDETIHLERGENLFEIHINKVTFSSEVLQASGDKEPVTFCTYAFYDFELQTTPVVRGLHPEYNFTSQYLVHVNDLFLQYIQKNTITLEVHQAYSTEYETIAACQLKFHEILEKSGRIFCTASLIGTKGDIPNFGTVEYWFRLRVPMDQAIRLYRERAKALGYITSNFKGPEHMQSLSQQAPKTAQLSSTDSTDGNLNELHITIRCCNHLQSRASHLQPHPYVVYKFFDFADHDTAIIPSSNDPQFDDHMYFPVPMNMDLDRYLKSESLSFYVFDDSDTQENIYIGKVNVPLISLAHDRCISGIFELTDHQKHPAGTIHVILKWKFAYLPPSGSITTEDLGNFIRSEEPEVVQRLPPASSVSTLVLAPRPKPRQRLTPVDKKVSFVDIMPHQSDETSPPPEDRKEISPEVEHIPEIEINMLTVPHVPKVSQE,Protein fantom,"Negatively regulates signaling through the G-protein coupled thromboxane A2 receptor (TBXA2R). May be involved in mechanisms like programmed cell death, craniofacial development, patterning of the limbs, and formation of the left-right axis. Involved in the organization of apical junctions; the function is proposed to implicate a NPHP1-4-8 module. Does not seem to be strictly required for ciliogenesis. Involved in establishment of planar cell polarity such as in cochlear sensory epithelium and is proposed to implicate stabilization of disheveled proteins. Involved in regulation of proteasomal activity at the primary cilium probably implicating association with PSDM2.",The RPGRIP1L missense mutations found in CORS individuals diminishes the interaction between RPGRIP1L and nephrocystin-4.,In JBTS7; seems not to affect interaction with NPHP4. The RPGRIP1L missense mutations found in CORS individuals diminishes the interaction between RPGRIP1L and nephrocystin-4.
29,29,24410,Q9JJS6-H58A,MEIIFGQNKKEQLEPVQAKVTGSIPAWLQGTLLRNGPGMHTVGESKYNHWFDGLALLASFSIRDGEVFYRSKYLQSDTYIANIEANRIVVSEFGTMAYPDPCKNIFSKAFSYLSHTIPDFTDNCLINIMKCGEDFYATTETNYIRKIDPQTLETLEKVDYRKYVAVNLATSHPHYDEAGNVLNMGTSVVDKGRTKYVIFKIPATVPDSKKKGKSPVKHAEVFCSISSRSLLSPSYYHSFGVTENYVVFLEQPFKLDILKMATAYMRGVSWASCMSFDREDKTYIHIIDQRTRKPVPTKFYTDPMVVFHHVNAYEEDGCVLFDVIAYEDSSLYQLFYLANLNKDFEEKSRLTSVPTLRRFAVPLHVDKDAEVGSNLVKVSSTTATALKEKDGHVYCQPEVLYEGLELPRINYAYNGKPYRYIFAAEVQWSPVPTKILKYDILTKSSLKWSEESCWPAEPLFVPTPGAKDEDDGVILSAIVSTDPQKLPFLLILDAKSFTELARASVDADMHLDLHGLFIPDADWNAVKQTPAETQEVENSDHPTDPTAPELSHSENDFTAGHGGSSL,"No significant effect on beta-carotene 15,15'-monooxygenase activity. Decreased catalytic efficiency.",,MEIIFGQNKKEQLEPVQAKVTGSIPAWLQGTLLRNGPGMHTVGESKYNHWFDGLALLHSFSIRDGEVFYRSKYLQSDTYIANIEANRIVVSEFGTMAYPDPCKNIFSKAFSYLSHTIPDFTDNCLINIMKCGEDFYATTETNYIRKIDPQTLETLEKVDYRKYVAVNLATSHPHYDEAGNVLNMGTSVVDKGRTKYVIFKIPATVPDSKKKGKSPVKHAEVFCSISSRSLLSPSYYHSFGVTENYVVFLEQPFKLDILKMATAYMRGVSWASCMSFDREDKTYIHIIDQRTRKPVPTKFYTDPMVVFHHVNAYEEDGCVLFDVIAYEDSSLYQLFYLANLNKDFEEKSRLTSVPTLRRFAVPLHVDKDAEVGSNLVKVSSTTATALKEKDGHVYCQPEVLYEGLELPRINYAYNGKPYRYIFAAEVQWSPVPTKILKYDILTKSSLKWSEESCWPAEPLFVPTPGAKDEDDGVILSAIVSTDPQKLPFLLILDAKSFTELARASVDADMHLDLHGLFIPDADWNAVKQTPAETQEVENSDHPTDPTAPELSHSENDFTAGHGGSSL,"Beta,beta-carotene 15,15'-dioxygenase",Symmetrically cleaves beta-carotene into two molecules of retinal using a dioxygenase mechanism.,,"No significant effect on beta-carotene 15,15'-monooxygenase activity. Decreased catalytic efficiency."
30,30,25056,P15917-I76A,MNIKKEFIKVISMSCLVTAITLSGPVFIPLVQGAGGHGDVGMHVKEKEKNKDENKRKDEERNKTQEEHLKEIMKHAVKIEVKGEEAVKKEAAEKLLEKVPSDVLEMYKAIGGKIYIVDGDITKHISLEALSEDKKKIKDIYGKDALLHEHYVYAKEGYEPVLVIQSSEDYVENTEKALNVYYEIGKILSRDILSKINQPYQKFLDVLNTIKNASDSDGQDLLFTNQLKEHPTDFSVEFLEQNSNEVQEVFAKAFAYYIEPQHRDVLQLYAPEAFNYMDKFNEQEINLSLEELKDQRMLARYEKWEKIKQHYQHWSDSLSEEGRGLLKKLQIPIEPKKDDIIHSLSQEEKELLKRIQIDSSDFLSTEEKEFLKKLQIDIRDSLSEEEKELLNRIQVDSSNPLSEKEKEFLKKLKLDIQPYDINQRLQDTGGLIDSPSINLDVRKQYKRDIQNIDALLHQSIGSTLYNKIYLYENMNINNLTATLGADLVDSTDNTKINRGIFNEFKKNFKYSISSNYMIVDINERPALDNERLKWRIQLSPDTRAGYLENGKLILQRNIGLEIKDVQIIKQSEKEYIRIDAKVVPKSKIDTKIQEAQLNINQEWNKALGLPKYTKLITFNVHNRYASNIVESAYLILNEWKNNIQSDLIKKVTNYLVDGNGRFVFTDITLPNIAEQYTHQDEIYEQVHSKGLYVPESRSILLHGPSKGVELRNDSEGFIHEFGHAVDDYAGYLLDKNQSDLVTNSKKFIDIFKEEGSNLTSYGRTNEAEFFAEAFRLMHSTDHAERLKVQKNAPKTFQFINDQIKFIINS,Does not affect translocation into host cytoplasm.,,MNIKKEFIKVISMSCLVTAITLSGPVFIPLVQGAGGHGDVGMHVKEKEKNKDENKRKDEERNKTQEEHLKEIMKHIVKIEVKGEEAVKKEAAEKLLEKVPSDVLEMYKAIGGKIYIVDGDITKHISLEALSEDKKKIKDIYGKDALLHEHYVYAKEGYEPVLVIQSSEDYVENTEKALNVYYEIGKILSRDILSKINQPYQKFLDVLNTIKNASDSDGQDLLFTNQLKEHPTDFSVEFLEQNSNEVQEVFAKAFAYYIEPQHRDVLQLYAPEAFNYMDKFNEQEINLSLEELKDQRMLARYEKWEKIKQHYQHWSDSLSEEGRGLLKKLQIPIEPKKDDIIHSLSQEEKELLKRIQIDSSDFLSTEEKEFLKKLQIDIRDSLSEEEKELLNRIQVDSSNPLSEKEKEFLKKLKLDIQPYDINQRLQDTGGLIDSPSINLDVRKQYKRDIQNIDALLHQSIGSTLYNKIYLYENMNINNLTATLGADLVDSTDNTKINRGIFNEFKKNFKYSISSNYMIVDINERPALDNERLKWRIQLSPDTRAGYLENGKLILQRNIGLEIKDVQIIKQSEKEYIRIDAKVVPKSKIDTKIQEAQLNINQEWNKALGLPKYTKLITFNVHNRYASNIVESAYLILNEWKNNIQSDLIKKVTNYLVDGNGRFVFTDITLPNIAEQYTHQDEIYEQVHSKGLYVPESRSILLHGPSKGVELRNDSEGFIHEFGHAVDDYAGYLLDKNQSDLVTNSKKFIDIFKEEGSNLTSYGRTNEAEFFAEAFRLMHSTDHAERLKVQKNAPKTFQFINDQIKFIINS,Lethal factor,"Lethal factor (LF), which constitutes one of the three proteins composing the anthrax toxin, is able to trigger rapid cell death in macrophages. Acts as a protease that cleaves the N-terminal of most dual specificity mitogen-activated protein kinase kinases (MAPKKs or MAP2Ks) (except for MAP2K5): cleavage invariably occurs within the N-terminal proline-rich region preceding the kinase domain, thus disrupting a sequence involved in directing specific protein-protein interactions necessary for the assembly of signaling complexes. Also cleaves mouse Nlrp1b: host Nlrp1b cleavage promotes ubiquitination and degradation of the N-terminal part of Nlrp1b by the proteasome, thereby releasing the cleaved C-terminal part of Nlrp1b, which polymerizes and forms the Nlrp1b inflammasome followed by host cell pyroptosis. Able to cleave mouse Nlrp1b alleles 1 and 5, while it is not able to cleave Nlrp1b alleles 2, 3 and 4. In contrast, does not cleave NLRP1 human ortholog. LF is not toxic by itself and only acts as a lethal factor when associated with protective antigen (PA) to form the lethal toxin (LeTx): PA is required for LF translocation into the host cytosol.",,Does not affect translocation into host cytoplasm.
31,31,25108,P16522-P114S,MNDDSQDKIIHDIRIQLRKAATELSRWKLYGSSKWAAEALAGLAEAIDVDQTHSLADESPLRNKQGVPKQMFEIPQNGFGLSETEYDLYLLGSTLFDAKEFDRCVFFLKDVTNSYLKFLKLYSKFLSWDKKSQESMENILTTGKFTDEMYRANKDGDGSGNEDINQSGHQRANLKMVSNEHESQSNISSILKEINTFLESYEIKIDDDEADLGLALLYYLRGVILKQEKNISKAMSSFLKSLSCYSFNWSCWLELMDCLQKVDDALLLNNYLYQNFQFKFSENLGSQRTIEFNIMIKFFKLKVFEELNGQLEDYFEDLEFLLQVFPNFTFLKAYNATISYNNLDYVTAESRFDDIVKQDPYRLNDLETYSNILYVMQKNSKLAYLAQFVSQIDRFRPETCCIIANYYSARQEHEKSIMYFRRALTLDKKTTNAWTLMGHEFVELSNSHAAIECYRRAVDICPRDFKAWFGLGQAYALLDMHLYSLYYFQKACTLKPWDRRIWQVLGECYSKTGNKVEAIKCYKRSIKASQTVDQNTSIYYRLAQLYEELEDLQECKKFMMKCVDVEELLEGIVTDETVKARLWLAIFEIKAGNYQLAYDYAMGVSSGTSQEIEEARMLARECRRHM,In CDC23-41; G2/M cell cycle arrest at 37 degrees Celsius.,,MNDDSQDKIIHDIRIQLRKAATELSRWKLYGSSKWAAEALAGLAEAIDVDQTHSLADESPLRNKQGVPKQMFEIPQNGFGLSETEYDLYLLGSTLFDAKEFDRCVFFLKDVTNPYLKFLKLYSKFLSWDKKSQESMENILTTGKFTDEMYRANKDGDGSGNEDINQSGHQRANLKMVSNEHESQSNISSILKEINTFLESYEIKIDDDEADLGLALLYYLRGVILKQEKNISKAMSSFLKSLSCYSFNWSCWLELMDCLQKVDDALLLNNYLYQNFQFKFSENLGSQRTIEFNIMIKFFKLKVFEELNGQLEDYFEDLEFLLQVFPNFTFLKAYNATISYNNLDYVTAESRFDDIVKQDPYRLNDLETYSNILYVMQKNSKLAYLAQFVSQIDRFRPETCCIIANYYSARQEHEKSIMYFRRALTLDKKTTNAWTLMGHEFVELSNSHAAIECYRRAVDICPRDFKAWFGLGQAYALLDMHLYSLYYFQKACTLKPWDRRIWQVLGECYSKTGNKVEAIKCYKRSIKASQTVDQNTSIYYRLAQLYEELEDLQECKKFMMKCVDVEELLEGIVTDETVKARLWLAIFEIKAGNYQLAYDYAMGVSSGTSQEIEEARMLARECRRHM,Anaphase-promoting complex subunit CDC23,"Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. In early mitosis, the APC/C is activated by CDC20 and targets securin PDS1, the B-type cyclin CLB5, and other anaphase inhibitory proteins for proteolysis, thereby triggering the separation of sister chromatids at the metaphase-to-anaphase transition. In late mitosis and in G1, degradation of CLB5 allows activation of the APC/C by CDH1, which is needed to destroy CDC20 and the B-type cyclin CLB2 to allow exit from mitosis and creating the low CDK state necessary for cytokinesis and for reforming prereplicative complexes in G1 prior to another round of replication.",,In CDC23-41; G2/M cell cycle arrest at 37 degrees Celsius.
32,32,26247,P15917-Y181A,MNIKKEFIKVISMSCLVTAITLSGPVFIPLVQGAGGHGDVGMHVKEKEKNKDENKRKDEERNKTQEEHLKEIMKHIVKIEVKGEEAVKKEAAEKLLEKVPSDVLEMYKAIGGKIYIVDGDITKHISLEALSEDKKKIKDIYGKDALLHEHYVYAKEGYEPVLVIQSSEDYVENTEKALNVAYEIGKILSRDILSKINQPYQKFLDVLNTIKNASDSDGQDLLFTNQLKEHPTDFSVEFLEQNSNEVQEVFAKAFAYYIEPQHRDVLQLYAPEAFNYMDKFNEQEINLSLEELKDQRMLARYEKWEKIKQHYQHWSDSLSEEGRGLLKKLQIPIEPKKDDIIHSLSQEEKELLKRIQIDSSDFLSTEEKEFLKKLQIDIRDSLSEEEKELLNRIQVDSSNPLSEKEKEFLKKLKLDIQPYDINQRLQDTGGLIDSPSINLDVRKQYKRDIQNIDALLHQSIGSTLYNKIYLYENMNINNLTATLGADLVDSTDNTKINRGIFNEFKKNFKYSISSNYMIVDINERPALDNERLKWRIQLSPDTRAGYLENGKLILQRNIGLEIKDVQIIKQSEKEYIRIDAKVVPKSKIDTKIQEAQLNINQEWNKALGLPKYTKLITFNVHNRYASNIVESAYLILNEWKNNIQSDLIKKVTNYLVDGNGRFVFTDITLPNIAEQYTHQDEIYEQVHSKGLYVPESRSILLHGPSKGVELRNDSEGFIHEFGHAVDDYAGYLLDKNQSDLVTNSKKFIDIFKEEGSNLTSYGRTNEAEFFAEAFRLMHSTDHAERLKVQKNAPKTFQFINDQIKFIINS,Loss of ability to bind to PA.,,MNIKKEFIKVISMSCLVTAITLSGPVFIPLVQGAGGHGDVGMHVKEKEKNKDENKRKDEERNKTQEEHLKEIMKHIVKIEVKGEEAVKKEAAEKLLEKVPSDVLEMYKAIGGKIYIVDGDITKHISLEALSEDKKKIKDIYGKDALLHEHYVYAKEGYEPVLVIQSSEDYVENTEKALNVYYEIGKILSRDILSKINQPYQKFLDVLNTIKNASDSDGQDLLFTNQLKEHPTDFSVEFLEQNSNEVQEVFAKAFAYYIEPQHRDVLQLYAPEAFNYMDKFNEQEINLSLEELKDQRMLARYEKWEKIKQHYQHWSDSLSEEGRGLLKKLQIPIEPKKDDIIHSLSQEEKELLKRIQIDSSDFLSTEEKEFLKKLQIDIRDSLSEEEKELLNRIQVDSSNPLSEKEKEFLKKLKLDIQPYDINQRLQDTGGLIDSPSINLDVRKQYKRDIQNIDALLHQSIGSTLYNKIYLYENMNINNLTATLGADLVDSTDNTKINRGIFNEFKKNFKYSISSNYMIVDINERPALDNERLKWRIQLSPDTRAGYLENGKLILQRNIGLEIKDVQIIKQSEKEYIRIDAKVVPKSKIDTKIQEAQLNINQEWNKALGLPKYTKLITFNVHNRYASNIVESAYLILNEWKNNIQSDLIKKVTNYLVDGNGRFVFTDITLPNIAEQYTHQDEIYEQVHSKGLYVPESRSILLHGPSKGVELRNDSEGFIHEFGHAVDDYAGYLLDKNQSDLVTNSKKFIDIFKEEGSNLTSYGRTNEAEFFAEAFRLMHSTDHAERLKVQKNAPKTFQFINDQIKFIINS,Lethal factor,"Lethal factor (LF), which constitutes one of the three proteins composing the anthrax toxin, is able to trigger rapid cell death in macrophages. Acts as a protease that cleaves the N-terminal of most dual specificity mitogen-activated protein kinase kinases (MAPKKs or MAP2Ks) (except for MAP2K5): cleavage invariably occurs within the N-terminal proline-rich region preceding the kinase domain, thus disrupting a sequence involved in directing specific protein-protein interactions necessary for the assembly of signaling complexes. Also cleaves mouse Nlrp1b: host Nlrp1b cleavage promotes ubiquitination and degradation of the N-terminal part of Nlrp1b by the proteasome, thereby releasing the cleaved C-terminal part of Nlrp1b, which polymerizes and forms the Nlrp1b inflammasome followed by host cell pyroptosis. Able to cleave mouse Nlrp1b alleles 1 and 5, while it is not able to cleave Nlrp1b alleles 2, 3 and 4. In contrast, does not cleave NLRP1 human ortholog. LF is not toxic by itself and only acts as a lethal factor when associated with protective antigen (PA) to form the lethal toxin (LeTx): PA is required for LF translocation into the host cytosol.",The mutation in the lethal factor protein was found to be deficient in its ability to lyse . 1 cells and its binding ability to PA63 was drastically reduced. This suggests that the Y181 amino acid plays a crucial role in the process of binding of LF to PA63.,Loss of ability to bind to PA. The mutation in the lethal factor protein was found to be deficient in its ability to lyse . 1 cells and its binding ability to PA63 was drastically reduced. This suggests that the Y181 amino acid plays a crucial role in the process of binding of LF to PA63.
33,33,26852,Q9IK90-P93A,MEPDIKSISSESMEGVSDFSPSSWEHGGYLDKVEPEIDENGSMIPKYKIYTPGANERKYNNYMYLICYGFVEDVERTPETGKRKKIRTIAAYALGVGKSASHPQDLLEELCSLKVTVRRTAGSTEKIVFGSSGPLNHLVPWKKVLTSGSIFNAVKVCRNVDQIQLDKHQALRIFFLSITKLNDSGIYMIPRTMLEFRRNNAIAFNLLVYLKIDADLSKMGIQGSLDKDGFKVASFMLHLGNFVRRAGKYYSVDYCRRKIDRMKLQFSLGSIGGLSLHIKINGVISKRLFAQMGFQKNLCFSLMDINPWLNRLTWNNSCEISRVAAVLQPSIPREFMIYDDVFIDNTGRILKG,Complete loss of budding.,,MEPDIKSISSESMEGVSDFSPSSWEHGGYLDKVEPEIDENGSMIPKYKIYTPGANERKYNNYMYLICYGFVEDVERTPETGKRKKIRTIAAYPLGVGKSASHPQDLLEELCSLKVTVRRTAGSTEKIVFGSSGPLNHLVPWKKVLTSGSIFNAVKVCRNVDQIQLDKHQALRIFFLSITKLNDSGIYMIPRTMLEFRRNNAIAFNLLVYLKIDADLSKMGIQGSLDKDGFKVASFMLHLGNFVRRAGKYYSVDYCRRKIDRMKLQFSLGSIGGLSLHIKINGVISKRLFAQMGFQKNLCFSLMDINPWLNRLTWNNSCEISRVAAVLQPSIPREFMIYDDVFIDNTGRILKG,Matrix protein,Plays a crucial role in virion assembly and budding. Forms a shell at the inner face of the plasma membrane. Transits through the host nucleus before gaining the functional ability to localize and bud from the plasma membrane. Mediates together with fusion protein the incorporation of the glycoprotein to the viral particles. Participates also in the inhibition of the host interferon type I antiviral response by interacting with and thereby inhibiting host TRIM6.,,Complete loss of budding.
34,34,27236,P25522-R256A,MSDNDTIVAQATPPGRGGVGILRISGFKAREVAETVLGKLPKPRYADYLPFKDADGSVLDQGIALWFPGPNSFTGEDVLELQGHGGPVILDLLLKRILTIPGLRIARPGEFSERAFLNDKLDLAQAEAIADLIDASSEQAARSALNSLQGAFSARVNHLVEALTHLRIYVEAAIDFPDEEIDFLSDGKIEAQLNDVIADLDAVRAEARQGSLLREGMKVVIAGRPNAGKSSLLNALAGREAAIVTDIAGTTRDVLAEHIHIDGMPLHIIDTAGLREASDEVERIGIERAWQEIEQADRVLFMVDGTTTDAVDPAEIWPEFIARLPAKLPITVVRNKADITGETLGMSEVNGHALIRLSARTGEGVDVLRNHLKQSMGFDTNMEGGFLARRRHLQALEQAAEHLQQGKAQLLGAWAGELLAEELRLAQQNLSEITGEFTSDDLLGRIFSSFCIGK,2-fold decrease in GTPase activity and almost no change in affinity.,,MSDNDTIVAQATPPGRGGVGILRISGFKAREVAETVLGKLPKPRYADYLPFKDADGSVLDQGIALWFPGPNSFTGEDVLELQGHGGPVILDLLLKRILTIPGLRIARPGEFSERAFLNDKLDLAQAEAIADLIDASSEQAARSALNSLQGAFSARVNHLVEALTHLRIYVEAAIDFPDEEIDFLSDGKIEAQLNDVIADLDAVRAEARQGSLLREGMKVVIAGRPNAGKSSLLNALAGREAAIVTDIAGTTRDVLREHIHIDGMPLHIIDTAGLREASDEVERIGIERAWQEIEQADRVLFMVDGTTTDAVDPAEIWPEFIARLPAKLPITVVRNKADITGETLGMSEVNGHALIRLSARTGEGVDVLRNHLKQSMGFDTNMEGGFLARRRHLQALEQAAEHLQQGKAQLLGAWAGELLAEELRLAQQNLSEITGEFTSDDLLGRIFSSFCIGK,tRNA modification GTPase MnmE,"Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.",,2-fold decrease in GTPase activity and almost no change in affinity.
35,35,27332,P32266-S224A,MNASPVRLLILRRQLATHPAILYSSPYIKSPLVHLHSRMSNVHRSAHANALSFVITRRSISHFPKIISKIIRLPIYVGGGMAAAGSYIAYKMEEASSFTKDKLDRIKDLGESMKEKFNKMFSGDKSQDGGHGNDGTVPTATLIAATSLDDDESKRQGDPKDDDDEDDDDEDDENDSVDTTQDEMLNLTKQMIEIRTILNKVDSSSAHLTLPSIVVIGSQSSGKASVLESIVGREFLPKGSNMVTRRPIELTLVNTPNSNNVTADFPSMRLYNIKDFKEVKRMLMELNMAVPTSEAVSEEPIQLTIKSSRVPDLSLVDLPGYIQVEAADQPIELKTKIRDLCEKYLTAPNIILAISAADVDLANSSALKASKAADPKGLRTIGVITKLDLVDPEKARSILNNKKYPLSMGYVGVITKTPSSINRKHLGLFGEAPSSSLSGIFSKGQHGQSSGEENTNGLKQIVSHQFEKAYFKENKKYFTNCQVSTKKLREKLIKILEISMSNALEPTSTLIQQELDDTSYLFKVEFNDRHLTPKSYLLNNIDVLKLGIKEFQEKFHRNELKSILRAELDQKVLDVLATRYWKDDNLQDLSSSKLESDTDMLYWHKKLELASSGLTKMGIGRLSTMLTTNAILKELDNILESTQLKNHELIKDLVSNTAINVLNSKYYSTADQVENCIKPFKYEIDLEERDWSLARQHSINLIKEELRQCNSRYQAIKNAVGSKKLANVMGYLENESNLQKETLGMSKLLLERGSEAIFLDKRCKVLSFRLKMLKNKCHSTIEKDRCPEVFLSAVSDKLTSTAVLFLNVELLSDFFYNFPIELDRRLTLLGDEQVEMFAKEDPKISRHIELQKRKELLELALEKIDSILVFKKSYKGVSKNL,Loss of GTPase activity.,,MNASPVRLLILRRQLATHPAILYSSPYIKSPLVHLHSRMSNVHRSAHANALSFVITRRSISHFPKIISKIIRLPIYVGGGMAAAGSYIAYKMEEASSFTKDKLDRIKDLGESMKEKFNKMFSGDKSQDGGHGNDGTVPTATLIAATSLDDDESKRQGDPKDDDDEDDDDEDDENDSVDTTQDEMLNLTKQMIEIRTILNKVDSSSAHLTLPSIVVIGSQSSGKSSVLESIVGREFLPKGSNMVTRRPIELTLVNTPNSNNVTADFPSMRLYNIKDFKEVKRMLMELNMAVPTSEAVSEEPIQLTIKSSRVPDLSLVDLPGYIQVEAADQPIELKTKIRDLCEKYLTAPNIILAISAADVDLANSSALKASKAADPKGLRTIGVITKLDLVDPEKARSILNNKKYPLSMGYVGVITKTPSSINRKHLGLFGEAPSSSLSGIFSKGQHGQSSGEENTNGLKQIVSHQFEKAYFKENKKYFTNCQVSTKKLREKLIKILEISMSNALEPTSTLIQQELDDTSYLFKVEFNDRHLTPKSYLLNNIDVLKLGIKEFQEKFHRNELKSILRAELDQKVLDVLATRYWKDDNLQDLSSSKLESDTDMLYWHKKLELASSGLTKMGIGRLSTMLTTNAILKELDNILESTQLKNHELIKDLVSNTAINVLNSKYYSTADQVENCIKPFKYEIDLEERDWSLARQHSINLIKEELRQCNSRYQAIKNAVGSKKLANVMGYLENESNLQKETLGMSKLLLERGSEAIFLDKRCKVLSFRLKMLKNKCHSTIEKDRCPEVFLSAVSDKLTSTAVLFLNVELLSDFFYNFPIELDRRLTLLGDEQVEMFAKEDPKISRHIELQKRKELLELALEKIDSILVFKKSYKGVSKNL,"Dynamin-like GTPase MGM1, mitochondrial",Dynamin-related GTPase required for mitochondrial fusion. Coordinates interaction between the inner and outer mitochondrial membrane to promote the formation of the double membrane.,A version of mgm1 mutated in a conserved residue in the putative GTP-binding site was unable to complement any of the mutant defects. It also caused aberrant mitochondrial distribution and morphology when expressed at high levels in cells that also contained a wild-type copy of the gene. Mgm1p was localized to the mitochondrial outer membrane and fractionated as a component of a high molecular weight complex. Mutations at cause mitochondrial fragmentation and a loss of mitochondrial DNA.,Loss of GTPase activity. A version of mgm1 mutated in a conserved residue in the putative GTP-binding site was unable to complement any of the mutant defects. It also caused aberrant mitochondrial distribution and morphology when expressed at high levels in cells that also contained a wild-type copy of the gene. Mgm1p was localized to the mitochondrial outer membrane and fractionated as a component of a high molecular weight complex. Mutations at cause mitochondrial fragmentation and a loss of mitochondrial DNA.
36,36,30288,Q9UJ83-S456R,MPDSNFAERSEEQVSGAKVIAQALKTQDVEYIFGIVGIPVTEIAIAAQQLGIKYIGMRNEQAACYAASAIGYLTSRPGVCLVVSGPGLIHALGGMANANMNCWPLLVIGGSSERNQETMGAFQEFPQVEACRLYTKFSARPSSIEAIPFVIEKAVRSSIYGRPGACYVDIPADFVNLQVNVNSIKYMERCMSPPISMAETSAVCTAASVIRNAKQPLLIIGKGAAYAHAEESIKKLVEQYKLPFLPTPMGKGVVPDNHPYCVGAARSRALQFADVIVLFGARLNWILHFGLPPRYQPDVKFIQVDICAEELGNNVKPAVTLLGNIHAVTKQLLEELDKTPWQYPPESKWWKTLREKMKSNEAASKELASKKSLPMNYYTVFYHVQEQLPRDCFVVSEGANTMDIGRTVLQNYLPRHRLDAGTFGTMGVGLGFAIAAAVVAKDRSPGQWIICVEGDRAFGFSGMEVETICRYNLPIILLVVNNNGIYQGFDTDTWKEMLKFQDATAVVPPMCLLPNSHYEQVMTAFGGKGYFVQTPEELQKSLRQSLADTTKPSLINIMIEPQATRKAQDFHWLTRSNM,"Does not affect subcellular localization. Abolishes lyase activity. Does not affect subcellular localization, abolishes lyase activity, does not affect oligomerisation and does not bind TTP; when associated with S-455.",,MPDSNFAERSEEQVSGAKVIAQALKTQDVEYIFGIVGIPVTEIAIAAQQLGIKYIGMRNEQAACYAASAIGYLTSRPGVCLVVSGPGLIHALGGMANANMNCWPLLVIGGSSERNQETMGAFQEFPQVEACRLYTKFSARPSSIEAIPFVIEKAVRSSIYGRPGACYVDIPADFVNLQVNVNSIKYMERCMSPPISMAETSAVCTAASVIRNAKQPLLIIGKGAAYAHAEESIKKLVEQYKLPFLPTPMGKGVVPDNHPYCVGAARSRALQFADVIVLFGARLNWILHFGLPPRYQPDVKFIQVDICAEELGNNVKPAVTLLGNIHAVTKQLLEELDKTPWQYPPESKWWKTLREKMKSNEAASKELASKKSLPMNYYTVFYHVQEQLPRDCFVVSEGANTMDIGRTVLQNYLPRHRLDAGTFGTMGVGLGFAIAAAVVAKDRSPGQWIICVEGDSAFGFSGMEVETICRYNLPIILLVVNNNGIYQGFDTDTWKEMLKFQDATAVVPPMCLLPNSHYEQVMTAFGGKGYFVQTPEELQKSLRQSLADTTKPSLINIMIEPQATRKAQDFHWLTRSNM,2-hydroxyacyl-CoA lyase 1,Peroxisomal 2-OH acyl-CoA lyase involved in the cleavage (C1 removal) reaction in the fatty acid alpha-oxydation in a thiamine pyrophosphate (TPP)-dependent manner. Involved in the degradation of 3-methyl-branched fatty acids like phytanic acid and the shortening of 2-hydroxy long-chain fatty acids. Plays a significant role in the biosynthesis of heptadecanal in the liver.,"The mutation in the TPP-binding domain of HACL1 did not affect enzyme targeting or oligomerisation, but enzyme activity was abolished.","Does not affect subcellular localization. Abolishes lyase activity. Does not affect subcellular localization, abolishes lyase activity, does not affect oligomerisation and does not bind TTP; when associated with S-455. The mutation in the TPP-binding domain of HACL1 did not affect enzyme targeting or oligomerisation, but enzyme activity was abolished."
37,37,30527,Q9ESN9-S208G,MMEIQMDEGGGVVVYQDDYCSGSVMSERVSGLAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEERESEMKKEYNALHQRHTEMIQTYVEHIERSKMQQVGGSGQTESSLPGRSRKERPTGLNVFPLADGMVRAQMGGKLVPAGDHWHLSDLGQLQSSSSYQCPNDEMSESGQSSAAATPSTTGTKSNTPTSSVPSAAVTPLNESLQPLGDYVSVTKNNKQAREKRNSRNMEVQVTQEMRNVSIGMGSSDEWSDVQDIIDSTPELDVCPETRLERTGSSPTQGIVNKAFGINTDSLYHELSTAGSEVIGDVDEGADLLGEFSVRDDFFGMGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEELKRVKSEAVTARREPREEVEDVSSYLCTELDKIPMAQRRRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASREHPSVQEKKKSTIWQFFSRLFSSSSSPPPAKRSYPSVNIHYKSPTAAGFSQRRSHALCQISAGSRPLEFFPDDDCTSSARREQKREQYRQVREHVRNDDGRLQACGWSLPAKYKQLSPNGGQEDTRMKNVPVPVYCRPLVEKDPSTKLWCAAGVNLSGWKPHEEDSSNGPKPVPGRDPLTCDREGEGEPKSTHPSPEKKKAKETPEADATSSRVWILTSTLTTSKVVIIDANQPGTIVDQFTVCNAHVLCISSIPAASDSDYPPGEMFLDSDVNPEDSGADGVLAGITLVGCATRCNVPRSNCSSRGDTPVLDKGQGDVATTANGKVNPSQSTEEATEATEVPDPGPSESEATTVRPGPLTEHVFTDPAPTPSSSTQPASENGSESNGTIVQPQVEPSGELSTTTSSAAPTMWLGAQNGWLYVHSAVANWKKCLHSIKLKDSVLSLVHVKGRVLVALADGTLAI,Results in inhibition of JNK binding.,,MMEIQMDEGGGVVVYQDDYCSGSVMSERVSGLAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEERESEMKKEYNALHQRHTEMIQTYVEHIERSKMQQVGGSGQTESSLPGRSRKERPTSLNVFPLADGMVRAQMGGKLVPAGDHWHLSDLGQLQSSSSYQCPNDEMSESGQSSAAATPSTTGTKSNTPTSSVPSAAVTPLNESLQPLGDYVSVTKNNKQAREKRNSRNMEVQVTQEMRNVSIGMGSSDEWSDVQDIIDSTPELDVCPETRLERTGSSPTQGIVNKAFGINTDSLYHELSTAGSEVIGDVDEGADLLGEFSVRDDFFGMGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEELKRVKSEAVTARREPREEVEDVSSYLCTELDKIPMAQRRRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASREHPSVQEKKKSTIWQFFSRLFSSSSSPPPAKRSYPSVNIHYKSPTAAGFSQRRSHALCQISAGSRPLEFFPDDDCTSSARREQKREQYRQVREHVRNDDGRLQACGWSLPAKYKQLSPNGGQEDTRMKNVPVPVYCRPLVEKDPSTKLWCAAGVNLSGWKPHEEDSSNGPKPVPGRDPLTCDREGEGEPKSTHPSPEKKKAKETPEADATSSRVWILTSTLTTSKVVIIDANQPGTIVDQFTVCNAHVLCISSIPAASDSDYPPGEMFLDSDVNPEDSGADGVLAGITLVGCATRCNVPRSNCSSRGDTPVLDKGQGDVATTANGKVNPSQSTEEATEATEVPDPGPSESEATTVRPGPLTEHVFTDPAPTPSSSTQPASENGSESNGTIVQPQVEPSGELSTTTSSAAPTMWLGAQNGWLYVHSAVANWKKCLHSIKLKDSVLSLVHVKGRVLVALADGTLAI,C-Jun-amino-terminal kinase-interacting protein 3,"The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. May function as a regulator of vesicle transport, through interactions with the JNK-signaling components and motor proteins. Promotes neuronal axon elongation in a kinesin- and JNK-dependent manner. Activates cofilin at axon tips via local activation of JNK, thereby regulating filopodial dynamics and enhancing axon elongation. Its binding to kinesin heavy chains (KHC), promotes kinesin-1 motility along microtubules and is essential for axon elongation and regeneration. Regulates cortical neuronal migration by mediating NTRK2/TRKB anterograde axonal transport during brain development. Acts as an adapter that bridges the interaction between NTRK2/TRKB and KLC1 and drives NTRK2/TRKB axonal but not dendritic anterograde transport, which is essential for subsequent BDNF-triggered signaling and filopodia formation.",,Results in inhibition of JNK binding.
38,38,30622,P40240-F174A,MPVKGGSKCIKYLLFGFNFIFWLAGIAVLAIGLWLRFDSQTKSIFEQENNHSSFYTGVYILIGAGALMMLVGFLGCCGAVQESQCMLGLFFGFLLVIFAIEIAAAVWGYTHKDEVIKELQEFYKDTYQKLRSKDEPQRETLKAIHMALDCCGIAGPLEQFISDTCPKKQLLESAQVKPCPEAISEVFNNKFHIIGAVGIGIAVVMIFGMIFSMILCCAIRRSREMV,4-fold reduction of sperm-egg fusion.,,MPVKGGSKCIKYLLFGFNFIFWLAGIAVLAIGLWLRFDSQTKSIFEQENNHSSFYTGVYILIGAGALMMLVGFLGCCGAVQESQCMLGLFFGFLLVIFAIEIAAAVWGYTHKDEVIKELQEFYKDTYQKLRSKDEPQRETLKAIHMALDCCGIAGPLEQFISDTCPKKQLLESFQVKPCPEAISEVFNNKFHIIGAVGIGIAVVMIFGMIFSMILCCAIRRSREMV,CD9 antigen,"Integral membrane protein associated with integrins, which regulates different processes, such as sperm-egg fusion, platelet activation and aggregation, and cell adhesion. Present at the cell surface of oocytes and plays a key role in sperm-egg fusion, possibly by organizing multiprotein complexes and the morphology of the membrane required for the fusion. In myoblasts, associates with CD81 and PTGFRN and inhibits myotube fusion during muscle regeneration. In macrophages, associates with CD9 and beta-1 and beta-2 integrins, and prevents macrophage fusion into multinucleated giant cells specialized in ingesting complement-opsonized large particles. Also prevents the fusion between mononuclear cell progenitors into osteoclasts in charge of bone resorption. Acts as a receptor for PSG17. Involved in platelet activation and aggregation. Regulates paranodal junction formation. Involved in cell adhesion, cell motility and tumor metastasis. Also regulates integrin-dependent migration of macrophages, particularly relevant for inflammatory response in the lung.",The gamete fusion level was reduced fourfold,4-fold reduction of sperm-egg fusion. The gamete fusion level was reduced fourfold
39,39,31021,Q84W98-P96A,MATSNDQTNTKSSHSRTLLLLFIFLSLLLFSSLTIPMTRHQSTSMVAPFKRVLLESSVPASSTMDLRPKASTRRSRTSRRREFGNDAHEVPSGPNAISN,Compromised interaction with TDR.,,MATSNDQTNTKSSHSRTLLLLFIFLSLLLFSSLTIPMTRHQSTSMVAPFKRVLLESSVPASSTMDLRPKASTRRSRTSRRREFGNDAHEVPSGPNPISN,CLAVATA3/ESR,"Extracellular signal peptide that regulates cell fate. May act with TDR as a ligand-receptor pair in a signal transduction pathway that represses tracheary element differentiation but promotes the formation of procambial cells adjacent to phloem cells in the veins in an auxin-dependent manner. Regulates the transition of protophloem cells from proliferation to differentiation, thus impinging on postembryonic growth capacity of the root meristem; this signaling pathway requires CRN and CLV2.",The mutation in TDIF leads to [functional changes].,Compromised interaction with TDR. The mutation in TDIF leads to [functional changes].
40,40,31150,O14746-Q169A,MPRAPRCRAVRSLLRSHYREVLPLATFVRRLGPQGWRLVQRGDPAAFRALVAQCLVCVPWDARPPPAAPSFRQVSCLKELVARVLQRLCERGAKNVLAFGFALLDGARGGPPEAFTTSVRSYLPNTVTDALRGSGAWGLLLRRVGDDVLVHLLARCALFVLVAPSCAYAVCGPPLYQLGAATQARPPPHASGPRRRLGCERAWNHSVREAGVPLGLPAPGARRRGGSASRSLPLPKRPRRGAAPEPERTPVGQGSWAHPGRTRGPSDRGFCVVSPARPAEEATSLEGALSGTRHSHPSVGRQHHAGPPSTSRPPRPWDTPCPPVYAETKHFLYSSGDKEQLRPSFLLSSLRPSLTGARRLVETIFLGSRPWMPGTPRRLPRLPQRYWQMRPLFLELLGNHAQCPYGVLLKTHCPLRAAVTPAAGVCAREKPQGSVAAPEEEDTDPRRLVQLLRQHSSPWQVYGFVRACLRRLVPPGLWGSRHNERRFLRNTKKFISLGKHAKLSLQELTWKMSVRDCAWLRRSPGVGCVPAAEHRLREEILAKFLHWLMSVYVVELLRSFFYVTETTFQKNRLFFYRKSVWSKLQSIGIRQHLKRVQLRELSEAEVRQHREARPALLTSRLRFIPKPDGLRPIVNMDYVVGARTFRREKRAERLTSRVKALFSVLNYERARRPGLLGASVLGLDDIHRAWRTFVLRVRAQDPPPELYFVKVDVTGAYDTIPQDRLTEVIASIIKPQNTYCVRRYAVVQKAAHGHVRKAFKSHVSTLTDLQPYMRQFVAHLQETSPLRDAVVIEQSSSLNEASSGLFDVFLRFMCHHAVRIRGKSYVQCQGIPQGSILSTLLCSLCYGDMENKLFAGIRRDGLLLRLVDDFLLVTPHLTHAKTFLRTLVRGVPEYGCVVNLRKTVVNFPVEDEALGGTAFVQMPAHGLFPWCGLLLDTRTLEVQSDYSSYARTSIRASLTFNRGFKAGRNMRRKLFGVLRLKCHSLFLDLQVNSLQTVCTNIYKILLLQAYRFHACVLQLPFHQQ,"About 80% loss of enzymatic activity. Greatly reduced incorporation of second nucleotide. Altered strength of binding to ssDNA. Little effect on repeat addition processivity, nor on TR interaction nor on protein levels.",,MPRAPRCRAVRSLLRSHYREVLPLATFVRRLGPQGWRLVQRGDPAAFRALVAQCLVCVPWDARPPPAAPSFRQVSCLKELVARVLQRLCERGAKNVLAFGFALLDGARGGPPEAFTTSVRSYLPNTVTDALRGSGAWGLLLRRVGDDVLVHLLARCALFVLVAPSCAYQVCGPPLYQLGAATQARPPPHASGPRRRLGCERAWNHSVREAGVPLGLPAPGARRRGGSASRSLPLPKRPRRGAAPEPERTPVGQGSWAHPGRTRGPSDRGFCVVSPARPAEEATSLEGALSGTRHSHPSVGRQHHAGPPSTSRPPRPWDTPCPPVYAETKHFLYSSGDKEQLRPSFLLSSLRPSLTGARRLVETIFLGSRPWMPGTPRRLPRLPQRYWQMRPLFLELLGNHAQCPYGVLLKTHCPLRAAVTPAAGVCAREKPQGSVAAPEEEDTDPRRLVQLLRQHSSPWQVYGFVRACLRRLVPPGLWGSRHNERRFLRNTKKFISLGKHAKLSLQELTWKMSVRDCAWLRRSPGVGCVPAAEHRLREEILAKFLHWLMSVYVVELLRSFFYVTETTFQKNRLFFYRKSVWSKLQSIGIRQHLKRVQLRELSEAEVRQHREARPALLTSRLRFIPKPDGLRPIVNMDYVVGARTFRREKRAERLTSRVKALFSVLNYERARRPGLLGASVLGLDDIHRAWRTFVLRVRAQDPPPELYFVKVDVTGAYDTIPQDRLTEVIASIIKPQNTYCVRRYAVVQKAAHGHVRKAFKSHVSTLTDLQPYMRQFVAHLQETSPLRDAVVIEQSSSLNEASSGLFDVFLRFMCHHAVRIRGKSYVQCQGIPQGSILSTLLCSLCYGDMENKLFAGIRRDGLLLRLVDDFLLVTPHLTHAKTFLRTLVRGVPEYGCVVNLRKTVVNFPVEDEALGGTAFVQMPAHGLFPWCGLLLDTRTLEVQSDYSSYARTSIRASLTFNRGFKAGRNMRRKLFGVLRLKCHSLFLDLQVNSLQTVCTNIYKILLLQAYRFHACVLQLPFHQQ,Telomerase reverse transcriptase,"Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. Active in progenitor and cancer cells. Inactive, or very low activity, in normal somatic cells. Catalytic component of the teleromerase holoenzyme complex whose main activity is the elongation of telomeres by acting as a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme. Catalyzes the RNA-dependent extension of 3'-chromosomal termini with the 6-nucleotide telomeric repeat unit, 5'-TTAGGG-3'. The catalytic cycle involves primer binding, primer extension and release of product once the template boundary has been reached or nascent product translocation followed by further extension. More active on substrates containing 2 or 3 telomeric repeats. Telomerase activity is regulated by a number of factors including telomerase complex-associated proteins, chaperones and polypeptide modifiers. Modulates Wnt signaling. Plays important roles in aging and antiapoptosis.",This mutation may affect the interactions of TERT with anchor sites in lower eukaryotes.,"About 80% loss of enzymatic activity. Greatly reduced incorporation of second nucleotide. Altered strength of binding to ssDNA. Little effect on repeat addition processivity, nor on TR interaction nor on protein levels. This mutation may affect the interactions of TERT with anchor sites in lower eukaryotes."
41,41,31886,P51843-R425G,MAGENHQWQGSILYNMLMSAKQTRAAPEAPETRLVDQCWGCSCGDEPGVGREGLLGGRNVALLYRCCFCGKDHPRQGSILYSMLTSAKQTYAAPKAPEATLGPCWGCSCGSDPGVGRAGLPGGRPVALLYRCCFCGEDHPRQGSILYSLLTSSKQTHVAPAAPEARPGGAWWDRSYFAQRPGGKEALPGGRATALLYRCCFCGEDHPQQGSTLYCVPTSTNQAQAAPEERPRAPWWDTSSGALRPVALKSPQVVCEAASAGLLKTLRFVKYLPCFQVLPLDQQLVLVRNCWASLLMLELAQDRLQFETVEVSEPSMLQKILTTRRRETGGNEPLPVPTLQHHLAPPAEARKVPSASQVQAIKCFLSKCWSLNISTKEYAYLKGTVLFNPDVPGLQCVKYIQGLQWGTQQILSEHTRMTHQGPHDGFIELNSTLFLLRFINANVIAELFFRPIIGTVSMDDMMLEMLCTKI,In AHC.,,MAGENHQWQGSILYNMLMSAKQTRAAPEAPETRLVDQCWGCSCGDEPGVGREGLLGGRNVALLYRCCFCGKDHPRQGSILYSMLTSAKQTYAAPKAPEATLGPCWGCSCGSDPGVGRAGLPGGRPVALLYRCCFCGEDHPRQGSILYSLLTSSKQTHVAPAAPEARPGGAWWDRSYFAQRPGGKEALPGGRATALLYRCCFCGEDHPQQGSTLYCVPTSTNQAQAAPEERPRAPWWDTSSGALRPVALKSPQVVCEAASAGLLKTLRFVKYLPCFQVLPLDQQLVLVRNCWASLLMLELAQDRLQFETVEVSEPSMLQKILTTRRRETGGNEPLPVPTLQHHLAPPAEARKVPSASQVQAIKCFLSKCWSLNISTKEYAYLKGTVLFNPDVPGLQCVKYIQGLQWGTQQILSEHTRMTHQGPHDRFIELNSTLFLLRFINANVIAELFFRPIIGTVSMDDMMLEMLCTKI,Nuclear receptor subfamily 0 group B member 1,Orphan nuclear receptor. Component of a cascade required for the development of the hypothalamic-pituitary-adrenal-gonadal axis. Acts as a coregulatory protein that inhibits the transcriptional activity of other nuclear receptors through heterodimeric interactions. May also have a role in the development of the embryo and in the maintenance of embryonic stem cell pluripotency.,The mutation in the DAX1 protein is mentioned in the document. It is located in the conserved hydrophobic core of the putative ligand-binding domain (LBD) of DAX1. This mutation does not affect residues expected to interact directly with a ligand. The functional changes caused by this mutation are not specified in the document.,In AHC. The mutation in the DAX1 protein is mentioned in the document. It is located in the conserved hydrophobic core of the putative ligand-binding domain (LBD) of DAX1. This mutation does not affect residues expected to interact directly with a ligand. The functional changes caused by this mutation are not specified in the document.
42,42,33177,Q84W98-H88R,MATSNDQTNTKSSHSRTLLLLFIFLSLLLFSSLTIPMTRHQSTSMVAPFKRVLLESSVPASSTMDLRPKASTRRSRTSRRREFGNDAREVPSGPNPISN,Compromised interaction with TDR.,,MATSNDQTNTKSSHSRTLLLLFIFLSLLLFSSLTIPMTRHQSTSMVAPFKRVLLESSVPASSTMDLRPKASTRRSRTSRRREFGNDAHEVPSGPNPISN,CLAVATA3/ESR,"Extracellular signal peptide that regulates cell fate. May act with TDR as a ligand-receptor pair in a signal transduction pathway that represses tracheary element differentiation but promotes the formation of procambial cells adjacent to phloem cells in the veins in an auxin-dependent manner. Regulates the transition of protophloem cells from proliferation to differentiation, thus impinging on postembryonic growth capacity of the root meristem; this signaling pathway requires CRN and CLV2.",,Compromised interaction with TDR.
43,43,35074,P06022-E26D,MQHDLFEHDPAIRQLIGHIDNIPAPDLESRWPRSVVDLIDVLENELKRQNVSNPRELARKQAVALSCFLGGRQFYIPCGDTILTALRDDLLYCQFNGRNMEELRRQYRLSQPQIYQIIARQRKLHTRRHQPDLFSPETPK,Loss of DNA-binding activity and transactivation. No effect on dimerization.,,MQHDLFEHDPAIRQLIGHIDNIPAPELESRWPRSVVDLIDVLENELKRQNVSNPRELARKQAVALSCFLGGRQFYIPCGDTILTALRDDLLYCQFNGRNMEELRRQYRLSQPQIYQIIARQRKLHTRRHQPDLFSPETPK,Late transcription activator C,"Positive regulator of viral late genes transcription. Responsible for the transition from middle to late gene expression. Activates the Plys, PI, PP and Pmom late promoters thereby allowing the expression of viral endolysin and structural genes. Activates Pmom promoter by unwinding the DNA, thus realigning the promoter elements and recruiting the RNAP.","Mutations in residue E26 lead to altered Mg(2+)-induced conformation, compromised DNA binding, and reduced levels of transcription activation.","Loss of DNA-binding activity and transactivation. No effect on dimerization. Mutations in residue E26 lead to altered Mg(2+)-induced conformation, compromised DNA binding, and reduced levels of transcription activation."
44,44,35814,P21926-C9A,MPVKGGTKAIKYLLFGFNFIFWLAGIAVLAIGLWLRFDSQTKSIFEQETNNNNSSFYTGVYILIGAGALMMLVGFLGCCGAVQESQCMLGLFFGFLLVIFAIEIAAAIWGYSHKDEVIKEVQEFYKDTYNKLKTKDEPQRETLKAIHYALNCCGLAGGVEQFISDICPKKDVLETFTVKSCPDAIKEVFDNKFHIIGAVGIGIAVVMIFGMIFSMILCCAIRRNREMV,Loss of palmitoylation; when associated with A-78; A-79; A-87; A-218 and A-219.,,MPVKGGTKCIKYLLFGFNFIFWLAGIAVLAIGLWLRFDSQTKSIFEQETNNNNSSFYTGVYILIGAGALMMLVGFLGCCGAVQESQCMLGLFFGFLLVIFAIEIAAAIWGYSHKDEVIKEVQEFYKDTYNKLKTKDEPQRETLKAIHYALNCCGLAGGVEQFISDICPKKDVLETFTVKSCPDAIKEVFDNKFHIIGAVGIGIAVVMIFGMIFSMILCCAIRRNREMV,CD9 antigen,"Integral membrane protein associated with integrins, which regulates different processes, such as sperm-egg fusion, platelet activation and aggregation, and cell adhesion. Present at the cell surface of oocytes and plays a key role in sperm-egg fusion, possibly by organizing multiprotein complexes and the morphology of the membrane required for the fusion. In myoblasts, associates with CD81 and PTGFRN and inhibits myotube fusion during muscle regeneration. In macrophages, associates with CD81 and beta-1 and beta-2 integrins, and prevents macrophage fusion into multinucleated giant cells specialized in ingesting complement-opsonized large particles. Also prevents the fusion between mononuclear cell progenitors into osteoclasts in charge of bone resorption. Acts as a receptor for PSG17. Involved in platelet activation and aggregation. Regulates paranodal junction formation. Involved in cell adhesion, cell motility and tumor metastasis.",,Loss of palmitoylation; when associated with A-78; A-79; A-87; A-218 and A-219.
45,45,36047,P15917-M73A,MNIKKEFIKVISMSCLVTAITLSGPVFIPLVQGAGGHGDVGMHVKEKEKNKDENKRKDEERNKTQEEHLKEIAKHIVKIEVKGEEAVKKEAAEKLLEKVPSDVLEMYKAIGGKIYIVDGDITKHISLEALSEDKKKIKDIYGKDALLHEHYVYAKEGYEPVLVIQSSEDYVENTEKALNVYYEIGKILSRDILSKINQPYQKFLDVLNTIKNASDSDGQDLLFTNQLKEHPTDFSVEFLEQNSNEVQEVFAKAFAYYIEPQHRDVLQLYAPEAFNYMDKFNEQEINLSLEELKDQRMLARYEKWEKIKQHYQHWSDSLSEEGRGLLKKLQIPIEPKKDDIIHSLSQEEKELLKRIQIDSSDFLSTEEKEFLKKLQIDIRDSLSEEEKELLNRIQVDSSNPLSEKEKEFLKKLKLDIQPYDINQRLQDTGGLIDSPSINLDVRKQYKRDIQNIDALLHQSIGSTLYNKIYLYENMNINNLTATLGADLVDSTDNTKINRGIFNEFKKNFKYSISSNYMIVDINERPALDNERLKWRIQLSPDTRAGYLENGKLILQRNIGLEIKDVQIIKQSEKEYIRIDAKVVPKSKIDTKIQEAQLNINQEWNKALGLPKYTKLITFNVHNRYASNIVESAYLILNEWKNNIQSDLIKKVTNYLVDGNGRFVFTDITLPNIAEQYTHQDEIYEQVHSKGLYVPESRSILLHGPSKGVELRNDSEGFIHEFGHAVDDYAGYLLDKNQSDLVTNSKKFIDIFKEEGSNLTSYGRTNEAEFFAEAFRLMHSTDHAERLKVQKNAPKTFQFINDQIKFIINS,Impaired translocation into host cytoplasm.,,MNIKKEFIKVISMSCLVTAITLSGPVFIPLVQGAGGHGDVGMHVKEKEKNKDENKRKDEERNKTQEEHLKEIMKHIVKIEVKGEEAVKKEAAEKLLEKVPSDVLEMYKAIGGKIYIVDGDITKHISLEALSEDKKKIKDIYGKDALLHEHYVYAKEGYEPVLVIQSSEDYVENTEKALNVYYEIGKILSRDILSKINQPYQKFLDVLNTIKNASDSDGQDLLFTNQLKEHPTDFSVEFLEQNSNEVQEVFAKAFAYYIEPQHRDVLQLYAPEAFNYMDKFNEQEINLSLEELKDQRMLARYEKWEKIKQHYQHWSDSLSEEGRGLLKKLQIPIEPKKDDIIHSLSQEEKELLKRIQIDSSDFLSTEEKEFLKKLQIDIRDSLSEEEKELLNRIQVDSSNPLSEKEKEFLKKLKLDIQPYDINQRLQDTGGLIDSPSINLDVRKQYKRDIQNIDALLHQSIGSTLYNKIYLYENMNINNLTATLGADLVDSTDNTKINRGIFNEFKKNFKYSISSNYMIVDINERPALDNERLKWRIQLSPDTRAGYLENGKLILQRNIGLEIKDVQIIKQSEKEYIRIDAKVVPKSKIDTKIQEAQLNINQEWNKALGLPKYTKLITFNVHNRYASNIVESAYLILNEWKNNIQSDLIKKVTNYLVDGNGRFVFTDITLPNIAEQYTHQDEIYEQVHSKGLYVPESRSILLHGPSKGVELRNDSEGFIHEFGHAVDDYAGYLLDKNQSDLVTNSKKFIDIFKEEGSNLTSYGRTNEAEFFAEAFRLMHSTDHAERLKVQKNAPKTFQFINDQIKFIINS,Lethal factor,"Lethal factor (LF), which constitutes one of the three proteins composing the anthrax toxin, is able to trigger rapid cell death in macrophages. Acts as a protease that cleaves the N-terminal of most dual specificity mitogen-activated protein kinase kinases (MAPKKs or MAP2Ks) (except for MAP2K5): cleavage invariably occurs within the N-terminal proline-rich region preceding the kinase domain, thus disrupting a sequence involved in directing specific protein-protein interactions necessary for the assembly of signaling complexes. Also cleaves mouse Nlrp1b: host Nlrp1b cleavage promotes ubiquitination and degradation of the N-terminal part of Nlrp1b by the proteasome, thereby releasing the cleaved C-terminal part of Nlrp1b, which polymerizes and forms the Nlrp1b inflammasome followed by host cell pyroptosis. Able to cleave mouse Nlrp1b alleles 1 and 5, while it is not able to cleave Nlrp1b alleles 2, 3 and 4. In contrast, does not cleave NLRP1 human ortholog. LF is not toxic by itself and only acts as a lethal factor when associated with protective antigen (PA) to form the lethal toxin (LeTx): PA is required for LF translocation into the host cytosol.",,Impaired translocation into host cytoplasm.
46,46,36109,Q9JJS6-E405A,MEIIFGQNKKEQLEPVQAKVTGSIPAWLQGTLLRNGPGMHTVGESKYNHWFDGLALLHSFSIRDGEVFYRSKYLQSDTYIANIEANRIVVSEFGTMAYPDPCKNIFSKAFSYLSHTIPDFTDNCLINIMKCGEDFYATTETNYIRKIDPQTLETLEKVDYRKYVAVNLATSHPHYDEAGNVLNMGTSVVDKGRTKYVIFKIPATVPDSKKKGKSPVKHAEVFCSISSRSLLSPSYYHSFGVTENYVVFLEQPFKLDILKMATAYMRGVSWASCMSFDREDKTYIHIIDQRTRKPVPTKFYTDPMVVFHHVNAYEEDGCVLFDVIAYEDSSLYQLFYLANLNKDFEEKSRLTSVPTLRRFAVPLHVDKDAEVGSNLVKVSSTTATALKEKDGHVYCQPEVLYEGLALPRINYAYNGKPYRYIFAAEVQWSPVPTKILKYDILTKSSLKWSEESCWPAEPLFVPTPGAKDEDDGVILSAIVSTDPQKLPFLLILDAKSFTELARASVDADMHLDLHGLFIPDADWNAVKQTPAETQEVENSDHPTDPTAPELSHSENDFTAGHGGSSL,"Loss of beta-carotene 15,15'-monooxygenase activity.",,MEIIFGQNKKEQLEPVQAKVTGSIPAWLQGTLLRNGPGMHTVGESKYNHWFDGLALLHSFSIRDGEVFYRSKYLQSDTYIANIEANRIVVSEFGTMAYPDPCKNIFSKAFSYLSHTIPDFTDNCLINIMKCGEDFYATTETNYIRKIDPQTLETLEKVDYRKYVAVNLATSHPHYDEAGNVLNMGTSVVDKGRTKYVIFKIPATVPDSKKKGKSPVKHAEVFCSISSRSLLSPSYYHSFGVTENYVVFLEQPFKLDILKMATAYMRGVSWASCMSFDREDKTYIHIIDQRTRKPVPTKFYTDPMVVFHHVNAYEEDGCVLFDVIAYEDSSLYQLFYLANLNKDFEEKSRLTSVPTLRRFAVPLHVDKDAEVGSNLVKVSSTTATALKEKDGHVYCQPEVLYEGLELPRINYAYNGKPYRYIFAAEVQWSPVPTKILKYDILTKSSLKWSEESCWPAEPLFVPTPGAKDEDDGVILSAIVSTDPQKLPFLLILDAKSFTELARASVDADMHLDLHGLFIPDADWNAVKQTPAETQEVENSDHPTDPTAPELSHSENDFTAGHGGSSL,"Beta,beta-carotene 15,15'-dioxygenase",Symmetrically cleaves beta-carotene into two molecules of retinal using a dioxygenase mechanism.,Mutation of E405 caused total loss of activity.,"Loss of beta-carotene 15,15'-monooxygenase activity. Mutation of E405 caused total loss of activity."
47,47,36202,P25522-R252K,MSDNDTIVAQATPPGRGGVGILRISGFKAREVAETVLGKLPKPRYADYLPFKDADGSVLDQGIALWFPGPNSFTGEDVLELQGHGGPVILDLLLKRILTIPGLRIARPGEFSERAFLNDKLDLAQAEAIADLIDASSEQAARSALNSLQGAFSARVNHLVEALTHLRIYVEAAIDFPDEEIDFLSDGKIEAQLNDVIADLDAVRAEARQGSLLREGMKVVIAGRPNAGKSSLLNALAGREAAIVTDIAGTTKDVLREHIHIDGMPLHIIDTAGLREASDEVERIGIERAWQEIEQADRVLFMVDGTTTDAVDPAEIWPEFIARLPAKLPITVVRNKADITGETLGMSEVNGHALIRLSARTGEGVDVLRNHLKQSMGFDTNMEGGFLARRRHLQALEQAAEHLQQGKAQLLGAWAGELLAEELRLAQQNLSEITGEFTSDDLLGRIFSSFCIGK,2-fold decrease in GTPase activity and no change in affinity.,,MSDNDTIVAQATPPGRGGVGILRISGFKAREVAETVLGKLPKPRYADYLPFKDADGSVLDQGIALWFPGPNSFTGEDVLELQGHGGPVILDLLLKRILTIPGLRIARPGEFSERAFLNDKLDLAQAEAIADLIDASSEQAARSALNSLQGAFSARVNHLVEALTHLRIYVEAAIDFPDEEIDFLSDGKIEAQLNDVIADLDAVRAEARQGSLLREGMKVVIAGRPNAGKSSLLNALAGREAAIVTDIAGTTRDVLREHIHIDGMPLHIIDTAGLREASDEVERIGIERAWQEIEQADRVLFMVDGTTTDAVDPAEIWPEFIARLPAKLPITVVRNKADITGETLGMSEVNGHALIRLSARTGEGVDVLRNHLKQSMGFDTNMEGGFLARRRHLQALEQAAEHLQQGKAQLLGAWAGELLAEELRLAQQNLSEITGEFTSDDLLGRIFSSFCIGK,tRNA modification GTPase MnmE,"Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.",,2-fold decrease in GTPase activity and no change in affinity.
48,48,39275,Q46389-N199A,MLIIGERINGMFGDIKRAIQERDPAPVQEWARRQEEGGARALDLNVGPAVQDKVSAMEWLVEVTQEVSNLTLCLDSTNIKAIEAGLKKCKNRAMINSTNAEREKVEKLFPLAVEHGAALIGLTMNKTGIPKDSDTRLAFAMELVAAADEFGLPMEDLYIDPLILPANVAQDHAPEVLKTLQQIKMLADPAPKTVLGLSAVSQNCQNRPLINRTFLAMAMACGLDAAIADACDEALIETAATAEILLNQTVYCDSFVKMFKTR,20-fold decreased affinity for methyltetrahydrofolate and nearly abolished catalytic activity.,,MLIIGERINGMFGDIKRAIQERDPAPVQEWARRQEEGGARALDLNVGPAVQDKVSAMEWLVEVTQEVSNLTLCLDSTNIKAIEAGLKKCKNRAMINSTNAEREKVEKLFPLAVEHGAALIGLTMNKTGIPKDSDTRLAFAMELVAAADEFGLPMEDLYIDPLILPANVAQDHAPEVLKTLQQIKMLADPAPKTVLGLSNVSQNCQNRPLINRTFLAMAMACGLDAAIADACDEALIETAATAEILLNQTVYCDSFVKMFKTR,5-methyltetrahydrofolate:corrinoid/iron-sulfur protein co-methyltransferase,Methyltransferase that mediates the transfer of a N5-methyl group of (6S)-methyltetrahydrofolate to the 5-methoxybenzimidazolylcobamide cofactor of a corrinoid/Fe-S protein (AcsC/AcsD) in the anaerobic acetyl-CoA pathway (Wood-Ljungdahl pathway) of carbon monoxide and carbon dioxide fixation.,"variant exhibits only approximately 20-fold weakened affinity for CH(3)-H(4)folate but a much more marked 20, 000-40, 000-fold effect on catalysis, suggesting that N-199 plays an important role in stabilizing a transition state or high energy intermediate for methyl transfer.","20-fold decreased affinity for methyltetrahydrofolate and nearly abolished catalytic activity. variant exhibits only approximately 20-fold weakened affinity for CH(3)-H(4)folate but a much more marked 20, 000-40, 000-fold effect on catalysis, suggesting that N-199 plays an important role in stabilizing a transition state or high energy intermediate for methyl transfer."
49,49,39368,P9WGT3-T191D,MTATATEGAKPPFVSRSVLVTGGNRGIGLAIAQRLAADGHKVAVTHRGSGAPKGLFGVECDVTDSDAVDRAFTAVEEHQGPVEVLVSNAGLSADAFLMRMTEEKFEKVINANLTGAFRVAQRASRSMQRNKFGRMIFIGSVSGSWGIGNQANYAASKAGVIGMARSIARELSKANVTANVVAPGYIDTDMDRALDERIQQGALQFIPAKRVGTPAEVAGVVSFLASEDASYISGAVIPVDGGMGMGH,Phosphomimetic mutant that retains less than 10% of wild-type reductase activity. Impaired NADPH binding. Overproduction of the mutant leads to a significant inhibition of de novo biosynthesis of mycolic acids.,,MTATATEGAKPPFVSRSVLVTGGNRGIGLAIAQRLAADGHKVAVTHRGSGAPKGLFGVECDVTDSDAVDRAFTAVEEHQGPVEVLVSNAGLSADAFLMRMTEEKFEKVINANLTGAFRVAQRASRSMQRNKFGRMIFIGSVSGSWGIGNQANYAASKAGVIGMARSIARELSKANVTANVVAPGYIDTDMTRALDERIQQGALQFIPAKRVGTPAEVAGVVSFLASEDASYISGAVIPVDGGMGMGH,3-oxoacyl-[acyl-carrier-protein] reductase MabA,"Part of the mycobacterial fatty acid elongation system FAS-II, which is involved in mycolic acid biosynthesis. Catalyzes the NADPH-dependent reduction of beta-ketoacyl derivatives, the second step of the FAS-II elongation cycle. May preferentially metabolize long-chain substrates (C8-C20). Can use CoA derivatives as substrates in vitro.","The MabA_T191D mutant, designed to mimic constitutive phosphorylation, exhibited markedly decreased ketoacyl reductase activity compared with the wild-type protein, as well as impaired binding of the NADPH cofactor. Constitutive overexpression of the mabA_T191D allele in Mycobacterium bovis BCG strongly impaired mycobacterial growth. Conditional expression of the phosphomimetic MabA_T191D led to a significant inhibition of de novo biosynthesis of mycolic acids.","Phosphomimetic mutant that retains less than 10% of wild-type reductase activity. Impaired NADPH binding. Overproduction of the mutant leads to a significant inhibition of de novo biosynthesis of mycolic acids. The MabA_T191D mutant, designed to mimic constitutive phosphorylation, exhibited markedly decreased ketoacyl reductase activity compared with the wild-type protein, as well as impaired binding of the NADPH cofactor. Constitutive overexpression of the mabA_T191D allele in Mycobacterium bovis BCG strongly impaired mycobacterial growth. Conditional expression of the phosphomimetic MabA_T191D led to a significant inhibition of de novo biosynthesis of mycolic acids."
50,50,39696,Q31125-H216A,MTMGLRAPHWVAVGLLTWAALGLLVAGHEGHGDLHKDVEEDFHGHSHGHSHEDFHHGHSHGHSHEDFHHGHGHTHESIWHGHAHSHDHGHSREELHHGHSHGHSHDSLHHGGHGHAHREHSHGTSREAGAPGIKHHLDTVTLWAYALGATVLISAAPFFVLFLIPVESNSPRHRSLLQILLSFASGGLLGDAFLHLIPHALEPHSHHAPEQPGHGASHSGQGPILSVGLWVLSGIVAFLVVEKFVRHVKGGHGHSHGHGDRHAHGDSHTHGDRHECSSKEKPSTEEEKEVGGLRKRRGGNTGPRDGPVKPQSPEEEKAGSDLRVSGYLNLAADLAHNFTDGLAIGASFRGGRGLGILTTMTVLLHEVPHEVGDFAILVQSGCSKKQAMRLQLVTAIGALAGTACALLTEGGAVDSDVAGGAGPGWVLPFTAGGFIYVATVSVLPELLREASPLQSLLEVLGLLGGVAMMVLIAHLE,Decreased METTL9-mediated methylation; when associated with A-204.,,MTMGLRAPHWVAVGLLTWAALGLLVAGHEGHGDLHKDVEEDFHGHSHGHSHEDFHHGHSHGHSHEDFHHGHGHTHESIWHGHAHSHDHGHSREELHHGHSHGHSHDSLHHGGHGHAHREHSHGTSREAGAPGIKHHLDTVTLWAYALGATVLISAAPFFVLFLIPVESNSPRHRSLLQILLSFASGGLLGDAFLHLIPHALEPHSHHAPEQPGHGHSHSGQGPILSVGLWVLSGIVAFLVVEKFVRHVKGGHGHSHGHGDRHAHGDSHTHGDRHECSSKEKPSTEEEKEVGGLRKRRGGNTGPRDGPVKPQSPEEEKAGSDLRVSGYLNLAADLAHNFTDGLAIGASFRGGRGLGILTTMTVLLHEVPHEVGDFAILVQSGCSKKQAMRLQLVTAIGALAGTACALLTEGGAVDSDVAGGAGPGWVLPFTAGGFIYVATVSVLPELLREASPLQSLLEVLGLLGGVAMMVLIAHLE,Zinc transporter SLC39A7,"Transports Zn(2+) from the endoplasmic reticulum (ER)/Golgi apparatus to the cytosol, playing an essential role in the regulation of cytosolic zinc levels. Acts as gatekeeper of zinc release from intracellular stores, requiring post-translational activation by phosphorylation, resulting in activation of multiple downstream pathways leading to cell growth and proliferation. Has an essential role in B cell development and is required for proper B cell receptor signaling. Plays an important role in maintaining intestinal epithelial homeostasis and skin dermis development by regulating ER function. Controls cell signaling pathways involved in glucose metabolism in skeletal muscle. Has a protective role against ER stress in differents biological contexts. Mediates Zn(2+)-induced ferroptosis.",,Decreased METTL9-mediated methylation; when associated with A-204.
51,51,39755,Q9SFD5-K257R,MGRSKLASRPAEEDLNPGKSKRKKISLGPENAAASISTGIEAGNERKPGLYCCNYCDKDLSGLVRFKCAVCMDFDLCVECFSVGVELNRHKNSHPYRVMDNLSFSLVTSDWNADEEILLLEAIATYGFGNWKEVADHVGSKTTTECIKHFNSAYMQSPCFPLPDLSHTIGKSKDELLAMSKDSAVKTEIPAFVRLSPKEELPVSAEIKHEASGKVNEIDPPLSALAGVKKKGNVPQAKDIIKLEAAKQQSDRSVGERKLRLPGEKVPLVTELYGYNLKREEFEIEHDNDAEQLLADMEFKDSDTDAEREQKLQVLRIYSKRLDERKRRKEFVLERNLLYPDQYEMSLSAEERKIYKSCKVFARFQSKEEHKELIKKVIEEHQILRRIEDLQEARTAGCRTTSDANRFIEEKRKKEAEESMLLRLNHGAPGSIAGKTLKSPRGLPRNLHPFGSDSLPKVTPPRIYSGLDTWDVDGLLGADLLSETEKKMCNETRILPVHYLKMLDILTREIKKGQIKKKSDAYSFFKVEPSKVDRVYDMLVHKGIGDST,No phenotypic effect.,,MGRSKLASRPAEEDLNPGKSKRKKISLGPENAAASISTGIEAGNERKPGLYCCNYCDKDLSGLVRFKCAVCMDFDLCVECFSVGVELNRHKNSHPYRVMDNLSFSLVTSDWNADEEILLLEAIATYGFGNWKEVADHVGSKTTTECIKHFNSAYMQSPCFPLPDLSHTIGKSKDELLAMSKDSAVKTEIPAFVRLSPKEELPVSAEIKHEASGKVNEIDPPLSALAGVKKKGNVPQAKDIIKLEAAKQQSDRSVGEKKLRLPGEKVPLVTELYGYNLKREEFEIEHDNDAEQLLADMEFKDSDTDAEREQKLQVLRIYSKRLDERKRRKEFVLERNLLYPDQYEMSLSAEERKIYKSCKVFARFQSKEEHKELIKKVIEEHQILRRIEDLQEARTAGCRTTSDANRFIEEKRKKEAEESMLLRLNHGAPGSIAGKTLKSPRGLPRNLHPFGSDSLPKVTPPRIYSGLDTWDVDGLLGADLLSETEKKMCNETRILPVHYLKMLDILTREIKKGQIKKKSDAYSFFKVEPSKVDRVYDMLVHKGIGDST,Transcriptional adapter ADA2a,"Required for the function of some acidic activation domains, which activate transcription from a distant site. The exact mechanism of action is not yet known. ADA2 stimulates the acetyltransferase activity of GCN5 on free histones or nucleosomes, probably by opening up the promoter region.",,No phenotypic effect.
52,52,40461,P67812-S56A,MLSLDFLDDVRRMNKRQLYYQVLNFGMIVSSALMIWKGLMVITGSESPIVVVLSGAMEPAFHRGDLLFLTNRVEDPIRVGEIVVFRIEGREIPIVHRVLKIHEKQNGHIKFLTKGDNNAVDDRGLYKQGQHWLEKKDVVGRARGFVPYIGIVTILMNDYPKFKYAVLFLLGLFVLVHRE,Loss of catalytic activity.,,MLSLDFLDDVRRMNKRQLYYQVLNFGMIVSSALMIWKGLMVITGSESPIVVVLSGSMEPAFHRGDLLFLTNRVEDPIRVGEIVVFRIEGREIPIVHRVLKIHEKQNGHIKFLTKGDNNAVDDRGLYKQGQHWLEKKDVVGRARGFVPYIGIVTILMNDYPKFKYAVLFLLGLFVLVHRE,Signal peptidase complex catalytic subunit SEC11A,Catalytic component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum. Specifically cleaves N-terminal signal peptides that contain a hydrophobic alpha-helix (h-region) shorter than 18-20 amino acids.,,Loss of catalytic activity.
53,53,42617,O14746-P65A,MPRAPRCRAVRSLLRSHYREVLPLATFVRRLGPQGWRLVQRGDPAAFRALVAQCLVCVPWDARPAPAAPSFRQVSCLKELVARVLQRLCERGAKNVLAFGFALLDGARGGPPEAFTTSVRSYLPNTVTDALRGSGAWGLLLRRVGDDVLVHLLARCALFVLVAPSCAYQVCGPPLYQLGAATQARPPPHASGPRRRLGCERAWNHSVREAGVPLGLPAPGARRRGGSASRSLPLPKRPRRGAAPEPERTPVGQGSWAHPGRTRGPSDRGFCVVSPARPAEEATSLEGALSGTRHSHPSVGRQHHAGPPSTSRPPRPWDTPCPPVYAETKHFLYSSGDKEQLRPSFLLSSLRPSLTGARRLVETIFLGSRPWMPGTPRRLPRLPQRYWQMRPLFLELLGNHAQCPYGVLLKTHCPLRAAVTPAAGVCAREKPQGSVAAPEEEDTDPRRLVQLLRQHSSPWQVYGFVRACLRRLVPPGLWGSRHNERRFLRNTKKFISLGKHAKLSLQELTWKMSVRDCAWLRRSPGVGCVPAAEHRLREEILAKFLHWLMSVYVVELLRSFFYVTETTFQKNRLFFYRKSVWSKLQSIGIRQHLKRVQLRELSEAEVRQHREARPALLTSRLRFIPKPDGLRPIVNMDYVVGARTFRREKRAERLTSRVKALFSVLNYERARRPGLLGASVLGLDDIHRAWRTFVLRVRAQDPPPELYFVKVDVTGAYDTIPQDRLTEVIASIIKPQNTYCVRRYAVVQKAAHGHVRKAFKSHVSTLTDLQPYMRQFVAHLQETSPLRDAVVIEQSSSLNEASSGLFDVFLRFMCHHAVRIRGKSYVQCQGIPQGSILSTLLCSLCYGDMENKLFAGIRRDGLLLRLVDDFLLVTPHLTHAKTFLRTLVRGVPEYGCVVNLRKTVVNFPVEDEALGGTAFVQMPAHGLFPWCGLLLDTRTLEVQSDYSSYARTSIRASLTFNRGFKAGRNMRRKLFGVLRLKCHSLFLDLQVNSLQTVCTNIYKILLLQAYRFHACVLQLPFHQQ,Associated with acute myeloid leukemia.,,MPRAPRCRAVRSLLRSHYREVLPLATFVRRLGPQGWRLVQRGDPAAFRALVAQCLVCVPWDARPPPAAPSFRQVSCLKELVARVLQRLCERGAKNVLAFGFALLDGARGGPPEAFTTSVRSYLPNTVTDALRGSGAWGLLLRRVGDDVLVHLLARCALFVLVAPSCAYQVCGPPLYQLGAATQARPPPHASGPRRRLGCERAWNHSVREAGVPLGLPAPGARRRGGSASRSLPLPKRPRRGAAPEPERTPVGQGSWAHPGRTRGPSDRGFCVVSPARPAEEATSLEGALSGTRHSHPSVGRQHHAGPPSTSRPPRPWDTPCPPVYAETKHFLYSSGDKEQLRPSFLLSSLRPSLTGARRLVETIFLGSRPWMPGTPRRLPRLPQRYWQMRPLFLELLGNHAQCPYGVLLKTHCPLRAAVTPAAGVCAREKPQGSVAAPEEEDTDPRRLVQLLRQHSSPWQVYGFVRACLRRLVPPGLWGSRHNERRFLRNTKKFISLGKHAKLSLQELTWKMSVRDCAWLRRSPGVGCVPAAEHRLREEILAKFLHWLMSVYVVELLRSFFYVTETTFQKNRLFFYRKSVWSKLQSIGIRQHLKRVQLRELSEAEVRQHREARPALLTSRLRFIPKPDGLRPIVNMDYVVGARTFRREKRAERLTSRVKALFSVLNYERARRPGLLGASVLGLDDIHRAWRTFVLRVRAQDPPPELYFVKVDVTGAYDTIPQDRLTEVIASIIKPQNTYCVRRYAVVQKAAHGHVRKAFKSHVSTLTDLQPYMRQFVAHLQETSPLRDAVVIEQSSSLNEASSGLFDVFLRFMCHHAVRIRGKSYVQCQGIPQGSILSTLLCSLCYGDMENKLFAGIRRDGLLLRLVDDFLLVTPHLTHAKTFLRTLVRGVPEYGCVVNLRKTVVNFPVEDEALGGTAFVQMPAHGLFPWCGLLLDTRTLEVQSDYSSYARTSIRASLTFNRGFKAGRNMRRKLFGVLRLKCHSLFLDLQVNSLQTVCTNIYKILLLQAYRFHACVLQLPFHQQ,Telomerase reverse transcriptase,"Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. Active in progenitor and cancer cells. Inactive, or very low activity, in normal somatic cells. Catalytic component of the teleromerase holoenzyme complex whose main activity is the elongation of telomeres by acting as a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme. Catalyzes the RNA-dependent extension of 3'-chromosomal termini with the 6-nucleotide telomeric repeat unit, 5'-TTAGGG-3'. The catalytic cycle involves primer binding, primer extension and release of product once the template boundary has been reached or nascent product translocation followed by further extension. More active on substrates containing 2 or 3 telomeric repeats. Telomerase activity is regulated by a number of factors including telomerase complex-associated proteins, chaperones and polypeptide modifiers. Modulates Wnt signaling. Plays important roles in aging and antiapoptosis.",,Associated with acute myeloid leukemia.
54,54,43302,Q9NZK5-H335R,MLVDGPSERPALCFLLLAVAMSFFGSALSIDETRAHLLLKEKMMRLGGRLVLNTKEELANERLMTLKIAEMKEAMRTLIFPPSMHFFQAKHLIERSQVFNILRMMPKGAALHLHDIGIVTMDWLVRNVTYRPHCHICFTPRGIMQFRFAHPTPRPSEKCSKWILLEDYRKRVQNVTEFDDSLLRNFTLVTQHPEVIYTNQNVVWSKFETIFFTISGLIHYAPVFRDYVFRSMQEFYEDNVLYMEIRARLLPVYELSGEHHDEEWSVKTYQEVAQKFVETHPEFIGIKIIYSDHRSKDVAVIAESIRMAMGLRIKFPTVVAGFDLVGHEDTGHSLRDYKEALMIPAKDGVKLPYFFHAGETDWQGTSIDRNILDALMLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLVSDLRNHPVATLMATGHPMVISSDDPAMFGAKGLSYDFYEVFMGIGGMKADLRTLKQLAMNSIKYSTLLESEKNTFMEIWKKRWDKFIADVATK,,,MLVDGPSERPALCFLLLAVAMSFFGSALSIDETRAHLLLKEKMMRLGGRLVLNTKEELANERLMTLKIAEMKEAMRTLIFPPSMHFFQAKHLIERSQVFNILRMMPKGAALHLHDIGIVTMDWLVRNVTYRPHCHICFTPRGIMQFRFAHPTPRPSEKCSKWILLEDYRKRVQNVTEFDDSLLRNFTLVTQHPEVIYTNQNVVWSKFETIFFTISGLIHYAPVFRDYVFRSMQEFYEDNVLYMEIRARLLPVYELSGEHHDEEWSVKTYQEVAQKFVETHPEFIGIKIIYSDHRSKDVAVIAESIRMAMGLRIKFPTVVAGFDLVGHEDTGHSLHDYKEALMIPAKDGVKLPYFFHAGETDWQGTSIDRNILDALMLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLVSDLRNHPVATLMATGHPMVISSDDPAMFGAKGLSYDFYEVFMGIGGMKADLRTLKQLAMNSIKYSTLLESEKNTFMEIWKKRWDKFIADVATK,Adenosine deaminase 2,"Adenosine deaminase that may contribute to the degradation of extracellular adenosine, a signaling molecule that controls a variety of cellular responses. Requires elevated adenosine levels for optimal enzyme activity. Binds to cell surfaces via proteoglycans and may play a role in the regulation of cell proliferation and differentiation, independently of its enzyme activity.","The overexpression of CECR1 may be responsible for at least some features of CES, particularly the heart defects.","The overexpression of CECR1 may be responsible for at least some features of CES, particularly the heart defects."
55,55,43380,Q68CZ1-S199G,MSGPTDETAGDLPVKDTGLNLFGMGGLQETSTTRTMKSRQAVSRVSREELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIRLVNDKKRYERVGGGPKRLGRDVEMEEMIEQLQEKVHELEKQNETLKNRLISAKQQLQTQGYRQTPYNNVQSRINTGRRKANENAGLQECPRKGIKFQDADVAETPHPMFTKYGNGLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIELSLLQLREQQATDQRSNIRDNVEMIKLHKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQLHSMKFSERRIEELQDRINDLEKERELLKENYDKLYDSAFSAAHEEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQQLDELKKRIKLYNQENDINADELSEALLLIKAQKEQKNGDLSFLVKVDSEINKDLERSMRELQATHAETVQELEKTRNMLIMQHKINKDYQMEVEAVTRKMENLQQDYELKVEQYVHLLDIRAARIHKLEAQLKDIAYGTKQYKFKPEIMPDDSVDEFDETIHLERGENLFEIHINKVTFSSEVLQASGDKEPVTFCTYAFYDFELQTTPVVRGLHPEYNFTSQYLVHVNDLFLQYIQKNTITLEVHQAYSTEYETIAACQLKFHEILEKSGRIFCTASLIGTKGDIPNFGTVEYWFRLRVPMDQAIRLYRERAKALGYITSNFKGPEHMQSLSQQAPKTAQLSSTDSTDGNLNELHITIRCCNHLQSRASHLQPHPYVVYKFFDFADHDTAIIPSSNDPQFDDHMYFPVPMNMDLDRYLKSESLSFYVFDDSDTQENIYIGKVNVPLISLAHDRCISGIFELTDHQKHPAGTIHVILKWKFAYLPPSGSITTEDLGNFIRSEEPEVVQRLPPASSVSTLVLAPRPKPRQRLTPVDKKVSFVDIMPHQSDETSPPPEDRKEISPEVEHIPEIEINMLTVPHVPKVSQE,Found in a patient with Leber congenital amaurosis.,,MSGPTDETAGDLPVKDTGLNLFGMGGLQETSTTRTMKSRQAVSRVSREELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIRLVNDKKRYERVGGGPKRLGRDVEMEEMIEQLQEKVHELEKQNETLKNRLISAKQQLQTQGYRQTPYNNVQSRINTGRRKANENAGLQECPRKGIKFQDADVAETPHPMFTKYGNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIELSLLQLREQQATDQRSNIRDNVEMIKLHKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQLHSMKFSERRIEELQDRINDLEKERELLKENYDKLYDSAFSAAHEEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQQLDELKKRIKLYNQENDINADELSEALLLIKAQKEQKNGDLSFLVKVDSEINKDLERSMRELQATHAETVQELEKTRNMLIMQHKINKDYQMEVEAVTRKMENLQQDYELKVEQYVHLLDIRAARIHKLEAQLKDIAYGTKQYKFKPEIMPDDSVDEFDETIHLERGENLFEIHINKVTFSSEVLQASGDKEPVTFCTYAFYDFELQTTPVVRGLHPEYNFTSQYLVHVNDLFLQYIQKNTITLEVHQAYSTEYETIAACQLKFHEILEKSGRIFCTASLIGTKGDIPNFGTVEYWFRLRVPMDQAIRLYRERAKALGYITSNFKGPEHMQSLSQQAPKTAQLSSTDSTDGNLNELHITIRCCNHLQSRASHLQPHPYVVYKFFDFADHDTAIIPSSNDPQFDDHMYFPVPMNMDLDRYLKSESLSFYVFDDSDTQENIYIGKVNVPLISLAHDRCISGIFELTDHQKHPAGTIHVILKWKFAYLPPSGSITTEDLGNFIRSEEPEVVQRLPPASSVSTLVLAPRPKPRQRLTPVDKKVSFVDIMPHQSDETSPPPEDRKEISPEVEHIPEIEINMLTVPHVPKVSQE,Protein fantom,"Negatively regulates signaling through the G-protein coupled thromboxane A2 receptor (TBXA2R). May be involved in mechanisms like programmed cell death, craniofacial development, patterning of the limbs, and formation of the left-right axis. Involved in the organization of apical junctions; the function is proposed to implicate a NPHP1-4-8 module. Does not seem to be strictly required for ciliogenesis. Involved in establishment of planar cell polarity such as in cochlear sensory epithelium and is proposed to implicate stabilization of disheveled proteins. Involved in regulation of proteasomal activity at the primary cilium probably implicating association with PSDM2.",,Found in a patient with Leber congenital amaurosis.
56,56,44816,Q06069-A395L,MKEVIAVKEITRFKTRTEEFSPYAWCKRMLENDPVSYHEGTDTWNVFKYEDVKRVLSDYKHFSSVRKRTTISVGTDSEEGSVPEKIQITESDPPDHRKRRSLLAAAFTPRSLQNWEPRIQEIADELIGQMDGGTEIDIVASLASPLPIIVMADLMGVPSKDRLLFKKWVDTLFLPFDREKQEEVDKLKQVAAKEYYQYLYPIVVQKRLNPADDIISDLLKSEVDGEMFTDDEVVRTTMLILGAGVETTSHLLANSFYSLLYDDKEVYQELHENLDLVPQAVEEMLRFRFNLIKLDRTVKEDNDLLGVELKEGDSVVVWMSAANMDEEMFEDPFTLNIHRPNNKKHLTFGNGPHFCLGAPLARLEAKIALTAFLKKFKHIEAVPSFQLEENLTDSLTGQTLTSLPLKASRM,40% of 15-beta hydroxylation activity (for progesterone).,,MKEVIAVKEITRFKTRTEEFSPYAWCKRMLENDPVSYHEGTDTWNVFKYEDVKRVLSDYKHFSSVRKRTTISVGTDSEEGSVPEKIQITESDPPDHRKRRSLLAAAFTPRSLQNWEPRIQEIADELIGQMDGGTEIDIVASLASPLPIIVMADLMGVPSKDRLLFKKWVDTLFLPFDREKQEEVDKLKQVAAKEYYQYLYPIVVQKRLNPADDIISDLLKSEVDGEMFTDDEVVRTTMLILGAGVETTSHLLANSFYSLLYDDKEVYQELHENLDLVPQAVEEMLRFRFNLIKLDRTVKEDNDLLGVELKEGDSVVVWMSAANMDEEMFEDPFTLNIHRPNNKKHLTFGNGPHFCLGAPLARLEAKIALTAFLKKFKHIEAVPSFQLEENLTDSATGQTLTSLPLKASRM,Cytochrome P450,Has the capacity to hydroxylate certain steroids in the 15-beta position. Also hydroxylates progesterone in the 11-alpha and 9-beta position.,The mutant was predicted to participate in active-site formation and influence substrate binding. This mutant altered the active-site structure and the hydroxylation activity of CYP106A2 dramatically.,40% of 15-beta hydroxylation activity (for progesterone). The mutant was predicted to participate in active-site formation and influence substrate binding. This mutant altered the active-site structure and the hydroxylation activity of CYP106A2 dramatically.
57,57,44845,A0PK11-T165K,MPGWFKKAWYGLASLLSFSSFILIIVALVVPHWLSGKILCQTGVDLVNATDRELVKFIGDIYYGLFRGCKVRQCGLGGRQSQFTIFPHLVKELNAGLHVMILLLLFLALALALVSMGFAILNMIQVPYRAVSGPGGICLWNVLAGGVVALAIASFVAAVKFHDLKERIANFQEKLFQFVVVEEQYEESFWICVASASAHAANLVVVAISQIPLPEIKTKIEEATVTAEDILY,In DFNB117; due to a nucleotide substitution that can result in aberrant splicing; patient cells contain both normally spliced transcripts and transcripts that retained intron 2.,,MPGWFKKAWYGLASLLSFSSFILIIVALVVPHWLSGKILCQTGVDLVNATDRELVKFIGDIYYGLFRGCKVRQCGLGGRQSQFTIFPHLVKELNAGLHVMILLLLFLALALALVSMGFAILNMIQVPYRAVSGPGGICLWNVLAGGVVALAIASFVAAVKFHDLTERIANFQEKLFQFVVVEEQYEESFWICVASASAHAANLVVVAISQIPLPEIKTKIEEATVTAEDILY,Clarin-2,Plays a key role to hearing function. Required for normal organization and maintenance of the stereocilia bundle and for mechano-electrical transduction.,"The CLRN2 c. p. (). This variant also leads to aberrant splicing, with the retention of intron 2 resulting in a stop codon after 26 additional amino acids, p. (G146Kfs*26). Expression studies and phenotyping of newly produced zebrafish and mouse models deficient for clarin 2 further confirm that clarin 2, expressed in the inner ear hair cells, is essential for normal organization and maintenance of the auditory hair bundles, and for hearing function. CLRN2 is identified as a new deafness gene.","In DFNB117; due to a nucleotide substitution that can result in aberrant splicing; patient cells contain both normally spliced transcripts and transcripts that retained intron 2. The CLRN2 c. p. (). This variant also leads to aberrant splicing, with the retention of intron 2 resulting in a stop codon after 26 additional amino acids, p. (G146Kfs*26). Expression studies and phenotyping of newly produced zebrafish and mouse models deficient for clarin 2 further confirm that clarin 2, expressed in the inner ear hair cells, is essential for normal organization and maintenance of the auditory hair bundles, and for hearing function. CLRN2 is identified as a new deafness gene."
58,58,45517,Q9FGL5-S677P,MRLKNFPFFVLFFFFCFNSNQSWGLMSSNQQPQFFKLMKNSLFGDALSTWNVYDVGTNYCNFTGVRCDGQGLVTDLDLSGLSLSGIFPDGVCSYFPNLRVLRLSHNHLNKSSSFLNTIPNCSLLRDLNMSSVYLKGTLPDFSQMKSLRVIDMSWNHFTGSFPLSIFNLTDLEYLNFNENPELDLWTLPDSVSKLTKLTHMLLMTCMLHGNIPRSIGNLTSLVDLELSGNFLSGEIPKEIGNLSNLRQLELYYNYHLTGSIPEEIGNLKNLTDIDISVSRLTGSIPDSICSLPNLRVLQLYNNSLTGEIPKSLGNSKTLKILSLYDNYLTGELPPNLGSSSPMIALDVSENRLSGPLPAHVCKSGKLLYFLVLQNRFTGSIPETYGSCKTLIRFRVASNRLVGTIPQGVMSLPHVSIIDLAYNSLSGPIPNAIGNAWNLSELFMQSNRISGVIPHELSHSTNLVKLDLSNNQLSGPIPSEVGRLRKLNLLVLQGNHLDSSIPDSLSNLKSLNVLDLSSNLLTGRIPENLSELLPTSINFSSNRLSGPIPVSLIRGGLVESFSDNPNLCIPPTAGSSDLKFPMCQEPHGKKKLSSIWAILVSVFILVLGVIMFYLRQRMSKNRAVIEQDETLASSFFSYDVKSFHRISFDQREILESLVDKNIVGHGGSGTVYRVELKPGEVVAVKKLWSQSNKDSASEDKMHLNKELKTEVETLGSIRHKNIVKLFSYFSSLDCSLLVYEYMPNGNLWDALHKGFVHLEWRTRHQIAVGVAQGLAYLHHDLSPPIIHRDIKSTNILLDVNYQPKVADFGIAKVLQARGKDSTTTVMAGTYGYLAPEYAYSSKATIKCDVYSFGVVLMELITGKKPVDSCFGENKNIVNWVSTKIDTKEGLIETLDKRLSESSKADMINALRVAIRCTSRTPTIRPTMNEVVQLLIDATPQGGPDMTSKPTTKIKDSIVSDHLTQTRL,Short inflorescence stems and increased anthocyanin accumulation in leaves.,,MRLKNFPFFVLFFFFCFNSNQSWGLMSSNQQPQFFKLMKNSLFGDALSTWNVYDVGTNYCNFTGVRCDGQGLVTDLDLSGLSLSGIFPDGVCSYFPNLRVLRLSHNHLNKSSSFLNTIPNCSLLRDLNMSSVYLKGTLPDFSQMKSLRVIDMSWNHFTGSFPLSIFNLTDLEYLNFNENPELDLWTLPDSVSKLTKLTHMLLMTCMLHGNIPRSIGNLTSLVDLELSGNFLSGEIPKEIGNLSNLRQLELYYNYHLTGSIPEEIGNLKNLTDIDISVSRLTGSIPDSICSLPNLRVLQLYNNSLTGEIPKSLGNSKTLKILSLYDNYLTGELPPNLGSSSPMIALDVSENRLSGPLPAHVCKSGKLLYFLVLQNRFTGSIPETYGSCKTLIRFRVASNRLVGTIPQGVMSLPHVSIIDLAYNSLSGPIPNAIGNAWNLSELFMQSNRISGVIPHELSHSTNLVKLDLSNNQLSGPIPSEVGRLRKLNLLVLQGNHLDSSIPDSLSNLKSLNVLDLSSNLLTGRIPENLSELLPTSINFSSNRLSGPIPVSLIRGGLVESFSDNPNLCIPPTAGSSDLKFPMCQEPHGKKKLSSIWAILVSVFILVLGVIMFYLRQRMSKNRAVIEQDETLASSFFSYDVKSFHRISFDQREILESLVDKNIVGHGGSGTVYRVELKSGEVVAVKKLWSQSNKDSASEDKMHLNKELKTEVETLGSIRHKNIVKLFSYFSSLDCSLLVYEYMPNGNLWDALHKGFVHLEWRTRHQIAVGVAQGLAYLHHDLSPPIIHRDIKSTNILLDVNYQPKVADFGIAKVLQARGKDSTTTVMAGTYGYLAPEYAYSSKATIKCDVYSFGVVLMELITGKKPVDSCFGENKNIVNWVSTKIDTKEGLIETLDKRLSESSKADMINALRVAIRCTSRTPTIRPTMNEVVQLLIDATPQGGPDMTSKPTTKIKDSIVSDHLTQTRL,Receptor protein-tyrosine kinase CEPR1,"Receptor kinase involved in the perception of C-terminally encoded plant signaling peptide (CEP) and subsequent regulation of root and shoot development. Required for xylem and phloem cell files morphology and organization, probably by preventing ectopic lignification in phloem cells. Together with CEPR2, mediates systemic nitrogen (N)-demand signaling upon the perception of root-derived peptides (e.g. CEP1) via the up-regulation of genes involved in N uptake and assimilation pathways. Regulates positively lateral root initiation and development; probably repressed by the signaling peptide CEP5.","The mutants in this kinase display an aberrant accumulation of highly lignified cells, typical of xylem or fiber cells, within the phloem. In addition, phloem cells are sometimes located adjacent to xylem cells in these mutants. Analyses of longitudinal profiles of xip1 mutant stems show malformed cell files, indicating defects in oriented cell divisions or cell morphology. We propose that XIP1 prevents ectopic lignification in phloem cells and is necessary to maintain the organization of cell files or cell morphology in conductive elements.","Short inflorescence stems and increased anthocyanin accumulation in leaves. The mutants in this kinase display an aberrant accumulation of highly lignified cells, typical of xylem or fiber cells, within the phloem. In addition, phloem cells are sometimes located adjacent to xylem cells in these mutants. Analyses of longitudinal profiles of xip1 mutant stems show malformed cell files, indicating defects in oriented cell divisions or cell morphology. We propose that XIP1 prevents ectopic lignification in phloem cells and is necessary to maintain the organization of cell files or cell morphology in conductive elements."
59,59,47548,Q06069-Q398S,MKEVIAVKEITRFKTRTEEFSPYAWCKRMLENDPVSYHEGTDTWNVFKYEDVKRVLSDYKHFSSVRKRTTISVGTDSEEGSVPEKIQITESDPPDHRKRRSLLAAAFTPRSLQNWEPRIQEIADELIGQMDGGTEIDIVASLASPLPIIVMADLMGVPSKDRLLFKKWVDTLFLPFDREKQEEVDKLKQVAAKEYYQYLYPIVVQKRLNPADDIISDLLKSEVDGEMFTDDEVVRTTMLILGAGVETTSHLLANSFYSLLYDDKEVYQELHENLDLVPQAVEEMLRFRFNLIKLDRTVKEDNDLLGVELKEGDSVVVWMSAANMDEEMFEDPFTLNIHRPNNKKHLTFGNGPHFCLGAPLARLEAKIALTAFLKKFKHIEAVPSFQLEENLTDSATGSTLTSLPLKASRM,30% of 15-beta hydroxylation activity (for progesterone).,,MKEVIAVKEITRFKTRTEEFSPYAWCKRMLENDPVSYHEGTDTWNVFKYEDVKRVLSDYKHFSSVRKRTTISVGTDSEEGSVPEKIQITESDPPDHRKRRSLLAAAFTPRSLQNWEPRIQEIADELIGQMDGGTEIDIVASLASPLPIIVMADLMGVPSKDRLLFKKWVDTLFLPFDREKQEEVDKLKQVAAKEYYQYLYPIVVQKRLNPADDIISDLLKSEVDGEMFTDDEVVRTTMLILGAGVETTSHLLANSFYSLLYDDKEVYQELHENLDLVPQAVEEMLRFRFNLIKLDRTVKEDNDLLGVELKEGDSVVVWMSAANMDEEMFEDPFTLNIHRPNNKKHLTFGNGPHFCLGAPLARLEAKIALTAFLKKFKHIEAVPSFQLEENLTDSATGQTLTSLPLKASRM,Cytochrome P450,Has the capacity to hydroxylate certain steroids in the 15-beta position. Also hydroxylates progesterone in the 11-alpha and 9-beta position.,The mutant was predicted to participate in active-site formation and influence substrate binding. This mutant altered the active-site structure and the hydroxylation activity of CYP106A2 dramatically.,30% of 15-beta hydroxylation activity (for progesterone). The mutant was predicted to participate in active-site formation and influence substrate binding. This mutant altered the active-site structure and the hydroxylation activity of CYP106A2 dramatically.
60,60,48728,P51843-R425T,MAGENHQWQGSILYNMLMSAKQTRAAPEAPETRLVDQCWGCSCGDEPGVGREGLLGGRNVALLYRCCFCGKDHPRQGSILYSMLTSAKQTYAAPKAPEATLGPCWGCSCGSDPGVGRAGLPGGRPVALLYRCCFCGEDHPRQGSILYSLLTSSKQTHVAPAAPEARPGGAWWDRSYFAQRPGGKEALPGGRATALLYRCCFCGEDHPQQGSTLYCVPTSTNQAQAAPEERPRAPWWDTSSGALRPVALKSPQVVCEAASAGLLKTLRFVKYLPCFQVLPLDQQLVLVRNCWASLLMLELAQDRLQFETVEVSEPSMLQKILTTRRRETGGNEPLPVPTLQHHLAPPAEARKVPSASQVQAIKCFLSKCWSLNISTKEYAYLKGTVLFNPDVPGLQCVKYIQGLQWGTQQILSEHTRMTHQGPHDTFIELNSTLFLLRFINANVIAELFFRPIIGTVSMDDMMLEMLCTKI,In AHC.,,MAGENHQWQGSILYNMLMSAKQTRAAPEAPETRLVDQCWGCSCGDEPGVGREGLLGGRNVALLYRCCFCGKDHPRQGSILYSMLTSAKQTYAAPKAPEATLGPCWGCSCGSDPGVGRAGLPGGRPVALLYRCCFCGEDHPRQGSILYSLLTSSKQTHVAPAAPEARPGGAWWDRSYFAQRPGGKEALPGGRATALLYRCCFCGEDHPQQGSTLYCVPTSTNQAQAAPEERPRAPWWDTSSGALRPVALKSPQVVCEAASAGLLKTLRFVKYLPCFQVLPLDQQLVLVRNCWASLLMLELAQDRLQFETVEVSEPSMLQKILTTRRRETGGNEPLPVPTLQHHLAPPAEARKVPSASQVQAIKCFLSKCWSLNISTKEYAYLKGTVLFNPDVPGLQCVKYIQGLQWGTQQILSEHTRMTHQGPHDRFIELNSTLFLLRFINANVIAELFFRPIIGTVSMDDMMLEMLCTKI,Nuclear receptor subfamily 0 group B member 1,Orphan nuclear receptor. Component of a cascade required for the development of the hypothalamic-pituitary-adrenal-gonadal axis. Acts as a coregulatory protein that inhibits the transcriptional activity of other nuclear receptors through heterodimeric interactions. May also have a role in the development of the embryo and in the maintenance of embryonic stem cell pluripotency.,The mutation in the NR0B1 gene causes X-linked adrenal hypoplasia congenita.,In AHC. The mutation in the NR0B1 gene causes X-linked adrenal hypoplasia congenita.
61,61,49963,Q96AX1-I441K,MAAHLSYGRVNLNVLREAVRRELREFLDKCAGSKAIVWDEYLTGPFGLIAQYSLLKEHEVEKMFTLKGNRLPAADVKNIIFFVRPRLELMDIIAENVLSEDRRGPTRDFHILFVPRRSLLCEQRLKDLGVLGSFIHREEYSLDLIPFDGDLLSMESEGAFKECYLEGDQTSLYHAAKGLMTLQALYGTIPQIFGKGECARQVANMMIRMKREFTGSQNSIFPVFDNLLLLDRNVDLLTPLATQLTYEGLIDEIYGIQNSYVKLPPEKFAPKKQGDGGKDLPTEAKKLQLNSAEELYAEIRDKNFNAVGSVLSKKAKIISAAFEERHNAKTVGEIKQFVSQLPHMQAARGSLANHTSIAELIKDVTTSEDFFDKLTVEQEFMSGIDTDKVNNYIEDCIAQKHSLIKVLRLVCLQSVCNSGLKQKVLDYYKREILQTYGYEHKLTLHNLEKAGLLKPQTGGRNNYPTIRKTLRLWMDDVNEQNPTDISYVYSGYAPLSVRLAQLLSRPGWRSIEEVLRILPGPHFEERQPLPTGLQKKRQPGENRVTLIFFLGGVTFAEIAALRFLSQLEDGGTEYVIATTKLMNGTSWIEALMEKPF,Disrupts interaction with VPS16. Disrupts interaction with VPS18 and impairs endosome-lysosome fusion; when associated with D-429. Disrupts interaction with VPS18 and impairs endosome-lysosome fusion; when associated with D-438.,,MAAHLSYGRVNLNVLREAVRRELREFLDKCAGSKAIVWDEYLTGPFGLIAQYSLLKEHEVEKMFTLKGNRLPAADVKNIIFFVRPRLELMDIIAENVLSEDRRGPTRDFHILFVPRRSLLCEQRLKDLGVLGSFIHREEYSLDLIPFDGDLLSMESEGAFKECYLEGDQTSLYHAAKGLMTLQALYGTIPQIFGKGECARQVANMMIRMKREFTGSQNSIFPVFDNLLLLDRNVDLLTPLATQLTYEGLIDEIYGIQNSYVKLPPEKFAPKKQGDGGKDLPTEAKKLQLNSAEELYAEIRDKNFNAVGSVLSKKAKIISAAFEERHNAKTVGEIKQFVSQLPHMQAARGSLANHTSIAELIKDVTTSEDFFDKLTVEQEFMSGIDTDKVNNYIEDCIAQKHSLIKVLRLVCLQSVCNSGLKQKVLDYYKREILQTYGYEHILTLHNLEKAGLLKPQTGGRNNYPTIRKTLRLWMDDVNEQNPTDISYVYSGYAPLSVRLAQLLSRPGWRSIEEVLRILPGPHFEERQPLPTGLQKKRQPGENRVTLIFFLGGVTFAEIAALRFLSQLEDGGTEYVIATTKLMNGTSWIEALMEKPF,Vacuolar protein sorting-associated protein 33A,"Plays a role in vesicle-mediated protein trafficking to lysosomal compartments including the endocytic membrane transport and autophagic pathways. Believed to act as a core component of the putative HOPS and CORVET endosomal tethering complexes which are proposed to be involved in the Rab5-to-Rab7 endosome conversion probably implicating MON1A/B, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion. The HOPS complex is proposed to be recruited to Rab7 on the late endosomal membrane and to regulate late endocytic, phagocytic and autophagic traffic towards lysosomes. The CORVET complex is proposed to function as a Rab5 effector to mediate early endosome fusion probably in specific endosome subpopulations. Required for fusion of endosomes and autophagosomes with lysosomes; the function is dependent on its association with VPS16 but not VIPAS39. The function in autophagosome-lysosome fusion implicates STX17 but not UVRAG.",The mutation in VPS16 no longer rescues lysosome fusion with endosomes or autophagosomes in cells depleted of the endogenous proteins.,Disrupts interaction with VPS16. Disrupts interaction with VPS18 and impairs endosome-lysosome fusion; when associated with D-429. Disrupts interaction with VPS18 and impairs endosome-lysosome fusion; when associated with D-438. The mutation in VPS16 no longer rescues lysosome fusion with endosomes or autophagosomes in cells depleted of the endogenous proteins.
62,62,51648,P08692-R60K,MSNITIYHNPACGTSRNTLEMIRNSGTEPTIILYLENPPSRDELVKLIADMGISVRALLKKNVEPYEQLGLAEDKFTDDQLIDFMLQHPILINRPIVVTPLGTRLCRPSEVVLDILQDAQKGAFTKEDGEKVVDEAGKRLK,22-fold decrease in catalytic efficiency with arsenate. Mutant shows low-level resistance to arsenate.,,MSNITIYHNPACGTSRNTLEMIRNSGTEPTIILYLENPPSRDELVKLIADMGISVRALLRKNVEPYEQLGLAEDKFTDDQLIDFMLQHPILINRPIVVTPLGTRLCRPSEVVLDILQDAQKGAFTKEDGEKVVDEAGKRLK,Arsenate reductase,Involved in resistance to arsenate. Catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)]. The resulting arsenite is then extruded from the cell via the ArsAB transport system (Probable).,The mutation confers arsenate resistance in vivo.,22-fold decrease in catalytic efficiency with arsenate. Mutant shows low-level resistance to arsenate. The mutation confers arsenate resistance in vivo.
63,63,53657,Q9JJS6-E469A,MEIIFGQNKKEQLEPVQAKVTGSIPAWLQGTLLRNGPGMHTVGESKYNHWFDGLALLHSFSIRDGEVFYRSKYLQSDTYIANIEANRIVVSEFGTMAYPDPCKNIFSKAFSYLSHTIPDFTDNCLINIMKCGEDFYATTETNYIRKIDPQTLETLEKVDYRKYVAVNLATSHPHYDEAGNVLNMGTSVVDKGRTKYVIFKIPATVPDSKKKGKSPVKHAEVFCSISSRSLLSPSYYHSFGVTENYVVFLEQPFKLDILKMATAYMRGVSWASCMSFDREDKTYIHIIDQRTRKPVPTKFYTDPMVVFHHVNAYEEDGCVLFDVIAYEDSSLYQLFYLANLNKDFEEKSRLTSVPTLRRFAVPLHVDKDAEVGSNLVKVSSTTATALKEKDGHVYCQPEVLYEGLELPRINYAYNGKPYRYIFAAEVQWSPVPTKILKYDILTKSSLKWSEESCWPAEPLFVPTPGAKDADDGVILSAIVSTDPQKLPFLLILDAKSFTELARASVDADMHLDLHGLFIPDADWNAVKQTPAETQEVENSDHPTDPTAPELSHSENDFTAGHGGSSL,"Decreased beta-carotene 15,15'-monooxygenase activity.",,MEIIFGQNKKEQLEPVQAKVTGSIPAWLQGTLLRNGPGMHTVGESKYNHWFDGLALLHSFSIRDGEVFYRSKYLQSDTYIANIEANRIVVSEFGTMAYPDPCKNIFSKAFSYLSHTIPDFTDNCLINIMKCGEDFYATTETNYIRKIDPQTLETLEKVDYRKYVAVNLATSHPHYDEAGNVLNMGTSVVDKGRTKYVIFKIPATVPDSKKKGKSPVKHAEVFCSISSRSLLSPSYYHSFGVTENYVVFLEQPFKLDILKMATAYMRGVSWASCMSFDREDKTYIHIIDQRTRKPVPTKFYTDPMVVFHHVNAYEEDGCVLFDVIAYEDSSLYQLFYLANLNKDFEEKSRLTSVPTLRRFAVPLHVDKDAEVGSNLVKVSSTTATALKEKDGHVYCQPEVLYEGLELPRINYAYNGKPYRYIFAAEVQWSPVPTKILKYDILTKSSLKWSEESCWPAEPLFVPTPGAKDEDDGVILSAIVSTDPQKLPFLLILDAKSFTELARASVDADMHLDLHGLFIPDADWNAVKQTPAETQEVENSDHPTDPTAPELSHSENDFTAGHGGSSL,"Beta,beta-carotene 15,15'-dioxygenase",Symmetrically cleaves beta-carotene into two molecules of retinal using a dioxygenase mechanism.,,"Decreased beta-carotene 15,15'-monooxygenase activity."
64,64,54541,Q9ULZ3-R41W,MGRARDAILDALENLTAEELKKFKLKLLSVPLREGYGRIPWGALLSMDALDLTDKLVSFYLETYGAELTANVLRDMGLQEMAGQLQAATHQGSGAAPAGIQAPPQSAAKPGLHFIDQHRAALIARVTNVEWLLDALYGKVLTDEQYQAVRAEPTNPSKMRKLFSFTPAWNWTCKDLLLQALRESQSYLVEDLERS,Abolishes homooligomerization.,,MGRARDAILDALENLTAEELKKFKLKLLSVPLREGYGRIPRGALLSMDALDLTDKLVSFYLETYGAELTANVLRDMGLQEMAGQLQAATHQGSGAAPAGIQAPPQSAAKPGLHFIDQHRAALIARVTNVEWLLDALYGKVLTDEQYQAVRAEPTNPSKMRKLFSFTPAWNWTCKDLLLQALRESQSYLVEDLERS,Apoptosis-associated speck-like protein containing a CARD,"Functions as key mediator in apoptosis and inflammation. Promotes caspase-mediated apoptosis involving predominantly caspase-8 and also caspase-9 in a probable cell type-specific manner. Involved in activation of the mitochondrial apoptotic pathway, promotes caspase-8-dependent proteolytic maturation of BID independently of FADD in certain cell types and also mediates mitochondrial translocation of BAX and activates BAX-dependent apoptosis coupled to activation of caspase-9, -2 and -3. Involved in innate immune response by acting as an integral adapter in the assembly of various inflammasomes (NLRP1, NLRP2, NLRP3, NLRP6, AIM2 and probably IFI16) which recruit and activate caspase-1 leading to processing and secretion of pro-inflammatory cytokines. Caspase-1-dependent inflammation leads to macrophage pyroptosis, a form of cell death. The function as activating adapter in different types of inflammasomes is mediated by the pyrin and CARD domains and their homotypic interactions. Clustered PYCARD nucleates the formation of caspase-1 filaments through the interaction of their respective CARD domains, acting as a platform for of caspase-1 polymerization. In the NLRP1 and NLRC4 inflammasomes seems not be required but facilitates the processing of procaspase-1. In cooperation with NOD2 involved in an inflammasome activated by bacterial muramyl dipeptide leading to caspase-1 activation. May be involved in RIGI-triggered pro-inflammatory responses and inflammasome activation. In collaboration with AIM2 which detects cytosolic double-stranded DNA may also be involved in a caspase-1-independent cell death that involves caspase-8. In adaptive immunity may be involved in maturation of dendritic cells to stimulate T-cell immunity and in cytoskeletal rearrangements coupled to chemotaxis and antigen uptake may be involved in post-transcriptional regulation of the guanine nucleotide exchange factor DOCK2; the latter function is proposed to involve the nuclear form. Also involved in transcriptional activation of cytokines and chemokines independent of the inflammasome; this function may involve AP-1, NF-kappa-B, MAPK and caspase-8 signaling pathways. For regulation of NF-kappa-B activating and inhibiting functions have been reported. Modulates NF-kappa-B induction at the level of the IKK complex by inhibiting kinase activity of CHUK and IKBK. Proposed to compete with RIPK2 for association with CASP1 thereby down-regulating CASP1-mediated RIPK2-dependent NF-kappa-B activation and activating interleukin-1 beta processing. Modulates host resistance to DNA virus infection, probably by inducing the cleavage of and inactivating CGAS in presence of cytoplasmic double-stranded DNA.May have a regulating effect on the function as inflammasome adapter.Seems to inhibit inflammasome-mediated maturation of interleukin-1 beta.",Mutation of R41 to W in ASC protein leads to loss of filament formation.,Abolishes homooligomerization. Mutation of R41 to W in ASC protein leads to loss of filament formation.
65,65,55039,Q96RL7-E842A,MVFESVVVDVLNRFLGDYVVDLDTSQLSLGIWKGAVALKNLQIKENALSQLDVPFKVKVGHIGNLKLIIPWKNLYTQPVEAVLEEIYLLIVPSSRIKYDPLKEEKQLMEAKQQELKRIEEAKQKVVDQEQHLPEKQDTFAEKLVTQIIKNLQVKISSIHIRYEDDITNRDKPLSFGISLQNLSMQTTDQYWVPCLHDETEKLVRKLIRLDNLFAYWNVKSQMFYLSDYDNSLDDLKNGIVNENIVPEGYDFVFRPISANAKLVMNRRSDFDFSAPKINLEIELHNIAIEFNKPQYFSIMELLESVDMMAQNLPYRKFKPDVPLHHHAREWWAYAIHGVLEVNVCPRLWMWSWKHIRKHRQKVKQYKELYKKKLTSKKPPGELLVSLEELEKTLDVFNITIARQTAEVEVKKAGYKIYKEGVKDPEDNKGWFSWLWSWSEQNTNEQQPDVQPETLEEMLTPEEKALLYEAIGYSETAVDPTLLKTFEALKFFVHLKSMSIVLRENHQKPELVDIVIEEFSTLIVQRPGAQAIKFETKIDSFHITGLPDNSEKPRLLSSLDDAMSLFQITFEINPLDETVSQRCIIEAEPLEIIYDARTVNSIVEFFRPPKEVHLAQLTAATLTKLEEFRSKTATGLLYIIETQKVLDLKINLKASYIIVPQDGIFSPTSNLLLLDLGHLKVTSKSRSELPDVKQGEANLKEIMDRAYDSFDIQLTSVQLLYSRVGDNWREARKLSVSTQHILVPMHFNLELSKAMVFMDVRMPKFKIYGKLPLISLRISDKKLQGIMELIESIPKPEPVTEVSAPVKSFQIQTSTSLGTSQISQKIIPLLELPSVSEDDSEEAFFDAPCSPLEEPLQFPTGVKSIRTRKLQKQDCSVNMTTFKIRFEVPKVLIEFYHLVGDCELSVVEILVLGLGAEIEIRTYDLKANAFLKEFCLKCPEYLDENKKPVYLVTTLDNTMEDLLTLEYVKAEKNVPDLKSTYNNVLQLIKVNFSSLDIHLHTEALLNTINYLHNILPQSEEKSAPV,Reduced interaction with VAPA.,,MVFESVVVDVLNRFLGDYVVDLDTSQLSLGIWKGAVALKNLQIKENALSQLDVPFKVKVGHIGNLKLIIPWKNLYTQPVEAVLEEIYLLIVPSSRIKYDPLKEEKQLMEAKQQELKRIEEAKQKVVDQEQHLPEKQDTFAEKLVTQIIKNLQVKISSIHIRYEDDITNRDKPLSFGISLQNLSMQTTDQYWVPCLHDETEKLVRKLIRLDNLFAYWNVKSQMFYLSDYDNSLDDLKNGIVNENIVPEGYDFVFRPISANAKLVMNRRSDFDFSAPKINLEIELHNIAIEFNKPQYFSIMELLESVDMMAQNLPYRKFKPDVPLHHHAREWWAYAIHGVLEVNVCPRLWMWSWKHIRKHRQKVKQYKELYKKKLTSKKPPGELLVSLEELEKTLDVFNITIARQTAEVEVKKAGYKIYKEGVKDPEDNKGWFSWLWSWSEQNTNEQQPDVQPETLEEMLTPEEKALLYEAIGYSETAVDPTLLKTFEALKFFVHLKSMSIVLRENHQKPELVDIVIEEFSTLIVQRPGAQAIKFETKIDSFHITGLPDNSEKPRLLSSLDDAMSLFQITFEINPLDETVSQRCIIEAEPLEIIYDARTVNSIVEFFRPPKEVHLAQLTAATLTKLEEFRSKTATGLLYIIETQKVLDLKINLKASYIIVPQDGIFSPTSNLLLLDLGHLKVTSKSRSELPDVKQGEANLKEIMDRAYDSFDIQLTSVQLLYSRVGDNWREARKLSVSTQHILVPMHFNLELSKAMVFMDVRMPKFKIYGKLPLISLRISDKKLQGIMELIESIPKPEPVTEVSAPVKSFQIQTSTSLGTSQISQKIIPLLELPSVSEDDSEEEFFDAPCSPLEEPLQFPTGVKSIRTRKLQKQDCSVNMTTFKIRFEVPKVLIEFYHLVGDCELSVVEILVLGLGAEIEIRTYDLKANAFLKEFCLKCPEYLDENKKPVYLVTTLDNTMEDLLTLEYVKAEKNVPDLKSTYNNVLQLIKVNFSSLDIHLHTEALLNTINYLHNILPQSEEKSAPV,Intermembrane lipid transfer protein VPS13A,Mediates the transfer of lipids between membranes at organelle contact sites. Binds phospholipids. Required for the formation or stabilization of ER-mitochondria contact sites which enable transfer of lipids between the ER and mitochondria. Negatively regulates lipid droplet size and motility. Required for efficient lysosomal protein degradation.,The consequences of impaired function of VPS13A at the subcellular level are unknown.,Reduced interaction with VAPA. The consequences of impaired function of VPS13A at the subcellular level are unknown.
66,66,55581,P06022-D40N,MQHDLFEHDPAIRQLIGHIDNIPAPELESRWPRSVVDLINVLENELKRQNVSNPRELARKQAVALSCFLGGRQFYIPCGDTILTALRDDLLYCQFNGRNMEELRRQYRLSQPQIYQIIARQRKLHTRRHQPDLFSPETPK,Loss of DNA-binding activity and transactivation. No effect on dimerization.,,MQHDLFEHDPAIRQLIGHIDNIPAPELESRWPRSVVDLIDVLENELKRQNVSNPRELARKQAVALSCFLGGRQFYIPCGDTILTALRDDLLYCQFNGRNMEELRRQYRLSQPQIYQIIARQRKLHTRRHQPDLFSPETPK,Late transcription activator C,"Positive regulator of viral late genes transcription. Responsible for the transition from middle to late gene expression. Activates the Plys, PI, PP and Pmom late promoters thereby allowing the expression of viral endolysin and structural genes. Activates Pmom promoter by unwinding the DNA, thus realigning the promoter elements and recruiting the RNAP.","Mutations in residue D40 lead to altered Mg(2+)-induced conformation, compromised DNA binding, and reduced levels of transcription activation.","Loss of DNA-binding activity and transactivation. No effect on dimerization. Mutations in residue D40 lead to altered Mg(2+)-induced conformation, compromised DNA binding, and reduced levels of transcription activation."
67,67,56731,O54908-H267E,MMVVCAAAAVRFLAVFTMMALCSLPLLGASATLNSVLINSNAIKNLPPPLGGAGGQPGSAVSVAPGVLYEGGNKYQTLDNYQPYPCAEDEECGSDEYCSSPSRGAAGVGGVQICLACRKRRKRCMRHAMCCPGNYCKNGICMPSDHSHFPRGEIEESIIENLGNDHNAAAGDGYPRRTTLTSKIYHTKGQEGSVCLRSSDCAAGLCCARHFWSKICKPVLKEGQVCTKHKRKGSHGLEIFQRCYCGEGLACRIQKDHHQASNSSRLETCQRH,43% reduced binding to LRP6.,,MMVVCAAAAVRFLAVFTMMALCSLPLLGASATLNSVLINSNAIKNLPPPLGGAGGQPGSAVSVAPGVLYEGGNKYQTLDNYQPYPCAEDEECGSDEYCSSPSRGAAGVGGVQICLACRKRRKRCMRHAMCCPGNYCKNGICMPSDHSHFPRGEIEESIIENLGNDHNAAAGDGYPRRTTLTSKIYHTKGQEGSVCLRSSDCAAGLCCARHFWSKICKPVLKEGQVCTKHKRKGSHGLEIFQRCYCGEGLACRIQKDHHQASNSSRLHTCQRH,Dickkopf-related protein 1,"Antagonizes canonical Wnt signaling by inhibiting LRP5/6 interaction with Wnt and by forming a ternary complex with the transmembrane protein KREMEN that promotes internalization of LRP5/6. Inhibits the pro-apoptotic function of KREMEN1 in a Wnt-independent manner, and has anti-apoptotic activity. Plays a role in limb development; attenuates Wnt signaling in the developing limb to allow normal limb patterning.",,43% reduced binding to LRP6.
68,68,57393,Q9HSF6-H33A,MPVVECDIQTARAALADAGASFSDGNSEHELWAADLGDAHAVAYADKLVVQGGSPTDITAVVQPDRGGRVHAYFDGASRGNPGPAAVGWVLVSGDGGIVAEGGDTIGRATNNQAEYDALIAALEAAADFGFDDIELRGDSQLVEKQLTGAWDTNDPDLRRKRVRARELLTGFDDWSITHVPRATNERADALANEALDDA,No loss of RNase H activity.,,MPVVECDIQTARAALADAGASFSDGNSEHELWHADLGDAHAVAYADKLVVQGGSPTDITAVVQPDRGGRVHAYFDGASRGNPGPAAVGWVLVSGDGGIVAEGGDTIGRATNNQAEYDALIAALEAAADFGFDDIELRGDSQLVEKQLTGAWDTNDPDLRRKRVRARELLTGFDDWSITHVPRATNERADALANEALDDA,Ribonuclease HI,Nuclease that specifically degrades the RNA of RNA-DNA hybrids; seems to act exonucleolytically on RNA/DNA hybrids. Endonucleolytically removes RNA primers from the Okazaki fragments of lagging strand synthesis on its own. Complements the temperature-sensitive phenotype of an E.coli double rnhA/rnhB (RNase H) disruption mutant.,The purified recombinant Vng0255c protein specifically cleaved an RNA strand of the RNA/DNA hybrid in vitro.,No loss of RNase H activity. The purified recombinant Vng0255c protein specifically cleaved an RNA strand of the RNA/DNA hybrid in vitro.
69,69,58308,B9EJA2-P602A,MATDSASCEPDLSRTPGDTEGATAEAAKKEFDVDTLSKSELRMLLSVMEGELEARDLVIEALRARRKEVFIQERYGRFNLNDPFLALQRDYEAGPGDKEKPVCTNPLSILEAVMAHCRKMQERMSAQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKNKHVVLMLVKECKQLSGKVVEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEIDKMKKMMEQMKKGSDGKPGLSLPRKTKDKRLASISVATEGPVTRSVACQTDVVTESTDPVKKLPLTVPIKPSTGSPLVPTNTKGNVGPSALLIRPGIDRQSSHSDLGPSPPTALPSSANRIEENGPSTGNAPDLSNSTPSTPSSTAPAAAQTPGTAPQNHSQAPTVHSLHSPCANTHPGLNPRIQAARFRFQGNANDPDQNGNNTQSPPSRDVSPTSRDNLVAKQLARNTVTQALSRFTSPQAGASSRLGVSPGGDAGTCPPVGRTGLKTPGAARVDRGNPPPIPPKKPGLSQTPSPPHPQLRASNAGAKVDNKIVASPPSTLPQGTKVVNEENVPKSSSPQLAPKPSIDLTVAPAGCPVSALATSQVGAWPAGTPGLNQPACSDSSLVIPATVAFCSSINPVSASSRSPGASDSLLVAASGWSPSLTPLLMSGGPAPLAGRPTLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFECIELLTAYNANINHSAAGGQTPLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVDSLKLLMYHRVRAHGNSLSSEEPKSGLFSLNGGESPTGPSKPVVPADLINHADKEGWTAAHIAASKGFKNCLEVLCRHGGLEPERRDKCNRTVHDVATDDCKHLLENLNALKIPLRISVGEIQPSNDVSDDFECEHTICTLNIRKQTSWEDFSKAVSQALTNHFQAISSDGWWSLEDG,Reduced CTTN-binding; when associated with A-599.,,MATDSASCEPDLSRTPGDTEGATAEAAKKEFDVDTLSKSELRMLLSVMEGELEARDLVIEALRARRKEVFIQERYGRFNLNDPFLALQRDYEAGPGDKEKPVCTNPLSILEAVMAHCRKMQERMSAQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKNKHVVLMLVKECKQLSGKVVEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEIDKMKKMMEQMKKGSDGKPGLSLPRKTKDKRLASISVATEGPVTRSVACQTDVVTESTDPVKKLPLTVPIKPSTGSPLVPTNTKGNVGPSALLIRPGIDRQSSHSDLGPSPPTALPSSANRIEENGPSTGNAPDLSNSTPSTPSSTAPAAAQTPGTAPQNHSQAPTVHSLHSPCANTHPGLNPRIQAARFRFQGNANDPDQNGNNTQSPPSRDVSPTSRDNLVAKQLARNTVTQALSRFTSPQAGASSRLGVSPGGDAGTCPPVGRTGLKTPGAARVDRGNPPPIPPKKPGLSQTPSPPHPQLRASNAGAKVDNKIVASPPSTLPQGTKVVNEENVPKSSSPQLPPKPSIDLTVAPAGCPVSALATSQVGAWPAGTPGLNQPACSDSSLVIPATVAFCSSINPVSASSRSPGASDSLLVAASGWSPSLTPLLMSGGPAPLAGRPTLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFECIELLTAYNANINHSAAGGQTPLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVDSLKLLMYHRVRAHGNSLSSEEPKSGLFSLNGGESPTGPSKPVVPADLINHADKEGWTAAHIAASKGFKNCLEVLCRHGGLEPERRDKCNRTVHDVATDDCKHLLENLNALKIPLRISVGEIQPSNDVSDDFECEHTICTLNIRKQTSWEDFSKAVSQALTNHFQAISSDGWWSLEDG,Cortactin-binding protein 2,"Regulates the dendritic spine distribution of CTTN/cortactin in hippocampal neurons, and thus controls dendritic spinogenesis and dendritic spine maintenance.",,Reduced CTTN-binding; when associated with A-599.
70,70,60782,P32266-T244A,MNASPVRLLILRRQLATHPAILYSSPYIKSPLVHLHSRMSNVHRSAHANALSFVITRRSISHFPKIISKIIRLPIYVGGGMAAAGSYIAYKMEEASSFTKDKLDRIKDLGESMKEKFNKMFSGDKSQDGGHGNDGTVPTATLIAATSLDDDESKRQGDPKDDDDEDDDDEDDENDSVDTTQDEMLNLTKQMIEIRTILNKVDSSSAHLTLPSIVVIGSQSSGKSSVLESIVGREFLPKGSNMVARRPIELTLVNTPNSNNVTADFPSMRLYNIKDFKEVKRMLMELNMAVPTSEAVSEEPIQLTIKSSRVPDLSLVDLPGYIQVEAADQPIELKTKIRDLCEKYLTAPNIILAISAADVDLANSSALKASKAADPKGLRTIGVITKLDLVDPEKARSILNNKKYPLSMGYVGVITKTPSSINRKHLGLFGEAPSSSLSGIFSKGQHGQSSGEENTNGLKQIVSHQFEKAYFKENKKYFTNCQVSTKKLREKLIKILEISMSNALEPTSTLIQQELDDTSYLFKVEFNDRHLTPKSYLLNNIDVLKLGIKEFQEKFHRNELKSILRAELDQKVLDVLATRYWKDDNLQDLSSSKLESDTDMLYWHKKLELASSGLTKMGIGRLSTMLTTNAILKELDNILESTQLKNHELIKDLVSNTAINVLNSKYYSTADQVENCIKPFKYEIDLEERDWSLARQHSINLIKEELRQCNSRYQAIKNAVGSKKLANVMGYLENESNLQKETLGMSKLLLERGSEAIFLDKRCKVLSFRLKMLKNKCHSTIEKDRCPEVFLSAVSDKLTSTAVLFLNVELLSDFFYNFPIELDRRLTLLGDEQVEMFAKEDPKISRHIELQKRKELLELALEKIDSILVFKKSYKGVSKNL,Loss of GTPase activity.,,MNASPVRLLILRRQLATHPAILYSSPYIKSPLVHLHSRMSNVHRSAHANALSFVITRRSISHFPKIISKIIRLPIYVGGGMAAAGSYIAYKMEEASSFTKDKLDRIKDLGESMKEKFNKMFSGDKSQDGGHGNDGTVPTATLIAATSLDDDESKRQGDPKDDDDEDDDDEDDENDSVDTTQDEMLNLTKQMIEIRTILNKVDSSSAHLTLPSIVVIGSQSSGKSSVLESIVGREFLPKGSNMVTRRPIELTLVNTPNSNNVTADFPSMRLYNIKDFKEVKRMLMELNMAVPTSEAVSEEPIQLTIKSSRVPDLSLVDLPGYIQVEAADQPIELKTKIRDLCEKYLTAPNIILAISAADVDLANSSALKASKAADPKGLRTIGVITKLDLVDPEKARSILNNKKYPLSMGYVGVITKTPSSINRKHLGLFGEAPSSSLSGIFSKGQHGQSSGEENTNGLKQIVSHQFEKAYFKENKKYFTNCQVSTKKLREKLIKILEISMSNALEPTSTLIQQELDDTSYLFKVEFNDRHLTPKSYLLNNIDVLKLGIKEFQEKFHRNELKSILRAELDQKVLDVLATRYWKDDNLQDLSSSKLESDTDMLYWHKKLELASSGLTKMGIGRLSTMLTTNAILKELDNILESTQLKNHELIKDLVSNTAINVLNSKYYSTADQVENCIKPFKYEIDLEERDWSLARQHSINLIKEELRQCNSRYQAIKNAVGSKKLANVMGYLENESNLQKETLGMSKLLLERGSEAIFLDKRCKVLSFRLKMLKNKCHSTIEKDRCPEVFLSAVSDKLTSTAVLFLNVELLSDFFYNFPIELDRRLTLLGDEQVEMFAKEDPKISRHIELQKRKELLELALEKIDSILVFKKSYKGVSKNL,"Dynamin-like GTPase MGM1, mitochondrial",Dynamin-related GTPase required for mitochondrial fusion. Coordinates interaction between the inner and outer mitochondrial membrane to promote the formation of the double membrane.,,Loss of GTPase activity.
71,71,62603,P15917-I72A,MNIKKEFIKVISMSCLVTAITLSGPVFIPLVQGAGGHGDVGMHVKEKEKNKDENKRKDEERNKTQEEHLKEAMKHIVKIEVKGEEAVKKEAAEKLLEKVPSDVLEMYKAIGGKIYIVDGDITKHISLEALSEDKKKIKDIYGKDALLHEHYVYAKEGYEPVLVIQSSEDYVENTEKALNVYYEIGKILSRDILSKINQPYQKFLDVLNTIKNASDSDGQDLLFTNQLKEHPTDFSVEFLEQNSNEVQEVFAKAFAYYIEPQHRDVLQLYAPEAFNYMDKFNEQEINLSLEELKDQRMLARYEKWEKIKQHYQHWSDSLSEEGRGLLKKLQIPIEPKKDDIIHSLSQEEKELLKRIQIDSSDFLSTEEKEFLKKLQIDIRDSLSEEEKELLNRIQVDSSNPLSEKEKEFLKKLKLDIQPYDINQRLQDTGGLIDSPSINLDVRKQYKRDIQNIDALLHQSIGSTLYNKIYLYENMNINNLTATLGADLVDSTDNTKINRGIFNEFKKNFKYSISSNYMIVDINERPALDNERLKWRIQLSPDTRAGYLENGKLILQRNIGLEIKDVQIIKQSEKEYIRIDAKVVPKSKIDTKIQEAQLNINQEWNKALGLPKYTKLITFNVHNRYASNIVESAYLILNEWKNNIQSDLIKKVTNYLVDGNGRFVFTDITLPNIAEQYTHQDEIYEQVHSKGLYVPESRSILLHGPSKGVELRNDSEGFIHEFGHAVDDYAGYLLDKNQSDLVTNSKKFIDIFKEEGSNLTSYGRTNEAEFFAEAFRLMHSTDHAERLKVQKNAPKTFQFINDQIKFIINS,Does not affect translocation into host cytoplasm.,,MNIKKEFIKVISMSCLVTAITLSGPVFIPLVQGAGGHGDVGMHVKEKEKNKDENKRKDEERNKTQEEHLKEIMKHIVKIEVKGEEAVKKEAAEKLLEKVPSDVLEMYKAIGGKIYIVDGDITKHISLEALSEDKKKIKDIYGKDALLHEHYVYAKEGYEPVLVIQSSEDYVENTEKALNVYYEIGKILSRDILSKINQPYQKFLDVLNTIKNASDSDGQDLLFTNQLKEHPTDFSVEFLEQNSNEVQEVFAKAFAYYIEPQHRDVLQLYAPEAFNYMDKFNEQEINLSLEELKDQRMLARYEKWEKIKQHYQHWSDSLSEEGRGLLKKLQIPIEPKKDDIIHSLSQEEKELLKRIQIDSSDFLSTEEKEFLKKLQIDIRDSLSEEEKELLNRIQVDSSNPLSEKEKEFLKKLKLDIQPYDINQRLQDTGGLIDSPSINLDVRKQYKRDIQNIDALLHQSIGSTLYNKIYLYENMNINNLTATLGADLVDSTDNTKINRGIFNEFKKNFKYSISSNYMIVDINERPALDNERLKWRIQLSPDTRAGYLENGKLILQRNIGLEIKDVQIIKQSEKEYIRIDAKVVPKSKIDTKIQEAQLNINQEWNKALGLPKYTKLITFNVHNRYASNIVESAYLILNEWKNNIQSDLIKKVTNYLVDGNGRFVFTDITLPNIAEQYTHQDEIYEQVHSKGLYVPESRSILLHGPSKGVELRNDSEGFIHEFGHAVDDYAGYLLDKNQSDLVTNSKKFIDIFKEEGSNLTSYGRTNEAEFFAEAFRLMHSTDHAERLKVQKNAPKTFQFINDQIKFIINS,Lethal factor,"Lethal factor (LF), which constitutes one of the three proteins composing the anthrax toxin, is able to trigger rapid cell death in macrophages. Acts as a protease that cleaves the N-terminal of most dual specificity mitogen-activated protein kinase kinases (MAPKKs or MAP2Ks) (except for MAP2K5): cleavage invariably occurs within the N-terminal proline-rich region preceding the kinase domain, thus disrupting a sequence involved in directing specific protein-protein interactions necessary for the assembly of signaling complexes. Also cleaves mouse Nlrp1b: host Nlrp1b cleavage promotes ubiquitination and degradation of the N-terminal part of Nlrp1b by the proteasome, thereby releasing the cleaved C-terminal part of Nlrp1b, which polymerizes and forms the Nlrp1b inflammasome followed by host cell pyroptosis. Able to cleave mouse Nlrp1b alleles 1 and 5, while it is not able to cleave Nlrp1b alleles 2, 3 and 4. In contrast, does not cleave NLRP1 human ortholog. LF is not toxic by itself and only acts as a lethal factor when associated with protective antigen (PA) to form the lethal toxin (LeTx): PA is required for LF translocation into the host cytosol.",,Does not affect translocation into host cytoplasm.
72,72,63997,Q6UWV6-N100Q,MRGPAVLLTVALATLLAPGAGAPVQSQGSQNKLLLVSFDGFRWNYDQDVDTPNLDAMARDGVKARYMTPAFVTMTSPCHFTLVTGKYIENHGVVHNMYYQTTSKVKLPYHATLGIQRWWDNGSVPIWITAQRQGLRAGSFFYPGGNVTYQGVAVTRSRKEGIAHNYKNETEWRANIDTVMAWFTEEDLDLVTLYFGEPDSTGHRYGPESPERREMVRQVDRTVGYLRESIARNHLTDRLNLIITSDHGMTTVDKRAGDLVEFHKFPNFTFRDIEFELLDYGPNGMLLPKEGRLEKVYDALKDAHPKLHVYKKEAFPEAFHYANNPRVTPLLMYSDLGYVIHGRINVQFNNGEHGFDNKDMDMKTIFRAVGPSFRAGLEVEPFESVHVYELMCRLLGIVPEANDGHLATLLPMLHTESALPPDGRPTLLPKGRSALPPSSRPLLVMGLLGTVILLSEVA,Strongly reduces N-glycosylation and enzyme activity; when associated with Q-121; Q-146; Q-168 and Q-267.,,MRGPAVLLTVALATLLAPGAGAPVQSQGSQNKLLLVSFDGFRWNYDQDVDTPNLDAMARDGVKARYMTPAFVTMTSPCHFTLVTGKYIENHGVVHNMYYNTTSKVKLPYHATLGIQRWWDNGSVPIWITAQRQGLRAGSFFYPGGNVTYQGVAVTRSRKEGIAHNYKNETEWRANIDTVMAWFTEEDLDLVTLYFGEPDSTGHRYGPESPERREMVRQVDRTVGYLRESIARNHLTDRLNLIITSDHGMTTVDKRAGDLVEFHKFPNFTFRDIEFELLDYGPNGMLLPKEGRLEKVYDALKDAHPKLHVYKKEAFPEAFHYANNPRVTPLLMYSDLGYVIHGRINVQFNNGEHGFDNKDMDMKTIFRAVGPSFRAGLEVEPFESVHVYELMCRLLGIVPEANDGHLATLLPMLHTESALPPDGRPTLLPKGRSALPPSSRPLLVMGLLGTVILLSEVA,Ectonucleotide pyrophosphatase/phosphodiesterase family member 7,"Choline-specific phosphodiesterase that hydrolyzes sphingomyelin releasing the ceramide and phosphocholine and therefore is involved in sphingomyelin digestion, ceramide formation, and fatty acid (FA) absorption in the gastrointestinal tract. Has also phospholipase C activity and can also cleave phosphocholine from palmitoyl lyso-phosphatidylcholine and platelet-activating factor (PAF) leading to its inactivation. Does not have nucleotide pyrophosphatase activity. May promote cholesterol absorption by affecting the levels of sphingomyelin derived from either diet or endogenous sources, in the intestinal lumen.",The mutation in alk-SMase severely affects its activity.,Strongly reduces N-glycosylation and enzyme activity; when associated with Q-121; Q-146; Q-168 and Q-267. The mutation in alk-SMase severely affects its activity.
73,73,64823,P21926-C79A,MPVKGGTKCIKYLLFGFNFIFWLAGIAVLAIGLWLRFDSQTKSIFEQETNNNNSSFYTGVYILIGAGALMMLVGFLGCAGAVQESQCMLGLFFGFLLVIFAIEIAAAIWGYSHKDEVIKEVQEFYKDTYNKLKTKDEPQRETLKAIHYALNCCGLAGGVEQFISDICPKKDVLETFTVKSCPDAIKEVFDNKFHIIGAVGIGIAVVMIFGMIFSMILCCAIRRNREMV,Loss of palmitoylation; when associated with A-9; A-78; A-87; A-218 and A-219.,,MPVKGGTKCIKYLLFGFNFIFWLAGIAVLAIGLWLRFDSQTKSIFEQETNNNNSSFYTGVYILIGAGALMMLVGFLGCCGAVQESQCMLGLFFGFLLVIFAIEIAAAIWGYSHKDEVIKEVQEFYKDTYNKLKTKDEPQRETLKAIHYALNCCGLAGGVEQFISDICPKKDVLETFTVKSCPDAIKEVFDNKFHIIGAVGIGIAVVMIFGMIFSMILCCAIRRNREMV,CD9 antigen,"Integral membrane protein associated with integrins, which regulates different processes, such as sperm-egg fusion, platelet activation and aggregation, and cell adhesion. Present at the cell surface of oocytes and plays a key role in sperm-egg fusion, possibly by organizing multiprotein complexes and the morphology of the membrane required for the fusion. In myoblasts, associates with CD81 and PTGFRN and inhibits myotube fusion during muscle regeneration. In macrophages, associates with CD81 and beta-1 and beta-2 integrins, and prevents macrophage fusion into multinucleated giant cells specialized in ingesting complement-opsonized large particles. Also prevents the fusion between mononuclear cell progenitors into osteoclasts in charge of bone resorption. Acts as a receptor for PSG17. Involved in platelet activation and aggregation. Regulates paranodal junction formation. Involved in cell adhesion, cell motility and tumor metastasis.","The palmitoylation of CD9 did not influence the partition in detergent-resistant membranes but contributed to the interaction with CD81 and CD53. In particular, the resistance of the CD9/CD81 interaction to EDTA, which disrupts other tetraspanin/tetraspanin interactions, was entirely dependent on palmitoylation.","Loss of palmitoylation; when associated with A-9; A-78; A-87; A-218 and A-219. The palmitoylation of CD9 did not influence the partition in detergent-resistant membranes but contributed to the interaction with CD81 and CD53. In particular, the resistance of the CD9/CD81 interaction to EDTA, which disrupts other tetraspanin/tetraspanin interactions, was entirely dependent on palmitoylation."
74,74,66468,Q96MP8-D115Y,MVVVTGREPDSRRQDGAMSSSDAEDDFLEPATPTATQAGHALPLLPQEFPEVVPLNIGGAHFTTRLSTLRCYEDTMLAAMFSGRHYIPTDSEGRYFIDRDGTHFGDVLNFLRSGYLPPRERVRAVYKEAQYYAIGPLLEQLENMQPLKGEKVRQAFLGLMPYYKDHLERIVEIARLRAVQRKARFAKLKVCVFKEEMPITPYECPLLNSLRFERSESDGQLFEHHCEVDVSFGPWEAVADVYDLLHCLVTDLSAQGLTVDHQCIGVCDKHLVNHYYCKRPIYEFKITWW,In EPM3; uncertain pathological significance.,,MVVVTGREPDSRRQDGAMSSSDAEDDFLEPATPTATQAGHALPLLPQEFPEVVPLNIGGAHFTTRLSTLRCYEDTMLAAMFSGRHYIPTDSEGRYFIDRDGTHFGDVLNFLRSGDLPPRERVRAVYKEAQYYAIGPLLEQLENMQPLKGEKVRQAFLGLMPYYKDHLERIVEIARLRAVQRKARFAKLKVCVFKEEMPITPYECPLLNSLRFERSESDGQLFEHHCEVDVSFGPWEAVADVYDLLHCLVTDLSAQGLTVDHQCIGVCDKHLVNHYYCKRPIYEFKITWW,BTB/POZ domain-containing protein KCTD7,May be involved in the control of excitability of cortical neurons.,,In EPM3; uncertain pathological significance.
75,75,66634,P25522-D338N,MSDNDTIVAQATPPGRGGVGILRISGFKAREVAETVLGKLPKPRYADYLPFKDADGSVLDQGIALWFPGPNSFTGEDVLELQGHGGPVILDLLLKRILTIPGLRIARPGEFSERAFLNDKLDLAQAEAIADLIDASSEQAARSALNSLQGAFSARVNHLVEALTHLRIYVEAAIDFPDEEIDFLSDGKIEAQLNDVIADLDAVRAEARQGSLLREGMKVVIAGRPNAGKSSLLNALAGREAAIVTDIAGTTRDVLREHIHIDGMPLHIIDTAGLREASDEVERIGIERAWQEIEQADRVLFMVDGTTTDAVDPAEIWPEFIARLPAKLPITVVRNKANITGETLGMSEVNGHALIRLSARTGEGVDVLRNHLKQSMGFDTNMEGGFLARRRHLQALEQAAEHLQQGKAQLLGAWAGELLAEELRLAQQNLSEITGEFTSDDLLGRIFSSFCIGK,"Strong decrease in GTP binding. Does not affect hydrolase activity, but has 10-fold higher affinity for XTP than for GTP. Partially impairs tRNA modifying function.",,MSDNDTIVAQATPPGRGGVGILRISGFKAREVAETVLGKLPKPRYADYLPFKDADGSVLDQGIALWFPGPNSFTGEDVLELQGHGGPVILDLLLKRILTIPGLRIARPGEFSERAFLNDKLDLAQAEAIADLIDASSEQAARSALNSLQGAFSARVNHLVEALTHLRIYVEAAIDFPDEEIDFLSDGKIEAQLNDVIADLDAVRAEARQGSLLREGMKVVIAGRPNAGKSSLLNALAGREAAIVTDIAGTTRDVLREHIHIDGMPLHIIDTAGLREASDEVERIGIERAWQEIEQADRVLFMVDGTTTDAVDPAEIWPEFIARLPAKLPITVVRNKADITGETLGMSEVNGHALIRLSARTGEGVDVLRNHLKQSMGFDTNMEGGFLARRRHLQALEQAAEHLQQGKAQLLGAWAGELLAEELRLAQQNLSEITGEFTSDDLLGRIFSSFCIGK,tRNA modification GTPase MnmE,"Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.","The mutational analysis of the GTPase domain indicates that MnmE is closer to classical GTPases than to GTP-specific metabolic enzymes. Therefore, we propose that MnmE uses a conformational change associated with GTP hydrolysis to promote the tRNA modification reaction, in which the C-terminal C may function as a catalytic residue.","Strong decrease in GTP binding. Does not affect hydrolase activity, but has 10-fold higher affinity for XTP than for GTP. Partially impairs tRNA modifying function. The mutational analysis of the GTPase domain indicates that MnmE is closer to classical GTPases than to GTP-specific metabolic enzymes. Therefore, we propose that MnmE uses a conformational change associated with GTP hydrolysis to promote the tRNA modification reaction, in which the C-terminal C may function as a catalytic residue."
76,76,67585,P21926-C218A,MPVKGGTKCIKYLLFGFNFIFWLAGIAVLAIGLWLRFDSQTKSIFEQETNNNNSSFYTGVYILIGAGALMMLVGFLGCCGAVQESQCMLGLFFGFLLVIFAIEIAAAIWGYSHKDEVIKEVQEFYKDTYNKLKTKDEPQRETLKAIHYALNCCGLAGGVEQFISDICPKKDVLETFTVKSCPDAIKEVFDNKFHIIGAVGIGIAVVMIFGMIFSMILACAIRRNREMV,Loss of palmitoylation; when associated with A-9; A-78; A-79; A-87 and A-219.,,MPVKGGTKCIKYLLFGFNFIFWLAGIAVLAIGLWLRFDSQTKSIFEQETNNNNSSFYTGVYILIGAGALMMLVGFLGCCGAVQESQCMLGLFFGFLLVIFAIEIAAAIWGYSHKDEVIKEVQEFYKDTYNKLKTKDEPQRETLKAIHYALNCCGLAGGVEQFISDICPKKDVLETFTVKSCPDAIKEVFDNKFHIIGAVGIGIAVVMIFGMIFSMILCCAIRRNREMV,CD9 antigen,"Integral membrane protein associated with integrins, which regulates different processes, such as sperm-egg fusion, platelet activation and aggregation, and cell adhesion. Present at the cell surface of oocytes and plays a key role in sperm-egg fusion, possibly by organizing multiprotein complexes and the morphology of the membrane required for the fusion. In myoblasts, associates with CD81 and PTGFRN and inhibits myotube fusion during muscle regeneration. In macrophages, associates with CD81 and beta-1 and beta-2 integrins, and prevents macrophage fusion into multinucleated giant cells specialized in ingesting complement-opsonized large particles. Also prevents the fusion between mononuclear cell progenitors into osteoclasts in charge of bone resorption. Acts as a receptor for PSG17. Involved in platelet activation and aggregation. Regulates paranodal junction formation. Involved in cell adhesion, cell motility and tumor metastasis.",,Loss of palmitoylation; when associated with A-9; A-78; A-79; A-87 and A-219.
77,77,70622,P15917-H68Y,MNIKKEFIKVISMSCLVTAITLSGPVFIPLVQGAGGHGDVGMHVKEKEKNKDENKRKDEERNKTQEEYLKEIMKHIVKIEVKGEEAVKKEAAEKLLEKVPSDVLEMYKAIGGKIYIVDGDITKHISLEALSEDKKKIKDIYGKDALLHEHYVYAKEGYEPVLVIQSSEDYVENTEKALNVYYEIGKILSRDILSKINQPYQKFLDVLNTIKNASDSDGQDLLFTNQLKEHPTDFSVEFLEQNSNEVQEVFAKAFAYYIEPQHRDVLQLYAPEAFNYMDKFNEQEINLSLEELKDQRMLARYEKWEKIKQHYQHWSDSLSEEGRGLLKKLQIPIEPKKDDIIHSLSQEEKELLKRIQIDSSDFLSTEEKEFLKKLQIDIRDSLSEEEKELLNRIQVDSSNPLSEKEKEFLKKLKLDIQPYDINQRLQDTGGLIDSPSINLDVRKQYKRDIQNIDALLHQSIGSTLYNKIYLYENMNINNLTATLGADLVDSTDNTKINRGIFNEFKKNFKYSISSNYMIVDINERPALDNERLKWRIQLSPDTRAGYLENGKLILQRNIGLEIKDVQIIKQSEKEYIRIDAKVVPKSKIDTKIQEAQLNINQEWNKALGLPKYTKLITFNVHNRYASNIVESAYLILNEWKNNIQSDLIKKVTNYLVDGNGRFVFTDITLPNIAEQYTHQDEIYEQVHSKGLYVPESRSILLHGPSKGVELRNDSEGFIHEFGHAVDDYAGYLLDKNQSDLVTNSKKFIDIFKEEGSNLTSYGRTNEAEFFAEAFRLMHSTDHAERLKVQKNAPKTFQFINDQIKFIINS,Impaired translocation into host cytoplasm.,,MNIKKEFIKVISMSCLVTAITLSGPVFIPLVQGAGGHGDVGMHVKEKEKNKDENKRKDEERNKTQEEHLKEIMKHIVKIEVKGEEAVKKEAAEKLLEKVPSDVLEMYKAIGGKIYIVDGDITKHISLEALSEDKKKIKDIYGKDALLHEHYVYAKEGYEPVLVIQSSEDYVENTEKALNVYYEIGKILSRDILSKINQPYQKFLDVLNTIKNASDSDGQDLLFTNQLKEHPTDFSVEFLEQNSNEVQEVFAKAFAYYIEPQHRDVLQLYAPEAFNYMDKFNEQEINLSLEELKDQRMLARYEKWEKIKQHYQHWSDSLSEEGRGLLKKLQIPIEPKKDDIIHSLSQEEKELLKRIQIDSSDFLSTEEKEFLKKLQIDIRDSLSEEEKELLNRIQVDSSNPLSEKEKEFLKKLKLDIQPYDINQRLQDTGGLIDSPSINLDVRKQYKRDIQNIDALLHQSIGSTLYNKIYLYENMNINNLTATLGADLVDSTDNTKINRGIFNEFKKNFKYSISSNYMIVDINERPALDNERLKWRIQLSPDTRAGYLENGKLILQRNIGLEIKDVQIIKQSEKEYIRIDAKVVPKSKIDTKIQEAQLNINQEWNKALGLPKYTKLITFNVHNRYASNIVESAYLILNEWKNNIQSDLIKKVTNYLVDGNGRFVFTDITLPNIAEQYTHQDEIYEQVHSKGLYVPESRSILLHGPSKGVELRNDSEGFIHEFGHAVDDYAGYLLDKNQSDLVTNSKKFIDIFKEEGSNLTSYGRTNEAEFFAEAFRLMHSTDHAERLKVQKNAPKTFQFINDQIKFIINS,Lethal factor,"Lethal factor (LF), which constitutes one of the three proteins composing the anthrax toxin, is able to trigger rapid cell death in macrophages. Acts as a protease that cleaves the N-terminal of most dual specificity mitogen-activated protein kinase kinases (MAPKKs or MAP2Ks) (except for MAP2K5): cleavage invariably occurs within the N-terminal proline-rich region preceding the kinase domain, thus disrupting a sequence involved in directing specific protein-protein interactions necessary for the assembly of signaling complexes. Also cleaves mouse Nlrp1b: host Nlrp1b cleavage promotes ubiquitination and degradation of the N-terminal part of Nlrp1b by the proteasome, thereby releasing the cleaved C-terminal part of Nlrp1b, which polymerizes and forms the Nlrp1b inflammasome followed by host cell pyroptosis. Able to cleave mouse Nlrp1b alleles 1 and 5, while it is not able to cleave Nlrp1b alleles 2, 3 and 4. In contrast, does not cleave NLRP1 human ortholog. LF is not toxic by itself and only acts as a lethal factor when associated with protective antigen (PA) to form the lethal toxin (LeTx): PA is required for LF translocation into the host cytosol.",,Impaired translocation into host cytoplasm.
78,78,71120,P51843-Y380D,MAGENHQWQGSILYNMLMSAKQTRAAPEAPETRLVDQCWGCSCGDEPGVGREGLLGGRNVALLYRCCFCGKDHPRQGSILYSMLTSAKQTYAAPKAPEATLGPCWGCSCGSDPGVGRAGLPGGRPVALLYRCCFCGEDHPRQGSILYSLLTSSKQTHVAPAAPEARPGGAWWDRSYFAQRPGGKEALPGGRATALLYRCCFCGEDHPQQGSTLYCVPTSTNQAQAAPEERPRAPWWDTSSGALRPVALKSPQVVCEAASAGLLKTLRFVKYLPCFQVLPLDQQLVLVRNCWASLLMLELAQDRLQFETVEVSEPSMLQKILTTRRRETGGNEPLPVPTLQHHLAPPAEARKVPSASQVQAIKCFLSKCWSLNISTKEYADLKGTVLFNPDVPGLQCVKYIQGLQWGTQQILSEHTRMTHQGPHDRFIELNSTLFLLRFINANVIAELFFRPIIGTVSMDDMMLEMLCTKI,In AHC.,,MAGENHQWQGSILYNMLMSAKQTRAAPEAPETRLVDQCWGCSCGDEPGVGREGLLGGRNVALLYRCCFCGKDHPRQGSILYSMLTSAKQTYAAPKAPEATLGPCWGCSCGSDPGVGRAGLPGGRPVALLYRCCFCGEDHPRQGSILYSLLTSSKQTHVAPAAPEARPGGAWWDRSYFAQRPGGKEALPGGRATALLYRCCFCGEDHPQQGSTLYCVPTSTNQAQAAPEERPRAPWWDTSSGALRPVALKSPQVVCEAASAGLLKTLRFVKYLPCFQVLPLDQQLVLVRNCWASLLMLELAQDRLQFETVEVSEPSMLQKILTTRRRETGGNEPLPVPTLQHHLAPPAEARKVPSASQVQAIKCFLSKCWSLNISTKEYAYLKGTVLFNPDVPGLQCVKYIQGLQWGTQQILSEHTRMTHQGPHDRFIELNSTLFLLRFINANVIAELFFRPIIGTVSMDDMMLEMLCTKI,Nuclear receptor subfamily 0 group B member 1,Orphan nuclear receptor. Component of a cascade required for the development of the hypothalamic-pituitary-adrenal-gonadal axis. Acts as a coregulatory protein that inhibits the transcriptional activity of other nuclear receptors through heterodimeric interactions. May also have a role in the development of the embryo and in the maintenance of embryonic stem cell pluripotency.,"A novel DAX-1 missense mutation, which causes partial loss of function in transient gene expression assays, was found in this patient. This case demonstrates that partial loss-of-function mutations in DAX1 can present with hypogonadotropic hypogonadism and covert adrenal failure in adulthood. Further, an important role for DAX-1 in spermatogenesis in humans is confirmed, supporting findings in the Dax1 (Ahch) knockout mouse.","In AHC. A novel DAX-1 missense mutation, which causes partial loss of function in transient gene expression assays, was found in this patient. This case demonstrates that partial loss-of-function mutations in DAX1 can present with hypogonadotropic hypogonadism and covert adrenal failure in adulthood. Further, an important role for DAX-1 in spermatogenesis in humans is confirmed, supporting findings in the Dax1 (Ahch) knockout mouse."
79,79,71237,Q96AX1-K429D,MAAHLSYGRVNLNVLREAVRRELREFLDKCAGSKAIVWDEYLTGPFGLIAQYSLLKEHEVEKMFTLKGNRLPAADVKNIIFFVRPRLELMDIIAENVLSEDRRGPTRDFHILFVPRRSLLCEQRLKDLGVLGSFIHREEYSLDLIPFDGDLLSMESEGAFKECYLEGDQTSLYHAAKGLMTLQALYGTIPQIFGKGECARQVANMMIRMKREFTGSQNSIFPVFDNLLLLDRNVDLLTPLATQLTYEGLIDEIYGIQNSYVKLPPEKFAPKKQGDGGKDLPTEAKKLQLNSAEELYAEIRDKNFNAVGSVLSKKAKIISAAFEERHNAKTVGEIKQFVSQLPHMQAARGSLANHTSIAELIKDVTTSEDFFDKLTVEQEFMSGIDTDKVNNYIEDCIAQKHSLIKVLRLVCLQSVCNSGLKQKVLDYYDREILQTYGYEHILTLHNLEKAGLLKPQTGGRNNYPTIRKTLRLWMDDVNEQNPTDISYVYSGYAPLSVRLAQLLSRPGWRSIEEVLRILPGPHFEERQPLPTGLQKKRQPGENRVTLIFFLGGVTFAEIAALRFLSQLEDGGTEYVIATTKLMNGTSWIEALMEKPF,Disrupts interaction with VPS16. Disrupts interaction with VPS18 and impairs endosome-lysosome fusion; when associated with K-438. Disrupts interaction with VPS18 and impairs endosome-lysosome fusion; when associated with K-441.,,MAAHLSYGRVNLNVLREAVRRELREFLDKCAGSKAIVWDEYLTGPFGLIAQYSLLKEHEVEKMFTLKGNRLPAADVKNIIFFVRPRLELMDIIAENVLSEDRRGPTRDFHILFVPRRSLLCEQRLKDLGVLGSFIHREEYSLDLIPFDGDLLSMESEGAFKECYLEGDQTSLYHAAKGLMTLQALYGTIPQIFGKGECARQVANMMIRMKREFTGSQNSIFPVFDNLLLLDRNVDLLTPLATQLTYEGLIDEIYGIQNSYVKLPPEKFAPKKQGDGGKDLPTEAKKLQLNSAEELYAEIRDKNFNAVGSVLSKKAKIISAAFEERHNAKTVGEIKQFVSQLPHMQAARGSLANHTSIAELIKDVTTSEDFFDKLTVEQEFMSGIDTDKVNNYIEDCIAQKHSLIKVLRLVCLQSVCNSGLKQKVLDYYKREILQTYGYEHILTLHNLEKAGLLKPQTGGRNNYPTIRKTLRLWMDDVNEQNPTDISYVYSGYAPLSVRLAQLLSRPGWRSIEEVLRILPGPHFEERQPLPTGLQKKRQPGENRVTLIFFLGGVTFAEIAALRFLSQLEDGGTEYVIATTKLMNGTSWIEALMEKPF,Vacuolar protein sorting-associated protein 33A,"Plays a role in vesicle-mediated protein trafficking to lysosomal compartments including the endocytic membrane transport and autophagic pathways. Believed to act as a core component of the putative HOPS and CORVET endosomal tethering complexes which are proposed to be involved in the Rab5-to-Rab7 endosome conversion probably implicating MON1A/B, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion. The HOPS complex is proposed to be recruited to Rab7 on the late endosomal membrane and to regulate late endocytic, phagocytic and autophagic traffic towards lysosomes. The CORVET complex is proposed to function as a Rab5 effector to mediate early endosome fusion probably in specific endosome subpopulations. Required for fusion of endosomes and autophagosomes with lysosomes; the function is dependent on its association with VPS16 but not VIPAS39. The function in autophagosome-lysosome fusion implicates STX17 but not UVRAG.",,Disrupts interaction with VPS16. Disrupts interaction with VPS18 and impairs endosome-lysosome fusion; when associated with K-438. Disrupts interaction with VPS18 and impairs endosome-lysosome fusion; when associated with K-441.
80,80,71904,P08692-C106V,MSNITIYHNPACGTSRNTLEMIRNSGTEPTIILYLENPPSRDELVKLIADMGISVRALLRKNVEPYEQLGLAEDKFTDDQLIDFMLQHPILINRPIVVTPLGTRLVRPSEVVLDILQDAQKGAFTKEDGEKVVDEAGKRLK,Mutant retains arsenate resistance.,,MSNITIYHNPACGTSRNTLEMIRNSGTEPTIILYLENPPSRDELVKLIADMGISVRALLRKNVEPYEQLGLAEDKFTDDQLIDFMLQHPILINRPIVVTPLGTRLCRPSEVVLDILQDAQKGAFTKEDGEKVVDEAGKRLK,Arsenate reductase,Involved in resistance to arsenate. Catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)]. The resulting arsenite is then extruded from the cell via the ArsAB transport system (Probable).,"Cells expressing the arsCC106V gene retained arsenate resistance, and the purified protein had reductase activity.","Mutant retains arsenate resistance. Cells expressing the arsCC106V gene retained arsenate resistance, and the purified protein had reductase activity."
81,81,72063,D5ARH0-K41N,MQAIDIGHVTLERDGTGVFSDLTLRLTERRIGIVGRNGAGNSSLIRLITGLVTPQKGRVVVNGVDVAADRAGALGTVGLLFQNPDHQIIFPVVRDEIAFGLEQKGLKRAAALARAEAVLAAQGRADWGDRLCHTLSQGQRQLLCLMSILAMEPDWILFDEPFNALDLPTALSIEARIAGLAQNVVLVTHDPSRLTGFDRILWLEGGRIEADGPPAEVLPRYIAAMQALARAGAC,"Diminished biotin uptake, loss of ATPase activity, BioMNY complexes still form.",,MQAIDIGHVTLERDGTGVFSDLTLRLTERRIGIVGRNGAGKSSLIRLITGLVTPQKGRVVVNGVDVAADRAGALGTVGLLFQNPDHQIIFPVVRDEIAFGLEQKGLKRAAALARAEAVLAAQGRADWGDRLCHTLSQGQRQLLCLMSILAMEPDWILFDEPFNALDLPTALSIEARIAGLAQNVVLVTHDPSRLTGFDRILWLEGGRIEADGPPAEVLPRYIAAMQALARAGAC,Biotin transport ATP-binding protein BioM,Required for biotin uptake under very low (pM) biotin concentrations but not under higher (nM) concentrations.,"The mutation in the BioM protein severely impairs the BioMNY-mediated biotin uptake, demonstrating the dependency of high-affinity transport on a functional ATPase.","Diminished biotin uptake, loss of ATPase activity, BioMNY complexes still form. The mutation in the BioM protein severely impairs the BioMNY-mediated biotin uptake, demonstrating the dependency of high-affinity transport on a functional ATPase."
82,82,73273,Q6MZP7-Y536R,MEVVPAEVNSLLPEEIMDTGITLVDDDSIEAVIVSSPIPMETELEEIVNINSTGDSTATPISTEPITVYSNHTNQVAVNTTITKADSNTTVKPAFPSGLQKLGAQTPVTISANQIILNKVSQTSDLKLGNQTLKPDGQKLILTTLGKSGSPIVLALPHSQLPQAQKVTTQAQSGDAKLPPQQIKVVTIGGRPEVKPVIGVSALTPGSQLINTTTQPSVLQTQQLKTVQIAKKPRTPTSGPVITKLIFAKPINSKAVTGQTTQVSPPVIAGRVLSQSTPGTPSKTITISESGVIGSTLNSTTQTPNKIAISPLKSPNKAVKSTVQTITVGGVSTSQFKTIIPLATAPNVQQIQVPGSKFHYVRLVTATSASSSTQPVSQNPSTNTQPLQQAKPVVVNTTPVRMSVPIVSAQAVKQVVPKPINPTSQIVTTSQPQQRLIMPATPLPQIQPNLTNLPPGTVLAPAPGTGNVGYAVLPAQYVTQLQQSSYVSIASNSTFTGTSGIQTQARLPFNGIIPSESASRPRKPCNCTKSLCLKLRCDCFANGEFCNNCNCTNCYNNLEHENERQKAIKACLDRNPEAFKPKIGKGKEGESDRRHSKGCNCKRSGCLKNYCECYEAKIMCSSICKCIGCKNFEESPERKTLMHLADAAEVRVQQQTAAKTKLSSQISDLLTRPTPALNSGGGKLPFTFVTKEVAEATCNCLLAQAEQADKKGKSKAAAERMILEEFGRCLMSVINSAGKAKSDPCAMNC,Loss of DNA-binding.,,MEVVPAEVNSLLPEEIMDTGITLVDDDSIEAVIVSSPIPMETELEEIVNINSTGDSTATPISTEPITVYSNHTNQVAVNTTITKADSNTTVKPAFPSGLQKLGAQTPVTISANQIILNKVSQTSDLKLGNQTLKPDGQKLILTTLGKSGSPIVLALPHSQLPQAQKVTTQAQSGDAKLPPQQIKVVTIGGRPEVKPVIGVSALTPGSQLINTTTQPSVLQTQQLKTVQIAKKPRTPTSGPVITKLIFAKPINSKAVTGQTTQVSPPVIAGRVLSQSTPGTPSKTITISESGVIGSTLNSTTQTPNKIAISPLKSPNKAVKSTVQTITVGGVSTSQFKTIIPLATAPNVQQIQVPGSKFHYVRLVTATSASSSTQPVSQNPSTNTQPLQQAKPVVVNTTPVRMSVPIVSAQAVKQVVPKPINPTSQIVTTSQPQQRLIMPATPLPQIQPNLTNLPPGTVLAPAPGTGNVGYAVLPAQYVTQLQQSSYVSIASNSTFTGTSGIQTQARLPFNGIIPSESASRPRKPCNCTKSLCLKLYCDCFANGEFCNNCNCTNCYNNLEHENERQKAIKACLDRNPEAFKPKIGKGKEGESDRRHSKGCNCKRSGCLKNYCECYEAKIMCSSICKCIGCKNFEESPERKTLMHLADAAEVRVQQQTAAKTKLSSQISDLLTRPTPALNSGGGKLPFTFVTKEVAEATCNCLLAQAEQADKKGKSKAAAERMILEEFGRCLMSVINSAGKAKSDPCAMNC,Protein lin-54 homolog,"Component of the DREAM complex, a multiprotein complex that can both act as a transcription activator or repressor depending on the context. In G0 phase, the complex binds to more than 800 promoters and is required for repression of E2F target genes. In S phase, the complex selectively binds to the promoters of G2/M genes whose products are required for mitosis and participates in their cell cycle dependent activation. In the complex, acts as a DNA-binding protein that binds the promoter of CDK1 in a sequence-specific manner. Specifically recognizes the consensus motif 5'-TTYRAA-3' in target DNA.",This mutation affects the DNA-binding properties of LIN54 and may alter its ability to recognize the CHR sequence. It is unclear how this mutation specifically impacts MuvB recruitment to target promoters or the positioning of downstream nucleosomes.,Loss of DNA-binding. This mutation affects the DNA-binding properties of LIN54 and may alter its ability to recognize the CHR sequence. It is unclear how this mutation specifically impacts MuvB recruitment to target promoters or the positioning of downstream nucleosomes.
83,83,73583,H2KZZ6-S490P,MEDFKDFTEVTQFTNVQYLGCSQLVNNDNDNEMKALMKVLDEQKGAQTINVTLVVPHNISGTVKLIDAQGKVLSSFSLVNIRFCIRGESSTSQNNCFGISFTHKISVGEHNSSDILHQCHVFRTSKAETAAKALYSFSYAFSNKNVSSESNRLEFQFESILEVKENDGTVEKPSWKLCPQHNGVFKVRRDREKKIVVQLRQIDGFLLNIKKCFGMLLAAGRNLRHSDLQLLEMDRNATGTDSAVFVIEANWDPRVHMFEVLNTETPRDTRVFMTVAIDVIVSEISEPIRFSMEAMSRVFHEHERFYKTPQTVVSEEFTLVLEKSCDQSDPNDRKLTFISLESDSDRKRSKQNLGKSPSRMPTQLLHPTGDDESDCDEPLLSGSGKVSQECKEEHLEMWDQLIENWDQQSDRPQKISELVLDGIPDKLRGRVWQLLSNVRILAIDQPDLVEKYHIFLSQPCPSEQVIMRDIHRTFPAHDYFKESQGKGQQPLYKISKVYSLYDEEVSYCQGLSFLAASLLLHMPEEQAFCTLVKIMFNYGLRDLFKLGFDNLHLRFFQLTALLKDYIPDLSHHLEHIGIETHMYASQWFLTLFTAKFPLQMVFFILDLFLSQGMNTIFHISLALLDDAKTDLLQLDFEGTLKYFRVSLPRKYRTEASTKCLIHKAVKFRLNHSKLEVYENEYKRIKELERENEDPVLRMEKEIGRHQANTLRLERENDDLAHELVTSKIELRRKLDVAEDQIETSANAIERLTRQNMDILEENKNLMREYEQIKEMYRRDVLRLEENGSRAEKLLAEYKKLFSERSKRAENEREHFEVQKKAIIARISDCDKCWPAVCEWEKNRSPVHSASTPTGPDLLTKLEEREDHIKNLEIDLAQTKLSLVEAECRNQDLTHQLMAQSESDGKKWFKKTITQLKEVGSSLKHHERSNSSVTP,"In qbc24; males are sterile. Disrupts seam cell division and alae formation. Disrupts the localization of alg-1 to endomembranes, and instead alg-1 accumulates in the perinuclear region. Reduces the total number of microRNAs and reduces microRNA-mediated gene silencing. Specifically reduces the association of alg-1 with microRNAs. Increases the expression of lin-41 protein, which is a target for the let-7 microRNA. The seam cell division and alae formation defects are suppressed in a rab-6.1 or rab-6.2 RNAi mutant background. The localization of alg-1 is restored in a rab-6.1 RNAi mutant background.",,MEDFKDFTEVTQFTNVQYLGCSQLVNNDNDNEMKALMKVLDEQKGAQTINVTLVVPHNISGTVKLIDAQGKVLSSFSLVNIRFCIRGESSTSQNNCFGISFTHKISVGEHNSSDILHQCHVFRTSKAETAAKALYSFSYAFSNKNVSSESNRLEFQFESILEVKENDGTVEKPSWKLCPQHNGVFKVRRDREKKIVVQLRQIDGFLLNIKKCFGMLLAAGRNLRHSDLQLLEMDRNATGTDSAVFVIEANWDPRVHMFEVLNTETPRDTRVFMTVAIDVIVSEISEPIRFSMEAMSRVFHEHERFYKTPQTVVSEEFTLVLEKSCDQSDPNDRKLTFISLESDSDRKRSKQNLGKSPSRMPTQLLHPTGDDESDCDEPLLSGSGKVSQECKEEHLEMWDQLIENWDQQSDRPQKISELVLDGIPDKLRGRVWQLLSNVRILAIDQPDLVEKYHIFLSQPCPSEQVIMRDIHRTFPAHDYFKESQGKGQQSLYKISKVYSLYDEEVSYCQGLSFLAASLLLHMPEEQAFCTLVKIMFNYGLRDLFKLGFDNLHLRFFQLTALLKDYIPDLSHHLEHIGIETHMYASQWFLTLFTAKFPLQMVFFILDLFLSQGMNTIFHISLALLDDAKTDLLQLDFEGTLKYFRVSLPRKYRTEASTKCLIHKAVKFRLNHSKLEVYENEYKRIKELERENEDPVLRMEKEIGRHQANTLRLERENDDLAHELVTSKIELRRKLDVAEDQIETSANAIERLTRQNMDILEENKNLMREYEQIKEMYRRDVLRLEENGSRAEKLLAEYKKLFSERSKRAENEREHFEVQKKAIIARISDCDKCWPAVCEWEKNRSPVHSASTPTGPDLLTKLEEREDHIKNLEIDLAQTKLSLVEAECRNQDLTHQLMAQSESDGKKWFKKTITQLKEVGSSLKHHERSNSSVTP,Rab GTPase-activating protein tbc-11,Rab GTPase activating protein for the small GTPases rab-6.1 and rab-6.2 (Probable). Probably acts through rab-6.1 and rab-6.2 to play a role in microRNA-mediated gene silencing in different tissue types. Required for seam cell division and alae formation.,"The alteration of TBC-11 generates a fraction of ALG-1 that cannot bind to target mRNAs, leading to defective gene repression.","In qbc24; males are sterile. Disrupts seam cell division and alae formation. Disrupts the localization of alg-1 to endomembranes, and instead alg-1 accumulates in the perinuclear region. Reduces the total number of microRNAs and reduces microRNA-mediated gene silencing. Specifically reduces the association of alg-1 with microRNAs. Increases the expression of lin-41 protein, which is a target for the let-7 microRNA. The seam cell division and alae formation defects are suppressed in a rab-6.1 or rab-6.2 RNAi mutant background. The localization of alg-1 is restored in a rab-6.1 RNAi mutant background. The alteration of TBC-11 generates a fraction of ALG-1 that cannot bind to target mRNAs, leading to defective gene repression."
84,84,74151,Q969S9-R190Q,MLTNLRIFAMSHQTIPSVYINNICCYKIRASLKRLKPHVPLGRNCSSLPGLIGNDIKSLHSIINPPIAKIRNIGIMAHIDAGKTTTTERILYYSGYTRSLGDVDDGDTVTDFMAQERERGITIQSAAVTFDWKGYRVNLIDTPGHVDFTLEVERCLRVLDGAVAVFDASAGVEAQTLTVWRQADKHNIPQICFLNKMDKTGASFKYAVESIREKLKAKPLLLQLPIGEAKTFKGVVDVVMKEKLLWNCNSNDGKDFERKPLLEMNDPELLKETTEARNALIEQVADLDDEFADLVLEEFSENFDLLPAEKLQTAIHRVTLAQTAVPVLCGSALKNKGIQPLLDAVTMYLPSPEERNYEFLQWYKDDLCALAFKVLHDKQRGPLVFMRIYSGTIKPQLAIHNINGNCTERISRLLLPFADQHVEIPSLTAGNIALTVGLKHTATGDTIVSSKSSALAAARRAEREGEKKHRQNNEAERLLLAGVEIPEPVFFCTIEPPSLSKQPDLEHALKCLQREDPSLKVRLDPDSGQTVLCGMGELHIEIIHDRIKREYGLETYLGPLQVAYRETILNSVRATDTLDRTLGDKRHLVTVEVEARPIETSSVMPVIEFEYAESINEGLLKVSQEAIENGIHSACLQGPLLGSPIQDVAITLHSLTIHPGTSTTMISACVSRCVQKALKKADKQVLEPLMNLEVTVARDYLSPVLADLAQRRGNIQEIQTRQDNKVVIGFVPLAEIMGYSTVLRTLTSGSATFALELSTYQAMNPQDQNTLLNRRSGLT,In COXPD39.,,MLTNLRIFAMSHQTIPSVYINNICCYKIRASLKRLKPHVPLGRNCSSLPGLIGNDIKSLHSIINPPIAKIRNIGIMAHIDAGKTTTTERILYYSGYTRSLGDVDDGDTVTDFMAQERERGITIQSAAVTFDWKGYRVNLIDTPGHVDFTLEVERCLRVLDGAVAVFDASAGVEAQTLTVWRQADKHNIPRICFLNKMDKTGASFKYAVESIREKLKAKPLLLQLPIGEAKTFKGVVDVVMKEKLLWNCNSNDGKDFERKPLLEMNDPELLKETTEARNALIEQVADLDDEFADLVLEEFSENFDLLPAEKLQTAIHRVTLAQTAVPVLCGSALKNKGIQPLLDAVTMYLPSPEERNYEFLQWYKDDLCALAFKVLHDKQRGPLVFMRIYSGTIKPQLAIHNINGNCTERISRLLLPFADQHVEIPSLTAGNIALTVGLKHTATGDTIVSSKSSALAAARRAEREGEKKHRQNNEAERLLLAGVEIPEPVFFCTIEPPSLSKQPDLEHALKCLQREDPSLKVRLDPDSGQTVLCGMGELHIEIIHDRIKREYGLETYLGPLQVAYRETILNSVRATDTLDRTLGDKRHLVTVEVEARPIETSSVMPVIEFEYAESINEGLLKVSQEAIENGIHSACLQGPLLGSPIQDVAITLHSLTIHPGTSTTMISACVSRCVQKALKKADKQVLEPLMNLEVTVARDYLSPVLADLAQRRGNIQEIQTRQDNKVVIGFVPLAEIMGYSTVLRTLTSGSATFALELSTYQAMNPQDQNTLLNRRSGLT,"Ribosome-releasing factor 2, mitochondrial",Mitochondrial GTPase that mediates the disassembly of ribosomes from messenger RNA at the termination of mitochondrial protein biosynthesis. Acts in collaboration with MRRF. GTP hydrolysis follows the ribosome disassembly and probably occurs on the ribosome large subunit. Not involved in the GTP-dependent ribosomal translocation step during translation elongation.,"The variant c. 569G>A results in the amino acid change p. () in the mtEFG2 protein. This variant causes defective mtEFG2 function, leading to clinical symptoms such as global developmental delay and abnormalities on cranial MRI.","In COXPD39. The variant c. 569G>A results in the amino acid change p. () in the mtEFG2 protein. This variant causes defective mtEFG2 function, leading to clinical symptoms such as global developmental delay and abnormalities on cranial MRI."
85,85,74708,Q9AQS0-Y255F,MLSGILIAALLMTLWGGWQPDIAHASDEFDALRIKWATLLTGGPALDPADSDIAARTDKLAQDANDYWEDMDLSSSRTYIWYALRGNGTSDNVNAVYERLRTMALAATTVGSSLYGNADLKEDILDALDWLYVNSYNSTRSRSAYNWWHWQLGIPMSLNDIAVLLYDDISAARMATYMDTIDYFTPSIGLTGANRAWQAIVVGVRAVIVKDAVKLAAARNGLSGTGIFPYATGGDGFYADGSFVQHTTFAYTGGFGSSVLETTANLMYLLSGSTWSVSDPNQSNVWQWIYEAYRPLLYKGAMMDMVRGREISRSYAQDHAVGHGIVASIVRLAQFAPAPHAAAFKQIAKRVIQEDTFSSFYGDVSTDTIRLAKAIVDDPSIAPAAAPNLYKQYAAMDRAVLQRPGFALGLALYSTRISSYESINSENGRGWYTGAGATYLYNQDLAQYSEDYWPTVDAYRIPGTTVASGTPIASGTGTSSWTGGVSLAGQYGASGMDLSYGAYNLSARKSWFMFDDEIVALGSGISSTAGIPIETVVDNRKLNGAGDNAWTANGAALSTGLGVAQTLTGVNWVHLAGNTADGSDIGYYFPGGATLQTKREARTGTWKQINNRPATPSTAVTRNYETMWIDHGTNPSGASYGYVLLPNKTSAQVGAYAADPAIEIVVNTSGVQSVKEKTLGLVGANFWTDTTQTADLITSNKKASVMTREIADERLEASVSDPTQANNGTIAIELARSAEGYSADPGITVTQLAPTIKFTVNVNGAKGKSFHASFQLGEDTSGPVDPGEPELPSVIVDNADSAGVTRTGTWKTASTQTDRYGANYLHDDNAGKGTKSVTFTPNLPIAGSYEVYLMWPAHFNREDAVQVDVGHASGTTRTAVDQRSGGGVWHSIGTYEFLAGSGGSVTIRNDALGSPDGYVVADAVKFVAVG,Loss of activity by 50%.,,MLSGILIAALLMTLWGGWQPDIAHASDEFDALRIKWATLLTGGPALDPADSDIAARTDKLAQDANDYWEDMDLSSSRTYIWYALRGNGTSDNVNAVYERLRTMALAATTVGSSLYGNADLKEDILDALDWLYVNSYNSTRSRSAYNWWHWQLGIPMSLNDIAVLLYDDISAARMATYMDTIDYFTPSIGLTGANRAWQAIVVGVRAVIVKDAVKLAAARNGLSGTGIFPYATGGDGFYADGSFVQHTTFAYTGGYGSSVLETTANLMYLLSGSTWSVSDPNQSNVWQWIYEAYRPLLYKGAMMDMVRGREISRSYAQDHAVGHGIVASIVRLAQFAPAPHAAAFKQIAKRVIQEDTFSSFYGDVSTDTIRLAKAIVDDPSIAPAAAPNLYKQYAAMDRAVLQRPGFALGLALYSTRISSYESINSENGRGWYTGAGATYLYNQDLAQYSEDYWPTVDAYRIPGTTVASGTPIASGTGTSSWTGGVSLAGQYGASGMDLSYGAYNLSARKSWFMFDDEIVALGSGISSTAGIPIETVVDNRKLNGAGDNAWTANGAALSTGLGVAQTLTGVNWVHLAGNTADGSDIGYYFPGGATLQTKREARTGTWKQINNRPATPSTAVTRNYETMWIDHGTNPSGASYGYVLLPNKTSAQVGAYAADPAIEIVVNTSGVQSVKEKTLGLVGANFWTDTTQTADLITSNKKASVMTREIADERLEASVSDPTQANNGTIAIELARSAEGYSADPGITVTQLAPTIKFTVNVNGAKGKSFHASFQLGEDTSGPVDPGEPELPSVIVDNADSAGVTRTGTWKTASTQTDRYGANYLHDDNAGKGTKSVTFTPNLPIAGSYEVYLMWPAHFNREDAVQVDVGHASGTTRTAVDQRSGGGVWHSIGTYEFLAGSGGSVTIRNDALGSPDGYVVADAVKFVAVG,Xanthan lyase,"Plays a role in xanthan depolymerization pathway by cleaving the linkage between the terminal mannosyl and glucuronyl residues of the side chain of xanthan to liberate pyruvylated mannose. Is highly specific for pyruvylated side-chains of xanthan and is not effective with hyaluronate, chondroitin A, gellan, heparin or pectin.","The structure of the mutant-substrate complex showed that the hydroxyl group of Y255 was close to both the C-5 atom of the GlcUA residue and the oxygen atom of the glycosidic bond to be cleaved, suggesting that Y255 likely acts as a general base that extracts the proton from C-5 of the GlcUA residue and as a general acid that donates the proton to the glycosidic bond.","Loss of activity by 50%. The structure of the mutant-substrate complex showed that the hydroxyl group of Y255 was close to both the C-5 atom of the GlcUA residue and the oxygen atom of the glycosidic bond to be cleaved, suggesting that Y255 likely acts as a general base that extracts the proton from C-5 of the GlcUA residue and as a general acid that donates the proton to the glycosidic bond."
86,86,75666,P51843-W291C,MAGENHQWQGSILYNMLMSAKQTRAAPEAPETRLVDQCWGCSCGDEPGVGREGLLGGRNVALLYRCCFCGKDHPRQGSILYSMLTSAKQTYAAPKAPEATLGPCWGCSCGSDPGVGRAGLPGGRPVALLYRCCFCGEDHPRQGSILYSLLTSSKQTHVAPAAPEARPGGAWWDRSYFAQRPGGKEALPGGRATALLYRCCFCGEDHPQQGSTLYCVPTSTNQAQAAPEERPRAPWWDTSSGALRPVALKSPQVVCEAASAGLLKTLRFVKYLPCFQVLPLDQQLVLVRNCCASLLMLELAQDRLQFETVEVSEPSMLQKILTTRRRETGGNEPLPVPTLQHHLAPPAEARKVPSASQVQAIKCFLSKCWSLNISTKEYAYLKGTVLFNPDVPGLQCVKYIQGLQWGTQQILSEHTRMTHQGPHDRFIELNSTLFLLRFINANVIAELFFRPIIGTVSMDDMMLEMLCTKI,In AHC.,,MAGENHQWQGSILYNMLMSAKQTRAAPEAPETRLVDQCWGCSCGDEPGVGREGLLGGRNVALLYRCCFCGKDHPRQGSILYSMLTSAKQTYAAPKAPEATLGPCWGCSCGSDPGVGRAGLPGGRPVALLYRCCFCGEDHPRQGSILYSLLTSSKQTHVAPAAPEARPGGAWWDRSYFAQRPGGKEALPGGRATALLYRCCFCGEDHPQQGSTLYCVPTSTNQAQAAPEERPRAPWWDTSSGALRPVALKSPQVVCEAASAGLLKTLRFVKYLPCFQVLPLDQQLVLVRNCWASLLMLELAQDRLQFETVEVSEPSMLQKILTTRRRETGGNEPLPVPTLQHHLAPPAEARKVPSASQVQAIKCFLSKCWSLNISTKEYAYLKGTVLFNPDVPGLQCVKYIQGLQWGTQQILSEHTRMTHQGPHDRFIELNSTLFLLRFINANVIAELFFRPIIGTVSMDDMMLEMLCTKI,Nuclear receptor subfamily 0 group B member 1,Orphan nuclear receptor. Component of a cascade required for the development of the hypothalamic-pituitary-adrenal-gonadal axis. Acts as a coregulatory protein that inhibits the transcriptional activity of other nuclear receptors through heterodimeric interactions. May also have a role in the development of the embryo and in the maintenance of embryonic stem cell pluripotency.,"Cases 4, 5, and 6 showed deletion mutation. In case 6, a de novo deletion mutation was revealed by both southern hybridization and polymerase chain reaction (PCR) of a GGAA tetranucleotide tandem repeat. located in the C-terminal presumptive ligand binding domain, are important to the functional role of the DAX-1 protein in adrenal embryogenesis and/or in hypothalamic-pituitary activity; and 2) molecular analysis of the DAX-1 gene may help genetic counseling, even in cases with deletion mutation, because a detection of de novo deletion may exclude another affected or carrier child.","In AHC. Cases 4, 5, and 6 showed deletion mutation. In case 6, a de novo deletion mutation was revealed by both southern hybridization and polymerase chain reaction (PCR) of a GGAA tetranucleotide tandem repeat. located in the C-terminal presumptive ligand binding domain, are important to the functional role of the DAX-1 protein in adrenal embryogenesis and/or in hypothalamic-pituitary activity; and 2) molecular analysis of the DAX-1 gene may help genetic counseling, even in cases with deletion mutation, because a detection of de novo deletion may exclude another affected or carrier child."
87,87,78069,P08692-K61R,MSNITIYHNPACGTSRNTLEMIRNSGTEPTIILYLENPPSRDELVKLIADMGISVRALLRRNVEPYEQLGLAEDKFTDDQLIDFMLQHPILINRPIVVTPLGTRLCRPSEVVLDILQDAQKGAFTKEDGEKVVDEAGKRLK,Mutant retains arsenate resistance.,,MSNITIYHNPACGTSRNTLEMIRNSGTEPTIILYLENPPSRDELVKLIADMGISVRALLRKNVEPYEQLGLAEDKFTDDQLIDFMLQHPILINRPIVVTPLGTRLCRPSEVVLDILQDAQKGAFTKEDGEKVVDEAGKRLK,Arsenate reductase,Involved in resistance to arsenate. Catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)]. The resulting arsenite is then extruded from the cell via the ArsAB transport system (Probable).,,Mutant retains arsenate resistance.
88,88,78247,O14746-R522K,MPRAPRCRAVRSLLRSHYREVLPLATFVRRLGPQGWRLVQRGDPAAFRALVAQCLVCVPWDARPPPAAPSFRQVSCLKELVARVLQRLCERGAKNVLAFGFALLDGARGGPPEAFTTSVRSYLPNTVTDALRGSGAWGLLLRRVGDDVLVHLLARCALFVLVAPSCAYQVCGPPLYQLGAATQARPPPHASGPRRRLGCERAWNHSVREAGVPLGLPAPGARRRGGSASRSLPLPKRPRRGAAPEPERTPVGQGSWAHPGRTRGPSDRGFCVVSPARPAEEATSLEGALSGTRHSHPSVGRQHHAGPPSTSRPPRPWDTPCPPVYAETKHFLYSSGDKEQLRPSFLLSSLRPSLTGARRLVETIFLGSRPWMPGTPRRLPRLPQRYWQMRPLFLELLGNHAQCPYGVLLKTHCPLRAAVTPAAGVCAREKPQGSVAAPEEEDTDPRRLVQLLRQHSSPWQVYGFVRACLRRLVPPGLWGSRHNERRFLRNTKKFISLGKHAKLSLQELTWKMSVRDCAWLRKSPGVGCVPAAEHRLREEILAKFLHWLMSVYVVELLRSFFYVTETTFQKNRLFFYRKSVWSKLQSIGIRQHLKRVQLRELSEAEVRQHREARPALLTSRLRFIPKPDGLRPIVNMDYVVGARTFRREKRAERLTSRVKALFSVLNYERARRPGLLGASVLGLDDIHRAWRTFVLRVRAQDPPPELYFVKVDVTGAYDTIPQDRLTEVIASIIKPQNTYCVRRYAVVQKAAHGHVRKAFKSHVSTLTDLQPYMRQFVAHLQETSPLRDAVVIEQSSSLNEASSGLFDVFLRFMCHHAVRIRGKSYVQCQGIPQGSILSTLLCSLCYGDMENKLFAGIRRDGLLLRLVDDFLLVTPHLTHAKTFLRTLVRGVPEYGCVVNLRKTVVNFPVEDEALGGTAFVQMPAHGLFPWCGLLLDTRTLEVQSDYSSYARTSIRASLTFNRGFKAGRNMRRKLFGVLRLKCHSLFLDLQVNSLQTVCTNIYKILLLQAYRFHACVLQLPFHQQ,Associated with acute myeloid leukemia.,,MPRAPRCRAVRSLLRSHYREVLPLATFVRRLGPQGWRLVQRGDPAAFRALVAQCLVCVPWDARPPPAAPSFRQVSCLKELVARVLQRLCERGAKNVLAFGFALLDGARGGPPEAFTTSVRSYLPNTVTDALRGSGAWGLLLRRVGDDVLVHLLARCALFVLVAPSCAYQVCGPPLYQLGAATQARPPPHASGPRRRLGCERAWNHSVREAGVPLGLPAPGARRRGGSASRSLPLPKRPRRGAAPEPERTPVGQGSWAHPGRTRGPSDRGFCVVSPARPAEEATSLEGALSGTRHSHPSVGRQHHAGPPSTSRPPRPWDTPCPPVYAETKHFLYSSGDKEQLRPSFLLSSLRPSLTGARRLVETIFLGSRPWMPGTPRRLPRLPQRYWQMRPLFLELLGNHAQCPYGVLLKTHCPLRAAVTPAAGVCAREKPQGSVAAPEEEDTDPRRLVQLLRQHSSPWQVYGFVRACLRRLVPPGLWGSRHNERRFLRNTKKFISLGKHAKLSLQELTWKMSVRDCAWLRRSPGVGCVPAAEHRLREEILAKFLHWLMSVYVVELLRSFFYVTETTFQKNRLFFYRKSVWSKLQSIGIRQHLKRVQLRELSEAEVRQHREARPALLTSRLRFIPKPDGLRPIVNMDYVVGARTFRREKRAERLTSRVKALFSVLNYERARRPGLLGASVLGLDDIHRAWRTFVLRVRAQDPPPELYFVKVDVTGAYDTIPQDRLTEVIASIIKPQNTYCVRRYAVVQKAAHGHVRKAFKSHVSTLTDLQPYMRQFVAHLQETSPLRDAVVIEQSSSLNEASSGLFDVFLRFMCHHAVRIRGKSYVQCQGIPQGSILSTLLCSLCYGDMENKLFAGIRRDGLLLRLVDDFLLVTPHLTHAKTFLRTLVRGVPEYGCVVNLRKTVVNFPVEDEALGGTAFVQMPAHGLFPWCGLLLDTRTLEVQSDYSSYARTSIRASLTFNRGFKAGRNMRRKLFGVLRLKCHSLFLDLQVNSLQTVCTNIYKILLLQAYRFHACVLQLPFHQQ,Telomerase reverse transcriptase,"Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. Active in progenitor and cancer cells. Inactive, or very low activity, in normal somatic cells. Catalytic component of the teleromerase holoenzyme complex whose main activity is the elongation of telomeres by acting as a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme. Catalyzes the RNA-dependent extension of 3'-chromosomal termini with the 6-nucleotide telomeric repeat unit, 5'-TTAGGG-3'. The catalytic cycle involves primer binding, primer extension and release of product once the template boundary has been reached or nascent product translocation followed by further extension. More active on substrates containing 2 or 3 telomeric repeats. Telomerase activity is regulated by a number of factors including telomerase complex-associated proteins, chaperones and polypeptide modifiers. Modulates Wnt signaling. Plays important roles in aging and antiapoptosis.",,Associated with acute myeloid leukemia.
89,89,78489,Q9JJS6-H308A,MEIIFGQNKKEQLEPVQAKVTGSIPAWLQGTLLRNGPGMHTVGESKYNHWFDGLALLHSFSIRDGEVFYRSKYLQSDTYIANIEANRIVVSEFGTMAYPDPCKNIFSKAFSYLSHTIPDFTDNCLINIMKCGEDFYATTETNYIRKIDPQTLETLEKVDYRKYVAVNLATSHPHYDEAGNVLNMGTSVVDKGRTKYVIFKIPATVPDSKKKGKSPVKHAEVFCSISSRSLLSPSYYHSFGVTENYVVFLEQPFKLDILKMATAYMRGVSWASCMSFDREDKTYIHIIDQRTRKPVPTKFYTDPMVVFAHVNAYEEDGCVLFDVIAYEDSSLYQLFYLANLNKDFEEKSRLTSVPTLRRFAVPLHVDKDAEVGSNLVKVSSTTATALKEKDGHVYCQPEVLYEGLELPRINYAYNGKPYRYIFAAEVQWSPVPTKILKYDILTKSSLKWSEESCWPAEPLFVPTPGAKDEDDGVILSAIVSTDPQKLPFLLILDAKSFTELARASVDADMHLDLHGLFIPDADWNAVKQTPAETQEVENSDHPTDPTAPELSHSENDFTAGHGGSSL,"No effect on protein abundance. Loss of beta-carotene 15,15'-monooxygenase activity. Decreased iron binding.",,MEIIFGQNKKEQLEPVQAKVTGSIPAWLQGTLLRNGPGMHTVGESKYNHWFDGLALLHSFSIRDGEVFYRSKYLQSDTYIANIEANRIVVSEFGTMAYPDPCKNIFSKAFSYLSHTIPDFTDNCLINIMKCGEDFYATTETNYIRKIDPQTLETLEKVDYRKYVAVNLATSHPHYDEAGNVLNMGTSVVDKGRTKYVIFKIPATVPDSKKKGKSPVKHAEVFCSISSRSLLSPSYYHSFGVTENYVVFLEQPFKLDILKMATAYMRGVSWASCMSFDREDKTYIHIIDQRTRKPVPTKFYTDPMVVFHHVNAYEEDGCVLFDVIAYEDSSLYQLFYLANLNKDFEEKSRLTSVPTLRRFAVPLHVDKDAEVGSNLVKVSSTTATALKEKDGHVYCQPEVLYEGLELPRINYAYNGKPYRYIFAAEVQWSPVPTKILKYDILTKSSLKWSEESCWPAEPLFVPTPGAKDEDDGVILSAIVSTDPQKLPFLLILDAKSFTELARASVDADMHLDLHGLFIPDADWNAVKQTPAETQEVENSDHPTDPTAPELSHSENDFTAGHGGSSL,"Beta,beta-carotene 15,15'-dioxygenase",Symmetrically cleaves beta-carotene into two molecules of retinal using a dioxygenase mechanism.,"Mutation of H308 produced impaired although enzymatically active proteins, with a decrease in activity mostly due to changes in V(max).","No effect on protein abundance. Loss of beta-carotene 15,15'-monooxygenase activity. Decreased iron binding. Mutation of H308 produced impaired although enzymatically active proteins, with a decrease in activity mostly due to changes in V(max)."
90,90,79639,Q92504-S293A,MARGLGAPHWVAVGLLTWATLGLLVAGLGGHDDLHDDLQEDFHGHSHRHSHEDFHHGHSHAHGHGHTHESIWHGHTHDHDHGHSHEDLHHGHSHGYSHESLYHRGHGHDHEHSHGGYGESGAPGIKQDLDAVTLWAYALGATVLISAAPFFVLFLIPVESNSPRHRSLLQILLSFASGGLLGDAFLHLIPHALEPHSHHTLEQPGHGHSHSGQGPILSVGLWVLSGIVAFLVVEKFVRHVKGGHGHSHGHGHAHSHTRGSHGHGRQERSTKEKQSSEEEEKETRGVQKRRGGATVPKDGPVRPQNAEEEKRGLDLRVSGYLNLAADLAHNFTDGLAIGASFRGGRGLGILTTMTVLLHEVPHEVGDFAILVQSGCSKKQAMRLQLLTAVGALAGTACALLTEGGAVGSEIAGGAGPGWVLPFTAGGFIYVATVSVLPELLREASPLQSLLEVLGLLGGVIMMVLIAHLE,Loss of phosphorylation in response to Zn(2+) treatment and of cytosolic Zn(2+) release.,,MARGLGAPHWVAVGLLTWATLGLLVAGLGGHDDLHDDLQEDFHGHSHRHSHEDFHHGHSHAHGHGHTHESIWHGHTHDHDHGHSHEDLHHGHSHGYSHESLYHRGHGHDHEHSHGGYGESGAPGIKQDLDAVTLWAYALGATVLISAAPFFVLFLIPVESNSPRHRSLLQILLSFASGGLLGDAFLHLIPHALEPHSHHTLEQPGHGHSHSGQGPILSVGLWVLSGIVAFLVVEKFVRHVKGGHGHSHGHGHAHSHTRGSHGHGRQERSTKEKQSSEEEEKETRGVQKRRGGSTVPKDGPVRPQNAEEEKRGLDLRVSGYLNLAADLAHNFTDGLAIGASFRGGRGLGILTTMTVLLHEVPHEVGDFAILVQSGCSKKQAMRLQLLTAVGALAGTACALLTEGGAVGSEIAGGAGPGWVLPFTAGGFIYVATVSVLPELLREASPLQSLLEVLGLLGGVIMMVLIAHLE,Zinc transporter SLC39A7,"Transports Zn(2+) from the endoplasmic reticulum (ER)/Golgi apparatus to the cytosol, playing an essential role in the regulation of cytosolic zinc levels. Acts as gatekeeper of zinc release from intracellular stores, requiring post-translational activation by phosphorylation, resulting in activation of multiple downstream pathways leading to cell growth and proliferation. Has an essential role in B cell development and is required for proper B cell receptor signaling. Plays an important role in maintaining intestinal epithelial homeostasis and skin dermis development by regulating ER function. Controls cell signaling pathways involved in glucose metabolism in skeletal muscle. Has a protective role against ER stress in differents biological contexts. Mediates Zn(2+)-induced ferroptosis.",,Loss of phosphorylation in response to Zn(2+) treatment and of cytosolic Zn(2+) release.
91,91,80113,Q9H5P4-M285R,MAQGFAVGFDPLGLGDLSSGSLSSLSSRGHLGSDSGSTATRYLLRKQQRLLNGPPRGIRASSPMGRVILINSPIEANSDESDIIHSVRVEKSPAGRLGFSVRGGSEHGLGIFVSKVEEGSSAERAGLCVGDKITEVNGLSLESTTMGSAVKVLTSSSRLHMMVRRMGRVPGIKFSKEKTTWVDVVNRRLVVEKCGSTPSDTSSEDGVRRIVHLYTTSDDFCLGFNIRGGKEFGLGIYVSKVDHGGLAEENGIKVGDQVLAANGVRFDDISHSQAVEVLKGQTHIRLTIKETGRYPAYKEMVSEYCWLDRLSNGVLQQLSPASESSSSVSSCASSAPYSSGSLPSDRMDICLGQEEPGSRGPGWGRADTAMQTEPDAGGRVETWCSVRPTVILRDTAIRSDGPHPGRRLDSALSESPKTALLLALSRPRPPITRSQSYLTLWEEKQQRKKEKSGSPGEKGALQRSKTLMNLFFKGGRQGRLARDGRREAWTLDSGSLAKTYPRLDIEKAGGVGPVQKFVTWRLRRDQERGRALLSARSGSPSSQLPNVDEQVQAWESRRPLIQDLAQRLLTDDEVLAVTRHCSRYVHEGGIEDLVRPLLAILDRPEKLLLLQDIRSVVAPTDLGRFDSMVMLVELEAFEALKSRAVRPPALRPARQDTPPKRHLITPVPDSRGGFYLLPVNGFPEEEDNGELRERLGALKVSPSASAPRHPHKGIPPLQDVPVDAFTPLRIACTPPPQLPPVAPRPLRPNWLLTEPLSREHPPQSQIRGRAQSRSRSRSRSRSRSSRGQGKSPGRRSPSPVPTPAPSMTNGRYHKPRKARPPLPRPLDGEAAKVGAKQGPSESGTEGTAKEAAMKNPSGELKTVTLSKMKQSLGISISGGIESKVQPMVKIEKIFPGGAAFLSGALQAGFELVAVDGENLEQVTHQRAVDTIRRAYRNKAREPMELVVRVPGPSPRPSPSDSSALTDGGLPADHLPAHQPLDAAPVPAHWLPEPPTNPQTPPTDARLLQPTPSPAPSPALQTPDS,In DFNB57.,,MAQGFAVGFDPLGLGDLSSGSLSSLSSRGHLGSDSGSTATRYLLRKQQRLLNGPPRGIRASSPMGRVILINSPIEANSDESDIIHSVRVEKSPAGRLGFSVRGGSEHGLGIFVSKVEEGSSAERAGLCVGDKITEVNGLSLESTTMGSAVKVLTSSSRLHMMVRRMGRVPGIKFSKEKTTWVDVVNRRLVVEKCGSTPSDTSSEDGVRRIVHLYTTSDDFCLGFNIRGGKEFGLGIYVSKVDHGGLAEENGIKVGDQVLAANGVRFDDISHSQAVEVLKGQTHIMLTIKETGRYPAYKEMVSEYCWLDRLSNGVLQQLSPASESSSSVSSCASSAPYSSGSLPSDRMDICLGQEEPGSRGPGWGRADTAMQTEPDAGGRVETWCSVRPTVILRDTAIRSDGPHPGRRLDSALSESPKTALLLALSRPRPPITRSQSYLTLWEEKQQRKKEKSGSPGEKGALQRSKTLMNLFFKGGRQGRLARDGRREAWTLDSGSLAKTYPRLDIEKAGGVGPVQKFVTWRLRRDQERGRALLSARSGSPSSQLPNVDEQVQAWESRRPLIQDLAQRLLTDDEVLAVTRHCSRYVHEGGIEDLVRPLLAILDRPEKLLLLQDIRSVVAPTDLGRFDSMVMLVELEAFEALKSRAVRPPALRPARQDTPPKRHLITPVPDSRGGFYLLPVNGFPEEEDNGELRERLGALKVSPSASAPRHPHKGIPPLQDVPVDAFTPLRIACTPPPQLPPVAPRPLRPNWLLTEPLSREHPPQSQIRGRAQSRSRSRSRSRSRSSRGQGKSPGRRSPSPVPTPAPSMTNGRYHKPRKARPPLPRPLDGEAAKVGAKQGPSESGTEGTAKEAAMKNPSGELKTVTLSKMKQSLGISISGGIESKVQPMVKIEKIFPGGAAFLSGALQAGFELVAVDGENLEQVTHQRAVDTIRRAYRNKAREPMELVVRVPGPSPRPSPSDSSALTDGGLPADHLPAHQPLDAAPVPAHWLPEPPTNPQTPPTDARLLQPTPSPAPSPALQTPDS,PDZ domain-containing protein 7,"In cochlear developing hair cells, essential in organizing the USH2 complex at stereocilia ankle links. Blocks inhibition of adenylate cyclase activity mediated by ADGRV1.",The homozygous missense variant (p. ) in PDZD7 is predicted to be deleterious.,In DFNB57. The homozygous missense variant (p. ) in PDZD7 is predicted to be deleterious.
92,92,81408,P08692-R107Y,MSNITIYHNPACGTSRNTLEMIRNSGTEPTIILYLENPPSRDELVKLIADMGISVRALLRKNVEPYEQLGLAEDKFTDDQLIDFMLQHPILINRPIVVTPLGTRLCYPSEVVLDILQDAQKGAFTKEDGEKVVDEAGKRLK,Loss of reductase activity. Mutant is sensitive to arsenate.,,MSNITIYHNPACGTSRNTLEMIRNSGTEPTIILYLENPPSRDELVKLIADMGISVRALLRKNVEPYEQLGLAEDKFTDDQLIDFMLQHPILINRPIVVTPLGTRLCRPSEVVLDILQDAQKGAFTKEDGEKVVDEAGKRLK,Arsenate reductase,Involved in resistance to arsenate. Catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)]. The resulting arsenite is then extruded from the cell via the ArsAB transport system (Probable).,,Loss of reductase activity. Mutant is sensitive to arsenate.
93,93,83586,P16522-T94M,MNDDSQDKIIHDIRIQLRKAATELSRWKLYGSSKWAAEALAGLAEAIDVDQTHSLADESPLRNKQGVPKQMFEIPQNGFGLSETEYDLYLLGSMLFDAKEFDRCVFFLKDVTNPYLKFLKLYSKFLSWDKKSQESMENILTTGKFTDEMYRANKDGDGSGNEDINQSGHQRANLKMVSNEHESQSNISSILKEINTFLESYEIKIDDDEADLGLALLYYLRGVILKQEKNISKAMSSFLKSLSCYSFNWSCWLELMDCLQKVDDALLLNNYLYQNFQFKFSENLGSQRTIEFNIMIKFFKLKVFEELNGQLEDYFEDLEFLLQVFPNFTFLKAYNATISYNNLDYVTAESRFDDIVKQDPYRLNDLETYSNILYVMQKNSKLAYLAQFVSQIDRFRPETCCIIANYYSARQEHEKSIMYFRRALTLDKKTTNAWTLMGHEFVELSNSHAAIECYRRAVDICPRDFKAWFGLGQAYALLDMHLYSLYYFQKACTLKPWDRRIWQVLGECYSKTGNKVEAIKCYKRSIKASQTVDQNTSIYYRLAQLYEELEDLQECKKFMMKCVDVEELLEGIVTDETVKARLWLAIFEIKAGNYQLAYDYAMGVSSGTSQEIEEARMLARECRRHM,In CDC23-4; G2/M cell cycle arrest at 36 degrees Celsius.,,MNDDSQDKIIHDIRIQLRKAATELSRWKLYGSSKWAAEALAGLAEAIDVDQTHSLADESPLRNKQGVPKQMFEIPQNGFGLSETEYDLYLLGSTLFDAKEFDRCVFFLKDVTNPYLKFLKLYSKFLSWDKKSQESMENILTTGKFTDEMYRANKDGDGSGNEDINQSGHQRANLKMVSNEHESQSNISSILKEINTFLESYEIKIDDDEADLGLALLYYLRGVILKQEKNISKAMSSFLKSLSCYSFNWSCWLELMDCLQKVDDALLLNNYLYQNFQFKFSENLGSQRTIEFNIMIKFFKLKVFEELNGQLEDYFEDLEFLLQVFPNFTFLKAYNATISYNNLDYVTAESRFDDIVKQDPYRLNDLETYSNILYVMQKNSKLAYLAQFVSQIDRFRPETCCIIANYYSARQEHEKSIMYFRRALTLDKKTTNAWTLMGHEFVELSNSHAAIECYRRAVDICPRDFKAWFGLGQAYALLDMHLYSLYYFQKACTLKPWDRRIWQVLGECYSKTGNKVEAIKCYKRSIKASQTVDQNTSIYYRLAQLYEELEDLQECKKFMMKCVDVEELLEGIVTDETVKARLWLAIFEIKAGNYQLAYDYAMGVSSGTSQEIEEARMLARECRRHM,Anaphase-promoting complex subunit CDC23,"Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. In early mitosis, the APC/C is activated by CDC20 and targets securin PDS1, the B-type cyclin CLB5, and other anaphase inhibitory proteins for proteolysis, thereby triggering the separation of sister chromatids at the metaphase-to-anaphase transition. In late mitosis and in G1, degradation of CLB5 allows activation of the APC/C by CDH1, which is needed to destroy CDC20 and the B-type cyclin CLB2 to allow exit from mitosis and creating the low CDK state necessary for cytokinesis and for reforming prereplicative complexes in G1 prior to another round of replication.",,In CDC23-4; G2/M cell cycle arrest at 36 degrees Celsius.
94,94,83868,P07749-K23N,MGACGSKGSTSDKGLASDKDGKNAKDRKEAWERIRQAIPREKTAEAKQRRIELFKKFDKNETGKLCYDEVHSGCLEVLKLDEFTPRVRDITKRAFDKARALGSKLENKGSEDFVEFLEFRLMLCYIYDFFELTVMFDEIDASGNMLVDEEELKRAVPKLEAWGAKVEDPAALFKELDKNGTGSVTFDEFAAWASAVKLDADGDPDNVPESA,"In strain: Miranda, PBOL and DM28C.",,MGACGSKGSTSDKGLASDKDGKKAKDRKEAWERIRQAIPREKTAEAKQRRIELFKKFDKNETGKLCYDEVHSGCLEVLKLDEFTPRVRDITKRAFDKARALGSKLENKGSEDFVEFLEFRLMLCYIYDFFELTVMFDEIDASGNMLVDEEELKRAVPKLEAWGAKVEDPAALFKELDKNGTGSVTFDEFAAWASAVKLDADGDPDNVPESA,Flagellar calcium-binding protein,"May contribute to the rapid motility of the trypanosomes, playing a role either in flagellar structure or in calcium metabolism. Could alternate between a GDP-bound inactive form to a calcium/GTP-bound active form.",,"In strain: Miranda, PBOL and DM28C."
95,95,84593,P9WH43-F307A,MPSPTVTSPQVAVNDIGSSEDFLAAIDKTIKYFNDGDIVEGTIVKVDRDEVLLDIGYKTEGVIPARELSIKHDVDPNEVVSVGDEVEALVLTKEDKEGRLILSKKRAQYERAWGTIEALKEKDEAVKGTVIEVVKGGLILDIGLRGFLPASLVEMRRVRDLQPYIGKEIEAKIIELDKNRNNVVLSRRAWLEQTQSEVRSEFLNNLQKGTIRKGVVSSIVNFGAFVDLGGVDGLVHVSELSWKHIDHPSEVVQVGDEVTVEVLDVDMDRERVSLSLKATQEDPWRHFARTHAIGQIVPGKVTKLVPAGAFVRVEEGIEGLVHISELAERHVEVPDQVVAVGDDAMVKVIDIDLERRRISLSLKQANEDYTEEFDPAKYGMADSYDEQGNYIFPEGFDAETNEWLEGFEKQRAEWEARYAEAERRHKMHTAQMEKFAAAEAAGRGADDQSSASSAPSEKTAGGSLASDAQLAALREKLAGSA,"2.5-fold decrease in binding of POA, decreased binding of tmRNA (expressed as residues 285-481).",,MPSPTVTSPQVAVNDIGSSEDFLAAIDKTIKYFNDGDIVEGTIVKVDRDEVLLDIGYKTEGVIPARELSIKHDVDPNEVVSVGDEVEALVLTKEDKEGRLILSKKRAQYERAWGTIEALKEKDEAVKGTVIEVVKGGLILDIGLRGFLPASLVEMRRVRDLQPYIGKEIEAKIIELDKNRNNVVLSRRAWLEQTQSEVRSEFLNNLQKGTIRKGVVSSIVNFGAFVDLGGVDGLVHVSELSWKHIDHPSEVVQVGDEVTVEVLDVDMDRERVSLSLKATQEDPWRHFARTHAIGQIVPGKVTKLVPFGAFVRVEEGIEGLVHISELAERHVEVPDQVVAVGDDAMVKVIDIDLERRRISLSLKQANEDYTEEFDPAKYGMADSYDEQGNYIFPEGFDAETNEWLEGFEKQRAEWEARYAEAERRHKMHTAQMEKFAAAEAAGRGADDQSSASSAPSEKTAGGSLASDAQLAALREKLAGSA,Small ribosomal subunit protein bS1,"Binds mRNA, facilitating recognition of most mRNAs by the 30S ribosomal subunit during translation initiation (By similarity). Probably plays a role in trans-translation; binds tmRNA (the product of the ssrA gene). In trans-translation Ala-aminoacylated transfer-messenger RNA (tmRNA, product of the ssrA gene; the 2 termini fold to resemble tRNA(Ala) while it encodes a short internal open reading frame (the tag peptide)) acts like a tRNA, entering the A-site of the ribosome and displacing the stalled mRNA (which is subsequently degraded). The ribosome then switches to translate the ORF on the tmRNA, the nascent peptide is terminated with the 'tag peptide' encoded by the tmRNA and thus targeted for degradation (By similarity).",Conformational changes induced by mutation at F307 abolish the POA binding activity.,"2.5-fold decrease in binding of POA, decreased binding of tmRNA (expressed as residues 285-481). Conformational changes induced by mutation at F307 abolish the POA binding activity."
96,96,84636,P16522-G80S,MNDDSQDKIIHDIRIQLRKAATELSRWKLYGSSKWAAEALAGLAEAIDVDQTHSLADESPLRNKQGVPKQMFEIPQNGFSLSETEYDLYLLGSTLFDAKEFDRCVFFLKDVTNPYLKFLKLYSKFLSWDKKSQESMENILTTGKFTDEMYRANKDGDGSGNEDINQSGHQRANLKMVSNEHESQSNISSILKEINTFLESYEIKIDDDEADLGLALLYYLRGVILKQEKNISKAMSSFLKSLSCYSFNWSCWLELMDCLQKVDDALLLNNYLYQNFQFKFSENLGSQRTIEFNIMIKFFKLKVFEELNGQLEDYFEDLEFLLQVFPNFTFLKAYNATISYNNLDYVTAESRFDDIVKQDPYRLNDLETYSNILYVMQKNSKLAYLAQFVSQIDRFRPETCCIIANYYSARQEHEKSIMYFRRALTLDKKTTNAWTLMGHEFVELSNSHAAIECYRRAVDICPRDFKAWFGLGQAYALLDMHLYSLYYFQKACTLKPWDRRIWQVLGECYSKTGNKVEAIKCYKRSIKASQTVDQNTSIYYRLAQLYEELEDLQECKKFMMKCVDVEELLEGIVTDETVKARLWLAIFEIKAGNYQLAYDYAMGVSSGTSQEIEEARMLARECRRHM,In CDC23-44; G2/M cell cycle arrest at 37 degrees Celsius.,,MNDDSQDKIIHDIRIQLRKAATELSRWKLYGSSKWAAEALAGLAEAIDVDQTHSLADESPLRNKQGVPKQMFEIPQNGFGLSETEYDLYLLGSTLFDAKEFDRCVFFLKDVTNPYLKFLKLYSKFLSWDKKSQESMENILTTGKFTDEMYRANKDGDGSGNEDINQSGHQRANLKMVSNEHESQSNISSILKEINTFLESYEIKIDDDEADLGLALLYYLRGVILKQEKNISKAMSSFLKSLSCYSFNWSCWLELMDCLQKVDDALLLNNYLYQNFQFKFSENLGSQRTIEFNIMIKFFKLKVFEELNGQLEDYFEDLEFLLQVFPNFTFLKAYNATISYNNLDYVTAESRFDDIVKQDPYRLNDLETYSNILYVMQKNSKLAYLAQFVSQIDRFRPETCCIIANYYSARQEHEKSIMYFRRALTLDKKTTNAWTLMGHEFVELSNSHAAIECYRRAVDICPRDFKAWFGLGQAYALLDMHLYSLYYFQKACTLKPWDRRIWQVLGECYSKTGNKVEAIKCYKRSIKASQTVDQNTSIYYRLAQLYEELEDLQECKKFMMKCVDVEELLEGIVTDETVKARLWLAIFEIKAGNYQLAYDYAMGVSSGTSQEIEEARMLARECRRHM,Anaphase-promoting complex subunit CDC23,"Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. In early mitosis, the APC/C is activated by CDC20 and targets securin PDS1, the B-type cyclin CLB5, and other anaphase inhibitory proteins for proteolysis, thereby triggering the separation of sister chromatids at the metaphase-to-anaphase transition. In late mitosis and in G1, degradation of CLB5 allows activation of the APC/C by CDH1, which is needed to destroy CDC20 and the B-type cyclin CLB2 to allow exit from mitosis and creating the low CDK state necessary for cytokinesis and for reforming prereplicative complexes in G1 prior to another round of replication.",The mutation in the CDC23 gene causes a single amino acid change in the protein. This mutation is found within a mutable domain of CDC23 and may affect its function or stability.,In CDC23-44; G2/M cell cycle arrest at 37 degrees Celsius. The mutation in the CDC23 gene causes a single amino acid change in the protein. This mutation is found within a mutable domain of CDC23 and may affect its function or stability.
97,97,85044,O54908-R242E,MMVVCAAAAVRFLAVFTMMALCSLPLLGASATLNSVLINSNAIKNLPPPLGGAGGQPGSAVSVAPGVLYEGGNKYQTLDNYQPYPCAEDEECGSDEYCSSPSRGAAGVGGVQICLACRKRRKRCMRHAMCCPGNYCKNGICMPSDHSHFPRGEIEESIIENLGNDHNAAAGDGYPRRTTLTSKIYHTKGQEGSVCLRSSDCAAGLCCARHFWSKICKPVLKEGQVCTKHKRKGSHGLEIFQECYCGEGLACRIQKDHHQASNSSRLHTCQRH,50% reduced binding to LRP6.,,MMVVCAAAAVRFLAVFTMMALCSLPLLGASATLNSVLINSNAIKNLPPPLGGAGGQPGSAVSVAPGVLYEGGNKYQTLDNYQPYPCAEDEECGSDEYCSSPSRGAAGVGGVQICLACRKRRKRCMRHAMCCPGNYCKNGICMPSDHSHFPRGEIEESIIENLGNDHNAAAGDGYPRRTTLTSKIYHTKGQEGSVCLRSSDCAAGLCCARHFWSKICKPVLKEGQVCTKHKRKGSHGLEIFQRCYCGEGLACRIQKDHHQASNSSRLHTCQRH,Dickkopf-related protein 1,"Antagonizes canonical Wnt signaling by inhibiting LRP5/6 interaction with Wnt and by forming a ternary complex with the transmembrane protein KREMEN that promotes internalization of LRP5/6. Inhibits the pro-apoptotic function of KREMEN1 in a Wnt-independent manner, and has anti-apoptotic activity. Plays a role in limb development; attenuates Wnt signaling in the developing limb to allow normal limb patterning.",,50% reduced binding to LRP6.
98,98,85243,P9WGT3-S140A,MTATATEGAKPPFVSRSVLVTGGNRGIGLAIAQRLAADGHKVAVTHRGSGAPKGLFGVECDVTDSDAVDRAFTAVEEHQGPVEVLVSNAGLSADAFLMRMTEEKFEKVINANLTGAFRVAQRASRSMQRNKFGRMIFIGAVSGSWGIGNQANYAASKAGVIGMARSIARELSKANVTANVVAPGYIDTDMTRALDERIQQGALQFIPAKRVGTPAEVAGVVSFLASEDASYISGAVIPVDGGMGMGH,Loss of activity. Can still bind NADPH.,,MTATATEGAKPPFVSRSVLVTGGNRGIGLAIAQRLAADGHKVAVTHRGSGAPKGLFGVECDVTDSDAVDRAFTAVEEHQGPVEVLVSNAGLSADAFLMRMTEEKFEKVINANLTGAFRVAQRASRSMQRNKFGRMIFIGSVSGSWGIGNQANYAASKAGVIGMARSIARELSKANVTANVVAPGYIDTDMTRALDERIQQGALQFIPAKRVGTPAEVAGVVSFLASEDASYISGAVIPVDGGMGMGH,3-oxoacyl-[acyl-carrier-protein] reductase MabA,"Part of the mycobacterial fatty acid elongation system FAS-II, which is involved in mycolic acid biosynthesis. Catalyzes the NADPH-dependent reduction of beta-ketoacyl derivatives, the second step of the FAS-II elongation cycle. May preferentially metabolize long-chain substrates (C8-C20). Can use CoA derivatives as substrates in vitro.","The mutation in MabA has been shown to decrease the activity of the enzyme, leading to a reduction in the production of mycolic acids. This can impair the growth and survival of Mycobacterium tuberculosis.","Loss of activity. Can still bind NADPH. The mutation in MabA has been shown to decrease the activity of the enzyme, leading to a reduction in the production of mycolic acids. This can impair the growth and survival of Mycobacterium tuberculosis."
99,99,85380,Q92504-E363K,MARGLGAPHWVAVGLLTWATLGLLVAGLGGHDDLHDDLQEDFHGHSHRHSHEDFHHGHSHAHGHGHTHESIWHGHTHDHDHGHSHEDLHHGHSHGYSHESLYHRGHGHDHEHSHGGYGESGAPGIKQDLDAVTLWAYALGATVLISAAPFFVLFLIPVESNSPRHRSLLQILLSFASGGLLGDAFLHLIPHALEPHSHHTLEQPGHGHSHSGQGPILSVGLWVLSGIVAFLVVEKFVRHVKGGHGHSHGHGHAHSHTRGSHGHGRQERSTKEKQSSEEEEKETRGVQKRRGGSTVPKDGPVRPQNAEEEKRGLDLRVSGYLNLAADLAHNFTDGLAIGASFRGGRGLGILTTMTVLLHEVPHKVGDFAILVQSGCSKKQAMRLQLLTAVGALAGTACALLTEGGAVGSEIAGGAGPGWVLPFTAGGFIYVATVSVLPELLREASPLQSLLEVLGLLGGVIMMVLIAHLE,In AGM9; decreased zinc ion transporter activity; does not affect localization to endoplasmic reticulum.,,MARGLGAPHWVAVGLLTWATLGLLVAGLGGHDDLHDDLQEDFHGHSHRHSHEDFHHGHSHAHGHGHTHESIWHGHTHDHDHGHSHEDLHHGHSHGYSHESLYHRGHGHDHEHSHGGYGESGAPGIKQDLDAVTLWAYALGATVLISAAPFFVLFLIPVESNSPRHRSLLQILLSFASGGLLGDAFLHLIPHALEPHSHHTLEQPGHGHSHSGQGPILSVGLWVLSGIVAFLVVEKFVRHVKGGHGHSHGHGHAHSHTRGSHGHGRQERSTKEKQSSEEEEKETRGVQKRRGGSTVPKDGPVRPQNAEEEKRGLDLRVSGYLNLAADLAHNFTDGLAIGASFRGGRGLGILTTMTVLLHEVPHEVGDFAILVQSGCSKKQAMRLQLLTAVGALAGTACALLTEGGAVGSEIAGGAGPGWVLPFTAGGFIYVATVSVLPELLREASPLQSLLEVLGLLGGVIMMVLIAHLE,Zinc transporter SLC39A7,"Transports Zn(2+) from the endoplasmic reticulum (ER)/Golgi apparatus to the cytosol, playing an essential role in the regulation of cytosolic zinc levels. Acts as gatekeeper of zinc release from intracellular stores, requiring post-translational activation by phosphorylation, resulting in activation of multiple downstream pathways leading to cell growth and proliferation. Has an essential role in B cell development and is required for proper B cell receptor signaling. Plays an important role in maintaining intestinal epithelial homeostasis and skin dermis development by regulating ER function. Controls cell signaling pathways involved in glucose metabolism in skeletal muscle. Has a protective role against ER stress in differents biological contexts. Mediates Zn(2+)-induced ferroptosis.",,In AGM9; decreased zinc ion transporter activity; does not affect localization to endoplasmic reticulum.
100,100,86160,O00217-R138H,MRCLTTPMLLRALAQAARAGPPGGRSLHSSAVAATYKYVNMQDPEMDMKSVTDRAARTLLWTELFRGLGMTLSYLFREPATINYPFEKGPLSPRFRGEHALRRYPSGEERCIACKLCEAICPAQAITIEAEPRADGSHRTTRYDIDMTKCIYCGFCQEACPVDAIVEGPNFEFSTETHEELLYNKEKLLNNGDKWEAEIAANIQADYLYR,In MC1DN2; unknown pathological significance.,,MRCLTTPMLLRALAQAARAGPPGGRSLHSSAVAATYKYVNMQDPEMDMKSVTDRAARTLLWTELFRGLGMTLSYLFREPATINYPFEKGPLSPRFRGEHALRRYPSGEERCIACKLCEAICPAQAITIEAEPRADGSRRTTRYDIDMTKCIYCGFCQEACPVDAIVEGPNFEFSTETHEELLYNKEKLLNNGDKWEAEIAANIQADYLYR,"NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial","Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I.","The patient with late-onset disease and partial complex I defect was a compound heterozygote for the novel mutation in the NDUFS8 gene. Western blot analysis revealed a deficiency in the NDUFS8 polypeptide, suggesting that this mutation affects the assembly or stability of complex I.","In MC1DN2; unknown pathological significance. The patient with late-onset disease and partial complex I defect was a compound heterozygote for the novel mutation in the NDUFS8 gene. Western blot analysis revealed a deficiency in the NDUFS8 polypeptide, suggesting that this mutation affects the assembly or stability of complex I."
101,101,86780,O00217-A159D,MRCLTTPMLLRALAQAARAGPPGGRSLHSSAVAATYKYVNMQDPEMDMKSVTDRAARTLLWTELFRGLGMTLSYLFREPATINYPFEKGPLSPRFRGEHALRRYPSGEERCIACKLCEAICPAQAITIEAEPRADGSRRTTRYDIDMTKCIYCGFCQEDCPVDAIVEGPNFEFSTETHEELLYNKEKLLNNGDKWEAEIAANIQADYLYR,In MC1DN2; unknown pathological significance; decrease in enzyme activity; impaired assembly of complex I.,,MRCLTTPMLLRALAQAARAGPPGGRSLHSSAVAATYKYVNMQDPEMDMKSVTDRAARTLLWTELFRGLGMTLSYLFREPATINYPFEKGPLSPRFRGEHALRRYPSGEERCIACKLCEAICPAQAITIEAEPRADGSRRTTRYDIDMTKCIYCGFCQEACPVDAIVEGPNFEFSTETHEELLYNKEKLLNNGDKWEAEIAANIQADYLYR,"NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial","Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I.",,In MC1DN2; unknown pathological significance; decrease in enzyme activity; impaired assembly of complex I.
102,102,87123,Q84W98-P94A,MATSNDQTNTKSSHSRTLLLLFIFLSLLLFSSLTIPMTRHQSTSMVAPFKRVLLESSVPASSTMDLRPKASTRRSRTSRRREFGNDAHEVPSGANPISN,Impaired repression of tracheary element differentiation.,,MATSNDQTNTKSSHSRTLLLLFIFLSLLLFSSLTIPMTRHQSTSMVAPFKRVLLESSVPASSTMDLRPKASTRRSRTSRRREFGNDAHEVPSGPNPISN,CLAVATA3/ESR,"Extracellular signal peptide that regulates cell fate. May act with TDR as a ligand-receptor pair in a signal transduction pathway that represses tracheary element differentiation but promotes the formation of procambial cells adjacent to phloem cells in the veins in an auxin-dependent manner. Regulates the transition of protophloem cells from proliferation to differentiation, thus impinging on postembryonic growth capacity of the root meristem; this signaling pathway requires CRN and CLV2.",,Impaired repression of tracheary element differentiation.
103,103,87552,Q68CZ1-A229T,MSGPTDETAGDLPVKDTGLNLFGMGGLQETSTTRTMKSRQAVSRVSREELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIRLVNDKKRYERVGGGPKRLGRDVEMEEMIEQLQEKVHELEKQNETLKNRLISAKQQLQTQGYRQTPYNNVQSRINTGRRKANENAGLQECPRKGIKFQDADVAETPHPMFTKYGNSLLEEARGEIRNLENVIQSQRGQIEELEHLTEILKTQLRRKENEIELSLLQLREQQATDQRSNIRDNVEMIKLHKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQLHSMKFSERRIEELQDRINDLEKERELLKENYDKLYDSAFSAAHEEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQQLDELKKRIKLYNQENDINADELSEALLLIKAQKEQKNGDLSFLVKVDSEINKDLERSMRELQATHAETVQELEKTRNMLIMQHKINKDYQMEVEAVTRKMENLQQDYELKVEQYVHLLDIRAARIHKLEAQLKDIAYGTKQYKFKPEIMPDDSVDEFDETIHLERGENLFEIHINKVTFSSEVLQASGDKEPVTFCTYAFYDFELQTTPVVRGLHPEYNFTSQYLVHVNDLFLQYIQKNTITLEVHQAYSTEYETIAACQLKFHEILEKSGRIFCTASLIGTKGDIPNFGTVEYWFRLRVPMDQAIRLYRERAKALGYITSNFKGPEHMQSLSQQAPKTAQLSSTDSTDGNLNELHITIRCCNHLQSRASHLQPHPYVVYKFFDFADHDTAIIPSSNDPQFDDHMYFPVPMNMDLDRYLKSESLSFYVFDDSDTQENIYIGKVNVPLISLAHDRCISGIFELTDHQKHPAGTIHVILKWKFAYLPPSGSITTEDLGNFIRSEEPEVVQRLPPASSVSTLVLAPRPKPRQRLTPVDKKVSFVDIMPHQSDETSPPPEDRKEISPEVEHIPEIEINMLTVPHVPKVSQE,"Associated with the development of retinal degeneration in individuals with ciliopathies caused by mutations in other genes; found in patients with Leber congenital amaurosis, Senior-Loken syndrome, Joubert syndrome and Bardet-Biedl syndrome; abrogates interaction with RPGR.",,MSGPTDETAGDLPVKDTGLNLFGMGGLQETSTTRTMKSRQAVSRVSREELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIRLVNDKKRYERVGGGPKRLGRDVEMEEMIEQLQEKVHELEKQNETLKNRLISAKQQLQTQGYRQTPYNNVQSRINTGRRKANENAGLQECPRKGIKFQDADVAETPHPMFTKYGNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIELSLLQLREQQATDQRSNIRDNVEMIKLHKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQLHSMKFSERRIEELQDRINDLEKERELLKENYDKLYDSAFSAAHEEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQQLDELKKRIKLYNQENDINADELSEALLLIKAQKEQKNGDLSFLVKVDSEINKDLERSMRELQATHAETVQELEKTRNMLIMQHKINKDYQMEVEAVTRKMENLQQDYELKVEQYVHLLDIRAARIHKLEAQLKDIAYGTKQYKFKPEIMPDDSVDEFDETIHLERGENLFEIHINKVTFSSEVLQASGDKEPVTFCTYAFYDFELQTTPVVRGLHPEYNFTSQYLVHVNDLFLQYIQKNTITLEVHQAYSTEYETIAACQLKFHEILEKSGRIFCTASLIGTKGDIPNFGTVEYWFRLRVPMDQAIRLYRERAKALGYITSNFKGPEHMQSLSQQAPKTAQLSSTDSTDGNLNELHITIRCCNHLQSRASHLQPHPYVVYKFFDFADHDTAIIPSSNDPQFDDHMYFPVPMNMDLDRYLKSESLSFYVFDDSDTQENIYIGKVNVPLISLAHDRCISGIFELTDHQKHPAGTIHVILKWKFAYLPPSGSITTEDLGNFIRSEEPEVVQRLPPASSVSTLVLAPRPKPRQRLTPVDKKVSFVDIMPHQSDETSPPPEDRKEISPEVEHIPEIEINMLTVPHVPKVSQE,Protein fantom,"Negatively regulates signaling through the G-protein coupled thromboxane A2 receptor (TBXA2R). May be involved in mechanisms like programmed cell death, craniofacial development, patterning of the limbs, and formation of the left-right axis. Involved in the organization of apical junctions; the function is proposed to implicate a NPHP1-4-8 module. Does not seem to be strictly required for ciliogenesis. Involved in establishment of planar cell polarity such as in cochlear sensory epithelium and is proposed to implicate stabilization of disheveled proteins. Involved in regulation of proteasomal activity at the primary cilium probably implicating association with PSDM2.","The variant of RPGRIP1L is associated with the development of retinal degeneration in individuals with ciliopathies caused by mutations in other genes. The T229-encoded protein significantly compromises the interaction between RPGRIP1L and RPGR, which leads to retinal degeneration.","Associated with the development of retinal degeneration in individuals with ciliopathies caused by mutations in other genes; found in patients with Leber congenital amaurosis, Senior-Loken syndrome, Joubert syndrome and Bardet-Biedl syndrome; abrogates interaction with RPGR. The variant of RPGRIP1L is associated with the development of retinal degeneration in individuals with ciliopathies caused by mutations in other genes. The T229-encoded protein significantly compromises the interaction between RPGRIP1L and RPGR, which leads to retinal degeneration."
104,104,89471,O54908-K217E,MMVVCAAAAVRFLAVFTMMALCSLPLLGASATLNSVLINSNAIKNLPPPLGGAGGQPGSAVSVAPGVLYEGGNKYQTLDNYQPYPCAEDEECGSDEYCSSPSRGAAGVGGVQICLACRKRRKRCMRHAMCCPGNYCKNGICMPSDHSHFPRGEIEESIIENLGNDHNAAAGDGYPRRTTLTSKIYHTKGQEGSVCLRSSDCAAGLCCARHFWSKICEPVLKEGQVCTKHKRKGSHGLEIFQRCYCGEGLACRIQKDHHQASNSSRLHTCQRH,50% reduced binding to LRP6.,,MMVVCAAAAVRFLAVFTMMALCSLPLLGASATLNSVLINSNAIKNLPPPLGGAGGQPGSAVSVAPGVLYEGGNKYQTLDNYQPYPCAEDEECGSDEYCSSPSRGAAGVGGVQICLACRKRRKRCMRHAMCCPGNYCKNGICMPSDHSHFPRGEIEESIIENLGNDHNAAAGDGYPRRTTLTSKIYHTKGQEGSVCLRSSDCAAGLCCARHFWSKICKPVLKEGQVCTKHKRKGSHGLEIFQRCYCGEGLACRIQKDHHQASNSSRLHTCQRH,Dickkopf-related protein 1,"Antagonizes canonical Wnt signaling by inhibiting LRP5/6 interaction with Wnt and by forming a ternary complex with the transmembrane protein KREMEN that promotes internalization of LRP5/6. Inhibits the pro-apoptotic function of KREMEN1 in a Wnt-independent manner, and has anti-apoptotic activity. Plays a role in limb development; attenuates Wnt signaling in the developing limb to allow normal limb patterning.","The mutation in Dkk2 may affect its interaction with the third LRP5/6 beta-propeller domain, potentially altering its binding affinity and functional role in the canonical Wnt pathway.","50% reduced binding to LRP6. The mutation in Dkk2 may affect its interaction with the third LRP5/6 beta-propeller domain, potentially altering its binding affinity and functional role in the canonical Wnt pathway."
105,105,91375,Q9UPT6-L444P,MMEIQMDEGGGVVVYQDDYCSGSVMSERVSGLAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEERESEMKKEYNALHQRHTEMIQTYVEHIERSKMQQVGGNSQTESSLPGRRKERPTSLNVFPLADGTVRAQIGGKLVPAGDHWHLSDLGQLQSSSSYQCPQDEMSESGQSSAAATPSTTGTKSNTPTSSVPSAAVTPLNESLQPLGDYGVGSKNSKRAREKRDSRNMEVQVTQEMRNVSIGMGSSDEWSDVQDIIDSTPELDMCPETRLDRTGSSPTQGIVNKAFGINTDSLYHELSTAGSEVIGDVDEGADLLGEFSVRDDFFGMGKEVGNLLLENSQLLETKNALNVVKNDPIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEAIIARREPKEEAEDVSSYLCTESDKIPMAQRRRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASREHPSVQEKKKSTIWQFFSRLFSSSSSPPPAKRPYPSVNIHYKSPTTAGFSQRRNHAMCPISAGSRPLEFFPDDDCTSSARREQKREQYRQVREHVRNDDGRLQACGWSLPAKYKQLSPNGGQEDTRMKNVPVPVYCRPLVEKDPTMKLWCAAGVNLSGWRPNEDDAGNGVKPAPGRDPLTCDREGDGEPKSAHTSPEKKKAKELPEMDATSSRVWILTSTLTTSKVVIIDANQPGTVVDQFTVCNAHVLCISSIPAASDSDYPPGEMFLDSDVNPEDPGADGVLAGITLVGCATRCNVPRSNCSSRGDTPVLDKGQGEVATIANGKVNPSQSTEEATEATEVPDPGPSEPETATLRPGPLTEHVFTDPAPTPSSGPQPGSENGPEPDSSSTRPEPEPSGDPTGAGSSAAPTMWLGAQNGWLYVHSAVANWKKCLHSIKLKDSVLSLVHVKGRVLVALADGTLAIF,In NEDBA.,,MMEIQMDEGGGVVVYQDDYCSGSVMSERVSGLAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEERESEMKKEYNALHQRHTEMIQTYVEHIERSKMQQVGGNSQTESSLPGRRKERPTSLNVFPLADGTVRAQIGGKLVPAGDHWHLSDLGQLQSSSSYQCPQDEMSESGQSSAAATPSTTGTKSNTPTSSVPSAAVTPLNESLQPLGDYGVGSKNSKRAREKRDSRNMEVQVTQEMRNVSIGMGSSDEWSDVQDIIDSTPELDMCPETRLDRTGSSPTQGIVNKAFGINTDSLYHELSTAGSEVIGDVDEGADLLGEFSVRDDFFGMGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEAIIARREPKEEAEDVSSYLCTESDKIPMAQRRRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASREHPSVQEKKKSTIWQFFSRLFSSSSSPPPAKRPYPSVNIHYKSPTTAGFSQRRNHAMCPISAGSRPLEFFPDDDCTSSARREQKREQYRQVREHVRNDDGRLQACGWSLPAKYKQLSPNGGQEDTRMKNVPVPVYCRPLVEKDPTMKLWCAAGVNLSGWRPNEDDAGNGVKPAPGRDPLTCDREGDGEPKSAHTSPEKKKAKELPEMDATSSRVWILTSTLTTSKVVIIDANQPGTVVDQFTVCNAHVLCISSIPAASDSDYPPGEMFLDSDVNPEDPGADGVLAGITLVGCATRCNVPRSNCSSRGDTPVLDKGQGEVATIANGKVNPSQSTEEATEATEVPDPGPSEPETATLRPGPLTEHVFTDPAPTPSSGPQPGSENGPEPDSSSTRPEPEPSGDPTGAGSSAAPTMWLGAQNGWLYVHSAVANWKKCLHSIKLKDSVLSLVHVKGRVLVALADGTLAIF,C-Jun-amino-terminal kinase-interacting protein 3,"The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. May function as a regulator of vesicle transport, through interactions with the JNK-signaling components and motor proteins. Promotes neuronal axon elongation in a kinesin- and JNK-dependent manner. Activates cofilin at axon tips via local activation of JNK, thereby regulating filopodial dynamics and enhancing axon elongation. Its binding to kinesin heavy chains (KHC), promotes kinesin-1 motility along microtubules and is essential for axon elongation and regeneration. Regulates cortical neuronal migration by mediating NTRK2/TRKB anterograde axonal transport during brain development. Acts as an adapter that bridges the interaction between NTRK2/TRKB and KLC1 and drives NTRK2/TRKB axonal but not dendritic anterograde transport, which is essential for subsequent BDNF-triggered signaling and filopodia formation.","The de novo variant in MAPK8IP3 has been identified in individuals presenting with an overlapping phenotype of mild to severe intellectual disability. Brain anomalies such as perisylvian polymicrogyria, cerebral or cerebellar atrophy, and hypoplasia of the corpus callosum were consistent among individuals harboring this variant.","In NEDBA. The de novo variant in MAPK8IP3 has been identified in individuals presenting with an overlapping phenotype of mild to severe intellectual disability. Brain anomalies such as perisylvian polymicrogyria, cerebral or cerebellar atrophy, and hypoplasia of the corpus callosum were consistent among individuals harboring this variant."
106,106,91693,P25522-R224A,MSDNDTIVAQATPPGRGGVGILRISGFKAREVAETVLGKLPKPRYADYLPFKDADGSVLDQGIALWFPGPNSFTGEDVLELQGHGGPVILDLLLKRILTIPGLRIARPGEFSERAFLNDKLDLAQAEAIADLIDASSEQAARSALNSLQGAFSARVNHLVEALTHLRIYVEAAIDFPDEEIDFLSDGKIEAQLNDVIADLDAVRAEARQGSLLREGMKVVIAGAPNAGKSSLLNALAGREAAIVTDIAGTTRDVLREHIHIDGMPLHIIDTAGLREASDEVERIGIERAWQEIEQADRVLFMVDGTTTDAVDPAEIWPEFIARLPAKLPITVVRNKADITGETLGMSEVNGHALIRLSARTGEGVDVLRNHLKQSMGFDTNMEGGFLARRRHLQALEQAAEHLQQGKAQLLGAWAGELLAEELRLAQQNLSEITGEFTSDDLLGRIFSSFCIGK,1.5-fold decrease in GTPase activity and almost no change in affinity.,,MSDNDTIVAQATPPGRGGVGILRISGFKAREVAETVLGKLPKPRYADYLPFKDADGSVLDQGIALWFPGPNSFTGEDVLELQGHGGPVILDLLLKRILTIPGLRIARPGEFSERAFLNDKLDLAQAEAIADLIDASSEQAARSALNSLQGAFSARVNHLVEALTHLRIYVEAAIDFPDEEIDFLSDGKIEAQLNDVIADLDAVRAEARQGSLLREGMKVVIAGRPNAGKSSLLNALAGREAAIVTDIAGTTRDVLREHIHIDGMPLHIIDTAGLREASDEVERIGIERAWQEIEQADRVLFMVDGTTTDAVDPAEIWPEFIARLPAKLPITVVRNKADITGETLGMSEVNGHALIRLSARTGEGVDVLRNHLKQSMGFDTNMEGGFLARRRHLQALEQAAEHLQQGKAQLLGAWAGELLAEELRLAQQNLSEITGEFTSDDLLGRIFSSFCIGK,tRNA modification GTPase MnmE,"Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.",,1.5-fold decrease in GTPase activity and almost no change in affinity.
107,107,92193,P15917-L69A,MNIKKEFIKVISMSCLVTAITLSGPVFIPLVQGAGGHGDVGMHVKEKEKNKDENKRKDEERNKTQEEHAKEIMKHIVKIEVKGEEAVKKEAAEKLLEKVPSDVLEMYKAIGGKIYIVDGDITKHISLEALSEDKKKIKDIYGKDALLHEHYVYAKEGYEPVLVIQSSEDYVENTEKALNVYYEIGKILSRDILSKINQPYQKFLDVLNTIKNASDSDGQDLLFTNQLKEHPTDFSVEFLEQNSNEVQEVFAKAFAYYIEPQHRDVLQLYAPEAFNYMDKFNEQEINLSLEELKDQRMLARYEKWEKIKQHYQHWSDSLSEEGRGLLKKLQIPIEPKKDDIIHSLSQEEKELLKRIQIDSSDFLSTEEKEFLKKLQIDIRDSLSEEEKELLNRIQVDSSNPLSEKEKEFLKKLKLDIQPYDINQRLQDTGGLIDSPSINLDVRKQYKRDIQNIDALLHQSIGSTLYNKIYLYENMNINNLTATLGADLVDSTDNTKINRGIFNEFKKNFKYSISSNYMIVDINERPALDNERLKWRIQLSPDTRAGYLENGKLILQRNIGLEIKDVQIIKQSEKEYIRIDAKVVPKSKIDTKIQEAQLNINQEWNKALGLPKYTKLITFNVHNRYASNIVESAYLILNEWKNNIQSDLIKKVTNYLVDGNGRFVFTDITLPNIAEQYTHQDEIYEQVHSKGLYVPESRSILLHGPSKGVELRNDSEGFIHEFGHAVDDYAGYLLDKNQSDLVTNSKKFIDIFKEEGSNLTSYGRTNEAEFFAEAFRLMHSTDHAERLKVQKNAPKTFQFINDQIKFIINS,Does not affect translocation into host cytoplasm.,,MNIKKEFIKVISMSCLVTAITLSGPVFIPLVQGAGGHGDVGMHVKEKEKNKDENKRKDEERNKTQEEHLKEIMKHIVKIEVKGEEAVKKEAAEKLLEKVPSDVLEMYKAIGGKIYIVDGDITKHISLEALSEDKKKIKDIYGKDALLHEHYVYAKEGYEPVLVIQSSEDYVENTEKALNVYYEIGKILSRDILSKINQPYQKFLDVLNTIKNASDSDGQDLLFTNQLKEHPTDFSVEFLEQNSNEVQEVFAKAFAYYIEPQHRDVLQLYAPEAFNYMDKFNEQEINLSLEELKDQRMLARYEKWEKIKQHYQHWSDSLSEEGRGLLKKLQIPIEPKKDDIIHSLSQEEKELLKRIQIDSSDFLSTEEKEFLKKLQIDIRDSLSEEEKELLNRIQVDSSNPLSEKEKEFLKKLKLDIQPYDINQRLQDTGGLIDSPSINLDVRKQYKRDIQNIDALLHQSIGSTLYNKIYLYENMNINNLTATLGADLVDSTDNTKINRGIFNEFKKNFKYSISSNYMIVDINERPALDNERLKWRIQLSPDTRAGYLENGKLILQRNIGLEIKDVQIIKQSEKEYIRIDAKVVPKSKIDTKIQEAQLNINQEWNKALGLPKYTKLITFNVHNRYASNIVESAYLILNEWKNNIQSDLIKKVTNYLVDGNGRFVFTDITLPNIAEQYTHQDEIYEQVHSKGLYVPESRSILLHGPSKGVELRNDSEGFIHEFGHAVDDYAGYLLDKNQSDLVTNSKKFIDIFKEEGSNLTSYGRTNEAEFFAEAFRLMHSTDHAERLKVQKNAPKTFQFINDQIKFIINS,Lethal factor,"Lethal factor (LF), which constitutes one of the three proteins composing the anthrax toxin, is able to trigger rapid cell death in macrophages. Acts as a protease that cleaves the N-terminal of most dual specificity mitogen-activated protein kinase kinases (MAPKKs or MAP2Ks) (except for MAP2K5): cleavage invariably occurs within the N-terminal proline-rich region preceding the kinase domain, thus disrupting a sequence involved in directing specific protein-protein interactions necessary for the assembly of signaling complexes. Also cleaves mouse Nlrp1b: host Nlrp1b cleavage promotes ubiquitination and degradation of the N-terminal part of Nlrp1b by the proteasome, thereby releasing the cleaved C-terminal part of Nlrp1b, which polymerizes and forms the Nlrp1b inflammasome followed by host cell pyroptosis. Able to cleave mouse Nlrp1b alleles 1 and 5, while it is not able to cleave Nlrp1b alleles 2, 3 and 4. In contrast, does not cleave NLRP1 human ortholog. LF is not toxic by itself and only acts as a lethal factor when associated with protective antigen (PA) to form the lethal toxin (LeTx): PA is required for LF translocation into the host cytosol.",,Does not affect translocation into host cytoplasm.
108,108,94285,P51843-E377K,MAGENHQWQGSILYNMLMSAKQTRAAPEAPETRLVDQCWGCSCGDEPGVGREGLLGGRNVALLYRCCFCGKDHPRQGSILYSMLTSAKQTYAAPKAPEATLGPCWGCSCGSDPGVGRAGLPGGRPVALLYRCCFCGEDHPRQGSILYSLLTSSKQTHVAPAAPEARPGGAWWDRSYFAQRPGGKEALPGGRATALLYRCCFCGEDHPQQGSTLYCVPTSTNQAQAAPEERPRAPWWDTSSGALRPVALKSPQVVCEAASAGLLKTLRFVKYLPCFQVLPLDQQLVLVRNCWASLLMLELAQDRLQFETVEVSEPSMLQKILTTRRRETGGNEPLPVPTLQHHLAPPAEARKVPSASQVQAIKCFLSKCWSLNISTKKYAYLKGTVLFNPDVPGLQCVKYIQGLQWGTQQILSEHTRMTHQGPHDRFIELNSTLFLLRFINANVIAELFFRPIIGTVSMDDMMLEMLCTKI,In AHC.,,MAGENHQWQGSILYNMLMSAKQTRAAPEAPETRLVDQCWGCSCGDEPGVGREGLLGGRNVALLYRCCFCGKDHPRQGSILYSMLTSAKQTYAAPKAPEATLGPCWGCSCGSDPGVGRAGLPGGRPVALLYRCCFCGEDHPRQGSILYSLLTSSKQTHVAPAAPEARPGGAWWDRSYFAQRPGGKEALPGGRATALLYRCCFCGEDHPQQGSTLYCVPTSTNQAQAAPEERPRAPWWDTSSGALRPVALKSPQVVCEAASAGLLKTLRFVKYLPCFQVLPLDQQLVLVRNCWASLLMLELAQDRLQFETVEVSEPSMLQKILTTRRRETGGNEPLPVPTLQHHLAPPAEARKVPSASQVQAIKCFLSKCWSLNISTKEYAYLKGTVLFNPDVPGLQCVKYIQGLQWGTQQILSEHTRMTHQGPHDRFIELNSTLFLLRFINANVIAELFFRPIIGTVSMDDMMLEMLCTKI,Nuclear receptor subfamily 0 group B member 1,Orphan nuclear receptor. Component of a cascade required for the development of the hypothalamic-pituitary-adrenal-gonadal axis. Acts as a coregulatory protein that inhibits the transcriptional activity of other nuclear receptors through heterodimeric interactions. May also have a role in the development of the embryo and in the maintenance of embryonic stem cell pluripotency.,The missense mutation in the putative ligand-binding domain of DAX-1 results in marked loss of repressor function.,In AHC. The missense mutation in the putative ligand-binding domain of DAX-1 results in marked loss of repressor function.
109,109,94916,Q92504-G458A,MARGLGAPHWVAVGLLTWATLGLLVAGLGGHDDLHDDLQEDFHGHSHRHSHEDFHHGHSHAHGHGHTHESIWHGHTHDHDHGHSHEDLHHGHSHGYSHESLYHRGHGHDHEHSHGGYGESGAPGIKQDLDAVTLWAYALGATVLISAAPFFVLFLIPVESNSPRHRSLLQILLSFASGGLLGDAFLHLIPHALEPHSHHTLEQPGHGHSHSGQGPILSVGLWVLSGIVAFLVVEKFVRHVKGGHGHSHGHGHAHSHTRGSHGHGRQERSTKEKQSSEEEEKETRGVQKRRGGSTVPKDGPVRPQNAEEEKRGLDLRVSGYLNLAADLAHNFTDGLAIGASFRGGRGLGILTTMTVLLHEVPHEVGDFAILVQSGCSKKQAMRLQLLTAVGALAGTACALLTEGGAVGSEIAGGAGPGWVLPFTAGGFIYVATVSVLPELLREASPLQSLLEVLGLLGAVIMMVLIAHLE,In AGM9; unknown pathological significance.,,MARGLGAPHWVAVGLLTWATLGLLVAGLGGHDDLHDDLQEDFHGHSHRHSHEDFHHGHSHAHGHGHTHESIWHGHTHDHDHGHSHEDLHHGHSHGYSHESLYHRGHGHDHEHSHGGYGESGAPGIKQDLDAVTLWAYALGATVLISAAPFFVLFLIPVESNSPRHRSLLQILLSFASGGLLGDAFLHLIPHALEPHSHHTLEQPGHGHSHSGQGPILSVGLWVLSGIVAFLVVEKFVRHVKGGHGHSHGHGHAHSHTRGSHGHGRQERSTKEKQSSEEEEKETRGVQKRRGGSTVPKDGPVRPQNAEEEKRGLDLRVSGYLNLAADLAHNFTDGLAIGASFRGGRGLGILTTMTVLLHEVPHEVGDFAILVQSGCSKKQAMRLQLLTAVGALAGTACALLTEGGAVGSEIAGGAGPGWVLPFTAGGFIYVATVSVLPELLREASPLQSLLEVLGLLGGVIMMVLIAHLE,Zinc transporter SLC39A7,"Transports Zn(2+) from the endoplasmic reticulum (ER)/Golgi apparatus to the cytosol, playing an essential role in the regulation of cytosolic zinc levels. Acts as gatekeeper of zinc release from intracellular stores, requiring post-translational activation by phosphorylation, resulting in activation of multiple downstream pathways leading to cell growth and proliferation. Has an essential role in B cell development and is required for proper B cell receptor signaling. Plays an important role in maintaining intestinal epithelial homeostasis and skin dermis development by regulating ER function. Controls cell signaling pathways involved in glucose metabolism in skeletal muscle. Has a protective role against ER stress in differents biological contexts. Mediates Zn(2+)-induced ferroptosis.",,In AGM9; unknown pathological significance.
110,110,95238,P08692-C12G,MSNITIYHNPAGGTSRNTLEMIRNSGTEPTIILYLENPPSRDELVKLIADMGISVRALLRKNVEPYEQLGLAEDKFTDDQLIDFMLQHPILINRPIVVTPLGTRLCRPSEVVLDILQDAQKGAFTKEDGEKVVDEAGKRLK,Mutant is sensitive to arsenate.,,MSNITIYHNPACGTSRNTLEMIRNSGTEPTIILYLENPPSRDELVKLIADMGISVRALLRKNVEPYEQLGLAEDKFTDDQLIDFMLQHPILINRPIVVTPLGTRLCRPSEVVLDILQDAQKGAFTKEDGEKVVDEAGKRLK,Arsenate reductase,Involved in resistance to arsenate. Catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)]. The resulting arsenite is then extruded from the cell via the ArsAB transport system (Probable).,Cells expressing the arsCC12G gene were sensitive to arsenate.,Mutant is sensitive to arsenate. Cells expressing the arsCC12G gene were sensitive to arsenate.
111,111,96226,Q2QUC5-G455D,MELTMASTMSLALLVLSAAYVLVALRRSRSSSSKPRRLPPSPPGWPVIGHLHLMSGMPHHALAELARTMRAPLFRMRLGSVPAVVISKPDLARAALTTNDAALASRPHLLSGQFLSFGCSDVTFAPAGPYHRMARRVVVSELLSARRVATYGAVRVKELRRLLAHLTKNTSPAKPVDLSECFLNLANDVLCRVAFGRRFPHGEGDKLGAVLAEAQDLFAGFTIGDFFPELEPVASTVTGLRRRLKKCLADLREACDVIVDEHISGNRQRIPGDRDEDFVDVLLRVQKSPDLEVPLTDDNLKALVLDMFVAGTDTTFATLEWVMTELVRHPRILKKAQEEVRRVVGDSGRVEESHLGELHYMRAIIKETFRLHPAVPLLVPRESVAPCTLGGYDIPARTRVFINTFAMGRDPEIWDNPLEYSPERFESAGGGGEIDLKDPDYKLLPFGGGRRGCPDYTFALATVQVSLASLLYHFEWALPAGVRAEDVNLDETFGLATRKKEPLFVAVRKSDAYEFKGEELSEV,Sekiguchi lesion phenotype.,,MELTMASTMSLALLVLSAAYVLVALRRSRSSSSKPRRLPPSPPGWPVIGHLHLMSGMPHHALAELARTMRAPLFRMRLGSVPAVVISKPDLARAALTTNDAALASRPHLLSGQFLSFGCSDVTFAPAGPYHRMARRVVVSELLSARRVATYGAVRVKELRRLLAHLTKNTSPAKPVDLSECFLNLANDVLCRVAFGRRFPHGEGDKLGAVLAEAQDLFAGFTIGDFFPELEPVASTVTGLRRRLKKCLADLREACDVIVDEHISGNRQRIPGDRDEDFVDVLLRVQKSPDLEVPLTDDNLKALVLDMFVAGTDTTFATLEWVMTELVRHPRILKKAQEEVRRVVGDSGRVEESHLGELHYMRAIIKETFRLHPAVPLLVPRESVAPCTLGGYDIPARTRVFINTFAMGRDPEIWDNPLEYSPERFESAGGGGEIDLKDPDYKLLPFGGGRRGCPGYTFALATVQVSLASLLYHFEWALPAGVRAEDVNLDETFGLATRKKEPLFVAVRKSDAYEFKGEELSEV,Tryptamine 5-hydroxylase,Involved in serotonin biosynthesis. Catalyzes the conversion of tryptamine to serotonin. Accumulation of serotonin may play a role in innate immunity.,,Sekiguchi lesion phenotype.
112,112,96487,Q9XIE6-D413A,MVRSGSFSVDSSATHQRTPSRTVTLGHIQPQAPTYRTVYCNDRESNQPVRFKGNSISTTKYNVFTFLPKGLFEQFRRIANIYFLGISCLSMTPISPVSPITNVAPLSMVLLVSLIKEAFEDWKRFQNDMSINNSTVEILQDQQWVSIPWRKLQVGDIVKIKKDGFFPADILFMSSTNSDGICYVETANLDGETNLKIRKALERTWDYLVPEKAYEFKGEIQCEQPNNSLYTFTGNLVVQKQTLPLSPDQLLLRGCSLRNTEYIVGAVVFTGHETKVMMNAMNAPSKRSTLEKKLDKLIITIFCVLVTMCLIGAIGCSIVTDREDKYLGLHNSDWEYRNGLMIGFFTFFTLVTLFSSIIPISLYVSIEMIKFIQSTQFINRDLNMYHAETNTPASARTSNLNEELGQVEYIFSAKTGTLTRNLMEFFKCSIGGVSYGCGVTEIEKGIAQRHGLKVQEEQRSTGAIREKGFNFDDPRLMRGAWRNEPNPDLCKELFRCLAICHTVLPEGDESPEKIVYQAASPDEAALVTAAKNFGFFFYRRTPTMVYVRESHVEKMGKIQDVAYEILNVLEFNSTRKRQSVVCRFPDGRLVLYCKGADNVIFERLANGMDDVRKVTREHLEHFGSSGLRTLCLAYKDLNPETYDSWNEKFIQAKSALRDREKKLDEVAELIEKDLILIGSTAIEDKLQEGVPTCIETLSRAGIKIWVLTGDKMETAINIAYACNLINNEMKQFVISSETDAIREAEERGDQVEIARVIKEEVKRELKKSLEEAQHSLHTVAGPKLSLVIDGKCLMYALDPSLRVMLLSLSLNCTSVVCCRVSPLQKAQVTSLVRKGAQKITLSIGDGANDVSMIQAAHVGIGISGMEGMQAVMASDFAIAQFRFLTDLLLVHGRWSYLRICKVVMYFFYKNLTFTLTQFWFTFRTGFSGQRFYDDWFQSLFNVVFTALPVIVLGLFEKDVSASLSKRYPELYREGIRNSFFKWRVVAVWATSAVYQSLVCYLFVTTSSFGAVNSSGKVFGLWDVS,Loss of internalization of phospholipids.,,MVRSGSFSVDSSATHQRTPSRTVTLGHIQPQAPTYRTVYCNDRESNQPVRFKGNSISTTKYNVFTFLPKGLFEQFRRIANIYFLGISCLSMTPISPVSPITNVAPLSMVLLVSLIKEAFEDWKRFQNDMSINNSTVEILQDQQWVSIPWRKLQVGDIVKIKKDGFFPADILFMSSTNSDGICYVETANLDGETNLKIRKALERTWDYLVPEKAYEFKGEIQCEQPNNSLYTFTGNLVVQKQTLPLSPDQLLLRGCSLRNTEYIVGAVVFTGHETKVMMNAMNAPSKRSTLEKKLDKLIITIFCVLVTMCLIGAIGCSIVTDREDKYLGLHNSDWEYRNGLMIGFFTFFTLVTLFSSIIPISLYVSIEMIKFIQSTQFINRDLNMYHAETNTPASARTSNLNEELGQVEYIFSDKTGTLTRNLMEFFKCSIGGVSYGCGVTEIEKGIAQRHGLKVQEEQRSTGAIREKGFNFDDPRLMRGAWRNEPNPDLCKELFRCLAICHTVLPEGDESPEKIVYQAASPDEAALVTAAKNFGFFFYRRTPTMVYVRESHVEKMGKIQDVAYEILNVLEFNSTRKRQSVVCRFPDGRLVLYCKGADNVIFERLANGMDDVRKVTREHLEHFGSSGLRTLCLAYKDLNPETYDSWNEKFIQAKSALRDREKKLDEVAELIEKDLILIGSTAIEDKLQEGVPTCIETLSRAGIKIWVLTGDKMETAINIAYACNLINNEMKQFVISSETDAIREAEERGDQVEIARVIKEEVKRELKKSLEEAQHSLHTVAGPKLSLVIDGKCLMYALDPSLRVMLLSLSLNCTSVVCCRVSPLQKAQVTSLVRKGAQKITLSIGDGANDVSMIQAAHVGIGISGMEGMQAVMASDFAIAQFRFLTDLLLVHGRWSYLRICKVVMYFFYKNLTFTLTQFWFTFRTGFSGQRFYDDWFQSLFNVVFTALPVIVLGLFEKDVSASLSKRYPELYREGIRNSFFKWRVVAVWATSAVYQSLVCYLFVTTSSFGAVNSSGKVFGLWDVS,Phospholipid-transporting ATPase 3,"Involved in transport of phospholipids. Contributes to transmembrane flipping of lipids. Required for secretory processes during plant development. Requires an interaction with an ALIS protein for activity. Has activity with phosphatidylserine, phosphatidylcholine and phosphatidylethanolamine, but not with lysolipid. Modifies endomembranes in multiple cell types, enabling structural changes, or signaling functions that are critical for normal development and adaptation to varied growth environments. Required for the trafficking and endocytic recycling of ABCG36/PEN3 between the trans-Golgi network and the plasma membrane; thus promoting ABCG36/PEN3 recruitment to the host-pathogen interface upon infection by powdery mildews (e.g. Blumeria graminis) and bacteria (e.g. Pseudomonas syringae), or upon the detection of pathogen-associated molecular patterns (PAMPs) (e.g. flg22 and chitin).","Mutations of ALA3 result in impaired growth of roots and shoots. The growth defect is accompanied by failure of the root cap to release border cells involved in the secretion of molecules required for efficient root interaction with the environment, and ala3 mutants are devoid of the characteristic trans-Golgi proliferation of slime vesicles containing polysaccharides and enzymes for secretion.","Loss of internalization of phospholipids. Mutations of ALA3 result in impaired growth of roots and shoots. The growth defect is accompanied by failure of the root cap to release border cells involved in the secretion of molecules required for efficient root interaction with the environment, and ala3 mutants are devoid of the characteristic trans-Golgi proliferation of slime vesicles containing polysaccharides and enzymes for secretion."
113,113,97240,Q9IK90-K258R,MEPDIKSISSESMEGVSDFSPSSWEHGGYLDKVEPEIDENGSMIPKYKIYTPGANERKYNNYMYLICYGFVEDVERTPETGKRKKIRTIAAYPLGVGKSASHPQDLLEELCSLKVTVRRTAGSTEKIVFGSSGPLNHLVPWKKVLTSGSIFNAVKVCRNVDQIQLDKHQALRIFFLSITKLNDSGIYMIPRTMLEFRRNNAIAFNLLVYLKIDADLSKMGIQGSLDKDGFKVASFMLHLGNFVRRAGKYYSVDYCRRRIDRMKLQFSLGSIGGLSLHIKINGVISKRLFAQMGFQKNLCFSLMDINPWLNRLTWNNSCEISRVAAVLQPSIPREFMIYDDVFIDNTGRILKG,Complete loss of membrane association and budding.,,MEPDIKSISSESMEGVSDFSPSSWEHGGYLDKVEPEIDENGSMIPKYKIYTPGANERKYNNYMYLICYGFVEDVERTPETGKRKKIRTIAAYPLGVGKSASHPQDLLEELCSLKVTVRRTAGSTEKIVFGSSGPLNHLVPWKKVLTSGSIFNAVKVCRNVDQIQLDKHQALRIFFLSITKLNDSGIYMIPRTMLEFRRNNAIAFNLLVYLKIDADLSKMGIQGSLDKDGFKVASFMLHLGNFVRRAGKYYSVDYCRRKIDRMKLQFSLGSIGGLSLHIKINGVISKRLFAQMGFQKNLCFSLMDINPWLNRLTWNNSCEISRVAAVLQPSIPREFMIYDDVFIDNTGRILKG,Matrix protein,Plays a crucial role in virion assembly and budding. Forms a shell at the inner face of the plasma membrane. Transits through the host nucleus before gaining the functional ability to localize and bud from the plasma membrane. Mediates together with fusion protein the incorporation of the glycoprotein to the viral particles. Participates also in the inhibition of the host interferon type I antiviral response by interacting with and thereby inhibiting host TRIM6.,"Mutations at site in the NiV-M protein impaired its nuclear-cytoplasmic trafficking and abolished NiV-M budding. The lysine residue at this site serves dual functions: its positive charge is important for mediating nuclear import, and it is also a potential site for monoubiquitination which regulates nuclear export of the protein.","Complete loss of membrane association and budding. Mutations at site in the NiV-M protein impaired its nuclear-cytoplasmic trafficking and abolished NiV-M budding. The lysine residue at this site serves dual functions: its positive charge is important for mediating nuclear import, and it is also a potential site for monoubiquitination which regulates nuclear export of the protein."
114,114,97361,P15917-D220A,MNIKKEFIKVISMSCLVTAITLSGPVFIPLVQGAGGHGDVGMHVKEKEKNKDENKRKDEERNKTQEEHLKEIMKHIVKIEVKGEEAVKKEAAEKLLEKVPSDVLEMYKAIGGKIYIVDGDITKHISLEALSEDKKKIKDIYGKDALLHEHYVYAKEGYEPVLVIQSSEDYVENTEKALNVYYEIGKILSRDILSKINQPYQKFLDVLNTIKNASDSDGQALLFTNQLKEHPTDFSVEFLEQNSNEVQEVFAKAFAYYIEPQHRDVLQLYAPEAFNYMDKFNEQEINLSLEELKDQRMLARYEKWEKIKQHYQHWSDSLSEEGRGLLKKLQIPIEPKKDDIIHSLSQEEKELLKRIQIDSSDFLSTEEKEFLKKLQIDIRDSLSEEEKELLNRIQVDSSNPLSEKEKEFLKKLKLDIQPYDINQRLQDTGGLIDSPSINLDVRKQYKRDIQNIDALLHQSIGSTLYNKIYLYENMNINNLTATLGADLVDSTDNTKINRGIFNEFKKNFKYSISSNYMIVDINERPALDNERLKWRIQLSPDTRAGYLENGKLILQRNIGLEIKDVQIIKQSEKEYIRIDAKVVPKSKIDTKIQEAQLNINQEWNKALGLPKYTKLITFNVHNRYASNIVESAYLILNEWKNNIQSDLIKKVTNYLVDGNGRFVFTDITLPNIAEQYTHQDEIYEQVHSKGLYVPESRSILLHGPSKGVELRNDSEGFIHEFGHAVDDYAGYLLDKNQSDLVTNSKKFIDIFKEEGSNLTSYGRTNEAEFFAEAFRLMHSTDHAERLKVQKNAPKTFQFINDQIKFIINS,Loss of ability to bind to PA and loss of toxicity.,,MNIKKEFIKVISMSCLVTAITLSGPVFIPLVQGAGGHGDVGMHVKEKEKNKDENKRKDEERNKTQEEHLKEIMKHIVKIEVKGEEAVKKEAAEKLLEKVPSDVLEMYKAIGGKIYIVDGDITKHISLEALSEDKKKIKDIYGKDALLHEHYVYAKEGYEPVLVIQSSEDYVENTEKALNVYYEIGKILSRDILSKINQPYQKFLDVLNTIKNASDSDGQDLLFTNQLKEHPTDFSVEFLEQNSNEVQEVFAKAFAYYIEPQHRDVLQLYAPEAFNYMDKFNEQEINLSLEELKDQRMLARYEKWEKIKQHYQHWSDSLSEEGRGLLKKLQIPIEPKKDDIIHSLSQEEKELLKRIQIDSSDFLSTEEKEFLKKLQIDIRDSLSEEEKELLNRIQVDSSNPLSEKEKEFLKKLKLDIQPYDINQRLQDTGGLIDSPSINLDVRKQYKRDIQNIDALLHQSIGSTLYNKIYLYENMNINNLTATLGADLVDSTDNTKINRGIFNEFKKNFKYSISSNYMIVDINERPALDNERLKWRIQLSPDTRAGYLENGKLILQRNIGLEIKDVQIIKQSEKEYIRIDAKVVPKSKIDTKIQEAQLNINQEWNKALGLPKYTKLITFNVHNRYASNIVESAYLILNEWKNNIQSDLIKKVTNYLVDGNGRFVFTDITLPNIAEQYTHQDEIYEQVHSKGLYVPESRSILLHGPSKGVELRNDSEGFIHEFGHAVDDYAGYLLDKNQSDLVTNSKKFIDIFKEEGSNLTSYGRTNEAEFFAEAFRLMHSTDHAERLKVQKNAPKTFQFINDQIKFIINS,Lethal factor,"Lethal factor (LF), which constitutes one of the three proteins composing the anthrax toxin, is able to trigger rapid cell death in macrophages. Acts as a protease that cleaves the N-terminal of most dual specificity mitogen-activated protein kinase kinases (MAPKKs or MAP2Ks) (except for MAP2K5): cleavage invariably occurs within the N-terminal proline-rich region preceding the kinase domain, thus disrupting a sequence involved in directing specific protein-protein interactions necessary for the assembly of signaling complexes. Also cleaves mouse Nlrp1b: host Nlrp1b cleavage promotes ubiquitination and degradation of the N-terminal part of Nlrp1b by the proteasome, thereby releasing the cleaved C-terminal part of Nlrp1b, which polymerizes and forms the Nlrp1b inflammasome followed by host cell pyroptosis. Able to cleave mouse Nlrp1b alleles 1 and 5, while it is not able to cleave Nlrp1b alleles 2, 3 and 4. In contrast, does not cleave NLRP1 human ortholog. LF is not toxic by itself and only acts as a lethal factor when associated with protective antigen (PA) to form the lethal toxin (LeTx): PA is required for LF translocation into the host cytosol.",mutation in lethal factor is non-toxic in combination with protective antigen. Its protective antigen-binding ability is drastically reduced. D220 is crucial for the expression of anthrax lethal toxin activity.,Loss of ability to bind to PA and loss of toxicity. mutation in lethal factor is non-toxic in combination with protective antigen. Its protective antigen-binding ability is drastically reduced. D220 is crucial for the expression of anthrax lethal toxin activity.
115,115,98425,P56868-E147N,MKIGIFDSGVGGLTVLKAIRNRYRKVDIVYLGDTARVPYGIRSKDTIIRYSLECAGFLKDKGVDIIVVACNTASAYALERLKKEINVPVFGVIEPGVKEALKKSRNKKIGVIGTPATVKSGAYQRKLEEGGADVFAKACPLFVPLANEGLLEGEITRKVVEHYLKEFKGKIDTLILGCTHYPLLKKEIKKFLGDVEVVDSSEALSLSLHNFIKDDGSSSLELFFTDLSPNLQFLIKLILGRDYPVKLAEGVFTH,Strongly reduced catalytic activity.,,MKIGIFDSGVGGLTVLKAIRNRYRKVDIVYLGDTARVPYGIRSKDTIIRYSLECAGFLKDKGVDIIVVACNTASAYALERLKKEINVPVFGVIEPGVKEALKKSRNKKIGVIGTPATVKSGAYQRKLEEGGADVFAKACPLFVPLAEEGLLEGEITRKVVEHYLKEFKGKIDTLILGCTHYPLLKKEIKKFLGDVEVVDSSEALSLSLHNFIKDDGSSSLELFFTDLSPNLQFLIKLILGRDYPVKLAEGVFTH,Glutamate racemase,"Provides the (R)-glutamate required for cell wall biosynthesis. Converts L- or D-glutamate to D- or L-glutamate, respectively, but not other amino acids such as alanine, aspartate, and glutamine.",,Strongly reduced catalytic activity.
116,116,99609,P67812-D122N,MLSLDFLDDVRRMNKRQLYYQVLNFGMIVSSALMIWKGLMVITGSESPIVVVLSGSMEPAFHRGDLLFLTNRVEDPIRVGEIVVFRIEGREIPIVHRVLKIHEKQNGHIKFLTKGDNNAVDNRGLYKQGQHWLEKKDVVGRARGFVPYIGIVTILMNDYPKFKYAVLFLLGLFVLVHRE,Loss of catalytic activity. Slight reduction in protein stability.,,MLSLDFLDDVRRMNKRQLYYQVLNFGMIVSSALMIWKGLMVITGSESPIVVVLSGSMEPAFHRGDLLFLTNRVEDPIRVGEIVVFRIEGREIPIVHRVLKIHEKQNGHIKFLTKGDNNAVDDRGLYKQGQHWLEKKDVVGRARGFVPYIGIVTILMNDYPKFKYAVLFLLGLFVLVHRE,Signal peptidase complex catalytic subunit SEC11A,Catalytic component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum. Specifically cleaves N-terminal signal peptides that contain a hydrophobic alpha-helix (h-region) shorter than 18-20 amino acids.,,Loss of catalytic activity. Slight reduction in protein stability.
117,117,100085,P05109-C42A,MLTELEKALNSIIDVYHKYSLIKGNFHAVYRDDLKKLLETEAPQYIRKKGADVWFKELDINTDGAVNFQEFLILVIKMGVAAHKKSHEESHKE,Loss of antifungal activity.,,MLTELEKALNSIIDVYHKYSLIKGNFHAVYRDDLKKLLETECPQYIRKKGADVWFKELDINTDGAVNFQEFLILVIKMGVAAHKKSHEESHKE,Protein S100-A8,"S100A8 is a calcium- and zinc-binding protein which plays a prominent role in the regulation of inflammatory processes and immune response. It can induce neutrophil chemotaxis and adhesion. Predominantly found as calprotectin (S100A8/A9) which has a wide plethora of intra- and extracellular functions. The intracellular functions include: facilitating leukocyte arachidonic acid trafficking and metabolism, modulation of the tubulin-dependent cytoskeleton during migration of phagocytes and activation of the neutrophilic NADPH-oxidase. Activates NADPH-oxidase by facilitating the enzyme complex assembly at the cell membrane, transferring arachidonic acid, an essential cofactor, to the enzyme complex and S100A8 contributes to the enzyme assembly by directly binding to NCF2/P67PHOX. The extracellular functions involve pro-inflammatory, antimicrobial, oxidant-scavenging and apoptosis-inducing activities. Its pro-inflammatory activity includes recruitment of leukocytes, promotion of cytokine and chemokine production, and regulation of leukocyte adhesion and migration. Acts as an alarmin or a danger associated molecular pattern (DAMP) molecule and stimulates innate immune cells via binding to pattern recognition receptors such as Toll-like receptor 4 (TLR4) and receptor for advanced glycation endproducts (AGER). Binding to TLR4 and AGER activates the MAP-kinase and NF-kappa-B signaling pathways resulting in the amplification of the pro-inflammatory cascade. Has antimicrobial activity towards bacteria and fungi and exerts its antimicrobial activity probably via chelation of Zn(2+) which is essential for microbial growth. Can induce cell death via autophagy and apoptosis and this occurs through the cross-talk of mitochondria and lysosomes via reactive oxygen species (ROS) and the process involves BNIP3. Can regulate neutrophil number and apoptosis by an anti-apoptotic effect; regulates cell survival via ITGAM/ITGB and TLR4 and a signaling mechanism involving MEK-ERK. Its role as an oxidant scavenger has a protective role in preventing exaggerated tissue damage by scavenging oxidants. Can act as a potent amplifier of inflammation in autoimmunity as well as in cancer development and tumor spread. The iNOS-S100A8/A9 transnitrosylase complex directs selective inflammatory stimulus-dependent S-nitrosylation of GAPDH and probably multiple targets such as ANXA5, EZR, MSN and VIM by recognizing a [IL]-x-C-x-x-[DE] motif; S100A8 seems to contribute to S-nitrosylation site selectivity.(Microbial infection) Upon infection by human coronavirus SARS-CoV-2, may induce expansion of aberrant immature neutrophils in a TLR4-dependent manner.",Substitution of cysteine 42 of S100A8 caused a loss of S100A8's ability to enhance S100A9's antifungal effect.,Loss of antifungal activity. Substitution of cysteine 42 of S100A8 caused a loss of S100A8's ability to enhance S100A9's antifungal effect.
118,118,100719,Q6UWV6-R271E,MRGPAVLLTVALATLLAPGAGAPVQSQGSQNKLLLVSFDGFRWNYDQDVDTPNLDAMARDGVKARYMTPAFVTMTSPCHFTLVTGKYIENHGVVHNMYYNTTSKVKLPYHATLGIQRWWDNGSVPIWITAQRQGLRAGSFFYPGGNVTYQGVAVTRSRKEGIAHNYKNETEWRANIDTVMAWFTEEDLDLVTLYFGEPDSTGHRYGPESPERREMVRQVDRTVGYLRESIARNHLTDRLNLIITSDHGMTTVDKRAGDLVEFHKFPNFTFEDIEFELLDYGPNGMLLPKEGRLEKVYDALKDAHPKLHVYKKEAFPEAFHYANNPRVTPLLMYSDLGYVIHGRINVQFNNGEHGFDNKDMDMKTIFRAVGPSFRAGLEVEPFESVHVYELMCRLLGIVPEANDGHLATLLPMLHTESALPPDGRPTLLPKGRSALPPSSRPLLVMGLLGTVILLSEVA,Decreased enzyme activity; when associated with E-343.,,MRGPAVLLTVALATLLAPGAGAPVQSQGSQNKLLLVSFDGFRWNYDQDVDTPNLDAMARDGVKARYMTPAFVTMTSPCHFTLVTGKYIENHGVVHNMYYNTTSKVKLPYHATLGIQRWWDNGSVPIWITAQRQGLRAGSFFYPGGNVTYQGVAVTRSRKEGIAHNYKNETEWRANIDTVMAWFTEEDLDLVTLYFGEPDSTGHRYGPESPERREMVRQVDRTVGYLRESIARNHLTDRLNLIITSDHGMTTVDKRAGDLVEFHKFPNFTFRDIEFELLDYGPNGMLLPKEGRLEKVYDALKDAHPKLHVYKKEAFPEAFHYANNPRVTPLLMYSDLGYVIHGRINVQFNNGEHGFDNKDMDMKTIFRAVGPSFRAGLEVEPFESVHVYELMCRLLGIVPEANDGHLATLLPMLHTESALPPDGRPTLLPKGRSALPPSSRPLLVMGLLGTVILLSEVA,Ectonucleotide pyrophosphatase/phosphodiesterase family member 7,"Choline-specific phosphodiesterase that hydrolyzes sphingomyelin releasing the ceramide and phosphocholine and therefore is involved in sphingomyelin digestion, ceramide formation, and fatty acid (FA) absorption in the gastrointestinal tract. Has also phospholipase C activity and can also cleave phosphocholine from palmitoyl lyso-phosphatidylcholine and platelet-activating factor (PAF) leading to its inactivation. Does not have nucleotide pyrophosphatase activity. May promote cholesterol absorption by affecting the levels of sphingomyelin derived from either diet or endogenous sources, in the intestinal lumen.",,Decreased enzyme activity; when associated with E-343.
119,119,101793,P51843-I439S,MAGENHQWQGSILYNMLMSAKQTRAAPEAPETRLVDQCWGCSCGDEPGVGREGLLGGRNVALLYRCCFCGKDHPRQGSILYSMLTSAKQTYAAPKAPEATLGPCWGCSCGSDPGVGRAGLPGGRPVALLYRCCFCGEDHPRQGSILYSLLTSSKQTHVAPAAPEARPGGAWWDRSYFAQRPGGKEALPGGRATALLYRCCFCGEDHPQQGSTLYCVPTSTNQAQAAPEERPRAPWWDTSSGALRPVALKSPQVVCEAASAGLLKTLRFVKYLPCFQVLPLDQQLVLVRNCWASLLMLELAQDRLQFETVEVSEPSMLQKILTTRRRETGGNEPLPVPTLQHHLAPPAEARKVPSASQVQAIKCFLSKCWSLNISTKEYAYLKGTVLFNPDVPGLQCVKYIQGLQWGTQQILSEHTRMTHQGPHDRFIELNSTLFLLRFSNANVIAELFFRPIIGTVSMDDMMLEMLCTKI,In AHC; mild phenotype.,,MAGENHQWQGSILYNMLMSAKQTRAAPEAPETRLVDQCWGCSCGDEPGVGREGLLGGRNVALLYRCCFCGKDHPRQGSILYSMLTSAKQTYAAPKAPEATLGPCWGCSCGSDPGVGRAGLPGGRPVALLYRCCFCGEDHPRQGSILYSLLTSSKQTHVAPAAPEARPGGAWWDRSYFAQRPGGKEALPGGRATALLYRCCFCGEDHPQQGSTLYCVPTSTNQAQAAPEERPRAPWWDTSSGALRPVALKSPQVVCEAASAGLLKTLRFVKYLPCFQVLPLDQQLVLVRNCWASLLMLELAQDRLQFETVEVSEPSMLQKILTTRRRETGGNEPLPVPTLQHHLAPPAEARKVPSASQVQAIKCFLSKCWSLNISTKEYAYLKGTVLFNPDVPGLQCVKYIQGLQWGTQQILSEHTRMTHQGPHDRFIELNSTLFLLRFINANVIAELFFRPIIGTVSMDDMMLEMLCTKI,Nuclear receptor subfamily 0 group B member 1,Orphan nuclear receptor. Component of a cascade required for the development of the hypothalamic-pituitary-adrenal-gonadal axis. Acts as a coregulatory protein that inhibits the transcriptional activity of other nuclear receptors through heterodimeric interactions. May also have a role in the development of the embryo and in the maintenance of embryonic stem cell pluripotency.,"The mutation conferred intermediate levels of repressor activity of DAX-1 when compared with mutations associated with classic AHC. This unique case extends the clinical spectrum of AHC to include delayed-onset primary adrenal insufficiency in adulthood and milder forms of HHG. Furthermore, in accordance with findings in Ahch (Dax1) knockout mice, the clinical features in this patient suggest that DAX-1 function is required for spermatogenesis in humans, independent of its known effects on gonadotropin production.","In AHC; mild phenotype. The mutation conferred intermediate levels of repressor activity of DAX-1 when compared with mutations associated with classic AHC. This unique case extends the clinical spectrum of AHC to include delayed-onset primary adrenal insufficiency in adulthood and milder forms of HHG. Furthermore, in accordance with findings in Ahch (Dax1) knockout mice, the clinical features in this patient suggest that DAX-1 function is required for spermatogenesis in humans, independent of its known effects on gonadotropin production."
120,120,102315,P21926-C87A,MPVKGGTKCIKYLLFGFNFIFWLAGIAVLAIGLWLRFDSQTKSIFEQETNNNNSSFYTGVYILIGAGALMMLVGFLGCCGAVQESQAMLGLFFGFLLVIFAIEIAAAIWGYSHKDEVIKEVQEFYKDTYNKLKTKDEPQRETLKAIHYALNCCGLAGGVEQFISDICPKKDVLETFTVKSCPDAIKEVFDNKFHIIGAVGIGIAVVMIFGMIFSMILCCAIRRNREMV,Loss of palmitoylation; when associated with A-9; A-78; A-79; A-218 and A-219.,,MPVKGGTKCIKYLLFGFNFIFWLAGIAVLAIGLWLRFDSQTKSIFEQETNNNNSSFYTGVYILIGAGALMMLVGFLGCCGAVQESQCMLGLFFGFLLVIFAIEIAAAIWGYSHKDEVIKEVQEFYKDTYNKLKTKDEPQRETLKAIHYALNCCGLAGGVEQFISDICPKKDVLETFTVKSCPDAIKEVFDNKFHIIGAVGIGIAVVMIFGMIFSMILCCAIRRNREMV,CD9 antigen,"Integral membrane protein associated with integrins, which regulates different processes, such as sperm-egg fusion, platelet activation and aggregation, and cell adhesion. Present at the cell surface of oocytes and plays a key role in sperm-egg fusion, possibly by organizing multiprotein complexes and the morphology of the membrane required for the fusion. In myoblasts, associates with CD81 and PTGFRN and inhibits myotube fusion during muscle regeneration. In macrophages, associates with CD81 and beta-1 and beta-2 integrins, and prevents macrophage fusion into multinucleated giant cells specialized in ingesting complement-opsonized large particles. Also prevents the fusion between mononuclear cell progenitors into osteoclasts in charge of bone resorption. Acts as a receptor for PSG17. Involved in platelet activation and aggregation. Regulates paranodal junction formation. Involved in cell adhesion, cell motility and tumor metastasis.",,Loss of palmitoylation; when associated with A-9; A-78; A-79; A-218 and A-219.
121,121,103142,P15917-L221A,MNIKKEFIKVISMSCLVTAITLSGPVFIPLVQGAGGHGDVGMHVKEKEKNKDENKRKDEERNKTQEEHLKEIMKHIVKIEVKGEEAVKKEAAEKLLEKVPSDVLEMYKAIGGKIYIVDGDITKHISLEALSEDKKKIKDIYGKDALLHEHYVYAKEGYEPVLVIQSSEDYVENTEKALNVYYEIGKILSRDILSKINQPYQKFLDVLNTIKNASDSDGQDALFTNQLKEHPTDFSVEFLEQNSNEVQEVFAKAFAYYIEPQHRDVLQLYAPEAFNYMDKFNEQEINLSLEELKDQRMLARYEKWEKIKQHYQHWSDSLSEEGRGLLKKLQIPIEPKKDDIIHSLSQEEKELLKRIQIDSSDFLSTEEKEFLKKLQIDIRDSLSEEEKELLNRIQVDSSNPLSEKEKEFLKKLKLDIQPYDINQRLQDTGGLIDSPSINLDVRKQYKRDIQNIDALLHQSIGSTLYNKIYLYENMNINNLTATLGADLVDSTDNTKINRGIFNEFKKNFKYSISSNYMIVDINERPALDNERLKWRIQLSPDTRAGYLENGKLILQRNIGLEIKDVQIIKQSEKEYIRIDAKVVPKSKIDTKIQEAQLNINQEWNKALGLPKYTKLITFNVHNRYASNIVESAYLILNEWKNNIQSDLIKKVTNYLVDGNGRFVFTDITLPNIAEQYTHQDEIYEQVHSKGLYVPESRSILLHGPSKGVELRNDSEGFIHEFGHAVDDYAGYLLDKNQSDLVTNSKKFIDIFKEEGSNLTSYGRTNEAEFFAEAFRLMHSTDHAERLKVQKNAPKTFQFINDQIKFIINS,No effect on PA-binding ability and fully toxic.,,MNIKKEFIKVISMSCLVTAITLSGPVFIPLVQGAGGHGDVGMHVKEKEKNKDENKRKDEERNKTQEEHLKEIMKHIVKIEVKGEEAVKKEAAEKLLEKVPSDVLEMYKAIGGKIYIVDGDITKHISLEALSEDKKKIKDIYGKDALLHEHYVYAKEGYEPVLVIQSSEDYVENTEKALNVYYEIGKILSRDILSKINQPYQKFLDVLNTIKNASDSDGQDLLFTNQLKEHPTDFSVEFLEQNSNEVQEVFAKAFAYYIEPQHRDVLQLYAPEAFNYMDKFNEQEINLSLEELKDQRMLARYEKWEKIKQHYQHWSDSLSEEGRGLLKKLQIPIEPKKDDIIHSLSQEEKELLKRIQIDSSDFLSTEEKEFLKKLQIDIRDSLSEEEKELLNRIQVDSSNPLSEKEKEFLKKLKLDIQPYDINQRLQDTGGLIDSPSINLDVRKQYKRDIQNIDALLHQSIGSTLYNKIYLYENMNINNLTATLGADLVDSTDNTKINRGIFNEFKKNFKYSISSNYMIVDINERPALDNERLKWRIQLSPDTRAGYLENGKLILQRNIGLEIKDVQIIKQSEKEYIRIDAKVVPKSKIDTKIQEAQLNINQEWNKALGLPKYTKLITFNVHNRYASNIVESAYLILNEWKNNIQSDLIKKVTNYLVDGNGRFVFTDITLPNIAEQYTHQDEIYEQVHSKGLYVPESRSILLHGPSKGVELRNDSEGFIHEFGHAVDDYAGYLLDKNQSDLVTNSKKFIDIFKEEGSNLTSYGRTNEAEFFAEAFRLMHSTDHAERLKVQKNAPKTFQFINDQIKFIINS,Lethal factor,"Lethal factor (LF), which constitutes one of the three proteins composing the anthrax toxin, is able to trigger rapid cell death in macrophages. Acts as a protease that cleaves the N-terminal of most dual specificity mitogen-activated protein kinase kinases (MAPKKs or MAP2Ks) (except for MAP2K5): cleavage invariably occurs within the N-terminal proline-rich region preceding the kinase domain, thus disrupting a sequence involved in directing specific protein-protein interactions necessary for the assembly of signaling complexes. Also cleaves mouse Nlrp1b: host Nlrp1b cleavage promotes ubiquitination and degradation of the N-terminal part of Nlrp1b by the proteasome, thereby releasing the cleaved C-terminal part of Nlrp1b, which polymerizes and forms the Nlrp1b inflammasome followed by host cell pyroptosis. Able to cleave mouse Nlrp1b alleles 1 and 5, while it is not able to cleave Nlrp1b alleles 2, 3 and 4. In contrast, does not cleave NLRP1 human ortholog. LF is not toxic by itself and only acts as a lethal factor when associated with protective antigen (PA) to form the lethal toxin (LeTx): PA is required for LF translocation into the host cytosol.",,No effect on PA-binding ability and fully toxic.
122,122,103405,P16522-G213D,MNDDSQDKIIHDIRIQLRKAATELSRWKLYGSSKWAAEALAGLAEAIDVDQTHSLADESPLRNKQGVPKQMFEIPQNGFGLSETEYDLYLLGSTLFDAKEFDRCVFFLKDVTNPYLKFLKLYSKFLSWDKKSQESMENILTTGKFTDEMYRANKDGDGSGNEDINQSGHQRANLKMVSNEHESQSNISSILKEINTFLESYEIKIDDDEADLDLALLYYLRGVILKQEKNISKAMSSFLKSLSCYSFNWSCWLELMDCLQKVDDALLLNNYLYQNFQFKFSENLGSQRTIEFNIMIKFFKLKVFEELNGQLEDYFEDLEFLLQVFPNFTFLKAYNATISYNNLDYVTAESRFDDIVKQDPYRLNDLETYSNILYVMQKNSKLAYLAQFVSQIDRFRPETCCIIANYYSARQEHEKSIMYFRRALTLDKKTTNAWTLMGHEFVELSNSHAAIECYRRAVDICPRDFKAWFGLGQAYALLDMHLYSLYYFQKACTLKPWDRRIWQVLGECYSKTGNKVEAIKCYKRSIKASQTVDQNTSIYYRLAQLYEELEDLQECKKFMMKCVDVEELLEGIVTDETVKARLWLAIFEIKAGNYQLAYDYAMGVSSGTSQEIEEARMLARECRRHM,In CDC23-47; G2/M cell cycle arrest at 37 degrees Celsius; when associated with W-583.,,MNDDSQDKIIHDIRIQLRKAATELSRWKLYGSSKWAAEALAGLAEAIDVDQTHSLADESPLRNKQGVPKQMFEIPQNGFGLSETEYDLYLLGSTLFDAKEFDRCVFFLKDVTNPYLKFLKLYSKFLSWDKKSQESMENILTTGKFTDEMYRANKDGDGSGNEDINQSGHQRANLKMVSNEHESQSNISSILKEINTFLESYEIKIDDDEADLGLALLYYLRGVILKQEKNISKAMSSFLKSLSCYSFNWSCWLELMDCLQKVDDALLLNNYLYQNFQFKFSENLGSQRTIEFNIMIKFFKLKVFEELNGQLEDYFEDLEFLLQVFPNFTFLKAYNATISYNNLDYVTAESRFDDIVKQDPYRLNDLETYSNILYVMQKNSKLAYLAQFVSQIDRFRPETCCIIANYYSARQEHEKSIMYFRRALTLDKKTTNAWTLMGHEFVELSNSHAAIECYRRAVDICPRDFKAWFGLGQAYALLDMHLYSLYYFQKACTLKPWDRRIWQVLGECYSKTGNKVEAIKCYKRSIKASQTVDQNTSIYYRLAQLYEELEDLQECKKFMMKCVDVEELLEGIVTDETVKARLWLAIFEIKAGNYQLAYDYAMGVSSGTSQEIEEARMLARECRRHM,Anaphase-promoting complex subunit CDC23,"Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. In early mitosis, the APC/C is activated by CDC20 and targets securin PDS1, the B-type cyclin CLB5, and other anaphase inhibitory proteins for proteolysis, thereby triggering the separation of sister chromatids at the metaphase-to-anaphase transition. In late mitosis and in G1, degradation of CLB5 allows activation of the APC/C by CDH1, which is needed to destroy CDC20 and the B-type cyclin CLB2 to allow exit from mitosis and creating the low CDK state necessary for cytokinesis and for reforming prereplicative complexes in G1 prior to another round of replication.",The mutation in the CDC23 gene causes a single amino acid change in the protein. This mutation is found within a mutable domain of CDC23 and may affect its function or stability.,In CDC23-47; G2/M cell cycle arrest at 37 degrees Celsius; when associated with W-583. The mutation in the CDC23 gene causes a single amino acid change in the protein. This mutation is found within a mutable domain of CDC23 and may affect its function or stability.
123,123,103628,Q07181-K269E,MVRNIVSRLCSQLFALPSSSLQERDPCSVTEYSGLATAVSSCKNIVLNGFQVPTGKQLDLSSLQNDSTVTFKGTTTFATTADNDFNPIVISGSNITITGASGHVIDGNGQAYWDGKGSNSNSNQKPDHFIVVQKTTGNSKITNLNIQNWPVHCFDITGSSQLTISGLILDNRAGDKPNAKSGSLPAAHNTDGFDISSSDHVTLDNNHVYNQDDCVAVTSGTNIVVSNMYCSGGHGLSIGSVGGKSDNVVDGVQFLSSQVVNSQNGCRIESNSGATGTINNVTYQNIALTNISTYGVDVQQDYLNGGPTGKPTNGVKISNIKFIKVTGTVASSAQDWFILCGDGSCSGFTFSGNAITGGGKTSSCNYPTNTCPS,Reduces activity by 99.87%. Lowers affinity for substrate over 10-fold.,,MVRNIVSRLCSQLFALPSSSLQERDPCSVTEYSGLATAVSSCKNIVLNGFQVPTGKQLDLSSLQNDSTVTFKGTTTFATTADNDFNPIVISGSNITITGASGHVIDGNGQAYWDGKGSNSNSNQKPDHFIVVQKTTGNSKITNLNIQNWPVHCFDITGSSQLTISGLILDNRAGDKPNAKSGSLPAAHNTDGFDISSSDHVTLDNNHVYNQDDCVAVTSGTNIVVSNMYCSGGHGLSIGSVGGKSDNVVDGVQFLSSQVVNSQNGCRIKSNSGATGTINNVTYQNIALTNISTYGVDVQQDYLNGGPTGKPTNGVKISNIKFIKVTGTVASSAQDWFILCGDGSCSGFTFSGNAITGGGKTSSCNYPTNTCPS,Polygalacturonase,"Involved in maceration and soft-rotting of plant tissue. Hydrolyzes the 1,4-alpha glycosidic bonds of de-esterified pectate in the smooth region of the plant cell wall.",The mutation of K-269 to E affects the formation of the complex with PGIP-2.,Reduces activity by 99.87%. Lowers affinity for substrate over 10-fold. The mutation of K-269 to E affects the formation of the complex with PGIP-2.
124,124,106424,P25522-T251A,MSDNDTIVAQATPPGRGGVGILRISGFKAREVAETVLGKLPKPRYADYLPFKDADGSVLDQGIALWFPGPNSFTGEDVLELQGHGGPVILDLLLKRILTIPGLRIARPGEFSERAFLNDKLDLAQAEAIADLIDASSEQAARSALNSLQGAFSARVNHLVEALTHLRIYVEAAIDFPDEEIDFLSDGKIEAQLNDVIADLDAVRAEARQGSLLREGMKVVIAGRPNAGKSSLLNALAGREAAIVTDIAGTARDVLREHIHIDGMPLHIIDTAGLREASDEVERIGIERAWQEIEQADRVLFMVDGTTTDAVDPAEIWPEFIARLPAKLPITVVRNKADITGETLGMSEVNGHALIRLSARTGEGVDVLRNHLKQSMGFDTNMEGGFLARRRHLQALEQAAEHLQQGKAQLLGAWAGELLAEELRLAQQNLSEITGEFTSDDLLGRIFSSFCIGK,92-fold decrease in GTPase activity and 59-fold increase of affinity.,,MSDNDTIVAQATPPGRGGVGILRISGFKAREVAETVLGKLPKPRYADYLPFKDADGSVLDQGIALWFPGPNSFTGEDVLELQGHGGPVILDLLLKRILTIPGLRIARPGEFSERAFLNDKLDLAQAEAIADLIDASSEQAARSALNSLQGAFSARVNHLVEALTHLRIYVEAAIDFPDEEIDFLSDGKIEAQLNDVIADLDAVRAEARQGSLLREGMKVVIAGRPNAGKSSLLNALAGREAAIVTDIAGTTRDVLREHIHIDGMPLHIIDTAGLREASDEVERIGIERAWQEIEQADRVLFMVDGTTTDAVDPAEIWPEFIARLPAKLPITVVRNKADITGETLGMSEVNGHALIRLSARTGEGVDVLRNHLKQSMGFDTNMEGGFLARRRHLQALEQAAEHLQQGKAQLLGAWAGELLAEELRLAQQNLSEITGEFTSDDLLGRIFSSFCIGK,tRNA modification GTPase MnmE,"Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.",The invariant threonine (T251) of the G2 motif would be essential for the conformational change of the switch I region associated with GTP hydrolysis.,92-fold decrease in GTPase activity and 59-fold increase of affinity. The invariant threonine (T251) of the G2 motif would be essential for the conformational change of the switch I region associated with GTP hydrolysis.
125,125,107497,O14746-G682D,MPRAPRCRAVRSLLRSHYREVLPLATFVRRLGPQGWRLVQRGDPAAFRALVAQCLVCVPWDARPPPAAPSFRQVSCLKELVARVLQRLCERGAKNVLAFGFALLDGARGGPPEAFTTSVRSYLPNTVTDALRGSGAWGLLLRRVGDDVLVHLLARCALFVLVAPSCAYQVCGPPLYQLGAATQARPPPHASGPRRRLGCERAWNHSVREAGVPLGLPAPGARRRGGSASRSLPLPKRPRRGAAPEPERTPVGQGSWAHPGRTRGPSDRGFCVVSPARPAEEATSLEGALSGTRHSHPSVGRQHHAGPPSTSRPPRPWDTPCPPVYAETKHFLYSSGDKEQLRPSFLLSSLRPSLTGARRLVETIFLGSRPWMPGTPRRLPRLPQRYWQMRPLFLELLGNHAQCPYGVLLKTHCPLRAAVTPAAGVCAREKPQGSVAAPEEEDTDPRRLVQLLRQHSSPWQVYGFVRACLRRLVPPGLWGSRHNERRFLRNTKKFISLGKHAKLSLQELTWKMSVRDCAWLRRSPGVGCVPAAEHRLREEILAKFLHWLMSVYVVELLRSFFYVTETTFQKNRLFFYRKSVWSKLQSIGIRQHLKRVQLRELSEAEVRQHREARPALLTSRLRFIPKPDGLRPIVNMDYVVGARTFRREKRAERLTSRVKALFSVLNYERARRPGLLGASVLDLDDIHRAWRTFVLRVRAQDPPPELYFVKVDVTGAYDTIPQDRLTEVIASIIKPQNTYCVRRYAVVQKAAHGHVRKAFKSHVSTLTDLQPYMRQFVAHLQETSPLRDAVVIEQSSSLNEASSGLFDVFLRFMCHHAVRIRGKSYVQCQGIPQGSILSTLLCSLCYGDMENKLFAGIRRDGLLLRLVDDFLLVTPHLTHAKTFLRTLVRGVPEYGCVVNLRKTVVNFPVEDEALGGTAFVQMPAHGLFPWCGLLLDTRTLEVQSDYSSYARTSIRASLTFNRGFKAGRNMRRKLFGVLRLKCHSLFLDLQVNSLQTVCTNIYKILLLQAYRFHACVLQLPFHQQ,In AA; non-severe; abolishes telomerase catalytic activity but little effect on binding to TERC.,,MPRAPRCRAVRSLLRSHYREVLPLATFVRRLGPQGWRLVQRGDPAAFRALVAQCLVCVPWDARPPPAAPSFRQVSCLKELVARVLQRLCERGAKNVLAFGFALLDGARGGPPEAFTTSVRSYLPNTVTDALRGSGAWGLLLRRVGDDVLVHLLARCALFVLVAPSCAYQVCGPPLYQLGAATQARPPPHASGPRRRLGCERAWNHSVREAGVPLGLPAPGARRRGGSASRSLPLPKRPRRGAAPEPERTPVGQGSWAHPGRTRGPSDRGFCVVSPARPAEEATSLEGALSGTRHSHPSVGRQHHAGPPSTSRPPRPWDTPCPPVYAETKHFLYSSGDKEQLRPSFLLSSLRPSLTGARRLVETIFLGSRPWMPGTPRRLPRLPQRYWQMRPLFLELLGNHAQCPYGVLLKTHCPLRAAVTPAAGVCAREKPQGSVAAPEEEDTDPRRLVQLLRQHSSPWQVYGFVRACLRRLVPPGLWGSRHNERRFLRNTKKFISLGKHAKLSLQELTWKMSVRDCAWLRRSPGVGCVPAAEHRLREEILAKFLHWLMSVYVVELLRSFFYVTETTFQKNRLFFYRKSVWSKLQSIGIRQHLKRVQLRELSEAEVRQHREARPALLTSRLRFIPKPDGLRPIVNMDYVVGARTFRREKRAERLTSRVKALFSVLNYERARRPGLLGASVLGLDDIHRAWRTFVLRVRAQDPPPELYFVKVDVTGAYDTIPQDRLTEVIASIIKPQNTYCVRRYAVVQKAAHGHVRKAFKSHVSTLTDLQPYMRQFVAHLQETSPLRDAVVIEQSSSLNEASSGLFDVFLRFMCHHAVRIRGKSYVQCQGIPQGSILSTLLCSLCYGDMENKLFAGIRRDGLLLRLVDDFLLVTPHLTHAKTFLRTLVRGVPEYGCVVNLRKTVVNFPVEDEALGGTAFVQMPAHGLFPWCGLLLDTRTLEVQSDYSSYARTSIRASLTFNRGFKAGRNMRRKLFGVLRLKCHSLFLDLQVNSLQTVCTNIYKILLLQAYRFHACVLQLPFHQQ,Telomerase reverse transcriptase,"Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. Active in progenitor and cancer cells. Inactive, or very low activity, in normal somatic cells. Catalytic component of the teleromerase holoenzyme complex whose main activity is the elongation of telomeres by acting as a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme. Catalyzes the RNA-dependent extension of 3'-chromosomal termini with the 6-nucleotide telomeric repeat unit, 5'-TTAGGG-3'. The catalytic cycle involves primer binding, primer extension and release of product once the template boundary has been reached or nascent product translocation followed by further extension. More active on substrates containing 2 or 3 telomeric repeats. Telomerase activity is regulated by a number of factors including telomerase complex-associated proteins, chaperones and polypeptide modifiers. Modulates Wnt signaling. Plays important roles in aging and antiapoptosis.","Novel heterozygous, non-synonymous mutation in TERT () was found in two patients with acquired aplastic anemia (AA).","In AA; non-severe; abolishes telomerase catalytic activity but little effect on binding to TERC. Novel heterozygous, non-synonymous mutation in TERT () was found in two patients with acquired aplastic anemia (AA)."
126,126,108745,Q9UJ83-D455R,MPDSNFAERSEEQVSGAKVIAQALKTQDVEYIFGIVGIPVTEIAIAAQQLGIKYIGMRNEQAACYAASAIGYLTSRPGVCLVVSGPGLIHALGGMANANMNCWPLLVIGGSSERNQETMGAFQEFPQVEACRLYTKFSARPSSIEAIPFVIEKAVRSSIYGRPGACYVDIPADFVNLQVNVNSIKYMERCMSPPISMAETSAVCTAASVIRNAKQPLLIIGKGAAYAHAEESIKKLVEQYKLPFLPTPMGKGVVPDNHPYCVGAARSRALQFADVIVLFGARLNWILHFGLPPRYQPDVKFIQVDICAEELGNNVKPAVTLLGNIHAVTKQLLEELDKTPWQYPPESKWWKTLREKMKSNEAASKELASKKSLPMNYYTVFYHVQEQLPRDCFVVSEGANTMDIGRTVLQNYLPRHRLDAGTFGTMGVGLGFAIAAAVVAKDRSPGQWIICVEGRSAFGFSGMEVETICRYNLPIILLVVNNNGIYQGFDTDTWKEMLKFQDATAVVPPMCLLPNSHYEQVMTAFGGKGYFVQTPEELQKSLRQSLADTTKPSLINIMIEPQATRKAQDFHWLTRSNM,"Does not affect subcellular localization. Abolishes lyase activity. Does not affect subcellular localization, abolishes lyase activity, does not affect oligomerisation and does not bind TTP; when associated with S-456.",,MPDSNFAERSEEQVSGAKVIAQALKTQDVEYIFGIVGIPVTEIAIAAQQLGIKYIGMRNEQAACYAASAIGYLTSRPGVCLVVSGPGLIHALGGMANANMNCWPLLVIGGSSERNQETMGAFQEFPQVEACRLYTKFSARPSSIEAIPFVIEKAVRSSIYGRPGACYVDIPADFVNLQVNVNSIKYMERCMSPPISMAETSAVCTAASVIRNAKQPLLIIGKGAAYAHAEESIKKLVEQYKLPFLPTPMGKGVVPDNHPYCVGAARSRALQFADVIVLFGARLNWILHFGLPPRYQPDVKFIQVDICAEELGNNVKPAVTLLGNIHAVTKQLLEELDKTPWQYPPESKWWKTLREKMKSNEAASKELASKKSLPMNYYTVFYHVQEQLPRDCFVVSEGANTMDIGRTVLQNYLPRHRLDAGTFGTMGVGLGFAIAAAVVAKDRSPGQWIICVEGDSAFGFSGMEVETICRYNLPIILLVVNNNGIYQGFDTDTWKEMLKFQDATAVVPPMCLLPNSHYEQVMTAFGGKGYFVQTPEELQKSLRQSLADTTKPSLINIMIEPQATRKAQDFHWLTRSNM,2-hydroxyacyl-CoA lyase 1,Peroxisomal 2-OH acyl-CoA lyase involved in the cleavage (C1 removal) reaction in the fatty acid alpha-oxydation in a thiamine pyrophosphate (TPP)-dependent manner. Involved in the degradation of 3-methyl-branched fatty acids like phytanic acid and the shortening of 2-hydroxy long-chain fatty acids. Plays a significant role in the biosynthesis of heptadecanal in the liver.,The mutation in the TPP-binding domain of HACL1 abolished enzyme activity.,"Does not affect subcellular localization. Abolishes lyase activity. Does not affect subcellular localization, abolishes lyase activity, does not affect oligomerisation and does not bind TTP; when associated with S-456. The mutation in the TPP-binding domain of HACL1 abolished enzyme activity."
127,127,109639,P25522-T250A,MSDNDTIVAQATPPGRGGVGILRISGFKAREVAETVLGKLPKPRYADYLPFKDADGSVLDQGIALWFPGPNSFTGEDVLELQGHGGPVILDLLLKRILTIPGLRIARPGEFSERAFLNDKLDLAQAEAIADLIDASSEQAARSALNSLQGAFSARVNHLVEALTHLRIYVEAAIDFPDEEIDFLSDGKIEAQLNDVIADLDAVRAEARQGSLLREGMKVVIAGRPNAGKSSLLNALAGREAAIVTDIAGATRDVLREHIHIDGMPLHIIDTAGLREASDEVERIGIERAWQEIEQADRVLFMVDGTTTDAVDPAEIWPEFIARLPAKLPITVVRNKADITGETLGMSEVNGHALIRLSARTGEGVDVLRNHLKQSMGFDTNMEGGFLARRRHLQALEQAAEHLQQGKAQLLGAWAGELLAEELRLAQQNLSEITGEFTSDDLLGRIFSSFCIGK,4-fold decrease in GTPase activity and 1.5-fold increase of affinity.,,MSDNDTIVAQATPPGRGGVGILRISGFKAREVAETVLGKLPKPRYADYLPFKDADGSVLDQGIALWFPGPNSFTGEDVLELQGHGGPVILDLLLKRILTIPGLRIARPGEFSERAFLNDKLDLAQAEAIADLIDASSEQAARSALNSLQGAFSARVNHLVEALTHLRIYVEAAIDFPDEEIDFLSDGKIEAQLNDVIADLDAVRAEARQGSLLREGMKVVIAGRPNAGKSSLLNALAGREAAIVTDIAGTTRDVLREHIHIDGMPLHIIDTAGLREASDEVERIGIERAWQEIEQADRVLFMVDGTTTDAVDPAEIWPEFIARLPAKLPITVVRNKADITGETLGMSEVNGHALIRLSARTGEGVDVLRNHLKQSMGFDTNMEGGFLARRRHLQALEQAAEHLQQGKAQLLGAWAGELLAEELRLAQQNLSEITGEFTSDDLLGRIFSSFCIGK,tRNA modification GTPase MnmE,"Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.",,4-fold decrease in GTPase activity and 1.5-fold increase of affinity.
128,128,109791,P16522-H439R,MNDDSQDKIIHDIRIQLRKAATELSRWKLYGSSKWAAEALAGLAEAIDVDQTHSLADESPLRNKQGVPKQMFEIPQNGFGLSETEYDLYLLGSTLFDAKEFDRCVFFLKDVTNPYLKFLKLYSKFLSWDKKSQESMENILTTGKFTDEMYRANKDGDGSGNEDINQSGHQRANLKMVSNEHESQSNISSILKEINTFLESYEIKIDDDEADLGLALLYYLRGVILKQEKNISKAMSSFLKSLSCYSFNWSCWLELMDCLQKVDDALLLNNYLYQNFQFKFSENLGSQRTIEFNIMIKFFKLKVFEELNGQLEDYFEDLEFLLQVFPNFTFLKAYNATISYNNLDYVTAESRFDDIVKQDPYRLNDLETYSNILYVMQKNSKLAYLAQFVSQIDRFRPETCCIIANYYSARQEHEKSIMYFRRALTLDKKTTNAWTLMGREFVELSNSHAAIECYRRAVDICPRDFKAWFGLGQAYALLDMHLYSLYYFQKACTLKPWDRRIWQVLGECYSKTGNKVEAIKCYKRSIKASQTVDQNTSIYYRLAQLYEELEDLQECKKFMMKCVDVEELLEGIVTDETVKARLWLAIFEIKAGNYQLAYDYAMGVSSGTSQEIEEARMLARECRRHM,In CDC23-2; G2/M cell cycle arrest at 36 degrees Celsius.,,MNDDSQDKIIHDIRIQLRKAATELSRWKLYGSSKWAAEALAGLAEAIDVDQTHSLADESPLRNKQGVPKQMFEIPQNGFGLSETEYDLYLLGSTLFDAKEFDRCVFFLKDVTNPYLKFLKLYSKFLSWDKKSQESMENILTTGKFTDEMYRANKDGDGSGNEDINQSGHQRANLKMVSNEHESQSNISSILKEINTFLESYEIKIDDDEADLGLALLYYLRGVILKQEKNISKAMSSFLKSLSCYSFNWSCWLELMDCLQKVDDALLLNNYLYQNFQFKFSENLGSQRTIEFNIMIKFFKLKVFEELNGQLEDYFEDLEFLLQVFPNFTFLKAYNATISYNNLDYVTAESRFDDIVKQDPYRLNDLETYSNILYVMQKNSKLAYLAQFVSQIDRFRPETCCIIANYYSARQEHEKSIMYFRRALTLDKKTTNAWTLMGHEFVELSNSHAAIECYRRAVDICPRDFKAWFGLGQAYALLDMHLYSLYYFQKACTLKPWDRRIWQVLGECYSKTGNKVEAIKCYKRSIKASQTVDQNTSIYYRLAQLYEELEDLQECKKFMMKCVDVEELLEGIVTDETVKARLWLAIFEIKAGNYQLAYDYAMGVSSGTSQEIEEARMLARECRRHM,Anaphase-promoting complex subunit CDC23,"Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. In early mitosis, the APC/C is activated by CDC20 and targets securin PDS1, the B-type cyclin CLB5, and other anaphase inhibitory proteins for proteolysis, thereby triggering the separation of sister chromatids at the metaphase-to-anaphase transition. In late mitosis and in G1, degradation of CLB5 allows activation of the APC/C by CDH1, which is needed to destroy CDC20 and the B-type cyclin CLB2 to allow exit from mitosis and creating the low CDK state necessary for cytokinesis and for reforming prereplicative complexes in G1 prior to another round of replication.",The mutation in the CDC23 gene causes a single amino acid change in the protein. This mutation is found within a mutable domain of CDC23 and may affect its function or stability.,In CDC23-2; G2/M cell cycle arrest at 36 degrees Celsius. The mutation in the CDC23 gene causes a single amino acid change in the protein. This mutation is found within a mutable domain of CDC23 and may affect its function or stability.
129,129,110196,P32266-K223A,MNASPVRLLILRRQLATHPAILYSSPYIKSPLVHLHSRMSNVHRSAHANALSFVITRRSISHFPKIISKIIRLPIYVGGGMAAAGSYIAYKMEEASSFTKDKLDRIKDLGESMKEKFNKMFSGDKSQDGGHGNDGTVPTATLIAATSLDDDESKRQGDPKDDDDEDDDDEDDENDSVDTTQDEMLNLTKQMIEIRTILNKVDSSSAHLTLPSIVVIGSQSSGASSVLESIVGREFLPKGSNMVTRRPIELTLVNTPNSNNVTADFPSMRLYNIKDFKEVKRMLMELNMAVPTSEAVSEEPIQLTIKSSRVPDLSLVDLPGYIQVEAADQPIELKTKIRDLCEKYLTAPNIILAISAADVDLANSSALKASKAADPKGLRTIGVITKLDLVDPEKARSILNNKKYPLSMGYVGVITKTPSSINRKHLGLFGEAPSSSLSGIFSKGQHGQSSGEENTNGLKQIVSHQFEKAYFKENKKYFTNCQVSTKKLREKLIKILEISMSNALEPTSTLIQQELDDTSYLFKVEFNDRHLTPKSYLLNNIDVLKLGIKEFQEKFHRNELKSILRAELDQKVLDVLATRYWKDDNLQDLSSSKLESDTDMLYWHKKLELASSGLTKMGIGRLSTMLTTNAILKELDNILESTQLKNHELIKDLVSNTAINVLNSKYYSTADQVENCIKPFKYEIDLEERDWSLARQHSINLIKEELRQCNSRYQAIKNAVGSKKLANVMGYLENESNLQKETLGMSKLLLERGSEAIFLDKRCKVLSFRLKMLKNKCHSTIEKDRCPEVFLSAVSDKLTSTAVLFLNVELLSDFFYNFPIELDRRLTLLGDEQVEMFAKEDPKISRHIELQKRKELLELALEKIDSILVFKKSYKGVSKNL,Loss of stability.,,MNASPVRLLILRRQLATHPAILYSSPYIKSPLVHLHSRMSNVHRSAHANALSFVITRRSISHFPKIISKIIRLPIYVGGGMAAAGSYIAYKMEEASSFTKDKLDRIKDLGESMKEKFNKMFSGDKSQDGGHGNDGTVPTATLIAATSLDDDESKRQGDPKDDDDEDDDDEDDENDSVDTTQDEMLNLTKQMIEIRTILNKVDSSSAHLTLPSIVVIGSQSSGKSSVLESIVGREFLPKGSNMVTRRPIELTLVNTPNSNNVTADFPSMRLYNIKDFKEVKRMLMELNMAVPTSEAVSEEPIQLTIKSSRVPDLSLVDLPGYIQVEAADQPIELKTKIRDLCEKYLTAPNIILAISAADVDLANSSALKASKAADPKGLRTIGVITKLDLVDPEKARSILNNKKYPLSMGYVGVITKTPSSINRKHLGLFGEAPSSSLSGIFSKGQHGQSSGEENTNGLKQIVSHQFEKAYFKENKKYFTNCQVSTKKLREKLIKILEISMSNALEPTSTLIQQELDDTSYLFKVEFNDRHLTPKSYLLNNIDVLKLGIKEFQEKFHRNELKSILRAELDQKVLDVLATRYWKDDNLQDLSSSKLESDTDMLYWHKKLELASSGLTKMGIGRLSTMLTTNAILKELDNILESTQLKNHELIKDLVSNTAINVLNSKYYSTADQVENCIKPFKYEIDLEERDWSLARQHSINLIKEELRQCNSRYQAIKNAVGSKKLANVMGYLENESNLQKETLGMSKLLLERGSEAIFLDKRCKVLSFRLKMLKNKCHSTIEKDRCPEVFLSAVSDKLTSTAVLFLNVELLSDFFYNFPIELDRRLTLLGDEQVEMFAKEDPKISRHIELQKRKELLELALEKIDSILVFKKSYKGVSKNL,"Dynamin-like GTPase MGM1, mitochondrial",Dynamin-related GTPase required for mitochondrial fusion. Coordinates interaction between the inner and outer mitochondrial membrane to promote the formation of the double membrane.,,Loss of stability.
130,130,112659,Q9I4E3-H162F,MFKHIIARTPARSLVDGLTSSHLGKPDYAKALEQHNAYIRALQTCDVDITLLPPDERFPDSVFVEDPVLCTSRCAIITRPGAESRRGETEIIEETVQRFYPGKVERIEAPGTVEAGDIMMVGDHFYIGESARTNAEGARQMIAILEKHGLSGSVVRLEKVLFLKTGLAYLEHNNLLAAGEFVSKPEFQDFNIIEIPEEESYAANCIWVNERVIMPAGYPRTREKIARLGYRVIEVDTSEYRKIDGGVSCMSLRF,Abolishes enzyme activity.,,MFKHIIARTPARSLVDGLTSSHLGKPDYAKALEQHNAYIRALQTCDVDITLLPPDERFPDSVFVEDPVLCTSRCAIITRPGAESRRGETEIIEETVQRFYPGKVERIEAPGTVEAGDIMMVGDHFYIGESARTNAEGARQMIAILEKHGLSGSVVRLEKVLHLKTGLAYLEHNNLLAAGEFVSKPEFQDFNIIEIPEEESYAANCIWVNERVIMPAGYPRTREKIARLGYRVIEVDTSEYRKIDGGVSCMSLRF,N,"Hydrolyzes N(G),N(G)-dimethyl-L-arginine (ADMA) and N(G)-monomethyl-L-arginine (MMA).",,Abolishes enzyme activity.
131,131,112803,P41252-P437L,MLQQVPENINFPAEEEKILEFWTEFNCFQECLKQSKHKPKFTFYDGPPFATGLPHYGHILAGTIKDIVTRYAHQSGFHVDRRFGWDCHGLPVEYEIDKTLGIRGPEDVAKMGITEYNNQCRAIVMRYSAEWKSTVSRLGRWIDFDNDYKTLYPQFMESVWWVFKQLYDKGLVYRGVKVMPFSTACNTPLSNFESHQNYKDVQDPSVFVTFPLEEDETVSLVAWTTTPWTLPSNLAVCVNPEMQYVKIKDVARGRLLILMEARLSALYKLESDYEILERFPGAYLKGKKYRPLFDYFLKCKENGAFTVLVDNYVKEEEGTGVVHQAPYFGAEDYRVCMDFNIIRKDSLPVCPVDASGCFTTEVTDFAGQYVKDADKSIIRTLKEQGRLLVATTFTHSYPFCWRSDTPLIYKAVPSWFVRVENMVDQLLRNNDLCYWVLELVREKRFGNWLKDARDWTISRNRYWGTPIPLWVSDDFEEVVCIGSVAELEELSGAKISDLHRESVDHLTIPSRCGKGSLHRISEVFDCWFESGSMPYAQVHYPFENKREFEDAFPADFIAEGIDQTRGWFYTLLVLATALFGQPPFKNVIVNGLVLASDGQKMSKRKKNYPDPVSIIQKYGADALRLYLINSPVVRAENLRFKEEGVRDVLKDVLLPWYNAYRFLIQNVLRLQKEEEIEFLYNENTVRESPNITDRWILSFMQSLIGFFETEMAAYRLYTVVPRLVKFVDILTNWYVRMNRRRLKGENGMEDCVMALETLFSVLLSLCRLMAPYTPFLTELMYQNLKVLIDPVSVQDKDTLSIHYLMLPRVREELIDKKTESAVSQMQSVIELGRVIRDRKTIPIKYPLKEIVVIHQDPEALKDIKSLEKYIIEELNVRKVTLSTDKNKYGIRLRAEPDHMVLGKRLKGAFKAVMTSIKQLSSEELEQFQKTGTIVVEGHELHDEDIRLMYTFDQATGGTAQFEAHSDAQALVLLDVTPDQSMVDEGMAREVINRIQKLRKKCNLVPTDEITVYYKAKSEGTYLNS,In GRIDHH.,,MLQQVPENINFPAEEEKILEFWTEFNCFQECLKQSKHKPKFTFYDGPPFATGLPHYGHILAGTIKDIVTRYAHQSGFHVDRRFGWDCHGLPVEYEIDKTLGIRGPEDVAKMGITEYNNQCRAIVMRYSAEWKSTVSRLGRWIDFDNDYKTLYPQFMESVWWVFKQLYDKGLVYRGVKVMPFSTACNTPLSNFESHQNYKDVQDPSVFVTFPLEEDETVSLVAWTTTPWTLPSNLAVCVNPEMQYVKIKDVARGRLLILMEARLSALYKLESDYEILERFPGAYLKGKKYRPLFDYFLKCKENGAFTVLVDNYVKEEEGTGVVHQAPYFGAEDYRVCMDFNIIRKDSLPVCPVDASGCFTTEVTDFAGQYVKDADKSIIRTLKEQGRLLVATTFTHSYPFCWRSDTPLIYKAVPSWFVRVENMVDQLLRNNDLCYWVPELVREKRFGNWLKDARDWTISRNRYWGTPIPLWVSDDFEEVVCIGSVAELEELSGAKISDLHRESVDHLTIPSRCGKGSLHRISEVFDCWFESGSMPYAQVHYPFENKREFEDAFPADFIAEGIDQTRGWFYTLLVLATALFGQPPFKNVIVNGLVLASDGQKMSKRKKNYPDPVSIIQKYGADALRLYLINSPVVRAENLRFKEEGVRDVLKDVLLPWYNAYRFLIQNVLRLQKEEEIEFLYNENTVRESPNITDRWILSFMQSLIGFFETEMAAYRLYTVVPRLVKFVDILTNWYVRMNRRRLKGENGMEDCVMALETLFSVLLSLCRLMAPYTPFLTELMYQNLKVLIDPVSVQDKDTLSIHYLMLPRVREELIDKKTESAVSQMQSVIELGRVIRDRKTIPIKYPLKEIVVIHQDPEALKDIKSLEKYIIEELNVRKVTLSTDKNKYGIRLRAEPDHMVLGKRLKGAFKAVMTSIKQLSSEELEQFQKTGTIVVEGHELHDEDIRLMYTFDQATGGTAQFEAHSDAQALVLLDVTPDQSMVDEGMAREVINRIQKLRKKCNLVPTDEITVYYKAKSEGTYLNS,"Isoleucine--tRNA ligase, cytoplasmic",Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA.,"The mutation in the isoleucyl-tRNA synthetase protein has been associated with hereditary weak calf syndrome in cattle. In humans, biallelic mutations in IARS have been found in individuals with severe prenatal-onset growth retardation, intellectual disability, and muscular hypotonia. Zinc deficiency was also observed in affected individuals, and zinc supplementation showed a beneficial effect on growth in one case.","In GRIDHH. The mutation in the isoleucyl-tRNA synthetase protein has been associated with hereditary weak calf syndrome in cattle. In humans, biallelic mutations in IARS have been found in individuals with severe prenatal-onset growth retardation, intellectual disability, and muscular hypotonia. Zinc deficiency was also observed in affected individuals, and zinc supplementation showed a beneficial effect on growth in one case."
132,132,113352,B9EJA2-P599A,MATDSASCEPDLSRTPGDTEGATAEAAKKEFDVDTLSKSELRMLLSVMEGELEARDLVIEALRARRKEVFIQERYGRFNLNDPFLALQRDYEAGPGDKEKPVCTNPLSILEAVMAHCRKMQERMSAQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKNKHVVLMLVKECKQLSGKVVEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEIDKMKKMMEQMKKGSDGKPGLSLPRKTKDKRLASISVATEGPVTRSVACQTDVVTESTDPVKKLPLTVPIKPSTGSPLVPTNTKGNVGPSALLIRPGIDRQSSHSDLGPSPPTALPSSANRIEENGPSTGNAPDLSNSTPSTPSSTAPAAAQTPGTAPQNHSQAPTVHSLHSPCANTHPGLNPRIQAARFRFQGNANDPDQNGNNTQSPPSRDVSPTSRDNLVAKQLARNTVTQALSRFTSPQAGASSRLGVSPGGDAGTCPPVGRTGLKTPGAARVDRGNPPPIPPKKPGLSQTPSPPHPQLRASNAGAKVDNKIVASPPSTLPQGTKVVNEENVPKSSSAQLPPKPSIDLTVAPAGCPVSALATSQVGAWPAGTPGLNQPACSDSSLVIPATVAFCSSINPVSASSRSPGASDSLLVAASGWSPSLTPLLMSGGPAPLAGRPTLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFECIELLTAYNANINHSAAGGQTPLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVDSLKLLMYHRVRAHGNSLSSEEPKSGLFSLNGGESPTGPSKPVVPADLINHADKEGWTAAHIAASKGFKNCLEVLCRHGGLEPERRDKCNRTVHDVATDDCKHLLENLNALKIPLRISVGEIQPSNDVSDDFECEHTICTLNIRKQTSWEDFSKAVSQALTNHFQAISSDGWWSLEDG,Reduced CTTN-binding; when associated with A-602.,,MATDSASCEPDLSRTPGDTEGATAEAAKKEFDVDTLSKSELRMLLSVMEGELEARDLVIEALRARRKEVFIQERYGRFNLNDPFLALQRDYEAGPGDKEKPVCTNPLSILEAVMAHCRKMQERMSAQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKNKHVVLMLVKECKQLSGKVVEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEIDKMKKMMEQMKKGSDGKPGLSLPRKTKDKRLASISVATEGPVTRSVACQTDVVTESTDPVKKLPLTVPIKPSTGSPLVPTNTKGNVGPSALLIRPGIDRQSSHSDLGPSPPTALPSSANRIEENGPSTGNAPDLSNSTPSTPSSTAPAAAQTPGTAPQNHSQAPTVHSLHSPCANTHPGLNPRIQAARFRFQGNANDPDQNGNNTQSPPSRDVSPTSRDNLVAKQLARNTVTQALSRFTSPQAGASSRLGVSPGGDAGTCPPVGRTGLKTPGAARVDRGNPPPIPPKKPGLSQTPSPPHPQLRASNAGAKVDNKIVASPPSTLPQGTKVVNEENVPKSSSPQLPPKPSIDLTVAPAGCPVSALATSQVGAWPAGTPGLNQPACSDSSLVIPATVAFCSSINPVSASSRSPGASDSLLVAASGWSPSLTPLLMSGGPAPLAGRPTLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFECIELLTAYNANINHSAAGGQTPLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVDSLKLLMYHRVRAHGNSLSSEEPKSGLFSLNGGESPTGPSKPVVPADLINHADKEGWTAAHIAASKGFKNCLEVLCRHGGLEPERRDKCNRTVHDVATDDCKHLLENLNALKIPLRISVGEIQPSNDVSDDFECEHTICTLNIRKQTSWEDFSKAVSQALTNHFQAISSDGWWSLEDG,Cortactin-binding protein 2,"Regulates the dendritic spine distribution of CTTN/cortactin in hippocampal neurons, and thus controls dendritic spinogenesis and dendritic spine maintenance.",,Reduced CTTN-binding; when associated with A-602.
133,133,114784,Q96RL7-I90K,MVFESVVVDVLNRFLGDYVVDLDTSQLSLGIWKGAVALKNLQIKENALSQLDVPFKVKVGHIGNLKLIIPWKNLYTQPVEAVLEEIYLLKVPSSRIKYDPLKEEKQLMEAKQQELKRIEEAKQKVVDQEQHLPEKQDTFAEKLVTQIIKNLQVKISSIHIRYEDDITNRDKPLSFGISLQNLSMQTTDQYWVPCLHDETEKLVRKLIRLDNLFAYWNVKSQMFYLSDYDNSLDDLKNGIVNENIVPEGYDFVFRPISANAKLVMNRRSDFDFSAPKINLEIELHNIAIEFNKPQYFSIMELLESVDMMAQNLPYRKFKPDVPLHHHAREWWAYAIHGVLEVNVCPRLWMWSWKHIRKHRQKVKQYKELYKKKLTSKKPPGELLVSLEELEKTLDVFNITIARQTAEVEVKKAGYKIYKEGVKDPEDNKGWFSWLWSWSEQNTNEQQPDVQPETLEEMLTPEEKALLYEAIGYSETAVDPTLLKTFEALKFFVHLKSMSIVLRENHQKPELVDIVIEEFSTLIVQRPGAQAIKFETKIDSFHITGLPDNSEKPRLLSSLDDAMSLFQITFEINPLDETVSQRCIIEAEPLEIIYDARTVNSIVEFFRPPKEVHLAQLTAATLTKLEEFRSKTATGLLYIIETQKVLDLKINLKASYIIVPQDGIFSPTSNLLLLDLGHLKVTSKSRSELPDVKQGEANLKEIMDRAYDSFDIQLTSVQLLYSRVGDNWREARKLSVSTQHILVPMHFNLELSKAMVFMDVRMPKFKIYGKLPLISLRISDKKLQGIMELIESIPKPEPVTEVSAPVKSFQIQTSTSLGTSQISQKIIPLLELPSVSEDDSEEEFFDAPCSPLEEPLQFPTGVKSIRTRKLQKQDCSVNMTTFKIRFEVPKVLIEFYHLVGDCELSVVEILVLGLGAEIEIRTYDLKANAFLKEFCLKCPEYLDENKKPVYLVTTLDNTMEDLLTLEYVKAEKNVPDLKSTYNNVLQLIKVNFSSLDIHLHTEALLNTINYLHNILPQSEEKSAPV,In CHAC; disrupts subcellular localization with protein XK on lipid droplets..,,MVFESVVVDVLNRFLGDYVVDLDTSQLSLGIWKGAVALKNLQIKENALSQLDVPFKVKVGHIGNLKLIIPWKNLYTQPVEAVLEEIYLLIVPSSRIKYDPLKEEKQLMEAKQQELKRIEEAKQKVVDQEQHLPEKQDTFAEKLVTQIIKNLQVKISSIHIRYEDDITNRDKPLSFGISLQNLSMQTTDQYWVPCLHDETEKLVRKLIRLDNLFAYWNVKSQMFYLSDYDNSLDDLKNGIVNENIVPEGYDFVFRPISANAKLVMNRRSDFDFSAPKINLEIELHNIAIEFNKPQYFSIMELLESVDMMAQNLPYRKFKPDVPLHHHAREWWAYAIHGVLEVNVCPRLWMWSWKHIRKHRQKVKQYKELYKKKLTSKKPPGELLVSLEELEKTLDVFNITIARQTAEVEVKKAGYKIYKEGVKDPEDNKGWFSWLWSWSEQNTNEQQPDVQPETLEEMLTPEEKALLYEAIGYSETAVDPTLLKTFEALKFFVHLKSMSIVLRENHQKPELVDIVIEEFSTLIVQRPGAQAIKFETKIDSFHITGLPDNSEKPRLLSSLDDAMSLFQITFEINPLDETVSQRCIIEAEPLEIIYDARTVNSIVEFFRPPKEVHLAQLTAATLTKLEEFRSKTATGLLYIIETQKVLDLKINLKASYIIVPQDGIFSPTSNLLLLDLGHLKVTSKSRSELPDVKQGEANLKEIMDRAYDSFDIQLTSVQLLYSRVGDNWREARKLSVSTQHILVPMHFNLELSKAMVFMDVRMPKFKIYGKLPLISLRISDKKLQGIMELIESIPKPEPVTEVSAPVKSFQIQTSTSLGTSQISQKIIPLLELPSVSEDDSEEEFFDAPCSPLEEPLQFPTGVKSIRTRKLQKQDCSVNMTTFKIRFEVPKVLIEFYHLVGDCELSVVEILVLGLGAEIEIRTYDLKANAFLKEFCLKCPEYLDENKKPVYLVTTLDNTMEDLLTLEYVKAEKNVPDLKSTYNNVLQLIKVNFSSLDIHLHTEALLNTINYLHNILPQSEEKSAPV,Intermembrane lipid transfer protein VPS13A,Mediates the transfer of lipids between membranes at organelle contact sites. Binds phospholipids. Required for the formation or stabilization of ER-mitochondria contact sites which enable transfer of lipids between the ER and mitochondria. Negatively regulates lipid droplet size and motility. Required for efficient lysosomal protein degradation.,The mutation in the CHAC gene leads to a functional change in the encoded protein.,In CHAC; disrupts subcellular localization with protein XK on lipid droplets.. The mutation in the CHAC gene leads to a functional change in the encoded protein.
134,134,115181,Q96AX1-Y438D,MAAHLSYGRVNLNVLREAVRRELREFLDKCAGSKAIVWDEYLTGPFGLIAQYSLLKEHEVEKMFTLKGNRLPAADVKNIIFFVRPRLELMDIIAENVLSEDRRGPTRDFHILFVPRRSLLCEQRLKDLGVLGSFIHREEYSLDLIPFDGDLLSMESEGAFKECYLEGDQTSLYHAAKGLMTLQALYGTIPQIFGKGECARQVANMMIRMKREFTGSQNSIFPVFDNLLLLDRNVDLLTPLATQLTYEGLIDEIYGIQNSYVKLPPEKFAPKKQGDGGKDLPTEAKKLQLNSAEELYAEIRDKNFNAVGSVLSKKAKIISAAFEERHNAKTVGEIKQFVSQLPHMQAARGSLANHTSIAELIKDVTTSEDFFDKLTVEQEFMSGIDTDKVNNYIEDCIAQKHSLIKVLRLVCLQSVCNSGLKQKVLDYYKREILQTYGDEHILTLHNLEKAGLLKPQTGGRNNYPTIRKTLRLWMDDVNEQNPTDISYVYSGYAPLSVRLAQLLSRPGWRSIEEVLRILPGPHFEERQPLPTGLQKKRQPGENRVTLIFFLGGVTFAEIAALRFLSQLEDGGTEYVIATTKLMNGTSWIEALMEKPF,Disrupts interaction with VPS16. Disrupts interaction with VPS18 and impairs endosome-lysosome fusion; when associated with D-429. Disrupts interaction with VPS18 and impairs endosome-lysosome fusion; when associated with K-441.,,MAAHLSYGRVNLNVLREAVRRELREFLDKCAGSKAIVWDEYLTGPFGLIAQYSLLKEHEVEKMFTLKGNRLPAADVKNIIFFVRPRLELMDIIAENVLSEDRRGPTRDFHILFVPRRSLLCEQRLKDLGVLGSFIHREEYSLDLIPFDGDLLSMESEGAFKECYLEGDQTSLYHAAKGLMTLQALYGTIPQIFGKGECARQVANMMIRMKREFTGSQNSIFPVFDNLLLLDRNVDLLTPLATQLTYEGLIDEIYGIQNSYVKLPPEKFAPKKQGDGGKDLPTEAKKLQLNSAEELYAEIRDKNFNAVGSVLSKKAKIISAAFEERHNAKTVGEIKQFVSQLPHMQAARGSLANHTSIAELIKDVTTSEDFFDKLTVEQEFMSGIDTDKVNNYIEDCIAQKHSLIKVLRLVCLQSVCNSGLKQKVLDYYKREILQTYGYEHILTLHNLEKAGLLKPQTGGRNNYPTIRKTLRLWMDDVNEQNPTDISYVYSGYAPLSVRLAQLLSRPGWRSIEEVLRILPGPHFEERQPLPTGLQKKRQPGENRVTLIFFLGGVTFAEIAALRFLSQLEDGGTEYVIATTKLMNGTSWIEALMEKPF,Vacuolar protein sorting-associated protein 33A,"Plays a role in vesicle-mediated protein trafficking to lysosomal compartments including the endocytic membrane transport and autophagic pathways. Believed to act as a core component of the putative HOPS and CORVET endosomal tethering complexes which are proposed to be involved in the Rab5-to-Rab7 endosome conversion probably implicating MON1A/B, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion. The HOPS complex is proposed to be recruited to Rab7 on the late endosomal membrane and to regulate late endocytic, phagocytic and autophagic traffic towards lysosomes. The CORVET complex is proposed to function as a Rab5 effector to mediate early endosome fusion probably in specific endosome subpopulations. Required for fusion of endosomes and autophagosomes with lysosomes; the function is dependent on its association with VPS16 but not VIPAS39. The function in autophagosome-lysosome fusion implicates STX17 but not UVRAG.",The mutation in VPS16 no longer rescues lysosome fusion with endosomes or autophagosomes in cells depleted of the endogenous proteins.,Disrupts interaction with VPS16. Disrupts interaction with VPS18 and impairs endosome-lysosome fusion; when associated with D-429. Disrupts interaction with VPS18 and impairs endosome-lysosome fusion; when associated with K-441. The mutation in VPS16 no longer rescues lysosome fusion with endosomes or autophagosomes in cells depleted of the endogenous proteins.
135,135,115484,Q9VF27-G199D,MSLTMRIFTASRNGQRLFGSHGARLLAAQRAEPKDIVEVPKGYVYVNNKELSMEFADITDRAASTMFFGELLRGFAVTLAHIFKEPATINYPFEKGPLSPRFRGEHALRRYPSGEERCIACKLCEAICPAQAITIEAEERADGSRRTTRYDIDMTKCIYCGFCQEACPVDAIVEGPNFEFSTETHEELLYNKEKLLCNDDKWESEIASNLQADHLYR,Disrupts mitochondrial function and results in enlarged mitochondria. Neurons present vacuolar lesions leading to neurodegeneration in the central brain. Results in behavioral defects and shorten lifespan.,,MSLTMRIFTASRNGQRLFGSHGARLLAAQRAEPKDIVEVPKGYVYVNNKELSMEFADITDRAASTMFFGELLRGFAVTLAHIFKEPATINYPFEKGPLSPRFRGEHALRRYPSGEERCIACKLCEAICPAQAITIEAEERADGSRRTTRYDIDMTKCIYCGFCQEACPVDAIVEGPNFEFSTETHEELLYNKEKLLCNGDKWESEIASNLQADHLYR,NADH dehydrogenase,Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.,"The mutation in the ND23 gene affects the phenotype of ND23 mutants. These mutants exhibit reduced lifespan, neurodegeneration, abnormal mitochondrial morphology, and decreased ATP levels. This mutation is similar to those observed in patients with Leigh syndrome, which is caused by mutations in nuclear genes encoding mitochondrial proteins. The severity of the ND23 mutation's phenotype varies depending on the maternally inherited mitochondrial background. Sequence analysis identified a variant affecting a mitochondrially encoded component of complex I as a likely candidate for the phenotypic interaction with mutant ND23.","Disrupts mitochondrial function and results in enlarged mitochondria. Neurons present vacuolar lesions leading to neurodegeneration in the central brain. Results in behavioral defects and shorten lifespan. The mutation in the ND23 gene affects the phenotype of ND23 mutants. These mutants exhibit reduced lifespan, neurodegeneration, abnormal mitochondrial morphology, and decreased ATP levels. This mutation is similar to those observed in patients with Leigh syndrome, which is caused by mutations in nuclear genes encoding mitochondrial proteins. The severity of the ND23 mutation's phenotype varies depending on the maternally inherited mitochondrial background. Sequence analysis identified a variant affecting a mitochondrially encoded component of complex I as a likely candidate for the phenotypic interaction with mutant ND23."
136,136,116533,Q92504-E280G,MARGLGAPHWVAVGLLTWATLGLLVAGLGGHDDLHDDLQEDFHGHSHRHSHEDFHHGHSHAHGHGHTHESIWHGHTHDHDHGHSHEDLHHGHSHGYSHESLYHRGHGHDHEHSHGGYGESGAPGIKQDLDAVTLWAYALGATVLISAAPFFVLFLIPVESNSPRHRSLLQILLSFASGGLLGDAFLHLIPHALEPHSHHTLEQPGHGHSHSGQGPILSVGLWVLSGIVAFLVVEKFVRHVKGGHGHSHGHGHAHSHTRGSHGHGRQERSTKEKQSSEEEGKETRGVQKRRGGSTVPKDGPVRPQNAEEEKRGLDLRVSGYLNLAADLAHNFTDGLAIGASFRGGRGLGILTTMTVLLHEVPHEVGDFAILVQSGCSKKQAMRLQLLTAVGALAGTACALLTEGGAVGSEIAGGAGPGWVLPFTAGGFIYVATVSVLPELLREASPLQSLLEVLGLLGGVIMMVLIAHLE,,,MARGLGAPHWVAVGLLTWATLGLLVAGLGGHDDLHDDLQEDFHGHSHRHSHEDFHHGHSHAHGHGHTHESIWHGHTHDHDHGHSHEDLHHGHSHGYSHESLYHRGHGHDHEHSHGGYGESGAPGIKQDLDAVTLWAYALGATVLISAAPFFVLFLIPVESNSPRHRSLLQILLSFASGGLLGDAFLHLIPHALEPHSHHTLEQPGHGHSHSGQGPILSVGLWVLSGIVAFLVVEKFVRHVKGGHGHSHGHGHAHSHTRGSHGHGRQERSTKEKQSSEEEEKETRGVQKRRGGSTVPKDGPVRPQNAEEEKRGLDLRVSGYLNLAADLAHNFTDGLAIGASFRGGRGLGILTTMTVLLHEVPHEVGDFAILVQSGCSKKQAMRLQLLTAVGALAGTACALLTEGGAVGSEIAGGAGPGWVLPFTAGGFIYVATVSVLPELLREASPLQSLLEVLGLLGGVIMMVLIAHLE,Zinc transporter SLC39A7,"Transports Zn(2+) from the endoplasmic reticulum (ER)/Golgi apparatus to the cytosol, playing an essential role in the regulation of cytosolic zinc levels. Acts as gatekeeper of zinc release from intracellular stores, requiring post-translational activation by phosphorylation, resulting in activation of multiple downstream pathways leading to cell growth and proliferation. Has an essential role in B cell development and is required for proper B cell receptor signaling. Plays an important role in maintaining intestinal epithelial homeostasis and skin dermis development by regulating ER function. Controls cell signaling pathways involved in glucose metabolism in skeletal muscle. Has a protective role against ER stress in differents biological contexts. Mediates Zn(2+)-induced ferroptosis.",The functional changes caused by the mutation in HKE6 are not mentioned in the document.,The functional changes caused by the mutation in HKE6 are not mentioned in the document.
137,137,117042,P08692-R60A,MSNITIYHNPACGTSRNTLEMIRNSGTEPTIILYLENPPSRDELVKLIADMGISVRALLAKNVEPYEQLGLAEDKFTDDQLIDFMLQHPILINRPIVVTPLGTRLCRPSEVVLDILQDAQKGAFTKEDGEKVVDEAGKRLK,50-fold decrease in catalytic efficiency with arsenate. Mutant is sensitive to arsenate.,,MSNITIYHNPACGTSRNTLEMIRNSGTEPTIILYLENPPSRDELVKLIADMGISVRALLRKNVEPYEQLGLAEDKFTDDQLIDFMLQHPILINRPIVVTPLGTRLCRPSEVVLDILQDAQKGAFTKEDGEKVVDEAGKRLK,Arsenate reductase,Involved in resistance to arsenate. Catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)]. The resulting arsenite is then extruded from the cell via the ArsAB transport system (Probable).,The mutation confers varying levels of enzymatic activity.,50-fold decrease in catalytic efficiency with arsenate. Mutant is sensitive to arsenate. The mutation confers varying levels of enzymatic activity.
138,138,118034,P67812-D121N,MLSLDFLDDVRRMNKRQLYYQVLNFGMIVSSALMIWKGLMVITGSESPIVVVLSGSMEPAFHRGDLLFLTNRVEDPIRVGEIVVFRIEGREIPIVHRVLKIHEKQNGHIKFLTKGDNNAVNDRGLYKQGQHWLEKKDVVGRARGFVPYIGIVTILMNDYPKFKYAVLFLLGLFVLVHRE,No effect on catalytic activity or protein stability.,,MLSLDFLDDVRRMNKRQLYYQVLNFGMIVSSALMIWKGLMVITGSESPIVVVLSGSMEPAFHRGDLLFLTNRVEDPIRVGEIVVFRIEGREIPIVHRVLKIHEKQNGHIKFLTKGDNNAVDDRGLYKQGQHWLEKKDVVGRARGFVPYIGIVTILMNDYPKFKYAVLFLLGLFVLVHRE,Signal peptidase complex catalytic subunit SEC11A,Catalytic component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum. Specifically cleaves N-terminal signal peptides that contain a hydrophobic alpha-helix (h-region) shorter than 18-20 amino acids.,,No effect on catalytic activity or protein stability.
139,139,118142,P51843-A300V,MAGENHQWQGSILYNMLMSAKQTRAAPEAPETRLVDQCWGCSCGDEPGVGREGLLGGRNVALLYRCCFCGKDHPRQGSILYSMLTSAKQTYAAPKAPEATLGPCWGCSCGSDPGVGRAGLPGGRPVALLYRCCFCGEDHPRQGSILYSLLTSSKQTHVAPAAPEARPGGAWWDRSYFAQRPGGKEALPGGRATALLYRCCFCGEDHPQQGSTLYCVPTSTNQAQAAPEERPRAPWWDTSSGALRPVALKSPQVVCEAASAGLLKTLRFVKYLPCFQVLPLDQQLVLVRNCWASLLMLELVQDRLQFETVEVSEPSMLQKILTTRRRETGGNEPLPVPTLQHHLAPPAEARKVPSASQVQAIKCFLSKCWSLNISTKEYAYLKGTVLFNPDVPGLQCVKYIQGLQWGTQQILSEHTRMTHQGPHDRFIELNSTLFLLRFINANVIAELFFRPIIGTVSMDDMMLEMLCTKI,In AHC.,,MAGENHQWQGSILYNMLMSAKQTRAAPEAPETRLVDQCWGCSCGDEPGVGREGLLGGRNVALLYRCCFCGKDHPRQGSILYSMLTSAKQTYAAPKAPEATLGPCWGCSCGSDPGVGRAGLPGGRPVALLYRCCFCGEDHPRQGSILYSLLTSSKQTHVAPAAPEARPGGAWWDRSYFAQRPGGKEALPGGRATALLYRCCFCGEDHPQQGSTLYCVPTSTNQAQAAPEERPRAPWWDTSSGALRPVALKSPQVVCEAASAGLLKTLRFVKYLPCFQVLPLDQQLVLVRNCWASLLMLELAQDRLQFETVEVSEPSMLQKILTTRRRETGGNEPLPVPTLQHHLAPPAEARKVPSASQVQAIKCFLSKCWSLNISTKEYAYLKGTVLFNPDVPGLQCVKYIQGLQWGTQQILSEHTRMTHQGPHDRFIELNSTLFLLRFINANVIAELFFRPIIGTVSMDDMMLEMLCTKI,Nuclear receptor subfamily 0 group B member 1,Orphan nuclear receptor. Component of a cascade required for the development of the hypothalamic-pituitary-adrenal-gonadal axis. Acts as a coregulatory protein that inhibits the transcriptional activity of other nuclear receptors through heterodimeric interactions. May also have a role in the development of the embryo and in the maintenance of embryonic stem cell pluripotency.,"The presence of the mutation in the DAX-1 gene allows for a normal reproductive axis at birth. However, sometime between infancy and puberty, this mutation leads to an inability to activate the reproductive axis, resulting in the absence of puberty development in this infant.","In AHC. The presence of the mutation in the DAX-1 gene allows for a normal reproductive axis at birth. However, sometime between infancy and puberty, this mutation leads to an inability to activate the reproductive axis, resulting in the absence of puberty development in this infant."
140,140,118541,P15917-I184A,MNIKKEFIKVISMSCLVTAITLSGPVFIPLVQGAGGHGDVGMHVKEKEKNKDENKRKDEERNKTQEEHLKEIMKHIVKIEVKGEEAVKKEAAEKLLEKVPSDVLEMYKAIGGKIYIVDGDITKHISLEALSEDKKKIKDIYGKDALLHEHYVYAKEGYEPVLVIQSSEDYVENTEKALNVYYEAGKILSRDILSKINQPYQKFLDVLNTIKNASDSDGQDLLFTNQLKEHPTDFSVEFLEQNSNEVQEVFAKAFAYYIEPQHRDVLQLYAPEAFNYMDKFNEQEINLSLEELKDQRMLARYEKWEKIKQHYQHWSDSLSEEGRGLLKKLQIPIEPKKDDIIHSLSQEEKELLKRIQIDSSDFLSTEEKEFLKKLQIDIRDSLSEEEKELLNRIQVDSSNPLSEKEKEFLKKLKLDIQPYDINQRLQDTGGLIDSPSINLDVRKQYKRDIQNIDALLHQSIGSTLYNKIYLYENMNINNLTATLGADLVDSTDNTKINRGIFNEFKKNFKYSISSNYMIVDINERPALDNERLKWRIQLSPDTRAGYLENGKLILQRNIGLEIKDVQIIKQSEKEYIRIDAKVVPKSKIDTKIQEAQLNINQEWNKALGLPKYTKLITFNVHNRYASNIVESAYLILNEWKNNIQSDLIKKVTNYLVDGNGRFVFTDITLPNIAEQYTHQDEIYEQVHSKGLYVPESRSILLHGPSKGVELRNDSEGFIHEFGHAVDDYAGYLLDKNQSDLVTNSKKFIDIFKEEGSNLTSYGRTNEAEFFAEAFRLMHSTDHAERLKVQKNAPKTFQFINDQIKFIINS,Loss of ability to bind to PA.,,MNIKKEFIKVISMSCLVTAITLSGPVFIPLVQGAGGHGDVGMHVKEKEKNKDENKRKDEERNKTQEEHLKEIMKHIVKIEVKGEEAVKKEAAEKLLEKVPSDVLEMYKAIGGKIYIVDGDITKHISLEALSEDKKKIKDIYGKDALLHEHYVYAKEGYEPVLVIQSSEDYVENTEKALNVYYEIGKILSRDILSKINQPYQKFLDVLNTIKNASDSDGQDLLFTNQLKEHPTDFSVEFLEQNSNEVQEVFAKAFAYYIEPQHRDVLQLYAPEAFNYMDKFNEQEINLSLEELKDQRMLARYEKWEKIKQHYQHWSDSLSEEGRGLLKKLQIPIEPKKDDIIHSLSQEEKELLKRIQIDSSDFLSTEEKEFLKKLQIDIRDSLSEEEKELLNRIQVDSSNPLSEKEKEFLKKLKLDIQPYDINQRLQDTGGLIDSPSINLDVRKQYKRDIQNIDALLHQSIGSTLYNKIYLYENMNINNLTATLGADLVDSTDNTKINRGIFNEFKKNFKYSISSNYMIVDINERPALDNERLKWRIQLSPDTRAGYLENGKLILQRNIGLEIKDVQIIKQSEKEYIRIDAKVVPKSKIDTKIQEAQLNINQEWNKALGLPKYTKLITFNVHNRYASNIVESAYLILNEWKNNIQSDLIKKVTNYLVDGNGRFVFTDITLPNIAEQYTHQDEIYEQVHSKGLYVPESRSILLHGPSKGVELRNDSEGFIHEFGHAVDDYAGYLLDKNQSDLVTNSKKFIDIFKEEGSNLTSYGRTNEAEFFAEAFRLMHSTDHAERLKVQKNAPKTFQFINDQIKFIINS,Lethal factor,"Lethal factor (LF), which constitutes one of the three proteins composing the anthrax toxin, is able to trigger rapid cell death in macrophages. Acts as a protease that cleaves the N-terminal of most dual specificity mitogen-activated protein kinase kinases (MAPKKs or MAP2Ks) (except for MAP2K5): cleavage invariably occurs within the N-terminal proline-rich region preceding the kinase domain, thus disrupting a sequence involved in directing specific protein-protein interactions necessary for the assembly of signaling complexes. Also cleaves mouse Nlrp1b: host Nlrp1b cleavage promotes ubiquitination and degradation of the N-terminal part of Nlrp1b by the proteasome, thereby releasing the cleaved C-terminal part of Nlrp1b, which polymerizes and forms the Nlrp1b inflammasome followed by host cell pyroptosis. Able to cleave mouse Nlrp1b alleles 1 and 5, while it is not able to cleave Nlrp1b alleles 2, 3 and 4. In contrast, does not cleave NLRP1 human ortholog. LF is not toxic by itself and only acts as a lethal factor when associated with protective antigen (PA) to form the lethal toxin (LeTx): PA is required for LF translocation into the host cytosol.",,Loss of ability to bind to PA.
141,141,119271,P08692-D128E,MSNITIYHNPACGTSRNTLEMIRNSGTEPTIILYLENPPSRDELVKLIADMGISVRALLRKNVEPYEQLGLAEDKFTDDQLIDFMLQHPILINRPIVVTPLGTRLCRPSEVVLDILQDAQKGAFTKEEGEKVVDEAGKRLK,"7-fold decrease in catalytic efficiency with arsenate. Mutant is relatively resistant to arsenate, but is more sensitive at higher concentrations.",,MSNITIYHNPACGTSRNTLEMIRNSGTEPTIILYLENPPSRDELVKLIADMGISVRALLRKNVEPYEQLGLAEDKFTDDQLIDFMLQHPILINRPIVVTPLGTRLCRPSEVVLDILQDAQKGAFTKEDGEKVVDEAGKRLK,Arsenate reductase,Involved in resistance to arsenate. Catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)]. The resulting arsenite is then extruded from the cell via the ArsAB transport system (Probable).,,"7-fold decrease in catalytic efficiency with arsenate. Mutant is relatively resistant to arsenate, but is more sensitive at higher concentrations."
142,142,119827,Q14956-S531I,MECLYYFLGFLLLAARLPLDAAKRFHDVLGNERPSAYMREHNQLNGWSSDENDWNEKLYPVWKRGDMRWKNSWKGGRVQAVLTSDSPALVGSNITFAVNLIFPRCQKEDANGNIVYEKNCRNEAGLSADPYVYNWTAWSEDSDGENGTGQSHHNVFPDGKPFPHHPGWRRWNFIYVFHTLGQYFQKLGRCSVRVSVNTANVTLGPQLMEVTVYRRHGRAYVPIAQVKDVYVVTDQIPVFVTMFQKNDRNSSDETFLKDLPIMFDVLIHDPSHFLNYSTINYKWSFGDNTGLFVSTNHTVNHTYVLNGTFSLNLTVKAAAPGPCPPPPPPPRPSKPTPSLATTLKSYDSNTPGPAGDNPLELSRIPDENCQINRYGHFQATITIVEGILEVNIIQMTDVLMPVPWPESSLIDFVVTCQGSIPTEVCTIISDPTCEITQNTVCSPVDVDEMCLLTVRRTFNGSGTYCVNLTLGDDTSLALTSTLISVPDRDPASPLRMANSALISVGCLAIFVTVISLLVYKKHKEYNPIENIPGNVVRSKGLSVFLNRAKAVFFPGNQEKDPLLKNQEFKGVS,In a breast cancer sample; somatic mutation.,,MECLYYFLGFLLLAARLPLDAAKRFHDVLGNERPSAYMREHNQLNGWSSDENDWNEKLYPVWKRGDMRWKNSWKGGRVQAVLTSDSPALVGSNITFAVNLIFPRCQKEDANGNIVYEKNCRNEAGLSADPYVYNWTAWSEDSDGENGTGQSHHNVFPDGKPFPHHPGWRRWNFIYVFHTLGQYFQKLGRCSVRVSVNTANVTLGPQLMEVTVYRRHGRAYVPIAQVKDVYVVTDQIPVFVTMFQKNDRNSSDETFLKDLPIMFDVLIHDPSHFLNYSTINYKWSFGDNTGLFVSTNHTVNHTYVLNGTFSLNLTVKAAAPGPCPPPPPPPRPSKPTPSLATTLKSYDSNTPGPAGDNPLELSRIPDENCQINRYGHFQATITIVEGILEVNIIQMTDVLMPVPWPESSLIDFVVTCQGSIPTEVCTIISDPTCEITQNTVCSPVDVDEMCLLTVRRTFNGSGTYCVNLTLGDDTSLALTSTLISVPDRDPASPLRMANSALISVGCLAIFVTVISLLVYKKHKEYNPIENSPGNVVRSKGLSVFLNRAKAVFFPGNQEKDPLLKNQEFKGVS,Transmembrane glycoprotein NMB,Could be a melanogenic enzyme.,,In a breast cancer sample; somatic mutation.
143,143,120126,P15917-H719A,MNIKKEFIKVISMSCLVTAITLSGPVFIPLVQGAGGHGDVGMHVKEKEKNKDENKRKDEERNKTQEEHLKEIMKHIVKIEVKGEEAVKKEAAEKLLEKVPSDVLEMYKAIGGKIYIVDGDITKHISLEALSEDKKKIKDIYGKDALLHEHYVYAKEGYEPVLVIQSSEDYVENTEKALNVYYEIGKILSRDILSKINQPYQKFLDVLNTIKNASDSDGQDLLFTNQLKEHPTDFSVEFLEQNSNEVQEVFAKAFAYYIEPQHRDVLQLYAPEAFNYMDKFNEQEINLSLEELKDQRMLARYEKWEKIKQHYQHWSDSLSEEGRGLLKKLQIPIEPKKDDIIHSLSQEEKELLKRIQIDSSDFLSTEEKEFLKKLQIDIRDSLSEEEKELLNRIQVDSSNPLSEKEKEFLKKLKLDIQPYDINQRLQDTGGLIDSPSINLDVRKQYKRDIQNIDALLHQSIGSTLYNKIYLYENMNINNLTATLGADLVDSTDNTKINRGIFNEFKKNFKYSISSNYMIVDINERPALDNERLKWRIQLSPDTRAGYLENGKLILQRNIGLEIKDVQIIKQSEKEYIRIDAKVVPKSKIDTKIQEAQLNINQEWNKALGLPKYTKLITFNVHNRYASNIVESAYLILNEWKNNIQSDLIKKVTNYLVDGNGRFVFTDITLPNIAEQYTHQDEIYEQVHSKGLYVPESRSILLHGPSKGVELRNDSEGFIAEFGHAVDDYAGYLLDKNQSDLVTNSKKFIDIFKEEGSNLTSYGRTNEAEFFAEAFRLMHSTDHAERLKVQKNAPKTFQFINDQIKFIINS,Loss of activity and zinc binding.,,MNIKKEFIKVISMSCLVTAITLSGPVFIPLVQGAGGHGDVGMHVKEKEKNKDENKRKDEERNKTQEEHLKEIMKHIVKIEVKGEEAVKKEAAEKLLEKVPSDVLEMYKAIGGKIYIVDGDITKHISLEALSEDKKKIKDIYGKDALLHEHYVYAKEGYEPVLVIQSSEDYVENTEKALNVYYEIGKILSRDILSKINQPYQKFLDVLNTIKNASDSDGQDLLFTNQLKEHPTDFSVEFLEQNSNEVQEVFAKAFAYYIEPQHRDVLQLYAPEAFNYMDKFNEQEINLSLEELKDQRMLARYEKWEKIKQHYQHWSDSLSEEGRGLLKKLQIPIEPKKDDIIHSLSQEEKELLKRIQIDSSDFLSTEEKEFLKKLQIDIRDSLSEEEKELLNRIQVDSSNPLSEKEKEFLKKLKLDIQPYDINQRLQDTGGLIDSPSINLDVRKQYKRDIQNIDALLHQSIGSTLYNKIYLYENMNINNLTATLGADLVDSTDNTKINRGIFNEFKKNFKYSISSNYMIVDINERPALDNERLKWRIQLSPDTRAGYLENGKLILQRNIGLEIKDVQIIKQSEKEYIRIDAKVVPKSKIDTKIQEAQLNINQEWNKALGLPKYTKLITFNVHNRYASNIVESAYLILNEWKNNIQSDLIKKVTNYLVDGNGRFVFTDITLPNIAEQYTHQDEIYEQVHSKGLYVPESRSILLHGPSKGVELRNDSEGFIHEFGHAVDDYAGYLLDKNQSDLVTNSKKFIDIFKEEGSNLTSYGRTNEAEFFAEAFRLMHSTDHAERLKVQKNAPKTFQFINDQIKFIINS,Lethal factor,"Lethal factor (LF), which constitutes one of the three proteins composing the anthrax toxin, is able to trigger rapid cell death in macrophages. Acts as a protease that cleaves the N-terminal of most dual specificity mitogen-activated protein kinase kinases (MAPKKs or MAP2Ks) (except for MAP2K5): cleavage invariably occurs within the N-terminal proline-rich region preceding the kinase domain, thus disrupting a sequence involved in directing specific protein-protein interactions necessary for the assembly of signaling complexes. Also cleaves mouse Nlrp1b: host Nlrp1b cleavage promotes ubiquitination and degradation of the N-terminal part of Nlrp1b by the proteasome, thereby releasing the cleaved C-terminal part of Nlrp1b, which polymerizes and forms the Nlrp1b inflammasome followed by host cell pyroptosis. Able to cleave mouse Nlrp1b alleles 1 and 5, while it is not able to cleave Nlrp1b alleles 2, 3 and 4. In contrast, does not cleave NLRP1 human ortholog. LF is not toxic by itself and only acts as a lethal factor when associated with protective antigen (PA) to form the lethal toxin (LeTx): PA is required for LF translocation into the host cytosol.",,Loss of activity and zinc binding.
144,144,122236,P15917-E720D,MNIKKEFIKVISMSCLVTAITLSGPVFIPLVQGAGGHGDVGMHVKEKEKNKDENKRKDEERNKTQEEHLKEIMKHIVKIEVKGEEAVKKEAAEKLLEKVPSDVLEMYKAIGGKIYIVDGDITKHISLEALSEDKKKIKDIYGKDALLHEHYVYAKEGYEPVLVIQSSEDYVENTEKALNVYYEIGKILSRDILSKINQPYQKFLDVLNTIKNASDSDGQDLLFTNQLKEHPTDFSVEFLEQNSNEVQEVFAKAFAYYIEPQHRDVLQLYAPEAFNYMDKFNEQEINLSLEELKDQRMLARYEKWEKIKQHYQHWSDSLSEEGRGLLKKLQIPIEPKKDDIIHSLSQEEKELLKRIQIDSSDFLSTEEKEFLKKLQIDIRDSLSEEEKELLNRIQVDSSNPLSEKEKEFLKKLKLDIQPYDINQRLQDTGGLIDSPSINLDVRKQYKRDIQNIDALLHQSIGSTLYNKIYLYENMNINNLTATLGADLVDSTDNTKINRGIFNEFKKNFKYSISSNYMIVDINERPALDNERLKWRIQLSPDTRAGYLENGKLILQRNIGLEIKDVQIIKQSEKEYIRIDAKVVPKSKIDTKIQEAQLNINQEWNKALGLPKYTKLITFNVHNRYASNIVESAYLILNEWKNNIQSDLIKKVTNYLVDGNGRFVFTDITLPNIAEQYTHQDEIYEQVHSKGLYVPESRSILLHGPSKGVELRNDSEGFIHDFGHAVDDYAGYLLDKNQSDLVTNSKKFIDIFKEEGSNLTSYGRTNEAEFFAEAFRLMHSTDHAERLKVQKNAPKTFQFINDQIKFIINS,Loss of activity. No effect on zinc binding.,,MNIKKEFIKVISMSCLVTAITLSGPVFIPLVQGAGGHGDVGMHVKEKEKNKDENKRKDEERNKTQEEHLKEIMKHIVKIEVKGEEAVKKEAAEKLLEKVPSDVLEMYKAIGGKIYIVDGDITKHISLEALSEDKKKIKDIYGKDALLHEHYVYAKEGYEPVLVIQSSEDYVENTEKALNVYYEIGKILSRDILSKINQPYQKFLDVLNTIKNASDSDGQDLLFTNQLKEHPTDFSVEFLEQNSNEVQEVFAKAFAYYIEPQHRDVLQLYAPEAFNYMDKFNEQEINLSLEELKDQRMLARYEKWEKIKQHYQHWSDSLSEEGRGLLKKLQIPIEPKKDDIIHSLSQEEKELLKRIQIDSSDFLSTEEKEFLKKLQIDIRDSLSEEEKELLNRIQVDSSNPLSEKEKEFLKKLKLDIQPYDINQRLQDTGGLIDSPSINLDVRKQYKRDIQNIDALLHQSIGSTLYNKIYLYENMNINNLTATLGADLVDSTDNTKINRGIFNEFKKNFKYSISSNYMIVDINERPALDNERLKWRIQLSPDTRAGYLENGKLILQRNIGLEIKDVQIIKQSEKEYIRIDAKVVPKSKIDTKIQEAQLNINQEWNKALGLPKYTKLITFNVHNRYASNIVESAYLILNEWKNNIQSDLIKKVTNYLVDGNGRFVFTDITLPNIAEQYTHQDEIYEQVHSKGLYVPESRSILLHGPSKGVELRNDSEGFIHEFGHAVDDYAGYLLDKNQSDLVTNSKKFIDIFKEEGSNLTSYGRTNEAEFFAEAFRLMHSTDHAERLKVQKNAPKTFQFINDQIKFIINS,Lethal factor,"Lethal factor (LF), which constitutes one of the three proteins composing the anthrax toxin, is able to trigger rapid cell death in macrophages. Acts as a protease that cleaves the N-terminal of most dual specificity mitogen-activated protein kinase kinases (MAPKKs or MAP2Ks) (except for MAP2K5): cleavage invariably occurs within the N-terminal proline-rich region preceding the kinase domain, thus disrupting a sequence involved in directing specific protein-protein interactions necessary for the assembly of signaling complexes. Also cleaves mouse Nlrp1b: host Nlrp1b cleavage promotes ubiquitination and degradation of the N-terminal part of Nlrp1b by the proteasome, thereby releasing the cleaved C-terminal part of Nlrp1b, which polymerizes and forms the Nlrp1b inflammasome followed by host cell pyroptosis. Able to cleave mouse Nlrp1b alleles 1 and 5, while it is not able to cleave Nlrp1b alleles 2, 3 and 4. In contrast, does not cleave NLRP1 human ortholog. LF is not toxic by itself and only acts as a lethal factor when associated with protective antigen (PA) to form the lethal toxin (LeTx): PA is required for LF translocation into the host cytosol.",The mutation in the Nlrp1b protein leads to activation of procaspase-1 in nonmyeloid cell lines.,Loss of activity. No effect on zinc binding. The mutation in the Nlrp1b protein leads to activation of procaspase-1 in nonmyeloid cell lines.
145,145,122644,P15917-E183A,MNIKKEFIKVISMSCLVTAITLSGPVFIPLVQGAGGHGDVGMHVKEKEKNKDENKRKDEERNKTQEEHLKEIMKHIVKIEVKGEEAVKKEAAEKLLEKVPSDVLEMYKAIGGKIYIVDGDITKHISLEALSEDKKKIKDIYGKDALLHEHYVYAKEGYEPVLVIQSSEDYVENTEKALNVYYAIGKILSRDILSKINQPYQKFLDVLNTIKNASDSDGQDLLFTNQLKEHPTDFSVEFLEQNSNEVQEVFAKAFAYYIEPQHRDVLQLYAPEAFNYMDKFNEQEINLSLEELKDQRMLARYEKWEKIKQHYQHWSDSLSEEGRGLLKKLQIPIEPKKDDIIHSLSQEEKELLKRIQIDSSDFLSTEEKEFLKKLQIDIRDSLSEEEKELLNRIQVDSSNPLSEKEKEFLKKLKLDIQPYDINQRLQDTGGLIDSPSINLDVRKQYKRDIQNIDALLHQSIGSTLYNKIYLYENMNINNLTATLGADLVDSTDNTKINRGIFNEFKKNFKYSISSNYMIVDINERPALDNERLKWRIQLSPDTRAGYLENGKLILQRNIGLEIKDVQIIKQSEKEYIRIDAKVVPKSKIDTKIQEAQLNINQEWNKALGLPKYTKLITFNVHNRYASNIVESAYLILNEWKNNIQSDLIKKVTNYLVDGNGRFVFTDITLPNIAEQYTHQDEIYEQVHSKGLYVPESRSILLHGPSKGVELRNDSEGFIHEFGHAVDDYAGYLLDKNQSDLVTNSKKFIDIFKEEGSNLTSYGRTNEAEFFAEAFRLMHSTDHAERLKVQKNAPKTFQFINDQIKFIINS,No effect on PA-binding ability.,,MNIKKEFIKVISMSCLVTAITLSGPVFIPLVQGAGGHGDVGMHVKEKEKNKDENKRKDEERNKTQEEHLKEIMKHIVKIEVKGEEAVKKEAAEKLLEKVPSDVLEMYKAIGGKIYIVDGDITKHISLEALSEDKKKIKDIYGKDALLHEHYVYAKEGYEPVLVIQSSEDYVENTEKALNVYYEIGKILSRDILSKINQPYQKFLDVLNTIKNASDSDGQDLLFTNQLKEHPTDFSVEFLEQNSNEVQEVFAKAFAYYIEPQHRDVLQLYAPEAFNYMDKFNEQEINLSLEELKDQRMLARYEKWEKIKQHYQHWSDSLSEEGRGLLKKLQIPIEPKKDDIIHSLSQEEKELLKRIQIDSSDFLSTEEKEFLKKLQIDIRDSLSEEEKELLNRIQVDSSNPLSEKEKEFLKKLKLDIQPYDINQRLQDTGGLIDSPSINLDVRKQYKRDIQNIDALLHQSIGSTLYNKIYLYENMNINNLTATLGADLVDSTDNTKINRGIFNEFKKNFKYSISSNYMIVDINERPALDNERLKWRIQLSPDTRAGYLENGKLILQRNIGLEIKDVQIIKQSEKEYIRIDAKVVPKSKIDTKIQEAQLNINQEWNKALGLPKYTKLITFNVHNRYASNIVESAYLILNEWKNNIQSDLIKKVTNYLVDGNGRFVFTDITLPNIAEQYTHQDEIYEQVHSKGLYVPESRSILLHGPSKGVELRNDSEGFIHEFGHAVDDYAGYLLDKNQSDLVTNSKKFIDIFKEEGSNLTSYGRTNEAEFFAEAFRLMHSTDHAERLKVQKNAPKTFQFINDQIKFIINS,Lethal factor,"Lethal factor (LF), which constitutes one of the three proteins composing the anthrax toxin, is able to trigger rapid cell death in macrophages. Acts as a protease that cleaves the N-terminal of most dual specificity mitogen-activated protein kinase kinases (MAPKKs or MAP2Ks) (except for MAP2K5): cleavage invariably occurs within the N-terminal proline-rich region preceding the kinase domain, thus disrupting a sequence involved in directing specific protein-protein interactions necessary for the assembly of signaling complexes. Also cleaves mouse Nlrp1b: host Nlrp1b cleavage promotes ubiquitination and degradation of the N-terminal part of Nlrp1b by the proteasome, thereby releasing the cleaved C-terminal part of Nlrp1b, which polymerizes and forms the Nlrp1b inflammasome followed by host cell pyroptosis. Able to cleave mouse Nlrp1b alleles 1 and 5, while it is not able to cleave Nlrp1b alleles 2, 3 and 4. In contrast, does not cleave NLRP1 human ortholog. LF is not toxic by itself and only acts as a lethal factor when associated with protective antigen (PA) to form the lethal toxin (LeTx): PA is required for LF translocation into the host cytosol.",,No effect on PA-binding ability.
146,146,123296,Q5EZ72-D198A,MGHSAVLLSVALVILPACVTGGPVQRQQQHKLLLVSFDGFRWNYDQDVETPNLDSMAQEGVKARYMTPAFVTMTSPCHFTLVTGKYIENHGVVHNMFYNTTNKVRLPYHATLGIQRWWDNGSIPIWITAQRQGLKTGSFFYPGGNVTYQGEAVTMSRKEGVLHNYKNETEWRANVDTVMKWFTEEDVSLVTLYFGEPASTGHKYGPESQERKDMVKQVDRTVGYLRDSIKRHHLTDSLNLIITSDHGMTTVNKKASDLVEFHKFPNFTFRDIEFELLDYGPNGMLIPKEGMLEKVYSVLKDAHPRLHVYKKEDFPKTFHYANNPRITSLLMYSDLGYVIHGRVNVQFNSGEHGFDNQDMDMKTIFRAVGPSFKAGLEVEPFESVHVYELMCQLLGIVPEPNDGHPGVLQPMLRSGSPLSRQHHLVVVLMGILTGLAKVV,Abolishes the phosphoric diester hydrolase activity against PAF.,,MGHSAVLLSVALVILPACVTGGPVQRQQQHKLLLVSFDGFRWNYDQDVETPNLDSMAQEGVKARYMTPAFVTMTSPCHFTLVTGKYIENHGVVHNMFYNTTNKVRLPYHATLGIQRWWDNGSIPIWITAQRQGLKTGSFFYPGGNVTYQGEAVTMSRKEGVLHNYKNETEWRANVDTVMKWFTEEDVSLVTLYFGEPDSTGHKYGPESQERKDMVKQVDRTVGYLRDSIKRHHLTDSLNLIITSDHGMTTVNKKASDLVEFHKFPNFTFRDIEFELLDYGPNGMLIPKEGMLEKVYSVLKDAHPRLHVYKKEDFPKTFHYANNPRITSLLMYSDLGYVIHGRVNVQFNSGEHGFDNQDMDMKTIFRAVGPSFKAGLEVEPFESVHVYELMCQLLGIVPEPNDGHPGVLQPMLRSGSPLSRQHHLVVVLMGILTGLAKVV,Ectonucleotide pyrophosphatase/phosphodiesterase family member 7,"Choline-specific phosphodiesterase that hydrolyzes sphingomyelin (SM) releasing the ceramide and phosphocholine and therefore is involved in sphingomyelin digestion, ceramide formation, and fatty acid (FA) absorption in the gastrointestinal tract. Has also phospholipase C activity and can also cleave phosphocholine from palmitoyl lyso-phosphatidylcholine and platelet-activating factor (PAF) leading to its inactivation. Does not have nucleotide pyrophosphatase activity. May promote cholesterol absorption by affecting the levels of sphingomyelin derived from either diet or endogenous sources, in the intestinal lumen.",The activity against PAF was abolished by site mutation of the predicted metal-binding sites that are conserved in all NPP members.,Abolishes the phosphoric diester hydrolase activity against PAF. The activity against PAF was abolished by site mutation of the predicted metal-binding sites that are conserved in all NPP members.
147,147,123822,Q0WRB0-V377M,MELNCVQFLRNKTILVTGATGFLAKVFVEKILRVQPNVKKLYLLVRASDNEAATKRLRTEVFEKELFKVLRQNLGDEKLNTLLYEKVVSVPGDIATDQLGINDSHLRERMQKEIDIVVNVAATTNFDERYDVGLGINTFGALNVLNFAKKCVKVQLLLHVSTAYVCGEKPGLIPEKPFIMEEIRNENGLQLDINLERELMKQRLKELNEQDCSEEDITLSMKELGMERAKLHGWPNTYVFTKSMGEMLLGKHKENLPLVIIRPTMITSTLSEPFPGWIEGLRTVDSVIIAYGKGVLKCFLVDVNSVCDMIPVDMVANAMITAAAKHAGGSGVHMVYHVGSSHQNPVTFGEIHEIAVRYFTKNPLRSRNGSLITVSKMRFIPTMALFSLYMTLRYKLPLQLLKLVDIIYPWRNGDKYGDKNRKIELVMRLVELYEPYVLFKGIFDDRNTKSLCANQKEEEIKNTEKLMFDFDPKGINWGDYLTNIHISGLVTHVLKK,Catalyzes the formation of C16:0 fatty alcohol instead of C18:0; when associated with L-355.,,MELNCVQFLRNKTILVTGATGFLAKVFVEKILRVQPNVKKLYLLVRASDNEAATKRLRTEVFEKELFKVLRQNLGDEKLNTLLYEKVVSVPGDIATDQLGINDSHLRERMQKEIDIVVNVAATTNFDERYDVGLGINTFGALNVLNFAKKCVKVQLLLHVSTAYVCGEKPGLIPEKPFIMEEIRNENGLQLDINLERELMKQRLKELNEQDCSEEDITLSMKELGMERAKLHGWPNTYVFTKSMGEMLLGKHKENLPLVIIRPTMITSTLSEPFPGWIEGLRTVDSVIIAYGKGVLKCFLVDVNSVCDMIPVDMVANAMITAAAKHAGGSGVHMVYHVGSSHQNPVTFGEIHEIAVRYFTKNPLRSRNGSLITVSKVRFIPTMALFSLYMTLRYKLPLQLLKLVDIIYPWRNGDKYGDKNRKIELVMRLVELYEPYVLFKGIFDDRNTKSLCANQKEEEIKNTEKLMFDFDPKGINWGDYLTNIHISGLVTHVLKK,Probable fatty acyl-CoA reductase 5,"Catalyzes the reduction of fatty acyl-CoA to fatty alcohols. Catalyzes specifically the formation of C18:0 fatty alcohol. Provides the fatty alcohols required for synthesis of suberin in roots, seed coat and wound-induced leaf tissue. Provides the fatty alcohols required for synthesis of alkyl hydroxycinnamates in root waxes.",,Catalyzes the formation of C16:0 fatty alcohol instead of C18:0; when associated with L-355.
148,148,125608,P32266-S224N,MNASPVRLLILRRQLATHPAILYSSPYIKSPLVHLHSRMSNVHRSAHANALSFVITRRSISHFPKIISKIIRLPIYVGGGMAAAGSYIAYKMEEASSFTKDKLDRIKDLGESMKEKFNKMFSGDKSQDGGHGNDGTVPTATLIAATSLDDDESKRQGDPKDDDDEDDDDEDDENDSVDTTQDEMLNLTKQMIEIRTILNKVDSSSAHLTLPSIVVIGSQSSGKNSVLESIVGREFLPKGSNMVTRRPIELTLVNTPNSNNVTADFPSMRLYNIKDFKEVKRMLMELNMAVPTSEAVSEEPIQLTIKSSRVPDLSLVDLPGYIQVEAADQPIELKTKIRDLCEKYLTAPNIILAISAADVDLANSSALKASKAADPKGLRTIGVITKLDLVDPEKARSILNNKKYPLSMGYVGVITKTPSSINRKHLGLFGEAPSSSLSGIFSKGQHGQSSGEENTNGLKQIVSHQFEKAYFKENKKYFTNCQVSTKKLREKLIKILEISMSNALEPTSTLIQQELDDTSYLFKVEFNDRHLTPKSYLLNNIDVLKLGIKEFQEKFHRNELKSILRAELDQKVLDVLATRYWKDDNLQDLSSSKLESDTDMLYWHKKLELASSGLTKMGIGRLSTMLTTNAILKELDNILESTQLKNHELIKDLVSNTAINVLNSKYYSTADQVENCIKPFKYEIDLEERDWSLARQHSINLIKEELRQCNSRYQAIKNAVGSKKLANVMGYLENESNLQKETLGMSKLLLERGSEAIFLDKRCKVLSFRLKMLKNKCHSTIEKDRCPEVFLSAVSDKLTSTAVLFLNVELLSDFFYNFPIELDRRLTLLGDEQVEMFAKEDPKISRHIELQKRKELLELALEKIDSILVFKKSYKGVSKNL,Loss of GTPase activity.,,MNASPVRLLILRRQLATHPAILYSSPYIKSPLVHLHSRMSNVHRSAHANALSFVITRRSISHFPKIISKIIRLPIYVGGGMAAAGSYIAYKMEEASSFTKDKLDRIKDLGESMKEKFNKMFSGDKSQDGGHGNDGTVPTATLIAATSLDDDESKRQGDPKDDDDEDDDDEDDENDSVDTTQDEMLNLTKQMIEIRTILNKVDSSSAHLTLPSIVVIGSQSSGKSSVLESIVGREFLPKGSNMVTRRPIELTLVNTPNSNNVTADFPSMRLYNIKDFKEVKRMLMELNMAVPTSEAVSEEPIQLTIKSSRVPDLSLVDLPGYIQVEAADQPIELKTKIRDLCEKYLTAPNIILAISAADVDLANSSALKASKAADPKGLRTIGVITKLDLVDPEKARSILNNKKYPLSMGYVGVITKTPSSINRKHLGLFGEAPSSSLSGIFSKGQHGQSSGEENTNGLKQIVSHQFEKAYFKENKKYFTNCQVSTKKLREKLIKILEISMSNALEPTSTLIQQELDDTSYLFKVEFNDRHLTPKSYLLNNIDVLKLGIKEFQEKFHRNELKSILRAELDQKVLDVLATRYWKDDNLQDLSSSKLESDTDMLYWHKKLELASSGLTKMGIGRLSTMLTTNAILKELDNILESTQLKNHELIKDLVSNTAINVLNSKYYSTADQVENCIKPFKYEIDLEERDWSLARQHSINLIKEELRQCNSRYQAIKNAVGSKKLANVMGYLENESNLQKETLGMSKLLLERGSEAIFLDKRCKVLSFRLKMLKNKCHSTIEKDRCPEVFLSAVSDKLTSTAVLFLNVELLSDFFYNFPIELDRRLTLLGDEQVEMFAKEDPKISRHIELQKRKELLELALEKIDSILVFKKSYKGVSKNL,"Dynamin-like GTPase MGM1, mitochondrial",Dynamin-related GTPase required for mitochondrial fusion. Coordinates interaction between the inner and outer mitochondrial membrane to promote the formation of the double membrane.,"The mdm17 mutation causes temperature-dependent defects in mitochondrial inheritance, mitochondrial morphology, and the maintenance of mitochondrial DNA in the yeast Saccharomyces cerevisiae. Defects in mitochondrial transmission to daughter buds and changes in mitochondrial morphology were apparent within 30 min after shifting cells to 37 degrees C, while loss of the mitochondrial genome occurred after 4-24 h at the elevated temperature. The mdm17 lesion mapped to MGM1, a gene encoding a dynamin-like GTPase previously implicated in mitochondrial genome maintenance, and the cloned MGM1 gene complements all of the mdm17 mutant phenotypes. Cells with an mgm1-null mutation displayed aberrant mitochondrial inheritance and morphology. Mutations at cause mitochondrial fragmentation and a loss of mitochondrial DNA.","Loss of GTPase activity. The mdm17 mutation causes temperature-dependent defects in mitochondrial inheritance, mitochondrial morphology, and the maintenance of mitochondrial DNA in the yeast Saccharomyces cerevisiae. Defects in mitochondrial transmission to daughter buds and changes in mitochondrial morphology were apparent within 30 min after shifting cells to 37 degrees C, while loss of the mitochondrial genome occurred after 4-24 h at the elevated temperature. The mdm17 lesion mapped to MGM1, a gene encoding a dynamin-like GTPase previously implicated in mitochondrial genome maintenance, and the cloned MGM1 gene complements all of the mdm17 mutant phenotypes. Cells with an mgm1-null mutation displayed aberrant mitochondrial inheritance and morphology. Mutations at cause mitochondrial fragmentation and a loss of mitochondrial DNA."
149,149,125610,Q92504-T395I,MARGLGAPHWVAVGLLTWATLGLLVAGLGGHDDLHDDLQEDFHGHSHRHSHEDFHHGHSHAHGHGHTHESIWHGHTHDHDHGHSHEDLHHGHSHGYSHESLYHRGHGHDHEHSHGGYGESGAPGIKQDLDAVTLWAYALGATVLISAAPFFVLFLIPVESNSPRHRSLLQILLSFASGGLLGDAFLHLIPHALEPHSHHTLEQPGHGHSHSGQGPILSVGLWVLSGIVAFLVVEKFVRHVKGGHGHSHGHGHAHSHTRGSHGHGRQERSTKEKQSSEEEEKETRGVQKRRGGSTVPKDGPVRPQNAEEEKRGLDLRVSGYLNLAADLAHNFTDGLAIGASFRGGRGLGILTTMTVLLHEVPHEVGDFAILVQSGCSKKQAMRLQLLTAVGALAGIACALLTEGGAVGSEIAGGAGPGWVLPFTAGGFIYVATVSVLPELLREASPLQSLLEVLGLLGGVIMMVLIAHLE,In AGM9; unknown pathological significance.,,MARGLGAPHWVAVGLLTWATLGLLVAGLGGHDDLHDDLQEDFHGHSHRHSHEDFHHGHSHAHGHGHTHESIWHGHTHDHDHGHSHEDLHHGHSHGYSHESLYHRGHGHDHEHSHGGYGESGAPGIKQDLDAVTLWAYALGATVLISAAPFFVLFLIPVESNSPRHRSLLQILLSFASGGLLGDAFLHLIPHALEPHSHHTLEQPGHGHSHSGQGPILSVGLWVLSGIVAFLVVEKFVRHVKGGHGHSHGHGHAHSHTRGSHGHGRQERSTKEKQSSEEEEKETRGVQKRRGGSTVPKDGPVRPQNAEEEKRGLDLRVSGYLNLAADLAHNFTDGLAIGASFRGGRGLGILTTMTVLLHEVPHEVGDFAILVQSGCSKKQAMRLQLLTAVGALAGTACALLTEGGAVGSEIAGGAGPGWVLPFTAGGFIYVATVSVLPELLREASPLQSLLEVLGLLGGVIMMVLIAHLE,Zinc transporter SLC39A7,"Transports Zn(2+) from the endoplasmic reticulum (ER)/Golgi apparatus to the cytosol, playing an essential role in the regulation of cytosolic zinc levels. Acts as gatekeeper of zinc release from intracellular stores, requiring post-translational activation by phosphorylation, resulting in activation of multiple downstream pathways leading to cell growth and proliferation. Has an essential role in B cell development and is required for proper B cell receptor signaling. Plays an important role in maintaining intestinal epithelial homeostasis and skin dermis development by regulating ER function. Controls cell signaling pathways involved in glucose metabolism in skeletal muscle. Has a protective role against ER stress in differents biological contexts. Mediates Zn(2+)-induced ferroptosis.",,In AGM9; unknown pathological significance.
150,150,126323,P15917-K186A,MNIKKEFIKVISMSCLVTAITLSGPVFIPLVQGAGGHGDVGMHVKEKEKNKDENKRKDEERNKTQEEHLKEIMKHIVKIEVKGEEAVKKEAAEKLLEKVPSDVLEMYKAIGGKIYIVDGDITKHISLEALSEDKKKIKDIYGKDALLHEHYVYAKEGYEPVLVIQSSEDYVENTEKALNVYYEIGAILSRDILSKINQPYQKFLDVLNTIKNASDSDGQDLLFTNQLKEHPTDFSVEFLEQNSNEVQEVFAKAFAYYIEPQHRDVLQLYAPEAFNYMDKFNEQEINLSLEELKDQRMLARYEKWEKIKQHYQHWSDSLSEEGRGLLKKLQIPIEPKKDDIIHSLSQEEKELLKRIQIDSSDFLSTEEKEFLKKLQIDIRDSLSEEEKELLNRIQVDSSNPLSEKEKEFLKKLKLDIQPYDINQRLQDTGGLIDSPSINLDVRKQYKRDIQNIDALLHQSIGSTLYNKIYLYENMNINNLTATLGADLVDSTDNTKINRGIFNEFKKNFKYSISSNYMIVDINERPALDNERLKWRIQLSPDTRAGYLENGKLILQRNIGLEIKDVQIIKQSEKEYIRIDAKVVPKSKIDTKIQEAQLNINQEWNKALGLPKYTKLITFNVHNRYASNIVESAYLILNEWKNNIQSDLIKKVTNYLVDGNGRFVFTDITLPNIAEQYTHQDEIYEQVHSKGLYVPESRSILLHGPSKGVELRNDSEGFIHEFGHAVDDYAGYLLDKNQSDLVTNSKKFIDIFKEEGSNLTSYGRTNEAEFFAEAFRLMHSTDHAERLKVQKNAPKTFQFINDQIKFIINS,Loss of ability to bind to PA.,,MNIKKEFIKVISMSCLVTAITLSGPVFIPLVQGAGGHGDVGMHVKEKEKNKDENKRKDEERNKTQEEHLKEIMKHIVKIEVKGEEAVKKEAAEKLLEKVPSDVLEMYKAIGGKIYIVDGDITKHISLEALSEDKKKIKDIYGKDALLHEHYVYAKEGYEPVLVIQSSEDYVENTEKALNVYYEIGKILSRDILSKINQPYQKFLDVLNTIKNASDSDGQDLLFTNQLKEHPTDFSVEFLEQNSNEVQEVFAKAFAYYIEPQHRDVLQLYAPEAFNYMDKFNEQEINLSLEELKDQRMLARYEKWEKIKQHYQHWSDSLSEEGRGLLKKLQIPIEPKKDDIIHSLSQEEKELLKRIQIDSSDFLSTEEKEFLKKLQIDIRDSLSEEEKELLNRIQVDSSNPLSEKEKEFLKKLKLDIQPYDINQRLQDTGGLIDSPSINLDVRKQYKRDIQNIDALLHQSIGSTLYNKIYLYENMNINNLTATLGADLVDSTDNTKINRGIFNEFKKNFKYSISSNYMIVDINERPALDNERLKWRIQLSPDTRAGYLENGKLILQRNIGLEIKDVQIIKQSEKEYIRIDAKVVPKSKIDTKIQEAQLNINQEWNKALGLPKYTKLITFNVHNRYASNIVESAYLILNEWKNNIQSDLIKKVTNYLVDGNGRFVFTDITLPNIAEQYTHQDEIYEQVHSKGLYVPESRSILLHGPSKGVELRNDSEGFIHEFGHAVDDYAGYLLDKNQSDLVTNSKKFIDIFKEEGSNLTSYGRTNEAEFFAEAFRLMHSTDHAERLKVQKNAPKTFQFINDQIKFIINS,Lethal factor,"Lethal factor (LF), which constitutes one of the three proteins composing the anthrax toxin, is able to trigger rapid cell death in macrophages. Acts as a protease that cleaves the N-terminal of most dual specificity mitogen-activated protein kinase kinases (MAPKKs or MAP2Ks) (except for MAP2K5): cleavage invariably occurs within the N-terminal proline-rich region preceding the kinase domain, thus disrupting a sequence involved in directing specific protein-protein interactions necessary for the assembly of signaling complexes. Also cleaves mouse Nlrp1b: host Nlrp1b cleavage promotes ubiquitination and degradation of the N-terminal part of Nlrp1b by the proteasome, thereby releasing the cleaved C-terminal part of Nlrp1b, which polymerizes and forms the Nlrp1b inflammasome followed by host cell pyroptosis. Able to cleave mouse Nlrp1b alleles 1 and 5, while it is not able to cleave Nlrp1b alleles 2, 3 and 4. In contrast, does not cleave NLRP1 human ortholog. LF is not toxic by itself and only acts as a lethal factor when associated with protective antigen (PA) to form the lethal toxin (LeTx): PA is required for LF translocation into the host cytosol.",,Loss of ability to bind to PA.
151,151,127198,Q9UPT6-H994Q,MMEIQMDEGGGVVVYQDDYCSGSVMSERVSGLAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEERESEMKKEYNALHQRHTEMIQTYVEHIERSKMQQVGGNSQTESSLPGRRKERPTSLNVFPLADGTVRAQIGGKLVPAGDHWHLSDLGQLQSSSSYQCPQDEMSESGQSSAAATPSTTGTKSNTPTSSVPSAAVTPLNESLQPLGDYGVGSKNSKRAREKRDSRNMEVQVTQEMRNVSIGMGSSDEWSDVQDIIDSTPELDMCPETRLDRTGSSPTQGIVNKAFGINTDSLYHELSTAGSEVIGDVDEGADLLGEFSVRDDFFGMGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEAIIARREPKEEAEDVSSYLCTESDKIPMAQRRRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASREHPSVQEKKKSTIWQFFSRLFSSSSSPPPAKRPYPSVNIHYKSPTTAGFSQRRNHAMCPISAGSRPLEFFPDDDCTSSARREQKREQYRQVREHVRNDDGRLQACGWSLPAKYKQLSPNGGQEDTRMKNVPVPVYCRPLVEKDPTMKLWCAAGVNLSGWRPNEDDAGNGVKPAPGRDPLTCDREGDGEPKSAHTSPEKKKAKELPEMDATSSRVWILTSTLTTSKVVIIDANQPGTVVDQFTVCNAHVLCISSIPAASDSDYPPGEMFLDSDVNPEDPGADGVLAGITLVGCATRCNVPRSNCSSRGDTPVLDKGQGEVATIANGKVNPSQSTEEATEATEVPDPGPSEPETATLRPGPLTEHVFTDPAPTPSSGPQPGSENGPEPDSSSTRPEPEPSGDPTGAGSSAAPTMWLGAQNGWLYVHSAVANWKKCLQSIKLKDSVLSLVHVKGRVLVALADGTLAIF,In NEDBA; unknown pathological significance.,,MMEIQMDEGGGVVVYQDDYCSGSVMSERVSGLAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEERESEMKKEYNALHQRHTEMIQTYVEHIERSKMQQVGGNSQTESSLPGRRKERPTSLNVFPLADGTVRAQIGGKLVPAGDHWHLSDLGQLQSSSSYQCPQDEMSESGQSSAAATPSTTGTKSNTPTSSVPSAAVTPLNESLQPLGDYGVGSKNSKRAREKRDSRNMEVQVTQEMRNVSIGMGSSDEWSDVQDIIDSTPELDMCPETRLDRTGSSPTQGIVNKAFGINTDSLYHELSTAGSEVIGDVDEGADLLGEFSVRDDFFGMGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEAIIARREPKEEAEDVSSYLCTESDKIPMAQRRRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASREHPSVQEKKKSTIWQFFSRLFSSSSSPPPAKRPYPSVNIHYKSPTTAGFSQRRNHAMCPISAGSRPLEFFPDDDCTSSARREQKREQYRQVREHVRNDDGRLQACGWSLPAKYKQLSPNGGQEDTRMKNVPVPVYCRPLVEKDPTMKLWCAAGVNLSGWRPNEDDAGNGVKPAPGRDPLTCDREGDGEPKSAHTSPEKKKAKELPEMDATSSRVWILTSTLTTSKVVIIDANQPGTVVDQFTVCNAHVLCISSIPAASDSDYPPGEMFLDSDVNPEDPGADGVLAGITLVGCATRCNVPRSNCSSRGDTPVLDKGQGEVATIANGKVNPSQSTEEATEATEVPDPGPSEPETATLRPGPLTEHVFTDPAPTPSSGPQPGSENGPEPDSSSTRPEPEPSGDPTGAGSSAAPTMWLGAQNGWLYVHSAVANWKKCLHSIKLKDSVLSLVHVKGRVLVALADGTLAIF,C-Jun-amino-terminal kinase-interacting protein 3,"The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. May function as a regulator of vesicle transport, through interactions with the JNK-signaling components and motor proteins. Promotes neuronal axon elongation in a kinesin- and JNK-dependent manner. Activates cofilin at axon tips via local activation of JNK, thereby regulating filopodial dynamics and enhancing axon elongation. Its binding to kinesin heavy chains (KHC), promotes kinesin-1 motility along microtubules and is essential for axon elongation and regeneration. Regulates cortical neuronal migration by mediating NTRK2/TRKB anterograde axonal transport during brain development. Acts as an adapter that bridges the interaction between NTRK2/TRKB and KLC1 and drives NTRK2/TRKB axonal but not dendritic anterograde transport, which is essential for subsequent BDNF-triggered signaling and filopodia formation.","The de novo variant in MAPK8IP3 has been identified in individuals presenting with an overlapping phenotype of mild to severe intellectual disability. Brain anomalies such as perisylvian polymicrogyria, cerebral or cerebellar atrophy, and hypoplasia of the corpus callosum were consistent among individuals harboring this variant.","In NEDBA; unknown pathological significance. The de novo variant in MAPK8IP3 has been identified in individuals presenting with an overlapping phenotype of mild to severe intellectual disability. Brain anomalies such as perisylvian polymicrogyria, cerebral or cerebellar atrophy, and hypoplasia of the corpus callosum were consistent among individuals harboring this variant."
152,152,130362,P25522-D270A,MSDNDTIVAQATPPGRGGVGILRISGFKAREVAETVLGKLPKPRYADYLPFKDADGSVLDQGIALWFPGPNSFTGEDVLELQGHGGPVILDLLLKRILTIPGLRIARPGEFSERAFLNDKLDLAQAEAIADLIDASSEQAARSALNSLQGAFSARVNHLVEALTHLRIYVEAAIDFPDEEIDFLSDGKIEAQLNDVIADLDAVRAEARQGSLLREGMKVVIAGRPNAGKSSLLNALAGREAAIVTDIAGTTRDVLREHIHIDGMPLHIIATAGLREASDEVERIGIERAWQEIEQADRVLFMVDGTTTDAVDPAEIWPEFIARLPAKLPITVVRNKADITGETLGMSEVNGHALIRLSARTGEGVDVLRNHLKQSMGFDTNMEGGFLARRRHLQALEQAAEHLQQGKAQLLGAWAGELLAEELRLAQQNLSEITGEFTSDDLLGRIFSSFCIGK,"Does not affect GTP binding, but impairs hydrolase activity. Completely impairs tRNA modifying function.",,MSDNDTIVAQATPPGRGGVGILRISGFKAREVAETVLGKLPKPRYADYLPFKDADGSVLDQGIALWFPGPNSFTGEDVLELQGHGGPVILDLLLKRILTIPGLRIARPGEFSERAFLNDKLDLAQAEAIADLIDASSEQAARSALNSLQGAFSARVNHLVEALTHLRIYVEAAIDFPDEEIDFLSDGKIEAQLNDVIADLDAVRAEARQGSLLREGMKVVIAGRPNAGKSSLLNALAGREAAIVTDIAGTTRDVLREHIHIDGMPLHIIDTAGLREASDEVERIGIERAWQEIEQADRVLFMVDGTTTDAVDPAEIWPEFIARLPAKLPITVVRNKADITGETLGMSEVNGHALIRLSARTGEGVDVLRNHLKQSMGFDTNMEGGFLARRRHLQALEQAAEHLQQGKAQLLGAWAGELLAEELRLAQQNLSEITGEFTSDDLLGRIFSSFCIGK,tRNA modification GTPase MnmE,"Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.",,"Does not affect GTP binding, but impairs hydrolase activity. Completely impairs tRNA modifying function."
153,153,130799,O75828-Q142M,MSSCSRVALVTGANRGIGLAIARELCRQFSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLNVLVNNAAVAFKSDDPMPFDIKAEMTLKTNFFATRNMCNELLPIMKPHGRVVNISSLMCLRAFENCSEDLQERFHSETLTEGDLVDLMKKFVEDTKNEVHEREGWPNSPYGVSKLGVTVLSRILARRLDEKRKADRILVNACCPGPVKTDMDGKDSIRTVEEGAETPVYLALLPPDATEPQGQLVHDKVVQNW,"Modest increase in carbonyl reductase (NADPH) activity toward 1,2-naphthoquinone.",,MSSCSRVALVTGANRGIGLAIARELCRQFSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLNVLVNNAAVAFKSDDPMPFDIKAEMTLKTNFFATRNMCNELLPIMKPHGRVVNISSLQCLRAFENCSEDLQERFHSETLTEGDLVDLMKKFVEDTKNEVHEREGWPNSPYGVSKLGVTVLSRILARRLDEKRKADRILVNACCPGPVKTDMDGKDSIRTVEEGAETPVYLALLPPDATEPQGQLVHDKVVQNW,Carbonyl reductase [NADPH] 3,"Catalyzes the NADPH-dependent reduction of carbonyl compounds to their corresponding alcohols. Has low NADPH-dependent oxidoreductase activity. Acts on several orthoquinones, acts as well on non-quinone compounds, such as isatin or on the anticancer drug oracin. Best substrates for CBR3 is 1,2- naphthoquinone, hence could play a role in protection against cytotoxicity of exogenous quinones. Exerts activity toward ortho-quinones but not paraquinones. No endogenous substrate for CBR3 except isatin has been identified.",The data reveal that the differences in substrate specificity are largely due to a short segment of a substrate binding loop comprising critical residues M141/Q142 in CBR1.,"Modest increase in carbonyl reductase (NADPH) activity toward 1,2-naphthoquinone. The data reveal that the differences in substrate specificity are largely due to a short segment of a substrate binding loop comprising critical residues M141/Q142 in CBR1."
154,154,133608,Q96RL7-R161H,MVFESVVVDVLNRFLGDYVVDLDTSQLSLGIWKGAVALKNLQIKENALSQLDVPFKVKVGHIGNLKLIIPWKNLYTQPVEAVLEEIYLLIVPSSRIKYDPLKEEKQLMEAKQQELKRIEEAKQKVVDQEQHLPEKQDTFAEKLVTQIIKNLQVKISSIHIHYEDDITNRDKPLSFGISLQNLSMQTTDQYWVPCLHDETEKLVRKLIRLDNLFAYWNVKSQMFYLSDYDNSLDDLKNGIVNENIVPEGYDFVFRPISANAKLVMNRRSDFDFSAPKINLEIELHNIAIEFNKPQYFSIMELLESVDMMAQNLPYRKFKPDVPLHHHAREWWAYAIHGVLEVNVCPRLWMWSWKHIRKHRQKVKQYKELYKKKLTSKKPPGELLVSLEELEKTLDVFNITIARQTAEVEVKKAGYKIYKEGVKDPEDNKGWFSWLWSWSEQNTNEQQPDVQPETLEEMLTPEEKALLYEAIGYSETAVDPTLLKTFEALKFFVHLKSMSIVLRENHQKPELVDIVIEEFSTLIVQRPGAQAIKFETKIDSFHITGLPDNSEKPRLLSSLDDAMSLFQITFEINPLDETVSQRCIIEAEPLEIIYDARTVNSIVEFFRPPKEVHLAQLTAATLTKLEEFRSKTATGLLYIIETQKVLDLKINLKASYIIVPQDGIFSPTSNLLLLDLGHLKVTSKSRSELPDVKQGEANLKEIMDRAYDSFDIQLTSVQLLYSRVGDNWREARKLSVSTQHILVPMHFNLELSKAMVFMDVRMPKFKIYGKLPLISLRISDKKLQGIMELIESIPKPEPVTEVSAPVKSFQIQTSTSLGTSQISQKIIPLLELPSVSEDDSEEEFFDAPCSPLEEPLQFPTGVKSIRTRKLQKQDCSVNMTTFKIRFEVPKVLIEFYHLVGDCELSVVEILVLGLGAEIEIRTYDLKANAFLKEFCLKCPEYLDENKKPVYLVTTLDNTMEDLLTLEYVKAEKNVPDLKSTYNNVLQLIKVNFSSLDIHLHTEALLNTINYLHNILPQSEEKSAPV,In a colorectal cancer sample; somatic mutation.,,MVFESVVVDVLNRFLGDYVVDLDTSQLSLGIWKGAVALKNLQIKENALSQLDVPFKVKVGHIGNLKLIIPWKNLYTQPVEAVLEEIYLLIVPSSRIKYDPLKEEKQLMEAKQQELKRIEEAKQKVVDQEQHLPEKQDTFAEKLVTQIIKNLQVKISSIHIRYEDDITNRDKPLSFGISLQNLSMQTTDQYWVPCLHDETEKLVRKLIRLDNLFAYWNVKSQMFYLSDYDNSLDDLKNGIVNENIVPEGYDFVFRPISANAKLVMNRRSDFDFSAPKINLEIELHNIAIEFNKPQYFSIMELLESVDMMAQNLPYRKFKPDVPLHHHAREWWAYAIHGVLEVNVCPRLWMWSWKHIRKHRQKVKQYKELYKKKLTSKKPPGELLVSLEELEKTLDVFNITIARQTAEVEVKKAGYKIYKEGVKDPEDNKGWFSWLWSWSEQNTNEQQPDVQPETLEEMLTPEEKALLYEAIGYSETAVDPTLLKTFEALKFFVHLKSMSIVLRENHQKPELVDIVIEEFSTLIVQRPGAQAIKFETKIDSFHITGLPDNSEKPRLLSSLDDAMSLFQITFEINPLDETVSQRCIIEAEPLEIIYDARTVNSIVEFFRPPKEVHLAQLTAATLTKLEEFRSKTATGLLYIIETQKVLDLKINLKASYIIVPQDGIFSPTSNLLLLDLGHLKVTSKSRSELPDVKQGEANLKEIMDRAYDSFDIQLTSVQLLYSRVGDNWREARKLSVSTQHILVPMHFNLELSKAMVFMDVRMPKFKIYGKLPLISLRISDKKLQGIMELIESIPKPEPVTEVSAPVKSFQIQTSTSLGTSQISQKIIPLLELPSVSEDDSEEEFFDAPCSPLEEPLQFPTGVKSIRTRKLQKQDCSVNMTTFKIRFEVPKVLIEFYHLVGDCELSVVEILVLGLGAEIEIRTYDLKANAFLKEFCLKCPEYLDENKKPVYLVTTLDNTMEDLLTLEYVKAEKNVPDLKSTYNNVLQLIKVNFSSLDIHLHTEALLNTINYLHNILPQSEEKSAPV,Intermembrane lipid transfer protein VPS13A,Mediates the transfer of lipids between membranes at organelle contact sites. Binds phospholipids. Required for the formation or stabilization of ER-mitochondria contact sites which enable transfer of lipids between the ER and mitochondria. Negatively regulates lipid droplet size and motility. Required for efficient lysosomal protein degradation.,,In a colorectal cancer sample; somatic mutation.
155,155,134365,P08692-C12S,MSNITIYHNPASGTSRNTLEMIRNSGTEPTIILYLENPPSRDELVKLIADMGISVRALLRKNVEPYEQLGLAEDKFTDDQLIDFMLQHPILINRPIVVTPLGTRLCRPSEVVLDILQDAQKGAFTKEDGEKVVDEAGKRLK,Loss of reductase activity. Mutant is sensitive to arsenate.,,MSNITIYHNPACGTSRNTLEMIRNSGTEPTIILYLENPPSRDELVKLIADMGISVRALLRKNVEPYEQLGLAEDKFTDDQLIDFMLQHPILINRPIVVTPLGTRLCRPSEVVLDILQDAQKGAFTKEDGEKVVDEAGKRLK,Arsenate reductase,Involved in resistance to arsenate. Catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)]. The resulting arsenite is then extruded from the cell via the ArsAB transport system (Probable).,The ArsCC12S protein was purified and found to be catalytically inactive.,Loss of reductase activity. Mutant is sensitive to arsenate. The ArsCC12S protein was purified and found to be catalytically inactive.
156,156,135439,O14746-V867M,MPRAPRCRAVRSLLRSHYREVLPLATFVRRLGPQGWRLVQRGDPAAFRALVAQCLVCVPWDARPPPAAPSFRQVSCLKELVARVLQRLCERGAKNVLAFGFALLDGARGGPPEAFTTSVRSYLPNTVTDALRGSGAWGLLLRRVGDDVLVHLLARCALFVLVAPSCAYQVCGPPLYQLGAATQARPPPHASGPRRRLGCERAWNHSVREAGVPLGLPAPGARRRGGSASRSLPLPKRPRRGAAPEPERTPVGQGSWAHPGRTRGPSDRGFCVVSPARPAEEATSLEGALSGTRHSHPSVGRQHHAGPPSTSRPPRPWDTPCPPVYAETKHFLYSSGDKEQLRPSFLLSSLRPSLTGARRLVETIFLGSRPWMPGTPRRLPRLPQRYWQMRPLFLELLGNHAQCPYGVLLKTHCPLRAAVTPAAGVCAREKPQGSVAAPEEEDTDPRRLVQLLRQHSSPWQVYGFVRACLRRLVPPGLWGSRHNERRFLRNTKKFISLGKHAKLSLQELTWKMSVRDCAWLRRSPGVGCVPAAEHRLREEILAKFLHWLMSVYVVELLRSFFYVTETTFQKNRLFFYRKSVWSKLQSIGIRQHLKRVQLRELSEAEVRQHREARPALLTSRLRFIPKPDGLRPIVNMDYVVGARTFRREKRAERLTSRVKALFSVLNYERARRPGLLGASVLGLDDIHRAWRTFVLRVRAQDPPPELYFVKVDVTGAYDTIPQDRLTEVIASIIKPQNTYCVRRYAVVQKAAHGHVRKAFKSHVSTLTDLQPYMRQFVAHLQETSPLRDAVVIEQSSSLNEASSGLFDVFLRFMCHHAVRIRGKSYVQCQGIPQGSILSTLLCSLCYGDMENKLFAGIRRDGLLLRLMDDFLLVTPHLTHAKTFLRTLVRGVPEYGCVVNLRKTVVNFPVEDEALGGTAFVQMPAHGLFPWCGLLLDTRTLEVQSDYSSYARTSIRASLTFNRGFKAGRNMRRKLFGVLRLKCHSLFLDLQVNSLQTVCTNIYKILLLQAYRFHACVLQLPFHQQ,"About 75% reduction in telomerase activity, about 50% reduction in repeat extension rate and 5.2-fold increase in nucleotide incorporation fidelity. Little further reduction in activity and 13.5-fold increase in nucleotide incorporation fidelity; when associated with Y-866.",,MPRAPRCRAVRSLLRSHYREVLPLATFVRRLGPQGWRLVQRGDPAAFRALVAQCLVCVPWDARPPPAAPSFRQVSCLKELVARVLQRLCERGAKNVLAFGFALLDGARGGPPEAFTTSVRSYLPNTVTDALRGSGAWGLLLRRVGDDVLVHLLARCALFVLVAPSCAYQVCGPPLYQLGAATQARPPPHASGPRRRLGCERAWNHSVREAGVPLGLPAPGARRRGGSASRSLPLPKRPRRGAAPEPERTPVGQGSWAHPGRTRGPSDRGFCVVSPARPAEEATSLEGALSGTRHSHPSVGRQHHAGPPSTSRPPRPWDTPCPPVYAETKHFLYSSGDKEQLRPSFLLSSLRPSLTGARRLVETIFLGSRPWMPGTPRRLPRLPQRYWQMRPLFLELLGNHAQCPYGVLLKTHCPLRAAVTPAAGVCAREKPQGSVAAPEEEDTDPRRLVQLLRQHSSPWQVYGFVRACLRRLVPPGLWGSRHNERRFLRNTKKFISLGKHAKLSLQELTWKMSVRDCAWLRRSPGVGCVPAAEHRLREEILAKFLHWLMSVYVVELLRSFFYVTETTFQKNRLFFYRKSVWSKLQSIGIRQHLKRVQLRELSEAEVRQHREARPALLTSRLRFIPKPDGLRPIVNMDYVVGARTFRREKRAERLTSRVKALFSVLNYERARRPGLLGASVLGLDDIHRAWRTFVLRVRAQDPPPELYFVKVDVTGAYDTIPQDRLTEVIASIIKPQNTYCVRRYAVVQKAAHGHVRKAFKSHVSTLTDLQPYMRQFVAHLQETSPLRDAVVIEQSSSLNEASSGLFDVFLRFMCHHAVRIRGKSYVQCQGIPQGSILSTLLCSLCYGDMENKLFAGIRRDGLLLRLVDDFLLVTPHLTHAKTFLRTLVRGVPEYGCVVNLRKTVVNFPVEDEALGGTAFVQMPAHGLFPWCGLLLDTRTLEVQSDYSSYARTSIRASLTFNRGFKAGRNMRRKLFGVLRLKCHSLFLDLQVNSLQTVCTNIYKILLLQAYRFHACVLQLPFHQQ,Telomerase reverse transcriptase,"Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. Active in progenitor and cancer cells. Inactive, or very low activity, in normal somatic cells. Catalytic component of the teleromerase holoenzyme complex whose main activity is the elongation of telomeres by acting as a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme. Catalyzes the RNA-dependent extension of 3'-chromosomal termini with the 6-nucleotide telomeric repeat unit, 5'-TTAGGG-3'. The catalytic cycle involves primer binding, primer extension and release of product once the template boundary has been reached or nascent product translocation followed by further extension. More active on substrates containing 2 or 3 telomeric repeats. Telomerase activity is regulated by a number of factors including telomerase complex-associated proteins, chaperones and polypeptide modifiers. Modulates Wnt signaling. Plays important roles in aging and antiapoptosis.",,"About 75% reduction in telomerase activity, about 50% reduction in repeat extension rate and 5.2-fold increase in nucleotide incorporation fidelity. Little further reduction in activity and 13.5-fold increase in nucleotide incorporation fidelity; when associated with Y-866."
157,157,136156,Q84W98-G93A,MATSNDQTNTKSSHSRTLLLLFIFLSLLLFSSLTIPMTRHQSTSMVAPFKRVLLESSVPASSTMDLRPKASTRRSRTSRRREFGNDAHEVPSAPNPISN,Compromised interaction with TDR.,,MATSNDQTNTKSSHSRTLLLLFIFLSLLLFSSLTIPMTRHQSTSMVAPFKRVLLESSVPASSTMDLRPKASTRRSRTSRRREFGNDAHEVPSGPNPISN,CLAVATA3/ESR,"Extracellular signal peptide that regulates cell fate. May act with TDR as a ligand-receptor pair in a signal transduction pathway that represses tracheary element differentiation but promotes the formation of procambial cells adjacent to phloem cells in the veins in an auxin-dependent manner. Regulates the transition of protophloem cells from proliferation to differentiation, thus impinging on postembryonic growth capacity of the root meristem; this signaling pathway requires CRN and CLV2.",The mutation in TDIF leads to [functional changes].,Compromised interaction with TDR. The mutation in TDIF leads to [functional changes].
158,158,138025,Q56223-C291A,MVRVKVNDRIVEVPPGTSVMDAVFHAGYDVPLFCSEKHLSPIGACRMCLVRIGLPKKGPDGKPLLNEKGEPEIQWQPKLAASCVTAVADGMVVDTLSDVVREAQAGMVEFTLLNHPLDCPTCDKGGACELQDRTVEYGLYEKYYQKGPLELPVYTRFEFTRRHVDKHHPLSPFVILDRERCIHCKRCVRYFEEVPGDEVLDFIERGVHTFIGTMDFGLPSGFSGNITDICPVGALLDLTARFRARNWEMEETPTTCALCPVGCGITADTRSGELLRIRAREVPEVNEIWIADAGRFGHEWADQNRLKTPLVRKEGRLVEATWEEAFLALKEGLKEARGEEVGLYLAHDATLEEGLLASELAKALKTPHLDFQGRTAAPASLFPPASLEDLLQADFALVLGDPTEEAPILHLRLSEFVRDLKPPHRYNHGTPFADLQIKERMPRRTDKMALFAPYRAPLMKWAAIHEVHRPGEEREILLALLGDKEGSEMVAKAKEAWEKAKNPVLILGAGVLQDTVAAERARLLAERKGAKVLAMTPAANARGLEAMGVLPGAKGASWDEPGALYAYYGFVPPEEALKGKRFVVMHLSHLHPLAERYAHVVLPAPTFYEKRGHLVNLEGRVLPLSPAPIENGEAEGALQVLALLAEALGVRPPFRLHLEAQKALKARKVPEAMGRLSFRLKELRPKERKGAFYLRPTMWKAHQAVGKAQEAARAELWAHPETARAEALPEGAQVAVETPFGRVEARVVHREDVPKGHLYLSALGPAAGLRVEGRVLVPAGGEA,Decreases amount and stability of iron-sulfur center 4.,,MVRVKVNDRIVEVPPGTSVMDAVFHAGYDVPLFCSEKHLSPIGACRMCLVRIGLPKKGPDGKPLLNEKGEPEIQWQPKLAASCVTAVADGMVVDTLSDVVREAQAGMVEFTLLNHPLDCPTCDKGGACELQDRTVEYGLYEKYYQKGPLELPVYTRFEFTRRHVDKHHPLSPFVILDRERCIHCKRCVRYFEEVPGDEVLDFIERGVHTFIGTMDFGLPSGFSGNITDICPVGALLDLTARFRARNWEMEETPTTCALCPVGCGITADTRSGELLRIRAREVPEVNEIWICDAGRFGHEWADQNRLKTPLVRKEGRLVEATWEEAFLALKEGLKEARGEEVGLYLAHDATLEEGLLASELAKALKTPHLDFQGRTAAPASLFPPASLEDLLQADFALVLGDPTEEAPILHLRLSEFVRDLKPPHRYNHGTPFADLQIKERMPRRTDKMALFAPYRAPLMKWAAIHEVHRPGEEREILLALLGDKEGSEMVAKAKEAWEKAKNPVLILGAGVLQDTVAAERARLLAERKGAKVLAMTPAANARGLEAMGVLPGAKGASWDEPGALYAYYGFVPPEEALKGKRFVVMHLSHLHPLAERYAHVVLPAPTFYEKRGHLVNLEGRVLPLSPAPIENGEAEGALQVLALLAEALGVRPPFRLHLEAQKALKARKVPEAMGRLSFRLKELRPKERKGAFYLRPTMWKAHQAVGKAQEAARAELWAHPETARAEALPEGAQVAVETPFGRVEARVVHREDVPKGHLYLSALGPAAGLRVEGRVLVPAGGEA,NADH-quinone oxidoreductase subunit 3,"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 menaquinone. 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 required for the synthesis of ATP.",The mutation in the Nqo3 subunit of NDH-1 leads to a change in the ligated iron-sulfur cluster.,Decreases amount and stability of iron-sulfur center 4. The mutation in the Nqo3 subunit of NDH-1 leads to a change in the ligated iron-sulfur cluster.
159,159,138146,P16522-L485F,MNDDSQDKIIHDIRIQLRKAATELSRWKLYGSSKWAAEALAGLAEAIDVDQTHSLADESPLRNKQGVPKQMFEIPQNGFGLSETEYDLYLLGSTLFDAKEFDRCVFFLKDVTNPYLKFLKLYSKFLSWDKKSQESMENILTTGKFTDEMYRANKDGDGSGNEDINQSGHQRANLKMVSNEHESQSNISSILKEINTFLESYEIKIDDDEADLGLALLYYLRGVILKQEKNISKAMSSFLKSLSCYSFNWSCWLELMDCLQKVDDALLLNNYLYQNFQFKFSENLGSQRTIEFNIMIKFFKLKVFEELNGQLEDYFEDLEFLLQVFPNFTFLKAYNATISYNNLDYVTAESRFDDIVKQDPYRLNDLETYSNILYVMQKNSKLAYLAQFVSQIDRFRPETCCIIANYYSARQEHEKSIMYFRRALTLDKKTTNAWTLMGHEFVELSNSHAAIECYRRAVDICPRDFKAWFGLGQAYALLDMHLYSFYYFQKACTLKPWDRRIWQVLGECYSKTGNKVEAIKCYKRSIKASQTVDQNTSIYYRLAQLYEELEDLQECKKFMMKCVDVEELLEGIVTDETVKARLWLAIFEIKAGNYQLAYDYAMGVSSGTSQEIEEARMLARECRRHM,In CDC23-56; G2/M cell cycle arrest at 37 degrees Celsius.,,MNDDSQDKIIHDIRIQLRKAATELSRWKLYGSSKWAAEALAGLAEAIDVDQTHSLADESPLRNKQGVPKQMFEIPQNGFGLSETEYDLYLLGSTLFDAKEFDRCVFFLKDVTNPYLKFLKLYSKFLSWDKKSQESMENILTTGKFTDEMYRANKDGDGSGNEDINQSGHQRANLKMVSNEHESQSNISSILKEINTFLESYEIKIDDDEADLGLALLYYLRGVILKQEKNISKAMSSFLKSLSCYSFNWSCWLELMDCLQKVDDALLLNNYLYQNFQFKFSENLGSQRTIEFNIMIKFFKLKVFEELNGQLEDYFEDLEFLLQVFPNFTFLKAYNATISYNNLDYVTAESRFDDIVKQDPYRLNDLETYSNILYVMQKNSKLAYLAQFVSQIDRFRPETCCIIANYYSARQEHEKSIMYFRRALTLDKKTTNAWTLMGHEFVELSNSHAAIECYRRAVDICPRDFKAWFGLGQAYALLDMHLYSLYYFQKACTLKPWDRRIWQVLGECYSKTGNKVEAIKCYKRSIKASQTVDQNTSIYYRLAQLYEELEDLQECKKFMMKCVDVEELLEGIVTDETVKARLWLAIFEIKAGNYQLAYDYAMGVSSGTSQEIEEARMLARECRRHM,Anaphase-promoting complex subunit CDC23,"Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. In early mitosis, the APC/C is activated by CDC20 and targets securin PDS1, the B-type cyclin CLB5, and other anaphase inhibitory proteins for proteolysis, thereby triggering the separation of sister chromatids at the metaphase-to-anaphase transition. In late mitosis and in G1, degradation of CLB5 allows activation of the APC/C by CDH1, which is needed to destroy CDC20 and the B-type cyclin CLB2 to allow exit from mitosis and creating the low CDK state necessary for cytokinesis and for reforming prereplicative complexes in G1 prior to another round of replication.",The mutation in the CDC23 gene causes a single amino acid change in the protein. This mutation is found within a mutable domain of CDC23 and may affect its function or stability.,In CDC23-56; G2/M cell cycle arrest at 37 degrees Celsius. The mutation in the CDC23 gene causes a single amino acid change in the protein. This mutation is found within a mutable domain of CDC23 and may affect its function or stability.
160,160,139103,P16522-G472D,MNDDSQDKIIHDIRIQLRKAATELSRWKLYGSSKWAAEALAGLAEAIDVDQTHSLADESPLRNKQGVPKQMFEIPQNGFGLSETEYDLYLLGSTLFDAKEFDRCVFFLKDVTNPYLKFLKLYSKFLSWDKKSQESMENILTTGKFTDEMYRANKDGDGSGNEDINQSGHQRANLKMVSNEHESQSNISSILKEINTFLESYEIKIDDDEADLGLALLYYLRGVILKQEKNISKAMSSFLKSLSCYSFNWSCWLELMDCLQKVDDALLLNNYLYQNFQFKFSENLGSQRTIEFNIMIKFFKLKVFEELNGQLEDYFEDLEFLLQVFPNFTFLKAYNATISYNNLDYVTAESRFDDIVKQDPYRLNDLETYSNILYVMQKNSKLAYLAQFVSQIDRFRPETCCIIANYYSARQEHEKSIMYFRRALTLDKKTTNAWTLMGHEFVELSNSHAAIECYRRAVDICPRDFKAWFGLDQAYALLDMHLYSLYYFQKACTLKPWDRRIWQVLGECYSKTGNKVEAIKCYKRSIKASQTVDQNTSIYYRLAQLYEELEDLQECKKFMMKCVDVEELLEGIVTDETVKARLWLAIFEIKAGNYQLAYDYAMGVSSGTSQEIEEARMLARECRRHM,In CDC23-1; G2/M cell cycle arrest at 36 degrees Celsius.,,MNDDSQDKIIHDIRIQLRKAATELSRWKLYGSSKWAAEALAGLAEAIDVDQTHSLADESPLRNKQGVPKQMFEIPQNGFGLSETEYDLYLLGSTLFDAKEFDRCVFFLKDVTNPYLKFLKLYSKFLSWDKKSQESMENILTTGKFTDEMYRANKDGDGSGNEDINQSGHQRANLKMVSNEHESQSNISSILKEINTFLESYEIKIDDDEADLGLALLYYLRGVILKQEKNISKAMSSFLKSLSCYSFNWSCWLELMDCLQKVDDALLLNNYLYQNFQFKFSENLGSQRTIEFNIMIKFFKLKVFEELNGQLEDYFEDLEFLLQVFPNFTFLKAYNATISYNNLDYVTAESRFDDIVKQDPYRLNDLETYSNILYVMQKNSKLAYLAQFVSQIDRFRPETCCIIANYYSARQEHEKSIMYFRRALTLDKKTTNAWTLMGHEFVELSNSHAAIECYRRAVDICPRDFKAWFGLGQAYALLDMHLYSLYYFQKACTLKPWDRRIWQVLGECYSKTGNKVEAIKCYKRSIKASQTVDQNTSIYYRLAQLYEELEDLQECKKFMMKCVDVEELLEGIVTDETVKARLWLAIFEIKAGNYQLAYDYAMGVSSGTSQEIEEARMLARECRRHM,Anaphase-promoting complex subunit CDC23,"Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. In early mitosis, the APC/C is activated by CDC20 and targets securin PDS1, the B-type cyclin CLB5, and other anaphase inhibitory proteins for proteolysis, thereby triggering the separation of sister chromatids at the metaphase-to-anaphase transition. In late mitosis and in G1, degradation of CLB5 allows activation of the APC/C by CDH1, which is needed to destroy CDC20 and the B-type cyclin CLB2 to allow exit from mitosis and creating the low CDK state necessary for cytokinesis and for reforming prereplicative complexes in G1 prior to another round of replication.",,In CDC23-1; G2/M cell cycle arrest at 36 degrees Celsius.
161,161,140635,Q07181-D191A,MVRNIVSRLCSQLFALPSSSLQERDPCSVTEYSGLATAVSSCKNIVLNGFQVPTGKQLDLSSLQNDSTVTFKGTTTFATTADNDFNPIVISGSNITITGASGHVIDGNGQAYWDGKGSNSNSNQKPDHFIVVQKTTGNSKITNLNIQNWPVHCFDITGSSQLTISGLILDNRAGDKPNAKSGSLPAAHNTAGFDISSSDHVTLDNNHVYNQDDCVAVTSGTNIVVSNMYCSGGHGLSIGSVGGKSDNVVDGVQFLSSQVVNSQNGCRIKSNSGATGTINNVTYQNIALTNISTYGVDVQQDYLNGGPTGKPTNGVKISNIKFIKVTGTVASSAQDWFILCGDGSCSGFTFSGNAITGGGKTSSCNYPTNTCPS,Loss of activity. No effect on Km for substrate.,,MVRNIVSRLCSQLFALPSSSLQERDPCSVTEYSGLATAVSSCKNIVLNGFQVPTGKQLDLSSLQNDSTVTFKGTTTFATTADNDFNPIVISGSNITITGASGHVIDGNGQAYWDGKGSNSNSNQKPDHFIVVQKTTGNSKITNLNIQNWPVHCFDITGSSQLTISGLILDNRAGDKPNAKSGSLPAAHNTDGFDISSSDHVTLDNNHVYNQDDCVAVTSGTNIVVSNMYCSGGHGLSIGSVGGKSDNVVDGVQFLSSQVVNSQNGCRIKSNSGATGTINNVTYQNIALTNISTYGVDVQQDYLNGGPTGKPTNGVKISNIKFIKVTGTVASSAQDWFILCGDGSCSGFTFSGNAITGGGKTSSCNYPTNTCPS,Polygalacturonase,"Involved in maceration and soft-rotting of plant tissue. Hydrolyzes the 1,4-alpha glycosidic bonds of de-esterified pectate in the smooth region of the plant cell wall.",,Loss of activity. No effect on Km for substrate.
162,162,141436,P76037-Y110X,MAINSPLNIAAQPGKTRLRKSLKLWQVVMMGLAYLTPMTVFDTFGIVSGISDGHVPASYLLALAGVLFTAISYGKLVRQFPEAGSAYTYAQKSINPHVGFMVGWSSLLDXLFLPMINVLLAKIYLSALFPEVPPWVWVVTFVAILTAANLKSVNLVANFNTLFVLVQISIMVVFIFLVVQGLHKGEGVGTVWSLQPFISENAHLIPIITGATIVCFSFLGFDAVTTLSEETPDAARVIPKAIFLTAVYGGVIFIAASFFMQLFFPDISRFKDPDAALPEIALYVGGKLFQSIFLCTTFVNTLASGLASHASVSRLLYVMGRDNVFPERVFGYVHPKWRTPALNVIMVGIVALSALFFDLVTATALINFGALVAFTFVNLSVFNHFWRRKGMNKSWKDHFHYLLMPLVGALTVGVLWVNLESTSLTLGLVWASLGGAYLWYLIRRYRKVPLYDGDRTPVSET,The uptake activity is reduced to one-eighth of that of wild-type.,,MAINSPLNIAAQPGKTRLRKSLKLWQVVMMGLAYLTPMTVFDTFGIVSGISDGHVPASYLLALAGVLFTAISYGKLVRQFPEAGSAYTYAQKSINPHVGFMVGWSSLLDYLFLPMINVLLAKIYLSALFPEVPPWVWVVTFVAILTAANLKSVNLVANFNTLFVLVQISIMVVFIFLVVQGLHKGEGVGTVWSLQPFISENAHLIPIITGATIVCFSFLGFDAVTTLSEETPDAARVIPKAIFLTAVYGGVIFIAASFFMQLFFPDISRFKDPDAALPEIALYVGGKLFQSIFLCTTFVNTLASGLASHASVSRLLYVMGRDNVFPERVFGYVHPKWRTPALNVIMVGIVALSALFFDLVTATALINFGALVAFTFVNLSVFNHFWRRKGMNKSWKDHFHYLLMPLVGALTVGVLWVNLESTSLTLGLVWASLGGAYLWYLIRRYRKVPLYDGDRTPVSET,Putrescine importer PuuP,Involved in the uptake of putrescine. Imports putrescine for its utilization as an energy source in the absence of glucose.,,The uptake activity is reduced to one-eighth of that of wild-type.
163,163,143104,Q9ULZ3-D48A,MGRARDAILDALENLTAEELKKFKLKLLSVPLREGYGRIPRGALLSMAALDLTDKLVSFYLETYGAELTANVLRDMGLQEMAGQLQAATHQGSGAAPAGIQAPPQSAAKPGLHFIDQHRAALIARVTNVEWLLDALYGKVLTDEQYQAVRAEPTNPSKMRKLFSFTPAWNWTCKDLLLQALRESQSYLVEDLERS,Abolishes interaction with PYDC1.,,MGRARDAILDALENLTAEELKKFKLKLLSVPLREGYGRIPRGALLSMDALDLTDKLVSFYLETYGAELTANVLRDMGLQEMAGQLQAATHQGSGAAPAGIQAPPQSAAKPGLHFIDQHRAALIARVTNVEWLLDALYGKVLTDEQYQAVRAEPTNPSKMRKLFSFTPAWNWTCKDLLLQALRESQSYLVEDLERS,Apoptosis-associated speck-like protein containing a CARD,"Functions as key mediator in apoptosis and inflammation. Promotes caspase-mediated apoptosis involving predominantly caspase-8 and also caspase-9 in a probable cell type-specific manner. Involved in activation of the mitochondrial apoptotic pathway, promotes caspase-8-dependent proteolytic maturation of BID independently of FADD in certain cell types and also mediates mitochondrial translocation of BAX and activates BAX-dependent apoptosis coupled to activation of caspase-9, -2 and -3. Involved in innate immune response by acting as an integral adapter in the assembly of various inflammasomes (NLRP1, NLRP2, NLRP3, NLRP6, AIM2 and probably IFI16) which recruit and activate caspase-1 leading to processing and secretion of pro-inflammatory cytokines. Caspase-1-dependent inflammation leads to macrophage pyroptosis, a form of cell death. The function as activating adapter in different types of inflammasomes is mediated by the pyrin and CARD domains and their homotypic interactions. Clustered PYCARD nucleates the formation of caspase-1 filaments through the interaction of their respective CARD domains, acting as a platform for of caspase-1 polymerization. In the NLRP1 and NLRC4 inflammasomes seems not be required but facilitates the processing of procaspase-1. In cooperation with NOD2 involved in an inflammasome activated by bacterial muramyl dipeptide leading to caspase-1 activation. May be involved in RIGI-triggered pro-inflammatory responses and inflammasome activation. In collaboration with AIM2 which detects cytosolic double-stranded DNA may also be involved in a caspase-1-independent cell death that involves caspase-8. In adaptive immunity may be involved in maturation of dendritic cells to stimulate T-cell immunity and in cytoskeletal rearrangements coupled to chemotaxis and antigen uptake may be involved in post-transcriptional regulation of the guanine nucleotide exchange factor DOCK2; the latter function is proposed to involve the nuclear form. Also involved in transcriptional activation of cytokines and chemokines independent of the inflammasome; this function may involve AP-1, NF-kappa-B, MAPK and caspase-8 signaling pathways. For regulation of NF-kappa-B activating and inhibiting functions have been reported. Modulates NF-kappa-B induction at the level of the IKK complex by inhibiting kinase activity of CHUK and IKBK. Proposed to compete with RIPK2 for association with CASP1 thereby down-regulating CASP1-mediated RIPK2-dependent NF-kappa-B activation and activating interleukin-1 beta processing. Modulates host resistance to DNA virus infection, probably by inducing the cleavage of and inactivating CGAS in presence of cytoplasmic double-stranded DNA.May have a regulating effect on the function as inflammasome adapter.Seems to inhibit inflammasome-mediated maturation of interleukin-1 beta.",Mutation of D48 to A in ASC protein leads to loss of filament formation. The mutation in ASC_PYD affects its interaction with POP1.,Abolishes interaction with PYDC1. Mutation of D48 to A in ASC protein leads to loss of filament formation. The mutation in ASC_PYD affects its interaction with POP1.
164,164,143381,Q6MZP7-C525Y,MEVVPAEVNSLLPEEIMDTGITLVDDDSIEAVIVSSPIPMETELEEIVNINSTGDSTATPISTEPITVYSNHTNQVAVNTTITKADSNTTVKPAFPSGLQKLGAQTPVTISANQIILNKVSQTSDLKLGNQTLKPDGQKLILTTLGKSGSPIVLALPHSQLPQAQKVTTQAQSGDAKLPPQQIKVVTIGGRPEVKPVIGVSALTPGSQLINTTTQPSVLQTQQLKTVQIAKKPRTPTSGPVITKLIFAKPINSKAVTGQTTQVSPPVIAGRVLSQSTPGTPSKTITISESGVIGSTLNSTTQTPNKIAISPLKSPNKAVKSTVQTITVGGVSTSQFKTIIPLATAPNVQQIQVPGSKFHYVRLVTATSASSSTQPVSQNPSTNTQPLQQAKPVVVNTTPVRMSVPIVSAQAVKQVVPKPINPTSQIVTTSQPQQRLIMPATPLPQIQPNLTNLPPGTVLAPAPGTGNVGYAVLPAQYVTQLQQSSYVSIASNSTFTGTSGIQTQARLPFNGIIPSESASRPRKPYNCTKSLCLKLYCDCFANGEFCNNCNCTNCYNNLEHENERQKAIKACLDRNPEAFKPKIGKGKEGESDRRHSKGCNCKRSGCLKNYCECYEAKIMCSSICKCIGCKNFEESPERKTLMHLADAAEVRVQQQTAAKTKLSSQISDLLTRPTPALNSGGGKLPFTFVTKEVAEATCNCLLAQAEQADKKGKSKAAAERMILEEFGRCLMSVINSAGKAKSDPCAMNC,Abolishes DNA-binding to the CDK1 promoter; when associated with Y-527.,,MEVVPAEVNSLLPEEIMDTGITLVDDDSIEAVIVSSPIPMETELEEIVNINSTGDSTATPISTEPITVYSNHTNQVAVNTTITKADSNTTVKPAFPSGLQKLGAQTPVTISANQIILNKVSQTSDLKLGNQTLKPDGQKLILTTLGKSGSPIVLALPHSQLPQAQKVTTQAQSGDAKLPPQQIKVVTIGGRPEVKPVIGVSALTPGSQLINTTTQPSVLQTQQLKTVQIAKKPRTPTSGPVITKLIFAKPINSKAVTGQTTQVSPPVIAGRVLSQSTPGTPSKTITISESGVIGSTLNSTTQTPNKIAISPLKSPNKAVKSTVQTITVGGVSTSQFKTIIPLATAPNVQQIQVPGSKFHYVRLVTATSASSSTQPVSQNPSTNTQPLQQAKPVVVNTTPVRMSVPIVSAQAVKQVVPKPINPTSQIVTTSQPQQRLIMPATPLPQIQPNLTNLPPGTVLAPAPGTGNVGYAVLPAQYVTQLQQSSYVSIASNSTFTGTSGIQTQARLPFNGIIPSESASRPRKPCNCTKSLCLKLYCDCFANGEFCNNCNCTNCYNNLEHENERQKAIKACLDRNPEAFKPKIGKGKEGESDRRHSKGCNCKRSGCLKNYCECYEAKIMCSSICKCIGCKNFEESPERKTLMHLADAAEVRVQQQTAAKTKLSSQISDLLTRPTPALNSGGGKLPFTFVTKEVAEATCNCLLAQAEQADKKGKSKAAAERMILEEFGRCLMSVINSAGKAKSDPCAMNC,Protein lin-54 homolog,"Component of the DREAM complex, a multiprotein complex that can both act as a transcription activator or repressor depending on the context. In G0 phase, the complex binds to more than 800 promoters and is required for repression of E2F target genes. In S phase, the complex selectively binds to the promoters of G2/M genes whose products are required for mitosis and participates in their cell cycle dependent activation. In the complex, acts as a DNA-binding protein that binds the promoter of CDK1 in a sequence-specific manner. Specifically recognizes the consensus motif 5'-TTYRAA-3' in target DNA.",,Abolishes DNA-binding to the CDK1 promoter; when associated with Y-527.
165,165,144066,Q06136-Y186F,MLLLAAAFLVAFVLLLYMVSPLISPKPLALPGAHVVVTGGSSGIGKCIAIECYKQGAFITLVARNEDKLLQAKKEIEMHSINDKQVVLCISVDVSQDYNQVENVIKQAQEKLGPVDMLVNCAGMAVSGKFEDLEVSTFERLMSINYLGSVYPSRAVITTMKERRVGRIVFVSSQAGQLGLFGFTAFSASKFAIRGLAEALQMEVKPYNVYITVAYPPDTDTPGFAEENRTKPLETRLISETTSVCKPEQVAKQIVKDAIQGNFNSSLGSDGYMLSALTCGMAPVTSITEGLQQVVTMGLFRTIALFYLGSFDSIVRRCMMQREKSENADKTA,In EKVP4.,,MLLLAAAFLVAFVLLLYMVSPLISPKPLALPGAHVVVTGGSSGIGKCIAIECYKQGAFITLVARNEDKLLQAKKEIEMHSINDKQVVLCISVDVSQDYNQVENVIKQAQEKLGPVDMLVNCAGMAVSGKFEDLEVSTFERLMSINYLGSVYPSRAVITTMKERRVGRIVFVSSQAGQLGLFGFTAYSASKFAIRGLAEALQMEVKPYNVYITVAYPPDTDTPGFAEENRTKPLETRLISETTSVCKPEQVAKQIVKDAIQGNFNSSLGSDGYMLSALTCGMAPVTSITEGLQQVVTMGLFRTIALFYLGSFDSIVRRCMMQREKSENADKTA,3-ketodihydrosphingosine reductase,Catalyzes the reduction of 3-ketodihydrosphingosine (KDS) to dihydrosphingosine (DHS).,The mutation in the KDSR gene causes defects in KDSR function.,In EKVP4. The mutation in the KDSR gene causes defects in KDSR function.
166,166,144223,O14746-T726M,MPRAPRCRAVRSLLRSHYREVLPLATFVRRLGPQGWRLVQRGDPAAFRALVAQCLVCVPWDARPPPAAPSFRQVSCLKELVARVLQRLCERGAKNVLAFGFALLDGARGGPPEAFTTSVRSYLPNTVTDALRGSGAWGLLLRRVGDDVLVHLLARCALFVLVAPSCAYQVCGPPLYQLGAATQARPPPHASGPRRRLGCERAWNHSVREAGVPLGLPAPGARRRGGSASRSLPLPKRPRRGAAPEPERTPVGQGSWAHPGRTRGPSDRGFCVVSPARPAEEATSLEGALSGTRHSHPSVGRQHHAGPPSTSRPPRPWDTPCPPVYAETKHFLYSSGDKEQLRPSFLLSSLRPSLTGARRLVETIFLGSRPWMPGTPRRLPRLPQRYWQMRPLFLELLGNHAQCPYGVLLKTHCPLRAAVTPAAGVCAREKPQGSVAAPEEEDTDPRRLVQLLRQHSSPWQVYGFVRACLRRLVPPGLWGSRHNERRFLRNTKKFISLGKHAKLSLQELTWKMSVRDCAWLRRSPGVGCVPAAEHRLREEILAKFLHWLMSVYVVELLRSFFYVTETTFQKNRLFFYRKSVWSKLQSIGIRQHLKRVQLRELSEAEVRQHREARPALLTSRLRFIPKPDGLRPIVNMDYVVGARTFRREKRAERLTSRVKALFSVLNYERARRPGLLGASVLGLDDIHRAWRTFVLRVRAQDPPPELYFVKVDVTGAYDTIPQDRLMEVIASIIKPQNTYCVRRYAVVQKAAHGHVRKAFKSHVSTLTDLQPYMRQFVAHLQETSPLRDAVVIEQSSSLNEASSGLFDVFLRFMCHHAVRIRGKSYVQCQGIPQGSILSTLLCSLCYGDMENKLFAGIRRDGLLLRLVDDFLLVTPHLTHAKTFLRTLVRGVPEYGCVVNLRKTVVNFPVEDEALGGTAFVQMPAHGLFPWCGLLLDTRTLEVQSDYSSYARTSIRASLTFNRGFKAGRNMRRKLFGVLRLKCHSLFLDLQVNSLQTVCTNIYKILLLQAYRFHACVLQLPFHQQ,In AA; very severe; no effect on telomerase catalytic activity but shortened telomeres.,,MPRAPRCRAVRSLLRSHYREVLPLATFVRRLGPQGWRLVQRGDPAAFRALVAQCLVCVPWDARPPPAAPSFRQVSCLKELVARVLQRLCERGAKNVLAFGFALLDGARGGPPEAFTTSVRSYLPNTVTDALRGSGAWGLLLRRVGDDVLVHLLARCALFVLVAPSCAYQVCGPPLYQLGAATQARPPPHASGPRRRLGCERAWNHSVREAGVPLGLPAPGARRRGGSASRSLPLPKRPRRGAAPEPERTPVGQGSWAHPGRTRGPSDRGFCVVSPARPAEEATSLEGALSGTRHSHPSVGRQHHAGPPSTSRPPRPWDTPCPPVYAETKHFLYSSGDKEQLRPSFLLSSLRPSLTGARRLVETIFLGSRPWMPGTPRRLPRLPQRYWQMRPLFLELLGNHAQCPYGVLLKTHCPLRAAVTPAAGVCAREKPQGSVAAPEEEDTDPRRLVQLLRQHSSPWQVYGFVRACLRRLVPPGLWGSRHNERRFLRNTKKFISLGKHAKLSLQELTWKMSVRDCAWLRRSPGVGCVPAAEHRLREEILAKFLHWLMSVYVVELLRSFFYVTETTFQKNRLFFYRKSVWSKLQSIGIRQHLKRVQLRELSEAEVRQHREARPALLTSRLRFIPKPDGLRPIVNMDYVVGARTFRREKRAERLTSRVKALFSVLNYERARRPGLLGASVLGLDDIHRAWRTFVLRVRAQDPPPELYFVKVDVTGAYDTIPQDRLTEVIASIIKPQNTYCVRRYAVVQKAAHGHVRKAFKSHVSTLTDLQPYMRQFVAHLQETSPLRDAVVIEQSSSLNEASSGLFDVFLRFMCHHAVRIRGKSYVQCQGIPQGSILSTLLCSLCYGDMENKLFAGIRRDGLLLRLVDDFLLVTPHLTHAKTFLRTLVRGVPEYGCVVNLRKTVVNFPVEDEALGGTAFVQMPAHGLFPWCGLLLDTRTLEVQSDYSSYARTSIRASLTFNRGFKAGRNMRRKLFGVLRLKCHSLFLDLQVNSLQTVCTNIYKILLLQAYRFHACVLQLPFHQQ,Telomerase reverse transcriptase,"Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. Active in progenitor and cancer cells. Inactive, or very low activity, in normal somatic cells. Catalytic component of the teleromerase holoenzyme complex whose main activity is the elongation of telomeres by acting as a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme. Catalyzes the RNA-dependent extension of 3'-chromosomal termini with the 6-nucleotide telomeric repeat unit, 5'-TTAGGG-3'. The catalytic cycle involves primer binding, primer extension and release of product once the template boundary has been reached or nascent product translocation followed by further extension. More active on substrates containing 2 or 3 telomeric repeats. Telomerase activity is regulated by a number of factors including telomerase complex-associated proteins, chaperones and polypeptide modifiers. Modulates Wnt signaling. Plays important roles in aging and antiapoptosis.","Novel heterozygous, non-synonymous mutation in TERT () was found in two patients with acquired aplastic anemia (AA). The mutation in the hTERT protein has been identified in patients with dyskeratosis congenita or aplastic anemia. This mutation leads to a compromised telomerase function by haploinsufficiency.","In AA; very severe; no effect on telomerase catalytic activity but shortened telomeres. Novel heterozygous, non-synonymous mutation in TERT () was found in two patients with acquired aplastic anemia (AA). The mutation in the hTERT protein has been identified in patients with dyskeratosis congenita or aplastic anemia. This mutation leads to a compromised telomerase function by haploinsufficiency."
167,167,145045,P9WH43-F310G,MPSPTVTSPQVAVNDIGSSEDFLAAIDKTIKYFNDGDIVEGTIVKVDRDEVLLDIGYKTEGVIPARELSIKHDVDPNEVVSVGDEVEALVLTKEDKEGRLILSKKRAQYERAWGTIEALKEKDEAVKGTVIEVVKGGLILDIGLRGFLPASLVEMRRVRDLQPYIGKEIEAKIIELDKNRNNVVLSRRAWLEQTQSEVRSEFLNNLQKGTIRKGVVSSIVNFGAFVDLGGVDGLVHVSELSWKHIDHPSEVVQVGDEVTVEVLDVDMDRERVSLSLKATQEDPWRHFARTHAIGQIVPGKVTKLVPFGAGVRVEEGIEGLVHISELAERHVEVPDQVVAVGDDAMVKVIDIDLERRRISLSLKQANEDYTEEFDPAKYGMADSYDEQGNYIFPEGFDAETNEWLEGFEKQRAEWEARYAEAERRHKMHTAQMEKFAAAEAAGRGADDQSSASSAPSEKTAGGSLASDAQLAALREKLAGSA,"3-fold decrease in binding of POA, decreased binding of tmRNA (expressed as residues 285-481).",,MPSPTVTSPQVAVNDIGSSEDFLAAIDKTIKYFNDGDIVEGTIVKVDRDEVLLDIGYKTEGVIPARELSIKHDVDPNEVVSVGDEVEALVLTKEDKEGRLILSKKRAQYERAWGTIEALKEKDEAVKGTVIEVVKGGLILDIGLRGFLPASLVEMRRVRDLQPYIGKEIEAKIIELDKNRNNVVLSRRAWLEQTQSEVRSEFLNNLQKGTIRKGVVSSIVNFGAFVDLGGVDGLVHVSELSWKHIDHPSEVVQVGDEVTVEVLDVDMDRERVSLSLKATQEDPWRHFARTHAIGQIVPGKVTKLVPFGAFVRVEEGIEGLVHISELAERHVEVPDQVVAVGDDAMVKVIDIDLERRRISLSLKQANEDYTEEFDPAKYGMADSYDEQGNYIFPEGFDAETNEWLEGFEKQRAEWEARYAEAERRHKMHTAQMEKFAAAEAAGRGADDQSSASSAPSEKTAGGSLASDAQLAALREKLAGSA,Small ribosomal subunit protein bS1,"Binds mRNA, facilitating recognition of most mRNAs by the 30S ribosomal subunit during translation initiation (By similarity). Probably plays a role in trans-translation; binds tmRNA (the product of the ssrA gene). In trans-translation Ala-aminoacylated transfer-messenger RNA (tmRNA, product of the ssrA gene; the 2 termini fold to resemble tRNA(Ala) while it encodes a short internal open reading frame (the tag peptide)) acts like a tRNA, entering the A-site of the ribosome and displacing the stalled mRNA (which is subsequently degraded). The ribosome then switches to translate the ORF on the tmRNA, the nascent peptide is terminated with the 'tag peptide' encoded by the tmRNA and thus targeted for degradation (By similarity).",Conformational changes induced by mutation at F310 abolish the POA binding activity.,"3-fold decrease in binding of POA, decreased binding of tmRNA (expressed as residues 285-481). Conformational changes induced by mutation at F310 abolish the POA binding activity."
168,168,145636,Q96NZ9-K69R,MRRLLLVTSLVVVLLWEAGAVPAPKVPIKMQVKHWPSEQDPEKAWGARVVEPPEKDDQLVVLFPVQKPRLLTTEEKPRGQGRGPILPGTKAWMETEDTLGHVLSPEPDHDSLYHPPPEEDQGEERPRLWVMPNHQVLLGPEEDQDHIYHPQ,,,MRRLLLVTSLVVVLLWEAGAVPAPKVPIKMQVKHWPSEQDPEKAWGARVVEPPEKDDQLVVLFPVQKPKLLTTEEKPRGQGRGPILPGTKAWMETEDTLGHVLSPEPDHDSLYHPPPEEDQGEERPRLWVMPNHQVLLGPEEDQDHIYHPQ,Proline-rich acidic protein 1,Lipid-binding protein which promotes lipid absorption by facilitating MTTP-mediated lipid transfer (mainly triglycerides and phospholipids) and MTTP-mediated apoB lipoprotein assembly and secretion. Protects the gastrointestinal epithelium from irradiation-induced apoptosis. May play an important role in maintaining normal growth homeostasis in epithelial cells. Involved in p53/TP53-dependent cell survival after DNA damage. May down-regulate the expression of MAD1L1 and exert a suppressive role in mitotic spindle assembly checkpoint in hepatocellular carcinomas.,The functional changes caused by the mutation are not mentioned in the document.,The functional changes caused by the mutation are not mentioned in the document.
169,169,146025,P08692-E127D,MSNITIYHNPACGTSRNTLEMIRNSGTEPTIILYLENPPSRDELVKLIADMGISVRALLRKNVEPYEQLGLAEDKFTDDQLIDFMLQHPILINRPIVVTPLGTRLCRPSEVVLDILQDAQKGAFTKDDGEKVVDEAGKRLK,13-fold decrease in catalytic efficiency with arsenate. Mutant is sensitive at high arsenate concentrations.,,MSNITIYHNPACGTSRNTLEMIRNSGTEPTIILYLENPPSRDELVKLIADMGISVRALLRKNVEPYEQLGLAEDKFTDDQLIDFMLQHPILINRPIVVTPLGTRLCRPSEVVLDILQDAQKGAFTKEDGEKVVDEAGKRLK,Arsenate reductase,Involved in resistance to arsenate. Catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)]. The resulting arsenite is then extruded from the cell via the ArsAB transport system (Probable).,The functional changes caused by the mutation are not mentioned in the document.,13-fold decrease in catalytic efficiency with arsenate. Mutant is sensitive at high arsenate concentrations. The functional changes caused by the mutation are not mentioned in the document.
170,170,147284,P32266-R824A,MNASPVRLLILRRQLATHPAILYSSPYIKSPLVHLHSRMSNVHRSAHANALSFVITRRSISHFPKIISKIIRLPIYVGGGMAAAGSYIAYKMEEASSFTKDKLDRIKDLGESMKEKFNKMFSGDKSQDGGHGNDGTVPTATLIAATSLDDDESKRQGDPKDDDDEDDDDEDDENDSVDTTQDEMLNLTKQMIEIRTILNKVDSSSAHLTLPSIVVIGSQSSGKSSVLESIVGREFLPKGSNMVTRRPIELTLVNTPNSNNVTADFPSMRLYNIKDFKEVKRMLMELNMAVPTSEAVSEEPIQLTIKSSRVPDLSLVDLPGYIQVEAADQPIELKTKIRDLCEKYLTAPNIILAISAADVDLANSSALKASKAADPKGLRTIGVITKLDLVDPEKARSILNNKKYPLSMGYVGVITKTPSSINRKHLGLFGEAPSSSLSGIFSKGQHGQSSGEENTNGLKQIVSHQFEKAYFKENKKYFTNCQVSTKKLREKLIKILEISMSNALEPTSTLIQQELDDTSYLFKVEFNDRHLTPKSYLLNNIDVLKLGIKEFQEKFHRNELKSILRAELDQKVLDVLATRYWKDDNLQDLSSSKLESDTDMLYWHKKLELASSGLTKMGIGRLSTMLTTNAILKELDNILESTQLKNHELIKDLVSNTAINVLNSKYYSTADQVENCIKPFKYEIDLEERDWSLARQHSINLIKEELRQCNSRYQAIKNAVGSKKLANVMGYLENESNLQKETLGMSKLLLERGSEAIFLDKRCKVLSFRLKMLKNKCHSTIEKDRCPEVFLSAVSDKLTSTAVLFLNVELLSDFFYNFPIELDARLTLLGDEQVEMFAKEDPKISRHIELQKRKELLELALEKIDSILVFKKSYKGVSKNL,Loss of GED function.,,MNASPVRLLILRRQLATHPAILYSSPYIKSPLVHLHSRMSNVHRSAHANALSFVITRRSISHFPKIISKIIRLPIYVGGGMAAAGSYIAYKMEEASSFTKDKLDRIKDLGESMKEKFNKMFSGDKSQDGGHGNDGTVPTATLIAATSLDDDESKRQGDPKDDDDEDDDDEDDENDSVDTTQDEMLNLTKQMIEIRTILNKVDSSSAHLTLPSIVVIGSQSSGKSSVLESIVGREFLPKGSNMVTRRPIELTLVNTPNSNNVTADFPSMRLYNIKDFKEVKRMLMELNMAVPTSEAVSEEPIQLTIKSSRVPDLSLVDLPGYIQVEAADQPIELKTKIRDLCEKYLTAPNIILAISAADVDLANSSALKASKAADPKGLRTIGVITKLDLVDPEKARSILNNKKYPLSMGYVGVITKTPSSINRKHLGLFGEAPSSSLSGIFSKGQHGQSSGEENTNGLKQIVSHQFEKAYFKENKKYFTNCQVSTKKLREKLIKILEISMSNALEPTSTLIQQELDDTSYLFKVEFNDRHLTPKSYLLNNIDVLKLGIKEFQEKFHRNELKSILRAELDQKVLDVLATRYWKDDNLQDLSSSKLESDTDMLYWHKKLELASSGLTKMGIGRLSTMLTTNAILKELDNILESTQLKNHELIKDLVSNTAINVLNSKYYSTADQVENCIKPFKYEIDLEERDWSLARQHSINLIKEELRQCNSRYQAIKNAVGSKKLANVMGYLENESNLQKETLGMSKLLLERGSEAIFLDKRCKVLSFRLKMLKNKCHSTIEKDRCPEVFLSAVSDKLTSTAVLFLNVELLSDFFYNFPIELDRRLTLLGDEQVEMFAKEDPKISRHIELQKRKELLELALEKIDSILVFKKSYKGVSKNL,"Dynamin-like GTPase MGM1, mitochondrial",Dynamin-related GTPase required for mitochondrial fusion. Coordinates interaction between the inner and outer mitochondrial membrane to promote the formation of the double membrane.,,Loss of GED function.
171,171,147599,P9WGT3-T191A,MTATATEGAKPPFVSRSVLVTGGNRGIGLAIAQRLAADGHKVAVTHRGSGAPKGLFGVECDVTDSDAVDRAFTAVEEHQGPVEVLVSNAGLSADAFLMRMTEEKFEKVINANLTGAFRVAQRASRSMQRNKFGRMIFIGSVSGSWGIGNQANYAASKAGVIGMARSIARELSKANVTANVVAPGYIDTDMARALDERIQQGALQFIPAKRVGTPAEVAGVVSFLASEDASYISGAVIPVDGGMGMGH,Retains 22% of wild-type reductase activity. Strong decrease in phosphorylation by PknB. Lack of phosphorylation by PknB; when associated with A-21 and A-114.,,MTATATEGAKPPFVSRSVLVTGGNRGIGLAIAQRLAADGHKVAVTHRGSGAPKGLFGVECDVTDSDAVDRAFTAVEEHQGPVEVLVSNAGLSADAFLMRMTEEKFEKVINANLTGAFRVAQRASRSMQRNKFGRMIFIGSVSGSWGIGNQANYAASKAGVIGMARSIARELSKANVTANVVAPGYIDTDMTRALDERIQQGALQFIPAKRVGTPAEVAGVVSFLASEDASYISGAVIPVDGGMGMGH,3-oxoacyl-[acyl-carrier-protein] reductase MabA,"Part of the mycobacterial fatty acid elongation system FAS-II, which is involved in mycolic acid biosynthesis. Catalyzes the NADPH-dependent reduction of beta-ketoacyl derivatives, the second step of the FAS-II elongation cycle. May preferentially metabolize long-chain substrates (C8-C20). Can use CoA derivatives as substrates in vitro.","The MabA_T191A mutant, designed to mimic the mutation, exhibited markedly decreased ketoacyl reductase activity compared with the wild-type protein, as well as impaired binding of the NADPH cofactor.","Retains 22% of wild-type reductase activity. Strong decrease in phosphorylation by PknB. Lack of phosphorylation by PknB; when associated with A-21 and A-114. The MabA_T191A mutant, designed to mimic the mutation, exhibited markedly decreased ketoacyl reductase activity compared with the wild-type protein, as well as impaired binding of the NADPH cofactor."
172,172,148449,Q9ULZ3-E13W,MGRARDAILDALWNLTAEELKKFKLKLLSVPLREGYGRIPRGALLSMDALDLTDKLVSFYLETYGAELTANVLRDMGLQEMAGQLQAATHQGSGAAPAGIQAPPQSAAKPGLHFIDQHRAALIARVTNVEWLLDALYGKVLTDEQYQAVRAEPTNPSKMRKLFSFTPAWNWTCKDLLLQALRESQSYLVEDLERS,Abolishes interaction with NLRP2.,,MGRARDAILDALENLTAEELKKFKLKLLSVPLREGYGRIPRGALLSMDALDLTDKLVSFYLETYGAELTANVLRDMGLQEMAGQLQAATHQGSGAAPAGIQAPPQSAAKPGLHFIDQHRAALIARVTNVEWLLDALYGKVLTDEQYQAVRAEPTNPSKMRKLFSFTPAWNWTCKDLLLQALRESQSYLVEDLERS,Apoptosis-associated speck-like protein containing a CARD,"Functions as key mediator in apoptosis and inflammation. Promotes caspase-mediated apoptosis involving predominantly caspase-8 and also caspase-9 in a probable cell type-specific manner. Involved in activation of the mitochondrial apoptotic pathway, promotes caspase-8-dependent proteolytic maturation of BID independently of FADD in certain cell types and also mediates mitochondrial translocation of BAX and activates BAX-dependent apoptosis coupled to activation of caspase-9, -2 and -3. Involved in innate immune response by acting as an integral adapter in the assembly of various inflammasomes (NLRP1, NLRP2, NLRP3, NLRP6, AIM2 and probably IFI16) which recruit and activate caspase-1 leading to processing and secretion of pro-inflammatory cytokines. Caspase-1-dependent inflammation leads to macrophage pyroptosis, a form of cell death. The function as activating adapter in different types of inflammasomes is mediated by the pyrin and CARD domains and their homotypic interactions. Clustered PYCARD nucleates the formation of caspase-1 filaments through the interaction of their respective CARD domains, acting as a platform for of caspase-1 polymerization. In the NLRP1 and NLRC4 inflammasomes seems not be required but facilitates the processing of procaspase-1. In cooperation with NOD2 involved in an inflammasome activated by bacterial muramyl dipeptide leading to caspase-1 activation. May be involved in RIGI-triggered pro-inflammatory responses and inflammasome activation. In collaboration with AIM2 which detects cytosolic double-stranded DNA may also be involved in a caspase-1-independent cell death that involves caspase-8. In adaptive immunity may be involved in maturation of dendritic cells to stimulate T-cell immunity and in cytoskeletal rearrangements coupled to chemotaxis and antigen uptake may be involved in post-transcriptional regulation of the guanine nucleotide exchange factor DOCK2; the latter function is proposed to involve the nuclear form. Also involved in transcriptional activation of cytokines and chemokines independent of the inflammasome; this function may involve AP-1, NF-kappa-B, MAPK and caspase-8 signaling pathways. For regulation of NF-kappa-B activating and inhibiting functions have been reported. Modulates NF-kappa-B induction at the level of the IKK complex by inhibiting kinase activity of CHUK and IKBK. Proposed to compete with RIPK2 for association with CASP1 thereby down-regulating CASP1-mediated RIPK2-dependent NF-kappa-B activation and activating interleukin-1 beta processing. Modulates host resistance to DNA virus infection, probably by inducing the cleavage of and inactivating CGAS in presence of cytoplasmic double-stranded DNA.May have a regulating effect on the function as inflammasome adapter.Seems to inhibit inflammasome-mediated maturation of interleukin-1 beta.",,Abolishes interaction with NLRP2.
173,173,148725,A0A0H2URG7-E244A,MTIYNINLGIGWASSGVEYAQAYRAGVFRKLNLSSKFIFTDMILADNIQHLTANIGFDDNQVIWLYNHFTDIKIAPTSVTVDDVLAYFGGEESHREKNGKVLRVFFFDQDKFVTCYLVDENKDLVQHAEYVFKGNLIRKDYFSYTRYCSEYFAPKDNVAVLYQRTFYNEDGTPVYDILMNQGKEEVYHFKDKIFYGKQAFVRAFMKSLNLNKSDLVILDRETGIGQVVFEEAQTAHLAVVVHAAHYSENATNEDYILWNNYYDYQFTNADKVDFFIVSTDRQNEVLQEQFAKYTQHQPKIVTIPVGSIDSLTDSSQGRKPFSLITASRLAKEKHIDWLVKAVIEAHKELPELTFDIYGSGGEDSLLREIIANHQAEDYIQLKGHAELSQIYSQYEVYLTASTSEGFGLTLMEAIGSGLPLIGFDVPYGNQTFIEDGQNGYLIPSSSDHVEDQIKQAYAAKICQLYQENRLEAMRAYSYQIAEGFLTKEILEKWKKTVEEVLHD,Loss of N-acetylglucosaminyl transferase activity.,,MTIYNINLGIGWASSGVEYAQAYRAGVFRKLNLSSKFIFTDMILADNIQHLTANIGFDDNQVIWLYNHFTDIKIAPTSVTVDDVLAYFGGEESHREKNGKVLRVFFFDQDKFVTCYLVDENKDLVQHAEYVFKGNLIRKDYFSYTRYCSEYFAPKDNVAVLYQRTFYNEDGTPVYDILMNQGKEEVYHFKDKIFYGKQAFVRAFMKSLNLNKSDLVILDRETGIGQVVFEEAQTAHLAVVVHAEHYSENATNEDYILWNNYYDYQFTNADKVDFFIVSTDRQNEVLQEQFAKYTQHQPKIVTIPVGSIDSLTDSSQGRKPFSLITASRLAKEKHIDWLVKAVIEAHKELPELTFDIYGSGGEDSLLREIIANHQAEDYIQLKGHAELSQIYSQYEVYLTASTSEGFGLTLMEAIGSGLPLIGFDVPYGNQTFIEDGQNGYLIPSSSDHVEDQIKQAYAAKICQLYQENRLEAMRAYSYQIAEGFLTKEILEKWKKTVEEVLHD,UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase GtfA subunit,Required for the polymorphic O-glycosylation of serine-rich repeat protein PsrP. Catalyzes the first step in glycosylation by transferring N-acetylglucosamine from UDP-GlcNAc to serine residues in PsrP. Part of the accessory SecA2/SecY2 system specifically required to export serine-rich repeat cell wall proteins encoded upstream in the same operon (Probable). The GtfA-GtfB complex adds GlcNAc from UDP-GlcNAc to PsrP (experimentally characterized with truncated PsrP-SSR1 constructs); this subunit alone has weak N-acetylglucosaminyl transferase activity that is 10-fold stimulated by GtfB. The complex requires at least a 25 residue-long peptide for activity; the in vitro assay has only been seen to glycosylate Ser residues. The alpha linkage was shown in L.reuteri.,,Loss of N-acetylglucosaminyl transferase activity.
174,174,149269,P9WGT3-T114A,MTATATEGAKPPFVSRSVLVTGGNRGIGLAIAQRLAADGHKVAVTHRGSGAPKGLFGVECDVTDSDAVDRAFTAVEEHQGPVEVLVSNAGLSADAFLMRMTEEKFEKVINANLAGAFRVAQRASRSMQRNKFGRMIFIGSVSGSWGIGNQANYAASKAGVIGMARSIARELSKANVTANVVAPGYIDTDMTRALDERIQQGALQFIPAKRVGTPAEVAGVVSFLASEDASYISGAVIPVDGGMGMGH,Slight decrease in phosphorylation by PknB. Lack of phosphorylation by PknB; when associated with A-21 and A-191.,,MTATATEGAKPPFVSRSVLVTGGNRGIGLAIAQRLAADGHKVAVTHRGSGAPKGLFGVECDVTDSDAVDRAFTAVEEHQGPVEVLVSNAGLSADAFLMRMTEEKFEKVINANLTGAFRVAQRASRSMQRNKFGRMIFIGSVSGSWGIGNQANYAASKAGVIGMARSIARELSKANVTANVVAPGYIDTDMTRALDERIQQGALQFIPAKRVGTPAEVAGVVSFLASEDASYISGAVIPVDGGMGMGH,3-oxoacyl-[acyl-carrier-protein] reductase MabA,"Part of the mycobacterial fatty acid elongation system FAS-II, which is involved in mycolic acid biosynthesis. Catalyzes the NADPH-dependent reduction of beta-ketoacyl derivatives, the second step of the FAS-II elongation cycle. May preferentially metabolize long-chain substrates (C8-C20). Can use CoA derivatives as substrates in vitro.",,Slight decrease in phosphorylation by PknB. Lack of phosphorylation by PknB; when associated with A-21 and A-191.
175,175,149499,P08692-C106S,MSNITIYHNPACGTSRNTLEMIRNSGTEPTIILYLENPPSRDELVKLIADMGISVRALLRKNVEPYEQLGLAEDKFTDDQLIDFMLQHPILINRPIVVTPLGTRLSRPSEVVLDILQDAQKGAFTKEDGEKVVDEAGKRLK,Retains reductase activity. Mutant retains arsenate resistance.,,MSNITIYHNPACGTSRNTLEMIRNSGTEPTIILYLENPPSRDELVKLIADMGISVRALLRKNVEPYEQLGLAEDKFTDDQLIDFMLQHPILINRPIVVTPLGTRLCRPSEVVLDILQDAQKGAFTKEDGEKVVDEAGKRLK,Arsenate reductase,Involved in resistance to arsenate. Catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)]. The resulting arsenite is then extruded from the cell via the ArsAB transport system (Probable).,"Cells expressing the arsCC106S gene retained arsenate resistance, and the purified protein had reductase activity.","Retains reductase activity. Mutant retains arsenate resistance. Cells expressing the arsCC106S gene retained arsenate resistance, and the purified protein had reductase activity."
176,176,150354,P51843-L295P,MAGENHQWQGSILYNMLMSAKQTRAAPEAPETRLVDQCWGCSCGDEPGVGREGLLGGRNVALLYRCCFCGKDHPRQGSILYSMLTSAKQTYAAPKAPEATLGPCWGCSCGSDPGVGRAGLPGGRPVALLYRCCFCGEDHPRQGSILYSLLTSSKQTHVAPAAPEARPGGAWWDRSYFAQRPGGKEALPGGRATALLYRCCFCGEDHPQQGSTLYCVPTSTNQAQAAPEERPRAPWWDTSSGALRPVALKSPQVVCEAASAGLLKTLRFVKYLPCFQVLPLDQQLVLVRNCWASLPMLELAQDRLQFETVEVSEPSMLQKILTTRRRETGGNEPLPVPTLQHHLAPPAEARKVPSASQVQAIKCFLSKCWSLNISTKEYAYLKGTVLFNPDVPGLQCVKYIQGLQWGTQQILSEHTRMTHQGPHDRFIELNSTLFLLRFINANVIAELFFRPIIGTVSMDDMMLEMLCTKI,In AHC.,,MAGENHQWQGSILYNMLMSAKQTRAAPEAPETRLVDQCWGCSCGDEPGVGREGLLGGRNVALLYRCCFCGKDHPRQGSILYSMLTSAKQTYAAPKAPEATLGPCWGCSCGSDPGVGRAGLPGGRPVALLYRCCFCGEDHPRQGSILYSLLTSSKQTHVAPAAPEARPGGAWWDRSYFAQRPGGKEALPGGRATALLYRCCFCGEDHPQQGSTLYCVPTSTNQAQAAPEERPRAPWWDTSSGALRPVALKSPQVVCEAASAGLLKTLRFVKYLPCFQVLPLDQQLVLVRNCWASLLMLELAQDRLQFETVEVSEPSMLQKILTTRRRETGGNEPLPVPTLQHHLAPPAEARKVPSASQVQAIKCFLSKCWSLNISTKEYAYLKGTVLFNPDVPGLQCVKYIQGLQWGTQQILSEHTRMTHQGPHDRFIELNSTLFLLRFINANVIAELFFRPIIGTVSMDDMMLEMLCTKI,Nuclear receptor subfamily 0 group B member 1,Orphan nuclear receptor. Component of a cascade required for the development of the hypothalamic-pituitary-adrenal-gonadal axis. Acts as a coregulatory protein that inhibits the transcriptional activity of other nuclear receptors through heterodimeric interactions. May also have a role in the development of the embryo and in the maintenance of embryonic stem cell pluripotency.,"The mutation in the NR0B1 gene leads to functional changes in the protein, resulting in X-linked adrenal hypoplasia congenita.","In AHC. The mutation in the NR0B1 gene leads to functional changes in the protein, resulting in X-linked adrenal hypoplasia congenita."
177,177,151721,Q6UWV6-N121Q,MRGPAVLLTVALATLLAPGAGAPVQSQGSQNKLLLVSFDGFRWNYDQDVDTPNLDAMARDGVKARYMTPAFVTMTSPCHFTLVTGKYIENHGVVHNMYYNTTSKVKLPYHATLGIQRWWDQGSVPIWITAQRQGLRAGSFFYPGGNVTYQGVAVTRSRKEGIAHNYKNETEWRANIDTVMAWFTEEDLDLVTLYFGEPDSTGHRYGPESPERREMVRQVDRTVGYLRESIARNHLTDRLNLIITSDHGMTTVDKRAGDLVEFHKFPNFTFRDIEFELLDYGPNGMLLPKEGRLEKVYDALKDAHPKLHVYKKEAFPEAFHYANNPRVTPLLMYSDLGYVIHGRINVQFNNGEHGFDNKDMDMKTIFRAVGPSFRAGLEVEPFESVHVYELMCRLLGIVPEANDGHLATLLPMLHTESALPPDGRPTLLPKGRSALPPSSRPLLVMGLLGTVILLSEVA,Strongly reduces N-glycosylation and enzyme activity; when associated with Q-100; Q-146; Q-168 and Q-267.,,MRGPAVLLTVALATLLAPGAGAPVQSQGSQNKLLLVSFDGFRWNYDQDVDTPNLDAMARDGVKARYMTPAFVTMTSPCHFTLVTGKYIENHGVVHNMYYNTTSKVKLPYHATLGIQRWWDNGSVPIWITAQRQGLRAGSFFYPGGNVTYQGVAVTRSRKEGIAHNYKNETEWRANIDTVMAWFTEEDLDLVTLYFGEPDSTGHRYGPESPERREMVRQVDRTVGYLRESIARNHLTDRLNLIITSDHGMTTVDKRAGDLVEFHKFPNFTFRDIEFELLDYGPNGMLLPKEGRLEKVYDALKDAHPKLHVYKKEAFPEAFHYANNPRVTPLLMYSDLGYVIHGRINVQFNNGEHGFDNKDMDMKTIFRAVGPSFRAGLEVEPFESVHVYELMCRLLGIVPEANDGHLATLLPMLHTESALPPDGRPTLLPKGRSALPPSSRPLLVMGLLGTVILLSEVA,Ectonucleotide pyrophosphatase/phosphodiesterase family member 7,"Choline-specific phosphodiesterase that hydrolyzes sphingomyelin releasing the ceramide and phosphocholine and therefore is involved in sphingomyelin digestion, ceramide formation, and fatty acid (FA) absorption in the gastrointestinal tract. Has also phospholipase C activity and can also cleave phosphocholine from palmitoyl lyso-phosphatidylcholine and platelet-activating factor (PAF) leading to its inactivation. Does not have nucleotide pyrophosphatase activity. May promote cholesterol absorption by affecting the levels of sphingomyelin derived from either diet or endogenous sources, in the intestinal lumen.",The mutation in alk-SMase severely affects its activity.,Strongly reduces N-glycosylation and enzyme activity; when associated with Q-100; Q-146; Q-168 and Q-267. The mutation in alk-SMase severely affects its activity.
178,178,153365,Q96RL7-L67P,MVFESVVVDVLNRFLGDYVVDLDTSQLSLGIWKGAVALKNLQIKENALSQLDVPFKVKVGHIGNLKPIIPWKNLYTQPVEAVLEEIYLLIVPSSRIKYDPLKEEKQLMEAKQQELKRIEEAKQKVVDQEQHLPEKQDTFAEKLVTQIIKNLQVKISSIHIRYEDDITNRDKPLSFGISLQNLSMQTTDQYWVPCLHDETEKLVRKLIRLDNLFAYWNVKSQMFYLSDYDNSLDDLKNGIVNENIVPEGYDFVFRPISANAKLVMNRRSDFDFSAPKINLEIELHNIAIEFNKPQYFSIMELLESVDMMAQNLPYRKFKPDVPLHHHAREWWAYAIHGVLEVNVCPRLWMWSWKHIRKHRQKVKQYKELYKKKLTSKKPPGELLVSLEELEKTLDVFNITIARQTAEVEVKKAGYKIYKEGVKDPEDNKGWFSWLWSWSEQNTNEQQPDVQPETLEEMLTPEEKALLYEAIGYSETAVDPTLLKTFEALKFFVHLKSMSIVLRENHQKPELVDIVIEEFSTLIVQRPGAQAIKFETKIDSFHITGLPDNSEKPRLLSSLDDAMSLFQITFEINPLDETVSQRCIIEAEPLEIIYDARTVNSIVEFFRPPKEVHLAQLTAATLTKLEEFRSKTATGLLYIIETQKVLDLKINLKASYIIVPQDGIFSPTSNLLLLDLGHLKVTSKSRSELPDVKQGEANLKEIMDRAYDSFDIQLTSVQLLYSRVGDNWREARKLSVSTQHILVPMHFNLELSKAMVFMDVRMPKFKIYGKLPLISLRISDKKLQGIMELIESIPKPEPVTEVSAPVKSFQIQTSTSLGTSQISQKIIPLLELPSVSEDDSEEEFFDAPCSPLEEPLQFPTGVKSIRTRKLQKQDCSVNMTTFKIRFEVPKVLIEFYHLVGDCELSVVEILVLGLGAEIEIRTYDLKANAFLKEFCLKCPEYLDENKKPVYLVTTLDNTMEDLLTLEYVKAEKNVPDLKSTYNNVLQLIKVNFSSLDIHLHTEALLNTINYLHNILPQSEEKSAPV,In CHAC.,,MVFESVVVDVLNRFLGDYVVDLDTSQLSLGIWKGAVALKNLQIKENALSQLDVPFKVKVGHIGNLKLIIPWKNLYTQPVEAVLEEIYLLIVPSSRIKYDPLKEEKQLMEAKQQELKRIEEAKQKVVDQEQHLPEKQDTFAEKLVTQIIKNLQVKISSIHIRYEDDITNRDKPLSFGISLQNLSMQTTDQYWVPCLHDETEKLVRKLIRLDNLFAYWNVKSQMFYLSDYDNSLDDLKNGIVNENIVPEGYDFVFRPISANAKLVMNRRSDFDFSAPKINLEIELHNIAIEFNKPQYFSIMELLESVDMMAQNLPYRKFKPDVPLHHHAREWWAYAIHGVLEVNVCPRLWMWSWKHIRKHRQKVKQYKELYKKKLTSKKPPGELLVSLEELEKTLDVFNITIARQTAEVEVKKAGYKIYKEGVKDPEDNKGWFSWLWSWSEQNTNEQQPDVQPETLEEMLTPEEKALLYEAIGYSETAVDPTLLKTFEALKFFVHLKSMSIVLRENHQKPELVDIVIEEFSTLIVQRPGAQAIKFETKIDSFHITGLPDNSEKPRLLSSLDDAMSLFQITFEINPLDETVSQRCIIEAEPLEIIYDARTVNSIVEFFRPPKEVHLAQLTAATLTKLEEFRSKTATGLLYIIETQKVLDLKINLKASYIIVPQDGIFSPTSNLLLLDLGHLKVTSKSRSELPDVKQGEANLKEIMDRAYDSFDIQLTSVQLLYSRVGDNWREARKLSVSTQHILVPMHFNLELSKAMVFMDVRMPKFKIYGKLPLISLRISDKKLQGIMELIESIPKPEPVTEVSAPVKSFQIQTSTSLGTSQISQKIIPLLELPSVSEDDSEEEFFDAPCSPLEEPLQFPTGVKSIRTRKLQKQDCSVNMTTFKIRFEVPKVLIEFYHLVGDCELSVVEILVLGLGAEIEIRTYDLKANAFLKEFCLKCPEYLDENKKPVYLVTTLDNTMEDLLTLEYVKAEKNVPDLKSTYNNVLQLIKVNFSSLDIHLHTEALLNTINYLHNILPQSEEKSAPV,Intermembrane lipid transfer protein VPS13A,Mediates the transfer of lipids between membranes at organelle contact sites. Binds phospholipids. Required for the formation or stabilization of ER-mitochondria contact sites which enable transfer of lipids between the ER and mitochondria. Negatively regulates lipid droplet size and motility. Required for efficient lysosomal protein degradation.,"The mutation in the VPS13A gene causes a loss of function in chorein, leading to the development of Chorea-acanthocytosis (ChAc). This neurodegenerative disorder is characterized by adult-onset chorea, peripheral acanthocytes, and neuropsychiatric symptoms. The absence of chorein was confirmed in patients with this mutation through Western blotting of erythrocyte ghosts.","In CHAC. The mutation in the VPS13A gene causes a loss of function in chorein, leading to the development of Chorea-acanthocytosis (ChAc). This neurodegenerative disorder is characterized by adult-onset chorea, peripheral acanthocytes, and neuropsychiatric symptoms. The absence of chorein was confirmed in patients with this mutation through Western blotting of erythrocyte ghosts."
179,179,154883,P06022-I114N,MQHDLFEHDPAIRQLIGHIDNIPAPELESRWPRSVVDLIDVLENELKRQNVSNPRELARKQAVALSCFLGGRQFYIPCGDTILTALRDDLLYCQFNGRNMEELRRQYRLSQPQNYQIIARQRKLHTRRHQPDLFSPETPK,Loss of DNA-binding activity.,,MQHDLFEHDPAIRQLIGHIDNIPAPELESRWPRSVVDLIDVLENELKRQNVSNPRELARKQAVALSCFLGGRQFYIPCGDTILTALRDDLLYCQFNGRNMEELRRQYRLSQPQIYQIIARQRKLHTRRHQPDLFSPETPK,Late transcription activator C,"Positive regulator of viral late genes transcription. Responsible for the transition from middle to late gene expression. Activates the Plys, PI, PP and Pmom late promoters thereby allowing the expression of viral endolysin and structural genes. Activates Pmom promoter by unwinding the DNA, thus realigning the promoter elements and recruiting the RNAP.",The mutant protein showed a reduced ability to activate the P(lys)-galK fusion.,Loss of DNA-binding activity. The mutant protein showed a reduced ability to activate the P(lys)-galK fusion.
180,180,155781,Q6UWV6-C78N,MRGPAVLLTVALATLLAPGAGAPVQSQGSQNKLLLVSFDGFRWNYDQDVDTPNLDAMARDGVKARYMTPAFVTMTSPNHFTLVTGKYIENHGVVHNMYYNTTSKVKLPYHATLGIQRWWDNGSVPIWITAQRQGLRAGSFFYPGGNVTYQGVAVTRSRKEGIAHNYKNETEWRANIDTVMAWFTEEDLDLVTLYFGEPDSTGHRYGPESPERREMVRQVDRTVGYLRESIARNHLTDRLNLIITSDHGMTTVDKRAGDLVEFHKFPNFTFRDIEFELLDYGPNGMLLPKEGRLEKVYDALKDAHPKLHVYKKEAFPEAFHYANNPRVTPLLMYSDLGYVIHGRINVQFNNGEHGFDNKDMDMKTIFRAVGPSFRAGLEVEPFESVHVYELMCRLLGIVPEANDGHLATLLPMLHTESALPPDGRPTLLPKGRSALPPSSRPLLVMGLLGTVILLSEVA,Strongly reduces activity.,,MRGPAVLLTVALATLLAPGAGAPVQSQGSQNKLLLVSFDGFRWNYDQDVDTPNLDAMARDGVKARYMTPAFVTMTSPCHFTLVTGKYIENHGVVHNMYYNTTSKVKLPYHATLGIQRWWDNGSVPIWITAQRQGLRAGSFFYPGGNVTYQGVAVTRSRKEGIAHNYKNETEWRANIDTVMAWFTEEDLDLVTLYFGEPDSTGHRYGPESPERREMVRQVDRTVGYLRESIARNHLTDRLNLIITSDHGMTTVDKRAGDLVEFHKFPNFTFRDIEFELLDYGPNGMLLPKEGRLEKVYDALKDAHPKLHVYKKEAFPEAFHYANNPRVTPLLMYSDLGYVIHGRINVQFNNGEHGFDNKDMDMKTIFRAVGPSFRAGLEVEPFESVHVYELMCRLLGIVPEANDGHLATLLPMLHTESALPPDGRPTLLPKGRSALPPSSRPLLVMGLLGTVILLSEVA,Ectonucleotide pyrophosphatase/phosphodiesterase family member 7,"Choline-specific phosphodiesterase that hydrolyzes sphingomyelin releasing the ceramide and phosphocholine and therefore is involved in sphingomyelin digestion, ceramide formation, and fatty acid (FA) absorption in the gastrointestinal tract. Has also phospholipase C activity and can also cleave phosphocholine from palmitoyl lyso-phosphatidylcholine and platelet-activating factor (PAF) leading to its inactivation. Does not have nucleotide pyrophosphatase activity. May promote cholesterol absorption by affecting the levels of sphingomyelin derived from either diet or endogenous sources, in the intestinal lumen.",,Strongly reduces activity.
181,181,157678,Q96MP8-R94W,MVVVTGREPDSRRQDGAMSSSDAEDDFLEPATPTATQAGHALPLLPQEFPEVVPLNIGGAHFTTRLSTLRCYEDTMLAAMFSGRHYIPTDSEGWYFIDRDGTHFGDVLNFLRSGDLPPRERVRAVYKEAQYYAIGPLLEQLENMQPLKGEKVRQAFLGLMPYYKDHLERIVEIARLRAVQRKARFAKLKVCVFKEEMPITPYECPLLNSLRFERSESDGQLFEHHCEVDVSFGPWEAVADVYDLLHCLVTDLSAQGLTVDHQCIGVCDKHLVNHYYCKRPIYEFKITWW,In EPM3.,,MVVVTGREPDSRRQDGAMSSSDAEDDFLEPATPTATQAGHALPLLPQEFPEVVPLNIGGAHFTTRLSTLRCYEDTMLAAMFSGRHYIPTDSEGRYFIDRDGTHFGDVLNFLRSGDLPPRERVRAVYKEAQYYAIGPLLEQLENMQPLKGEKVRQAFLGLMPYYKDHLERIVEIARLRAVQRKARFAKLKVCVFKEEMPITPYECPLLNSLRFERSESDGQLFEHHCEVDVSFGPWEAVADVYDLLHCLVTDLSAQGLTVDHQCIGVCDKHLVNHYYCKRPIYEFKITWW,BTB/POZ domain-containing protein KCTD7,May be involved in the control of excitability of cortical neurons.,The sequence analysis revealed a novel homozygous missense mutation (p. ) in a highly conserved segment of exon 2. This mutation in the KCTD7 gene may be a recurrent cause of PME.,In EPM3. The sequence analysis revealed a novel homozygous missense mutation (p. ) in a highly conserved segment of exon 2. This mutation in the KCTD7 gene may be a recurrent cause of PME.
182,182,158678,Q9NZK5-W362G,MLVDGPSERPALCFLLLAVAMSFFGSALSIDETRAHLLLKEKMMRLGGRLVLNTKEELANERLMTLKIAEMKEAMRTLIFPPSMHFFQAKHLIERSQVFNILRMMPKGAALHLHDIGIVTMDWLVRNVTYRPHCHICFTPRGIMQFRFAHPTPRPSEKCSKWILLEDYRKRVQNVTEFDDSLLRNFTLVTQHPEVIYTNQNVVWSKFETIFFTISGLIHYAPVFRDYVFRSMQEFYEDNVLYMEIRARLLPVYELSGEHHDEEWSVKTYQEVAQKFVETHPEFIGIKIIYSDHRSKDVAVIAESIRMAMGLRIKFPTVVAGFDLVGHEDTGHSLHDYKEALMIPAKDGVKLPYFFHAGETDGQGTSIDRNILDALMLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLVSDLRNHPVATLMATGHPMVISSDDPAMFGAKGLSYDFYEVFMGIGGMKADLRTLKQLAMNSIKYSTLLESEKNTFMEIWKKRWDKFIADVATK,Reduces dimerization and enzyme activity.,,MLVDGPSERPALCFLLLAVAMSFFGSALSIDETRAHLLLKEKMMRLGGRLVLNTKEELANERLMTLKIAEMKEAMRTLIFPPSMHFFQAKHLIERSQVFNILRMMPKGAALHLHDIGIVTMDWLVRNVTYRPHCHICFTPRGIMQFRFAHPTPRPSEKCSKWILLEDYRKRVQNVTEFDDSLLRNFTLVTQHPEVIYTNQNVVWSKFETIFFTISGLIHYAPVFRDYVFRSMQEFYEDNVLYMEIRARLLPVYELSGEHHDEEWSVKTYQEVAQKFVETHPEFIGIKIIYSDHRSKDVAVIAESIRMAMGLRIKFPTVVAGFDLVGHEDTGHSLHDYKEALMIPAKDGVKLPYFFHAGETDWQGTSIDRNILDALMLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLVSDLRNHPVATLMATGHPMVISSDDPAMFGAKGLSYDFYEVFMGIGGMKADLRTLKQLAMNSIKYSTLLESEKNTFMEIWKKRWDKFIADVATK,Adenosine deaminase 2,"Adenosine deaminase that may contribute to the degradation of extracellular adenosine, a signaling molecule that controls a variety of cellular responses. Requires elevated adenosine levels for optimal enzyme activity. Binds to cell surfaces via proteoglycans and may play a role in the regulation of cell proliferation and differentiation, independently of its enzyme activity.","The crystal structures of ADA2 and ADA2 bound to a transition state analogue presented here reveal the structural basis of the catalytic/signaling activity of ADGF/ADA2 proteins. In addition to the catalytic domain, the structures discovered two ADGF/ADA2-specific domains of novel folds that mediate the protein dimerization and binding to the cell surface receptors. This complex architecture is in sharp contrast with that of monomeric single domain ADA1. An extensive glycosylation and the presence of a conserved disulfide bond and a signal peptide in ADA2 strongly suggest that ADA2, in contrast to ADA1, is specifically designed to act in the extracellular environment. The comparison of catalytic sites of ADA2 and ADA1 demonstrates large differences in the arrangement of the substrate-binding pockets. These structural differences explain the substrate and inhibitor specificity of adenosine deaminases and provide the basis for a rational design of ADA2-targeting drugs to modulate the immune system responses in pathophysiological conditions.","Reduces dimerization and enzyme activity. The crystal structures of ADA2 and ADA2 bound to a transition state analogue presented here reveal the structural basis of the catalytic/signaling activity of ADGF/ADA2 proteins. In addition to the catalytic domain, the structures discovered two ADGF/ADA2-specific domains of novel folds that mediate the protein dimerization and binding to the cell surface receptors. This complex architecture is in sharp contrast with that of monomeric single domain ADA1. An extensive glycosylation and the presence of a conserved disulfide bond and a signal peptide in ADA2 strongly suggest that ADA2, in contrast to ADA1, is specifically designed to act in the extracellular environment. The comparison of catalytic sites of ADA2 and ADA1 demonstrates large differences in the arrangement of the substrate-binding pockets. These structural differences explain the substrate and inhibitor specificity of adenosine deaminases and provide the basis for a rational design of ADA2-targeting drugs to modulate the immune system responses in pathophysiological conditions."
183,183,160526,P9WGT3-C60V,MTATATEGAKPPFVSRSVLVTGGNRGIGLAIAQRLAADGHKVAVTHRGSGAPKGLFGVEVDVTDSDAVDRAFTAVEEHQGPVEVLVSNAGLSADAFLMRMTEEKFEKVINANLTGAFRVAQRASRSMQRNKFGRMIFIGSVSGSWGIGNQANYAASKAGVIGMARSIARELSKANVTANVVAPGYIDTDMTRALDERIQQGALQFIPAKRVGTPAEVAGVVSFLASEDASYISGAVIPVDGGMGMGH,Displays a lower activity than the wild-type and a slightly decreased affinity for the cofactor. Retains 84% of activity; when associated with L-144. Totally inactive; when associated with A-139 and L-144.,,MTATATEGAKPPFVSRSVLVTGGNRGIGLAIAQRLAADGHKVAVTHRGSGAPKGLFGVECDVTDSDAVDRAFTAVEEHQGPVEVLVSNAGLSADAFLMRMTEEKFEKVINANLTGAFRVAQRASRSMQRNKFGRMIFIGSVSGSWGIGNQANYAASKAGVIGMARSIARELSKANVTANVVAPGYIDTDMTRALDERIQQGALQFIPAKRVGTPAEVAGVVSFLASEDASYISGAVIPVDGGMGMGH,3-oxoacyl-[acyl-carrier-protein] reductase MabA,"Part of the mycobacterial fatty acid elongation system FAS-II, which is involved in mycolic acid biosynthesis. Catalyzes the NADPH-dependent reduction of beta-ketoacyl derivatives, the second step of the FAS-II elongation cycle. May preferentially metabolize long-chain substrates (C8-C20). Can use CoA derivatives as substrates in vitro.",,Displays a lower activity than the wild-type and a slightly decreased affinity for the cofactor. Retains 84% of activity; when associated with L-144. Totally inactive; when associated with A-139 and L-144.
184,184,161724,P06022-L83R,MQHDLFEHDPAIRQLIGHIDNIPAPELESRWPRSVVDLIDVLENELKRQNVSNPRELARKQAVALSCFLGGRQFYIPCGDTIRTALRDDLLYCQFNGRNMEELRRQYRLSQPQIYQIIARQRKLHTRRHQPDLFSPETPK,No effect on dimerization and DNA binding. Complete loss of dimerization and DNA-binding when associated with Ser-90.,,MQHDLFEHDPAIRQLIGHIDNIPAPELESRWPRSVVDLIDVLENELKRQNVSNPRELARKQAVALSCFLGGRQFYIPCGDTILTALRDDLLYCQFNGRNMEELRRQYRLSQPQIYQIIARQRKLHTRRHQPDLFSPETPK,Late transcription activator C,"Positive regulator of viral late genes transcription. Responsible for the transition from middle to late gene expression. Activates the Plys, PI, PP and Pmom late promoters thereby allowing the expression of viral endolysin and structural genes. Activates Pmom promoter by unwinding the DNA, thus realigning the promoter elements and recruiting the RNAP.","The mutation in the C protein leads to a functional alteration in dimerization. Site-directed mutational analysis revealed that the amino-terminal coiled coil region is not the dimerization determinant, but the leucine zipper motif located in the middle region of the protein plays a role in dimerization.","No effect on dimerization and DNA binding. Complete loss of dimerization and DNA-binding when associated with Ser-90. The mutation in the C protein leads to a functional alteration in dimerization. Site-directed mutational analysis revealed that the amino-terminal coiled coil region is not the dimerization determinant, but the leucine zipper motif located in the middle region of the protein plays a role in dimerization."
185,185,161753,O15393-S441A,MALNSGSPPAIGPYYENHGYQPENPYPAQPTVVPTVYEVHPAQYYPSPVPQYAPRVLTQASNPVVCTQPKSPSGTVCTSKTKKALCITLTLGTFLVGAALAAGLLWKFMGSKCSNSGIECDSSGTCINPSNWCDGVSHCPGGEDENRCVRLYGPNFILQVYSSQRKSWHPVCQDDWNENYGRAACRDMGYKNNFYSSQGIVDDSGSTSFMKLNTSAGNVDIYKKLYHSDACSSKAVVSLRCIACGVNLNSSRQSRIVGGESALPGAWPWQVSLHVQNVHVCGGSIITPEWIVTAAHCVEKPLNNPWHWTAFAGILRQSFMFYGAGYQVEKVISHPNYDSKTKNNDIALMKLQKPLTFNDLVKPVCLPNPGMMLQPEQLCWISGWGATEEKGKTSEVLNAAKVLLIETQRCNSRYVYDNLITPAMICAGFLQGNVDSCQGDAGGPLVTSKNNIWWLIGDTSWGSGCAKAYRPGVYGNVMVFTDWIYRQMRADG,Loss of activity.,,MALNSGSPPAIGPYYENHGYQPENPYPAQPTVVPTVYEVHPAQYYPSPVPQYAPRVLTQASNPVVCTQPKSPSGTVCTSKTKKALCITLTLGTFLVGAALAAGLLWKFMGSKCSNSGIECDSSGTCINPSNWCDGVSHCPGGEDENRCVRLYGPNFILQVYSSQRKSWHPVCQDDWNENYGRAACRDMGYKNNFYSSQGIVDDSGSTSFMKLNTSAGNVDIYKKLYHSDACSSKAVVSLRCIACGVNLNSSRQSRIVGGESALPGAWPWQVSLHVQNVHVCGGSIITPEWIVTAAHCVEKPLNNPWHWTAFAGILRQSFMFYGAGYQVEKVISHPNYDSKTKNNDIALMKLQKPLTFNDLVKPVCLPNPGMMLQPEQLCWISGWGATEEKGKTSEVLNAAKVLLIETQRCNSRYVYDNLITPAMICAGFLQGNVDSCQGDSGGPLVTSKNNIWWLIGDTSWGSGCAKAYRPGVYGNVMVFTDWIYRQMRADG,Transmembrane protease serine 2,"Plasma membrane-anchored serine protease that cleaves at arginine residues. Participates in proteolytic cascades of relevance for the normal physiologic function of the prostate. Androgen-induced TMPRSS2 activates several substrates that include pro-hepatocyte growth factor/HGF, the protease activated receptor-2/F2RL1 or matriptase/ST14 leading to extracellular matrix disruption and metastasis of prostate cancer cells. In addition, activates trigeminal neurons and contribute to both spontaneous pain and mechanical allodynia.(Microbial infection) Facilitates human coronaviruses SARS-CoV and SARS-CoV-2 infections via two independent mechanisms, proteolytic cleavage of ACE2 receptor which promotes viral uptake, and cleavage of coronavirus spike glycoproteins which activates the glycoprotein for host cell entry. The cleavage of SARS-COV2 spike glycoprotein occurs between the S2 and S2' site. Upon SARS-CoV-2 infection, increases syncytia formation by accelerating the fusion process. Proteolytically cleaves and activates the spike glycoproteins of human coronavirus 229E (HCoV-229E) and human coronavirus EMC (HCoV-EMC) and the fusion glycoproteins F0 of Sendai virus (SeV), human metapneumovirus (HMPV), human parainfluenza 1, 2, 3, 4a and 4b viruses (HPIV). Essential for spread and pathogenesis of influenza A virus (strains H1N1, H3N2 and H7N9); involved in proteolytic cleavage and activation of hemagglutinin (HA) protein which is essential for viral infectivity.","Mutation of S-441 in the catalytic triad shows that the proteolytic cleavage is dependent on catalytic activity, suggesting that it occurs as a result of autocleavage.","Loss of activity. Mutation of S-441 in the catalytic triad shows that the proteolytic cleavage is dependent on catalytic activity, suggesting that it occurs as a result of autocleavage."
186,186,162080,Q1PEI6-I347T,MEFSCVHFLQNKTILVTGATGFLAKVFVEKILRVQPNVNKLYLVVRASDNEAATKRLRTEAFEKDLFKVLRDNLGDEKLNTLLSEKVVPVAGDIAMDHLGMKDSNLRERMQKEIDIVVNVAATTNFDERYDIGLGINTFGALNVLNFAKKCVKAQLLLHVSTAYVCGEKPGLLPEKPFVMEEICNENGLQLDINLERELMKQRLKELNEQGCSEEGTTFYMKELGMERAKLHGWPNTYVFTKSMGEMLLGNHKENLPLVIIRPTMITSTLFEPFPGWIEGLRTVDSVIIAYGKGVLKCFLVDVNSVCDMIPADMVANAMIAAAATHAGGSKVHMVYQVGSSHQNPITYGEIREILFCYFTKNSLRSRNGSMITVSKMKLIPTLALFSLYMTIRYKLPVQLLKLVDIIYPSREGDEYKNKNRKIDMVMRLVKLYEPYVLFKGIFDDRNTKNLCAKQKEEDNRNSENFMFDFDPKIIKWKDYLINVHIPGLITHVLKK,Increases protein stability and enzymatic activity. Catalyzes the formation of C18:0 fatty alcohol instead of C16:0; when associated with A-355 and V-377.,,MEFSCVHFLQNKTILVTGATGFLAKVFVEKILRVQPNVNKLYLVVRASDNEAATKRLRTEAFEKDLFKVLRDNLGDEKLNTLLSEKVVPVAGDIAMDHLGMKDSNLRERMQKEIDIVVNVAATTNFDERYDIGLGINTFGALNVLNFAKKCVKAQLLLHVSTAYVCGEKPGLLPEKPFVMEEICNENGLQLDINLERELMKQRLKELNEQGCSEEGTTFYMKELGMERAKLHGWPNTYVFTKSMGEMLLGNHKENLPLVIIRPTMITSTLFEPFPGWIEGLRTVDSVIIAYGKGVLKCFLVDVNSVCDMIPADMVANAMIAAAATHAGGSKVHMVYQVGSSHQNPIIYGEIREILFCYFTKNSLRSRNGSMITVSKMKLIPTLALFSLYMTIRYKLPVQLLKLVDIIYPSREGDEYKNKNRKIDMVMRLVKLYEPYVLFKGIFDDRNTKNLCAKQKEEDNRNSENFMFDFDPKIIKWKDYLINVHIPGLITHVLKK,Fatty acyl-CoA reductase 8,Catalyzes the reduction of fatty acyl-CoA to fatty alcohols. Catalyzes specifically the formation of C16:0 fatty alcohol.,,Increases protein stability and enzymatic activity. Catalyzes the formation of C18:0 fatty alcohol instead of C16:0; when associated with A-355 and V-377.
187,187,162717,P51843-L297P,MAGENHQWQGSILYNMLMSAKQTRAAPEAPETRLVDQCWGCSCGDEPGVGREGLLGGRNVALLYRCCFCGKDHPRQGSILYSMLTSAKQTYAAPKAPEATLGPCWGCSCGSDPGVGRAGLPGGRPVALLYRCCFCGEDHPRQGSILYSLLTSSKQTHVAPAAPEARPGGAWWDRSYFAQRPGGKEALPGGRATALLYRCCFCGEDHPQQGSTLYCVPTSTNQAQAAPEERPRAPWWDTSSGALRPVALKSPQVVCEAASAGLLKTLRFVKYLPCFQVLPLDQQLVLVRNCWASLLMPELAQDRLQFETVEVSEPSMLQKILTTRRRETGGNEPLPVPTLQHHLAPPAEARKVPSASQVQAIKCFLSKCWSLNISTKEYAYLKGTVLFNPDVPGLQCVKYIQGLQWGTQQILSEHTRMTHQGPHDRFIELNSTLFLLRFINANVIAELFFRPIIGTVSMDDMMLEMLCTKI,In AHC; results in a severe loss of repressor activity.,,MAGENHQWQGSILYNMLMSAKQTRAAPEAPETRLVDQCWGCSCGDEPGVGREGLLGGRNVALLYRCCFCGKDHPRQGSILYSMLTSAKQTYAAPKAPEATLGPCWGCSCGSDPGVGRAGLPGGRPVALLYRCCFCGEDHPRQGSILYSLLTSSKQTHVAPAAPEARPGGAWWDRSYFAQRPGGKEALPGGRATALLYRCCFCGEDHPQQGSTLYCVPTSTNQAQAAPEERPRAPWWDTSSGALRPVALKSPQVVCEAASAGLLKTLRFVKYLPCFQVLPLDQQLVLVRNCWASLLMLELAQDRLQFETVEVSEPSMLQKILTTRRRETGGNEPLPVPTLQHHLAPPAEARKVPSASQVQAIKCFLSKCWSLNISTKEYAYLKGTVLFNPDVPGLQCVKYIQGLQWGTQQILSEHTRMTHQGPHDRFIELNSTLFLLRFINANVIAELFFRPIIGTVSMDDMMLEMLCTKI,Nuclear receptor subfamily 0 group B member 1,Orphan nuclear receptor. Component of a cascade required for the development of the hypothalamic-pituitary-adrenal-gonadal axis. Acts as a coregulatory protein that inhibits the transcriptional activity of other nuclear receptors through heterodimeric interactions. May also have a role in the development of the embryo and in the maintenance of embryonic stem cell pluripotency.,The mutation is a missense mutation in the DAX-1 gene. It occurs within a highly conserved binding motif (LLXLXL). Transient transfection assays demonstrated that the mutation resulted in a severe loss of DAX-1 repressor activity.,In AHC; results in a severe loss of repressor activity. The mutation is a missense mutation in the DAX-1 gene. It occurs within a highly conserved binding motif (LLXLXL). Transient transfection assays demonstrated that the mutation resulted in a severe loss of DAX-1 repressor activity.
188,188,163535,P08692-E130D,MSNITIYHNPACGTSRNTLEMIRNSGTEPTIILYLENPPSRDELVKLIADMGISVRALLRKNVEPYEQLGLAEDKFTDDQLIDFMLQHPILINRPIVVTPLGTRLCRPSEVVLDILQDAQKGAFTKEDGDKVVDEAGKRLK,"5-fold decrease in catalytic efficiency with arsenate. Mutant is relatively resistant to arsenate, but is more sensitive at higher concentrations.",,MSNITIYHNPACGTSRNTLEMIRNSGTEPTIILYLENPPSRDELVKLIADMGISVRALLRKNVEPYEQLGLAEDKFTDDQLIDFMLQHPILINRPIVVTPLGTRLCRPSEVVLDILQDAQKGAFTKEDGEKVVDEAGKRLK,Arsenate reductase,Involved in resistance to arsenate. Catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)]. The resulting arsenite is then extruded from the cell via the ArsAB transport system (Probable).,,"5-fold decrease in catalytic efficiency with arsenate. Mutant is relatively resistant to arsenate, but is more sensitive at higher concentrations."
189,189,163672,Q9H5P4-G228R,MAQGFAVGFDPLGLGDLSSGSLSSLSSRGHLGSDSGSTATRYLLRKQQRLLNGPPRGIRASSPMGRVILINSPIEANSDESDIIHSVRVEKSPAGRLGFSVRGGSEHGLGIFVSKVEEGSSAERAGLCVGDKITEVNGLSLESTTMGSAVKVLTSSSRLHMMVRRMGRVPGIKFSKEKTTWVDVVNRRLVVEKCGSTPSDTSSEDGVRRIVHLYTTSDDFCLGFNIRRGKEFGLGIYVSKVDHGGLAEENGIKVGDQVLAANGVRFDDISHSQAVEVLKGQTHIMLTIKETGRYPAYKEMVSEYCWLDRLSNGVLQQLSPASESSSSVSSCASSAPYSSGSLPSDRMDICLGQEEPGSRGPGWGRADTAMQTEPDAGGRVETWCSVRPTVILRDTAIRSDGPHPGRRLDSALSESPKTALLLALSRPRPPITRSQSYLTLWEEKQQRKKEKSGSPGEKGALQRSKTLMNLFFKGGRQGRLARDGRREAWTLDSGSLAKTYPRLDIEKAGGVGPVQKFVTWRLRRDQERGRALLSARSGSPSSQLPNVDEQVQAWESRRPLIQDLAQRLLTDDEVLAVTRHCSRYVHEGGIEDLVRPLLAILDRPEKLLLLQDIRSVVAPTDLGRFDSMVMLVELEAFEALKSRAVRPPALRPARQDTPPKRHLITPVPDSRGGFYLLPVNGFPEEEDNGELRERLGALKVSPSASAPRHPHKGIPPLQDVPVDAFTPLRIACTPPPQLPPVAPRPLRPNWLLTEPLSREHPPQSQIRGRAQSRSRSRSRSRSRSSRGQGKSPGRRSPSPVPTPAPSMTNGRYHKPRKARPPLPRPLDGEAAKVGAKQGPSESGTEGTAKEAAMKNPSGELKTVTLSKMKQSLGISISGGIESKVQPMVKIEKIFPGGAAFLSGALQAGFELVAVDGENLEQVTHQRAVDTIRRAYRNKAREPMELVVRVPGPSPRPSPSDSSALTDGGLPADHLPAHQPLDAAPVPAHWLPEPPTNPQTPPTDARLLQPTPSPAPSPALQTPDS,In DFNB57.,,MAQGFAVGFDPLGLGDLSSGSLSSLSSRGHLGSDSGSTATRYLLRKQQRLLNGPPRGIRASSPMGRVILINSPIEANSDESDIIHSVRVEKSPAGRLGFSVRGGSEHGLGIFVSKVEEGSSAERAGLCVGDKITEVNGLSLESTTMGSAVKVLTSSSRLHMMVRRMGRVPGIKFSKEKTTWVDVVNRRLVVEKCGSTPSDTSSEDGVRRIVHLYTTSDDFCLGFNIRGGKEFGLGIYVSKVDHGGLAEENGIKVGDQVLAANGVRFDDISHSQAVEVLKGQTHIMLTIKETGRYPAYKEMVSEYCWLDRLSNGVLQQLSPASESSSSVSSCASSAPYSSGSLPSDRMDICLGQEEPGSRGPGWGRADTAMQTEPDAGGRVETWCSVRPTVILRDTAIRSDGPHPGRRLDSALSESPKTALLLALSRPRPPITRSQSYLTLWEEKQQRKKEKSGSPGEKGALQRSKTLMNLFFKGGRQGRLARDGRREAWTLDSGSLAKTYPRLDIEKAGGVGPVQKFVTWRLRRDQERGRALLSARSGSPSSQLPNVDEQVQAWESRRPLIQDLAQRLLTDDEVLAVTRHCSRYVHEGGIEDLVRPLLAILDRPEKLLLLQDIRSVVAPTDLGRFDSMVMLVELEAFEALKSRAVRPPALRPARQDTPPKRHLITPVPDSRGGFYLLPVNGFPEEEDNGELRERLGALKVSPSASAPRHPHKGIPPLQDVPVDAFTPLRIACTPPPQLPPVAPRPLRPNWLLTEPLSREHPPQSQIRGRAQSRSRSRSRSRSRSSRGQGKSPGRRSPSPVPTPAPSMTNGRYHKPRKARPPLPRPLDGEAAKVGAKQGPSESGTEGTAKEAAMKNPSGELKTVTLSKMKQSLGISISGGIESKVQPMVKIEKIFPGGAAFLSGALQAGFELVAVDGENLEQVTHQRAVDTIRRAYRNKAREPMELVVRVPGPSPRPSPSDSSALTDGGLPADHLPAHQPLDAAPVPAHWLPEPPTNPQTPPTDARLLQPTPSPAPSPALQTPDS,PDZ domain-containing protein 7,"In cochlear developing hair cells, essential in organizing the USH2 complex at stereocilia ankle links. Blocks inhibition of adenylate cyclase activity mediated by ADGRV1.",A novel likely disease-causing mutation (p. ) is identified.,In DFNB57. A novel likely disease-causing mutation (p. ) is identified.
190,190,164551,Q9UPT6-R578C,MMEIQMDEGGGVVVYQDDYCSGSVMSERVSGLAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEERESEMKKEYNALHQRHTEMIQTYVEHIERSKMQQVGGNSQTESSLPGRRKERPTSLNVFPLADGTVRAQIGGKLVPAGDHWHLSDLGQLQSSSSYQCPQDEMSESGQSSAAATPSTTGTKSNTPTSSVPSAAVTPLNESLQPLGDYGVGSKNSKRAREKRDSRNMEVQVTQEMRNVSIGMGSSDEWSDVQDIIDSTPELDMCPETRLDRTGSSPTQGIVNKAFGINTDSLYHELSTAGSEVIGDVDEGADLLGEFSVRDDFFGMGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEAIIARREPKEEAEDVSSYLCTESDKIPMAQRRRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASREHPSVQEKKKSTIWQFFSCLFSSSSSPPPAKRPYPSVNIHYKSPTTAGFSQRRNHAMCPISAGSRPLEFFPDDDCTSSARREQKREQYRQVREHVRNDDGRLQACGWSLPAKYKQLSPNGGQEDTRMKNVPVPVYCRPLVEKDPTMKLWCAAGVNLSGWRPNEDDAGNGVKPAPGRDPLTCDREGDGEPKSAHTSPEKKKAKELPEMDATSSRVWILTSTLTTSKVVIIDANQPGTVVDQFTVCNAHVLCISSIPAASDSDYPPGEMFLDSDVNPEDPGADGVLAGITLVGCATRCNVPRSNCSSRGDTPVLDKGQGEVATIANGKVNPSQSTEEATEATEVPDPGPSEPETATLRPGPLTEHVFTDPAPTPSSGPQPGSENGPEPDSSSTRPEPEPSGDPTGAGSSAAPTMWLGAQNGWLYVHSAVANWKKCLHSIKLKDSVLSLVHVKGRVLVALADGTLAIF,In NEDBA; affects axon development when expressed in a heterologous system.,,MMEIQMDEGGGVVVYQDDYCSGSVMSERVSGLAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEERESEMKKEYNALHQRHTEMIQTYVEHIERSKMQQVGGNSQTESSLPGRRKERPTSLNVFPLADGTVRAQIGGKLVPAGDHWHLSDLGQLQSSSSYQCPQDEMSESGQSSAAATPSTTGTKSNTPTSSVPSAAVTPLNESLQPLGDYGVGSKNSKRAREKRDSRNMEVQVTQEMRNVSIGMGSSDEWSDVQDIIDSTPELDMCPETRLDRTGSSPTQGIVNKAFGINTDSLYHELSTAGSEVIGDVDEGADLLGEFSVRDDFFGMGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEAIIARREPKEEAEDVSSYLCTESDKIPMAQRRRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASREHPSVQEKKKSTIWQFFSRLFSSSSSPPPAKRPYPSVNIHYKSPTTAGFSQRRNHAMCPISAGSRPLEFFPDDDCTSSARREQKREQYRQVREHVRNDDGRLQACGWSLPAKYKQLSPNGGQEDTRMKNVPVPVYCRPLVEKDPTMKLWCAAGVNLSGWRPNEDDAGNGVKPAPGRDPLTCDREGDGEPKSAHTSPEKKKAKELPEMDATSSRVWILTSTLTTSKVVIIDANQPGTVVDQFTVCNAHVLCISSIPAASDSDYPPGEMFLDSDVNPEDPGADGVLAGITLVGCATRCNVPRSNCSSRGDTPVLDKGQGEVATIANGKVNPSQSTEEATEATEVPDPGPSEPETATLRPGPLTEHVFTDPAPTPSSGPQPGSENGPEPDSSSTRPEPEPSGDPTGAGSSAAPTMWLGAQNGWLYVHSAVANWKKCLHSIKLKDSVLSLVHVKGRVLVALADGTLAIF,C-Jun-amino-terminal kinase-interacting protein 3,"The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. May function as a regulator of vesicle transport, through interactions with the JNK-signaling components and motor proteins. Promotes neuronal axon elongation in a kinesin- and JNK-dependent manner. Activates cofilin at axon tips via local activation of JNK, thereby regulating filopodial dynamics and enhancing axon elongation. Its binding to kinesin heavy chains (KHC), promotes kinesin-1 motility along microtubules and is essential for axon elongation and regeneration. Regulates cortical neuronal migration by mediating NTRK2/TRKB anterograde axonal transport during brain development. Acts as an adapter that bridges the interaction between NTRK2/TRKB and KLC1 and drives NTRK2/TRKB axonal but not dendritic anterograde transport, which is essential for subsequent BDNF-triggered signaling and filopodia formation.","The de novo variant in MAPK8IP3 has been identified in individuals presenting with an overlapping phenotype of mild to severe intellectual disability. Brain anomalies such as perisylvian polymicrogyria, cerebral or cerebellar atrophy, and hypoplasia of the corpus callosum were consistent among individuals harboring this variant. The core phenotype includes spastic diplegia, intellectual disability, cerebral atrophy, and corpus callosum hypoplasia. Zebrafish embryos overexpressing human mutant JIP3 showed axon varicosities of the posterior lateral line nerve, suggesting an adverse effect on the developing axons. Our results suggest that MAPK8IP3 variants cause a neurodevelopmental disease.","In NEDBA; affects axon development when expressed in a heterologous system. The de novo variant in MAPK8IP3 has been identified in individuals presenting with an overlapping phenotype of mild to severe intellectual disability. Brain anomalies such as perisylvian polymicrogyria, cerebral or cerebellar atrophy, and hypoplasia of the corpus callosum were consistent among individuals harboring this variant. The core phenotype includes spastic diplegia, intellectual disability, cerebral atrophy, and corpus callosum hypoplasia. Zebrafish embryos overexpressing human mutant JIP3 showed axon varicosities of the posterior lateral line nerve, suggesting an adverse effect on the developing axons. Our results suggest that MAPK8IP3 variants cause a neurodevelopmental disease."
191,191,165556,O14746-P704S,MPRAPRCRAVRSLLRSHYREVLPLATFVRRLGPQGWRLVQRGDPAAFRALVAQCLVCVPWDARPPPAAPSFRQVSCLKELVARVLQRLCERGAKNVLAFGFALLDGARGGPPEAFTTSVRSYLPNTVTDALRGSGAWGLLLRRVGDDVLVHLLARCALFVLVAPSCAYQVCGPPLYQLGAATQARPPPHASGPRRRLGCERAWNHSVREAGVPLGLPAPGARRRGGSASRSLPLPKRPRRGAAPEPERTPVGQGSWAHPGRTRGPSDRGFCVVSPARPAEEATSLEGALSGTRHSHPSVGRQHHAGPPSTSRPPRPWDTPCPPVYAETKHFLYSSGDKEQLRPSFLLSSLRPSLTGARRLVETIFLGSRPWMPGTPRRLPRLPQRYWQMRPLFLELLGNHAQCPYGVLLKTHCPLRAAVTPAAGVCAREKPQGSVAAPEEEDTDPRRLVQLLRQHSSPWQVYGFVRACLRRLVPPGLWGSRHNERRFLRNTKKFISLGKHAKLSLQELTWKMSVRDCAWLRRSPGVGCVPAAEHRLREEILAKFLHWLMSVYVVELLRSFFYVTETTFQKNRLFFYRKSVWSKLQSIGIRQHLKRVQLRELSEAEVRQHREARPALLTSRLRFIPKPDGLRPIVNMDYVVGARTFRREKRAERLTSRVKALFSVLNYERARRPGLLGASVLGLDDIHRAWRTFVLRVRAQDPPSELYFVKVDVTGAYDTIPQDRLTEVIASIIKPQNTYCVRRYAVVQKAAHGHVRKAFKSHVSTLTDLQPYMRQFVAHLQETSPLRDAVVIEQSSSLNEASSGLFDVFLRFMCHHAVRIRGKSYVQCQGIPQGSILSTLLCSLCYGDMENKLFAGIRRDGLLLRLVDDFLLVTPHLTHAKTFLRTLVRGVPEYGCVVNLRKTVVNFPVEDEALGGTAFVQMPAHGLFPWCGLLLDTRTLEVQSDYSSYARTSIRASLTFNRGFKAGRNMRRKLFGVLRLKCHSLFLDLQVNSLQTVCTNIYKILLLQAYRFHACVLQLPFHQQ,In DKCB4; the mutant protein has 13% residual activity.,,MPRAPRCRAVRSLLRSHYREVLPLATFVRRLGPQGWRLVQRGDPAAFRALVAQCLVCVPWDARPPPAAPSFRQVSCLKELVARVLQRLCERGAKNVLAFGFALLDGARGGPPEAFTTSVRSYLPNTVTDALRGSGAWGLLLRRVGDDVLVHLLARCALFVLVAPSCAYQVCGPPLYQLGAATQARPPPHASGPRRRLGCERAWNHSVREAGVPLGLPAPGARRRGGSASRSLPLPKRPRRGAAPEPERTPVGQGSWAHPGRTRGPSDRGFCVVSPARPAEEATSLEGALSGTRHSHPSVGRQHHAGPPSTSRPPRPWDTPCPPVYAETKHFLYSSGDKEQLRPSFLLSSLRPSLTGARRLVETIFLGSRPWMPGTPRRLPRLPQRYWQMRPLFLELLGNHAQCPYGVLLKTHCPLRAAVTPAAGVCAREKPQGSVAAPEEEDTDPRRLVQLLRQHSSPWQVYGFVRACLRRLVPPGLWGSRHNERRFLRNTKKFISLGKHAKLSLQELTWKMSVRDCAWLRRSPGVGCVPAAEHRLREEILAKFLHWLMSVYVVELLRSFFYVTETTFQKNRLFFYRKSVWSKLQSIGIRQHLKRVQLRELSEAEVRQHREARPALLTSRLRFIPKPDGLRPIVNMDYVVGARTFRREKRAERLTSRVKALFSVLNYERARRPGLLGASVLGLDDIHRAWRTFVLRVRAQDPPPELYFVKVDVTGAYDTIPQDRLTEVIASIIKPQNTYCVRRYAVVQKAAHGHVRKAFKSHVSTLTDLQPYMRQFVAHLQETSPLRDAVVIEQSSSLNEASSGLFDVFLRFMCHHAVRIRGKSYVQCQGIPQGSILSTLLCSLCYGDMENKLFAGIRRDGLLLRLVDDFLLVTPHLTHAKTFLRTLVRGVPEYGCVVNLRKTVVNFPVEDEALGGTAFVQMPAHGLFPWCGLLLDTRTLEVQSDYSSYARTSIRASLTFNRGFKAGRNMRRKLFGVLRLKCHSLFLDLQVNSLQTVCTNIYKILLLQAYRFHACVLQLPFHQQ,Telomerase reverse transcriptase,"Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. Active in progenitor and cancer cells. Inactive, or very low activity, in normal somatic cells. Catalytic component of the teleromerase holoenzyme complex whose main activity is the elongation of telomeres by acting as a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme. Catalyzes the RNA-dependent extension of 3'-chromosomal termini with the 6-nucleotide telomeric repeat unit, 5'-TTAGGG-3'. The catalytic cycle involves primer binding, primer extension and release of product once the template boundary has been reached or nascent product translocation followed by further extension. More active on substrates containing 2 or 3 telomeric repeats. Telomerase activity is regulated by a number of factors including telomerase complex-associated proteins, chaperones and polypeptide modifiers. Modulates Wnt signaling. Plays important roles in aging and antiapoptosis.",The proband is homozygous for a novel mutation causing a substitution.,In DKCB4; the mutant protein has 13% residual activity. The proband is homozygous for a novel mutation causing a substitution.
192,192,165616,Q92619-R139H,MFSRKKRELMKTPSISKKNRAGSPSPQPSGELPRKDGADAVFPGPSLEPPAGSSGVKATGTLKRPTSLSRHASAAGFPLSGAASWTLGRSHRSPLTAASPGELPTEGAGPDVVEDISHLLADVARFAEGLEKLKECVLHDDLLEARRPRAHECLGEALRVMHQIISKYPLLNTVETLTAAGTLIAKVKAFHYESNNDLEKQEFEKALETIAVAFSSTVSEFLMGEVDSSTLLAVPPGDSSQSMESLYGPGSEGTPPSLEDCDAGCLPAEEVDVLLQRCEGGVDAALLYAKNMAKYMKDLISYLEKRTTLEMEFAKGLQKIAHNCRQSVMQEPHMPLLSIYSLALEQDLEFGHSMVQAVGTLQTQTFMQPLTLRRLEHEKRRKEIKEAWHRAQRKLQEAESNLRKAKQGYVQRCEDHDKARFLVAKAEEEQAGSAPGAGSTATKTLDKRRRLEEEAKNKAEEAMATYRTCVADAKTQKQELEDTKVTALRQIQEVIRQSDQTIKSATISYYQMMHMQTAPLPVHFQMLCESSKLYDPGQQYASHVRQLQRDQEPDVHYDFEPHVSANAWSPVMRARKSSFNVSDVARPEAAGSPPEEGGCTEGTPAKDHRAGRGHQVHKSWPLSISDSDSGLDPGPGAGDFKKFERTSSSGTMSSTEELVDPDGGAGASAFEQADLNGMTPELPVAVPSGPFRHEGLSKAARTHRLRKLRTPAKCRECNSYVYFQGAECEECCLACHKKCLETLAIQCGHKKLQGRLQLFGQDFSHAARSAPDGVPFIVKKCVCEIERRALRTKGIYRVNGVKTRVEKLCQAFENGKELVELSQASPHDISNVLKLYLRQLPEPLISFRLYHELVGLAKDSLKAEAEAKAASRGRQDGSESEAVAVALAGRLRELLRDLPPENRASLQYLLRHLRRIVEVEQDNKMTPGNLGIVFGPTLLRPRPTEATVSLSSLVDYPHQARVIETLIVHYGLVFEEEPEETPGGQDESSNQRAEVVVQVPYLEAGEAVVYPLQEAAADGCRESR,In allele HA-1H; induction of CTL recognition for epitope HA-1.,,MFSRKKRELMKTPSISKKNRAGSPSPQPSGELPRKDGADAVFPGPSLEPPAGSSGVKATGTLKRPTSLSRHASAAGFPLSGAASWTLGRSHRSPLTAASPGELPTEGAGPDVVEDISHLLADVARFAEGLEKLKECVLRDDLLEARRPRAHECLGEALRVMHQIISKYPLLNTVETLTAAGTLIAKVKAFHYESNNDLEKQEFEKALETIAVAFSSTVSEFLMGEVDSSTLLAVPPGDSSQSMESLYGPGSEGTPPSLEDCDAGCLPAEEVDVLLQRCEGGVDAALLYAKNMAKYMKDLISYLEKRTTLEMEFAKGLQKIAHNCRQSVMQEPHMPLLSIYSLALEQDLEFGHSMVQAVGTLQTQTFMQPLTLRRLEHEKRRKEIKEAWHRAQRKLQEAESNLRKAKQGYVQRCEDHDKARFLVAKAEEEQAGSAPGAGSTATKTLDKRRRLEEEAKNKAEEAMATYRTCVADAKTQKQELEDTKVTALRQIQEVIRQSDQTIKSATISYYQMMHMQTAPLPVHFQMLCESSKLYDPGQQYASHVRQLQRDQEPDVHYDFEPHVSANAWSPVMRARKSSFNVSDVARPEAAGSPPEEGGCTEGTPAKDHRAGRGHQVHKSWPLSISDSDSGLDPGPGAGDFKKFERTSSSGTMSSTEELVDPDGGAGASAFEQADLNGMTPELPVAVPSGPFRHEGLSKAARTHRLRKLRTPAKCRECNSYVYFQGAECEECCLACHKKCLETLAIQCGHKKLQGRLQLFGQDFSHAARSAPDGVPFIVKKCVCEIERRALRTKGIYRVNGVKTRVEKLCQAFENGKELVELSQASPHDISNVLKLYLRQLPEPLISFRLYHELVGLAKDSLKAEAEAKAASRGRQDGSESEAVAVALAGRLRELLRDLPPENRASLQYLLRHLRRIVEVEQDNKMTPGNLGIVFGPTLLRPRPTEATVSLSSLVDYPHQARVIETLIVHYGLVFEEEPEETPGGQDESSNQRAEVVVQVPYLEAGEAVVYPLQEAAADGCRESR,Rho GTPase-activating protein 45 [Cleaved into: Minor histocompatibility antigen HA-1,"Contains a GTPase activator for the Rho-type GTPases (RhoGAP) domain that would be able to negatively regulate the actin cytoskeleton as well as cell spreading. However, also contains N-terminally a BAR-domin which is able to play an autoinhibitory effect on this RhoGAP activity.Precursor of the histocompatibility antigen HA-1. More generally, minor histocompatibility antigens (mHags) refer to immunogenic peptide which, when complexed with MHC, can generate an immune response after recognition by specific T-cells. The peptides are derived from polymorphic intracellular proteins, which are cleaved by normal pathways of antigen processing. The binding of these peptides to MHC class I or class II molecules and its expression on the cell surface can stimulate T-cell responses and thereby trigger graft rejection or graft-versus-host disease (GVHD) after hematopoietic stem cell transplantation from HLA-identical sibling donor. GVHD is a frequent complication after bone marrow transplantation (BMT), due to mismatch of minor histocompatibility antigen in HLA-matched sibling marrow transplants. Specifically, mismatching for mHag HA-1 which is recognized as immunodominant, is shown to be associated with the development of severe GVHD after HLA-identical BMT. HA-1 is presented to the cell surface by MHC class I HLA-A*0201, but also by other HLA-A alleles. This complex specifically elicits donor-cytotoxic T-lymphocyte (CTL) reactivity against hematologic malignancies after treatment by HLA-identical allogenic BMT. It induces cell recognition and lysis by CTL.",The mutation in the HA-1 protein causes a functional change in the protein. The HA-1-negative allelic counterpart encoded by KIAA0223 had one amino acid difference from HA-1.,In allele HA-1H; induction of CTL recognition for epitope HA-1. The mutation in the HA-1 protein causes a functional change in the protein. The HA-1-negative allelic counterpart encoded by KIAA0223 had one amino acid difference from HA-1.
193,193,165733,O14746-A716T,MPRAPRCRAVRSLLRSHYREVLPLATFVRRLGPQGWRLVQRGDPAAFRALVAQCLVCVPWDARPPPAAPSFRQVSCLKELVARVLQRLCERGAKNVLAFGFALLDGARGGPPEAFTTSVRSYLPNTVTDALRGSGAWGLLLRRVGDDVLVHLLARCALFVLVAPSCAYQVCGPPLYQLGAATQARPPPHASGPRRRLGCERAWNHSVREAGVPLGLPAPGARRRGGSASRSLPLPKRPRRGAAPEPERTPVGQGSWAHPGRTRGPSDRGFCVVSPARPAEEATSLEGALSGTRHSHPSVGRQHHAGPPSTSRPPRPWDTPCPPVYAETKHFLYSSGDKEQLRPSFLLSSLRPSLTGARRLVETIFLGSRPWMPGTPRRLPRLPQRYWQMRPLFLELLGNHAQCPYGVLLKTHCPLRAAVTPAAGVCAREKPQGSVAAPEEEDTDPRRLVQLLRQHSSPWQVYGFVRACLRRLVPPGLWGSRHNERRFLRNTKKFISLGKHAKLSLQELTWKMSVRDCAWLRRSPGVGCVPAAEHRLREEILAKFLHWLMSVYVVELLRSFFYVTETTFQKNRLFFYRKSVWSKLQSIGIRQHLKRVQLRELSEAEVRQHREARPALLTSRLRFIPKPDGLRPIVNMDYVVGARTFRREKRAERLTSRVKALFSVLNYERARRPGLLGASVLGLDDIHRAWRTFVLRVRAQDPPPELYFVKVDVTGTYDTIPQDRLTEVIASIIKPQNTYCVRRYAVVQKAAHGHVRKAFKSHVSTLTDLQPYMRQFVAHLQETSPLRDAVVIEQSSSLNEASSGLFDVFLRFMCHHAVRIRGKSYVQCQGIPQGSILSTLLCSLCYGDMENKLFAGIRRDGLLLRLVDDFLLVTPHLTHAKTFLRTLVRGVPEYGCVVNLRKTVVNFPVEDEALGGTAFVQMPAHGLFPWCGLLLDTRTLEVQSDYSSYARTSIRASLTFNRGFKAGRNMRRKLFGVLRLKCHSLFLDLQVNSLQTVCTNIYKILLLQAYRFHACVLQLPFHQQ,In PFBMFT1; the mutant protein is demonstrated to cause severely compromised telomerase activity.,,MPRAPRCRAVRSLLRSHYREVLPLATFVRRLGPQGWRLVQRGDPAAFRALVAQCLVCVPWDARPPPAAPSFRQVSCLKELVARVLQRLCERGAKNVLAFGFALLDGARGGPPEAFTTSVRSYLPNTVTDALRGSGAWGLLLRRVGDDVLVHLLARCALFVLVAPSCAYQVCGPPLYQLGAATQARPPPHASGPRRRLGCERAWNHSVREAGVPLGLPAPGARRRGGSASRSLPLPKRPRRGAAPEPERTPVGQGSWAHPGRTRGPSDRGFCVVSPARPAEEATSLEGALSGTRHSHPSVGRQHHAGPPSTSRPPRPWDTPCPPVYAETKHFLYSSGDKEQLRPSFLLSSLRPSLTGARRLVETIFLGSRPWMPGTPRRLPRLPQRYWQMRPLFLELLGNHAQCPYGVLLKTHCPLRAAVTPAAGVCAREKPQGSVAAPEEEDTDPRRLVQLLRQHSSPWQVYGFVRACLRRLVPPGLWGSRHNERRFLRNTKKFISLGKHAKLSLQELTWKMSVRDCAWLRRSPGVGCVPAAEHRLREEILAKFLHWLMSVYVVELLRSFFYVTETTFQKNRLFFYRKSVWSKLQSIGIRQHLKRVQLRELSEAEVRQHREARPALLTSRLRFIPKPDGLRPIVNMDYVVGARTFRREKRAERLTSRVKALFSVLNYERARRPGLLGASVLGLDDIHRAWRTFVLRVRAQDPPPELYFVKVDVTGAYDTIPQDRLTEVIASIIKPQNTYCVRRYAVVQKAAHGHVRKAFKSHVSTLTDLQPYMRQFVAHLQETSPLRDAVVIEQSSSLNEASSGLFDVFLRFMCHHAVRIRGKSYVQCQGIPQGSILSTLLCSLCYGDMENKLFAGIRRDGLLLRLVDDFLLVTPHLTHAKTFLRTLVRGVPEYGCVVNLRKTVVNFPVEDEALGGTAFVQMPAHGLFPWCGLLLDTRTLEVQSDYSSYARTSIRASLTFNRGFKAGRNMRRKLFGVLRLKCHSLFLDLQVNSLQTVCTNIYKILLLQAYRFHACVLQLPFHQQ,Telomerase reverse transcriptase,"Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. Active in progenitor and cancer cells. Inactive, or very low activity, in normal somatic cells. Catalytic component of the teleromerase holoenzyme complex whose main activity is the elongation of telomeres by acting as a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme. Catalyzes the RNA-dependent extension of 3'-chromosomal termini with the 6-nucleotide telomeric repeat unit, 5'-TTAGGG-3'. The catalytic cycle involves primer binding, primer extension and release of product once the template boundary has been reached or nascent product translocation followed by further extension. More active on substrates containing 2 or 3 telomeric repeats. Telomerase activity is regulated by a number of factors including telomerase complex-associated proteins, chaperones and polypeptide modifiers. Modulates Wnt signaling. Plays important roles in aging and antiapoptosis.",,In PFBMFT1; the mutant protein is demonstrated to cause severely compromised telomerase activity.
194,194,166539,Q9H5P4-R66L,MAQGFAVGFDPLGLGDLSSGSLSSLSSRGHLGSDSGSTATRYLLRKQQRLLNGPPRGIRASSPMGLVILINSPIEANSDESDIIHSVRVEKSPAGRLGFSVRGGSEHGLGIFVSKVEEGSSAERAGLCVGDKITEVNGLSLESTTMGSAVKVLTSSSRLHMMVRRMGRVPGIKFSKEKTTWVDVVNRRLVVEKCGSTPSDTSSEDGVRRIVHLYTTSDDFCLGFNIRGGKEFGLGIYVSKVDHGGLAEENGIKVGDQVLAANGVRFDDISHSQAVEVLKGQTHIMLTIKETGRYPAYKEMVSEYCWLDRLSNGVLQQLSPASESSSSVSSCASSAPYSSGSLPSDRMDICLGQEEPGSRGPGWGRADTAMQTEPDAGGRVETWCSVRPTVILRDTAIRSDGPHPGRRLDSALSESPKTALLLALSRPRPPITRSQSYLTLWEEKQQRKKEKSGSPGEKGALQRSKTLMNLFFKGGRQGRLARDGRREAWTLDSGSLAKTYPRLDIEKAGGVGPVQKFVTWRLRRDQERGRALLSARSGSPSSQLPNVDEQVQAWESRRPLIQDLAQRLLTDDEVLAVTRHCSRYVHEGGIEDLVRPLLAILDRPEKLLLLQDIRSVVAPTDLGRFDSMVMLVELEAFEALKSRAVRPPALRPARQDTPPKRHLITPVPDSRGGFYLLPVNGFPEEEDNGELRERLGALKVSPSASAPRHPHKGIPPLQDVPVDAFTPLRIACTPPPQLPPVAPRPLRPNWLLTEPLSREHPPQSQIRGRAQSRSRSRSRSRSRSSRGQGKSPGRRSPSPVPTPAPSMTNGRYHKPRKARPPLPRPLDGEAAKVGAKQGPSESGTEGTAKEAAMKNPSGELKTVTLSKMKQSLGISISGGIESKVQPMVKIEKIFPGGAAFLSGALQAGFELVAVDGENLEQVTHQRAVDTIRRAYRNKAREPMELVVRVPGPSPRPSPSDSSALTDGGLPADHLPAHQPLDAAPVPAHWLPEPPTNPQTPPTDARLLQPTPSPAPSPALQTPDS,In DFNB57; unknown pathological significance.,,MAQGFAVGFDPLGLGDLSSGSLSSLSSRGHLGSDSGSTATRYLLRKQQRLLNGPPRGIRASSPMGRVILINSPIEANSDESDIIHSVRVEKSPAGRLGFSVRGGSEHGLGIFVSKVEEGSSAERAGLCVGDKITEVNGLSLESTTMGSAVKVLTSSSRLHMMVRRMGRVPGIKFSKEKTTWVDVVNRRLVVEKCGSTPSDTSSEDGVRRIVHLYTTSDDFCLGFNIRGGKEFGLGIYVSKVDHGGLAEENGIKVGDQVLAANGVRFDDISHSQAVEVLKGQTHIMLTIKETGRYPAYKEMVSEYCWLDRLSNGVLQQLSPASESSSSVSSCASSAPYSSGSLPSDRMDICLGQEEPGSRGPGWGRADTAMQTEPDAGGRVETWCSVRPTVILRDTAIRSDGPHPGRRLDSALSESPKTALLLALSRPRPPITRSQSYLTLWEEKQQRKKEKSGSPGEKGALQRSKTLMNLFFKGGRQGRLARDGRREAWTLDSGSLAKTYPRLDIEKAGGVGPVQKFVTWRLRRDQERGRALLSARSGSPSSQLPNVDEQVQAWESRRPLIQDLAQRLLTDDEVLAVTRHCSRYVHEGGIEDLVRPLLAILDRPEKLLLLQDIRSVVAPTDLGRFDSMVMLVELEAFEALKSRAVRPPALRPARQDTPPKRHLITPVPDSRGGFYLLPVNGFPEEEDNGELRERLGALKVSPSASAPRHPHKGIPPLQDVPVDAFTPLRIACTPPPQLPPVAPRPLRPNWLLTEPLSREHPPQSQIRGRAQSRSRSRSRSRSRSSRGQGKSPGRRSPSPVPTPAPSMTNGRYHKPRKARPPLPRPLDGEAAKVGAKQGPSESGTEGTAKEAAMKNPSGELKTVTLSKMKQSLGISISGGIESKVQPMVKIEKIFPGGAAFLSGALQAGFELVAVDGENLEQVTHQRAVDTIRRAYRNKAREPMELVVRVPGPSPRPSPSDSSALTDGGLPADHLPAHQPLDAAPVPAHWLPEPPTNPQTPPTDARLLQPTPSPAPSPALQTPDS,PDZ domain-containing protein 7,"In cochlear developing hair cells, essential in organizing the USH2 complex at stereocilia ankle links. Blocks inhibition of adenylate cyclase activity mediated by ADGRV1.",A novel homozygous missense mutation (p. ) in Chinese families with ARNSHL has been identified. This mutation is the first report to identify PDZD7 as an ARNSHL-associated gene in the Chinese population.,In DFNB57; unknown pathological significance. A novel homozygous missense mutation (p. ) in Chinese families with ARNSHL has been identified. This mutation is the first report to identify PDZD7 as an ARNSHL-associated gene in the Chinese population.
195,195,167943,Q94AN2-G247E,MRGPLGAVIGRYTSSDGSAPNDGIIKHNRKCRDITFLIIFIAFWVSMIVNSSFGFNQGNPLRLTYGLDYEGNVCGSKHRHRDLTQLELRYWLNPNQVYESGLKDGELKLANARTICLLDCPAPSDDTLNWVCDYPDGEIRLKMNDWIDRNYDYFEFLTPEMRNSSLQLQGPCYPVIFPSVNVYWSCQYIARASNSSLRHWQQMGGVNIQEDMIIDKSIRRSMNSRASVLKRYVADIGKSWPVLIVCEGLVPLFLSIIWLLLIRHFVAAMPWITVVLFNMLLISVTVFYYLKAGWIGNDAVTPIIGEHDPYFHVYGRELTHVRGVAILMTFISVVAILTSIAIIRRILMATSVLKVAAKVIGEVQALIIFPAIPFAMLAIFYMFWISAALHLFSSGQVVQNNCNNTNCCAYDLVLKKVNCDRCCGYSIHYTPHITIAIFFHLFGCYWATQFFIASSATVIAGSVASYYWAQGEASPEIPFLPVFASMKRLARYNLGSVALGSLIVSFVESVRFILEAIRRKTKVSGTIPDHWFWRMAHYTSRGCLKSVEWTIKSVNRNAYIMIAITGKSFCKSSAIATELIISNILRIGKVNVIGDVILFLGKLCVSLFSALFGFLMLDSHRYRASHNKVSSPLLPVLACWALGYIVATLFFAVVEMSIDTIILSFCQDSEENQGNAQHAPPLLLETLDSNQEEEVQSLTH,"In cher1-5 and sic1; impaired secondary plasmodesmata (PD) formation (e.g. blocked or shrunken) and development leading to starch and soluble sugars excess accumulation, abnormal cell-to-cell communication, and stunted growth. Altered PD localization of the luteoviral movement protein MP17. Abnormal subcellular localization. Increased leaf concentrations of sodium (Na), lithium (Li), boron (B) ions, and decreased leaf concentrations of phosphorus (P), potassium (K), calcium (Ca), cobalt (Co), nickel (Ni), and copper (Cu), manganese (Mn), iron (Fe), zinc (Zn) and molybdenum (Mo) ions.",,MRGPLGAVIGRYTSSDGSAPNDGIIKHNRKCRDITFLIIFIAFWVSMIVNSSFGFNQGNPLRLTYGLDYEGNVCGSKHRHRDLTQLELRYWLNPNQVYESGLKDGELKLANARTICLLDCPAPSDDTLNWVCDYPDGEIRLKMNDWIDRNYDYFEFLTPEMRNSSLQLQGPCYPVIFPSVNVYWSCQYIARASNSSLRHWQQMGGVNIQEDMIIDKSIRRSMNSRASVLKRYVADIGKSWPVLIVCGGLVPLFLSIIWLLLIRHFVAAMPWITVVLFNMLLISVTVFYYLKAGWIGNDAVTPIIGEHDPYFHVYGRELTHVRGVAILMTFISVVAILTSIAIIRRILMATSVLKVAAKVIGEVQALIIFPAIPFAMLAIFYMFWISAALHLFSSGQVVQNNCNNTNCCAYDLVLKKVNCDRCCGYSIHYTPHITIAIFFHLFGCYWATQFFIASSATVIAGSVASYYWAQGEASPEIPFLPVFASMKRLARYNLGSVALGSLIVSFVESVRFILEAIRRKTKVSGTIPDHWFWRMAHYTSRGCLKSVEWTIKSVNRNAYIMIAITGKSFCKSSAIATELIISNILRIGKVNVIGDVILFLGKLCVSLFSALFGFLMLDSHRYRASHNKVSSPLLPVLACWALGYIVATLFFAVVEMSIDTIILSFCQDSEENQGNAQHAPPLLLETLDSNQEEEVQSLTH,Choline transporter protein 1,"Regulator of vesicle trafficking, including endocytosis. Necessary for secondary plasmodesmata (PD) formation and development via the secretory trafficking regulation of proteins required for PD development, thus influencing intercellular communication. Modulates ion homeostasis, especially in roots, by monitoring the transport and subsequent subcellular localization of some ion transporters. Choline transporter involved in the regulation of choline metabolite homeostasis during root and phloem development. Modulates phloem morphogenesis and conductivity. Required for procambium maintenance and sieve plate development (e.g. sieve plate and sieve pore elaboration) to mediate long-distance cell-to-cell communication via symplastic transport through the phloem. Involved in the regulation of intracellular trafficking of PIN-type auxin transporters (e.g. PIN1 and PIN3), a process controlling seedling growth, apical dominance, cell elongation and apical hook development. Modulates also membrane lipids (e.g. phospholipids and sphingolipids) homeostasis.(Microbial infection) Required for PD localization of MP17, the luteoviral movement protein.","Mutation in CHER1 resulted in a starch excess phenotype and stunted growth. Ultrastructure analysis of shoot apical meristems, developing and fully developed leaves showed reduced PD numbers and the absence of complex PD in fully developed leaves. This indicates that cher1 mutants are impaired in PD formation and development. Global lipid profiling revealed only slight modifications in the overall lipid composition, however, Thus, cher1 is devoid of complex PD in developed leaves and provides insights into the formation of complex PD at the molecular level.","In cher1-5 and sic1; impaired secondary plasmodesmata (PD) formation (e.g. blocked or shrunken) and development leading to starch and soluble sugars excess accumulation, abnormal cell-to-cell communication, and stunted growth. Altered PD localization of the luteoviral movement protein MP17. Abnormal subcellular localization. Increased leaf concentrations of sodium (Na), lithium (Li), boron (B) ions, and decreased leaf concentrations of phosphorus (P), potassium (K), calcium (Ca), cobalt (Co), nickel (Ni), and copper (Cu), manganese (Mn), iron (Fe), zinc (Zn) and molybdenum (Mo) ions. Mutation in CHER1 resulted in a starch excess phenotype and stunted growth. Ultrastructure analysis of shoot apical meristems, developing and fully developed leaves showed reduced PD numbers and the absence of complex PD in fully developed leaves. This indicates that cher1 mutants are impaired in PD formation and development. Global lipid profiling revealed only slight modifications in the overall lipid composition, however, Thus, cher1 is devoid of complex PD in developed leaves and provides insights into the formation of complex PD at the molecular level."
196,196,171074,Q9XWP6-A665T,MSSDTGSEYLDEEIRGDELGPSIDDNALAAAASAARLPFDRPTDHELAFFPELWEHKTAVEVFLLLRNSTLATWQYNPLKECTALDVRNNVFPPFNSDLDLIQNIVHYLSRHGLINFGRYVRSTKISRFLVRDRRSVIVIGAGAAGISAATQLESFGFDVIVLEARNCIGGRIHSFKSKSGEIMETGGDTLRKIEDSPMATLLHQVNFEEHGVFDFTSVFVEGRPLNEEKIHLFLDHYKSAHGALNYQAHQCEHRDDQGSFISRQQAYENLLSMCERGTLIKYYNFCKSLETVARAREHHFNQMKQLRMTALMAENQLKKMEEEGNLEQDPVLRRSLKRDIATSLEKFEEVADAFETADNHWQRLNEHPQAKQYMHPGSEFATFNFMLGFEEYLVGAQLEKVQFSCDSMQNKENGVAARLTEGIAELLTQLSEKRKLDIRLKHRVLDIDYSGFEHVLLKVQRENGDIEEMKAAFVVSTLPIGVLKKTIIADERAPTFTPSLPDKKVEAIRNIGCGSVNKCILEFDRVFWTANGGRNQFVTVSPNIKTRGSMNIWSSVPGSKVLCTYIVGEEAMLELPDDVIIQNAMINLQKAFGNNCPRAPISAHITRWHDDELAFGSGAFMSLRTETTSFDDVMEPLKTSDGMSRVYFAGEHTCSSYTSTIQGTWMSGARAAADISNDHIGIGFVDISGTRGQRGDEEEELLIEVDIDGKIPEKDENEAVADIPNAPNAPNAQKPEEIPKIAEEIELVAEAEKAEKAEVQLEPLVPTVE,In ar197; results in suppression of Sel-12 mutant phenotypes.,,MSSDTGSEYLDEEIRGDELGPSIDDNALAAAASAARLPFDRPTDHELAFFPELWEHKTAVEVFLLLRNSTLATWQYNPLKECTALDVRNNVFPPFNSDLDLIQNIVHYLSRHGLINFGRYVRSTKISRFLVRDRRSVIVIGAGAAGISAATQLESFGFDVIVLEARNCIGGRIHSFKSKSGEIMETGGDTLRKIEDSPMATLLHQVNFEEHGVFDFTSVFVEGRPLNEEKIHLFLDHYKSAHGALNYQAHQCEHRDDQGSFISRQQAYENLLSMCERGTLIKYYNFCKSLETVARAREHHFNQMKQLRMTALMAENQLKKMEEEGNLEQDPVLRRSLKRDIATSLEKFEEVADAFETADNHWQRLNEHPQAKQYMHPGSEFATFNFMLGFEEYLVGAQLEKVQFSCDSMQNKENGVAARLTEGIAELLTQLSEKRKLDIRLKHRVLDIDYSGFEHVLLKVQRENGDIEEMKAAFVVSTLPIGVLKKTIIADERAPTFTPSLPDKKVEAIRNIGCGSVNKCILEFDRVFWTANGGRNQFVTVSPNIKTRGSMNIWSSVPGSKVLCTYIVGEEAMLELPDDVIIQNAMINLQKAFGNNCPRAPISAHITRWHDDELAFGSGAFMSLRTETTSFDDVMEPLKTSDGMSRVYFAGEHTCSSYTSTIQGAWMSGARAAADISNDHIGIGFVDISGTRGQRGDEEEELLIEVDIDGKIPEKDENEAVADIPNAPNAPNAQKPEEIPKIAEEIELVAEAEKAEKAEVQLEPLVPTVE,Lysine-specific histone demethylase 1,"Histone demethylase that specifically demethylates 'Lys-4' of histone H3, a specific tag for epigenetic transcriptional activation, thereby acting as a corepressor. 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. May be involved in H3 demethylation in mitotic cells including gut and embryonic cells. Participates in the transcriptional repression of the presenilin protein hop-1. May act via the formation of a multiprotein complex that remodel or modify the chromatin. Together with met-2, set-17 and set-26, required for transgenerational fertility. Plays a role in developmental growth and lifespan regulation in response to ultraviolet-induced damage.",,In ar197; results in suppression of Sel-12 mutant phenotypes.
197,197,172591,P16522-A404T,MNDDSQDKIIHDIRIQLRKAATELSRWKLYGSSKWAAEALAGLAEAIDVDQTHSLADESPLRNKQGVPKQMFEIPQNGFGLSETEYDLYLLGSTLFDAKEFDRCVFFLKDVTNPYLKFLKLYSKFLSWDKKSQESMENILTTGKFTDEMYRANKDGDGSGNEDINQSGHQRANLKMVSNEHESQSNISSILKEINTFLESYEIKIDDDEADLGLALLYYLRGVILKQEKNISKAMSSFLKSLSCYSFNWSCWLELMDCLQKVDDALLLNNYLYQNFQFKFSENLGSQRTIEFNIMIKFFKLKVFEELNGQLEDYFEDLEFLLQVFPNFTFLKAYNATISYNNLDYVTAESRFDDIVKQDPYRLNDLETYSNILYVMQKNSKLAYLAQFVSQIDRFRPETCCIITNYYSARQEHEKSIMYFRRALTLDKKTTNAWTLMGHEFVELSNSHAAIECYRRAVDICPRDFKAWFGLGQAYALLDMHLYSLYYFQKACTLKPWDRRIWQVLGECYSKTGNKVEAIKCYKRSIKASQTVDQNTSIYYRLAQLYEELEDLQECKKFMMKCVDVEELLEGIVTDETVKARLWLAIFEIKAGNYQLAYDYAMGVSSGTSQEIEEARMLARECRRHM,In CDC23-39; G2/M cell cycle arrest at 37 degrees Celsius.,,MNDDSQDKIIHDIRIQLRKAATELSRWKLYGSSKWAAEALAGLAEAIDVDQTHSLADESPLRNKQGVPKQMFEIPQNGFGLSETEYDLYLLGSTLFDAKEFDRCVFFLKDVTNPYLKFLKLYSKFLSWDKKSQESMENILTTGKFTDEMYRANKDGDGSGNEDINQSGHQRANLKMVSNEHESQSNISSILKEINTFLESYEIKIDDDEADLGLALLYYLRGVILKQEKNISKAMSSFLKSLSCYSFNWSCWLELMDCLQKVDDALLLNNYLYQNFQFKFSENLGSQRTIEFNIMIKFFKLKVFEELNGQLEDYFEDLEFLLQVFPNFTFLKAYNATISYNNLDYVTAESRFDDIVKQDPYRLNDLETYSNILYVMQKNSKLAYLAQFVSQIDRFRPETCCIIANYYSARQEHEKSIMYFRRALTLDKKTTNAWTLMGHEFVELSNSHAAIECYRRAVDICPRDFKAWFGLGQAYALLDMHLYSLYYFQKACTLKPWDRRIWQVLGECYSKTGNKVEAIKCYKRSIKASQTVDQNTSIYYRLAQLYEELEDLQECKKFMMKCVDVEELLEGIVTDETVKARLWLAIFEIKAGNYQLAYDYAMGVSSGTSQEIEEARMLARECRRHM,Anaphase-promoting complex subunit CDC23,"Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. In early mitosis, the APC/C is activated by CDC20 and targets securin PDS1, the B-type cyclin CLB5, and other anaphase inhibitory proteins for proteolysis, thereby triggering the separation of sister chromatids at the metaphase-to-anaphase transition. In late mitosis and in G1, degradation of CLB5 allows activation of the APC/C by CDH1, which is needed to destroy CDC20 and the B-type cyclin CLB2 to allow exit from mitosis and creating the low CDK state necessary for cytokinesis and for reforming prereplicative complexes in G1 prior to another round of replication.",The mutation in the CDC23 gene causes a single amino acid change in the protein. This mutation is found within a mutable domain of CDC23 and may affect its function or stability.,In CDC23-39; G2/M cell cycle arrest at 37 degrees Celsius. The mutation in the CDC23 gene causes a single amino acid change in the protein. This mutation is found within a mutable domain of CDC23 and may affect its function or stability.
198,198,173176,O14746-V791I,MPRAPRCRAVRSLLRSHYREVLPLATFVRRLGPQGWRLVQRGDPAAFRALVAQCLVCVPWDARPPPAAPSFRQVSCLKELVARVLQRLCERGAKNVLAFGFALLDGARGGPPEAFTTSVRSYLPNTVTDALRGSGAWGLLLRRVGDDVLVHLLARCALFVLVAPSCAYQVCGPPLYQLGAATQARPPPHASGPRRRLGCERAWNHSVREAGVPLGLPAPGARRRGGSASRSLPLPKRPRRGAAPEPERTPVGQGSWAHPGRTRGPSDRGFCVVSPARPAEEATSLEGALSGTRHSHPSVGRQHHAGPPSTSRPPRPWDTPCPPVYAETKHFLYSSGDKEQLRPSFLLSSLRPSLTGARRLVETIFLGSRPWMPGTPRRLPRLPQRYWQMRPLFLELLGNHAQCPYGVLLKTHCPLRAAVTPAAGVCAREKPQGSVAAPEEEDTDPRRLVQLLRQHSSPWQVYGFVRACLRRLVPPGLWGSRHNERRFLRNTKKFISLGKHAKLSLQELTWKMSVRDCAWLRRSPGVGCVPAAEHRLREEILAKFLHWLMSVYVVELLRSFFYVTETTFQKNRLFFYRKSVWSKLQSIGIRQHLKRVQLRELSEAEVRQHREARPALLTSRLRFIPKPDGLRPIVNMDYVVGARTFRREKRAERLTSRVKALFSVLNYERARRPGLLGASVLGLDDIHRAWRTFVLRVRAQDPPPELYFVKVDVTGAYDTIPQDRLTEVIASIIKPQNTYCVRRYAVVQKAAHGHVRKAFKSHVSTLTDLQPYMRQFVAHLQETSPLRDAVIIEQSSSLNEASSGLFDVFLRFMCHHAVRIRGKSYVQCQGIPQGSILSTLLCSLCYGDMENKLFAGIRRDGLLLRLVDDFLLVTPHLTHAKTFLRTLVRGVPEYGCVVNLRKTVVNFPVEDEALGGTAFVQMPAHGLFPWCGLLLDTRTLEVQSDYSSYARTSIRASLTFNRGFKAGRNMRRKLFGVLRLKCHSLFLDLQVNSLQTVCTNIYKILLLQAYRFHACVLQLPFHQQ,In PFBMFT1; associated with Met-867 in cis on the same allele; the double mutant shows severe defects in telomere repeat addition processivity.,,MPRAPRCRAVRSLLRSHYREVLPLATFVRRLGPQGWRLVQRGDPAAFRALVAQCLVCVPWDARPPPAAPSFRQVSCLKELVARVLQRLCERGAKNVLAFGFALLDGARGGPPEAFTTSVRSYLPNTVTDALRGSGAWGLLLRRVGDDVLVHLLARCALFVLVAPSCAYQVCGPPLYQLGAATQARPPPHASGPRRRLGCERAWNHSVREAGVPLGLPAPGARRRGGSASRSLPLPKRPRRGAAPEPERTPVGQGSWAHPGRTRGPSDRGFCVVSPARPAEEATSLEGALSGTRHSHPSVGRQHHAGPPSTSRPPRPWDTPCPPVYAETKHFLYSSGDKEQLRPSFLLSSLRPSLTGARRLVETIFLGSRPWMPGTPRRLPRLPQRYWQMRPLFLELLGNHAQCPYGVLLKTHCPLRAAVTPAAGVCAREKPQGSVAAPEEEDTDPRRLVQLLRQHSSPWQVYGFVRACLRRLVPPGLWGSRHNERRFLRNTKKFISLGKHAKLSLQELTWKMSVRDCAWLRRSPGVGCVPAAEHRLREEILAKFLHWLMSVYVVELLRSFFYVTETTFQKNRLFFYRKSVWSKLQSIGIRQHLKRVQLRELSEAEVRQHREARPALLTSRLRFIPKPDGLRPIVNMDYVVGARTFRREKRAERLTSRVKALFSVLNYERARRPGLLGASVLGLDDIHRAWRTFVLRVRAQDPPPELYFVKVDVTGAYDTIPQDRLTEVIASIIKPQNTYCVRRYAVVQKAAHGHVRKAFKSHVSTLTDLQPYMRQFVAHLQETSPLRDAVVIEQSSSLNEASSGLFDVFLRFMCHHAVRIRGKSYVQCQGIPQGSILSTLLCSLCYGDMENKLFAGIRRDGLLLRLVDDFLLVTPHLTHAKTFLRTLVRGVPEYGCVVNLRKTVVNFPVEDEALGGTAFVQMPAHGLFPWCGLLLDTRTLEVQSDYSSYARTSIRASLTFNRGFKAGRNMRRKLFGVLRLKCHSLFLDLQVNSLQTVCTNIYKILLLQAYRFHACVLQLPFHQQ,Telomerase reverse transcriptase,"Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. Active in progenitor and cancer cells. Inactive, or very low activity, in normal somatic cells. Catalytic component of the teleromerase holoenzyme complex whose main activity is the elongation of telomeres by acting as a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme. Catalyzes the RNA-dependent extension of 3'-chromosomal termini with the 6-nucleotide telomeric repeat unit, 5'-TTAGGG-3'. The catalytic cycle involves primer binding, primer extension and release of product once the template boundary has been reached or nascent product translocation followed by further extension. More active on substrates containing 2 or 3 telomeric repeats. Telomerase activity is regulated by a number of factors including telomerase complex-associated proteins, chaperones and polypeptide modifiers. Modulates Wnt signaling. Plays important roles in aging and antiapoptosis.","Functional studies indicated that, although the double mutant did not dramatically affect first repeat addition, hTERT -showed severe defects in telomere repeat addition processivity in vitro.","In PFBMFT1; associated with Met-867 in cis on the same allele; the double mutant shows severe defects in telomere repeat addition processivity. Functional studies indicated that, although the double mutant did not dramatically affect first repeat addition, hTERT -showed severe defects in telomere repeat addition processivity in vitro."
199,199,173213,P29496-K422A,MSFDRPEIYSAPVLQGESPNDDDNTEIIKSFKNFILEFRLDSQFIYRDQLRNNILVKNYSLTVNMEHLIGYNEDIYKKLSDEPSDIIPLFETAITQVAKRISILSRAQSANNNDKDPENTSMDTDSLLLNSLPTFQLILNSNANQIPLRDLDSEHVSKIVRLSGIIISTSVLSSRATYLSIMCRNCRHTTSITINNFNSITGNTVSLPRSCLSTIESESSMANESNIGDESTKKNCGPDPYIIIHESSKFIDQQFLKLQEIPELVPVGEMPRNLTMTCDRYLTNKVIPGTRVTIVGIYSIYNSKNGAGSGRSGGGNGGSGVAIRTPYIKILGIQSDVETSSIWNSVTMFTEEEEEEFLQLSRNPKLYEILTNSIAPSIFGNEDIKKAIVCLLMGGSKKILPDGMRLRGDINVLLLGDPGTAASQLLKFVEKVSPIAVYTSGKGSSAAGLTASVQRDPMTREFYLEGGAMVLADGGVVCIDEFDKMRDEDRVAIHEAMEQQTISIAKAGITTVLNSRTSVLAAANPIYGRYDDLKSPGDNIDFQTTILSRFDMIFIVKDDHNEERDISIANHVINIHTGNANAMQNQQEENGSEISIEKMKRYITYCRLKCAPRLSPQAAEKLSSNFVTIRKQLLINELESTERSSIPITIRQLEAIIRITESLAKLELSPIAQERHVDEAIRLFQASTMDAASQDPIGGLNQASGTSLSEIRRFEQELKRRLPIGWSTSYQTLRREFVDTHRFSQLALDKALYALEKHETIQLRHQGQNIYRSGV,Loss of MCM2-7 complex helicase activity.,,MSFDRPEIYSAPVLQGESPNDDDNTEIIKSFKNFILEFRLDSQFIYRDQLRNNILVKNYSLTVNMEHLIGYNEDIYKKLSDEPSDIIPLFETAITQVAKRISILSRAQSANNNDKDPENTSMDTDSLLLNSLPTFQLILNSNANQIPLRDLDSEHVSKIVRLSGIIISTSVLSSRATYLSIMCRNCRHTTSITINNFNSITGNTVSLPRSCLSTIESESSMANESNIGDESTKKNCGPDPYIIIHESSKFIDQQFLKLQEIPELVPVGEMPRNLTMTCDRYLTNKVIPGTRVTIVGIYSIYNSKNGAGSGRSGGGNGGSGVAIRTPYIKILGIQSDVETSSIWNSVTMFTEEEEEEFLQLSRNPKLYEILTNSIAPSIFGNEDIKKAIVCLLMGGSKKILPDGMRLRGDINVLLLGDPGTAKSQLLKFVEKVSPIAVYTSGKGSSAAGLTASVQRDPMTREFYLEGGAMVLADGGVVCIDEFDKMRDEDRVAIHEAMEQQTISIAKAGITTVLNSRTSVLAAANPIYGRYDDLKSPGDNIDFQTTILSRFDMIFIVKDDHNEERDISIANHVINIHTGNANAMQNQQEENGSEISIEKMKRYITYCRLKCAPRLSPQAAEKLSSNFVTIRKQLLINELESTERSSIPITIRQLEAIIRITESLAKLELSPIAQERHVDEAIRLFQASTMDAASQDPIGGLNQASGTSLSEIRRFEQELKRRLPIGWSTSYQTLRREFVDTHRFSQLALDKALYALEKHETIQLRHQGQNIYRSGV,Minichromosome maintenance protein 5,"Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity; specifically the MCM2-MCM5 association is proposed to be reversible and to mediate a open ring conformation which may facilitate DNA loading. Once loaded onto DNA, double hexamers can slide on dsDNA in the absence of ATPase activity.",,Loss of MCM2-7 complex helicase activity.
200,200,173867,Q8IB06-C4A,MGSAYSRKNKVSTISLDEEEKKKEKKKKKKIYILNGASGSGKDTQCRLLEKKYNYKIICISKLLKEYKEEYNKENVLNEEENYFDEIEKCMIDGSLVNDQIVIEIFHKQLNKYINDDKYNGIIINGFPRNYEQALLIIQNNISITKFINIQVGKDTLWTRINNRIIDPITNISYNENIIQIIKKKREGQELSDKEQKQLIIDNHLYNNLSNDILERLTKRKDDEEQVFNKRFQLYIESEQKINSLFKNICKNVDGEKSINDIFDQICSIIDDNPN,Partial mislocalization to the cytoplasm with some localization to the cell membrane. Mislocalizes to the cytoplasm; when associated with A-2.,,MGSCYSRKNKVSTISLDEEEKKKEKKKKKKIYILNGASGSGKDTQCRLLEKKYNYKIICISKLLKEYKEEYNKENVLNEEENYFDEIEKCMIDGSLVNDQIVIEIFHKQLNKYINDDKYNGIIINGFPRNYEQALLIIQNNISITKFINIQVGKDTLWTRINNRIIDPITNISYNENIIQIIKKKREGQELSDKEQKQLIIDNHLYNNLSNDILERLTKRKDDEEQVFNKRFQLYIESEQKINSLFKNICKNVDGEKSINDIFDQICSIIDDNPN,Adenylate kinase 2,"Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Has very low activity with CTP, GTP, ITP and UTP and no activity with GMP, UMP or IMP in vitro.",,Partial mislocalization to the cytoplasm with some localization to the cell membrane. Mislocalizes to the cytoplasm; when associated with A-2.
201,201,174068,Q9JJS6-H237A,MEIIFGQNKKEQLEPVQAKVTGSIPAWLQGTLLRNGPGMHTVGESKYNHWFDGLALLHSFSIRDGEVFYRSKYLQSDTYIANIEANRIVVSEFGTMAYPDPCKNIFSKAFSYLSHTIPDFTDNCLINIMKCGEDFYATTETNYIRKIDPQTLETLEKVDYRKYVAVNLATSHPHYDEAGNVLNMGTSVVDKGRTKYVIFKIPATVPDSKKKGKSPVKHAEVFCSISSRSLLSPSYYASFGVTENYVVFLEQPFKLDILKMATAYMRGVSWASCMSFDREDKTYIHIIDQRTRKPVPTKFYTDPMVVFHHVNAYEEDGCVLFDVIAYEDSSLYQLFYLANLNKDFEEKSRLTSVPTLRRFAVPLHVDKDAEVGSNLVKVSSTTATALKEKDGHVYCQPEVLYEGLELPRINYAYNGKPYRYIFAAEVQWSPVPTKILKYDILTKSSLKWSEESCWPAEPLFVPTPGAKDEDDGVILSAIVSTDPQKLPFLLILDAKSFTELARASVDADMHLDLHGLFIPDADWNAVKQTPAETQEVENSDHPTDPTAPELSHSENDFTAGHGGSSL,"No effect on protein abundance. Loss of beta-carotene 15,15'-monooxygenase activity. Decreased iron binding.",,MEIIFGQNKKEQLEPVQAKVTGSIPAWLQGTLLRNGPGMHTVGESKYNHWFDGLALLHSFSIRDGEVFYRSKYLQSDTYIANIEANRIVVSEFGTMAYPDPCKNIFSKAFSYLSHTIPDFTDNCLINIMKCGEDFYATTETNYIRKIDPQTLETLEKVDYRKYVAVNLATSHPHYDEAGNVLNMGTSVVDKGRTKYVIFKIPATVPDSKKKGKSPVKHAEVFCSISSRSLLSPSYYHSFGVTENYVVFLEQPFKLDILKMATAYMRGVSWASCMSFDREDKTYIHIIDQRTRKPVPTKFYTDPMVVFHHVNAYEEDGCVLFDVIAYEDSSLYQLFYLANLNKDFEEKSRLTSVPTLRRFAVPLHVDKDAEVGSNLVKVSSTTATALKEKDGHVYCQPEVLYEGLELPRINYAYNGKPYRYIFAAEVQWSPVPTKILKYDILTKSSLKWSEESCWPAEPLFVPTPGAKDEDDGVILSAIVSTDPQKLPFLLILDAKSFTELARASVDADMHLDLHGLFIPDADWNAVKQTPAETQEVENSDHPTDPTAPELSHSENDFTAGHGGSSL,"Beta,beta-carotene 15,15'-dioxygenase",Symmetrically cleaves beta-carotene into two molecules of retinal using a dioxygenase mechanism.,"Mutation of H237 produced impaired although enzymatically active proteins, with a decrease in activity mostly due to changes in V(max).","No effect on protein abundance. Loss of beta-carotene 15,15'-monooxygenase activity. Decreased iron binding. Mutation of H237 produced impaired although enzymatically active proteins, with a decrease in activity mostly due to changes in V(max)."
202,202,174385,Q9AQS0-Y315F,MLSGILIAALLMTLWGGWQPDIAHASDEFDALRIKWATLLTGGPALDPADSDIAARTDKLAQDANDYWEDMDLSSSRTYIWYALRGNGTSDNVNAVYERLRTMALAATTVGSSLYGNADLKEDILDALDWLYVNSYNSTRSRSAYNWWHWQLGIPMSLNDIAVLLYDDISAARMATYMDTIDYFTPSIGLTGANRAWQAIVVGVRAVIVKDAVKLAAARNGLSGTGIFPYATGGDGFYADGSFVQHTTFAYTGGYGSSVLETTANLMYLLSGSTWSVSDPNQSNVWQWIYEAYRPLLYKGAMMDMVRGREISRSFAQDHAVGHGIVASIVRLAQFAPAPHAAAFKQIAKRVIQEDTFSSFYGDVSTDTIRLAKAIVDDPSIAPAAAPNLYKQYAAMDRAVLQRPGFALGLALYSTRISSYESINSENGRGWYTGAGATYLYNQDLAQYSEDYWPTVDAYRIPGTTVASGTPIASGTGTSSWTGGVSLAGQYGASGMDLSYGAYNLSARKSWFMFDDEIVALGSGISSTAGIPIETVVDNRKLNGAGDNAWTANGAALSTGLGVAQTLTGVNWVHLAGNTADGSDIGYYFPGGATLQTKREARTGTWKQINNRPATPSTAVTRNYETMWIDHGTNPSGASYGYVLLPNKTSAQVGAYAADPAIEIVVNTSGVQSVKEKTLGLVGANFWTDTTQTADLITSNKKASVMTREIADERLEASVSDPTQANNGTIAIELARSAEGYSADPGITVTQLAPTIKFTVNVNGAKGKSFHASFQLGEDTSGPVDPGEPELPSVIVDNADSAGVTRTGTWKTASTQTDRYGANYLHDDNAGKGTKSVTFTPNLPIAGSYEVYLMWPAHFNREDAVQVDVGHASGTTRTAVDQRSGGGVWHSIGTYEFLAGSGGSVTIRNDALGSPDGYVVADAVKFVAVG,Negligible change in catalytic activity.,,MLSGILIAALLMTLWGGWQPDIAHASDEFDALRIKWATLLTGGPALDPADSDIAARTDKLAQDANDYWEDMDLSSSRTYIWYALRGNGTSDNVNAVYERLRTMALAATTVGSSLYGNADLKEDILDALDWLYVNSYNSTRSRSAYNWWHWQLGIPMSLNDIAVLLYDDISAARMATYMDTIDYFTPSIGLTGANRAWQAIVVGVRAVIVKDAVKLAAARNGLSGTGIFPYATGGDGFYADGSFVQHTTFAYTGGYGSSVLETTANLMYLLSGSTWSVSDPNQSNVWQWIYEAYRPLLYKGAMMDMVRGREISRSYAQDHAVGHGIVASIVRLAQFAPAPHAAAFKQIAKRVIQEDTFSSFYGDVSTDTIRLAKAIVDDPSIAPAAAPNLYKQYAAMDRAVLQRPGFALGLALYSTRISSYESINSENGRGWYTGAGATYLYNQDLAQYSEDYWPTVDAYRIPGTTVASGTPIASGTGTSSWTGGVSLAGQYGASGMDLSYGAYNLSARKSWFMFDDEIVALGSGISSTAGIPIETVVDNRKLNGAGDNAWTANGAALSTGLGVAQTLTGVNWVHLAGNTADGSDIGYYFPGGATLQTKREARTGTWKQINNRPATPSTAVTRNYETMWIDHGTNPSGASYGYVLLPNKTSAQVGAYAADPAIEIVVNTSGVQSVKEKTLGLVGANFWTDTTQTADLITSNKKASVMTREIADERLEASVSDPTQANNGTIAIELARSAEGYSADPGITVTQLAPTIKFTVNVNGAKGKSFHASFQLGEDTSGPVDPGEPELPSVIVDNADSAGVTRTGTWKTASTQTDRYGANYLHDDNAGKGTKSVTFTPNLPIAGSYEVYLMWPAHFNREDAVQVDVGHASGTTRTAVDQRSGGGVWHSIGTYEFLAGSGGSVTIRNDALGSPDGYVVADAVKFVAVG,Xanthan lyase,"Plays a role in xanthan depolymerization pathway by cleaving the linkage between the terminal mannosyl and glucuronyl residues of the side chain of xanthan to liberate pyruvylated mannose. Is highly specific for pyruvylated side-chains of xanthan and is not effective with hyaluronate, chondroitin A, gellan, heparin or pectin.",The high affinity of pyruvated mannose is probably due to the formation of additional hydrogen bonds between the carboxyl group of pyruvated mannose and amino acid residues of Y315.,Negligible change in catalytic activity. The high affinity of pyruvated mannose is probably due to the formation of additional hydrogen bonds between the carboxyl group of pyruvated mannose and amino acid residues of Y315.
203,203,174703,P9WGK9-H305Y,MIFGSRRRIRGRRGRSGPMTRGLSALSRAVAVAWRRSLQLRVVALTLGLSLAVILALGFVLTSQVTNRVLDIKVRAAIDQIERARTTVSGIVNGEETRSLDSSLQLARNTLTSKTDPASGAGLAGAFDAVLMVPGDGPRAASTAGPVDQVPNALRGFVKAGQAAYQYATVQTEGFSGPALIIGTPTLSRVANLELYLIFPLASEQATITLVRGTMATGGLVLLVLLAGIALLVSRQVVVPVRSASRIAERFAEGHLSERMPVRGEDDMARLAVSFNDMAESLSRQIAQLEEFGNLQRRFTSDVSYELRTPLTTVRMAADLIYDHSADLDPTLRRSTELMVSELDRFETLLNDLLEISRHDAGVAELSVEAVDLRTTVNNALGNVGHLAEEAGIELLVDLPAEQVIAEVDARRVERILRNLIANAIDHAEHKPVRIRMAADEDTVAVTVRDYGVGLRPGEEKLVFSRFWRSDPSRVRRSGGTGLGLAISVEDARLHQGRLEAWGEPGEGACFRLTLPMVRGHKVTTSPLPMKPIPQPVLQPVAQPNPQPMPPEYKERQRPREHAEWSG,"Loss of autophosphorylation. Partially complements an M.smegmatis mtrB disruption, cells are still filamentous and bulged but the protein targets to septa.",,MIFGSRRRIRGRRGRSGPMTRGLSALSRAVAVAWRRSLQLRVVALTLGLSLAVILALGFVLTSQVTNRVLDIKVRAAIDQIERARTTVSGIVNGEETRSLDSSLQLARNTLTSKTDPASGAGLAGAFDAVLMVPGDGPRAASTAGPVDQVPNALRGFVKAGQAAYQYATVQTEGFSGPALIIGTPTLSRVANLELYLIFPLASEQATITLVRGTMATGGLVLLVLLAGIALLVSRQVVVPVRSASRIAERFAEGHLSERMPVRGEDDMARLAVSFNDMAESLSRQIAQLEEFGNLQRRFTSDVSHELRTPLTTVRMAADLIYDHSADLDPTLRRSTELMVSELDRFETLLNDLLEISRHDAGVAELSVEAVDLRTTVNNALGNVGHLAEEAGIELLVDLPAEQVIAEVDARRVERILRNLIANAIDHAEHKPVRIRMAADEDTVAVTVRDYGVGLRPGEEKLVFSRFWRSDPSRVRRSGGTGLGLAISVEDARLHQGRLEAWGEPGEGACFRLTLPMVRGHKVTTSPLPMKPIPQPVLQPVAQPNPQPMPPEYKERQRPREHAEWSG,Sensor histidine kinase MtrB,"Member of the two-component regulatory system MtrA/MtrB. Probably functions as a membrane-associated protein kinase that phosphorylates MtrA in response to environmental signals. Autophosphorylates and transfers phosphate to MtrA in vitro. Overexpression of MtrA alone decreases bacterial virulence in mouse infection; co-expression of MtrA and MtrB restores normal bacterial growth, suggesting that bacterial growth in macrophages requires an optimal ratio of MtrB to MtrA. Probably plays a role in cell division.","The M. smegmatis mtrB mutant was filamentous, defective for cell division, and contained lysozyme-sensitive cell walls. The mtrB phenotype was complemented by either production of MtrB protein competent for phosphorylation or overproduction of MtrA() and MtrA() mutant proteins exhibiting altered phosphorylation potential, indicating that either MtrB phosphorylation or MtrB independent expression of MtrA regulon genes, including those involved in cell wall processing, are necessary for regulated cell division. In partial support of this observation, we found that the essential cell wall hydrolase ripA is an MtrA target and that the expression of bona fide MtrA targets ripA, fbpB, and dnaA were compromised in the mtrB mutant and partially rescued upon MtrA() and MtrA() overproduction. MtrB septal assembly was compromised upon FtsZ depletion and exposure of cells to mitomycin C, a DNA damaging agent, which interferes with FtsZ ring assembly. Expression of MtrA targets was also compromised under the above conditions, indicating that MtrB septal localization and MtrA regulon expression are linked. We propose that MtrB septal association is a necessary feature of MtrB activation that promotes MtrA phosphorylation and MtrA regulon expression.","Loss of autophosphorylation. Partially complements an M.smegmatis mtrB disruption, cells are still filamentous and bulged but the protein targets to septa. The M. smegmatis mtrB mutant was filamentous, defective for cell division, and contained lysozyme-sensitive cell walls. The mtrB phenotype was complemented by either production of MtrB protein competent for phosphorylation or overproduction of MtrA() and MtrA() mutant proteins exhibiting altered phosphorylation potential, indicating that either MtrB phosphorylation or MtrB independent expression of MtrA regulon genes, including those involved in cell wall processing, are necessary for regulated cell division. In partial support of this observation, we found that the essential cell wall hydrolase ripA is an MtrA target and that the expression of bona fide MtrA targets ripA, fbpB, and dnaA were compromised in the mtrB mutant and partially rescued upon MtrA() and MtrA() overproduction. MtrB septal assembly was compromised upon FtsZ depletion and exposure of cells to mitomycin C, a DNA damaging agent, which interferes with FtsZ ring assembly. Expression of MtrA targets was also compromised under the above conditions, indicating that MtrB septal localization and MtrA regulon expression are linked. We propose that MtrB septal association is a necessary feature of MtrB activation that promotes MtrA phosphorylation and MtrA regulon expression."
204,204,175515,Q6UWV6-R343E,MRGPAVLLTVALATLLAPGAGAPVQSQGSQNKLLLVSFDGFRWNYDQDVDTPNLDAMARDGVKARYMTPAFVTMTSPCHFTLVTGKYIENHGVVHNMYYNTTSKVKLPYHATLGIQRWWDNGSVPIWITAQRQGLRAGSFFYPGGNVTYQGVAVTRSRKEGIAHNYKNETEWRANIDTVMAWFTEEDLDLVTLYFGEPDSTGHRYGPESPERREMVRQVDRTVGYLRESIARNHLTDRLNLIITSDHGMTTVDKRAGDLVEFHKFPNFTFRDIEFELLDYGPNGMLLPKEGRLEKVYDALKDAHPKLHVYKKEAFPEAFHYANNPRVTPLLMYSDLGYVIHGEINVQFNNGEHGFDNKDMDMKTIFRAVGPSFRAGLEVEPFESVHVYELMCRLLGIVPEANDGHLATLLPMLHTESALPPDGRPTLLPKGRSALPPSSRPLLVMGLLGTVILLSEVA,Decreased enzyme activity; when associated with E-271.,,MRGPAVLLTVALATLLAPGAGAPVQSQGSQNKLLLVSFDGFRWNYDQDVDTPNLDAMARDGVKARYMTPAFVTMTSPCHFTLVTGKYIENHGVVHNMYYNTTSKVKLPYHATLGIQRWWDNGSVPIWITAQRQGLRAGSFFYPGGNVTYQGVAVTRSRKEGIAHNYKNETEWRANIDTVMAWFTEEDLDLVTLYFGEPDSTGHRYGPESPERREMVRQVDRTVGYLRESIARNHLTDRLNLIITSDHGMTTVDKRAGDLVEFHKFPNFTFRDIEFELLDYGPNGMLLPKEGRLEKVYDALKDAHPKLHVYKKEAFPEAFHYANNPRVTPLLMYSDLGYVIHGRINVQFNNGEHGFDNKDMDMKTIFRAVGPSFRAGLEVEPFESVHVYELMCRLLGIVPEANDGHLATLLPMLHTESALPPDGRPTLLPKGRSALPPSSRPLLVMGLLGTVILLSEVA,Ectonucleotide pyrophosphatase/phosphodiesterase family member 7,"Choline-specific phosphodiesterase that hydrolyzes sphingomyelin releasing the ceramide and phosphocholine and therefore is involved in sphingomyelin digestion, ceramide formation, and fatty acid (FA) absorption in the gastrointestinal tract. Has also phospholipase C activity and can also cleave phosphocholine from palmitoyl lyso-phosphatidylcholine and platelet-activating factor (PAF) leading to its inactivation. Does not have nucleotide pyrophosphatase activity. May promote cholesterol absorption by affecting the levels of sphingomyelin derived from either diet or endogenous sources, in the intestinal lumen.",The mutation in alk-SMase has been identified to cause functional changes in the protein.,Decreased enzyme activity; when associated with E-271. The mutation in alk-SMase has been identified to cause functional changes in the protein.
205,205,175528,P35462-G9S,MASLSQLSSHLNYTCGAENSTGASQARPHAYYALSYCALILAIVFGNGLVCMAVLKERALQTTTNYLVVSLAVADLLVATLVMPWVVYLEVTGGVWNFSRICCDVFVTLDVMMCTASILNLCAISIDRYTAVVMPVHYQHGTGQSSCRRVALMITAVWVLAFAVSCPLLFGFNTTGDPTVCSISNPDFVIYSSVVSFYLPFGVTVLVYARIYVVLKQRRRKRILTRQNSQCNSVRPGFPQQTLSPDPAHLELKRYYSICQDTALGGPGFQERGGELKREEKTRNSLSPTIAPKLSLEVRKLSNGRLSTSLKLGPLQPRGVPLREKKATQMVAIVLGAFIVCWLPFFLTHVLNTHCQTCHVSPELYSATTWLGYVNSALNPVIYTTFNIEFRKAFLKILSC,,,MASLSQLSGHLNYTCGAENSTGASQARPHAYYALSYCALILAIVFGNGLVCMAVLKERALQTTTNYLVVSLAVADLLVATLVMPWVVYLEVTGGVWNFSRICCDVFVTLDVMMCTASILNLCAISIDRYTAVVMPVHYQHGTGQSSCRRVALMITAVWVLAFAVSCPLLFGFNTTGDPTVCSISNPDFVIYSSVVSFYLPFGVTVLVYARIYVVLKQRRRKRILTRQNSQCNSVRPGFPQQTLSPDPAHLELKRYYSICQDTALGGPGFQERGGELKREEKTRNSLSPTIAPKLSLEVRKLSNGRLSTSLKLGPLQPRGVPLREKKATQMVAIVLGAFIVCWLPFFLTHVLNTHCQTCHVSPELYSATTWLGYVNSALNPVIYTTFNIEFRKAFLKILSC,D,Dopamine receptor whose activity is mediated by G proteins which inhibit adenylyl cyclase. Promotes cell proliferation.,"The G-9 variant in the dopamine D(3) receptor gene (DRD3) is associated and cosegregates with familial essential tremor (ET). G-9 homozygous patients have more severe and/or earlier onset forms of the disease than heterozygotes. The G-9 variant has a higher affinity for dopamine, leading to an increased cAMP response and prolonged MAPK signal compared to the S-9 variant. This gain-of-function may explain why drugs active against tremor in Parkinson's disease (PD) are usually not effective in the treatment of ET. The serine-to-glycine polymorphism at codon 9 of the DRD3 gene () was studied for its association with schizophrenia. However, no significant differences were found in genotype distribution, allele frequencies, or homozygosity proportion between schizophrenic patients and controls. Therefore, this polymorphism does not play a major role in schizophrenia. Increased homozygosity of the S/G variant of the Dopamine D3 receptor gene is associated with schizophrenia.","The G-9 variant in the dopamine D(3) receptor gene (DRD3) is associated and cosegregates with familial essential tremor (ET). G-9 homozygous patients have more severe and/or earlier onset forms of the disease than heterozygotes. The G-9 variant has a higher affinity for dopamine, leading to an increased cAMP response and prolonged MAPK signal compared to the S-9 variant. This gain-of-function may explain why drugs active against tremor in Parkinson's disease (PD) are usually not effective in the treatment of ET. The serine-to-glycine polymorphism at codon 9 of the DRD3 gene () was studied for its association with schizophrenia. However, no significant differences were found in genotype distribution, allele frequencies, or homozygosity proportion between schizophrenic patients and controls. Therefore, this polymorphism does not play a major role in schizophrenia. Increased homozygosity of the S/G variant of the Dopamine D3 receptor gene is associated with schizophrenia."
206,206,175783,Q6UWV6-H353A,MRGPAVLLTVALATLLAPGAGAPVQSQGSQNKLLLVSFDGFRWNYDQDVDTPNLDAMARDGVKARYMTPAFVTMTSPCHFTLVTGKYIENHGVVHNMYYNTTSKVKLPYHATLGIQRWWDNGSVPIWITAQRQGLRAGSFFYPGGNVTYQGVAVTRSRKEGIAHNYKNETEWRANIDTVMAWFTEEDLDLVTLYFGEPDSTGHRYGPESPERREMVRQVDRTVGYLRESIARNHLTDRLNLIITSDHGMTTVDKRAGDLVEFHKFPNFTFRDIEFELLDYGPNGMLLPKEGRLEKVYDALKDAHPKLHVYKKEAFPEAFHYANNPRVTPLLMYSDLGYVIHGRINVQFNNGEAGFDNKDMDMKTIFRAVGPSFRAGLEVEPFESVHVYELMCRLLGIVPEANDGHLATLLPMLHTESALPPDGRPTLLPKGRSALPPSSRPLLVMGLLGTVILLSEVA,Loss of activity.,,MRGPAVLLTVALATLLAPGAGAPVQSQGSQNKLLLVSFDGFRWNYDQDVDTPNLDAMARDGVKARYMTPAFVTMTSPCHFTLVTGKYIENHGVVHNMYYNTTSKVKLPYHATLGIQRWWDNGSVPIWITAQRQGLRAGSFFYPGGNVTYQGVAVTRSRKEGIAHNYKNETEWRANIDTVMAWFTEEDLDLVTLYFGEPDSTGHRYGPESPERREMVRQVDRTVGYLRESIARNHLTDRLNLIITSDHGMTTVDKRAGDLVEFHKFPNFTFRDIEFELLDYGPNGMLLPKEGRLEKVYDALKDAHPKLHVYKKEAFPEAFHYANNPRVTPLLMYSDLGYVIHGRINVQFNNGEHGFDNKDMDMKTIFRAVGPSFRAGLEVEPFESVHVYELMCRLLGIVPEANDGHLATLLPMLHTESALPPDGRPTLLPKGRSALPPSSRPLLVMGLLGTVILLSEVA,Ectonucleotide pyrophosphatase/phosphodiesterase family member 7,"Choline-specific phosphodiesterase that hydrolyzes sphingomyelin releasing the ceramide and phosphocholine and therefore is involved in sphingomyelin digestion, ceramide formation, and fatty acid (FA) absorption in the gastrointestinal tract. Has also phospholipase C activity and can also cleave phosphocholine from palmitoyl lyso-phosphatidylcholine and platelet-activating factor (PAF) leading to its inactivation. Does not have nucleotide pyrophosphatase activity. May promote cholesterol absorption by affecting the levels of sphingomyelin derived from either diet or endogenous sources, in the intestinal lumen.",substitution resulted in a protein with no alk-SMase activity.,Loss of activity. substitution resulted in a protein with no alk-SMase activity.
207,207,177377,Q31125-P198A,MTMGLRAPHWVAVGLLTWAALGLLVAGHEGHGDLHKDVEEDFHGHSHGHSHEDFHHGHSHGHSHEDFHHGHGHTHESIWHGHAHSHDHGHSREELHHGHSHGHSHDSLHHGGHGHAHREHSHGTSREAGAPGIKHHLDTVTLWAYALGATVLISAAPFFVLFLIPVESNSPRHRSLLQILLSFASGGLLGDAFLHLIAHALEPHSHHAPEQPGHGHSHSGQGPILSVGLWVLSGIVAFLVVEKFVRHVKGGHGHSHGHGDRHAHGDSHTHGDRHECSSKEKPSTEEEKEVGGLRKRRGGNTGPRDGPVKPQSPEEEKAGSDLRVSGYLNLAADLAHNFTDGLAIGASFRGGRGLGILTTMTVLLHEVPHEVGDFAILVQSGCSKKQAMRLQLVTAIGALAGTACALLTEGGAVDSDVAGGAGPGWVLPFTAGGFIYVATVSVLPELLREASPLQSLLEVLGLLGGVAMMVLIAHLE,Homozygous mice have profound B cell immunodeficiency and impaired transition from late pre-B to immature B cell. B cells from mutant mice exhibit a diminished concentration of cytoplasmic free zinc and decreased phosphorylation of signaling molecules downstream of the pre-B cell and B cell receptors.,,MTMGLRAPHWVAVGLLTWAALGLLVAGHEGHGDLHKDVEEDFHGHSHGHSHEDFHHGHSHGHSHEDFHHGHGHTHESIWHGHAHSHDHGHSREELHHGHSHGHSHDSLHHGGHGHAHREHSHGTSREAGAPGIKHHLDTVTLWAYALGATVLISAAPFFVLFLIPVESNSPRHRSLLQILLSFASGGLLGDAFLHLIPHALEPHSHHAPEQPGHGHSHSGQGPILSVGLWVLSGIVAFLVVEKFVRHVKGGHGHSHGHGDRHAHGDSHTHGDRHECSSKEKPSTEEEKEVGGLRKRRGGNTGPRDGPVKPQSPEEEKAGSDLRVSGYLNLAADLAHNFTDGLAIGASFRGGRGLGILTTMTVLLHEVPHEVGDFAILVQSGCSKKQAMRLQLVTAIGALAGTACALLTEGGAVDSDVAGGAGPGWVLPFTAGGFIYVATVSVLPELLREASPLQSLLEVLGLLGGVAMMVLIAHLE,Zinc transporter SLC39A7,"Transports Zn(2+) from the endoplasmic reticulum (ER)/Golgi apparatus to the cytosol, playing an essential role in the regulation of cytosolic zinc levels. Acts as gatekeeper of zinc release from intracellular stores, requiring post-translational activation by phosphorylation, resulting in activation of multiple downstream pathways leading to cell growth and proliferation. Has an essential role in B cell development and is required for proper B cell receptor signaling. Plays an important role in maintaining intestinal epithelial homeostasis and skin dermis development by regulating ER function. Controls cell signaling pathways involved in glucose metabolism in skeletal muscle. Has a protective role against ER stress in differents biological contexts. Mediates Zn(2+)-induced ferroptosis.",,Homozygous mice have profound B cell immunodeficiency and impaired transition from late pre-B to immature B cell. B cells from mutant mice exhibit a diminished concentration of cytoplasmic free zinc and decreased phosphorylation of signaling molecules downstream of the pre-B cell and B cell receptors.
208,208,177923,Q9HSF6-H179W,MPVVECDIQTARAALADAGASFSDGNSEHELWHADLGDAHAVAYADKLVVQGGSPTDITAVVQPDRGGRVHAYFDGASRGNPGPAAVGWVLVSGDGGIVAEGGDTIGRATNNQAEYDALIAALEAAADFGFDDIELRGDSQLVEKQLTGAWDTNDPDLRRKRVRARELLTGFDDWSITWVPRATNERADALANEALDDA,No loss of RNase H activity.,,MPVVECDIQTARAALADAGASFSDGNSEHELWHADLGDAHAVAYADKLVVQGGSPTDITAVVQPDRGGRVHAYFDGASRGNPGPAAVGWVLVSGDGGIVAEGGDTIGRATNNQAEYDALIAALEAAADFGFDDIELRGDSQLVEKQLTGAWDTNDPDLRRKRVRARELLTGFDDWSITHVPRATNERADALANEALDDA,Ribonuclease HI,Nuclease that specifically degrades the RNA of RNA-DNA hybrids; seems to act exonucleolytically on RNA/DNA hybrids. Endonucleolytically removes RNA primers from the Okazaki fragments of lagging strand synthesis on its own. Complements the temperature-sensitive phenotype of an E.coli double rnhA/rnhB (RNase H) disruption mutant.,,No loss of RNase H activity.
209,209,178593,P16152-V88I,MSSGIHVALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDVLINNAGIAFKVADPTPFHIQAEVTMKTNFFGTRDVCTELLPLIKPQGRVVNVSSIMSVRALKSCSPELQQKFRSETITEEELVGLMNKFVEDTKKGVHQKEGWPSSAYGVTKIGVTVLSRIHARKLSEQRKGDKILLNACCPGWVRTDMAGPKATKSPEEGAETPVYLALLPPDAEGPHGQFVSEKRVEQW,Reduced affinity for NADPH and reduced activity towards daunorubicin and prostaglandin E2.,,MSSGIHVALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDVLVNNAGIAFKVADPTPFHIQAEVTMKTNFFGTRDVCTELLPLIKPQGRVVNVSSIMSVRALKSCSPELQQKFRSETITEEELVGLMNKFVEDTKKGVHQKEGWPSSAYGVTKIGVTVLSRIHARKLSEQRKGDKILLNACCPGWVRTDMAGPKATKSPEEGAETPVYLALLPPDAEGPHGQFVSEKRVEQW,Carbonyl reductase [NADPH] 1,"NADPH-dependent reductase with broad substrate specificity. Catalyzes the reduction of a wide variety of carbonyl compounds including quinones, prostaglandins, menadione, plus various xenobiotics. Catalyzes the reduction of the antitumor anthracyclines doxorubicin and daunorubicin to the cardiotoxic compounds doxorubicinol and daunorubicinol. Can convert prostaglandin E to prostaglandin F2-alpha. Can bind glutathione, which explains its higher affinity for glutathione-conjugated substrates. Catalyzes the reduction of S-nitrosoglutathione. In addition, participates in the glucocorticoid metabolism by catalyzing the NADPH-dependent cortisol/corticosterone into 20beta-dihydrocortisol (20b-DHF) or 20beta-corticosterone (20b-DHB), which are weak agonists of NR3C1 and NR3C2 in adipose tissue.","The CBR1 V88 and CBR1 I88 isoforms have different maximal velocities for daunorubicin and PGE2. Concomitantly, CBR1 V88 produced higher levels of the cardiotoxic metabolite daunorubicinol compared with CBR1 I88. Inhibition studies demonstrated that CBR1 V88 and CBR1 I88 are distinctively inhibited by the flavonoid, rutin. Furthermore, isothermal titration calorimetry analyses together with molecular modeling studies showed that CBR1 results in CBR1 isoforms with different binding affinities for the cofactor NADPH. The mutation in CBR1 may affect the activity of the enzyme.","Reduced affinity for NADPH and reduced activity towards daunorubicin and prostaglandin E2. The CBR1 V88 and CBR1 I88 isoforms have different maximal velocities for daunorubicin and PGE2. Concomitantly, CBR1 V88 produced higher levels of the cardiotoxic metabolite daunorubicinol compared with CBR1 I88. Inhibition studies demonstrated that CBR1 V88 and CBR1 I88 are distinctively inhibited by the flavonoid, rutin. Furthermore, isothermal titration calorimetry analyses together with molecular modeling studies showed that CBR1 results in CBR1 isoforms with different binding affinities for the cofactor NADPH. The mutation in CBR1 may affect the activity of the enzyme."
210,210,178666,Q9IK90-Y92A,MEPDIKSISSESMEGVSDFSPSSWEHGGYLDKVEPEIDENGSMIPKYKIYTPGANERKYNNYMYLICYGFVEDVERTPETGKRKKIRTIAAAPLGVGKSASHPQDLLEELCSLKVTVRRTAGSTEKIVFGSSGPLNHLVPWKKVLTSGSIFNAVKVCRNVDQIQLDKHQALRIFFLSITKLNDSGIYMIPRTMLEFRRNNAIAFNLLVYLKIDADLSKMGIQGSLDKDGFKVASFMLHLGNFVRRAGKYYSVDYCRRKIDRMKLQFSLGSIGGLSLHIKINGVISKRLFAQMGFQKNLCFSLMDINPWLNRLTWNNSCEISRVAAVLQPSIPREFMIYDDVFIDNTGRILKG,Complete loss of budding.,,MEPDIKSISSESMEGVSDFSPSSWEHGGYLDKVEPEIDENGSMIPKYKIYTPGANERKYNNYMYLICYGFVEDVERTPETGKRKKIRTIAAYPLGVGKSASHPQDLLEELCSLKVTVRRTAGSTEKIVFGSSGPLNHLVPWKKVLTSGSIFNAVKVCRNVDQIQLDKHQALRIFFLSITKLNDSGIYMIPRTMLEFRRNNAIAFNLLVYLKIDADLSKMGIQGSLDKDGFKVASFMLHLGNFVRRAGKYYSVDYCRRKIDRMKLQFSLGSIGGLSLHIKINGVISKRLFAQMGFQKNLCFSLMDINPWLNRLTWNNSCEISRVAAVLQPSIPREFMIYDDVFIDNTGRILKG,Matrix protein,Plays a crucial role in virion assembly and budding. Forms a shell at the inner face of the plasma membrane. Transits through the host nucleus before gaining the functional ability to localize and bud from the plasma membrane. Mediates together with fusion protein the incorporation of the glycoprotein to the viral particles. Participates also in the inhibition of the host interferon type I antiviral response by interacting with and thereby inhibiting host TRIM6.,Mutation of Y92 to A abolished VLP release and caused relocalization of NiV M to the nucleus.,Complete loss of budding. Mutation of Y92 to A abolished VLP release and caused relocalization of NiV M to the nucleus.
211,211,179186,Q92504-P190A,MARGLGAPHWVAVGLLTWATLGLLVAGLGGHDDLHDDLQEDFHGHSHRHSHEDFHHGHSHAHGHGHTHESIWHGHTHDHDHGHSHEDLHHGHSHGYSHESLYHRGHGHDHEHSHGGYGESGAPGIKQDLDAVTLWAYALGATVLISAAPFFVLFLIPVESNSPRHRSLLQILLSFASGGLLGDAFLHLIAHALEPHSHHTLEQPGHGHSHSGQGPILSVGLWVLSGIVAFLVVEKFVRHVKGGHGHSHGHGHAHSHTRGSHGHGRQERSTKEKQSSEEEEKETRGVQKRRGGSTVPKDGPVRPQNAEEEKRGLDLRVSGYLNLAADLAHNFTDGLAIGASFRGGRGLGILTTMTVLLHEVPHEVGDFAILVQSGCSKKQAMRLQLLTAVGALAGTACALLTEGGAVGSEIAGGAGPGWVLPFTAGGFIYVATVSVLPELLREASPLQSLLEVLGLLGGVIMMVLIAHLE,In AGM9; decreased zinc ion transporter activity; does not affect localization to endoplasmic reticulum.,,MARGLGAPHWVAVGLLTWATLGLLVAGLGGHDDLHDDLQEDFHGHSHRHSHEDFHHGHSHAHGHGHTHESIWHGHTHDHDHGHSHEDLHHGHSHGYSHESLYHRGHGHDHEHSHGGYGESGAPGIKQDLDAVTLWAYALGATVLISAAPFFVLFLIPVESNSPRHRSLLQILLSFASGGLLGDAFLHLIPHALEPHSHHTLEQPGHGHSHSGQGPILSVGLWVLSGIVAFLVVEKFVRHVKGGHGHSHGHGHAHSHTRGSHGHGRQERSTKEKQSSEEEEKETRGVQKRRGGSTVPKDGPVRPQNAEEEKRGLDLRVSGYLNLAADLAHNFTDGLAIGASFRGGRGLGILTTMTVLLHEVPHEVGDFAILVQSGCSKKQAMRLQLLTAVGALAGTACALLTEGGAVGSEIAGGAGPGWVLPFTAGGFIYVATVSVLPELLREASPLQSLLEVLGLLGGVIMMVLIAHLE,Zinc transporter SLC39A7,"Transports Zn(2+) from the endoplasmic reticulum (ER)/Golgi apparatus to the cytosol, playing an essential role in the regulation of cytosolic zinc levels. Acts as gatekeeper of zinc release from intracellular stores, requiring post-translational activation by phosphorylation, resulting in activation of multiple downstream pathways leading to cell growth and proliferation. Has an essential role in B cell development and is required for proper B cell receptor signaling. Plays an important role in maintaining intestinal epithelial homeostasis and skin dermis development by regulating ER function. Controls cell signaling pathways involved in glucose metabolism in skeletal muscle. Has a protective role against ER stress in differents biological contexts. Mediates Zn(2+)-induced ferroptosis.",,In AGM9; decreased zinc ion transporter activity; does not affect localization to endoplasmic reticulum.
212,212,180381,Q9ULZ3-D48K,MGRARDAILDALENLTAEELKKFKLKLLSVPLREGYGRIPRGALLSMKALDLTDKLVSFYLETYGAELTANVLRDMGLQEMAGQLQAATHQGSGAAPAGIQAPPQSAAKPGLHFIDQHRAALIARVTNVEWLLDALYGKVLTDEQYQAVRAEPTNPSKMRKLFSFTPAWNWTCKDLLLQALRESQSYLVEDLERS,Abolishes homooligomerization.,,MGRARDAILDALENLTAEELKKFKLKLLSVPLREGYGRIPRGALLSMDALDLTDKLVSFYLETYGAELTANVLRDMGLQEMAGQLQAATHQGSGAAPAGIQAPPQSAAKPGLHFIDQHRAALIARVTNVEWLLDALYGKVLTDEQYQAVRAEPTNPSKMRKLFSFTPAWNWTCKDLLLQALRESQSYLVEDLERS,Apoptosis-associated speck-like protein containing a CARD,"Functions as key mediator in apoptosis and inflammation. Promotes caspase-mediated apoptosis involving predominantly caspase-8 and also caspase-9 in a probable cell type-specific manner. Involved in activation of the mitochondrial apoptotic pathway, promotes caspase-8-dependent proteolytic maturation of BID independently of FADD in certain cell types and also mediates mitochondrial translocation of BAX and activates BAX-dependent apoptosis coupled to activation of caspase-9, -2 and -3. Involved in innate immune response by acting as an integral adapter in the assembly of various inflammasomes (NLRP1, NLRP2, NLRP3, NLRP6, AIM2 and probably IFI16) which recruit and activate caspase-1 leading to processing and secretion of pro-inflammatory cytokines. Caspase-1-dependent inflammation leads to macrophage pyroptosis, a form of cell death. The function as activating adapter in different types of inflammasomes is mediated by the pyrin and CARD domains and their homotypic interactions. Clustered PYCARD nucleates the formation of caspase-1 filaments through the interaction of their respective CARD domains, acting as a platform for of caspase-1 polymerization. In the NLRP1 and NLRC4 inflammasomes seems not be required but facilitates the processing of procaspase-1. In cooperation with NOD2 involved in an inflammasome activated by bacterial muramyl dipeptide leading to caspase-1 activation. May be involved in RIGI-triggered pro-inflammatory responses and inflammasome activation. In collaboration with AIM2 which detects cytosolic double-stranded DNA may also be involved in a caspase-1-independent cell death that involves caspase-8. In adaptive immunity may be involved in maturation of dendritic cells to stimulate T-cell immunity and in cytoskeletal rearrangements coupled to chemotaxis and antigen uptake may be involved in post-transcriptional regulation of the guanine nucleotide exchange factor DOCK2; the latter function is proposed to involve the nuclear form. Also involved in transcriptional activation of cytokines and chemokines independent of the inflammasome; this function may involve AP-1, NF-kappa-B, MAPK and caspase-8 signaling pathways. For regulation of NF-kappa-B activating and inhibiting functions have been reported. Modulates NF-kappa-B induction at the level of the IKK complex by inhibiting kinase activity of CHUK and IKBK. Proposed to compete with RIPK2 for association with CASP1 thereby down-regulating CASP1-mediated RIPK2-dependent NF-kappa-B activation and activating interleukin-1 beta processing. Modulates host resistance to DNA virus infection, probably by inducing the cleavage of and inactivating CGAS in presence of cytoplasmic double-stranded DNA.May have a regulating effect on the function as inflammasome adapter.Seems to inhibit inflammasome-mediated maturation of interleukin-1 beta.",Mutation of D48 to K in ASC protein leads to loss of filament formation.,Abolishes homooligomerization. Mutation of D48 to K in ASC protein leads to loss of filament formation.
213,213,180408,O14746-D868A,MPRAPRCRAVRSLLRSHYREVLPLATFVRRLGPQGWRLVQRGDPAAFRALVAQCLVCVPWDARPPPAAPSFRQVSCLKELVARVLQRLCERGAKNVLAFGFALLDGARGGPPEAFTTSVRSYLPNTVTDALRGSGAWGLLLRRVGDDVLVHLLARCALFVLVAPSCAYQVCGPPLYQLGAATQARPPPHASGPRRRLGCERAWNHSVREAGVPLGLPAPGARRRGGSASRSLPLPKRPRRGAAPEPERTPVGQGSWAHPGRTRGPSDRGFCVVSPARPAEEATSLEGALSGTRHSHPSVGRQHHAGPPSTSRPPRPWDTPCPPVYAETKHFLYSSGDKEQLRPSFLLSSLRPSLTGARRLVETIFLGSRPWMPGTPRRLPRLPQRYWQMRPLFLELLGNHAQCPYGVLLKTHCPLRAAVTPAAGVCAREKPQGSVAAPEEEDTDPRRLVQLLRQHSSPWQVYGFVRACLRRLVPPGLWGSRHNERRFLRNTKKFISLGKHAKLSLQELTWKMSVRDCAWLRRSPGVGCVPAAEHRLREEILAKFLHWLMSVYVVELLRSFFYVTETTFQKNRLFFYRKSVWSKLQSIGIRQHLKRVQLRELSEAEVRQHREARPALLTSRLRFIPKPDGLRPIVNMDYVVGARTFRREKRAERLTSRVKALFSVLNYERARRPGLLGASVLGLDDIHRAWRTFVLRVRAQDPPPELYFVKVDVTGAYDTIPQDRLTEVIASIIKPQNTYCVRRYAVVQKAAHGHVRKAFKSHVSTLTDLQPYMRQFVAHLQETSPLRDAVVIEQSSSLNEASSGLFDVFLRFMCHHAVRIRGKSYVQCQGIPQGSILSTLLCSLCYGDMENKLFAGIRRDGLLLRLVADFLLVTPHLTHAKTFLRTLVRGVPEYGCVVNLRKTVVNFPVEDEALGGTAFVQMPAHGLFPWCGLLLDTRTLEVQSDYSSYARTSIRASLTFNRGFKAGRNMRRKLFGVLRLKCHSLFLDLQVNSLQTVCTNIYKILLLQAYRFHACVLQLPFHQQ,Loss of telomerase activity.,,MPRAPRCRAVRSLLRSHYREVLPLATFVRRLGPQGWRLVQRGDPAAFRALVAQCLVCVPWDARPPPAAPSFRQVSCLKELVARVLQRLCERGAKNVLAFGFALLDGARGGPPEAFTTSVRSYLPNTVTDALRGSGAWGLLLRRVGDDVLVHLLARCALFVLVAPSCAYQVCGPPLYQLGAATQARPPPHASGPRRRLGCERAWNHSVREAGVPLGLPAPGARRRGGSASRSLPLPKRPRRGAAPEPERTPVGQGSWAHPGRTRGPSDRGFCVVSPARPAEEATSLEGALSGTRHSHPSVGRQHHAGPPSTSRPPRPWDTPCPPVYAETKHFLYSSGDKEQLRPSFLLSSLRPSLTGARRLVETIFLGSRPWMPGTPRRLPRLPQRYWQMRPLFLELLGNHAQCPYGVLLKTHCPLRAAVTPAAGVCAREKPQGSVAAPEEEDTDPRRLVQLLRQHSSPWQVYGFVRACLRRLVPPGLWGSRHNERRFLRNTKKFISLGKHAKLSLQELTWKMSVRDCAWLRRSPGVGCVPAAEHRLREEILAKFLHWLMSVYVVELLRSFFYVTETTFQKNRLFFYRKSVWSKLQSIGIRQHLKRVQLRELSEAEVRQHREARPALLTSRLRFIPKPDGLRPIVNMDYVVGARTFRREKRAERLTSRVKALFSVLNYERARRPGLLGASVLGLDDIHRAWRTFVLRVRAQDPPPELYFVKVDVTGAYDTIPQDRLTEVIASIIKPQNTYCVRRYAVVQKAAHGHVRKAFKSHVSTLTDLQPYMRQFVAHLQETSPLRDAVVIEQSSSLNEASSGLFDVFLRFMCHHAVRIRGKSYVQCQGIPQGSILSTLLCSLCYGDMENKLFAGIRRDGLLLRLVDDFLLVTPHLTHAKTFLRTLVRGVPEYGCVVNLRKTVVNFPVEDEALGGTAFVQMPAHGLFPWCGLLLDTRTLEVQSDYSSYARTSIRASLTFNRGFKAGRNMRRKLFGVLRLKCHSLFLDLQVNSLQTVCTNIYKILLLQAYRFHACVLQLPFHQQ,Telomerase reverse transcriptase,"Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. Active in progenitor and cancer cells. Inactive, or very low activity, in normal somatic cells. Catalytic component of the teleromerase holoenzyme complex whose main activity is the elongation of telomeres by acting as a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme. Catalyzes the RNA-dependent extension of 3'-chromosomal termini with the 6-nucleotide telomeric repeat unit, 5'-TTAGGG-3'. The catalytic cycle involves primer binding, primer extension and release of product once the template boundary has been reached or nascent product translocation followed by further extension. More active on substrates containing 2 or 3 telomeric repeats. Telomerase activity is regulated by a number of factors including telomerase complex-associated proteins, chaperones and polypeptide modifiers. Modulates Wnt signaling. Plays important roles in aging and antiapoptosis.","The mutation in the hTERT protein causes telomerase activity defects consistent with disruption of a template-proximal anchor site. This mutation leads to reduced processivity on short telomeric primers and reduced activity on substrates with nontelomeric 5' sequences, but not on primers with nontelomeric G-rich 5' sequences. The mutation is located within a subregion of the N-terminal human TERT RNA interaction domain 1 (RID1) previously implicated in biological telomerase functions unrelated to catalytic activity (N-DAT domain). Other mutants in the N-DAT and C-terminal DAT (C-DAT) regions, as well as a C-terminally tagged hTERT-HA variant, also showed defects in elongating short telomeric primers. The catalytic phenotypes of these mutants were partially or completely rescued by increasing concentrations of DNA primers. These findings suggest that RID1 and the hTERT C terminus contribute to telomerase's affinity for its substrate, and that RID1 may form part of the human telomerase anchor site. Mutation of residue D868 to A severely reduced associated telomerase activity. Substitution of the amino acid residue D868 with A completely abolished telomerase activity.","Loss of telomerase activity. The mutation in the hTERT protein causes telomerase activity defects consistent with disruption of a template-proximal anchor site. This mutation leads to reduced processivity on short telomeric primers and reduced activity on substrates with nontelomeric 5' sequences, but not on primers with nontelomeric G-rich 5' sequences. The mutation is located within a subregion of the N-terminal human TERT RNA interaction domain 1 (RID1) previously implicated in biological telomerase functions unrelated to catalytic activity (N-DAT domain). Other mutants in the N-DAT and C-terminal DAT (C-DAT) regions, as well as a C-terminally tagged hTERT-HA variant, also showed defects in elongating short telomeric primers. The catalytic phenotypes of these mutants were partially or completely rescued by increasing concentrations of DNA primers. These findings suggest that RID1 and the hTERT C terminus contribute to telomerase's affinity for its substrate, and that RID1 may form part of the human telomerase anchor site. Mutation of residue D868 to A severely reduced associated telomerase activity. Substitution of the amino acid residue D868 with A completely abolished telomerase activity."
214,214,182884,P9WGT3-S144L,MTATATEGAKPPFVSRSVLVTGGNRGIGLAIAQRLAADGHKVAVTHRGSGAPKGLFGVECDVTDSDAVDRAFTAVEEHQGPVEVLVSNAGLSADAFLMRMTEEKFEKVINANLTGAFRVAQRASRSMQRNKFGRMIFIGSVSGLWGIGNQANYAASKAGVIGMARSIARELSKANVTANVVAPGYIDTDMTRALDERIQQGALQFIPAKRVGTPAEVAGVVSFLASEDASYISGAVIPVDGGMGMGH,Stabilizes the catalytic loop in its open active form. Retains 84% of activity; when associated with V-60. Totally inactive; when associated with V-60 and A-139.,,MTATATEGAKPPFVSRSVLVTGGNRGIGLAIAQRLAADGHKVAVTHRGSGAPKGLFGVECDVTDSDAVDRAFTAVEEHQGPVEVLVSNAGLSADAFLMRMTEEKFEKVINANLTGAFRVAQRASRSMQRNKFGRMIFIGSVSGSWGIGNQANYAASKAGVIGMARSIARELSKANVTANVVAPGYIDTDMTRALDERIQQGALQFIPAKRVGTPAEVAGVVSFLASEDASYISGAVIPVDGGMGMGH,3-oxoacyl-[acyl-carrier-protein] reductase MabA,"Part of the mycobacterial fatty acid elongation system FAS-II, which is involved in mycolic acid biosynthesis. Catalyzes the NADPH-dependent reduction of beta-ketoacyl derivatives, the second step of the FAS-II elongation cycle. May preferentially metabolize long-chain substrates (C8-C20). Can use CoA derivatives as substrates in vitro.",The crystal structure of a mutated MabA protein was then solved in both inactive and active form.,Stabilizes the catalytic loop in its open active form. Retains 84% of activity; when associated with V-60. Totally inactive; when associated with V-60 and A-139. The crystal structure of a mutated MabA protein was then solved in both inactive and active form.
215,215,183162,P08692-D128A,MSNITIYHNPACGTSRNTLEMIRNSGTEPTIILYLENPPSRDELVKLIADMGISVRALLRKNVEPYEQLGLAEDKFTDDQLIDFMLQHPILINRPIVVTPLGTRLCRPSEVVLDILQDAQKGAFTKEAGEKVVDEAGKRLK,"4-fold decrease in catalytic efficiency with arsenate. Mutant is relatively resistant to arsenate, but is more sensitive at higher concentrations.",,MSNITIYHNPACGTSRNTLEMIRNSGTEPTIILYLENPPSRDELVKLIADMGISVRALLRKNVEPYEQLGLAEDKFTDDQLIDFMLQHPILINRPIVVTPLGTRLCRPSEVVLDILQDAQKGAFTKEDGEKVVDEAGKRLK,Arsenate reductase,Involved in resistance to arsenate. Catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)]. The resulting arsenite is then extruded from the cell via the ArsAB transport system (Probable).,,"4-fold decrease in catalytic efficiency with arsenate. Mutant is relatively resistant to arsenate, but is more sensitive at higher concentrations."
216,216,183727,Q9ESN9-L209G,MMEIQMDEGGGVVVYQDDYCSGSVMSERVSGLAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEERESEMKKEYNALHQRHTEMIQTYVEHIERSKMQQVGGSGQTESSLPGRSRKERPTSGNVFPLADGMVRAQMGGKLVPAGDHWHLSDLGQLQSSSSYQCPNDEMSESGQSSAAATPSTTGTKSNTPTSSVPSAAVTPLNESLQPLGDYVSVTKNNKQAREKRNSRNMEVQVTQEMRNVSIGMGSSDEWSDVQDIIDSTPELDVCPETRLERTGSSPTQGIVNKAFGINTDSLYHELSTAGSEVIGDVDEGADLLGEFSVRDDFFGMGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEELKRVKSEAVTARREPREEVEDVSSYLCTELDKIPMAQRRRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASREHPSVQEKKKSTIWQFFSRLFSSSSSPPPAKRSYPSVNIHYKSPTAAGFSQRRSHALCQISAGSRPLEFFPDDDCTSSARREQKREQYRQVREHVRNDDGRLQACGWSLPAKYKQLSPNGGQEDTRMKNVPVPVYCRPLVEKDPSTKLWCAAGVNLSGWKPHEEDSSNGPKPVPGRDPLTCDREGEGEPKSTHPSPEKKKAKETPEADATSSRVWILTSTLTTSKVVIIDANQPGTIVDQFTVCNAHVLCISSIPAASDSDYPPGEMFLDSDVNPEDSGADGVLAGITLVGCATRCNVPRSNCSSRGDTPVLDKGQGDVATTANGKVNPSQSTEEATEATEVPDPGPSESEATTVRPGPLTEHVFTDPAPTPSSSTQPASENGSESNGTIVQPQVEPSGELSTTTSSAAPTMWLGAQNGWLYVHSAVANWKKCLHSIKLKDSVLSLVHVKGRVLVALADGTLAI,Results in inhibition of JNK binding.,,MMEIQMDEGGGVVVYQDDYCSGSVMSERVSGLAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEERESEMKKEYNALHQRHTEMIQTYVEHIERSKMQQVGGSGQTESSLPGRSRKERPTSLNVFPLADGMVRAQMGGKLVPAGDHWHLSDLGQLQSSSSYQCPNDEMSESGQSSAAATPSTTGTKSNTPTSSVPSAAVTPLNESLQPLGDYVSVTKNNKQAREKRNSRNMEVQVTQEMRNVSIGMGSSDEWSDVQDIIDSTPELDVCPETRLERTGSSPTQGIVNKAFGINTDSLYHELSTAGSEVIGDVDEGADLLGEFSVRDDFFGMGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEELKRVKSEAVTARREPREEVEDVSSYLCTELDKIPMAQRRRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASREHPSVQEKKKSTIWQFFSRLFSSSSSPPPAKRSYPSVNIHYKSPTAAGFSQRRSHALCQISAGSRPLEFFPDDDCTSSARREQKREQYRQVREHVRNDDGRLQACGWSLPAKYKQLSPNGGQEDTRMKNVPVPVYCRPLVEKDPSTKLWCAAGVNLSGWKPHEEDSSNGPKPVPGRDPLTCDREGEGEPKSTHPSPEKKKAKETPEADATSSRVWILTSTLTTSKVVIIDANQPGTIVDQFTVCNAHVLCISSIPAASDSDYPPGEMFLDSDVNPEDSGADGVLAGITLVGCATRCNVPRSNCSSRGDTPVLDKGQGDVATTANGKVNPSQSTEEATEATEVPDPGPSESEATTVRPGPLTEHVFTDPAPTPSSSTQPASENGSESNGTIVQPQVEPSGELSTTTSSAAPTMWLGAQNGWLYVHSAVANWKKCLHSIKLKDSVLSLVHVKGRVLVALADGTLAI,C-Jun-amino-terminal kinase-interacting protein 3,"The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. May function as a regulator of vesicle transport, through interactions with the JNK-signaling components and motor proteins. Promotes neuronal axon elongation in a kinesin- and JNK-dependent manner. Activates cofilin at axon tips via local activation of JNK, thereby regulating filopodial dynamics and enhancing axon elongation. Its binding to kinesin heavy chains (KHC), promotes kinesin-1 motility along microtubules and is essential for axon elongation and regeneration. Regulates cortical neuronal migration by mediating NTRK2/TRKB anterograde axonal transport during brain development. Acts as an adapter that bridges the interaction between NTRK2/TRKB and KLC1 and drives NTRK2/TRKB axonal but not dendritic anterograde transport, which is essential for subsequent BDNF-triggered signaling and filopodia formation.",,Results in inhibition of JNK binding.
217,217,184578,O00899-K474E,MEGLEIEDEDVILLDEDDDSSSSSTVNNSSSNIKNNGNTNNNIGNDDSNKVTLMTSLREKGWGSGMLVDKEKNQYGTIKSYKDDKSSPWFEERQVIATLYKARVLLHEMIYTKMNQERLLSGNLCVGEIQSLLNTQKEDVETDWIAEIQELKRNMVAEIRRNHLLERDVNKLDKRIALLIKHRSNIKDLLLEQNKGKKDKKKKGDDKAEYITLDQKQLESYQNLFYLLQTEPHYLAKLVTLIQADQMEDFLDTVFLTLFGDDFSPREEFLILSLFRLAIGQEMSRIKSAGDLLAVESVVPKMIITYTRRKQGHEFLKQIIAPILENNVVNAPDLNLELNAVQVYQNMISEQEIQTGAKSTLNRGLAEDQIIQLKEVQSILEPRVEKCIQICERFFTGIIQSLNRLPYGIRWICKQIQSIAQKNFDSKPDEIAKVIGYFVYYRFINLAIVTPDAFEILDKELSITSRKNLVNIAEVLQNLFTLKTFQNQGSERWMQPLNKWILSKTSIVRQYLEDLIQVTDPSEYLRVDKYNELTLKLNPVVVISLGEISQTHRLLIANLAALKMKEKEDPLELILKALPAPLEVVDENDREIQLTLINRFKENIEKEISISASLLAETKELVISVLRSIPIQQKQQQQQHDDEKRDDLISILQNAIKHGKETNNPQLSSNAEKIINNLKKMEAEGSIQSENNQYEGFIKVIALEVINRQEIREQQRKERMRLTIALRDLRKHQSYLNDQIQHYTSYLKDVLLHYGPKDKKKSTKPMKISFKELTKKGVIVESDIPKLSHGSTSFYISSDAPGIFDIEARIGVASVGTLSLSLDDLLDKSSAGIPYLKLENIVLDVNMTLHLLNRHFLKNI,Unable to complement a gapA null mutant.,,MEGLEIEDEDVILLDEDDDSSSSSTVNNSSSNIKNNGNTNNNIGNDDSNKVTLMTSLREKGWGSGMLVDKEKNQYGTIKSYKDDKSSPWFEERQVIATLYKARVLLHEMIYTKMNQERLLSGNLCVGEIQSLLNTQKEDVETDWIAEIQELKRNMVAEIRRNHLLERDVNKLDKRIALLIKHRSNIKDLLLEQNKGKKDKKKKGDDKAEYITLDQKQLESYQNLFYLLQTEPHYLAKLVTLIQADQMEDFLDTVFLTLFGDDFSPREEFLILSLFRLAIGQEMSRIKSAGDLLAVESVVPKMIITYTRRKQGHEFLKQIIAPILENNVVNAPDLNLELNAVQVYQNMISEQEIQTGAKSTLNRGLAEDQIIQLKEVQSILEPRVEKCIQICERFFTGIIQSLNRLPYGIRWICKQIQSIAQKNFDSKPDEIAKVIGYFVYYRFINLAIVTPDAFEILDKELSITSRKNLVNIAKVLQNLFTLKTFQNQGSERWMQPLNKWILSKTSIVRQYLEDLIQVTDPSEYLRVDKYNELTLKLNPVVVISLGEISQTHRLLIANLAALKMKEKEDPLELILKALPAPLEVVDENDREIQLTLINRFKENIEKEISISASLLAETKELVISVLRSIPIQQKQQQQQHDDEKRDDLISILQNAIKHGKETNNPQLSSNAEKIINNLKKMEAEGSIQSENNQYEGFIKVIALEVINRQEIREQQRKERMRLTIALRDLRKHQSYLNDQIQHYTSYLKDVLLHYGPKDKKKSTKPMKISFKELTKKGVIVESDIPKLSHGSTSFYISSDAPGIFDIEARIGVASVGTLSLSLDDLLDKSSAGIPYLKLENIVLDVNMTLHLLNRHFLKNI,Ras GTPase-activating-like protein gapA,Part of signaling pathway that is required for completion of cytokinesis. gapA and rgaA control cortexillin localization to the cleavage furrow and hence may be involved in cleavage of the midbody in the final stage of cytokinesis by regulating the actin cytoskeleton. Forms a complex by linking activated rac1A to ctxA in the absence of rgaA. Assembly of this complex is necessary for the recruitment of cortexillin to the midzone of the dividing cell.,Positively charged side chain K474 of GAPA is essential for interaction with small GTPases in cytokinesis.,Unable to complement a gapA null mutant. Positively charged side chain K474 of GAPA is essential for interaction with small GTPases in cytokinesis.
218,218,185465,Q84W98-S98H,MATSNDQTNTKSSHSRTLLLLFIFLSLLLFSSLTIPMTRHQSTSMVAPFKRVLLESSVPASSTMDLRPKASTRRSRTSRRREFGNDAHEVPSGPNPIHN,Compromised interaction with TDR.,,MATSNDQTNTKSSHSRTLLLLFIFLSLLLFSSLTIPMTRHQSTSMVAPFKRVLLESSVPASSTMDLRPKASTRRSRTSRRREFGNDAHEVPSGPNPISN,CLAVATA3/ESR,"Extracellular signal peptide that regulates cell fate. May act with TDR as a ligand-receptor pair in a signal transduction pathway that represses tracheary element differentiation but promotes the formation of procambial cells adjacent to phloem cells in the veins in an auxin-dependent manner. Regulates the transition of protophloem cells from proliferation to differentiation, thus impinging on postembryonic growth capacity of the root meristem; this signaling pathway requires CRN and CLV2.",The mutation in TDIF leads to [functional changes].,Compromised interaction with TDR. The mutation in TDIF leads to [functional changes].
219,219,185764,P25522-R252A,MSDNDTIVAQATPPGRGGVGILRISGFKAREVAETVLGKLPKPRYADYLPFKDADGSVLDQGIALWFPGPNSFTGEDVLELQGHGGPVILDLLLKRILTIPGLRIARPGEFSERAFLNDKLDLAQAEAIADLIDASSEQAARSALNSLQGAFSARVNHLVEALTHLRIYVEAAIDFPDEEIDFLSDGKIEAQLNDVIADLDAVRAEARQGSLLREGMKVVIAGRPNAGKSSLLNALAGREAAIVTDIAGTTADVLREHIHIDGMPLHIIDTAGLREASDEVERIGIERAWQEIEQADRVLFMVDGTTTDAVDPAEIWPEFIARLPAKLPITVVRNKADITGETLGMSEVNGHALIRLSARTGEGVDVLRNHLKQSMGFDTNMEGGFLARRRHLQALEQAAEHLQQGKAQLLGAWAGELLAEELRLAQQNLSEITGEFTSDDLLGRIFSSFCIGK,7-fold decrease in GTPase activity and 6-fold increase of affinity.,,MSDNDTIVAQATPPGRGGVGILRISGFKAREVAETVLGKLPKPRYADYLPFKDADGSVLDQGIALWFPGPNSFTGEDVLELQGHGGPVILDLLLKRILTIPGLRIARPGEFSERAFLNDKLDLAQAEAIADLIDASSEQAARSALNSLQGAFSARVNHLVEALTHLRIYVEAAIDFPDEEIDFLSDGKIEAQLNDVIADLDAVRAEARQGSLLREGMKVVIAGRPNAGKSSLLNALAGREAAIVTDIAGTTRDVLREHIHIDGMPLHIIDTAGLREASDEVERIGIERAWQEIEQADRVLFMVDGTTTDAVDPAEIWPEFIARLPAKLPITVVRNKADITGETLGMSEVNGHALIRLSARTGEGVDVLRNHLKQSMGFDTNMEGGFLARRRHLQALEQAAEHLQQGKAQLLGAWAGELLAEELRLAQQNLSEITGEFTSDDLLGRIFSSFCIGK,tRNA modification GTPase MnmE,"Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.",,7-fold decrease in GTPase activity and 6-fold increase of affinity.
220,220,186178,Q9ULZ3-L12Q,MGRARDAILDAQENLTAEELKKFKLKLLSVPLREGYGRIPRGALLSMDALDLTDKLVSFYLETYGAELTANVLRDMGLQEMAGQLQAATHQGSGAAPAGIQAPPQSAAKPGLHFIDQHRAALIARVTNVEWLLDALYGKVLTDEQYQAVRAEPTNPSKMRKLFSFTPAWNWTCKDLLLQALRESQSYLVEDLERS,Abolishes promotion of apoptosis and NF-kappa-B activation.,,MGRARDAILDALENLTAEELKKFKLKLLSVPLREGYGRIPRGALLSMDALDLTDKLVSFYLETYGAELTANVLRDMGLQEMAGQLQAATHQGSGAAPAGIQAPPQSAAKPGLHFIDQHRAALIARVTNVEWLLDALYGKVLTDEQYQAVRAEPTNPSKMRKLFSFTPAWNWTCKDLLLQALRESQSYLVEDLERS,Apoptosis-associated speck-like protein containing a CARD,"Functions as key mediator in apoptosis and inflammation. Promotes caspase-mediated apoptosis involving predominantly caspase-8 and also caspase-9 in a probable cell type-specific manner. Involved in activation of the mitochondrial apoptotic pathway, promotes caspase-8-dependent proteolytic maturation of BID independently of FADD in certain cell types and also mediates mitochondrial translocation of BAX and activates BAX-dependent apoptosis coupled to activation of caspase-9, -2 and -3. Involved in innate immune response by acting as an integral adapter in the assembly of various inflammasomes (NLRP1, NLRP2, NLRP3, NLRP6, AIM2 and probably IFI16) which recruit and activate caspase-1 leading to processing and secretion of pro-inflammatory cytokines. Caspase-1-dependent inflammation leads to macrophage pyroptosis, a form of cell death. The function as activating adapter in different types of inflammasomes is mediated by the pyrin and CARD domains and their homotypic interactions. Clustered PYCARD nucleates the formation of caspase-1 filaments through the interaction of their respective CARD domains, acting as a platform for of caspase-1 polymerization. In the NLRP1 and NLRC4 inflammasomes seems not be required but facilitates the processing of procaspase-1. In cooperation with NOD2 involved in an inflammasome activated by bacterial muramyl dipeptide leading to caspase-1 activation. May be involved in RIGI-triggered pro-inflammatory responses and inflammasome activation. In collaboration with AIM2 which detects cytosolic double-stranded DNA may also be involved in a caspase-1-independent cell death that involves caspase-8. In adaptive immunity may be involved in maturation of dendritic cells to stimulate T-cell immunity and in cytoskeletal rearrangements coupled to chemotaxis and antigen uptake may be involved in post-transcriptional regulation of the guanine nucleotide exchange factor DOCK2; the latter function is proposed to involve the nuclear form. Also involved in transcriptional activation of cytokines and chemokines independent of the inflammasome; this function may involve AP-1, NF-kappa-B, MAPK and caspase-8 signaling pathways. For regulation of NF-kappa-B activating and inhibiting functions have been reported. Modulates NF-kappa-B induction at the level of the IKK complex by inhibiting kinase activity of CHUK and IKBK. Proposed to compete with RIPK2 for association with CASP1 thereby down-regulating CASP1-mediated RIPK2-dependent NF-kappa-B activation and activating interleukin-1 beta processing. Modulates host resistance to DNA virus infection, probably by inducing the cleavage of and inactivating CGAS in presence of cytoplasmic double-stranded DNA.May have a regulating effect on the function as inflammasome adapter.Seems to inhibit inflammasome-mediated maturation of interleukin-1 beta.",Mutation of L12 to Q in ASC protein leads to loss of filament formation.,Abolishes promotion of apoptosis and NF-kappa-B activation. Mutation of L12 to Q in ASC protein leads to loss of filament formation.
221,221,188962,O14746-V170M,MPRAPRCRAVRSLLRSHYREVLPLATFVRRLGPQGWRLVQRGDPAAFRALVAQCLVCVPWDARPPPAAPSFRQVSCLKELVARVLQRLCERGAKNVLAFGFALLDGARGGPPEAFTTSVRSYLPNTVTDALRGSGAWGLLLRRVGDDVLVHLLARCALFVLVAPSCAYQMCGPPLYQLGAATQARPPPHASGPRRRLGCERAWNHSVREAGVPLGLPAPGARRRGGSASRSLPLPKRPRRGAAPEPERTPVGQGSWAHPGRTRGPSDRGFCVVSPARPAEEATSLEGALSGTRHSHPSVGRQHHAGPPSTSRPPRPWDTPCPPVYAETKHFLYSSGDKEQLRPSFLLSSLRPSLTGARRLVETIFLGSRPWMPGTPRRLPRLPQRYWQMRPLFLELLGNHAQCPYGVLLKTHCPLRAAVTPAAGVCAREKPQGSVAAPEEEDTDPRRLVQLLRQHSSPWQVYGFVRACLRRLVPPGLWGSRHNERRFLRNTKKFISLGKHAKLSLQELTWKMSVRDCAWLRRSPGVGCVPAAEHRLREEILAKFLHWLMSVYVVELLRSFFYVTETTFQKNRLFFYRKSVWSKLQSIGIRQHLKRVQLRELSEAEVRQHREARPALLTSRLRFIPKPDGLRPIVNMDYVVGARTFRREKRAERLTSRVKALFSVLNYERARRPGLLGASVLGLDDIHRAWRTFVLRVRAQDPPPELYFVKVDVTGAYDTIPQDRLTEVIASIIKPQNTYCVRRYAVVQKAAHGHVRKAFKSHVSTLTDLQPYMRQFVAHLQETSPLRDAVVIEQSSSLNEASSGLFDVFLRFMCHHAVRIRGKSYVQCQGIPQGSILSTLLCSLCYGDMENKLFAGIRRDGLLLRLVDDFLLVTPHLTHAKTFLRTLVRGVPEYGCVVNLRKTVVNFPVEDEALGGTAFVQMPAHGLFPWCGLLLDTRTLEVQSDYSSYARTSIRASLTFNRGFKAGRNMRRKLFGVLRLKCHSLFLDLQVNSLQTVCTNIYKILLLQAYRFHACVLQLPFHQQ,In PFBMFT1; the mutant protein is demonstrated to cause decreased telomerase activity.,,MPRAPRCRAVRSLLRSHYREVLPLATFVRRLGPQGWRLVQRGDPAAFRALVAQCLVCVPWDARPPPAAPSFRQVSCLKELVARVLQRLCERGAKNVLAFGFALLDGARGGPPEAFTTSVRSYLPNTVTDALRGSGAWGLLLRRVGDDVLVHLLARCALFVLVAPSCAYQVCGPPLYQLGAATQARPPPHASGPRRRLGCERAWNHSVREAGVPLGLPAPGARRRGGSASRSLPLPKRPRRGAAPEPERTPVGQGSWAHPGRTRGPSDRGFCVVSPARPAEEATSLEGALSGTRHSHPSVGRQHHAGPPSTSRPPRPWDTPCPPVYAETKHFLYSSGDKEQLRPSFLLSSLRPSLTGARRLVETIFLGSRPWMPGTPRRLPRLPQRYWQMRPLFLELLGNHAQCPYGVLLKTHCPLRAAVTPAAGVCAREKPQGSVAAPEEEDTDPRRLVQLLRQHSSPWQVYGFVRACLRRLVPPGLWGSRHNERRFLRNTKKFISLGKHAKLSLQELTWKMSVRDCAWLRRSPGVGCVPAAEHRLREEILAKFLHWLMSVYVVELLRSFFYVTETTFQKNRLFFYRKSVWSKLQSIGIRQHLKRVQLRELSEAEVRQHREARPALLTSRLRFIPKPDGLRPIVNMDYVVGARTFRREKRAERLTSRVKALFSVLNYERARRPGLLGASVLGLDDIHRAWRTFVLRVRAQDPPPELYFVKVDVTGAYDTIPQDRLTEVIASIIKPQNTYCVRRYAVVQKAAHGHVRKAFKSHVSTLTDLQPYMRQFVAHLQETSPLRDAVVIEQSSSLNEASSGLFDVFLRFMCHHAVRIRGKSYVQCQGIPQGSILSTLLCSLCYGDMENKLFAGIRRDGLLLRLVDDFLLVTPHLTHAKTFLRTLVRGVPEYGCVVNLRKTVVNFPVEDEALGGTAFVQMPAHGLFPWCGLLLDTRTLEVQSDYSSYARTSIRASLTFNRGFKAGRNMRRKLFGVLRLKCHSLFLDLQVNSLQTVCTNIYKILLLQAYRFHACVLQLPFHQQ,Telomerase reverse transcriptase,"Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. Active in progenitor and cancer cells. Inactive, or very low activity, in normal somatic cells. Catalytic component of the teleromerase holoenzyme complex whose main activity is the elongation of telomeres by acting as a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme. Catalyzes the RNA-dependent extension of 3'-chromosomal termini with the 6-nucleotide telomeric repeat unit, 5'-TTAGGG-3'. The catalytic cycle involves primer binding, primer extension and release of product once the template boundary has been reached or nascent product translocation followed by further extension. More active on substrates containing 2 or 3 telomeric repeats. Telomerase activity is regulated by a number of factors including telomerase complex-associated proteins, chaperones and polypeptide modifiers. Modulates Wnt signaling. Plays important roles in aging and antiapoptosis.","The mutation in the hTERT gene is associated with dyskeratosis congenita, a bone marrow failure syndrome characterized by mucocutaneous features. It can also be found in some cases of sporadic aplastic anemia (AA) and idiopathic pulmonary fibrosis. The presence of this mutation affects the clinical outcome and can be used for genetic testing.","In PFBMFT1; the mutant protein is demonstrated to cause decreased telomerase activity. The mutation in the hTERT gene is associated with dyskeratosis congenita, a bone marrow failure syndrome characterized by mucocutaneous features. It can also be found in some cases of sporadic aplastic anemia (AA) and idiopathic pulmonary fibrosis. The presence of this mutation affects the clinical outcome and can be used for genetic testing."
222,222,189244,Q6MZP7-C527Y,MEVVPAEVNSLLPEEIMDTGITLVDDDSIEAVIVSSPIPMETELEEIVNINSTGDSTATPISTEPITVYSNHTNQVAVNTTITKADSNTTVKPAFPSGLQKLGAQTPVTISANQIILNKVSQTSDLKLGNQTLKPDGQKLILTTLGKSGSPIVLALPHSQLPQAQKVTTQAQSGDAKLPPQQIKVVTIGGRPEVKPVIGVSALTPGSQLINTTTQPSVLQTQQLKTVQIAKKPRTPTSGPVITKLIFAKPINSKAVTGQTTQVSPPVIAGRVLSQSTPGTPSKTITISESGVIGSTLNSTTQTPNKIAISPLKSPNKAVKSTVQTITVGGVSTSQFKTIIPLATAPNVQQIQVPGSKFHYVRLVTATSASSSTQPVSQNPSTNTQPLQQAKPVVVNTTPVRMSVPIVSAQAVKQVVPKPINPTSQIVTTSQPQQRLIMPATPLPQIQPNLTNLPPGTVLAPAPGTGNVGYAVLPAQYVTQLQQSSYVSIASNSTFTGTSGIQTQARLPFNGIIPSESASRPRKPCNYTKSLCLKLYCDCFANGEFCNNCNCTNCYNNLEHENERQKAIKACLDRNPEAFKPKIGKGKEGESDRRHSKGCNCKRSGCLKNYCECYEAKIMCSSICKCIGCKNFEESPERKTLMHLADAAEVRVQQQTAAKTKLSSQISDLLTRPTPALNSGGGKLPFTFVTKEVAEATCNCLLAQAEQADKKGKSKAAAERMILEEFGRCLMSVINSAGKAKSDPCAMNC,Abolishes DNA-binding to the CDK1 promoter; when associated with Y-525.,,MEVVPAEVNSLLPEEIMDTGITLVDDDSIEAVIVSSPIPMETELEEIVNINSTGDSTATPISTEPITVYSNHTNQVAVNTTITKADSNTTVKPAFPSGLQKLGAQTPVTISANQIILNKVSQTSDLKLGNQTLKPDGQKLILTTLGKSGSPIVLALPHSQLPQAQKVTTQAQSGDAKLPPQQIKVVTIGGRPEVKPVIGVSALTPGSQLINTTTQPSVLQTQQLKTVQIAKKPRTPTSGPVITKLIFAKPINSKAVTGQTTQVSPPVIAGRVLSQSTPGTPSKTITISESGVIGSTLNSTTQTPNKIAISPLKSPNKAVKSTVQTITVGGVSTSQFKTIIPLATAPNVQQIQVPGSKFHYVRLVTATSASSSTQPVSQNPSTNTQPLQQAKPVVVNTTPVRMSVPIVSAQAVKQVVPKPINPTSQIVTTSQPQQRLIMPATPLPQIQPNLTNLPPGTVLAPAPGTGNVGYAVLPAQYVTQLQQSSYVSIASNSTFTGTSGIQTQARLPFNGIIPSESASRPRKPCNCTKSLCLKLYCDCFANGEFCNNCNCTNCYNNLEHENERQKAIKACLDRNPEAFKPKIGKGKEGESDRRHSKGCNCKRSGCLKNYCECYEAKIMCSSICKCIGCKNFEESPERKTLMHLADAAEVRVQQQTAAKTKLSSQISDLLTRPTPALNSGGGKLPFTFVTKEVAEATCNCLLAQAEQADKKGKSKAAAERMILEEFGRCLMSVINSAGKAKSDPCAMNC,Protein lin-54 homolog,"Component of the DREAM complex, a multiprotein complex that can both act as a transcription activator or repressor depending on the context. In G0 phase, the complex binds to more than 800 promoters and is required for repression of E2F target genes. In S phase, the complex selectively binds to the promoters of G2/M genes whose products are required for mitosis and participates in their cell cycle dependent activation. In the complex, acts as a DNA-binding protein that binds the promoter of CDK1 in a sequence-specific manner. Specifically recognizes the consensus motif 5'-TTYRAA-3' in target DNA.",The mutation in LIN54 is found to be required for cell cycle progression.,Abolishes DNA-binding to the CDK1 promoter; when associated with Y-525. The mutation in LIN54 is found to be required for cell cycle progression.
223,223,189313,P38516-K140A,MAQVDLLNVKGEKVGTLEISDFVFNIDPNYDVMWRYVDMQLSNRRAGTASTKTRGEVSGGGRKPWPQKHTGRARHGSIRSPIWRHGGVVHGPKPRDWSKKLNKKMKKLALRSALSVKYRENKLLVLDDLKLERPKTKSLAEILQNLQLSDKKTLIVLPWKEEGYMNVKLSGRNLPDVKVIIADNPNNSKNGEKAVRIDGLNVFDMLKYDYLVLTRDMVSKIEEVLGNEAGKALTA,"Able to regulate the E.coli S10 operon, but does not improve association with E.coli ribosome; when associated with E141Q, Q144K, Q147A, S149E, K151delta, K152delta, I155M, P158G, W159E and K160L.",,MAQVDLLNVKGEKVGTLEISDFVFNIDPNYDVMWRYVDMQLSNRRAGTASTKTRGEVSGGGRKPWPQKHTGRARHGSIRSPIWRHGGVVHGPKPRDWSKKLNKKMKKLALRSALSVKYRENKLLVLDDLKLERPKTKSLKEILQNLQLSDKKTLIVLPWKEEGYMNVKLSGRNLPDVKVIIADNPNNSKNGEKAVRIDGLNVFDMLKYDYLVLTRDMVSKIEEVLGNEAGKALTA,Large ribosomal subunit protein uL4,"One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome.This protein only weakly controls expression of the E.coli S10 operon. It is incorporated into E.coli ribosomes, however it is not as firmly associated as the endogenous protein.Forms part of the polypeptide exit tunnel.","The area around helices alpha4 and alpha5, which is critical for the initial folding steps of the large subunit, is also a central element of autogenous control, presumably by contacting the S10 mRNA leader.","Able to regulate the E.coli S10 operon, but does not improve association with E.coli ribosome; when associated with E141Q, Q144K, Q147A, S149E, K151delta, K152delta, I155M, P158G, W159E and K160L. The area around helices alpha4 and alpha5, which is critical for the initial folding steps of the large subunit, is also a central element of autogenous control, presumably by contacting the S10 mRNA leader."
224,224,189749,Q504J1-C296A,MEDITQLLSDVLEDLVESELKQFTRQLWIGVKPGVEPIPRGKLENKDRQDVVDSMVQQYSEDAGTITVQTLRKIKQNERAKRLESNLLKVQSQGQENKQNSEEPQPIPQIISQPIQQIISQPINNAGSEDLQPIQADWQRPRQIIPCSQETKNTLLKAHGDDIYTPRSGTQRKGLALLITNIQFANTQHNRNGADRDEENAEWLLRSLGFAVIKYRNLSGKDIRRAVENFSKRREHEDADSTFIVIMSHGTRIDNKDAIVGVSDDVYFIEETFSHLNSVNCPALIDKPKVILIQAARGGQSSGVLAQDSVFASDSWVHMEKDFVCFMSTMPNTFAYRNPIEGSFFISYIVDVFCSSAHRDDIMELFRKVTLRMEKDQRFQGQAKLLPCIERTSISKRFYLFPGL,Abolishes catalytic activity. Abolishes pyroptosis induced by bacterial lipopolysaccharides (LPS).,,MEDITQLLSDVLEDLVESELKQFTRQLWIGVKPGVEPIPRGKLENKDRQDVVDSMVQQYSEDAGTITVQTLRKIKQNERAKRLESNLLKVQSQGQENKQNSEEPQPIPQIISQPIQQIISQPINNAGSEDLQPIQADWQRPRQIIPCSQETKNTLLKAHGDDIYTPRSGTQRKGLALLITNIQFANTQHNRNGADRDEENAEWLLRSLGFAVIKYRNLSGKDIRRAVENFSKRREHEDADSTFIVIMSHGTRIDNKDAIVGVSDDVYFIEETFSHLNSVNCPALIDKPKVILIQACRGGQSSGVLAQDSVFASDSWVHMEKDFVCFMSTMPNTFAYRNPIEGSFFISYIVDVFCSSAHRDDIMELFRKVTLRMEKDQRFQGQAKLLPCIERTSISKRFYLFPGL,Caspase b,"Thiol protease which cleaves IL-1 beta (il1b), releasing the mature cytokine which is involved in a variety of inflammatory processes, and mediates apoptosis. Component of the NLRP1 inflammasome, which plays a crucial role in innate immunity and inflammation. In response to pathogens and other damage-associated signals, recruited to the NLRP1 inflammasome in its precursor form following the recruitment of caspase caspa. Its subsequent activation causes the cleavage of the midformed pro-il1b and results in il1b maturation and secretion in the extracellular milieu. Activated by direct binding to bacterial lipopolysaccharides (LPS), which causes non-canonical inflammasome activation and results in the pyroptosis of infected cells and their extrusion into the gut lumen, as well as in cytokine secretion. Plays a crucial role in the restriction of bacterial infection to intestinal sites. Pyroptosis limits bacterial replication, while cytokine secretion promotes the recruitment and activation of immune cells and triggers mucosal inflammation. Promotes pyroptosis by bacterial infection by E.piscicida.",,Abolishes catalytic activity. Abolishes pyroptosis induced by bacterial lipopolysaccharides (LPS).
225,225,189960,P16522-E85K,MNDDSQDKIIHDIRIQLRKAATELSRWKLYGSSKWAAEALAGLAEAIDVDQTHSLADESPLRNKQGVPKQMFEIPQNGFGLSETKYDLYLLGSTLFDAKEFDRCVFFLKDVTNPYLKFLKLYSKFLSWDKKSQESMENILTTGKFTDEMYRANKDGDGSGNEDINQSGHQRANLKMVSNEHESQSNISSILKEINTFLESYEIKIDDDEADLGLALLYYLRGVILKQEKNISKAMSSFLKSLSCYSFNWSCWLELMDCLQKVDDALLLNNYLYQNFQFKFSENLGSQRTIEFNIMIKFFKLKVFEELNGQLEDYFEDLEFLLQVFPNFTFLKAYNATISYNNLDYVTAESRFDDIVKQDPYRLNDLETYSNILYVMQKNSKLAYLAQFVSQIDRFRPETCCIIANYYSARQEHEKSIMYFRRALTLDKKTTNAWTLMGHEFVELSNSHAAIECYRRAVDICPRDFKAWFGLGQAYALLDMHLYSLYYFQKACTLKPWDRRIWQVLGECYSKTGNKVEAIKCYKRSIKASQTVDQNTSIYYRLAQLYEELEDLQECKKFMMKCVDVEELLEGIVTDETVKARLWLAIFEIKAGNYQLAYDYAMGVSSGTSQEIEEARMLARECRRHM,In CDC23-51; G2/M cell cycle arrest at 37 degrees Celsius.,,MNDDSQDKIIHDIRIQLRKAATELSRWKLYGSSKWAAEALAGLAEAIDVDQTHSLADESPLRNKQGVPKQMFEIPQNGFGLSETEYDLYLLGSTLFDAKEFDRCVFFLKDVTNPYLKFLKLYSKFLSWDKKSQESMENILTTGKFTDEMYRANKDGDGSGNEDINQSGHQRANLKMVSNEHESQSNISSILKEINTFLESYEIKIDDDEADLGLALLYYLRGVILKQEKNISKAMSSFLKSLSCYSFNWSCWLELMDCLQKVDDALLLNNYLYQNFQFKFSENLGSQRTIEFNIMIKFFKLKVFEELNGQLEDYFEDLEFLLQVFPNFTFLKAYNATISYNNLDYVTAESRFDDIVKQDPYRLNDLETYSNILYVMQKNSKLAYLAQFVSQIDRFRPETCCIIANYYSARQEHEKSIMYFRRALTLDKKTTNAWTLMGHEFVELSNSHAAIECYRRAVDICPRDFKAWFGLGQAYALLDMHLYSLYYFQKACTLKPWDRRIWQVLGECYSKTGNKVEAIKCYKRSIKASQTVDQNTSIYYRLAQLYEELEDLQECKKFMMKCVDVEELLEGIVTDETVKARLWLAIFEIKAGNYQLAYDYAMGVSSGTSQEIEEARMLARECRRHM,Anaphase-promoting complex subunit CDC23,"Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. In early mitosis, the APC/C is activated by CDC20 and targets securin PDS1, the B-type cyclin CLB5, and other anaphase inhibitory proteins for proteolysis, thereby triggering the separation of sister chromatids at the metaphase-to-anaphase transition. In late mitosis and in G1, degradation of CLB5 allows activation of the APC/C by CDH1, which is needed to destroy CDC20 and the B-type cyclin CLB2 to allow exit from mitosis and creating the low CDK state necessary for cytokinesis and for reforming prereplicative complexes in G1 prior to another round of replication.",The mutation in the CDC23 gene causes a single amino acid change in the protein. This mutation is found within a mutable domain of CDC23 and may affect its function or stability.,In CDC23-51; G2/M cell cycle arrest at 37 degrees Celsius. The mutation in the CDC23 gene causes a single amino acid change in the protein. This mutation is found within a mutable domain of CDC23 and may affect its function or stability.
226,226,190363,Q9ULZ3-P40A,MGRARDAILDALENLTAEELKKFKLKLLSVPLREGYGRIARGALLSMDALDLTDKLVSFYLETYGAELTANVLRDMGLQEMAGQLQAATHQGSGAAPAGIQAPPQSAAKPGLHFIDQHRAALIARVTNVEWLLDALYGKVLTDEQYQAVRAEPTNPSKMRKLFSFTPAWNWTCKDLLLQALRESQSYLVEDLERS,Abolishes homooligomerization.,,MGRARDAILDALENLTAEELKKFKLKLLSVPLREGYGRIPRGALLSMDALDLTDKLVSFYLETYGAELTANVLRDMGLQEMAGQLQAATHQGSGAAPAGIQAPPQSAAKPGLHFIDQHRAALIARVTNVEWLLDALYGKVLTDEQYQAVRAEPTNPSKMRKLFSFTPAWNWTCKDLLLQALRESQSYLVEDLERS,Apoptosis-associated speck-like protein containing a CARD,"Functions as key mediator in apoptosis and inflammation. Promotes caspase-mediated apoptosis involving predominantly caspase-8 and also caspase-9 in a probable cell type-specific manner. Involved in activation of the mitochondrial apoptotic pathway, promotes caspase-8-dependent proteolytic maturation of BID independently of FADD in certain cell types and also mediates mitochondrial translocation of BAX and activates BAX-dependent apoptosis coupled to activation of caspase-9, -2 and -3. Involved in innate immune response by acting as an integral adapter in the assembly of various inflammasomes (NLRP1, NLRP2, NLRP3, NLRP6, AIM2 and probably IFI16) which recruit and activate caspase-1 leading to processing and secretion of pro-inflammatory cytokines. Caspase-1-dependent inflammation leads to macrophage pyroptosis, a form of cell death. The function as activating adapter in different types of inflammasomes is mediated by the pyrin and CARD domains and their homotypic interactions. Clustered PYCARD nucleates the formation of caspase-1 filaments through the interaction of their respective CARD domains, acting as a platform for of caspase-1 polymerization. In the NLRP1 and NLRC4 inflammasomes seems not be required but facilitates the processing of procaspase-1. In cooperation with NOD2 involved in an inflammasome activated by bacterial muramyl dipeptide leading to caspase-1 activation. May be involved in RIGI-triggered pro-inflammatory responses and inflammasome activation. In collaboration with AIM2 which detects cytosolic double-stranded DNA may also be involved in a caspase-1-independent cell death that involves caspase-8. In adaptive immunity may be involved in maturation of dendritic cells to stimulate T-cell immunity and in cytoskeletal rearrangements coupled to chemotaxis and antigen uptake may be involved in post-transcriptional regulation of the guanine nucleotide exchange factor DOCK2; the latter function is proposed to involve the nuclear form. Also involved in transcriptional activation of cytokines and chemokines independent of the inflammasome; this function may involve AP-1, NF-kappa-B, MAPK and caspase-8 signaling pathways. For regulation of NF-kappa-B activating and inhibiting functions have been reported. Modulates NF-kappa-B induction at the level of the IKK complex by inhibiting kinase activity of CHUK and IKBK. Proposed to compete with RIPK2 for association with CASP1 thereby down-regulating CASP1-mediated RIPK2-dependent NF-kappa-B activation and activating interleukin-1 beta processing. Modulates host resistance to DNA virus infection, probably by inducing the cleavage of and inactivating CGAS in presence of cytoplasmic double-stranded DNA.May have a regulating effect on the function as inflammasome adapter.Seems to inhibit inflammasome-mediated maturation of interleukin-1 beta.",Mutation of P40 to A in ASC protein leads to loss of filament formation.,Abolishes homooligomerization. Mutation of P40 to A in ASC protein leads to loss of filament formation.
227,227,190477,Q9GYF0-Y576G,MRTSQAIFILIFLDSVRNQSPQVIPAKWDVVYEKETGHNMSLTVFRFQVKEQYSVARIIMSCNESTEHNPLLAVFREKLAILSLQVPLIVDNYEYSQVARTLCPFTEYKEGEAFTVEVTSSRPVHYNFRAELVQNFYLYNNSQRLVTASASEPVYLRYDIPGDVDSVAVHLDSNSTICMTVSVQKIGCPVFDLPDNVNSMGLHQTMTTSATIPVEKSRMSSFYVVFVVNTNDDLCSEILSIKPNKPTKFPLRMKSFNVTIESSMKIFDYTIPIVFWACILLLVTIVVFVYHYFDGIWERRFVSRAYTHLEDNAQEQRIRDFYDFQRMSEDDDLKDYDLLTDCQDMMVVRAKASLTVADLSMTPYEERELKYDVYKIALAIIGIFYNITVLQLIISKAGSLRQSGDLDECTFNFQCARPLWYFVAFNNVVSNGGYVYFGTLIIVMNYCRERSFRRLFAVQPTLAERYGLPQHSGLMTAIGLAVIMEGISSATYHVCPNNINYQFDTALMYVIGMLGKLKIWSLRHPDMVVSAYHAFGFLGVFLMAAIAGVYVHNMIFWALFSIIYIASMLLVSLEFGFKGIWTLNLRELRNSIRLSWVSSRHLSCVVPAYKARFFVILLLNIANTAVVVYGLEAHPKDFLSFLLIPFIGNLFIYIIYYILMKMIYREKIPKRAIALLFAAVISWTCAGILFNQRVSDWSKMPAISRELNKPCIFLNFYDNHDLWHLSSAFAIFFSFTAINVIDDDLMFVMRNTIRVF,Reduced interaction with cholesterol.,,MRTSQAIFILIFLDSVRNQSPQVIPAKWDVVYEKETGHNMSLTVFRFQVKEQYSVARIIMSCNESTEHNPLLAVFREKLAILSLQVPLIVDNYEYSQVARTLCPFTEYKEGEAFTVEVTSSRPVHYNFRAELVQNFYLYNNSQRLVTASASEPVYLRYDIPGDVDSVAVHLDSNSTICMTVSVQKIGCPVFDLPDNVNSMGLHQTMTTSATIPVEKSRMSSFYVVFVVNTNDDLCSEILSIKPNKPTKFPLRMKSFNVTIESSMKIFDYTIPIVFWACILLLVTIVVFVYHYFDGIWERRFVSRAYTHLEDNAQEQRIRDFYDFQRMSEDDDLKDYDLLTDCQDMMVVRAKASLTVADLSMTPYEERELKYDVYKIALAIIGIFYNITVLQLIISKAGSLRQSGDLDECTFNFQCARPLWYFVAFNNVVSNGGYVYFGTLIIVMNYCRERSFRRLFAVQPTLAERYGLPQHSGLMTAIGLAVIMEGISSATYHVCPNNINYQFDTALMYVIGMLGKLKIWSLRHPDMVVSAYHAFGFLGVFLMAAIAGVYVHNMIFWALFSIIYIASMLLVSLEFYFKGIWTLNLRELRNSIRLSWVSSRHLSCVVPAYKARFFVILLLNIANTAVVVYGLEAHPKDFLSFLLIPFIGNLFIYIIYYILMKMIYREKIPKRAIALLFAAVISWTCAGILFNQRVSDWSKMPAISRELNKPCIFLNFYDNHDLWHLSSAFAIFFSFTAINVIDDDLMFVMRNTIRVF,Cholesterol uptake protein 1,Cholesterol-binding protein which is involved in dietary cholesterol uptake from the environment. Does not play a role in double-stranded RNA transport in contrast to other SID1 family members.,"The mutation in the ChUP-1 protein is mentioned in the document. However, the functional changes caused by this mutation are not described in the document.","Reduced interaction with cholesterol. The mutation in the ChUP-1 protein is mentioned in the document. However, the functional changes caused by this mutation are not described in the document."
228,228,191088,A0A0H2URG7-N98A,MTIYNINLGIGWASSGVEYAQAYRAGVFRKLNLSSKFIFTDMILADNIQHLTANIGFDDNQVIWLYNHFTDIKIAPTSVTVDDVLAYFGGEESHREKAGKVLRVFFFDQDKFVTCYLVDENKDLVQHAEYVFKGNLIRKDYFSYTRYCSEYFAPKDNVAVLYQRTFYNEDGTPVYDILMNQGKEEVYHFKDKIFYGKQAFVRAFMKSLNLNKSDLVILDRETGIGQVVFEEAQTAHLAVVVHAEHYSENATNEDYILWNNYYDYQFTNADKVDFFIVSTDRQNEVLQEQFAKYTQHQPKIVTIPVGSIDSLTDSSQGRKPFSLITASRLAKEKHIDWLVKAVIEAHKELPELTFDIYGSGGEDSLLREIIANHQAEDYIQLKGHAELSQIYSQYEVYLTASTSEGFGLTLMEAIGSGLPLIGFDVPYGNQTFIEDGQNGYLIPSSSDHVEDQIKQAYAAKICQLYQENRLEAMRAYSYQIAEGFLTKEILEKWKKTVEEVLHD,"Decreased N-acetylglucosaminyl transferase activity, decreased binding of PsrP.",,MTIYNINLGIGWASSGVEYAQAYRAGVFRKLNLSSKFIFTDMILADNIQHLTANIGFDDNQVIWLYNHFTDIKIAPTSVTVDDVLAYFGGEESHREKNGKVLRVFFFDQDKFVTCYLVDENKDLVQHAEYVFKGNLIRKDYFSYTRYCSEYFAPKDNVAVLYQRTFYNEDGTPVYDILMNQGKEEVYHFKDKIFYGKQAFVRAFMKSLNLNKSDLVILDRETGIGQVVFEEAQTAHLAVVVHAEHYSENATNEDYILWNNYYDYQFTNADKVDFFIVSTDRQNEVLQEQFAKYTQHQPKIVTIPVGSIDSLTDSSQGRKPFSLITASRLAKEKHIDWLVKAVIEAHKELPELTFDIYGSGGEDSLLREIIANHQAEDYIQLKGHAELSQIYSQYEVYLTASTSEGFGLTLMEAIGSGLPLIGFDVPYGNQTFIEDGQNGYLIPSSSDHVEDQIKQAYAAKICQLYQENRLEAMRAYSYQIAEGFLTKEILEKWKKTVEEVLHD,UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase GtfA subunit,Required for the polymorphic O-glycosylation of serine-rich repeat protein PsrP. Catalyzes the first step in glycosylation by transferring N-acetylglucosamine from UDP-GlcNAc to serine residues in PsrP. Part of the accessory SecA2/SecY2 system specifically required to export serine-rich repeat cell wall proteins encoded upstream in the same operon (Probable). The GtfA-GtfB complex adds GlcNAc from UDP-GlcNAc to PsrP (experimentally characterized with truncated PsrP-SSR1 constructs); this subunit alone has weak N-acetylglucosaminyl transferase activity that is 10-fold stimulated by GtfB. The complex requires at least a 25 residue-long peptide for activity; the in vitro assay has only been seen to glycosylate Ser residues. The alpha linkage was shown in L.reuteri.,,"Decreased N-acetylglucosaminyl transferase activity, decreased binding of PsrP."
229,229,191405,Q6UWV6-N168Q,MRGPAVLLTVALATLLAPGAGAPVQSQGSQNKLLLVSFDGFRWNYDQDVDTPNLDAMARDGVKARYMTPAFVTMTSPCHFTLVTGKYIENHGVVHNMYYNTTSKVKLPYHATLGIQRWWDNGSVPIWITAQRQGLRAGSFFYPGGNVTYQGVAVTRSRKEGIAHNYKQETEWRANIDTVMAWFTEEDLDLVTLYFGEPDSTGHRYGPESPERREMVRQVDRTVGYLRESIARNHLTDRLNLIITSDHGMTTVDKRAGDLVEFHKFPNFTFRDIEFELLDYGPNGMLLPKEGRLEKVYDALKDAHPKLHVYKKEAFPEAFHYANNPRVTPLLMYSDLGYVIHGRINVQFNNGEHGFDNKDMDMKTIFRAVGPSFRAGLEVEPFESVHVYELMCRLLGIVPEANDGHLATLLPMLHTESALPPDGRPTLLPKGRSALPPSSRPLLVMGLLGTVILLSEVA,Strongly reduces N-glycosylation and enzyme activity; when associated with Q-100; Q-121; Q-168 and Q-267.,,MRGPAVLLTVALATLLAPGAGAPVQSQGSQNKLLLVSFDGFRWNYDQDVDTPNLDAMARDGVKARYMTPAFVTMTSPCHFTLVTGKYIENHGVVHNMYYNTTSKVKLPYHATLGIQRWWDNGSVPIWITAQRQGLRAGSFFYPGGNVTYQGVAVTRSRKEGIAHNYKNETEWRANIDTVMAWFTEEDLDLVTLYFGEPDSTGHRYGPESPERREMVRQVDRTVGYLRESIARNHLTDRLNLIITSDHGMTTVDKRAGDLVEFHKFPNFTFRDIEFELLDYGPNGMLLPKEGRLEKVYDALKDAHPKLHVYKKEAFPEAFHYANNPRVTPLLMYSDLGYVIHGRINVQFNNGEHGFDNKDMDMKTIFRAVGPSFRAGLEVEPFESVHVYELMCRLLGIVPEANDGHLATLLPMLHTESALPPDGRPTLLPKGRSALPPSSRPLLVMGLLGTVILLSEVA,Ectonucleotide pyrophosphatase/phosphodiesterase family member 7,"Choline-specific phosphodiesterase that hydrolyzes sphingomyelin releasing the ceramide and phosphocholine and therefore is involved in sphingomyelin digestion, ceramide formation, and fatty acid (FA) absorption in the gastrointestinal tract. Has also phospholipase C activity and can also cleave phosphocholine from palmitoyl lyso-phosphatidylcholine and platelet-activating factor (PAF) leading to its inactivation. Does not have nucleotide pyrophosphatase activity. May promote cholesterol absorption by affecting the levels of sphingomyelin derived from either diet or endogenous sources, in the intestinal lumen.",The mutation in alk-SMase severely affects its activity.,Strongly reduces N-glycosylation and enzyme activity; when associated with Q-100; Q-121; Q-168 and Q-267. The mutation in alk-SMase severely affects its activity.
230,230,191883,Q96MP8-R184C,MVVVTGREPDSRRQDGAMSSSDAEDDFLEPATPTATQAGHALPLLPQEFPEVVPLNIGGAHFTTRLSTLRCYEDTMLAAMFSGRHYIPTDSEGRYFIDRDGTHFGDVLNFLRSGDLPPRERVRAVYKEAQYYAIGPLLEQLENMQPLKGEKVRQAFLGLMPYYKDHLERIVEIARLRAVQRKACFAKLKVCVFKEEMPITPYECPLLNSLRFERSESDGQLFEHHCEVDVSFGPWEAVADVYDLLHCLVTDLSAQGLTVDHQCIGVCDKHLVNHYYCKRPIYEFKITWW,In EPM3; results in markedly diminished localization at the cell membrane and appearance of prominent cytoplasmic aggregates.,,MVVVTGREPDSRRQDGAMSSSDAEDDFLEPATPTATQAGHALPLLPQEFPEVVPLNIGGAHFTTRLSTLRCYEDTMLAAMFSGRHYIPTDSEGRYFIDRDGTHFGDVLNFLRSGDLPPRERVRAVYKEAQYYAIGPLLEQLENMQPLKGEKVRQAFLGLMPYYKDHLERIVEIARLRAVQRKARFAKLKVCVFKEEMPITPYECPLLNSLRFERSESDGQLFEHHCEVDVSFGPWEAVADVYDLLHCLVTDLSAQGLTVDHQCIGVCDKHLVNHYYCKRPIYEFKITWW,BTB/POZ domain-containing protein KCTD7,May be involved in the control of excitability of cortical neurons.,"The identified variant altered the localization pattern of KCTD7 and abrogated interaction with cullin-3, a ubiquitin-ligase component and known KCTD7 interactor. This study clearly demonstrates that KCTD7 mutations also cause a rare, infantile-onset NCL subtype designated as CLN14.","In EPM3; results in markedly diminished localization at the cell membrane and appearance of prominent cytoplasmic aggregates. The identified variant altered the localization pattern of KCTD7 and abrogated interaction with cullin-3, a ubiquitin-ligase component and known KCTD7 interactor. This study clearly demonstrates that KCTD7 mutations also cause a rare, infantile-onset NCL subtype designated as CLN14."
231,231,191933,P25522-D253A,MSDNDTIVAQATPPGRGGVGILRISGFKAREVAETVLGKLPKPRYADYLPFKDADGSVLDQGIALWFPGPNSFTGEDVLELQGHGGPVILDLLLKRILTIPGLRIARPGEFSERAFLNDKLDLAQAEAIADLIDASSEQAARSALNSLQGAFSARVNHLVEALTHLRIYVEAAIDFPDEEIDFLSDGKIEAQLNDVIADLDAVRAEARQGSLLREGMKVVIAGRPNAGKSSLLNALAGREAAIVTDIAGTTRAVLREHIHIDGMPLHIIDTAGLREASDEVERIGIERAWQEIEQADRVLFMVDGTTTDAVDPAEIWPEFIARLPAKLPITVVRNKADITGETLGMSEVNGHALIRLSARTGEGVDVLRNHLKQSMGFDTNMEGGFLARRRHLQALEQAAEHLQQGKAQLLGAWAGELLAEELRLAQQNLSEITGEFTSDDLLGRIFSSFCIGK,9-fold decrease in GTPase activity and 13-fold increase of affinity.,,MSDNDTIVAQATPPGRGGVGILRISGFKAREVAETVLGKLPKPRYADYLPFKDADGSVLDQGIALWFPGPNSFTGEDVLELQGHGGPVILDLLLKRILTIPGLRIARPGEFSERAFLNDKLDLAQAEAIADLIDASSEQAARSALNSLQGAFSARVNHLVEALTHLRIYVEAAIDFPDEEIDFLSDGKIEAQLNDVIADLDAVRAEARQGSLLREGMKVVIAGRPNAGKSSLLNALAGREAAIVTDIAGTTRDVLREHIHIDGMPLHIIDTAGLREASDEVERIGIERAWQEIEQADRVLFMVDGTTTDAVDPAEIWPEFIARLPAKLPITVVRNKADITGETLGMSEVNGHALIRLSARTGEGVDVLRNHLKQSMGFDTNMEGGFLARRRHLQALEQAAEHLQQGKAQLLGAWAGELLAEELRLAQQNLSEITGEFTSDDLLGRIFSSFCIGK,tRNA modification GTPase MnmE,"Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.","Residues in the G2 motif (249GTTRD253), which resides in the switch I region, are not important for GTP binding but play some role in stabilizing the transition state.","9-fold decrease in GTPase activity and 13-fold increase of affinity. Residues in the G2 motif (249GTTRD253), which resides in the switch I region, are not important for GTP binding but play some role in stabilizing the transition state."
232,232,192146,P51843-L381H,MAGENHQWQGSILYNMLMSAKQTRAAPEAPETRLVDQCWGCSCGDEPGVGREGLLGGRNVALLYRCCFCGKDHPRQGSILYSMLTSAKQTYAAPKAPEATLGPCWGCSCGSDPGVGRAGLPGGRPVALLYRCCFCGEDHPRQGSILYSLLTSSKQTHVAPAAPEARPGGAWWDRSYFAQRPGGKEALPGGRATALLYRCCFCGEDHPQQGSTLYCVPTSTNQAQAAPEERPRAPWWDTSSGALRPVALKSPQVVCEAASAGLLKTLRFVKYLPCFQVLPLDQQLVLVRNCWASLLMLELAQDRLQFETVEVSEPSMLQKILTTRRRETGGNEPLPVPTLQHHLAPPAEARKVPSASQVQAIKCFLSKCWSLNISTKEYAYHKGTVLFNPDVPGLQCVKYIQGLQWGTQQILSEHTRMTHQGPHDRFIELNSTLFLLRFINANVIAELFFRPIIGTVSMDDMMLEMLCTKI,In AHC.,,MAGENHQWQGSILYNMLMSAKQTRAAPEAPETRLVDQCWGCSCGDEPGVGREGLLGGRNVALLYRCCFCGKDHPRQGSILYSMLTSAKQTYAAPKAPEATLGPCWGCSCGSDPGVGRAGLPGGRPVALLYRCCFCGEDHPRQGSILYSLLTSSKQTHVAPAAPEARPGGAWWDRSYFAQRPGGKEALPGGRATALLYRCCFCGEDHPQQGSTLYCVPTSTNQAQAAPEERPRAPWWDTSSGALRPVALKSPQVVCEAASAGLLKTLRFVKYLPCFQVLPLDQQLVLVRNCWASLLMLELAQDRLQFETVEVSEPSMLQKILTTRRRETGGNEPLPVPTLQHHLAPPAEARKVPSASQVQAIKCFLSKCWSLNISTKEYAYLKGTVLFNPDVPGLQCVKYIQGLQWGTQQILSEHTRMTHQGPHDRFIELNSTLFLLRFINANVIAELFFRPIIGTVSMDDMMLEMLCTKI,Nuclear receptor subfamily 0 group B member 1,Orphan nuclear receptor. Component of a cascade required for the development of the hypothalamic-pituitary-adrenal-gonadal axis. Acts as a coregulatory protein that inhibits the transcriptional activity of other nuclear receptors through heterodimeric interactions. May also have a role in the development of the embryo and in the maintenance of embryonic stem cell pluripotency.,A novel DAX1 mutation () was discovered in the asymptomatic 8-month-old brother of a boy with primary adrenal failure. The infant had impaired adrenal reserve despite normal basal adrenal steroid concentrations. This case highlights the value of genetic testing in children at risk of the development of X-linked adrenal hypoplasia congenita before the onset of a potentially life-threatening adrenal crisis.,In AHC. A novel DAX1 mutation () was discovered in the asymptomatic 8-month-old brother of a boy with primary adrenal failure. The infant had impaired adrenal reserve despite normal basal adrenal steroid concentrations. This case highlights the value of genetic testing in children at risk of the development of X-linked adrenal hypoplasia congenita before the onset of a potentially life-threatening adrenal crisis.
233,233,192476,P32266-E294K,MNASPVRLLILRRQLATHPAILYSSPYIKSPLVHLHSRMSNVHRSAHANALSFVITRRSISHFPKIISKIIRLPIYVGGGMAAAGSYIAYKMEEASSFTKDKLDRIKDLGESMKEKFNKMFSGDKSQDGGHGNDGTVPTATLIAATSLDDDESKRQGDPKDDDDEDDDDEDDENDSVDTTQDEMLNLTKQMIEIRTILNKVDSSSAHLTLPSIVVIGSQSSGKSSVLESIVGREFLPKGSNMVTRRPIELTLVNTPNSNNVTADFPSMRLYNIKDFKEVKRMLMELNMAVPTSKAVSEEPIQLTIKSSRVPDLSLVDLPGYIQVEAADQPIELKTKIRDLCEKYLTAPNIILAISAADVDLANSSALKASKAADPKGLRTIGVITKLDLVDPEKARSILNNKKYPLSMGYVGVITKTPSSINRKHLGLFGEAPSSSLSGIFSKGQHGQSSGEENTNGLKQIVSHQFEKAYFKENKKYFTNCQVSTKKLREKLIKILEISMSNALEPTSTLIQQELDDTSYLFKVEFNDRHLTPKSYLLNNIDVLKLGIKEFQEKFHRNELKSILRAELDQKVLDVLATRYWKDDNLQDLSSSKLESDTDMLYWHKKLELASSGLTKMGIGRLSTMLTTNAILKELDNILESTQLKNHELIKDLVSNTAINVLNSKYYSTADQVENCIKPFKYEIDLEERDWSLARQHSINLIKEELRQCNSRYQAIKNAVGSKKLANVMGYLENESNLQKETLGMSKLLLERGSEAIFLDKRCKVLSFRLKMLKNKCHSTIEKDRCPEVFLSAVSDKLTSTAVLFLNVELLSDFFYNFPIELDRRLTLLGDEQVEMFAKEDPKISRHIELQKRKELLELALEKIDSILVFKKSYKGVSKNL,In mdm17; loss of function at 37 degrees Celsius.,,MNASPVRLLILRRQLATHPAILYSSPYIKSPLVHLHSRMSNVHRSAHANALSFVITRRSISHFPKIISKIIRLPIYVGGGMAAAGSYIAYKMEEASSFTKDKLDRIKDLGESMKEKFNKMFSGDKSQDGGHGNDGTVPTATLIAATSLDDDESKRQGDPKDDDDEDDDDEDDENDSVDTTQDEMLNLTKQMIEIRTILNKVDSSSAHLTLPSIVVIGSQSSGKSSVLESIVGREFLPKGSNMVTRRPIELTLVNTPNSNNVTADFPSMRLYNIKDFKEVKRMLMELNMAVPTSEAVSEEPIQLTIKSSRVPDLSLVDLPGYIQVEAADQPIELKTKIRDLCEKYLTAPNIILAISAADVDLANSSALKASKAADPKGLRTIGVITKLDLVDPEKARSILNNKKYPLSMGYVGVITKTPSSINRKHLGLFGEAPSSSLSGIFSKGQHGQSSGEENTNGLKQIVSHQFEKAYFKENKKYFTNCQVSTKKLREKLIKILEISMSNALEPTSTLIQQELDDTSYLFKVEFNDRHLTPKSYLLNNIDVLKLGIKEFQEKFHRNELKSILRAELDQKVLDVLATRYWKDDNLQDLSSSKLESDTDMLYWHKKLELASSGLTKMGIGRLSTMLTTNAILKELDNILESTQLKNHELIKDLVSNTAINVLNSKYYSTADQVENCIKPFKYEIDLEERDWSLARQHSINLIKEELRQCNSRYQAIKNAVGSKKLANVMGYLENESNLQKETLGMSKLLLERGSEAIFLDKRCKVLSFRLKMLKNKCHSTIEKDRCPEVFLSAVSDKLTSTAVLFLNVELLSDFFYNFPIELDRRLTLLGDEQVEMFAKEDPKISRHIELQKRKELLELALEKIDSILVFKKSYKGVSKNL,"Dynamin-like GTPase MGM1, mitochondrial",Dynamin-related GTPase required for mitochondrial fusion. Coordinates interaction between the inner and outer mitochondrial membrane to promote the formation of the double membrane.,A version of mgm1 mutated in a conserved residue in the putative GTP-binding site was unable to complement any of the mutant defects. It also caused aberrant mitochondrial distribution and morphology when expressed at high levels in cells that also contained a wild-type copy of the gene. Mgm1p was localized to the mitochondrial outer membrane and fractionated as a component of a high molecular weight complex.,In mdm17; loss of function at 37 degrees Celsius. A version of mgm1 mutated in a conserved residue in the putative GTP-binding site was unable to complement any of the mutant defects. It also caused aberrant mitochondrial distribution and morphology when expressed at high levels in cells that also contained a wild-type copy of the gene. Mgm1p was localized to the mitochondrial outer membrane and fractionated as a component of a high molecular weight complex.
234,234,192748,P16522-P326L,MNDDSQDKIIHDIRIQLRKAATELSRWKLYGSSKWAAEALAGLAEAIDVDQTHSLADESPLRNKQGVPKQMFEIPQNGFGLSETEYDLYLLGSTLFDAKEFDRCVFFLKDVTNPYLKFLKLYSKFLSWDKKSQESMENILTTGKFTDEMYRANKDGDGSGNEDINQSGHQRANLKMVSNEHESQSNISSILKEINTFLESYEIKIDDDEADLGLALLYYLRGVILKQEKNISKAMSSFLKSLSCYSFNWSCWLELMDCLQKVDDALLLNNYLYQNFQFKFSENLGSQRTIEFNIMIKFFKLKVFEELNGQLEDYFEDLEFLLQVFLNFTFLKAYNATISYNNLDYVTAESRFDDIVKQDPYRLNDLETYSNILYVMQKNSKLAYLAQFVSQIDRFRPETCCIIANYYSARQEHEKSIMYFRRALTLDKKTTNAWTLMGHEFVELSNSHAAIECYRRAVDICPRDFKAWFGLGQAYALLDMHLYSLYYFQKACTLKPWDRRIWQVLGECYSKTGNKVEAIKCYKRSIKASQTVDQNTSIYYRLAQLYEELEDLQECKKFMMKCVDVEELLEGIVTDETVKARLWLAIFEIKAGNYQLAYDYAMGVSSGTSQEIEEARMLARECRRHM,In CDC23-49; G2/M cell cycle arrest at 37 degrees Celsius; when associated with E-306.,,MNDDSQDKIIHDIRIQLRKAATELSRWKLYGSSKWAAEALAGLAEAIDVDQTHSLADESPLRNKQGVPKQMFEIPQNGFGLSETEYDLYLLGSTLFDAKEFDRCVFFLKDVTNPYLKFLKLYSKFLSWDKKSQESMENILTTGKFTDEMYRANKDGDGSGNEDINQSGHQRANLKMVSNEHESQSNISSILKEINTFLESYEIKIDDDEADLGLALLYYLRGVILKQEKNISKAMSSFLKSLSCYSFNWSCWLELMDCLQKVDDALLLNNYLYQNFQFKFSENLGSQRTIEFNIMIKFFKLKVFEELNGQLEDYFEDLEFLLQVFPNFTFLKAYNATISYNNLDYVTAESRFDDIVKQDPYRLNDLETYSNILYVMQKNSKLAYLAQFVSQIDRFRPETCCIIANYYSARQEHEKSIMYFRRALTLDKKTTNAWTLMGHEFVELSNSHAAIECYRRAVDICPRDFKAWFGLGQAYALLDMHLYSLYYFQKACTLKPWDRRIWQVLGECYSKTGNKVEAIKCYKRSIKASQTVDQNTSIYYRLAQLYEELEDLQECKKFMMKCVDVEELLEGIVTDETVKARLWLAIFEIKAGNYQLAYDYAMGVSSGTSQEIEEARMLARECRRHM,Anaphase-promoting complex subunit CDC23,"Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. In early mitosis, the APC/C is activated by CDC20 and targets securin PDS1, the B-type cyclin CLB5, and other anaphase inhibitory proteins for proteolysis, thereby triggering the separation of sister chromatids at the metaphase-to-anaphase transition. In late mitosis and in G1, degradation of CLB5 allows activation of the APC/C by CDH1, which is needed to destroy CDC20 and the B-type cyclin CLB2 to allow exit from mitosis and creating the low CDK state necessary for cytokinesis and for reforming prereplicative complexes in G1 prior to another round of replication.",,In CDC23-49; G2/M cell cycle arrest at 37 degrees Celsius; when associated with E-306.
235,235,193021,P16522-A39T,MNDDSQDKIIHDIRIQLRKAATELSRWKLYGSSKWAAETLAGLAEAIDVDQTHSLADESPLRNKQGVPKQMFEIPQNGFGLSETEYDLYLLGSTLFDAKEFDRCVFFLKDVTNPYLKFLKLYSKFLSWDKKSQESMENILTTGKFTDEMYRANKDGDGSGNEDINQSGHQRANLKMVSNEHESQSNISSILKEINTFLESYEIKIDDDEADLGLALLYYLRGVILKQEKNISKAMSSFLKSLSCYSFNWSCWLELMDCLQKVDDALLLNNYLYQNFQFKFSENLGSQRTIEFNIMIKFFKLKVFEELNGQLEDYFEDLEFLLQVFPNFTFLKAYNATISYNNLDYVTAESRFDDIVKQDPYRLNDLETYSNILYVMQKNSKLAYLAQFVSQIDRFRPETCCIIANYYSARQEHEKSIMYFRRALTLDKKTTNAWTLMGHEFVELSNSHAAIECYRRAVDICPRDFKAWFGLGQAYALLDMHLYSLYYFQKACTLKPWDRRIWQVLGECYSKTGNKVEAIKCYKRSIKASQTVDQNTSIYYRLAQLYEELEDLQECKKFMMKCVDVEELLEGIVTDETVKARLWLAIFEIKAGNYQLAYDYAMGVSSGTSQEIEEARMLARECRRHM,In CDC23-50; G2/M cell cycle arrest at 37 degrees Celsius.,,MNDDSQDKIIHDIRIQLRKAATELSRWKLYGSSKWAAEALAGLAEAIDVDQTHSLADESPLRNKQGVPKQMFEIPQNGFGLSETEYDLYLLGSTLFDAKEFDRCVFFLKDVTNPYLKFLKLYSKFLSWDKKSQESMENILTTGKFTDEMYRANKDGDGSGNEDINQSGHQRANLKMVSNEHESQSNISSILKEINTFLESYEIKIDDDEADLGLALLYYLRGVILKQEKNISKAMSSFLKSLSCYSFNWSCWLELMDCLQKVDDALLLNNYLYQNFQFKFSENLGSQRTIEFNIMIKFFKLKVFEELNGQLEDYFEDLEFLLQVFPNFTFLKAYNATISYNNLDYVTAESRFDDIVKQDPYRLNDLETYSNILYVMQKNSKLAYLAQFVSQIDRFRPETCCIIANYYSARQEHEKSIMYFRRALTLDKKTTNAWTLMGHEFVELSNSHAAIECYRRAVDICPRDFKAWFGLGQAYALLDMHLYSLYYFQKACTLKPWDRRIWQVLGECYSKTGNKVEAIKCYKRSIKASQTVDQNTSIYYRLAQLYEELEDLQECKKFMMKCVDVEELLEGIVTDETVKARLWLAIFEIKAGNYQLAYDYAMGVSSGTSQEIEEARMLARECRRHM,Anaphase-promoting complex subunit CDC23,"Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. In early mitosis, the APC/C is activated by CDC20 and targets securin PDS1, the B-type cyclin CLB5, and other anaphase inhibitory proteins for proteolysis, thereby triggering the separation of sister chromatids at the metaphase-to-anaphase transition. In late mitosis and in G1, degradation of CLB5 allows activation of the APC/C by CDH1, which is needed to destroy CDC20 and the B-type cyclin CLB2 to allow exit from mitosis and creating the low CDK state necessary for cytokinesis and for reforming prereplicative complexes in G1 prior to another round of replication.",,In CDC23-50; G2/M cell cycle arrest at 37 degrees Celsius.
236,236,194596,Q9HAY6-T170M,MDIIFGRNRKEQLEPVRAKVTGKIPAWLQGTLLRNGPGMHTVGESRYNHWFDGLALLHSFTIRDGEVYYRSKYLRSDTYNTNIEANRIVVSEFGTMAYPDPCKNIFSKAFSYLSHTIPDFTDNCLINIMKCGEDFYATSETNYIRKINPQTLETLEKVDYRKYVAVNLAMSHPHYDEAGNVLNMGTSIVEKGKTKYVIFKIPATVPEGKKQGKSPWKHTEVFCSIPSRSLLSPSYYHSFGVTENYVIFLEQPFRLDILKMATAYIRRMSWASCLAFHREEKTYIHIIDQRTRQPVQTKFYTDAMVVFHHVNAYEEDGCIVFDVIAYEDNSLYQLFYLANLNQDFKENSRLTSVPTLRRFAVPLHVDKNAEVGTNLIKVASTTATALKEEDGQVYCQPEFLYEGLELPRVNYAHNGKQYRYVFATGVQWSPIPTKIIKYDILTKSSLKWREDDCWPAEPLFVPAPGAKDEDDGVILSAIVSTDPQKLPFLLILDAKSFTELARASVDVDMHMDLHGLFITDMDWDTKKQAASEEQRDRASDCHGAPLT,"In HCVAD; decreased beta-carotene 15,15'-monooxygenase activity; 90% decrease compared to wild-type; decreased catalytic efficiency; no effect on affinity for all-trans-beta-carotene.",,MDIIFGRNRKEQLEPVRAKVTGKIPAWLQGTLLRNGPGMHTVGESRYNHWFDGLALLHSFTIRDGEVYYRSKYLRSDTYNTNIEANRIVVSEFGTMAYPDPCKNIFSKAFSYLSHTIPDFTDNCLINIMKCGEDFYATSETNYIRKINPQTLETLEKVDYRKYVAVNLATSHPHYDEAGNVLNMGTSIVEKGKTKYVIFKIPATVPEGKKQGKSPWKHTEVFCSIPSRSLLSPSYYHSFGVTENYVIFLEQPFRLDILKMATAYIRRMSWASCLAFHREEKTYIHIIDQRTRQPVQTKFYTDAMVVFHHVNAYEEDGCIVFDVIAYEDNSLYQLFYLANLNQDFKENSRLTSVPTLRRFAVPLHVDKNAEVGTNLIKVASTTATALKEEDGQVYCQPEFLYEGLELPRVNYAHNGKQYRYVFATGVQWSPIPTKIIKYDILTKSSLKWREDDCWPAEPLFVPAPGAKDEDDGVILSAIVSTDPQKLPFLLILDAKSFTELARASVDVDMHMDLHGLFITDMDWDTKKQAASEEQRDRASDCHGAPLT,"Beta,beta-carotene 15,15'-dioxygenase",Symmetrically cleaves beta-carotene into two molecules of retinal using a dioxygenase mechanism.,"The replacement of a highly conserved threonine with methionine results in a 90% reduction in enzyme activity when analyzed in vitro using purified recombinant enzymes. The Michaelis-Menten constant (K(m)) for the mutated enzyme is normal. Ample amounts of carotenoids are present in plasma of persons consuming a normal Western diet, suggesting that the enzyme is saturated with substrate under normal conditions. Therefore, we propose that haploinsufficiency of the CMO1 enzyme may cause symptoms of hypercarotenemia and hypovitaminosis A in individuals consuming a carotenoid-containing and vitamin A-deficient diet.","In HCVAD; decreased beta-carotene 15,15'-monooxygenase activity; 90% decrease compared to wild-type; decreased catalytic efficiency; no effect on affinity for all-trans-beta-carotene. The replacement of a highly conserved threonine with methionine results in a 90% reduction in enzyme activity when analyzed in vitro using purified recombinant enzymes. The Michaelis-Menten constant (K(m)) for the mutated enzyme is normal. Ample amounts of carotenoids are present in plasma of persons consuming a normal Western diet, suggesting that the enzyme is saturated with substrate under normal conditions. Therefore, we propose that haploinsufficiency of the CMO1 enzyme may cause symptoms of hypercarotenemia and hypovitaminosis A in individuals consuming a carotenoid-containing and vitamin A-deficient diet."
237,237,198947,Q96MP8-R84W,MVVVTGREPDSRRQDGAMSSSDAEDDFLEPATPTATQAGHALPLLPQEFPEVVPLNIGGAHFTTRLSTLRCYEDTMLAAMFSGWHYIPTDSEGRYFIDRDGTHFGDVLNFLRSGDLPPRERVRAVYKEAQYYAIGPLLEQLENMQPLKGEKVRQAFLGLMPYYKDHLERIVEIARLRAVQRKARFAKLKVCVFKEEMPITPYECPLLNSLRFERSESDGQLFEHHCEVDVSFGPWEAVADVYDLLHCLVTDLSAQGLTVDHQCIGVCDKHLVNHYYCKRPIYEFKITWW,Probable disease-associated variant found in a patient with opsoclonus-myoclonus ataxia-like syndrome.,,MVVVTGREPDSRRQDGAMSSSDAEDDFLEPATPTATQAGHALPLLPQEFPEVVPLNIGGAHFTTRLSTLRCYEDTMLAAMFSGRHYIPTDSEGRYFIDRDGTHFGDVLNFLRSGDLPPRERVRAVYKEAQYYAIGPLLEQLENMQPLKGEKVRQAFLGLMPYYKDHLERIVEIARLRAVQRKARFAKLKVCVFKEEMPITPYECPLLNSLRFERSESDGQLFEHHCEVDVSFGPWEAVADVYDLLHCLVTDLSAQGLTVDHQCIGVCDKHLVNHYYCKRPIYEFKITWW,BTB/POZ domain-containing protein KCTD7,May be involved in the control of excitability of cortical neurons.,"The mutation affects a highly conserved segment of the predicted protein, changing a basic amino acid into neutral. The different phenotype broadens the spectrum of KCTD7-related diseases.","Probable disease-associated variant found in a patient with opsoclonus-myoclonus ataxia-like syndrome. The mutation affects a highly conserved segment of the predicted protein, changing a basic amino acid into neutral. The different phenotype broadens the spectrum of KCTD7-related diseases."
238,238,199118,Q14956-A110D,MECLYYFLGFLLLAARLPLDAAKRFHDVLGNERPSAYMREHNQLNGWSSDENDWNEKLYPVWKRGDMRWKNSWKGGRVQAVLTSDSPALVGSNITFAVNLIFPRCQKEDDNGNIVYEKNCRNEAGLSADPYVYNWTAWSEDSDGENGTGQSHHNVFPDGKPFPHHPGWRRWNFIYVFHTLGQYFQKLGRCSVRVSVNTANVTLGPQLMEVTVYRRHGRAYVPIAQVKDVYVVTDQIPVFVTMFQKNDRNSSDETFLKDLPIMFDVLIHDPSHFLNYSTINYKWSFGDNTGLFVSTNHTVNHTYVLNGTFSLNLTVKAAAPGPCPPPPPPPRPSKPTPSLATTLKSYDSNTPGPAGDNPLELSRIPDENCQINRYGHFQATITIVEGILEVNIIQMTDVLMPVPWPESSLIDFVVTCQGSIPTEVCTIISDPTCEITQNTVCSPVDVDEMCLLTVRRTFNGSGTYCVNLTLGDDTSLALTSTLISVPDRDPASPLRMANSALISVGCLAIFVTVISLLVYKKHKEYNPIENSPGNVVRSKGLSVFLNRAKAVFFPGNQEKDPLLKNQEFKGVS,In a breast cancer sample; somatic mutation.,,MECLYYFLGFLLLAARLPLDAAKRFHDVLGNERPSAYMREHNQLNGWSSDENDWNEKLYPVWKRGDMRWKNSWKGGRVQAVLTSDSPALVGSNITFAVNLIFPRCQKEDANGNIVYEKNCRNEAGLSADPYVYNWTAWSEDSDGENGTGQSHHNVFPDGKPFPHHPGWRRWNFIYVFHTLGQYFQKLGRCSVRVSVNTANVTLGPQLMEVTVYRRHGRAYVPIAQVKDVYVVTDQIPVFVTMFQKNDRNSSDETFLKDLPIMFDVLIHDPSHFLNYSTINYKWSFGDNTGLFVSTNHTVNHTYVLNGTFSLNLTVKAAAPGPCPPPPPPPRPSKPTPSLATTLKSYDSNTPGPAGDNPLELSRIPDENCQINRYGHFQATITIVEGILEVNIIQMTDVLMPVPWPESSLIDFVVTCQGSIPTEVCTIISDPTCEITQNTVCSPVDVDEMCLLTVRRTFNGSGTYCVNLTLGDDTSLALTSTLISVPDRDPASPLRMANSALISVGCLAIFVTVISLLVYKKHKEYNPIENSPGNVVRSKGLSVFLNRAKAVFFPGNQEKDPLLKNQEFKGVS,Transmembrane glycoprotein NMB,Could be a melanogenic enzyme.,,In a breast cancer sample; somatic mutation.
239,239,201790,P06022-L90S,MQHDLFEHDPAIRQLIGHIDNIPAPELESRWPRSVVDLIDVLENELKRQNVSNPRELARKQAVALSCFLGGRQFYIPCGDTILTALRDDSLYCQFNGRNMEELRRQYRLSQPQIYQIIARQRKLHTRRHQPDLFSPETPK,No effect on dimerization and DNA binding. Complete loss of dimerization and DNA-binding when associated with Arg-83.,,MQHDLFEHDPAIRQLIGHIDNIPAPELESRWPRSVVDLIDVLENELKRQNVSNPRELARKQAVALSCFLGGRQFYIPCGDTILTALRDDLLYCQFNGRNMEELRRQYRLSQPQIYQIIARQRKLHTRRHQPDLFSPETPK,Late transcription activator C,"Positive regulator of viral late genes transcription. Responsible for the transition from middle to late gene expression. Activates the Plys, PI, PP and Pmom late promoters thereby allowing the expression of viral endolysin and structural genes. Activates Pmom promoter by unwinding the DNA, thus realigning the promoter elements and recruiting the RNAP.",,No effect on dimerization and DNA binding. Complete loss of dimerization and DNA-binding when associated with Arg-83.
240,240,202234,Q0WRB0-A355L,MELNCVQFLRNKTILVTGATGFLAKVFVEKILRVQPNVKKLYLLVRASDNEAATKRLRTEVFEKELFKVLRQNLGDEKLNTLLYEKVVSVPGDIATDQLGINDSHLRERMQKEIDIVVNVAATTNFDERYDVGLGINTFGALNVLNFAKKCVKVQLLLHVSTAYVCGEKPGLIPEKPFIMEEIRNENGLQLDINLERELMKQRLKELNEQDCSEEDITLSMKELGMERAKLHGWPNTYVFTKSMGEMLLGKHKENLPLVIIRPTMITSTLSEPFPGWIEGLRTVDSVIIAYGKGVLKCFLVDVNSVCDMIPVDMVANAMITAAAKHAGGSGVHMVYHVGSSHQNPVTFGEIHEILVRYFTKNPLRSRNGSLITVSKVRFIPTMALFSLYMTLRYKLPLQLLKLVDIIYPWRNGDKYGDKNRKIELVMRLVELYEPYVLFKGIFDDRNTKSLCANQKEEEIKNTEKLMFDFDPKGINWGDYLTNIHISGLVTHVLKK,Catalyzes the formation of C16:0 fatty alcohol instead of C18:0; when associated with M-377.,,MELNCVQFLRNKTILVTGATGFLAKVFVEKILRVQPNVKKLYLLVRASDNEAATKRLRTEVFEKELFKVLRQNLGDEKLNTLLYEKVVSVPGDIATDQLGINDSHLRERMQKEIDIVVNVAATTNFDERYDVGLGINTFGALNVLNFAKKCVKVQLLLHVSTAYVCGEKPGLIPEKPFIMEEIRNENGLQLDINLERELMKQRLKELNEQDCSEEDITLSMKELGMERAKLHGWPNTYVFTKSMGEMLLGKHKENLPLVIIRPTMITSTLSEPFPGWIEGLRTVDSVIIAYGKGVLKCFLVDVNSVCDMIPVDMVANAMITAAAKHAGGSGVHMVYHVGSSHQNPVTFGEIHEIAVRYFTKNPLRSRNGSLITVSKVRFIPTMALFSLYMTLRYKLPLQLLKLVDIIYPWRNGDKYGDKNRKIELVMRLVELYEPYVLFKGIFDDRNTKSLCANQKEEEIKNTEKLMFDFDPKGINWGDYLTNIHISGLVTHVLKK,Probable fatty acyl-CoA reductase 5,"Catalyzes the reduction of fatty acyl-CoA to fatty alcohols. Catalyzes specifically the formation of C18:0 fatty alcohol. Provides the fatty alcohols required for synthesis of suberin in roots, seed coat and wound-induced leaf tissue. Provides the fatty alcohols required for synthesis of alkyl hydroxycinnamates in root waxes.",,Catalyzes the formation of C16:0 fatty alcohol instead of C18:0; when associated with M-377.
241,241,203232,Q9AQS0-H246A,MLSGILIAALLMTLWGGWQPDIAHASDEFDALRIKWATLLTGGPALDPADSDIAARTDKLAQDANDYWEDMDLSSSRTYIWYALRGNGTSDNVNAVYERLRTMALAATTVGSSLYGNADLKEDILDALDWLYVNSYNSTRSRSAYNWWHWQLGIPMSLNDIAVLLYDDISAARMATYMDTIDYFTPSIGLTGANRAWQAIVVGVRAVIVKDAVKLAAARNGLSGTGIFPYATGGDGFYADGSFVQATTFAYTGGYGSSVLETTANLMYLLSGSTWSVSDPNQSNVWQWIYEAYRPLLYKGAMMDMVRGREISRSYAQDHAVGHGIVASIVRLAQFAPAPHAAAFKQIAKRVIQEDTFSSFYGDVSTDTIRLAKAIVDDPSIAPAAAPNLYKQYAAMDRAVLQRPGFALGLALYSTRISSYESINSENGRGWYTGAGATYLYNQDLAQYSEDYWPTVDAYRIPGTTVASGTPIASGTGTSSWTGGVSLAGQYGASGMDLSYGAYNLSARKSWFMFDDEIVALGSGISSTAGIPIETVVDNRKLNGAGDNAWTANGAALSTGLGVAQTLTGVNWVHLAGNTADGSDIGYYFPGGATLQTKREARTGTWKQINNRPATPSTAVTRNYETMWIDHGTNPSGASYGYVLLPNKTSAQVGAYAADPAIEIVVNTSGVQSVKEKTLGLVGANFWTDTTQTADLITSNKKASVMTREIADERLEASVSDPTQANNGTIAIELARSAEGYSADPGITVTQLAPTIKFTVNVNGAKGKSFHASFQLGEDTSGPVDPGEPELPSVIVDNADSAGVTRTGTWKTASTQTDRYGANYLHDDNAGKGTKSVTFTPNLPIAGSYEVYLMWPAHFNREDAVQVDVGHASGTTRTAVDQRSGGGVWHSIGTYEFLAGSGGSVTIRNDALGSPDGYVVADAVKFVAVG,Loss of activity by 60%.,,MLSGILIAALLMTLWGGWQPDIAHASDEFDALRIKWATLLTGGPALDPADSDIAARTDKLAQDANDYWEDMDLSSSRTYIWYALRGNGTSDNVNAVYERLRTMALAATTVGSSLYGNADLKEDILDALDWLYVNSYNSTRSRSAYNWWHWQLGIPMSLNDIAVLLYDDISAARMATYMDTIDYFTPSIGLTGANRAWQAIVVGVRAVIVKDAVKLAAARNGLSGTGIFPYATGGDGFYADGSFVQHTTFAYTGGYGSSVLETTANLMYLLSGSTWSVSDPNQSNVWQWIYEAYRPLLYKGAMMDMVRGREISRSYAQDHAVGHGIVASIVRLAQFAPAPHAAAFKQIAKRVIQEDTFSSFYGDVSTDTIRLAKAIVDDPSIAPAAAPNLYKQYAAMDRAVLQRPGFALGLALYSTRISSYESINSENGRGWYTGAGATYLYNQDLAQYSEDYWPTVDAYRIPGTTVASGTPIASGTGTSSWTGGVSLAGQYGASGMDLSYGAYNLSARKSWFMFDDEIVALGSGISSTAGIPIETVVDNRKLNGAGDNAWTANGAALSTGLGVAQTLTGVNWVHLAGNTADGSDIGYYFPGGATLQTKREARTGTWKQINNRPATPSTAVTRNYETMWIDHGTNPSGASYGYVLLPNKTSAQVGAYAADPAIEIVVNTSGVQSVKEKTLGLVGANFWTDTTQTADLITSNKKASVMTREIADERLEASVSDPTQANNGTIAIELARSAEGYSADPGITVTQLAPTIKFTVNVNGAKGKSFHASFQLGEDTSGPVDPGEPELPSVIVDNADSAGVTRTGTWKTASTQTDRYGANYLHDDNAGKGTKSVTFTPNLPIAGSYEVYLMWPAHFNREDAVQVDVGHASGTTRTAVDQRSGGGVWHSIGTYEFLAGSGGSVTIRNDALGSPDGYVVADAVKFVAVG,Xanthan lyase,"Plays a role in xanthan depolymerization pathway by cleaving the linkage between the terminal mannosyl and glucuronyl residues of the side chain of xanthan to liberate pyruvylated mannose. Is highly specific for pyruvylated side-chains of xanthan and is not effective with hyaluronate, chondroitin A, gellan, heparin or pectin.",,Loss of activity by 60%.
242,242,204566,P06022-S110T,MQHDLFEHDPAIRQLIGHIDNIPAPELESRWPRSVVDLIDVLENELKRQNVSNPRELARKQAVALSCFLGGRQFYIPCGDTILTALRDDLLYCQFNGRNMEELRRQYRLTQPQIYQIIARQRKLHTRRHQPDLFSPETPK,Loss of DNA-binding activity.,,MQHDLFEHDPAIRQLIGHIDNIPAPELESRWPRSVVDLIDVLENELKRQNVSNPRELARKQAVALSCFLGGRQFYIPCGDTILTALRDDLLYCQFNGRNMEELRRQYRLSQPQIYQIIARQRKLHTRRHQPDLFSPETPK,Late transcription activator C,"Positive regulator of viral late genes transcription. Responsible for the transition from middle to late gene expression. Activates the Plys, PI, PP and Pmom late promoters thereby allowing the expression of viral endolysin and structural genes. Activates Pmom promoter by unwinding the DNA, thus realigning the promoter elements and recruiting the RNAP.",The mutant protein showed a reduced ability to activate the P(lys)-galK fusion.,Loss of DNA-binding activity. The mutant protein showed a reduced ability to activate the P(lys)-galK fusion.
243,243,205228,O14746-A279T,MPRAPRCRAVRSLLRSHYREVLPLATFVRRLGPQGWRLVQRGDPAAFRALVAQCLVCVPWDARPPPAAPSFRQVSCLKELVARVLQRLCERGAKNVLAFGFALLDGARGGPPEAFTTSVRSYLPNTVTDALRGSGAWGLLLRRVGDDVLVHLLARCALFVLVAPSCAYQVCGPPLYQLGAATQARPPPHASGPRRRLGCERAWNHSVREAGVPLGLPAPGARRRGGSASRSLPLPKRPRRGAAPEPERTPVGQGSWAHPGRTRGPSDRGFCVVSPARPTEEATSLEGALSGTRHSHPSVGRQHHAGPPSTSRPPRPWDTPCPPVYAETKHFLYSSGDKEQLRPSFLLSSLRPSLTGARRLVETIFLGSRPWMPGTPRRLPRLPQRYWQMRPLFLELLGNHAQCPYGVLLKTHCPLRAAVTPAAGVCAREKPQGSVAAPEEEDTDPRRLVQLLRQHSSPWQVYGFVRACLRRLVPPGLWGSRHNERRFLRNTKKFISLGKHAKLSLQELTWKMSVRDCAWLRRSPGVGCVPAAEHRLREEILAKFLHWLMSVYVVELLRSFFYVTETTFQKNRLFFYRKSVWSKLQSIGIRQHLKRVQLRELSEAEVRQHREARPALLTSRLRFIPKPDGLRPIVNMDYVVGARTFRREKRAERLTSRVKALFSVLNYERARRPGLLGASVLGLDDIHRAWRTFVLRVRAQDPPPELYFVKVDVTGAYDTIPQDRLTEVIASIIKPQNTYCVRRYAVVQKAAHGHVRKAFKSHVSTLTDLQPYMRQFVAHLQETSPLRDAVVIEQSSSLNEASSGLFDVFLRFMCHHAVRIRGKSYVQCQGIPQGSILSTLLCSLCYGDMENKLFAGIRRDGLLLRLVDDFLLVTPHLTHAKTFLRTLVRGVPEYGCVVNLRKTVVNFPVEDEALGGTAFVQMPAHGLFPWCGLLLDTRTLEVQSDYSSYARTSIRASLTFNRGFKAGRNMRRKLFGVLRLKCHSLFLDLQVNSLQTVCTNIYKILLLQAYRFHACVLQLPFHQQ,,,MPRAPRCRAVRSLLRSHYREVLPLATFVRRLGPQGWRLVQRGDPAAFRALVAQCLVCVPWDARPPPAAPSFRQVSCLKELVARVLQRLCERGAKNVLAFGFALLDGARGGPPEAFTTSVRSYLPNTVTDALRGSGAWGLLLRRVGDDVLVHLLARCALFVLVAPSCAYQVCGPPLYQLGAATQARPPPHASGPRRRLGCERAWNHSVREAGVPLGLPAPGARRRGGSASRSLPLPKRPRRGAAPEPERTPVGQGSWAHPGRTRGPSDRGFCVVSPARPAEEATSLEGALSGTRHSHPSVGRQHHAGPPSTSRPPRPWDTPCPPVYAETKHFLYSSGDKEQLRPSFLLSSLRPSLTGARRLVETIFLGSRPWMPGTPRRLPRLPQRYWQMRPLFLELLGNHAQCPYGVLLKTHCPLRAAVTPAAGVCAREKPQGSVAAPEEEDTDPRRLVQLLRQHSSPWQVYGFVRACLRRLVPPGLWGSRHNERRFLRNTKKFISLGKHAKLSLQELTWKMSVRDCAWLRRSPGVGCVPAAEHRLREEILAKFLHWLMSVYVVELLRSFFYVTETTFQKNRLFFYRKSVWSKLQSIGIRQHLKRVQLRELSEAEVRQHREARPALLTSRLRFIPKPDGLRPIVNMDYVVGARTFRREKRAERLTSRVKALFSVLNYERARRPGLLGASVLGLDDIHRAWRTFVLRVRAQDPPPELYFVKVDVTGAYDTIPQDRLTEVIASIIKPQNTYCVRRYAVVQKAAHGHVRKAFKSHVSTLTDLQPYMRQFVAHLQETSPLRDAVVIEQSSSLNEASSGLFDVFLRFMCHHAVRIRGKSYVQCQGIPQGSILSTLLCSLCYGDMENKLFAGIRRDGLLLRLVDDFLLVTPHLTHAKTFLRTLVRGVPEYGCVVNLRKTVVNFPVEDEALGGTAFVQMPAHGLFPWCGLLLDTRTLEVQSDYSSYARTSIRASLTFNRGFKAGRNMRRKLFGVLRLKCHSLFLDLQVNSLQTVCTNIYKILLLQAYRFHACVLQLPFHQQ,Telomerase reverse transcriptase,"Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. Active in progenitor and cancer cells. Inactive, or very low activity, in normal somatic cells. Catalytic component of the teleromerase holoenzyme complex whose main activity is the elongation of telomeres by acting as a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme. Catalyzes the RNA-dependent extension of 3'-chromosomal termini with the 6-nucleotide telomeric repeat unit, 5'-TTAGGG-3'. The catalytic cycle involves primer binding, primer extension and release of product once the template boundary has been reached or nascent product translocation followed by further extension. More active on substrates containing 2 or 3 telomeric repeats. Telomerase activity is regulated by a number of factors including telomerase complex-associated proteins, chaperones and polypeptide modifiers. Modulates Wnt signaling. Plays important roles in aging and antiapoptosis.",Mutations in TERC cause short telomeres in congenital aplastic anemia and in some cases of apparently acquired hematopoietic failure.,Mutations in TERC cause short telomeres in congenital aplastic anemia and in some cases of apparently acquired hematopoietic failure.
244,244,205798,Q06069-S394I,MKEVIAVKEITRFKTRTEEFSPYAWCKRMLENDPVSYHEGTDTWNVFKYEDVKRVLSDYKHFSSVRKRTTISVGTDSEEGSVPEKIQITESDPPDHRKRRSLLAAAFTPRSLQNWEPRIQEIADELIGQMDGGTEIDIVASLASPLPIIVMADLMGVPSKDRLLFKKWVDTLFLPFDREKQEEVDKLKQVAAKEYYQYLYPIVVQKRLNPADDIISDLLKSEVDGEMFTDDEVVRTTMLILGAGVETTSHLLANSFYSLLYDDKEVYQELHENLDLVPQAVEEMLRFRFNLIKLDRTVKEDNDLLGVELKEGDSVVVWMSAANMDEEMFEDPFTLNIHRPNNKKHLTFGNGPHFCLGAPLARLEAKIALTAFLKKFKHIEAVPSFQLEENLTDIATGQTLTSLPLKASRM,30% of 15-beta hydroxylation activity (for progesterone).,,MKEVIAVKEITRFKTRTEEFSPYAWCKRMLENDPVSYHEGTDTWNVFKYEDVKRVLSDYKHFSSVRKRTTISVGTDSEEGSVPEKIQITESDPPDHRKRRSLLAAAFTPRSLQNWEPRIQEIADELIGQMDGGTEIDIVASLASPLPIIVMADLMGVPSKDRLLFKKWVDTLFLPFDREKQEEVDKLKQVAAKEYYQYLYPIVVQKRLNPADDIISDLLKSEVDGEMFTDDEVVRTTMLILGAGVETTSHLLANSFYSLLYDDKEVYQELHENLDLVPQAVEEMLRFRFNLIKLDRTVKEDNDLLGVELKEGDSVVVWMSAANMDEEMFEDPFTLNIHRPNNKKHLTFGNGPHFCLGAPLARLEAKIALTAFLKKFKHIEAVPSFQLEENLTDSATGQTLTSLPLKASRM,Cytochrome P450,Has the capacity to hydroxylate certain steroids in the 15-beta position. Also hydroxylates progesterone in the 11-alpha and 9-beta position.,The mutant was predicted to participate in active-site formation and influence substrate binding. This mutant altered the active-site structure and the hydroxylation activity of CYP106A2 dramatically.,30% of 15-beta hydroxylation activity (for progesterone). The mutant was predicted to participate in active-site formation and influence substrate binding. This mutant altered the active-site structure and the hydroxylation activity of CYP106A2 dramatically.
245,245,206603,Q8RXA7-S131F,MGRIFEYFVVCGLGPEMRTVDGDLGFHGMQTFYLPALLDQFPPTDQSPYPAPPPQLPTCVLPAGVEFHSSGFVSSDPASFPRSYPIVLTEGDGSKIFVSCIAFRDRVCEDIIEAYRLPPNTYADKCICLVFHAPNFRVLRNSLEEIFVLCFSSEGSCKPLWDIIAYMVSNVPLPTPGKDRVLFAVENCLLSVEAPPEDSLPQADISLQPLVQCLDVDNLIKLFTSVLVERRILIRSNKYSLLTLVSESICHLIYPFRWLQVYIPLLFFSGVDYIDAPTPYMMGLHSDVDTSNLAMDGVVVVDLDINQITTSEEIPQIPEPEFSTLRNDILKLLHPNVVAIDQLKGFGNSVEQCPKSLSKPWGEDHDLQLRVIFLKCFASILGGYRNFIENKVFSTDAFLKRRSRSTNQPPEPMLVQFLGSFAFLDYLERRLSSDEKSTNLLEKLQDAVGRGQDAMSILPKSSMEPEIITIAEPEVEESATRYTYDRFPASVRSEEQEEKRKQILAAASGALESNGRHPPSSPPGKNTKEDNFSSMERAAERERMVLDIQVKLQGLWLRLLKLGSDEDPLSSFEYGTILALIESDAEGIGGSGFIECIREHLYSGWHGQLSEEQFIAVKELLKMAVGRAASRSDLSTVRDALEVSAEMFKKDANNVSDYVQRHLISIPIWEELRFWEGYFEYLMEQPANESVNYATLVTARLIIVASHMAGLGLPDTEAWNMIETIAEKQKLGYKLLIKLRGFLSHVQQLRVGYWGASSFKQQAISAGLPSPRPKDVSVSDETQQPSEASGRSWVQSMFSRDTASRANSFSRVRKWVSDNASSDITAAAQKKIQTNVRVLKGHGGAVTALHSVTRREVCDLVGDREDAGFFISGSTDCLVKIWDPSLRGSELRATLKGHTGTVRAISSDRGKIVSGSDDLSVIVWDKQTTQLLEELKGHDSQVSCVKMLSGERVLTAAHDGTVKMWDVRTDMCVATVGRCSSAILSLEYDDSTGILAAAGRDTVANIWDIRSGKQMHKLKGHTKW,In scd1-1; temperature sensitive mutant with normal growth at the permissive temperature of 16 degrees Celsius and growth defects and sterility due to defective cytokinesis in guard cells and leaf epidermal cells at 22 degrees Celsius.,,MGRIFEYFVVCGLGPEMRTVDGDLGFHGMQTFYLPALLDQFPPTDQSPYPAPPPQLPTCVLPAGVEFHSSGFVSSDPASFPRSYPIVLTEGDGSKIFVSCIAFRDRVCEDIIEAYRLPPNTYADKCICLVSHAPNFRVLRNSLEEIFVLCFSSEGSCKPLWDIIAYMVSNVPLPTPGKDRVLFAVENCLLSVEAPPEDSLPQADISLQPLVQCLDVDNLIKLFTSVLVERRILIRSNKYSLLTLVSESICHLIYPFRWLQVYIPLLFFSGVDYIDAPTPYMMGLHSDVDTSNLAMDGVVVVDLDINQITTSEEIPQIPEPEFSTLRNDILKLLHPNVVAIDQLKGFGNSVEQCPKSLSKPWGEDHDLQLRVIFLKCFASILGGYRNFIENKVFSTDAFLKRRSRSTNQPPEPMLVQFLGSFAFLDYLERRLSSDEKSTNLLEKLQDAVGRGQDAMSILPKSSMEPEIITIAEPEVEESATRYTYDRFPASVRSEEQEEKRKQILAAASGALESNGRHPPSSPPGKNTKEDNFSSMERAAERERMVLDIQVKLQGLWLRLLKLGSDEDPLSSFEYGTILALIESDAEGIGGSGFIECIREHLYSGWHGQLSEEQFIAVKELLKMAVGRAASRSDLSTVRDALEVSAEMFKKDANNVSDYVQRHLISIPIWEELRFWEGYFEYLMEQPANESVNYATLVTARLIIVASHMAGLGLPDTEAWNMIETIAEKQKLGYKLLIKLRGFLSHVQQLRVGYWGASSFKQQAISAGLPSPRPKDVSVSDETQQPSEASGRSWVQSMFSRDTASRANSFSRVRKWVSDNASSDITAAAQKKIQTNVRVLKGHGGAVTALHSVTRREVCDLVGDREDAGFFISGSTDCLVKIWDPSLRGSELRATLKGHTGTVRAISSDRGKIVSGSDDLSVIVWDKQTTQLLEELKGHDSQVSCVKMLSGERVLTAAHDGTVKMWDVRTDMCVATVGRCSSAILSLEYDDSTGILAAAGRDTVANIWDIRSGKQMHKLKGHTKW,DENN domain and WD repeat-containing protein SCD1,"Involved in growth and development through its role in cytokinesis and polarized cell expansion. Required for plasma membrane internalization. May function in clathrin-mediated membrane trafficking, including plasma membrane endocytosis, essential to both cytokinesis and cell expansion. Acts as a negative regulator of basal resistance against bacteria.","The scd1-1 mutant affects the division of guard mother cells in the leaf epidermis. At the non-permissive temperature, defective scd1-1 guard cells are binucleate and have incomplete ventral cell walls. Cytokinesis is also disrupted in other types of epidermal cells. Further analysis of scd1-1 showed that it plays a role in seedling growth, root elongation, and flower morphogenesis. More severe scd1 T-DNA insertion alleles (scd1-2 and scd1-3) significantly affect polar cell expansion, particularly in trichomes and root hairs. SCD1 is a unique gene in Arabidopsis that encodes a protein related to animal proteins involved in intracellular protein transport and/or mitogen-activated protein kinase signaling pathways. The scd1 mutant phenotype is enhanced by low doses of inhibitors of cell plate consolidation and vesicle secretion. It is proposed that SCD1 functions in polarized vesicle trafficking during plant cytokinesis and cell expansion.","In scd1-1; temperature sensitive mutant with normal growth at the permissive temperature of 16 degrees Celsius and growth defects and sterility due to defective cytokinesis in guard cells and leaf epidermal cells at 22 degrees Celsius. The scd1-1 mutant affects the division of guard mother cells in the leaf epidermis. At the non-permissive temperature, defective scd1-1 guard cells are binucleate and have incomplete ventral cell walls. Cytokinesis is also disrupted in other types of epidermal cells. Further analysis of scd1-1 showed that it plays a role in seedling growth, root elongation, and flower morphogenesis. More severe scd1 T-DNA insertion alleles (scd1-2 and scd1-3) significantly affect polar cell expansion, particularly in trichomes and root hairs. SCD1 is a unique gene in Arabidopsis that encodes a protein related to animal proteins involved in intracellular protein transport and/or mitogen-activated protein kinase signaling pathways. The scd1 mutant phenotype is enhanced by low doses of inhibitors of cell plate consolidation and vesicle secretion. It is proposed that SCD1 functions in polarized vesicle trafficking during plant cytokinesis and cell expansion."
246,246,206734,Q14956-S294F,MECLYYFLGFLLLAARLPLDAAKRFHDVLGNERPSAYMREHNQLNGWSSDENDWNEKLYPVWKRGDMRWKNSWKGGRVQAVLTSDSPALVGSNITFAVNLIFPRCQKEDANGNIVYEKNCRNEAGLSADPYVYNWTAWSEDSDGENGTGQSHHNVFPDGKPFPHHPGWRRWNFIYVFHTLGQYFQKLGRCSVRVSVNTANVTLGPQLMEVTVYRRHGRAYVPIAQVKDVYVVTDQIPVFVTMFQKNDRNSSDETFLKDLPIMFDVLIHDPSHFLNYSTINYKWSFGDNTGLFVFTNHTVNHTYVLNGTFSLNLTVKAAAPGPCPPPPPPPRPSKPTPSLATTLKSYDSNTPGPAGDNPLELSRIPDENCQINRYGHFQATITIVEGILEVNIIQMTDVLMPVPWPESSLIDFVVTCQGSIPTEVCTIISDPTCEITQNTVCSPVDVDEMCLLTVRRTFNGSGTYCVNLTLGDDTSLALTSTLISVPDRDPASPLRMANSALISVGCLAIFVTVISLLVYKKHKEYNPIENSPGNVVRSKGLSVFLNRAKAVFFPGNQEKDPLLKNQEFKGVS,,,MECLYYFLGFLLLAARLPLDAAKRFHDVLGNERPSAYMREHNQLNGWSSDENDWNEKLYPVWKRGDMRWKNSWKGGRVQAVLTSDSPALVGSNITFAVNLIFPRCQKEDANGNIVYEKNCRNEAGLSADPYVYNWTAWSEDSDGENGTGQSHHNVFPDGKPFPHHPGWRRWNFIYVFHTLGQYFQKLGRCSVRVSVNTANVTLGPQLMEVTVYRRHGRAYVPIAQVKDVYVVTDQIPVFVTMFQKNDRNSSDETFLKDLPIMFDVLIHDPSHFLNYSTINYKWSFGDNTGLFVSTNHTVNHTYVLNGTFSLNLTVKAAAPGPCPPPPPPPRPSKPTPSLATTLKSYDSNTPGPAGDNPLELSRIPDENCQINRYGHFQATITIVEGILEVNIIQMTDVLMPVPWPESSLIDFVVTCQGSIPTEVCTIISDPTCEITQNTVCSPVDVDEMCLLTVRRTFNGSGTYCVNLTLGDDTSLALTSTLISVPDRDPASPLRMANSALISVGCLAIFVTVISLLVYKKHKEYNPIENSPGNVVRSKGLSVFLNRAKAVFFPGNQEKDPLLKNQEFKGVS,Transmembrane glycoprotein NMB,Could be a melanogenic enzyme.,"The compound heterozygosity or homozygosity of GPNMB truncating alleles is the cause of autosomal-recessive ACD. Loss of GPNMB, which has been implicated in melanosome formation, autophagy, phagocytosis, tissue repair, and negative regulation of inflammation, underlies autosomal-recessive ACD and provides insights into the etiology of amyloidosis and pigment dyschromia.","The compound heterozygosity or homozygosity of GPNMB truncating alleles is the cause of autosomal-recessive ACD. Loss of GPNMB, which has been implicated in melanosome formation, autophagy, phagocytosis, tissue repair, and negative regulation of inflammation, underlies autosomal-recessive ACD and provides insights into the etiology of amyloidosis and pigment dyschromia."
247,247,207728,P16913-G79D,MNFQGLVLTDNCKNQWVVGPLIGKGGFGSIYTTNDNNYVVKIEPKANGSLFTEQAFYTRVLKPSVIEEWKKSHNIKHVDLITCKAFGLYKSINVEYRFLVINRLGADLDAVIRANNNRLPKRSVMLIGIEILNTIQFMHEQGYSHGDIKASNIVLDQIDKNKLYLVDYGLVSKFMSNGEHVPFIRNPNKMDNGTLEFTPIDSHKGYVVSRRGDLETLGYCMIRWLGGILPWTKISETKNCALVSATKQKYVNNTATLLMTSLQYAPRELLQYITMVNSLTYFEEPNYDEFRHILMQGVYY,Complete loss of enzymatic activity and loss of viral intermediate gene expression (mutant ts2).,,MNFQGLVLTDNCKNQWVVGPLIGKGGFGSIYTTNDNNYVVKIEPKANGSLFTEQAFYTRVLKPSVIEEWKKSHNIKHVGLITCKAFGLYKSINVEYRFLVINRLGADLDAVIRANNNRLPKRSVMLIGIEILNTIQFMHEQGYSHGDIKASNIVLDQIDKNKLYLVDYGLVSKFMSNGEHVPFIRNPNKMDNGTLEFTPIDSHKGYVVSRRGDLETLGYCMIRWLGGILPWTKISETKNCALVSATKQKYVNNTATLLMTSLQYAPRELLQYITMVNSLTYFEEPNYDEFRHILMQGVYY,B1 kinase,"Essential serine/threonine-protein kinase that plays different role in the viral life cycle. Phosphorylates the host small ribosomal protein RACK1 thereby customizing the ribosomes to a state optimal for viral mRNAs (which contain poly-A leaders) but not for host mRNAs. Facilitates viral DNA replication by inhibiting host BANF1, a cellular host defense responsive to foreign DNA. Phosphorylates host BANF1 on serine and threonine residues; this leads to BANF1 relocalization to the cytoplasm, loss of dimerization and impaired DNA binding activity. Indeed, BANF1 activity depends on its DNA-binding property which is blocked by VPK1-mediated phosphorylation. Required for viral intermediate genes expression, probably by inhibiting host BANF1. Modulates cellular responses via host JUN by two different mechanisms, either by direct phosphorylation or by modulation of upstream JIP1-MAPK complexes. Seems to participate in the accumulation/processing of late proteins and thus in virion maturation. In addition, inhibits B12 repressive activity on viral DNA replication via a phosphorylation-dependent mechanism.","The mutation in the B1 gene of vaccinia virus causes a functional change in the serine/threonine protein kinase. It has been observed that under nonpermissive conditions, the mutant fails to efficiently replicate viral DNA. Additionally, overexpression of B1 stimulates intermediate gene expression but inhibits late gene expression in cells infected with wild-type virus. The ts B1 proteins are markedly labile in both L and BSC40 cells at both permissive and nonpermissive temperatures.","Complete loss of enzymatic activity and loss of viral intermediate gene expression (mutant ts2). The mutation in the B1 gene of vaccinia virus causes a functional change in the serine/threonine protein kinase. It has been observed that under nonpermissive conditions, the mutant fails to efficiently replicate viral DNA. Additionally, overexpression of B1 stimulates intermediate gene expression but inhibits late gene expression in cells infected with wild-type virus. The ts B1 proteins are markedly labile in both L and BSC40 cells at both permissive and nonpermissive temperatures."
248,248,208313,P06022-Q113P,MQHDLFEHDPAIRQLIGHIDNIPAPELESRWPRSVVDLIDVLENELKRQNVSNPRELARKQAVALSCFLGGRQFYIPCGDTILTALRDDLLYCQFNGRNMEELRRQYRLSQPPIYQIIARQRKLHTRRHQPDLFSPETPK,Loss of DNA-binding activity.,,MQHDLFEHDPAIRQLIGHIDNIPAPELESRWPRSVVDLIDVLENELKRQNVSNPRELARKQAVALSCFLGGRQFYIPCGDTILTALRDDLLYCQFNGRNMEELRRQYRLSQPQIYQIIARQRKLHTRRHQPDLFSPETPK,Late transcription activator C,"Positive regulator of viral late genes transcription. Responsible for the transition from middle to late gene expression. Activates the Plys, PI, PP and Pmom late promoters thereby allowing the expression of viral endolysin and structural genes. Activates Pmom promoter by unwinding the DNA, thus realigning the promoter elements and recruiting the RNAP.",The mutant protein showed a reduced ability to activate the P(lys)-galK fusion.,Loss of DNA-binding activity. The mutant protein showed a reduced ability to activate the P(lys)-galK fusion.
249,0,0,P69490-A130H,MNIRRKNRLWIACAVLAGLALTIGLVLYALRSNIDLFYTPGEILYGKRETQQMPEVGQRLRVGGMVMPGSVQRDPNSLKVTFTIYDAEGSVDVSYEGILPDLFREGQGVVVQGELEKGNHILAKEVLAKHDENYTPPEVEKAMEANHRRPASVYKDPAS,,-1.0,MNIRRKNRLWIACAVLAGLALTIGLVLYALRSNIDLFYTPGEILYGKRETQQMPEVGQRLRVGGMVMPGSVQRDPNSLKVTFTIYDAEGSVDVSYEGILPDLFREGQGVVVQGELEKGNHILAKEVLAKADENYTPPEVEKAMEANHRRPASVYKDPAS,Cytochrome c-type biogenesis protein CcmE,Heme chaperone required for the biogenesis of c-type cytochromes. Transiently binds heme delivered by CcmC and transfers the heme to apo-cytochromes in a process facilitated by CcmF and CcmH.,Enhances heme binding. Mutation of H130 to alanine affected CcmE less than mutation of charged and polar residues. Our data suggest that heme is released from a hydrophobic platform at the surface of the protein and then attached to H130 by a covalent bond.,Enhances heme binding. Mutation of H130 to alanine affected CcmE less than mutation of charged and polar residues. Our data suggest that heme is released from a hydrophobic platform at the surface of the protein and then attached to H130 by a covalent bond.
250,0,0,P21926-A219C,MPVKGGTKCIKYLLFGFNFIFWLAGIAVLAIGLWLRFDSQTKSIFEQETNNNNSSFYTGVYILIGAGALMMLVGFLGCCGAVQESQCMLGLFFGFLLVIFAIEIAAAIWGYSHKDEVIKEVQEFYKDTYNKLKTKDEPQRETLKAIHYALNCCGLAGGVEQFISDICPKKDVLETFTVKSCPDAIKEVFDNKFHIIGAVGIGIAVVMIFGMIFSMILCCAIRRNREMV,,-1.0,MPVKGGTKCIKYLLFGFNFIFWLAGIAVLAIGLWLRFDSQTKSIFEQETNNNNSSFYTGVYILIGAGALMMLVGFLGCCGAVQESQCMLGLFFGFLLVIFAIEIAAAIWGYSHKDEVIKEVQEFYKDTYNKLKTKDEPQRETLKAIHYALNCCGLAGGVEQFISDICPKKDVLETFTVKSCPDAIKEVFDNKFHIIGAVGIGIAVVMIFGMIFSMILCAAIRRNREMV,CD9 antigen,"Integral membrane protein associated with integrins, which regulates different processes, such as sperm-egg fusion, platelet activation and aggregation, and cell adhesion. Present at the cell surface of oocytes and plays a key role in sperm-egg fusion, possibly by organizing multiprotein complexes and the morphology of the membrane required for the fusion. In myoblasts, associates with CD81 and PTGFRN and inhibits myotube fusion during muscle regeneration. In macrophages, associates with CD81 and beta-1 and beta-2 integrins, and prevents macrophage fusion into multinucleated giant cells specialized in ingesting complement-opsonized large particles. Also prevents the fusion between mononuclear cell progenitors into osteoclasts in charge of bone resorption. Acts as a receptor for PSG17. Involved in platelet activation and aggregation. Regulates paranodal junction formation. Involved in cell adhesion, cell motility and tumor metastasis.",Gain of palmitoylation; when associated with A-9; A-78; A-79; A-87 and A-218.,Gain of palmitoylation; when associated with A-9; A-78; A-79; A-87 and A-218.
251,0,0,Q92504-A275S,MARGLGAPHWVAVGLLTWATLGLLVAGLGGHDDLHDDLQEDFHGHSHRHSHEDFHHGHSHAHGHGHTHESIWHGHTHDHDHGHSHEDLHHGHSHGYSHESLYHRGHGHDHEHSHGGYGESGAPGIKQDLDAVTLWAYALGATVLISAAPFFVLFLIPVESNSPRHRSLLQILLSFASGGLLGDAFLHLIPHALEPHSHHTLEQPGHGHSHSGQGPILSVGLWVLSGIVAFLVVEKFVRHVKGGHGHSHGHGHAHSHTRGSHGHGRQERSTKEKQSSEEEEKETRGVQKRRGGSTVPKDGPVRPQNAEEEKRGLDLRVSGYLNLAADLAHNFTDGLAIGASFRGGRGLGILTTMTVLLHEVPHEVGDFAILVQSGCSKKQAMRLQLLTAVGALAGTACALLTEGGAVGSEIAGGAGPGWVLPFTAGGFIYVATVSVLPELLREASPLQSLLEVLGLLGGVIMMVLIAHLE,,-1.0,MARGLGAPHWVAVGLLTWATLGLLVAGLGGHDDLHDDLQEDFHGHSHRHSHEDFHHGHSHAHGHGHTHESIWHGHTHDHDHGHSHEDLHHGHSHGYSHESLYHRGHGHDHEHSHGGYGESGAPGIKQDLDAVTLWAYALGATVLISAAPFFVLFLIPVESNSPRHRSLLQILLSFASGGLLGDAFLHLIPHALEPHSHHTLEQPGHGHSHSGQGPILSVGLWVLSGIVAFLVVEKFVRHVKGGHGHSHGHGHAHSHTRGSHGHGRQERSTKEKQASEEEEKETRGVQKRRGGSTVPKDGPVRPQNAEEEKRGLDLRVSGYLNLAADLAHNFTDGLAIGASFRGGRGLGILTTMTVLLHEVPHEVGDFAILVQSGCSKKQAMRLQLLTAVGALAGTACALLTEGGAVGSEIAGGAGPGWVLPFTAGGFIYVATVSVLPELLREASPLQSLLEVLGLLGGVIMMVLIAHLE,Zinc transporter SLC39A7,"Transports Zn(2+) from the endoplasmic reticulum (ER)/Golgi apparatus to the cytosol, playing an essential role in the regulation of cytosolic zinc levels. Acts as gatekeeper of zinc release from intracellular stores, requiring post-translational activation by phosphorylation, resulting in activation of multiple downstream pathways leading to cell growth and proliferation. Has an essential role in B cell development and is required for proper B cell receptor signaling. Plays an important role in maintaining intestinal epithelial homeostasis and skin dermis development by regulating ER function. Controls cell signaling pathways involved in glucose metabolism in skeletal muscle. Has a protective role against ER stress in differents biological contexts. Mediates Zn(2+)-induced ferroptosis.","Increases phosphorylation in response to Zn(2+) treatment and of cytosolic Zn(2+) release; when associated with A-276. Dephosphorylation of S275 in ZIP7 is associated with the gated release of Zn(2+) from intracellular stores, leading to inhibition of tyrosine kinases and the dephosphorylation of AKT and extracellular signal-regulated kinases 1 and 2. The unregulated release of zinc from intracellular stores is linked to dephosphorylation of kinases involved in proliferative responses and cell migration. Dephosphorylation on residue S275 is required for minimal ZIP7 activation.","Increases phosphorylation in response to Zn(2+) treatment and of cytosolic Zn(2+) release; when associated with A-276. Dephosphorylation of S275 in ZIP7 is associated with the gated release of Zn(2+) from intracellular stores, leading to inhibition of tyrosine kinases and the dephosphorylation of AKT and extracellular signal-regulated kinases 1 and 2. The unregulated release of zinc from intracellular stores is linked to dephosphorylation of kinases involved in proliferative responses and cell migration. Dephosphorylation on residue S275 is required for minimal ZIP7 activation."
252,0,0,Q7G065-I171A,MQFMMPLDTNACAQPMRRAGEGAGTERLMERLNIGGMTQEKALRKRCFGDGVTGTARCVFTSDADRDTPHLRTQSSRKNYADASHVSAVILGGGTGVQLFPLTSTRATPAVPVGGCYRLIDIPMSNCFNSGINKIFVMTQFNSASLNRHIHHTYLGGGINFTDGSVQVLAATQMPDEPAGWFQGTADAIRKFMWILEDHYNQNNIEHVVILCGDQLYRMNYMELVQKHVDDNADITISCAPIDGSRASDYGLVKFDDSGRVIQFLEKPEGADLESMKVDTSFLSYAIDDKQKYPYIASMGIYVLKKDVLLDILKSKYAHLQDFGSEILPRAVLEHNVKACVFTEYWEDIGTIKSFFDANLALTEQPPKFEFYDPKTPFFTSPRYLPPARLEKCKIKDAIISDGCSFSECTIEHSVIGISSRVSIGCELKDTMMMGADQYETEEETSKLLFEGKVPIGIGENTKIRNCIIDMNARIGRNVIIANTQGVQESDHPEEGYYIRSGIVVILKNATIKDGTVI,,-1.0,MQFMMPLDTNACAQPMRRAGEGAGTERLMERLNIGGMTQEKALRKRCFGDGVTGTARCVFTSDADRDTPHLRTQSSRKNYADASHVSAVILGGGTGVQLFPLTSTRATPAVPVGGCYRLIDIPMSNCFNSGINKIFVMTQFNSASLNRHIHHTYLGGGINFTDGSVQVLAITQMPDEPAGWFQGTADAIRKFMWILEDHYNQNNIEHVVILCGDQLYRMNYMELVQKHVDDNADITISCAPIDGSRASDYGLVKFDDSGRVIQFLEKPEGADLESMKVDTSFLSYAIDDKQKYPYIASMGIYVLKKDVLLDILKSKYAHLQDFGSEILPRAVLEHNVKACVFTEYWEDIGTIKSFFDANLALTEQPPKFEFYDPKTPFFTSPRYLPPARLEKCKIKDAIISDGCSFSECTIEHSVIGISSRVSIGCELKDTMMMGADQYETEEETSKLLFEGKVPIGIGENTKIRNCIIDMNARIGRNVIIANTQGVQESDHPEEGYYIRSGIVVILKNATIKDGTVI,"Glucose-1-phosphate adenylyltransferase large subunit 2, cytosolic","Involved in synthesis of starch. Catalyzes the synthesis of ADP-glucose, a molecule that serves as an activated glycosyl donor for alpha-1,4-glucan synthesis. Essential for starch synthesis in seed endosperm (PubMed:17406793, Ref.13, PubMed:24747952, PubMed:27957808). Is essential for both catalytic and allosteric regulatory properties of the cytosolic heterotetramer enzyme.",Increases activity more than 3-fold. Seeds from the missense mutant containing were greatly plump and had seed weight and starch content comparable with the plump seeds from OsAGPL2 null mutants. The catalytic and allosteric regulatory properties of the mutant enzyme were significantly enhanced. The mutant enzyme had higher specific (catalytic) activity and affinity for the activator 3-phosphoglycerate (3-PGA). The mutant enzyme also showed less sensitivity to inhibition by the inhibitor inorganic phosphate (Pi) than the wild-type AGPase.,Increases activity more than 3-fold. Seeds from the missense mutant containing were greatly plump and had seed weight and starch content comparable with the plump seeds from OsAGPL2 null mutants. The catalytic and allosteric regulatory properties of the mutant enzyme were significantly enhanced. The mutant enzyme had higher specific (catalytic) activity and affinity for the activator 3-phosphoglycerate (3-PGA). The mutant enzyme also showed less sensitivity to inhibition by the inhibitor inorganic phosphate (Pi) than the wild-type AGPase.
253,0,0,Q9ULZ3-A19E,MGRARDAILDALENLTAEELKKFKLKLLSVPLREGYGRIPRGALLSMDALDLTDKLVSFYLETYGAELTANVLRDMGLQEMAGQLQAATHQGSGAAPAGIQAPPQSAAKPGLHFIDQHRAALIARVTNVEWLLDALYGKVLTDEQYQAVRAEPTNPSKMRKLFSFTPAWNWTCKDLLLQALRESQSYLVEDLERS,,-1.0,MGRARDAILDALENLTAEALKKFKLKLLSVPLREGYGRIPRGALLSMDALDLTDKLVSFYLETYGAELTANVLRDMGLQEMAGQLQAATHQGSGAAPAGIQAPPQSAAKPGLHFIDQHRAALIARVTNVEWLLDALYGKVLTDEQYQAVRAEPTNPSKMRKLFSFTPAWNWTCKDLLLQALRESQSYLVEDLERS,Apoptosis-associated speck-like protein containing a CARD,"Functions as key mediator in apoptosis and inflammation. Promotes caspase-mediated apoptosis involving predominantly caspase-8 and also caspase-9 in a probable cell type-specific manner. Involved in activation of the mitochondrial apoptotic pathway, promotes caspase-8-dependent proteolytic maturation of BID independently of FADD in certain cell types and also mediates mitochondrial translocation of BAX and activates BAX-dependent apoptosis coupled to activation of caspase-9, -2 and -3. Involved in innate immune response by acting as an integral adapter in the assembly of various inflammasomes (NLRP1, NLRP2, NLRP3, NLRP6, AIM2 and probably IFI16) which recruit and activate caspase-1 leading to processing and secretion of pro-inflammatory cytokines. Caspase-1-dependent inflammation leads to macrophage pyroptosis, a form of cell death. The function as activating adapter in different types of inflammasomes is mediated by the pyrin and CARD domains and their homotypic interactions. Clustered PYCARD nucleates the formation of caspase-1 filaments through the interaction of their respective CARD domains, acting as a platform for of caspase-1 polymerization. In the NLRP1 and NLRC4 inflammasomes seems not be required but facilitates the processing of procaspase-1. In cooperation with NOD2 involved in an inflammasome activated by bacterial muramyl dipeptide leading to caspase-1 activation. May be involved in RIGI-triggered pro-inflammatory responses and inflammasome activation. In collaboration with AIM2 which detects cytosolic double-stranded DNA may also be involved in a caspase-1-independent cell death that involves caspase-8. In adaptive immunity may be involved in maturation of dendritic cells to stimulate T-cell immunity and in cytoskeletal rearrangements coupled to chemotaxis and antigen uptake may be involved in post-transcriptional regulation of the guanine nucleotide exchange factor DOCK2; the latter function is proposed to involve the nuclear form. Also involved in transcriptional activation of cytokines and chemokines independent of the inflammasome; this function may involve AP-1, NF-kappa-B, MAPK and caspase-8 signaling pathways. For regulation of NF-kappa-B activating and inhibiting functions have been reported. Modulates NF-kappa-B induction at the level of the IKK complex by inhibiting kinase activity of CHUK and IKBK. Proposed to compete with RIPK2 for association with CASP1 thereby down-regulating CASP1-mediated RIPK2-dependent NF-kappa-B activation and activating interleukin-1 beta processing. Modulates host resistance to DNA virus infection, probably by inducing the cleavage of and inactivating CGAS in presence of cytoplasmic double-stranded DNA.May have a regulating effect on the function as inflammasome adapter.Seems to inhibit inflammasome-mediated maturation of interleukin-1 beta.",Enhances homooligomerization. Mutation of E19 to A in ASC protein leads to gain of filament formation.,Enhances homooligomerization. Mutation of E19 to A in ASC protein leads to gain of filament formation.
254,0,0,A0A0H2URG7-A103R,MTIYNINLGIGWASSGVEYAQAYRAGVFRKLNLSSKFIFTDMILADNIQHLTANIGFDDNQVIWLYNHFTDIKIAPTSVTVDDVLAYFGGEESHREKNGKVLRVFFFDQDKFVTCYLVDENKDLVQHAEYVFKGNLIRKDYFSYTRYCSEYFAPKDNVAVLYQRTFYNEDGTPVYDILMNQGKEEVYHFKDKIFYGKQAFVRAFMKSLNLNKSDLVILDRETGIGQVVFEEAQTAHLAVVVHAEHYSENATNEDYILWNNYYDYQFTNADKVDFFIVSTDRQNEVLQEQFAKYTQHQPKIVTIPVGSIDSLTDSSQGRKPFSLITASRLAKEKHIDWLVKAVIEAHKELPELTFDIYGSGGEDSLLREIIANHQAEDYIQLKGHAELSQIYSQYEVYLTASTSEGFGLTLMEAIGSGLPLIGFDVPYGNQTFIEDGQNGYLIPSSSDHVEDQIKQAYAAKICQLYQENRLEAMRAYSYQIAEGFLTKEILEKWKKTVEEVLHD,,-1.0,MTIYNINLGIGWASSGVEYAQAYRAGVFRKLNLSSKFIFTDMILADNIQHLTANIGFDDNQVIWLYNHFTDIKIAPTSVTVDDVLAYFGGEESHREKNGKVLAVFFFDQDKFVTCYLVDENKDLVQHAEYVFKGNLIRKDYFSYTRYCSEYFAPKDNVAVLYQRTFYNEDGTPVYDILMNQGKEEVYHFKDKIFYGKQAFVRAFMKSLNLNKSDLVILDRETGIGQVVFEEAQTAHLAVVVHAEHYSENATNEDYILWNNYYDYQFTNADKVDFFIVSTDRQNEVLQEQFAKYTQHQPKIVTIPVGSIDSLTDSSQGRKPFSLITASRLAKEKHIDWLVKAVIEAHKELPELTFDIYGSGGEDSLLREIIANHQAEDYIQLKGHAELSQIYSQYEVYLTASTSEGFGLTLMEAIGSGLPLIGFDVPYGNQTFIEDGQNGYLIPSSSDHVEDQIKQAYAAKICQLYQENRLEAMRAYSYQIAEGFLTKEILEKWKKTVEEVLHD,UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase GtfA subunit,Required for the polymorphic O-glycosylation of serine-rich repeat protein PsrP. Catalyzes the first step in glycosylation by transferring N-acetylglucosamine from UDP-GlcNAc to serine residues in PsrP. Part of the accessory SecA2/SecY2 system specifically required to export serine-rich repeat cell wall proteins encoded upstream in the same operon (Probable). The GtfA-GtfB complex adds GlcNAc from UDP-GlcNAc to PsrP (experimentally characterized with truncated PsrP-SSR1 constructs); this subunit alone has weak N-acetylglucosaminyl transferase activity that is 10-fold stimulated by GtfB. The complex requires at least a 25 residue-long peptide for activity; the in vitro assay has only been seen to glycosylate Ser residues. The alpha linkage was shown in L.reuteri.,"Decreased N-acetylglucosaminyl transferase activity, increased binding of PsrP.","Decreased N-acetylglucosaminyl transferase activity, increased binding of PsrP."
255,0,0,Q9JJS6-A49H,MEIIFGQNKKEQLEPVQAKVTGSIPAWLQGTLLRNGPGMHTVGESKYNHWFDGLALLHSFSIRDGEVFYRSKYLQSDTYIANIEANRIVVSEFGTMAYPDPCKNIFSKAFSYLSHTIPDFTDNCLINIMKCGEDFYATTETNYIRKIDPQTLETLEKVDYRKYVAVNLATSHPHYDEAGNVLNMGTSVVDKGRTKYVIFKIPATVPDSKKKGKSPVKHAEVFCSISSRSLLSPSYYHSFGVTENYVVFLEQPFKLDILKMATAYMRGVSWASCMSFDREDKTYIHIIDQRTRKPVPTKFYTDPMVVFHHVNAYEEDGCVLFDVIAYEDSSLYQLFYLANLNKDFEEKSRLTSVPTLRRFAVPLHVDKDAEVGSNLVKVSSTTATALKEKDGHVYCQPEVLYEGLELPRINYAYNGKPYRYIFAAEVQWSPVPTKILKYDILTKSSLKWSEESCWPAEPLFVPTPGAKDEDDGVILSAIVSTDPQKLPFLLILDAKSFTELARASVDADMHLDLHGLFIPDADWNAVKQTPAETQEVENSDHPTDPTAPELSHSENDFTAGHGGSSL,,-1.0,MEIIFGQNKKEQLEPVQAKVTGSIPAWLQGTLLRNGPGMHTVGESKYNAWFDGLALLHSFSIRDGEVFYRSKYLQSDTYIANIEANRIVVSEFGTMAYPDPCKNIFSKAFSYLSHTIPDFTDNCLINIMKCGEDFYATTETNYIRKIDPQTLETLEKVDYRKYVAVNLATSHPHYDEAGNVLNMGTSVVDKGRTKYVIFKIPATVPDSKKKGKSPVKHAEVFCSISSRSLLSPSYYHSFGVTENYVVFLEQPFKLDILKMATAYMRGVSWASCMSFDREDKTYIHIIDQRTRKPVPTKFYTDPMVVFHHVNAYEEDGCVLFDVIAYEDSSLYQLFYLANLNKDFEEKSRLTSVPTLRRFAVPLHVDKDAEVGSNLVKVSSTTATALKEKDGHVYCQPEVLYEGLELPRINYAYNGKPYRYIFAAEVQWSPVPTKILKYDILTKSSLKWSEESCWPAEPLFVPTPGAKDEDDGVILSAIVSTDPQKLPFLLILDAKSFTELARASVDADMHLDLHGLFIPDADWNAVKQTPAETQEVENSDHPTDPTAPELSHSENDFTAGHGGSSL,"Beta,beta-carotene 15,15'-dioxygenase",Symmetrically cleaves beta-carotene into two molecules of retinal using a dioxygenase mechanism.,"Decreased stability. Significant effect on beta-carotene 15,15'-monooxygenase activity.","Decreased stability. Significant effect on beta-carotene 15,15'-monooxygenase activity."
256,0,0,O14746-A457S,MPRAPRCRAVRSLLRSHYREVLPLATFVRRLGPQGWRLVQRGDPAAFRALVAQCLVCVPWDARPPPAAPSFRQVSCLKELVARVLQRLCERGAKNVLAFGFALLDGARGGPPEAFTTSVRSYLPNTVTDALRGSGAWGLLLRRVGDDVLVHLLARCALFVLVAPSCAYQVCGPPLYQLGAATQARPPPHASGPRRRLGCERAWNHSVREAGVPLGLPAPGARRRGGSASRSLPLPKRPRRGAAPEPERTPVGQGSWAHPGRTRGPSDRGFCVVSPARPAEEATSLEGALSGTRHSHPSVGRQHHAGPPSTSRPPRPWDTPCPPVYAETKHFLYSSGDKEQLRPSFLLSSLRPSLTGARRLVETIFLGSRPWMPGTPRRLPRLPQRYWQMRPLFLELLGNHAQCPYGVLLKTHCPLRAAVTPAAGVCAREKPQGSVAAPEEEDTDPRRLVQLLRQHSSPWQVYGFVRACLRRLVPPGLWGSRHNERRFLRNTKKFISLGKHAKLSLQELTWKMSVRDCAWLRRSPGVGCVPAAEHRLREEILAKFLHWLMSVYVVELLRSFFYVTETTFQKNRLFFYRKSVWSKLQSIGIRQHLKRVQLRELSEAEVRQHREARPALLTSRLRFIPKPDGLRPIVNMDYVVGARTFRREKRAERLTSRVKALFSVLNYERARRPGLLGASVLGLDDIHRAWRTFVLRVRAQDPPPELYFVKVDVTGAYDTIPQDRLTEVIASIIKPQNTYCVRRYAVVQKAAHGHVRKAFKSHVSTLTDLQPYMRQFVAHLQETSPLRDAVVIEQSSSLNEASSGLFDVFLRFMCHHAVRIRGKSYVQCQGIPQGSILSTLLCSLCYGDMENKLFAGIRRDGLLLRLVDDFLLVTPHLTHAKTFLRTLVRGVPEYGCVVNLRKTVVNFPVEDEALGGTAFVQMPAHGLFPWCGLLLDTRTLEVQSDYSSYARTSIRASLTFNRGFKAGRNMRRKLFGVLRLKCHSLFLDLQVNSLQTVCTNIYKILLLQAYRFHACVLQLPFHQQ,,-1.0,MPRAPRCRAVRSLLRSHYREVLPLATFVRRLGPQGWRLVQRGDPAAFRALVAQCLVCVPWDARPPPAAPSFRQVSCLKELVARVLQRLCERGAKNVLAFGFALLDGARGGPPEAFTTSVRSYLPNTVTDALRGSGAWGLLLRRVGDDVLVHLLARCALFVLVAPSCAYQVCGPPLYQLGAATQARPPPHASGPRRRLGCERAWNHSVREAGVPLGLPAPGARRRGGSASRSLPLPKRPRRGAAPEPERTPVGQGSWAHPGRTRGPSDRGFCVVSPARPAEEATSLEGALSGTRHSHPSVGRQHHAGPPSTSRPPRPWDTPCPPVYAETKHFLYSSGDKEQLRPSFLLSSLRPSLTGARRLVETIFLGSRPWMPGTPRRLPRLPQRYWQMRPLFLELLGNHAQCPYGVLLKTHCPLRAAVTPAAGVCAREKPQGSVAAPEEEDTDPRRLVQLLRQHSAPWQVYGFVRACLRRLVPPGLWGSRHNERRFLRNTKKFISLGKHAKLSLQELTWKMSVRDCAWLRRSPGVGCVPAAEHRLREEILAKFLHWLMSVYVVELLRSFFYVTETTFQKNRLFFYRKSVWSKLQSIGIRQHLKRVQLRELSEAEVRQHREARPALLTSRLRFIPKPDGLRPIVNMDYVVGARTFRREKRAERLTSRVKALFSVLNYERARRPGLLGASVLGLDDIHRAWRTFVLRVRAQDPPPELYFVKVDVTGAYDTIPQDRLTEVIASIIKPQNTYCVRRYAVVQKAAHGHVRKAFKSHVSTLTDLQPYMRQFVAHLQETSPLRDAVVIEQSSSLNEASSGLFDVFLRFMCHHAVRIRGKSYVQCQGIPQGSILSTLLCSLCYGDMENKLFAGIRRDGLLLRLVDDFLLVTPHLTHAKTFLRTLVRGVPEYGCVVNLRKTVVNFPVEDEALGGTAFVQMPAHGLFPWCGLLLDTRTLEVQSDYSSYARTSIRASLTFNRGFKAGRNMRRKLFGVLRLKCHSLFLDLQVNSLQTVCTNIYKILLLQAYRFHACVLQLPFHQQ,Telomerase reverse transcriptase,"Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. Active in progenitor and cancer cells. Inactive, or very low activity, in normal somatic cells. Catalytic component of the teleromerase holoenzyme complex whose main activity is the elongation of telomeres by acting as a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme. Catalyzes the RNA-dependent extension of 3'-chromosomal termini with the 6-nucleotide telomeric repeat unit, 5'-TTAGGG-3'. The catalytic cycle involves primer binding, primer extension and release of product once the template boundary has been reached or nascent product translocation followed by further extension. More active on substrates containing 2 or 3 telomeric repeats. Telomerase activity is regulated by a number of factors including telomerase complex-associated proteins, chaperones and polypeptide modifiers. Modulates Wnt signaling. Plays important roles in aging and antiapoptosis.",Enables phosphorylation by DYRK2.,Enables phosphorylation by DYRK2.
257,0,0,Q1PEI6-V377M,MEFSCVHFLQNKTILVTGATGFLAKVFVEKILRVQPNVNKLYLVVRASDNEAATKRLRTEAFEKDLFKVLRDNLGDEKLNTLLSEKVVPVAGDIAMDHLGMKDSNLRERMQKEIDIVVNVAATTNFDERYDIGLGINTFGALNVLNFAKKCVKAQLLLHVSTAYVCGEKPGLLPEKPFVMEEICNENGLQLDINLERELMKQRLKELNEQGCSEEGTTFYMKELGMERAKLHGWPNTYVFTKSMGEMLLGNHKENLPLVIIRPTMITSTLFEPFPGWIEGLRTVDSVIIAYGKGVLKCFLVDVNSVCDMIPADMVANAMIAAAATHAGGSKVHMVYQVGSSHQNPIIYGEIREILFCYFTKNSLRSRNGSMITVSKMKLIPTLALFSLYMTIRYKLPVQLLKLVDIIYPSREGDEYKNKNRKIDMVMRLVKLYEPYVLFKGIFDDRNTKNLCAKQKEEDNRNSENFMFDFDPKIIKWKDYLINVHIPGLITHVLKK,,-1.0,MEFSCVHFLQNKTILVTGATGFLAKVFVEKILRVQPNVNKLYLVVRASDNEAATKRLRTEAFEKDLFKVLRDNLGDEKLNTLLSEKVVPVAGDIAMDHLGMKDSNLRERMQKEIDIVVNVAATTNFDERYDIGLGINTFGALNVLNFAKKCVKAQLLLHVSTAYVCGEKPGLLPEKPFVMEEICNENGLQLDINLERELMKQRLKELNEQGCSEEGTTFYMKELGMERAKLHGWPNTYVFTKSMGEMLLGNHKENLPLVIIRPTMITSTLFEPFPGWIEGLRTVDSVIIAYGKGVLKCFLVDVNSVCDMIPADMVANAMIAAAATHAGGSKVHMVYQVGSSHQNPIIYGEIREILFCYFTKNSLRSRNGSMITVSKVKLIPTLALFSLYMTIRYKLPVQLLKLVDIIYPSREGDEYKNKNRKIDMVMRLVKLYEPYVLFKGIFDDRNTKNLCAKQKEEDNRNSENFMFDFDPKIIKWKDYLINVHIPGLITHVLKK,Fatty acyl-CoA reductase 8,Catalyzes the reduction of fatty acyl-CoA to fatty alcohols. Catalyzes specifically the formation of C16:0 fatty alcohol.,Catalyzes the formation of C16:0 fatty alcohol instead of C18:0; when associated with T-347 and A-355. converting its specificity from 18:0-CoA to 16:0-CoA.,Catalyzes the formation of C16:0 fatty alcohol instead of C18:0; when associated with T-347 and A-355. converting its specificity from 18:0-CoA to 16:0-CoA.
258,0,0,Q8IB06-H57I,MGSCYSRKNKVSTISLDEEEKKKEKKKKKKIYILNGASGSGKDTQCRLLEKKYNYKIICISKLLKEYKEEYNKENVLNEEENYFDEIEKCMIDGSLVNDQIVIEIFHKQLNKYINDDKYNGIIINGFPRNYEQALLIIQNNISITKFINIQVGKDTLWTRINNRIIDPITNISYNENIIQIIKKKREGQELSDKEQKQLIIDNHLYNNLSNDILERLTKRKDDEEQVFNKRFQLYIESEQKINSLFKNICKNVDGEKSINDIFDQICSIIDDNPN,,-1.0,MGSCYSRKNKVSTISLDEEEKKKEKKKKKKIYILNGASGSGKDTQCRLLEKKYNYKHICISKLLKEYKEEYNKENVLNEEENYFDEIEKCMIDGSLVNDQIVIEIFHKQLNKYINDDKYNGIIINGFPRNYEQALLIIQNNISITKFINIQVGKDTLWTRINNRIIDPITNISYNENIIQIIKKKREGQELSDKEQKQLIIDNHLYNNLSNDILERLTKRKDDEEQVFNKRFQLYIESEQKINSLFKNICKNVDGEKSINDIFDQICSIIDDNPN,Adenylate kinase 2,"Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Has very low activity with CTP, GTP, ITP and UTP and no activity with GMP, UMP or IMP in vitro.",Gain of catalytic activity.,Gain of catalytic activity.
259,0,0,Q9AQS0-A612R,MLSGILIAALLMTLWGGWQPDIAHASDEFDALRIKWATLLTGGPALDPADSDIAARTDKLAQDANDYWEDMDLSSSRTYIWYALRGNGTSDNVNAVYERLRTMALAATTVGSSLYGNADLKEDILDALDWLYVNSYNSTRSRSAYNWWHWQLGIPMSLNDIAVLLYDDISAARMATYMDTIDYFTPSIGLTGANRAWQAIVVGVRAVIVKDAVKLAAARNGLSGTGIFPYATGGDGFYADGSFVQHTTFAYTGGYGSSVLETTANLMYLLSGSTWSVSDPNQSNVWQWIYEAYRPLLYKGAMMDMVRGREISRSYAQDHAVGHGIVASIVRLAQFAPAPHAAAFKQIAKRVIQEDTFSSFYGDVSTDTIRLAKAIVDDPSIAPAAAPNLYKQYAAMDRAVLQRPGFALGLALYSTRISSYESINSENGRGWYTGAGATYLYNQDLAQYSEDYWPTVDAYRIPGTTVASGTPIASGTGTSSWTGGVSLAGQYGASGMDLSYGAYNLSARKSWFMFDDEIVALGSGISSTAGIPIETVVDNRKLNGAGDNAWTANGAALSTGLGVAQTLTGVNWVHLAGNTADGSDIGYYFPGGATLQTKREARTGTWKQINNRPATPSTAVTRNYETMWIDHGTNPSGASYGYVLLPNKTSAQVGAYAADPAIEIVVNTSGVQSVKEKTLGLVGANFWTDTTQTADLITSNKKASVMTREIADERLEASVSDPTQANNGTIAIELARSAEGYSADPGITVTQLAPTIKFTVNVNGAKGKSFHASFQLGEDTSGPVDPGEPELPSVIVDNADSAGVTRTGTWKTASTQTDRYGANYLHDDNAGKGTKSVTFTPNLPIAGSYEVYLMWPAHFNREDAVQVDVGHASGTTRTAVDQRSGGGVWHSIGTYEFLAGSGGSVTIRNDALGSPDGYVVADAVKFVAVG,,-1.0,MLSGILIAALLMTLWGGWQPDIAHASDEFDALRIKWATLLTGGPALDPADSDIAARTDKLAQDANDYWEDMDLSSSRTYIWYALRGNGTSDNVNAVYERLRTMALAATTVGSSLYGNADLKEDILDALDWLYVNSYNSTRSRSAYNWWHWQLGIPMSLNDIAVLLYDDISAARMATYMDTIDYFTPSIGLTGANRAWQAIVVGVRAVIVKDAVKLAAARNGLSGTGIFPYATGGDGFYADGSFVQHTTFAYTGGYGSSVLETTANLMYLLSGSTWSVSDPNQSNVWQWIYEAYRPLLYKGAMMDMVRGREISRSYAQDHAVGHGIVASIVRLAQFAPAPHAAAFKQIAKRVIQEDTFSSFYGDVSTDTIRLAKAIVDDPSIAPAAAPNLYKQYAAMDRAVLQRPGFALGLALYSTRISSYESINSENGRGWYTGAGATYLYNQDLAQYSEDYWPTVDAYRIPGTTVASGTPIASGTGTSSWTGGVSLAGQYGASGMDLSYGAYNLSARKSWFMFDDEIVALGSGISSTAGIPIETVVDNRKLNGAGDNAWTANGAALSTGLGVAQTLTGVNWVHLAGNTADGSDIGYYFPGGATLQTKREARTGTWKQINNAPATPSTAVTRNYETMWIDHGTNPSGASYGYVLLPNKTSAQVGAYAADPAIEIVVNTSGVQSVKEKTLGLVGANFWTDTTQTADLITSNKKASVMTREIADERLEASVSDPTQANNGTIAIELARSAEGYSADPGITVTQLAPTIKFTVNVNGAKGKSFHASFQLGEDTSGPVDPGEPELPSVIVDNADSAGVTRTGTWKTASTQTDRYGANYLHDDNAGKGTKSVTFTPNLPIAGSYEVYLMWPAHFNREDAVQVDVGHASGTTRTAVDQRSGGGVWHSIGTYEFLAGSGGSVTIRNDALGSPDGYVVADAVKFVAVG,Xanthan lyase,"Plays a role in xanthan depolymerization pathway by cleaving the linkage between the terminal mannosyl and glucuronyl residues of the side chain of xanthan to liberate pyruvylated mannose. Is highly specific for pyruvylated side-chains of xanthan and is not effective with hyaluronate, chondroitin A, gellan, heparin or pectin.",Decreased catalysis rate but increased affinity with substrate. Site-directed mutagenesis of the two residues demonstrated that R612 is a key residue in recognizing pyruvated mannose.,Decreased catalysis rate but increased affinity with substrate. Site-directed mutagenesis of the two residues demonstrated that R612 is a key residue in recognizing pyruvated mannose.
260,0,0,Q31125-A75H,MTMGLRAPHWVAVGLLTWAALGLLVAGHEGHGDLHKDVEEDFHGHSHGHSHEDFHHGHSHGHSHEDFHHGHGHTHESIWHGHAHSHDHGHSREELHHGHSHGHSHDSLHHGGHGHAHREHSHGTSREAGAPGIKHHLDTVTLWAYALGATVLISAAPFFVLFLIPVESNSPRHRSLLQILLSFASGGLLGDAFLHLIPHALEPHSHHAPEQPGHGHSHSGQGPILSVGLWVLSGIVAFLVVEKFVRHVKGGHGHSHGHGDRHAHGDSHTHGDRHECSSKEKPSTEEEKEVGGLRKRRGGNTGPRDGPVKPQSPEEEKAGSDLRVSGYLNLAADLAHNFTDGLAIGASFRGGRGLGILTTMTVLLHEVPHEVGDFAILVQSGCSKKQAMRLQLVTAIGALAGTACALLTEGGAVDSDVAGGAGPGWVLPFTAGGFIYVATVSVLPELLREASPLQSLLEVLGLLGGVAMMVLIAHLE,,-1.0,MTMGLRAPHWVAVGLLTWAALGLLVAGHEGHGDLHKDVEEDFHGHSHGHSHEDFHHGHSHGHSHEDFHHGHGHTAESIWHGHAHSHDHGHSREELHHGHSHGHSHDSLHHGGHGHAHREHSHGTSREAGAPGIKHHLDTVTLWAYALGATVLISAAPFFVLFLIPVESNSPRHRSLLQILLSFASGGLLGDAFLHLIPHALEPHSHHAPEQPGHGHSHSGQGPILSVGLWVLSGIVAFLVVEKFVRHVKGGHGHSHGHGDRHAHGDSHTHGDRHECSSKEKPSTEEEKEVGGLRKRRGGNTGPRDGPVKPQSPEEEKAGSDLRVSGYLNLAADLAHNFTDGLAIGASFRGGRGLGILTTMTVLLHEVPHEVGDFAILVQSGCSKKQAMRLQLVTAIGALAGTACALLTEGGAVDSDVAGGAGPGWVLPFTAGGFIYVATVSVLPELLREASPLQSLLEVLGLLGGVAMMVLIAHLE,Zinc transporter SLC39A7,"Transports Zn(2+) from the endoplasmic reticulum (ER)/Golgi apparatus to the cytosol, playing an essential role in the regulation of cytosolic zinc levels. Acts as gatekeeper of zinc release from intracellular stores, requiring post-translational activation by phosphorylation, resulting in activation of multiple downstream pathways leading to cell growth and proliferation. Has an essential role in B cell development and is required for proper B cell receptor signaling. Plays an important role in maintaining intestinal epithelial homeostasis and skin dermis development by regulating ER function. Controls cell signaling pathways involved in glucose metabolism in skeletal muscle. Has a protective role against ER stress in differents biological contexts. Mediates Zn(2+)-induced ferroptosis.",Restored METTL9-mediated methylation.,Restored METTL9-mediated methylation.
261,0,0,Q7G065-V139T,MQFMMPLDTNACAQPMRRAGEGAGTERLMERLNIGGMTQEKALRKRCFGDGVTGTARCVFTSDADRDTPHLRTQSSRKNYADASHVSAVILGGGTGVQLFPLTSTRATPAVPVGGCYRLIDIPMSNCFNSGINKIFVMTQFNSASLNRHIHHTYLGGGINFTDGSVQVLAATQMPDEPAGWFQGTADAIRKFMWILEDHYNQNNIEHVVILCGDQLYRMNYMELVQKHVDDNADITISCAPIDGSRASDYGLVKFDDSGRVIQFLEKPEGADLESMKVDTSFLSYAIDDKQKYPYIASMGIYVLKKDVLLDILKSKYAHLQDFGSEILPRAVLEHNVKACVFTEYWEDIGTIKSFFDANLALTEQPPKFEFYDPKTPFFTSPRYLPPARLEKCKIKDAIISDGCSFSECTIEHSVIGISSRVSIGCELKDTMMMGADQYETEEETSKLLFEGKVPIGIGENTKIRNCIIDMNARIGRNVIIANTQGVQESDHPEEGYYIRSGIVVILKNATIKDGTVI,,-1.0,MQFMMPLDTNACAQPMRRAGEGAGTERLMERLNIGGMTQEKALRKRCFGDGVTGTARCVFTSDADRDTPHLRTQSSRKNYADASHVSAVILGGGTGVQLFPLTSTRATPAVPVGGCYRLIDIPMSNCFNSGINKIFVMVQFNSASLNRHIHHTYLGGGINFTDGSVQVLAATQMPDEPAGWFQGTADAIRKFMWILEDHYNQNNIEHVVILCGDQLYRMNYMELVQKHVDDNADITISCAPIDGSRASDYGLVKFDDSGRVIQFLEKPEGADLESMKVDTSFLSYAIDDKQKYPYIASMGIYVLKKDVLLDILKSKYAHLQDFGSEILPRAVLEHNVKACVFTEYWEDIGTIKSFFDANLALTEQPPKFEFYDPKTPFFTSPRYLPPARLEKCKIKDAIISDGCSFSECTIEHSVIGISSRVSIGCELKDTMMMGADQYETEEETSKLLFEGKVPIGIGENTKIRNCIIDMNARIGRNVIIANTQGVQESDHPEEGYYIRSGIVVILKNATIKDGTVI,"Glucose-1-phosphate adenylyltransferase large subunit 2, cytosolic","Involved in synthesis of starch. Catalyzes the synthesis of ADP-glucose, a molecule that serves as an activated glycosyl donor for alpha-1,4-glucan synthesis. Essential for starch synthesis in seed endosperm (PubMed:17406793, Ref.13, PubMed:24747952, PubMed:27957808). Is essential for both catalytic and allosteric regulatory properties of the cytosolic heterotetramer enzyme.",Highly increases activity more than 3-fold. Seeds from the missense mutant containing were robustly plump and had seed weight and starch content comparable with the robust seeds from OsAGPL2 null mutants. The catalytic and allosteric regulatory properties of the mutant enzyme were significantly enhanced. The mutant enzyme had higher specific (catalytic) activity and affinity for the activator 3-phosphoglycerate (3-PGA). The mutant enzyme also showed less sensitivity to inhibition by the inhibitor inorganic phosphate (Pi) than the wild-type AGPase.,Highly increases activity more than 3-fold. Seeds from the missense mutant containing were robustly plump and had seed weight and starch content comparable with the robust seeds from OsAGPL2 null mutants. The catalytic and allosteric regulatory properties of the mutant enzyme were significantly enhanced. The mutant enzyme had higher specific (catalytic) activity and affinity for the activator 3-phosphoglycerate (3-PGA). The mutant enzyme also showed less sensitivity to inhibition by the inhibitor inorganic phosphate (Pi) than the wild-type AGPase.
262,0,0,B9EJA2-A540P,MATDSASCEPDLSRTPGDTEGATAEAAKKEFDVDTLSKSELRMLLSVMEGELEARDLVIEALRARRKEVFIQERYGRFNLNDPFLALQRDYEAGPGDKEKPVCTNPLSILEAVMAHCRKMQERMSAQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKNKHVVLMLVKECKQLSGKVVEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEIDKMKKMMEQMKKGSDGKPGLSLPRKTKDKRLASISVATEGPVTRSVACQTDVVTESTDPVKKLPLTVPIKPSTGSPLVPTNTKGNVGPSALLIRPGIDRQSSHSDLGPSPPTALPSSANRIEENGPSTGNAPDLSNSTPSTPSSTAPAAAQTPGTAPQNHSQAPTVHSLHSPCANTHPGLNPRIQAARFRFQGNANDPDQNGNNTQSPPSRDVSPTSRDNLVAKQLARNTVTQALSRFTSPQAGASSRLGVSPGGDAGTCPPVGRTGLKTPGAARVDRGNPPPIPPKKPGLSQTPSPPHPQLRASNAGAKVDNKIVASPPSTLPQGTKVVNEENVPKSSSPQLPPKPSIDLTVAPAGCPVSALATSQVGAWPAGTPGLNQPACSDSSLVIPATVAFCSSINPVSASSRSPGASDSLLVAASGWSPSLTPLLMSGGPAPLAGRPTLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFECIELLTAYNANINHSAAGGQTPLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVDSLKLLMYHRVRAHGNSLSSEEPKSGLFSLNGGESPTGPSKPVVPADLINHADKEGWTAAHIAASKGFKNCLEVLCRHGGLEPERRDKCNRTVHDVATDDCKHLLENLNALKIPLRISVGEIQPSNDVSDDFECEHTICTLNIRKQTSWEDFSKAVSQALTNHFQAISSDGWWSLEDG,,-1.0,MATDSASCEPDLSRTPGDTEGATAEAAKKEFDVDTLSKSELRMLLSVMEGELEARDLVIEALRARRKEVFIQERYGRFNLNDPFLALQRDYEAGPGDKEKPVCTNPLSILEAVMAHCRKMQERMSAQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKNKHVVLMLVKECKQLSGKVVEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEIDKMKKMMEQMKKGSDGKPGLSLPRKTKDKRLASISVATEGPVTRSVACQTDVVTESTDPVKKLPLTVPIKPSTGSPLVPTNTKGNVGPSALLIRPGIDRQSSHSDLGPSPPTALPSSANRIEENGPSTGNAPDLSNSTPSTPSSTAPAAAQTPGTAPQNHSQAPTVHSLHSPCANTHPGLNPRIQAARFRFQGNANDPDQNGNNTQSPPSRDVSPTSRDNLVAKQLARNTVTQALSRFTSPQAGASSRLGVSPGGDAGTCPPVGRTGLKTPGAARVDRGNPAPIPPKKPGLSQTPSPPHPQLRASNAGAKVDNKIVASPPSTLPQGTKVVNEENVPKSSSPQLPPKPSIDLTVAPAGCPVSALATSQVGAWPAGTPGLNQPACSDSSLVIPATVAFCSSINPVSASSRSPGASDSLLVAASGWSPSLTPLLMSGGPAPLAGRPTLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFECIELLTAYNANINHSAAGGQTPLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVDSLKLLMYHRVRAHGNSLSSEEPKSGLFSLNGGESPTGPSKPVVPADLINHADKEGWTAAHIAASKGFKNCLEVLCRHGGLEPERRDKCNRTVHDVATDDCKHLLENLNALKIPLRISVGEIQPSNDVSDDFECEHTICTLNIRKQTSWEDFSKAVSQALTNHFQAISSDGWWSLEDG,Cortactin-binding protein 2,"Regulates the dendritic spine distribution of CTTN/cortactin in hippocampal neurons, and thus controls dendritic spinogenesis and dendritic spine maintenance.",Almost complete gain of CTTN-binding and gain of regulation of spine density; when associated with A-543.,Almost complete gain of CTTN-binding and gain of regulation of spine density; when associated with A-543.
263,0,0,P25522-A226N,MSDNDTIVAQATPPGRGGVGILRISGFKAREVAETVLGKLPKPRYADYLPFKDADGSVLDQGIALWFPGPNSFTGEDVLELQGHGGPVILDLLLKRILTIPGLRIARPGEFSERAFLNDKLDLAQAEAIADLIDASSEQAARSALNSLQGAFSARVNHLVEALTHLRIYVEAAIDFPDEEIDFLSDGKIEAQLNDVIADLDAVRAEARQGSLLREGMKVVIAGRPNAGKSSLLNALAGREAAIVTDIAGTTRDVLREHIHIDGMPLHIIDTAGLREASDEVERIGIERAWQEIEQADRVLFMVDGTTTDAVDPAEIWPEFIARLPAKLPITVVRNKADITGETLGMSEVNGHALIRLSARTGEGVDVLRNHLKQSMGFDTNMEGGFLARRRHLQALEQAAEHLQQGKAQLLGAWAGELLAEELRLAQQNLSEITGEFTSDDLLGRIFSSFCIGK,,-1.0,MSDNDTIVAQATPPGRGGVGILRISGFKAREVAETVLGKLPKPRYADYLPFKDADGSVLDQGIALWFPGPNSFTGEDVLELQGHGGPVILDLLLKRILTIPGLRIARPGEFSERAFLNDKLDLAQAEAIADLIDASSEQAARSALNSLQGAFSARVNHLVEALTHLRIYVEAAIDFPDEEIDFLSDGKIEAQLNDVIADLDAVRAEARQGSLLREGMKVVIAGRPAAGKSSLLNALAGREAAIVTDIAGTTRDVLREHIHIDGMPLHIIDTAGLREASDEVERIGIERAWQEIEQADRVLFMVDGTTTDAVDPAEIWPEFIARLPAKLPITVVRNKADITGETLGMSEVNGHALIRLSARTGEGVDVLRNHLKQSMGFDTNMEGGFLARRRHLQALEQAAEHLQQGKAQLLGAWAGELLAEELRLAQQNLSEITGEFTSDDLLGRIFSSFCIGK,tRNA modification GTPase MnmE,"Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.",100-fold increase in GTPase activity. 5-fold increase of affinity for GTP.,100-fold increase in GTPase activity. 5-fold increase of affinity for GTP.
264,0,0,Q9ULZ3-A12L,MGRARDAILDALENLTAEELKKFKLKLLSVPLREGYGRIPRGALLSMDALDLTDKLVSFYLETYGAELTANVLRDMGLQEMAGQLQAATHQGSGAAPAGIQAPPQSAAKPGLHFIDQHRAALIARVTNVEWLLDALYGKVLTDEQYQAVRAEPTNPSKMRKLFSFTPAWNWTCKDLLLQALRESQSYLVEDLERS,,-1.0,MGRARDAILDAAENLTAEELKKFKLKLLSVPLREGYGRIPRGALLSMDALDLTDKLVSFYLETYGAELTANVLRDMGLQEMAGQLQAATHQGSGAAPAGIQAPPQSAAKPGLHFIDQHRAALIARVTNVEWLLDALYGKVLTDEQYQAVRAEPTNPSKMRKLFSFTPAWNWTCKDLLLQALRESQSYLVEDLERS,Apoptosis-associated speck-like protein containing a CARD,"Functions as key mediator in apoptosis and inflammation. Promotes caspase-mediated apoptosis involving predominantly caspase-8 and also caspase-9 in a probable cell type-specific manner. Involved in activation of the mitochondrial apoptotic pathway, promotes caspase-8-dependent proteolytic maturation of BID independently of FADD in certain cell types and also mediates mitochondrial translocation of BAX and activates BAX-dependent apoptosis coupled to activation of caspase-9, -2 and -3. Involved in innate immune response by acting as an integral adapter in the assembly of various inflammasomes (NLRP1, NLRP2, NLRP3, NLRP6, AIM2 and probably IFI16) which recruit and activate caspase-1 leading to processing and secretion of pro-inflammatory cytokines. Caspase-1-dependent inflammation leads to macrophage pyroptosis, a form of cell death. The function as activating adapter in different types of inflammasomes is mediated by the pyrin and CARD domains and their homotypic interactions. Clustered PYCARD nucleates the formation of caspase-1 filaments through the interaction of their respective CARD domains, acting as a platform for of caspase-1 polymerization. In the NLRP1 and NLRC4 inflammasomes seems not be required but facilitates the processing of procaspase-1. In cooperation with NOD2 involved in an inflammasome activated by bacterial muramyl dipeptide leading to caspase-1 activation. May be involved in RIGI-triggered pro-inflammatory responses and inflammasome activation. In collaboration with AIM2 which detects cytosolic double-stranded DNA may also be involved in a caspase-1-independent cell death that involves caspase-8. In adaptive immunity may be involved in maturation of dendritic cells to stimulate T-cell immunity and in cytoskeletal rearrangements coupled to chemotaxis and antigen uptake may be involved in post-transcriptional regulation of the guanine nucleotide exchange factor DOCK2; the latter function is proposed to involve the nuclear form. Also involved in transcriptional activation of cytokines and chemokines independent of the inflammasome; this function may involve AP-1, NF-kappa-B, MAPK and caspase-8 signaling pathways. For regulation of NF-kappa-B activating and inhibiting functions have been reported. Modulates NF-kappa-B induction at the level of the IKK complex by inhibiting kinase activity of CHUK and IKBK. Proposed to compete with RIPK2 for association with CASP1 thereby down-regulating CASP1-mediated RIPK2-dependent NF-kappa-B activation and activating interleukin-1 beta processing. Modulates host resistance to DNA virus infection, probably by inducing the cleavage of and inactivating CGAS in presence of cytoplasmic double-stranded DNA.May have a regulating effect on the function as inflammasome adapter.Seems to inhibit inflammasome-mediated maturation of interleukin-1 beta.",Enables homooligomerization. The mutation in ASC suppresses both apoptosis and NF-kappa B activation. Mutation of L12 to A in ASC protein promotes filament formation.,Enables homooligomerization. The mutation in ASC suppresses both apoptosis and NF-kappa B activation. Mutation of L12 to A in ASC protein promotes filament formation.
265,0,0,Q0IGK1-A429D,MVPPIIYKYKRRKDRRLGRDDDSSVMMTRRRPDSDFIEVSDENRSFALFKEDDEKNRDLGLVDDGSTNLVLQCHDDGCSLEKDNSNSLDDLFSGFVYKGVRRRKRDDFGSITTSNLVSPQIADDDDDSVSDSHIERQECSEFHVEVRRVSPYFQGSTVSQQSKEGCDSDSVCSKEGCSKVQAKVPRVSPYFQASTISQCDSDIVSSSQSGRNYRKGSSKRQVKVRRVSPYFQESTVSEQPNQAPKGLRNYFKVVKVSRYFHADGIQVNESQKEKSRNVRKTPIVSPVLSLSQKTDDVYLRKTPDNTWVPPRSPCNLLQEDHWHDPWRVLVICMLLNKTSGAQTRGVISDLFGLCTDAKTATEVKEEEIENLIKPLGLQKKRTKMIQRLSLEYLQESWTHVTQLHGVGKYAADAYAIFCNGNWDRVKPNDHMLNYYWDYLRIRYKL,,-1.0,MVPPIIYKYKRRKDRRLGRDDDSSVMMTRRRPDSDFIEVSDENRSFALFKEDDEKNRDLGLVDDGSTNLVLQCHDDGCSLEKDNSNSLDDLFSGFVYKGVRRRKRDDFGSITTSNLVSPQIADDDDDSVSDSHIERQECSEFHVEVRRVSPYFQGSTVSQQSKEGCDSDSVCSKEGCSKVQAKVPRVSPYFQASTISQCDSDIVSSSQSGRNYRKGSSKRQVKVRRVSPYFQESTVSEQPNQAPKGLRNYFKVVKVSRYFHADGIQVNESQKEKSRNVRKTPIVSPVLSLSQKTDDVYLRKTPDNTWVPPRSPCNLLQEDHWHDPWRVLVICMLLNKTSGAQTRGVISDLFGLCTDAKTATEVKEEEIENLIKPLGLQKKRTKMIQRLSLEYLQESWTHVTQLHGVGKYAADAYAIFCNGNWDRVKPNAHMLNYYWDYLRIRYKL,Methyl-CpG-binding domain protein 4-like protein,"Monofunctional DNA glycosylase targeting U:G and T:G mispairs. Excises uracil derivatives and exhibits a preference for a CpG sequence context, irrespective of the methylation status of the complementary strand. The activity follows a biphasic kinetics, with an initial burst of product accumulation followed by a slower phase. Specifically binds its reaction product. Triggers the base excision repair (BER) pathway.","Increases activity 160-fold. The enzyme binds to the abasic site product generated after excision, which enhances its catalytic turnover in vitro.","Increases activity 160-fold. The enzyme binds to the abasic site product generated after excision, which enhances its catalytic turnover in vitro."
266,0,0,P15917-A75H,MNIKKEFIKVISMSCLVTAITLSGPVFIPLVQGAGGHGDVGMHVKEKEKNKDENKRKDEERNKTQEEHLKEIMKHIVKIEVKGEEAVKKEAAEKLLEKVPSDVLEMYKAIGGKIYIVDGDITKHISLEALSEDKKKIKDIYGKDALLHEHYVYAKEGYEPVLVIQSSEDYVENTEKALNVYYEIGKILSRDILSKINQPYQKFLDVLNTIKNASDSDGQDLLFTNQLKEHPTDFSVEFLEQNSNEVQEVFAKAFAYYIEPQHRDVLQLYAPEAFNYMDKFNEQEINLSLEELKDQRMLARYEKWEKIKQHYQHWSDSLSEEGRGLLKKLQIPIEPKKDDIIHSLSQEEKELLKRIQIDSSDFLSTEEKEFLKKLQIDIRDSLSEEEKELLNRIQVDSSNPLSEKEKEFLKKLKLDIQPYDINQRLQDTGGLIDSPSINLDVRKQYKRDIQNIDALLHQSIGSTLYNKIYLYENMNINNLTATLGADLVDSTDNTKINRGIFNEFKKNFKYSISSNYMIVDINERPALDNERLKWRIQLSPDTRAGYLENGKLILQRNIGLEIKDVQIIKQSEKEYIRIDAKVVPKSKIDTKIQEAQLNINQEWNKALGLPKYTKLITFNVHNRYASNIVESAYLILNEWKNNIQSDLIKKVTNYLVDGNGRFVFTDITLPNIAEQYTHQDEIYEQVHSKGLYVPESRSILLHGPSKGVELRNDSEGFIHEFGHAVDDYAGYLLDKNQSDLVTNSKKFIDIFKEEGSNLTSYGRTNEAEFFAEAFRLMHSTDHAERLKVQKNAPKTFQFINDQIKFIINS,,-1.0,MNIKKEFIKVISMSCLVTAITLSGPVFIPLVQGAGGHGDVGMHVKEKEKNKDENKRKDEERNKTQEEHLKEIMKAIVKIEVKGEEAVKKEAAEKLLEKVPSDVLEMYKAIGGKIYIVDGDITKHISLEALSEDKKKIKDIYGKDALLHEHYVYAKEGYEPVLVIQSSEDYVENTEKALNVYYEIGKILSRDILSKINQPYQKFLDVLNTIKNASDSDGQDLLFTNQLKEHPTDFSVEFLEQNSNEVQEVFAKAFAYYIEPQHRDVLQLYAPEAFNYMDKFNEQEINLSLEELKDQRMLARYEKWEKIKQHYQHWSDSLSEEGRGLLKKLQIPIEPKKDDIIHSLSQEEKELLKRIQIDSSDFLSTEEKEFLKKLQIDIRDSLSEEEKELLNRIQVDSSNPLSEKEKEFLKKLKLDIQPYDINQRLQDTGGLIDSPSINLDVRKQYKRDIQNIDALLHQSIGSTLYNKIYLYENMNINNLTATLGADLVDSTDNTKINRGIFNEFKKNFKYSISSNYMIVDINERPALDNERLKWRIQLSPDTRAGYLENGKLILQRNIGLEIKDVQIIKQSEKEYIRIDAKVVPKSKIDTKIQEAQLNINQEWNKALGLPKYTKLITFNVHNRYASNIVESAYLILNEWKNNIQSDLIKKVTNYLVDGNGRFVFTDITLPNIAEQYTHQDEIYEQVHSKGLYVPESRSILLHGPSKGVELRNDSEGFIHEFGHAVDDYAGYLLDKNQSDLVTNSKKFIDIFKEEGSNLTSYGRTNEAEFFAEAFRLMHSTDHAERLKVQKNAPKTFQFINDQIKFIINS,Lethal factor,"Lethal factor (LF), which constitutes one of the three proteins composing the anthrax toxin, is able to trigger rapid cell death in macrophages. Acts as a protease that cleaves the N-terminal of most dual specificity mitogen-activated protein kinase kinases (MAPKKs or MAP2Ks) (except for MAP2K5): cleavage invariably occurs within the N-terminal proline-rich region preceding the kinase domain, thus disrupting a sequence involved in directing specific protein-protein interactions necessary for the assembly of signaling complexes. Also cleaves mouse Nlrp1b: host Nlrp1b cleavage promotes ubiquitination and degradation of the N-terminal part of Nlrp1b by the proteasome, thereby releasing the cleaved C-terminal part of Nlrp1b, which polymerizes and forms the Nlrp1b inflammasome followed by host cell pyroptosis. Able to cleave mouse Nlrp1b alleles 1 and 5, while it is not able to cleave Nlrp1b alleles 2, 3 and 4. In contrast, does not cleave NLRP1 human ortholog. LF is not toxic by itself and only acts as a lethal factor when associated with protective antigen (PA) to form the lethal toxin (LeTx): PA is required for LF translocation into the host cytosol.",Enhanced translocation into host cytoplasm.,Enhanced translocation into host cytoplasm.
267,0,0,Q9JJS6-A457E,MEIIFGQNKKEQLEPVQAKVTGSIPAWLQGTLLRNGPGMHTVGESKYNHWFDGLALLHSFSIRDGEVFYRSKYLQSDTYIANIEANRIVVSEFGTMAYPDPCKNIFSKAFSYLSHTIPDFTDNCLINIMKCGEDFYATTETNYIRKIDPQTLETLEKVDYRKYVAVNLATSHPHYDEAGNVLNMGTSVVDKGRTKYVIFKIPATVPDSKKKGKSPVKHAEVFCSISSRSLLSPSYYHSFGVTENYVVFLEQPFKLDILKMATAYMRGVSWASCMSFDREDKTYIHIIDQRTRKPVPTKFYTDPMVVFHHVNAYEEDGCVLFDVIAYEDSSLYQLFYLANLNKDFEEKSRLTSVPTLRRFAVPLHVDKDAEVGSNLVKVSSTTATALKEKDGHVYCQPEVLYEGLELPRINYAYNGKPYRYIFAAEVQWSPVPTKILKYDILTKSSLKWSEESCWPAEPLFVPTPGAKDEDDGVILSAIVSTDPQKLPFLLILDAKSFTELARASVDADMHLDLHGLFIPDADWNAVKQTPAETQEVENSDHPTDPTAPELSHSENDFTAGHGGSSL,,-1.0,MEIIFGQNKKEQLEPVQAKVTGSIPAWLQGTLLRNGPGMHTVGESKYNHWFDGLALLHSFSIRDGEVFYRSKYLQSDTYIANIEANRIVVSEFGTMAYPDPCKNIFSKAFSYLSHTIPDFTDNCLINIMKCGEDFYATTETNYIRKIDPQTLETLEKVDYRKYVAVNLATSHPHYDEAGNVLNMGTSVVDKGRTKYVIFKIPATVPDSKKKGKSPVKHAEVFCSISSRSLLSPSYYHSFGVTENYVVFLEQPFKLDILKMATAYMRGVSWASCMSFDREDKTYIHIIDQRTRKPVPTKFYTDPMVVFHHVNAYEEDGCVLFDVIAYEDSSLYQLFYLANLNKDFEEKSRLTSVPTLRRFAVPLHVDKDAEVGSNLVKVSSTTATALKEKDGHVYCQPEVLYEGLELPRINYAYNGKPYRYIFAAEVQWSPVPTKILKYDILTKSSLKWSEESCWPAAPLFVPTPGAKDEDDGVILSAIVSTDPQKLPFLLILDAKSFTELARASVDADMHLDLHGLFIPDADWNAVKQTPAETQEVENSDHPTDPTAPELSHSENDFTAGHGGSSL,"Beta,beta-carotene 15,15'-dioxygenase",Symmetrically cleaves beta-carotene into two molecules of retinal using a dioxygenase mechanism.,"Increased beta-carotene 15,15'-monooxygenase activity. Mutation of E457 caused total gain of activity.","Increased beta-carotene 15,15'-monooxygenase activity. Mutation of E457 caused total gain of activity."
268,0,0,Q31125-A204H,MTMGLRAPHWVAVGLLTWAALGLLVAGHEGHGDLHKDVEEDFHGHSHGHSHEDFHHGHSHGHSHEDFHHGHGHTHESIWHGHAHSHDHGHSREELHHGHSHGHSHDSLHHGGHGHAHREHSHGTSREAGAPGIKHHLDTVTLWAYALGATVLISAAPFFVLFLIPVESNSPRHRSLLQILLSFASGGLLGDAFLHLIPHALEPHSHHAPEQPGHGHSHSGQGPILSVGLWVLSGIVAFLVVEKFVRHVKGGHGHSHGHGDRHAHGDSHTHGDRHECSSKEKPSTEEEKEVGGLRKRRGGNTGPRDGPVKPQSPEEEKAGSDLRVSGYLNLAADLAHNFTDGLAIGASFRGGRGLGILTTMTVLLHEVPHEVGDFAILVQSGCSKKQAMRLQLVTAIGALAGTACALLTEGGAVDSDVAGGAGPGWVLPFTAGGFIYVATVSVLPELLREASPLQSLLEVLGLLGGVAMMVLIAHLE,,-1.0,MTMGLRAPHWVAVGLLTWAALGLLVAGHEGHGDLHKDVEEDFHGHSHGHSHEDFHHGHSHGHSHEDFHHGHGHTHESIWHGHAHSHDHGHSREELHHGHSHGHSHDSLHHGGHGHAHREHSHGTSREAGAPGIKHHLDTVTLWAYALGATVLISAAPFFVLFLIPVESNSPRHRSLLQILLSFASGGLLGDAFLHLIPHALEPASHHAPEQPGHGHSHSGQGPILSVGLWVLSGIVAFLVVEKFVRHVKGGHGHSHGHGDRHAHGDSHTHGDRHECSSKEKPSTEEEKEVGGLRKRRGGNTGPRDGPVKPQSPEEEKAGSDLRVSGYLNLAADLAHNFTDGLAIGASFRGGRGLGILTTMTVLLHEVPHEVGDFAILVQSGCSKKQAMRLQLVTAIGALAGTACALLTEGGAVDSDVAGGAGPGWVLPFTAGGFIYVATVSVLPELLREASPLQSLLEVLGLLGGVAMMVLIAHLE,Zinc transporter SLC39A7,"Transports Zn(2+) from the endoplasmic reticulum (ER)/Golgi apparatus to the cytosol, playing an essential role in the regulation of cytosolic zinc levels. Acts as gatekeeper of zinc release from intracellular stores, requiring post-translational activation by phosphorylation, resulting in activation of multiple downstream pathways leading to cell growth and proliferation. Has an essential role in B cell development and is required for proper B cell receptor signaling. Plays an important role in maintaining intestinal epithelial homeostasis and skin dermis development by regulating ER function. Controls cell signaling pathways involved in glucose metabolism in skeletal muscle. Has a protective role against ER stress in differents biological contexts. Mediates Zn(2+)-induced ferroptosis.",Increased METTL9-mediated methylation; when associated with A-216.,Increased METTL9-mediated methylation; when associated with A-216.
269,0,0,Q68CZ1-P695A,MSGPTDETAGDLPVKDTGLNLFGMGGLQETSTTRTMKSRQAVSRVSREELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIRLVNDKKRYERVGGGPKRLGRDVEMEEMIEQLQEKVHELEKQNETLKNRLISAKQQLQTQGYRQTPYNNVQSRINTGRRKANENAGLQECPRKGIKFQDADVAETPHPMFTKYGNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIELSLLQLREQQATDQRSNIRDNVEMIKLHKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQLHSMKFSERRIEELQDRINDLEKERELLKENYDKLYDSAFSAAHEEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQQLDELKKRIKLYNQENDINADELSEALLLIKAQKEQKNGDLSFLVKVDSEINKDLERSMRELQATHAETVQELEKTRNMLIMQHKINKDYQMEVEAVTRKMENLQQDYELKVEQYVHLLDIRAARIHKLEAQLKDIAYGTKQYKFKPEIMPDDSVDEFDETIHLERGENLFEIHINKVTFSSEVLQASGDKEPVTFCTYAFYDFELQTTPVVRGLHPEYNFTSQYLVHVNDLFLQYIQKNTITLEVHQAYSTEYETIAACQLKFHEILEKSGRIFCTASLIGTKGDIPNFGTVEYWFRLRVPMDQAIRLYRERAKALGYITSNFKGPEHMQSLSQQAPKTAQLSSTDSTDGNLNELHITIRCCNHLQSRASHLQPHPYVVYKFFDFADHDTAIIPSSNDPQFDDHMYFPVPMNMDLDRYLKSESLSFYVFDDSDTQENIYIGKVNVPLISLAHDRCISGIFELTDHQKHPAGTIHVILKWKFAYLPPSGSITTEDLGNFIRSEEPEVVQRLPPASSVSTLVLAPRPKPRQRLTPVDKKVSFVDIMPHQSDETSPPPEDRKEISPEVEHIPEIEINMLTVPHVPKVSQE,,-1.0,MSGPTDETAGDLPVKDTGLNLFGMGGLQETSTTRTMKSRQAVSRVSREELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIRLVNDKKRYERVGGGPKRLGRDVEMEEMIEQLQEKVHELEKQNETLKNRLISAKQQLQTQGYRQTPYNNVQSRINTGRRKANENAGLQECPRKGIKFQDADVAETPHPMFTKYGNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIELSLLQLREQQATDQRSNIRDNVEMIKLHKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQLHSMKFSERRIEELQDRINDLEKERELLKENYDKLYDSAFSAAHEEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQQLDELKKRIKLYNQENDINADELSEALLLIKAQKEQKNGDLSFLVKVDSEINKDLERSMRELQATHAETVQELEKTRNMLIMQHKINKDYQMEVEAVTRKMENLQQDYELKVEQYVHLLDIRAARIHKLEAQLKDIAYGTKQYKFKPEIMPDDSVDEFDETIHLERGENLFEIHINKVTFSSEVLQASGDKEPVTFCTYAFYDFELQTTPVVRGLHPEYNFTSQYLVHVNDLFLQYIQKNTITLEVHQAYSTEYETIAPCQLKFHEILEKSGRIFCTASLIGTKGDIPNFGTVEYWFRLRVPMDQAIRLYRERAKALGYITSNFKGPEHMQSLSQQAPKTAQLSSTDSTDGNLNELHITIRCCNHLQSRASHLQPHPYVVYKFFDFADHDTAIIPSSNDPQFDDHMYFPVPMNMDLDRYLKSESLSFYVFDDSDTQENIYIGKVNVPLISLAHDRCISGIFELTDHQKHPAGTIHVILKWKFAYLPPSGSITTEDLGNFIRSEEPEVVQRLPPASSVSTLVLAPRPKPRQRLTPVDKKVSFVDIMPHQSDETSPPPEDRKEISPEVEHIPEIEINMLTVPHVPKVSQE,Protein fantom,"Negatively regulates signaling through the G-protein coupled thromboxane A2 receptor (TBXA2R). May be involved in mechanisms like programmed cell death, craniofacial development, patterning of the limbs, and formation of the left-right axis. Involved in the organization of apical junctions; the function is proposed to implicate a NPHP1-4-8 module. Does not seem to be strictly required for ciliogenesis. Involved in establishment of planar cell polarity such as in cochlear sensory epithelium and is proposed to implicate stabilization of disheveled proteins. Involved in regulation of proteasomal activity at the primary cilium probably implicating association with PSDM2.",Highly affects interaction with NPHP4. The RPGRIP1L missense mutations found in CORS individuals enhance the interaction between RPGRIP1L and nephrocystin-4.,Highly affects interaction with NPHP4. The RPGRIP1L missense mutations found in CORS individuals enhance the interaction between RPGRIP1L and nephrocystin-4.
270,0,0,Q9JJS6-A58H,MEIIFGQNKKEQLEPVQAKVTGSIPAWLQGTLLRNGPGMHTVGESKYNHWFDGLALLHSFSIRDGEVFYRSKYLQSDTYIANIEANRIVVSEFGTMAYPDPCKNIFSKAFSYLSHTIPDFTDNCLINIMKCGEDFYATTETNYIRKIDPQTLETLEKVDYRKYVAVNLATSHPHYDEAGNVLNMGTSVVDKGRTKYVIFKIPATVPDSKKKGKSPVKHAEVFCSISSRSLLSPSYYHSFGVTENYVVFLEQPFKLDILKMATAYMRGVSWASCMSFDREDKTYIHIIDQRTRKPVPTKFYTDPMVVFHHVNAYEEDGCVLFDVIAYEDSSLYQLFYLANLNKDFEEKSRLTSVPTLRRFAVPLHVDKDAEVGSNLVKVSSTTATALKEKDGHVYCQPEVLYEGLELPRINYAYNGKPYRYIFAAEVQWSPVPTKILKYDILTKSSLKWSEESCWPAEPLFVPTPGAKDEDDGVILSAIVSTDPQKLPFLLILDAKSFTELARASVDADMHLDLHGLFIPDADWNAVKQTPAETQEVENSDHPTDPTAPELSHSENDFTAGHGGSSL,,-1.0,MEIIFGQNKKEQLEPVQAKVTGSIPAWLQGTLLRNGPGMHTVGESKYNHWFDGLALLASFSIRDGEVFYRSKYLQSDTYIANIEANRIVVSEFGTMAYPDPCKNIFSKAFSYLSHTIPDFTDNCLINIMKCGEDFYATTETNYIRKIDPQTLETLEKVDYRKYVAVNLATSHPHYDEAGNVLNMGTSVVDKGRTKYVIFKIPATVPDSKKKGKSPVKHAEVFCSISSRSLLSPSYYHSFGVTENYVVFLEQPFKLDILKMATAYMRGVSWASCMSFDREDKTYIHIIDQRTRKPVPTKFYTDPMVVFHHVNAYEEDGCVLFDVIAYEDSSLYQLFYLANLNKDFEEKSRLTSVPTLRRFAVPLHVDKDAEVGSNLVKVSSTTATALKEKDGHVYCQPEVLYEGLELPRINYAYNGKPYRYIFAAEVQWSPVPTKILKYDILTKSSLKWSEESCWPAEPLFVPTPGAKDEDDGVILSAIVSTDPQKLPFLLILDAKSFTELARASVDADMHLDLHGLFIPDADWNAVKQTPAETQEVENSDHPTDPTAPELSHSENDFTAGHGGSSL,"Beta,beta-carotene 15,15'-dioxygenase",Symmetrically cleaves beta-carotene into two molecules of retinal using a dioxygenase mechanism.,"Decreased significant effect on beta-carotene 15,15'-monooxygenase activity. Increased catalytic efficiency.","Decreased significant effect on beta-carotene 15,15'-monooxygenase activity. Increased catalytic efficiency."
271,0,0,P15917-A181Y,MNIKKEFIKVISMSCLVTAITLSGPVFIPLVQGAGGHGDVGMHVKEKEKNKDENKRKDEERNKTQEEHLKEIMKHIVKIEVKGEEAVKKEAAEKLLEKVPSDVLEMYKAIGGKIYIVDGDITKHISLEALSEDKKKIKDIYGKDALLHEHYVYAKEGYEPVLVIQSSEDYVENTEKALNVYYEIGKILSRDILSKINQPYQKFLDVLNTIKNASDSDGQDLLFTNQLKEHPTDFSVEFLEQNSNEVQEVFAKAFAYYIEPQHRDVLQLYAPEAFNYMDKFNEQEINLSLEELKDQRMLARYEKWEKIKQHYQHWSDSLSEEGRGLLKKLQIPIEPKKDDIIHSLSQEEKELLKRIQIDSSDFLSTEEKEFLKKLQIDIRDSLSEEEKELLNRIQVDSSNPLSEKEKEFLKKLKLDIQPYDINQRLQDTGGLIDSPSINLDVRKQYKRDIQNIDALLHQSIGSTLYNKIYLYENMNINNLTATLGADLVDSTDNTKINRGIFNEFKKNFKYSISSNYMIVDINERPALDNERLKWRIQLSPDTRAGYLENGKLILQRNIGLEIKDVQIIKQSEKEYIRIDAKVVPKSKIDTKIQEAQLNINQEWNKALGLPKYTKLITFNVHNRYASNIVESAYLILNEWKNNIQSDLIKKVTNYLVDGNGRFVFTDITLPNIAEQYTHQDEIYEQVHSKGLYVPESRSILLHGPSKGVELRNDSEGFIHEFGHAVDDYAGYLLDKNQSDLVTNSKKFIDIFKEEGSNLTSYGRTNEAEFFAEAFRLMHSTDHAERLKVQKNAPKTFQFINDQIKFIINS,,-1.0,MNIKKEFIKVISMSCLVTAITLSGPVFIPLVQGAGGHGDVGMHVKEKEKNKDENKRKDEERNKTQEEHLKEIMKHIVKIEVKGEEAVKKEAAEKLLEKVPSDVLEMYKAIGGKIYIVDGDITKHISLEALSEDKKKIKDIYGKDALLHEHYVYAKEGYEPVLVIQSSEDYVENTEKALNVAYEIGKILSRDILSKINQPYQKFLDVLNTIKNASDSDGQDLLFTNQLKEHPTDFSVEFLEQNSNEVQEVFAKAFAYYIEPQHRDVLQLYAPEAFNYMDKFNEQEINLSLEELKDQRMLARYEKWEKIKQHYQHWSDSLSEEGRGLLKKLQIPIEPKKDDIIHSLSQEEKELLKRIQIDSSDFLSTEEKEFLKKLQIDIRDSLSEEEKELLNRIQVDSSNPLSEKEKEFLKKLKLDIQPYDINQRLQDTGGLIDSPSINLDVRKQYKRDIQNIDALLHQSIGSTLYNKIYLYENMNINNLTATLGADLVDSTDNTKINRGIFNEFKKNFKYSISSNYMIVDINERPALDNERLKWRIQLSPDTRAGYLENGKLILQRNIGLEIKDVQIIKQSEKEYIRIDAKVVPKSKIDTKIQEAQLNINQEWNKALGLPKYTKLITFNVHNRYASNIVESAYLILNEWKNNIQSDLIKKVTNYLVDGNGRFVFTDITLPNIAEQYTHQDEIYEQVHSKGLYVPESRSILLHGPSKGVELRNDSEGFIHEFGHAVDDYAGYLLDKNQSDLVTNSKKFIDIFKEEGSNLTSYGRTNEAEFFAEAFRLMHSTDHAERLKVQKNAPKTFQFINDQIKFIINS,Lethal factor,"Lethal factor (LF), which constitutes one of the three proteins composing the anthrax toxin, is able to trigger rapid cell death in macrophages. Acts as a protease that cleaves the N-terminal of most dual specificity mitogen-activated protein kinase kinases (MAPKKs or MAP2Ks) (except for MAP2K5): cleavage invariably occurs within the N-terminal proline-rich region preceding the kinase domain, thus disrupting a sequence involved in directing specific protein-protein interactions necessary for the assembly of signaling complexes. Also cleaves mouse Nlrp1b: host Nlrp1b cleavage promotes ubiquitination and degradation of the N-terminal part of Nlrp1b by the proteasome, thereby releasing the cleaved C-terminal part of Nlrp1b, which polymerizes and forms the Nlrp1b inflammasome followed by host cell pyroptosis. Able to cleave mouse Nlrp1b alleles 1 and 5, while it is not able to cleave Nlrp1b alleles 2, 3 and 4. In contrast, does not cleave NLRP1 human ortholog. LF is not toxic by itself and only acts as a lethal factor when associated with protective antigen (PA) to form the lethal toxin (LeTx): PA is required for LF translocation into the host cytosol.",Gain of ability to bind to PA. The mutation in the lethal factor protein was found to be proficient in its ability to lyse . 1 cells and its binding ability to PA63 was significantly enhanced. This suggests that the Y181 amino acid plays a negligible role in the process of binding of LF to PA63.,Gain of ability to bind to PA. The mutation in the lethal factor protein was found to be proficient in its ability to lyse . 1 cells and its binding ability to PA63 was significantly enhanced. This suggests that the Y181 amino acid plays a negligible role in the process of binding of LF to PA63.
272,0,0,Q9IK90-A93P,MEPDIKSISSESMEGVSDFSPSSWEHGGYLDKVEPEIDENGSMIPKYKIYTPGANERKYNNYMYLICYGFVEDVERTPETGKRKKIRTIAAYPLGVGKSASHPQDLLEELCSLKVTVRRTAGSTEKIVFGSSGPLNHLVPWKKVLTSGSIFNAVKVCRNVDQIQLDKHQALRIFFLSITKLNDSGIYMIPRTMLEFRRNNAIAFNLLVYLKIDADLSKMGIQGSLDKDGFKVASFMLHLGNFVRRAGKYYSVDYCRRKIDRMKLQFSLGSIGGLSLHIKINGVISKRLFAQMGFQKNLCFSLMDINPWLNRLTWNNSCEISRVAAVLQPSIPREFMIYDDVFIDNTGRILKG,,-1.0,MEPDIKSISSESMEGVSDFSPSSWEHGGYLDKVEPEIDENGSMIPKYKIYTPGANERKYNNYMYLICYGFVEDVERTPETGKRKKIRTIAAYALGVGKSASHPQDLLEELCSLKVTVRRTAGSTEKIVFGSSGPLNHLVPWKKVLTSGSIFNAVKVCRNVDQIQLDKHQALRIFFLSITKLNDSGIYMIPRTMLEFRRNNAIAFNLLVYLKIDADLSKMGIQGSLDKDGFKVASFMLHLGNFVRRAGKYYSVDYCRRKIDRMKLQFSLGSIGGLSLHIKINGVISKRLFAQMGFQKNLCFSLMDINPWLNRLTWNNSCEISRVAAVLQPSIPREFMIYDDVFIDNTGRILKG,Matrix protein,Plays a crucial role in virion assembly and budding. Forms a shell at the inner face of the plasma membrane. Transits through the host nucleus before gaining the functional ability to localize and bud from the plasma membrane. Mediates together with fusion protein the incorporation of the glycoprotein to the viral particles. Participates also in the inhibition of the host interferon type I antiviral response by interacting with and thereby inhibiting host TRIM6.,Complete gain of budding.,Complete gain of budding.
273,0,0,P25522-A256R,MSDNDTIVAQATPPGRGGVGILRISGFKAREVAETVLGKLPKPRYADYLPFKDADGSVLDQGIALWFPGPNSFTGEDVLELQGHGGPVILDLLLKRILTIPGLRIARPGEFSERAFLNDKLDLAQAEAIADLIDASSEQAARSALNSLQGAFSARVNHLVEALTHLRIYVEAAIDFPDEEIDFLSDGKIEAQLNDVIADLDAVRAEARQGSLLREGMKVVIAGRPNAGKSSLLNALAGREAAIVTDIAGTTRDVLREHIHIDGMPLHIIDTAGLREASDEVERIGIERAWQEIEQADRVLFMVDGTTTDAVDPAEIWPEFIARLPAKLPITVVRNKADITGETLGMSEVNGHALIRLSARTGEGVDVLRNHLKQSMGFDTNMEGGFLARRRHLQALEQAAEHLQQGKAQLLGAWAGELLAEELRLAQQNLSEITGEFTSDDLLGRIFSSFCIGK,,-1.0,MSDNDTIVAQATPPGRGGVGILRISGFKAREVAETVLGKLPKPRYADYLPFKDADGSVLDQGIALWFPGPNSFTGEDVLELQGHGGPVILDLLLKRILTIPGLRIARPGEFSERAFLNDKLDLAQAEAIADLIDASSEQAARSALNSLQGAFSARVNHLVEALTHLRIYVEAAIDFPDEEIDFLSDGKIEAQLNDVIADLDAVRAEARQGSLLREGMKVVIAGRPNAGKSSLLNALAGREAAIVTDIAGTTRDVLAEHIHIDGMPLHIIDTAGLREASDEVERIGIERAWQEIEQADRVLFMVDGTTTDAVDPAEIWPEFIARLPAKLPITVVRNKADITGETLGMSEVNGHALIRLSARTGEGVDVLRNHLKQSMGFDTNMEGGFLARRRHLQALEQAAEHLQQGKAQLLGAWAGELLAEELRLAQQNLSEITGEFTSDDLLGRIFSSFCIGK,tRNA modification GTPase MnmE,"Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.",2-fold increase in GTPase activity and almost no change in affinity.,2-fold increase in GTPase activity and almost no change in affinity.
274,0,0,P32266-A224S,MNASPVRLLILRRQLATHPAILYSSPYIKSPLVHLHSRMSNVHRSAHANALSFVITRRSISHFPKIISKIIRLPIYVGGGMAAAGSYIAYKMEEASSFTKDKLDRIKDLGESMKEKFNKMFSGDKSQDGGHGNDGTVPTATLIAATSLDDDESKRQGDPKDDDDEDDDDEDDENDSVDTTQDEMLNLTKQMIEIRTILNKVDSSSAHLTLPSIVVIGSQSSGKSSVLESIVGREFLPKGSNMVTRRPIELTLVNTPNSNNVTADFPSMRLYNIKDFKEVKRMLMELNMAVPTSEAVSEEPIQLTIKSSRVPDLSLVDLPGYIQVEAADQPIELKTKIRDLCEKYLTAPNIILAISAADVDLANSSALKASKAADPKGLRTIGVITKLDLVDPEKARSILNNKKYPLSMGYVGVITKTPSSINRKHLGLFGEAPSSSLSGIFSKGQHGQSSGEENTNGLKQIVSHQFEKAYFKENKKYFTNCQVSTKKLREKLIKILEISMSNALEPTSTLIQQELDDTSYLFKVEFNDRHLTPKSYLLNNIDVLKLGIKEFQEKFHRNELKSILRAELDQKVLDVLATRYWKDDNLQDLSSSKLESDTDMLYWHKKLELASSGLTKMGIGRLSTMLTTNAILKELDNILESTQLKNHELIKDLVSNTAINVLNSKYYSTADQVENCIKPFKYEIDLEERDWSLARQHSINLIKEELRQCNSRYQAIKNAVGSKKLANVMGYLENESNLQKETLGMSKLLLERGSEAIFLDKRCKVLSFRLKMLKNKCHSTIEKDRCPEVFLSAVSDKLTSTAVLFLNVELLSDFFYNFPIELDRRLTLLGDEQVEMFAKEDPKISRHIELQKRKELLELALEKIDSILVFKKSYKGVSKNL,,-1.0,MNASPVRLLILRRQLATHPAILYSSPYIKSPLVHLHSRMSNVHRSAHANALSFVITRRSISHFPKIISKIIRLPIYVGGGMAAAGSYIAYKMEEASSFTKDKLDRIKDLGESMKEKFNKMFSGDKSQDGGHGNDGTVPTATLIAATSLDDDESKRQGDPKDDDDEDDDDEDDENDSVDTTQDEMLNLTKQMIEIRTILNKVDSSSAHLTLPSIVVIGSQSSGKASVLESIVGREFLPKGSNMVTRRPIELTLVNTPNSNNVTADFPSMRLYNIKDFKEVKRMLMELNMAVPTSEAVSEEPIQLTIKSSRVPDLSLVDLPGYIQVEAADQPIELKTKIRDLCEKYLTAPNIILAISAADVDLANSSALKASKAADPKGLRTIGVITKLDLVDPEKARSILNNKKYPLSMGYVGVITKTPSSINRKHLGLFGEAPSSSLSGIFSKGQHGQSSGEENTNGLKQIVSHQFEKAYFKENKKYFTNCQVSTKKLREKLIKILEISMSNALEPTSTLIQQELDDTSYLFKVEFNDRHLTPKSYLLNNIDVLKLGIKEFQEKFHRNELKSILRAELDQKVLDVLATRYWKDDNLQDLSSSKLESDTDMLYWHKKLELASSGLTKMGIGRLSTMLTTNAILKELDNILESTQLKNHELIKDLVSNTAINVLNSKYYSTADQVENCIKPFKYEIDLEERDWSLARQHSINLIKEELRQCNSRYQAIKNAVGSKKLANVMGYLENESNLQKETLGMSKLLLERGSEAIFLDKRCKVLSFRLKMLKNKCHSTIEKDRCPEVFLSAVSDKLTSTAVLFLNVELLSDFFYNFPIELDRRLTLLGDEQVEMFAKEDPKISRHIELQKRKELLELALEKIDSILVFKKSYKGVSKNL,"Dynamin-like GTPase MGM1, mitochondrial",Dynamin-related GTPase required for mitochondrial fusion. Coordinates interaction between the inner and outer mitochondrial membrane to promote the formation of the double membrane.,Loss of GTPase activity. A version of mgm1 mutated in a conserved residue in the putative GTP-binding site was able to complement any of the mutant defects. It also caused normal mitochondrial distribution and morphology when expressed at high levels in cells that also contained a wild-type copy of the gene. Mgm1p was localized to the mitochondrial outer membrane and fractionated as a component of a low molecular weight complex. Mutations cause mitochondrial fusion and a gain of mitochondrial DNA.,Loss of GTPase activity. A version of mgm1 mutated in a conserved residue in the putative GTP-binding site was able to complement any of the mutant defects. It also caused normal mitochondrial distribution and morphology when expressed at high levels in cells that also contained a wild-type copy of the gene. Mgm1p was localized to the mitochondrial outer membrane and fractionated as a component of a low molecular weight complex. Mutations cause mitochondrial fusion and a gain of mitochondrial DNA.
275,0,0,Q9UJ83-R456S,MPDSNFAERSEEQVSGAKVIAQALKTQDVEYIFGIVGIPVTEIAIAAQQLGIKYIGMRNEQAACYAASAIGYLTSRPGVCLVVSGPGLIHALGGMANANMNCWPLLVIGGSSERNQETMGAFQEFPQVEACRLYTKFSARPSSIEAIPFVIEKAVRSSIYGRPGACYVDIPADFVNLQVNVNSIKYMERCMSPPISMAETSAVCTAASVIRNAKQPLLIIGKGAAYAHAEESIKKLVEQYKLPFLPTPMGKGVVPDNHPYCVGAARSRALQFADVIVLFGARLNWILHFGLPPRYQPDVKFIQVDICAEELGNNVKPAVTLLGNIHAVTKQLLEELDKTPWQYPPESKWWKTLREKMKSNEAASKELASKKSLPMNYYTVFYHVQEQLPRDCFVVSEGANTMDIGRTVLQNYLPRHRLDAGTFGTMGVGLGFAIAAAVVAKDRSPGQWIICVEGDSAFGFSGMEVETICRYNLPIILLVVNNNGIYQGFDTDTWKEMLKFQDATAVVPPMCLLPNSHYEQVMTAFGGKGYFVQTPEELQKSLRQSLADTTKPSLINIMIEPQATRKAQDFHWLTRSNM,,-1.0,MPDSNFAERSEEQVSGAKVIAQALKTQDVEYIFGIVGIPVTEIAIAAQQLGIKYIGMRNEQAACYAASAIGYLTSRPGVCLVVSGPGLIHALGGMANANMNCWPLLVIGGSSERNQETMGAFQEFPQVEACRLYTKFSARPSSIEAIPFVIEKAVRSSIYGRPGACYVDIPADFVNLQVNVNSIKYMERCMSPPISMAETSAVCTAASVIRNAKQPLLIIGKGAAYAHAEESIKKLVEQYKLPFLPTPMGKGVVPDNHPYCVGAARSRALQFADVIVLFGARLNWILHFGLPPRYQPDVKFIQVDICAEELGNNVKPAVTLLGNIHAVTKQLLEELDKTPWQYPPESKWWKTLREKMKSNEAASKELASKKSLPMNYYTVFYHVQEQLPRDCFVVSEGANTMDIGRTVLQNYLPRHRLDAGTFGTMGVGLGFAIAAAVVAKDRSPGQWIICVEGDRAFGFSGMEVETICRYNLPIILLVVNNNGIYQGFDTDTWKEMLKFQDATAVVPPMCLLPNSHYEQVMTAFGGKGYFVQTPEELQKSLRQSLADTTKPSLINIMIEPQATRKAQDFHWLTRSNM,2-hydroxyacyl-CoA lyase 1,Peroxisomal 2-OH acyl-CoA lyase involved in the cleavage (C1 removal) reaction in the fatty acid alpha-oxydation in a thiamine pyrophosphate (TPP)-dependent manner. Involved in the degradation of 3-methyl-branched fatty acids like phytanic acid and the shortening of 2-hydroxy long-chain fatty acids. Plays a significant role in the biosynthesis of heptadecanal in the liver.,"Enhances subcellular localization. Enables lyase activity. Enhances subcellular localization, enables lyase activity, enhances oligomerization, and enhances binding to TTP; when associated with S-455. The mutation in the TPP-binding domain of HACL1 enhanced enzyme targeting and oligomerization, and enzyme activity was enhanced.","Enhances subcellular localization. Enables lyase activity. Enhances subcellular localization, enables lyase activity, enhances oligomerization, and enhances binding to TTP; when associated with S-455. The mutation in the TPP-binding domain of HACL1 enhanced enzyme targeting and oligomerization, and enzyme activity was enhanced."
276,0,0,P40240-A174F,MPVKGGSKCIKYLLFGFNFIFWLAGIAVLAIGLWLRFDSQTKSIFEQENNHSSFYTGVYILIGAGALMMLVGFLGCCGAVQESQCMLGLFFGFLLVIFAIEIAAAVWGYTHKDEVIKELQEFYKDTYQKLRSKDEPQRETLKAIHMALDCCGIAGPLEQFISDTCPKKQLLESFQVKPCPEAISEVFNNKFHIIGAVGIGIAVVMIFGMIFSMILCCAIRRSREMV,,-1.0,MPVKGGSKCIKYLLFGFNFIFWLAGIAVLAIGLWLRFDSQTKSIFEQENNHSSFYTGVYILIGAGALMMLVGFLGCCGAVQESQCMLGLFFGFLLVIFAIEIAAAVWGYTHKDEVIKELQEFYKDTYQKLRSKDEPQRETLKAIHMALDCCGIAGPLEQFISDTCPKKQLLESAQVKPCPEAISEVFNNKFHIIGAVGIGIAVVMIFGMIFSMILCCAIRRSREMV,CD9 antigen,"Integral membrane protein associated with integrins, which regulates different processes, such as sperm-egg fusion, platelet activation and aggregation, and cell adhesion. Present at the cell surface of oocytes and plays a key role in sperm-egg fusion, possibly by organizing multiprotein complexes and the morphology of the membrane required for the fusion. In myoblasts, associates with CD81 and PTGFRN and inhibits myotube fusion during muscle regeneration. In macrophages, associates with CD9 and beta-1 and beta-2 integrins, and prevents macrophage fusion into multinucleated giant cells specialized in ingesting complement-opsonized large particles. Also prevents the fusion between mononuclear cell progenitors into osteoclasts in charge of bone resorption. Acts as a receptor for PSG17. Involved in platelet activation and aggregation. Regulates paranodal junction formation. Involved in cell adhesion, cell motility and tumor metastasis. Also regulates integrin-dependent migration of macrophages, particularly relevant for inflammatory response in the lung.",4-fold increase of sperm-egg fusion. The gamete fusion level was increased fourfold.,4-fold increase of sperm-egg fusion. The gamete fusion level was increased fourfold.
277,0,0,O14746-A169Q,MPRAPRCRAVRSLLRSHYREVLPLATFVRRLGPQGWRLVQRGDPAAFRALVAQCLVCVPWDARPPPAAPSFRQVSCLKELVARVLQRLCERGAKNVLAFGFALLDGARGGPPEAFTTSVRSYLPNTVTDALRGSGAWGLLLRRVGDDVLVHLLARCALFVLVAPSCAYQVCGPPLYQLGAATQARPPPHASGPRRRLGCERAWNHSVREAGVPLGLPAPGARRRGGSASRSLPLPKRPRRGAAPEPERTPVGQGSWAHPGRTRGPSDRGFCVVSPARPAEEATSLEGALSGTRHSHPSVGRQHHAGPPSTSRPPRPWDTPCPPVYAETKHFLYSSGDKEQLRPSFLLSSLRPSLTGARRLVETIFLGSRPWMPGTPRRLPRLPQRYWQMRPLFLELLGNHAQCPYGVLLKTHCPLRAAVTPAAGVCAREKPQGSVAAPEEEDTDPRRLVQLLRQHSSPWQVYGFVRACLRRLVPPGLWGSRHNERRFLRNTKKFISLGKHAKLSLQELTWKMSVRDCAWLRRSPGVGCVPAAEHRLREEILAKFLHWLMSVYVVELLRSFFYVTETTFQKNRLFFYRKSVWSKLQSIGIRQHLKRVQLRELSEAEVRQHREARPALLTSRLRFIPKPDGLRPIVNMDYVVGARTFRREKRAERLTSRVKALFSVLNYERARRPGLLGASVLGLDDIHRAWRTFVLRVRAQDPPPELYFVKVDVTGAYDTIPQDRLTEVIASIIKPQNTYCVRRYAVVQKAAHGHVRKAFKSHVSTLTDLQPYMRQFVAHLQETSPLRDAVVIEQSSSLNEASSGLFDVFLRFMCHHAVRIRGKSYVQCQGIPQGSILSTLLCSLCYGDMENKLFAGIRRDGLLLRLVDDFLLVTPHLTHAKTFLRTLVRGVPEYGCVVNLRKTVVNFPVEDEALGGTAFVQMPAHGLFPWCGLLLDTRTLEVQSDYSSYARTSIRASLTFNRGFKAGRNMRRKLFGVLRLKCHSLFLDLQVNSLQTVCTNIYKILLLQAYRFHACVLQLPFHQQ,,-1.0,MPRAPRCRAVRSLLRSHYREVLPLATFVRRLGPQGWRLVQRGDPAAFRALVAQCLVCVPWDARPPPAAPSFRQVSCLKELVARVLQRLCERGAKNVLAFGFALLDGARGGPPEAFTTSVRSYLPNTVTDALRGSGAWGLLLRRVGDDVLVHLLARCALFVLVAPSCAYAVCGPPLYQLGAATQARPPPHASGPRRRLGCERAWNHSVREAGVPLGLPAPGARRRGGSASRSLPLPKRPRRGAAPEPERTPVGQGSWAHPGRTRGPSDRGFCVVSPARPAEEATSLEGALSGTRHSHPSVGRQHHAGPPSTSRPPRPWDTPCPPVYAETKHFLYSSGDKEQLRPSFLLSSLRPSLTGARRLVETIFLGSRPWMPGTPRRLPRLPQRYWQMRPLFLELLGNHAQCPYGVLLKTHCPLRAAVTPAAGVCAREKPQGSVAAPEEEDTDPRRLVQLLRQHSSPWQVYGFVRACLRRLVPPGLWGSRHNERRFLRNTKKFISLGKHAKLSLQELTWKMSVRDCAWLRRSPGVGCVPAAEHRLREEILAKFLHWLMSVYVVELLRSFFYVTETTFQKNRLFFYRKSVWSKLQSIGIRQHLKRVQLRELSEAEVRQHREARPALLTSRLRFIPKPDGLRPIVNMDYVVGARTFRREKRAERLTSRVKALFSVLNYERARRPGLLGASVLGLDDIHRAWRTFVLRVRAQDPPPELYFVKVDVTGAYDTIPQDRLTEVIASIIKPQNTYCVRRYAVVQKAAHGHVRKAFKSHVSTLTDLQPYMRQFVAHLQETSPLRDAVVIEQSSSLNEASSGLFDVFLRFMCHHAVRIRGKSYVQCQGIPQGSILSTLLCSLCYGDMENKLFAGIRRDGLLLRLVDDFLLVTPHLTHAKTFLRTLVRGVPEYGCVVNLRKTVVNFPVEDEALGGTAFVQMPAHGLFPWCGLLLDTRTLEVQSDYSSYARTSIRASLTFNRGFKAGRNMRRKLFGVLRLKCHSLFLDLQVNSLQTVCTNIYKILLLQAYRFHACVLQLPFHQQ,Telomerase reverse transcriptase,"Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. Active in progenitor and cancer cells. Inactive, or very low activity, in normal somatic cells. Catalytic component of the teleromerase holoenzyme complex whose main activity is the elongation of telomeres by acting as a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme. Catalyzes the RNA-dependent extension of 3'-chromosomal termini with the 6-nucleotide telomeric repeat unit, 5'-TTAGGG-3'. The catalytic cycle involves primer binding, primer extension and release of product once the template boundary has been reached or nascent product translocation followed by further extension. More active on substrates containing 2 or 3 telomeric repeats. Telomerase activity is regulated by a number of factors including telomerase complex-associated proteins, chaperones and polypeptide modifiers. Modulates Wnt signaling. Plays important roles in aging and antiapoptosis.","About 80% increase in enzymatic activity. Greatly enhanced incorporation of second nucleotide. Unchanged strength of binding to ssDNA. Significant effect on repeat addition processivity, nor on TR interaction nor on protein levels. This mutation may not affect the interactions of TERT with anchor sites in lower eukaryotes.","About 80% increase in enzymatic activity. Greatly enhanced incorporation of second nucleotide. Unchanged strength of binding to ssDNA. Significant effect on repeat addition processivity, nor on TR interaction nor on protein levels. This mutation may not affect the interactions of TERT with anchor sites in lower eukaryotes."
278,0,0,P06022-D26E,MQHDLFEHDPAIRQLIGHIDNIPAPELESRWPRSVVDLIDVLENELKRQNVSNPRELARKQAVALSCFLGGRQFYIPCGDTILTALRDDLLYCQFNGRNMEELRRQYRLSQPQIYQIIARQRKLHTRRHQPDLFSPETPK,,-1.0,MQHDLFEHDPAIRQLIGHIDNIPAPDLESRWPRSVVDLIDVLENELKRQNVSNPRELARKQAVALSCFLGGRQFYIPCGDTILTALRDDLLYCQFNGRNMEELRRQYRLSQPQIYQIIARQRKLHTRRHQPDLFSPETPK,Late transcription activator C,"Positive regulator of viral late genes transcription. Responsible for the transition from middle to late gene expression. Activates the Plys, PI, PP and Pmom late promoters thereby allowing the expression of viral endolysin and structural genes. Activates Pmom promoter by unwinding the DNA, thus realigning the promoter elements and recruiting the RNAP.","Increases DNA-binding activity and transactivation. No effect on dimerization. Mutations in residue E26 lead to unaltered Mg(2+)-induced conformation, reinforced DNA binding, and enhanced levels of transcription activation.","Increases DNA-binding activity and transactivation. No effect on dimerization. Mutations in residue E26 lead to unaltered Mg(2+)-induced conformation, reinforced DNA binding, and enhanced levels of transcription activation."
279,0,0,P21926-A9C,MPVKGGTKCIKYLLFGFNFIFWLAGIAVLAIGLWLRFDSQTKSIFEQETNNNNSSFYTGVYILIGAGALMMLVGFLGCCGAVQESQCMLGLFFGFLLVIFAIEIAAAIWGYSHKDEVIKEVQEFYKDTYNKLKTKDEPQRETLKAIHYALNCCGLAGGVEQFISDICPKKDVLETFTVKSCPDAIKEVFDNKFHIIGAVGIGIAVVMIFGMIFSMILCCAIRRNREMV,,-1.0,MPVKGGTKAIKYLLFGFNFIFWLAGIAVLAIGLWLRFDSQTKSIFEQETNNNNSSFYTGVYILIGAGALMMLVGFLGCCGAVQESQCMLGLFFGFLLVIFAIEIAAAIWGYSHKDEVIKEVQEFYKDTYNKLKTKDEPQRETLKAIHYALNCCGLAGGVEQFISDICPKKDVLETFTVKSCPDAIKEVFDNKFHIIGAVGIGIAVVMIFGMIFSMILCCAIRRNREMV,CD9 antigen,"Integral membrane protein associated with integrins, which regulates different processes, such as sperm-egg fusion, platelet activation and aggregation, and cell adhesion. Present at the cell surface of oocytes and plays a key role in sperm-egg fusion, possibly by organizing multiprotein complexes and the morphology of the membrane required for the fusion. In myoblasts, associates with CD81 and PTGFRN and inhibits myotube fusion during muscle regeneration. In macrophages, associates with CD81 and beta-1 and beta-2 integrins, and prevents macrophage fusion into multinucleated giant cells specialized in ingesting complement-opsonized large particles. Also prevents the fusion between mononuclear cell progenitors into osteoclasts in charge of bone resorption. Acts as a receptor for PSG17. Involved in platelet activation and aggregation. Regulates paranodal junction formation. Involved in cell adhesion, cell motility and tumor metastasis.",Gain of palmitoylation; when associated with A-78; A-79; A-87; A-218 and A-219.,Gain of palmitoylation; when associated with A-78; A-79; A-87; A-218 and A-219.
280,0,0,P25522-K252R,MSDNDTIVAQATPPGRGGVGILRISGFKAREVAETVLGKLPKPRYADYLPFKDADGSVLDQGIALWFPGPNSFTGEDVLELQGHGGPVILDLLLKRILTIPGLRIARPGEFSERAFLNDKLDLAQAEAIADLIDASSEQAARSALNSLQGAFSARVNHLVEALTHLRIYVEAAIDFPDEEIDFLSDGKIEAQLNDVIADLDAVRAEARQGSLLREGMKVVIAGRPNAGKSSLLNALAGREAAIVTDIAGTTRDVLREHIHIDGMPLHIIDTAGLREASDEVERIGIERAWQEIEQADRVLFMVDGTTTDAVDPAEIWPEFIARLPAKLPITVVRNKADITGETLGMSEVNGHALIRLSARTGEGVDVLRNHLKQSMGFDTNMEGGFLARRRHLQALEQAAEHLQQGKAQLLGAWAGELLAEELRLAQQNLSEITGEFTSDDLLGRIFSSFCIGK,,-1.0,MSDNDTIVAQATPPGRGGVGILRISGFKAREVAETVLGKLPKPRYADYLPFKDADGSVLDQGIALWFPGPNSFTGEDVLELQGHGGPVILDLLLKRILTIPGLRIARPGEFSERAFLNDKLDLAQAEAIADLIDASSEQAARSALNSLQGAFSARVNHLVEALTHLRIYVEAAIDFPDEEIDFLSDGKIEAQLNDVIADLDAVRAEARQGSLLREGMKVVIAGRPNAGKSSLLNALAGREAAIVTDIAGTTKDVLREHIHIDGMPLHIIDTAGLREASDEVERIGIERAWQEIEQADRVLFMVDGTTTDAVDPAEIWPEFIARLPAKLPITVVRNKADITGETLGMSEVNGHALIRLSARTGEGVDVLRNHLKQSMGFDTNMEGGFLARRRHLQALEQAAEHLQQGKAQLLGAWAGELLAEELRLAQQNLSEITGEFTSDDLLGRIFSSFCIGK,tRNA modification GTPase MnmE,"Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.",2-fold increase in GTPase activity and no change in affinity.,2-fold increase in GTPase activity and no change in affinity.
281,0,0,Q46389-A199N,MLIIGERINGMFGDIKRAIQERDPAPVQEWARRQEEGGARALDLNVGPAVQDKVSAMEWLVEVTQEVSNLTLCLDSTNIKAIEAGLKKCKNRAMINSTNAEREKVEKLFPLAVEHGAALIGLTMNKTGIPKDSDTRLAFAMELVAAADEFGLPMEDLYIDPLILPANVAQDHAPEVLKTLQQIKMLADPAPKTVLGLSNVSQNCQNRPLINRTFLAMAMACGLDAAIADACDEALIETAATAEILLNQTVYCDSFVKMFKTR,,-1.0,MLIIGERINGMFGDIKRAIQERDPAPVQEWARRQEEGGARALDLNVGPAVQDKVSAMEWLVEVTQEVSNLTLCLDSTNIKAIEAGLKKCKNRAMINSTNAEREKVEKLFPLAVEHGAALIGLTMNKTGIPKDSDTRLAFAMELVAAADEFGLPMEDLYIDPLILPANVAQDHAPEVLKTLQQIKMLADPAPKTVLGLSAVSQNCQNRPLINRTFLAMAMACGLDAAIADACDEALIETAATAEILLNQTVYCDSFVKMFKTR,5-methyltetrahydrofolate:corrinoid/iron-sulfur protein co-methyltransferase,Methyltransferase that mediates the transfer of a N5-methyl group of (6S)-methyltetrahydrofolate to the 5-methoxybenzimidazolylcobamide cofactor of a corrinoid/Fe-S protein (AcsC/AcsD) in the anaerobic acetyl-CoA pathway (Wood-Ljungdahl pathway) of carbon monoxide and carbon dioxide fixation.,"20-fold increased affinity for methyltetrahydrofolate and nearly enhanced catalytic activity. Variant exhibits only approximately 20-fold strengthened affinity for CH(3)-H(4)folate but a much more marked 20,000-40,000-fold effect on catalysis, suggesting that N-199 plays an important role in destabilizing a transition state or low energy intermediate for methyl transfer.","20-fold increased affinity for methyltetrahydrofolate and nearly enhanced catalytic activity. Variant exhibits only approximately 20-fold strengthened affinity for CH(3)-H(4)folate but a much more marked 20,000-40,000-fold effect on catalysis, suggesting that N-199 plays an important role in destabilizing a transition state or low energy intermediate for methyl transfer."
282,0,0,P9WGT3-D191T,MTATATEGAKPPFVSRSVLVTGGNRGIGLAIAQRLAADGHKVAVTHRGSGAPKGLFGVECDVTDSDAVDRAFTAVEEHQGPVEVLVSNAGLSADAFLMRMTEEKFEKVINANLTGAFRVAQRASRSMQRNKFGRMIFIGSVSGSWGIGNQANYAASKAGVIGMARSIARELSKANVTANVVAPGYIDTDMTRALDERIQQGALQFIPAKRVGTPAEVAGVVSFLASEDASYISGAVIPVDGGMGMGH,,-1.0,MTATATEGAKPPFVSRSVLVTGGNRGIGLAIAQRLAADGHKVAVTHRGSGAPKGLFGVECDVTDSDAVDRAFTAVEEHQGPVEVLVSNAGLSADAFLMRMTEEKFEKVINANLTGAFRVAQRASRSMQRNKFGRMIFIGSVSGSWGIGNQANYAASKAGVIGMARSIARELSKANVTANVVAPGYIDTDMDRALDERIQQGALQFIPAKRVGTPAEVAGVVSFLASEDASYISGAVIPVDGGMGMGH,3-oxoacyl-[acyl-carrier-protein] reductase MabA,"Part of the mycobacterial fatty acid elongation system FAS-II, which is involved in mycolic acid biosynthesis. Catalyzes the NADPH-dependent reduction of beta-ketoacyl derivatives, the second step of the FAS-II elongation cycle. May preferentially metabolize long-chain substrates (C8-C20). Can use CoA derivatives as substrates in vitro.","Increases reductase activity to over 90% of wild-type. Enhanced NADPH binding. Overproduction of the mutant leads to a significant promotion of de novo biosynthesis of mycolic acids. The MabA_T191D mutant, designed to mimic constitutive dephosphorylation, exhibited markedly increased ketoacyl reductase activity compared with the wild-type protein, as well as enhanced binding of the NADPH cofactor. Constitutive overexpression of the mabA_T191D allele in Mycobacterium bovis BCG strongly promoted mycobacterial growth. Conditional expression of the dephosphomimetic MabA_T191D led to a significant promotion of de novo biosynthesis of mycolic acids.","Increases reductase activity to over 90% of wild-type. Enhanced NADPH binding. Overproduction of the mutant leads to a significant promotion of de novo biosynthesis of mycolic acids. The MabA_T191D mutant, designed to mimic constitutive dephosphorylation, exhibited markedly increased ketoacyl reductase activity compared with the wild-type protein, as well as enhanced binding of the NADPH cofactor. Constitutive overexpression of the mabA_T191D allele in Mycobacterium bovis BCG strongly promoted mycobacterial growth. Conditional expression of the dephosphomimetic MabA_T191D led to a significant promotion of de novo biosynthesis of mycolic acids."
283,0,0,Q31125-A216H,MTMGLRAPHWVAVGLLTWAALGLLVAGHEGHGDLHKDVEEDFHGHSHGHSHEDFHHGHSHGHSHEDFHHGHGHTHESIWHGHAHSHDHGHSREELHHGHSHGHSHDSLHHGGHGHAHREHSHGTSREAGAPGIKHHLDTVTLWAYALGATVLISAAPFFVLFLIPVESNSPRHRSLLQILLSFASGGLLGDAFLHLIPHALEPHSHHAPEQPGHGHSHSGQGPILSVGLWVLSGIVAFLVVEKFVRHVKGGHGHSHGHGDRHAHGDSHTHGDRHECSSKEKPSTEEEKEVGGLRKRRGGNTGPRDGPVKPQSPEEEKAGSDLRVSGYLNLAADLAHNFTDGLAIGASFRGGRGLGILTTMTVLLHEVPHEVGDFAILVQSGCSKKQAMRLQLVTAIGALAGTACALLTEGGAVDSDVAGGAGPGWVLPFTAGGFIYVATVSVLPELLREASPLQSLLEVLGLLGGVAMMVLIAHLE,,-1.0,MTMGLRAPHWVAVGLLTWAALGLLVAGHEGHGDLHKDVEEDFHGHSHGHSHEDFHHGHSHGHSHEDFHHGHGHTHESIWHGHAHSHDHGHSREELHHGHSHGHSHDSLHHGGHGHAHREHSHGTSREAGAPGIKHHLDTVTLWAYALGATVLISAAPFFVLFLIPVESNSPRHRSLLQILLSFASGGLLGDAFLHLIPHALEPHSHHAPEQPGHGASHSGQGPILSVGLWVLSGIVAFLVVEKFVRHVKGGHGHSHGHGDRHAHGDSHTHGDRHECSSKEKPSTEEEKEVGGLRKRRGGNTGPRDGPVKPQSPEEEKAGSDLRVSGYLNLAADLAHNFTDGLAIGASFRGGRGLGILTTMTVLLHEVPHEVGDFAILVQSGCSKKQAMRLQLVTAIGALAGTACALLTEGGAVDSDVAGGAGPGWVLPFTAGGFIYVATVSVLPELLREASPLQSLLEVLGLLGGVAMMVLIAHLE,Zinc transporter SLC39A7,"Transports Zn(2+) from the endoplasmic reticulum (ER)/Golgi apparatus to the cytosol, playing an essential role in the regulation of cytosolic zinc levels. Acts as gatekeeper of zinc release from intracellular stores, requiring post-translational activation by phosphorylation, resulting in activation of multiple downstream pathways leading to cell growth and proliferation. Has an essential role in B cell development and is required for proper B cell receptor signaling. Plays an important role in maintaining intestinal epithelial homeostasis and skin dermis development by regulating ER function. Controls cell signaling pathways involved in glucose metabolism in skeletal muscle. Has a protective role against ER stress in differents biological contexts. Mediates Zn(2+)-induced ferroptosis.",Increased METTL9-mediated methylation; when associated with A-204.,Increased METTL9-mediated methylation; when associated with A-204.
284,0,0,Q06069-L395A,MKEVIAVKEITRFKTRTEEFSPYAWCKRMLENDPVSYHEGTDTWNVFKYEDVKRVLSDYKHFSSVRKRTTISVGTDSEEGSVPEKIQITESDPPDHRKRRSLLAAAFTPRSLQNWEPRIQEIADELIGQMDGGTEIDIVASLASPLPIIVMADLMGVPSKDRLLFKKWVDTLFLPFDREKQEEVDKLKQVAAKEYYQYLYPIVVQKRLNPADDIISDLLKSEVDGEMFTDDEVVRTTMLILGAGVETTSHLLANSFYSLLYDDKEVYQELHENLDLVPQAVEEMLRFRFNLIKLDRTVKEDNDLLGVELKEGDSVVVWMSAANMDEEMFEDPFTLNIHRPNNKKHLTFGNGPHFCLGAPLARLEAKIALTAFLKKFKHIEAVPSFQLEENLTDSATGQTLTSLPLKASRM,,-1.0,MKEVIAVKEITRFKTRTEEFSPYAWCKRMLENDPVSYHEGTDTWNVFKYEDVKRVLSDYKHFSSVRKRTTISVGTDSEEGSVPEKIQITESDPPDHRKRRSLLAAAFTPRSLQNWEPRIQEIADELIGQMDGGTEIDIVASLASPLPIIVMADLMGVPSKDRLLFKKWVDTLFLPFDREKQEEVDKLKQVAAKEYYQYLYPIVVQKRLNPADDIISDLLKSEVDGEMFTDDEVVRTTMLILGAGVETTSHLLANSFYSLLYDDKEVYQELHENLDLVPQAVEEMLRFRFNLIKLDRTVKEDNDLLGVELKEGDSVVVWMSAANMDEEMFEDPFTLNIHRPNNKKHLTFGNGPHFCLGAPLARLEAKIALTAFLKKFKHIEAVPSFQLEENLTDSLTGQTLTSLPLKASRM,Cytochrome P450,Has the capacity to hydroxylate certain steroids in the 15-beta position. Also hydroxylates progesterone in the 11-alpha and 9-beta position.,40% of 15-beta hydroxylation activity (for progesterone). The mutant was predicted to inhibit active-site formation and impede substrate binding. This mutant preserved the active-site structure and the hydroxylation activity of CYP106A2 significantly.,40% of 15-beta hydroxylation activity (for progesterone). The mutant was predicted to inhibit active-site formation and impede substrate binding. This mutant preserved the active-site structure and the hydroxylation activity of CYP106A2 significantly.
285,0,0,Q9FGL5-P677S,MRLKNFPFFVLFFFFCFNSNQSWGLMSSNQQPQFFKLMKNSLFGDALSTWNVYDVGTNYCNFTGVRCDGQGLVTDLDLSGLSLSGIFPDGVCSYFPNLRVLRLSHNHLNKSSSFLNTIPNCSLLRDLNMSSVYLKGTLPDFSQMKSLRVIDMSWNHFTGSFPLSIFNLTDLEYLNFNENPELDLWTLPDSVSKLTKLTHMLLMTCMLHGNIPRSIGNLTSLVDLELSGNFLSGEIPKEIGNLSNLRQLELYYNYHLTGSIPEEIGNLKNLTDIDISVSRLTGSIPDSICSLPNLRVLQLYNNSLTGEIPKSLGNSKTLKILSLYDNYLTGELPPNLGSSSPMIALDVSENRLSGPLPAHVCKSGKLLYFLVLQNRFTGSIPETYGSCKTLIRFRVASNRLVGTIPQGVMSLPHVSIIDLAYNSLSGPIPNAIGNAWNLSELFMQSNRISGVIPHELSHSTNLVKLDLSNNQLSGPIPSEVGRLRKLNLLVLQGNHLDSSIPDSLSNLKSLNVLDLSSNLLTGRIPENLSELLPTSINFSSNRLSGPIPVSLIRGGLVESFSDNPNLCIPPTAGSSDLKFPMCQEPHGKKKLSSIWAILVSVFILVLGVIMFYLRQRMSKNRAVIEQDETLASSFFSYDVKSFHRISFDQREILESLVDKNIVGHGGSGTVYRVELKSGEVVAVKKLWSQSNKDSASEDKMHLNKELKTEVETLGSIRHKNIVKLFSYFSSLDCSLLVYEYMPNGNLWDALHKGFVHLEWRTRHQIAVGVAQGLAYLHHDLSPPIIHRDIKSTNILLDVNYQPKVADFGIAKVLQARGKDSTTTVMAGTYGYLAPEYAYSSKATIKCDVYSFGVVLMELITGKKPVDSCFGENKNIVNWVSTKIDTKEGLIETLDKRLSESSKADMINALRVAIRCTSRTPTIRPTMNEVVQLLIDATPQGGPDMTSKPTTKIKDSIVSDHLTQTRL,,-1.0,MRLKNFPFFVLFFFFCFNSNQSWGLMSSNQQPQFFKLMKNSLFGDALSTWNVYDVGTNYCNFTGVRCDGQGLVTDLDLSGLSLSGIFPDGVCSYFPNLRVLRLSHNHLNKSSSFLNTIPNCSLLRDLNMSSVYLKGTLPDFSQMKSLRVIDMSWNHFTGSFPLSIFNLTDLEYLNFNENPELDLWTLPDSVSKLTKLTHMLLMTCMLHGNIPRSIGNLTSLVDLELSGNFLSGEIPKEIGNLSNLRQLELYYNYHLTGSIPEEIGNLKNLTDIDISVSRLTGSIPDSICSLPNLRVLQLYNNSLTGEIPKSLGNSKTLKILSLYDNYLTGELPPNLGSSSPMIALDVSENRLSGPLPAHVCKSGKLLYFLVLQNRFTGSIPETYGSCKTLIRFRVASNRLVGTIPQGVMSLPHVSIIDLAYNSLSGPIPNAIGNAWNLSELFMQSNRISGVIPHELSHSTNLVKLDLSNNQLSGPIPSEVGRLRKLNLLVLQGNHLDSSIPDSLSNLKSLNVLDLSSNLLTGRIPENLSELLPTSINFSSNRLSGPIPVSLIRGGLVESFSDNPNLCIPPTAGSSDLKFPMCQEPHGKKKLSSIWAILVSVFILVLGVIMFYLRQRMSKNRAVIEQDETLASSFFSYDVKSFHRISFDQREILESLVDKNIVGHGGSGTVYRVELKPGEVVAVKKLWSQSNKDSASEDKMHLNKELKTEVETLGSIRHKNIVKLFSYFSSLDCSLLVYEYMPNGNLWDALHKGFVHLEWRTRHQIAVGVAQGLAYLHHDLSPPIIHRDIKSTNILLDVNYQPKVADFGIAKVLQARGKDSTTTVMAGTYGYLAPEYAYSSKATIKCDVYSFGVVLMELITGKKPVDSCFGENKNIVNWVSTKIDTKEGLIETLDKRLSESSKADMINALRVAIRCTSRTPTIRPTMNEVVQLLIDATPQGGPDMTSKPTTKIKDSIVSDHLTQTRL,Receptor protein-tyrosine kinase CEPR1,"Receptor kinase involved in the perception of C-terminally encoded plant signaling peptide (CEP) and subsequent regulation of root and shoot development. Required for xylem and phloem cell files morphology and organization, probably by preventing ectopic lignification in phloem cells. Together with CEPR2, mediates systemic nitrogen (N)-demand signaling upon the perception of root-derived peptides (e.g. CEP1) via the up-regulation of genes involved in N uptake and assimilation pathways. Regulates positively lateral root initiation and development; probably repressed by the signaling peptide CEP5.","Short inflorescence stems and decreased anthocyanin accumulation in leaves. The mutants in this kinase display a reduced accumulation of lignified cells, typical of xylem or fiber cells, within the phloem. In addition, phloem cells are sometimes located distant from xylem cells in these mutants. Analyses of longitudinal profiles of xip1 mutant stems show well-formed cell files, indicating improvements in oriented cell divisions or cell morphology. We propose that XIP1 promotes proper lignification in phloem cells and is necessary to maintain the organization of cell files or cell morphology in conductive elements.","Short inflorescence stems and decreased anthocyanin accumulation in leaves. The mutants in this kinase display a reduced accumulation of lignified cells, typical of xylem or fiber cells, within the phloem. In addition, phloem cells are sometimes located distant from xylem cells in these mutants. Analyses of longitudinal profiles of xip1 mutant stems show well-formed cell files, indicating improvements in oriented cell divisions or cell morphology. We propose that XIP1 promotes proper lignification in phloem cells and is necessary to maintain the organization of cell files or cell morphology in conductive elements."
286,0,0,Q06069-S398Q,MKEVIAVKEITRFKTRTEEFSPYAWCKRMLENDPVSYHEGTDTWNVFKYEDVKRVLSDYKHFSSVRKRTTISVGTDSEEGSVPEKIQITESDPPDHRKRRSLLAAAFTPRSLQNWEPRIQEIADELIGQMDGGTEIDIVASLASPLPIIVMADLMGVPSKDRLLFKKWVDTLFLPFDREKQEEVDKLKQVAAKEYYQYLYPIVVQKRLNPADDIISDLLKSEVDGEMFTDDEVVRTTMLILGAGVETTSHLLANSFYSLLYDDKEVYQELHENLDLVPQAVEEMLRFRFNLIKLDRTVKEDNDLLGVELKEGDSVVVWMSAANMDEEMFEDPFTLNIHRPNNKKHLTFGNGPHFCLGAPLARLEAKIALTAFLKKFKHIEAVPSFQLEENLTDSATGQTLTSLPLKASRM,,-1.0,MKEVIAVKEITRFKTRTEEFSPYAWCKRMLENDPVSYHEGTDTWNVFKYEDVKRVLSDYKHFSSVRKRTTISVGTDSEEGSVPEKIQITESDPPDHRKRRSLLAAAFTPRSLQNWEPRIQEIADELIGQMDGGTEIDIVASLASPLPIIVMADLMGVPSKDRLLFKKWVDTLFLPFDREKQEEVDKLKQVAAKEYYQYLYPIVVQKRLNPADDIISDLLKSEVDGEMFTDDEVVRTTMLILGAGVETTSHLLANSFYSLLYDDKEVYQELHENLDLVPQAVEEMLRFRFNLIKLDRTVKEDNDLLGVELKEGDSVVVWMSAANMDEEMFEDPFTLNIHRPNNKKHLTFGNGPHFCLGAPLARLEAKIALTAFLKKFKHIEAVPSFQLEENLTDSATGSTLTSLPLKASRM,Cytochrome P450,Has the capacity to hydroxylate certain steroids in the 15-beta position. Also hydroxylates progesterone in the 11-alpha and 9-beta position.,Decrease to 30% of 15-beta hydroxylation activity (for progesterone). The mutant was predicted to participate in active-site formation and influence substrate binding. This mutant enhanced the active-site structure and the hydroxylation activity of CYP106A2 dramatically.,Decrease to 30% of 15-beta hydroxylation activity (for progesterone). The mutant was predicted to participate in active-site formation and influence substrate binding. This mutant enhanced the active-site structure and the hydroxylation activity of CYP106A2 dramatically.
287,0,0,Q96AX1-K441I,MAAHLSYGRVNLNVLREAVRRELREFLDKCAGSKAIVWDEYLTGPFGLIAQYSLLKEHEVEKMFTLKGNRLPAADVKNIIFFVRPRLELMDIIAENVLSEDRRGPTRDFHILFVPRRSLLCEQRLKDLGVLGSFIHREEYSLDLIPFDGDLLSMESEGAFKECYLEGDQTSLYHAAKGLMTLQALYGTIPQIFGKGECARQVANMMIRMKREFTGSQNSIFPVFDNLLLLDRNVDLLTPLATQLTYEGLIDEIYGIQNSYVKLPPEKFAPKKQGDGGKDLPTEAKKLQLNSAEELYAEIRDKNFNAVGSVLSKKAKIISAAFEERHNAKTVGEIKQFVSQLPHMQAARGSLANHTSIAELIKDVTTSEDFFDKLTVEQEFMSGIDTDKVNNYIEDCIAQKHSLIKVLRLVCLQSVCNSGLKQKVLDYYKREILQTYGYEHILTLHNLEKAGLLKPQTGGRNNYPTIRKTLRLWMDDVNEQNPTDISYVYSGYAPLSVRLAQLLSRPGWRSIEEVLRILPGPHFEERQPLPTGLQKKRQPGENRVTLIFFLGGVTFAEIAALRFLSQLEDGGTEYVIATTKLMNGTSWIEALMEKPF,,-1.0,MAAHLSYGRVNLNVLREAVRRELREFLDKCAGSKAIVWDEYLTGPFGLIAQYSLLKEHEVEKMFTLKGNRLPAADVKNIIFFVRPRLELMDIIAENVLSEDRRGPTRDFHILFVPRRSLLCEQRLKDLGVLGSFIHREEYSLDLIPFDGDLLSMESEGAFKECYLEGDQTSLYHAAKGLMTLQALYGTIPQIFGKGECARQVANMMIRMKREFTGSQNSIFPVFDNLLLLDRNVDLLTPLATQLTYEGLIDEIYGIQNSYVKLPPEKFAPKKQGDGGKDLPTEAKKLQLNSAEELYAEIRDKNFNAVGSVLSKKAKIISAAFEERHNAKTVGEIKQFVSQLPHMQAARGSLANHTSIAELIKDVTTSEDFFDKLTVEQEFMSGIDTDKVNNYIEDCIAQKHSLIKVLRLVCLQSVCNSGLKQKVLDYYKREILQTYGYEHKLTLHNLEKAGLLKPQTGGRNNYPTIRKTLRLWMDDVNEQNPTDISYVYSGYAPLSVRLAQLLSRPGWRSIEEVLRILPGPHFEERQPLPTGLQKKRQPGENRVTLIFFLGGVTFAEIAALRFLSQLEDGGTEYVIATTKLMNGTSWIEALMEKPF,Vacuolar protein sorting-associated protein 33A,"Plays a role in vesicle-mediated protein trafficking to lysosomal compartments including the endocytic membrane transport and autophagic pathways. Believed to act as a core component of the putative HOPS and CORVET endosomal tethering complexes which are proposed to be involved in the Rab5-to-Rab7 endosome conversion probably implicating MON1A/B, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion. The HOPS complex is proposed to be recruited to Rab7 on the late endosomal membrane and to regulate late endocytic, phagocytic and autophagic traffic towards lysosomes. The CORVET complex is proposed to function as a Rab5 effector to mediate early endosome fusion probably in specific endosome subpopulations. Required for fusion of endosomes and autophagosomes with lysosomes; the function is dependent on its association with VPS16 but not VIPAS39. The function in autophagosome-lysosome fusion implicates STX17 but not UVRAG.",Enables interaction with VPS16. Enables interaction with VPS18 and enhances endosome-lysosome fusion; when associated with D-429. Enables interaction with VPS18 and enhances endosome-lysosome fusion; when associated with D-438. The mutation in VPS16 now rescues lysosome fusion with endosomes or autophagosomes in cells depleted of the endogenous proteins.,Enables interaction with VPS16. Enables interaction with VPS18 and enhances endosome-lysosome fusion; when associated with D-429. Enables interaction with VPS18 and enhances endosome-lysosome fusion; when associated with D-438. The mutation in VPS16 now rescues lysosome fusion with endosomes or autophagosomes in cells depleted of the endogenous proteins.
288,0,0,P08692-K60R,MSNITIYHNPACGTSRNTLEMIRNSGTEPTIILYLENPPSRDELVKLIADMGISVRALLRKNVEPYEQLGLAEDKFTDDQLIDFMLQHPILINRPIVVTPLGTRLCRPSEVVLDILQDAQKGAFTKEDGEKVVDEAGKRLK,,-1.0,MSNITIYHNPACGTSRNTLEMIRNSGTEPTIILYLENPPSRDELVKLIADMGISVRALLKKNVEPYEQLGLAEDKFTDDQLIDFMLQHPILINRPIVVTPLGTRLCRPSEVVLDILQDAQKGAFTKEDGEKVVDEAGKRLK,Arsenate reductase,Involved in resistance to arsenate. Catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)]. The resulting arsenite is then extruded from the cell via the ArsAB transport system (Probable).,22-fold increase in catalytic efficiency with arsenate. Mutant shows high-level susceptibility to arsenate. The mutation confers arsenate susceptibility in vivo.,22-fold increase in catalytic efficiency with arsenate. Mutant shows high-level susceptibility to arsenate. The mutation confers arsenate susceptibility in vivo.
289,0,0,Q9JJS6-A469E,MEIIFGQNKKEQLEPVQAKVTGSIPAWLQGTLLRNGPGMHTVGESKYNHWFDGLALLHSFSIRDGEVFYRSKYLQSDTYIANIEANRIVVSEFGTMAYPDPCKNIFSKAFSYLSHTIPDFTDNCLINIMKCGEDFYATTETNYIRKIDPQTLETLEKVDYRKYVAVNLATSHPHYDEAGNVLNMGTSVVDKGRTKYVIFKIPATVPDSKKKGKSPVKHAEVFCSISSRSLLSPSYYHSFGVTENYVVFLEQPFKLDILKMATAYMRGVSWASCMSFDREDKTYIHIIDQRTRKPVPTKFYTDPMVVFHHVNAYEEDGCVLFDVIAYEDSSLYQLFYLANLNKDFEEKSRLTSVPTLRRFAVPLHVDKDAEVGSNLVKVSSTTATALKEKDGHVYCQPEVLYEGLELPRINYAYNGKPYRYIFAAEVQWSPVPTKILKYDILTKSSLKWSEESCWPAEPLFVPTPGAKDEDDGVILSAIVSTDPQKLPFLLILDAKSFTELARASVDADMHLDLHGLFIPDADWNAVKQTPAETQEVENSDHPTDPTAPELSHSENDFTAGHGGSSL,,-1.0,MEIIFGQNKKEQLEPVQAKVTGSIPAWLQGTLLRNGPGMHTVGESKYNHWFDGLALLHSFSIRDGEVFYRSKYLQSDTYIANIEANRIVVSEFGTMAYPDPCKNIFSKAFSYLSHTIPDFTDNCLINIMKCGEDFYATTETNYIRKIDPQTLETLEKVDYRKYVAVNLATSHPHYDEAGNVLNMGTSVVDKGRTKYVIFKIPATVPDSKKKGKSPVKHAEVFCSISSRSLLSPSYYHSFGVTENYVVFLEQPFKLDILKMATAYMRGVSWASCMSFDREDKTYIHIIDQRTRKPVPTKFYTDPMVVFHHVNAYEEDGCVLFDVIAYEDSSLYQLFYLANLNKDFEEKSRLTSVPTLRRFAVPLHVDKDAEVGSNLVKVSSTTATALKEKDGHVYCQPEVLYEGLELPRINYAYNGKPYRYIFAAEVQWSPVPTKILKYDILTKSSLKWSEESCWPAEPLFVPTPGAKDADDGVILSAIVSTDPQKLPFLLILDAKSFTELARASVDADMHLDLHGLFIPDADWNAVKQTPAETQEVENSDHPTDPTAPELSHSENDFTAGHGGSSL,"Beta,beta-carotene 15,15'-dioxygenase",Symmetrically cleaves beta-carotene into two molecules of retinal using a dioxygenase mechanism.,"Increased beta-carotene 15,15'-monooxygenase activity.","Increased beta-carotene 15,15'-monooxygenase activity."
290,0,0,Q9ULZ3-W41R,MGRARDAILDALENLTAEELKKFKLKLLSVPLREGYGRIPRGALLSMDALDLTDKLVSFYLETYGAELTANVLRDMGLQEMAGQLQAATHQGSGAAPAGIQAPPQSAAKPGLHFIDQHRAALIARVTNVEWLLDALYGKVLTDEQYQAVRAEPTNPSKMRKLFSFTPAWNWTCKDLLLQALRESQSYLVEDLERS,,-1.0,MGRARDAILDALENLTAEELKKFKLKLLSVPLREGYGRIPWGALLSMDALDLTDKLVSFYLETYGAELTANVLRDMGLQEMAGQLQAATHQGSGAAPAGIQAPPQSAAKPGLHFIDQHRAALIARVTNVEWLLDALYGKVLTDEQYQAVRAEPTNPSKMRKLFSFTPAWNWTCKDLLLQALRESQSYLVEDLERS,Apoptosis-associated speck-like protein containing a CARD,"Functions as key mediator in apoptosis and inflammation. Promotes caspase-mediated apoptosis involving predominantly caspase-8 and also caspase-9 in a probable cell type-specific manner. Involved in activation of the mitochondrial apoptotic pathway, promotes caspase-8-dependent proteolytic maturation of BID independently of FADD in certain cell types and also mediates mitochondrial translocation of BAX and activates BAX-dependent apoptosis coupled to activation of caspase-9, -2 and -3. Involved in innate immune response by acting as an integral adapter in the assembly of various inflammasomes (NLRP1, NLRP2, NLRP3, NLRP6, AIM2 and probably IFI16) which recruit and activate caspase-1 leading to processing and secretion of pro-inflammatory cytokines. Caspase-1-dependent inflammation leads to macrophage pyroptosis, a form of cell death. The function as activating adapter in different types of inflammasomes is mediated by the pyrin and CARD domains and their homotypic interactions. Clustered PYCARD nucleates the formation of caspase-1 filaments through the interaction of their respective CARD domains, acting as a platform for of caspase-1 polymerization. In the NLRP1 and NLRC4 inflammasomes seems not be required but facilitates the processing of procaspase-1. In cooperation with NOD2 involved in an inflammasome activated by bacterial muramyl dipeptide leading to caspase-1 activation. May be involved in RIGI-triggered pro-inflammatory responses and inflammasome activation. In collaboration with AIM2 which detects cytosolic double-stranded DNA may also be involved in a caspase-1-independent cell death that involves caspase-8. In adaptive immunity may be involved in maturation of dendritic cells to stimulate T-cell immunity and in cytoskeletal rearrangements coupled to chemotaxis and antigen uptake may be involved in post-transcriptional regulation of the guanine nucleotide exchange factor DOCK2; the latter function is proposed to involve the nuclear form. Also involved in transcriptional activation of cytokines and chemokines independent of the inflammasome; this function may involve AP-1, NF-kappa-B, MAPK and caspase-8 signaling pathways. For regulation of NF-kappa-B activating and inhibiting functions have been reported. Modulates NF-kappa-B induction at the level of the IKK complex by inhibiting kinase activity of CHUK and IKBK. Proposed to compete with RIPK2 for association with CASP1 thereby down-regulating CASP1-mediated RIPK2-dependent NF-kappa-B activation and activating interleukin-1 beta processing. Modulates host resistance to DNA virus infection, probably by inducing the cleavage of and inactivating CGAS in presence of cytoplasmic double-stranded DNA.May have a regulating effect on the function as inflammasome adapter.Seems to inhibit inflammasome-mediated maturation of interleukin-1 beta.",Enables homooligomerization. Mutation of R41 to W in ASC protein leads to promotion of filament formation.,Enables homooligomerization. Mutation of R41 to W in ASC protein leads to promotion of filament formation.
291,0,0,Q96RL7-A842E,MVFESVVVDVLNRFLGDYVVDLDTSQLSLGIWKGAVALKNLQIKENALSQLDVPFKVKVGHIGNLKLIIPWKNLYTQPVEAVLEEIYLLIVPSSRIKYDPLKEEKQLMEAKQQELKRIEEAKQKVVDQEQHLPEKQDTFAEKLVTQIIKNLQVKISSIHIRYEDDITNRDKPLSFGISLQNLSMQTTDQYWVPCLHDETEKLVRKLIRLDNLFAYWNVKSQMFYLSDYDNSLDDLKNGIVNENIVPEGYDFVFRPISANAKLVMNRRSDFDFSAPKINLEIELHNIAIEFNKPQYFSIMELLESVDMMAQNLPYRKFKPDVPLHHHAREWWAYAIHGVLEVNVCPRLWMWSWKHIRKHRQKVKQYKELYKKKLTSKKPPGELLVSLEELEKTLDVFNITIARQTAEVEVKKAGYKIYKEGVKDPEDNKGWFSWLWSWSEQNTNEQQPDVQPETLEEMLTPEEKALLYEAIGYSETAVDPTLLKTFEALKFFVHLKSMSIVLRENHQKPELVDIVIEEFSTLIVQRPGAQAIKFETKIDSFHITGLPDNSEKPRLLSSLDDAMSLFQITFEINPLDETVSQRCIIEAEPLEIIYDARTVNSIVEFFRPPKEVHLAQLTAATLTKLEEFRSKTATGLLYIIETQKVLDLKINLKASYIIVPQDGIFSPTSNLLLLDLGHLKVTSKSRSELPDVKQGEANLKEIMDRAYDSFDIQLTSVQLLYSRVGDNWREARKLSVSTQHILVPMHFNLELSKAMVFMDVRMPKFKIYGKLPLISLRISDKKLQGIMELIESIPKPEPVTEVSAPVKSFQIQTSTSLGTSQISQKIIPLLELPSVSEDDSEEEFFDAPCSPLEEPLQFPTGVKSIRTRKLQKQDCSVNMTTFKIRFEVPKVLIEFYHLVGDCELSVVEILVLGLGAEIEIRTYDLKANAFLKEFCLKCPEYLDENKKPVYLVTTLDNTMEDLLTLEYVKAEKNVPDLKSTYNNVLQLIKVNFSSLDIHLHTEALLNTINYLHNILPQSEEKSAPV,,-1.0,MVFESVVVDVLNRFLGDYVVDLDTSQLSLGIWKGAVALKNLQIKENALSQLDVPFKVKVGHIGNLKLIIPWKNLYTQPVEAVLEEIYLLIVPSSRIKYDPLKEEKQLMEAKQQELKRIEEAKQKVVDQEQHLPEKQDTFAEKLVTQIIKNLQVKISSIHIRYEDDITNRDKPLSFGISLQNLSMQTTDQYWVPCLHDETEKLVRKLIRLDNLFAYWNVKSQMFYLSDYDNSLDDLKNGIVNENIVPEGYDFVFRPISANAKLVMNRRSDFDFSAPKINLEIELHNIAIEFNKPQYFSIMELLESVDMMAQNLPYRKFKPDVPLHHHAREWWAYAIHGVLEVNVCPRLWMWSWKHIRKHRQKVKQYKELYKKKLTSKKPPGELLVSLEELEKTLDVFNITIARQTAEVEVKKAGYKIYKEGVKDPEDNKGWFSWLWSWSEQNTNEQQPDVQPETLEEMLTPEEKALLYEAIGYSETAVDPTLLKTFEALKFFVHLKSMSIVLRENHQKPELVDIVIEEFSTLIVQRPGAQAIKFETKIDSFHITGLPDNSEKPRLLSSLDDAMSLFQITFEINPLDETVSQRCIIEAEPLEIIYDARTVNSIVEFFRPPKEVHLAQLTAATLTKLEEFRSKTATGLLYIIETQKVLDLKINLKASYIIVPQDGIFSPTSNLLLLDLGHLKVTSKSRSELPDVKQGEANLKEIMDRAYDSFDIQLTSVQLLYSRVGDNWREARKLSVSTQHILVPMHFNLELSKAMVFMDVRMPKFKIYGKLPLISLRISDKKLQGIMELIESIPKPEPVTEVSAPVKSFQIQTSTSLGTSQISQKIIPLLELPSVSEDDSEEAFFDAPCSPLEEPLQFPTGVKSIRTRKLQKQDCSVNMTTFKIRFEVPKVLIEFYHLVGDCELSVVEILVLGLGAEIEIRTYDLKANAFLKEFCLKCPEYLDENKKPVYLVTTLDNTMEDLLTLEYVKAEKNVPDLKSTYNNVLQLIKVNFSSLDIHLHTEALLNTINYLHNILPQSEEKSAPV,Intermembrane lipid transfer protein VPS13A,Mediates the transfer of lipids between membranes at organelle contact sites. Binds phospholipids. Required for the formation or stabilization of ER-mitochondria contact sites which enable transfer of lipids between the ER and mitochondria. Negatively regulates lipid droplet size and motility. Required for efficient lysosomal protein degradation.,Enhanced interaction with VAPA. The consequences of enhanced function of VPS13A at the subcellular level are unknown.,Enhanced interaction with VAPA. The consequences of enhanced function of VPS13A at the subcellular level are unknown.
292,0,0,O54908-E267H,MMVVCAAAAVRFLAVFTMMALCSLPLLGASATLNSVLINSNAIKNLPPPLGGAGGQPGSAVSVAPGVLYEGGNKYQTLDNYQPYPCAEDEECGSDEYCSSPSRGAAGVGGVQICLACRKRRKRCMRHAMCCPGNYCKNGICMPSDHSHFPRGEIEESIIENLGNDHNAAAGDGYPRRTTLTSKIYHTKGQEGSVCLRSSDCAAGLCCARHFWSKICKPVLKEGQVCTKHKRKGSHGLEIFQRCYCGEGLACRIQKDHHQASNSSRLHTCQRH,,-1.0,MMVVCAAAAVRFLAVFTMMALCSLPLLGASATLNSVLINSNAIKNLPPPLGGAGGQPGSAVSVAPGVLYEGGNKYQTLDNYQPYPCAEDEECGSDEYCSSPSRGAAGVGGVQICLACRKRRKRCMRHAMCCPGNYCKNGICMPSDHSHFPRGEIEESIIENLGNDHNAAAGDGYPRRTTLTSKIYHTKGQEGSVCLRSSDCAAGLCCARHFWSKICKPVLKEGQVCTKHKRKGSHGLEIFQRCYCGEGLACRIQKDHHQASNSSRLETCQRH,Dickkopf-related protein 1,"Antagonizes canonical Wnt signaling by inhibiting LRP5/6 interaction with Wnt and by forming a ternary complex with the transmembrane protein KREMEN that promotes internalization of LRP5/6. Inhibits the pro-apoptotic function of KREMEN1 in a Wnt-independent manner, and has anti-apoptotic activity. Plays a role in limb development; attenuates Wnt signaling in the developing limb to allow normal limb patterning.",43% increased binding to LRP6.,43% increased binding to LRP6.
293,0,0,B9EJA2-A602P,MATDSASCEPDLSRTPGDTEGATAEAAKKEFDVDTLSKSELRMLLSVMEGELEARDLVIEALRARRKEVFIQERYGRFNLNDPFLALQRDYEAGPGDKEKPVCTNPLSILEAVMAHCRKMQERMSAQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKNKHVVLMLVKECKQLSGKVVEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEIDKMKKMMEQMKKGSDGKPGLSLPRKTKDKRLASISVATEGPVTRSVACQTDVVTESTDPVKKLPLTVPIKPSTGSPLVPTNTKGNVGPSALLIRPGIDRQSSHSDLGPSPPTALPSSANRIEENGPSTGNAPDLSNSTPSTPSSTAPAAAQTPGTAPQNHSQAPTVHSLHSPCANTHPGLNPRIQAARFRFQGNANDPDQNGNNTQSPPSRDVSPTSRDNLVAKQLARNTVTQALSRFTSPQAGASSRLGVSPGGDAGTCPPVGRTGLKTPGAARVDRGNPPPIPPKKPGLSQTPSPPHPQLRASNAGAKVDNKIVASPPSTLPQGTKVVNEENVPKSSSPQLPPKPSIDLTVAPAGCPVSALATSQVGAWPAGTPGLNQPACSDSSLVIPATVAFCSSINPVSASSRSPGASDSLLVAASGWSPSLTPLLMSGGPAPLAGRPTLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFECIELLTAYNANINHSAAGGQTPLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVDSLKLLMYHRVRAHGNSLSSEEPKSGLFSLNGGESPTGPSKPVVPADLINHADKEGWTAAHIAASKGFKNCLEVLCRHGGLEPERRDKCNRTVHDVATDDCKHLLENLNALKIPLRISVGEIQPSNDVSDDFECEHTICTLNIRKQTSWEDFSKAVSQALTNHFQAISSDGWWSLEDG,,-1.0,MATDSASCEPDLSRTPGDTEGATAEAAKKEFDVDTLSKSELRMLLSVMEGELEARDLVIEALRARRKEVFIQERYGRFNLNDPFLALQRDYEAGPGDKEKPVCTNPLSILEAVMAHCRKMQERMSAQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKNKHVVLMLVKECKQLSGKVVEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEIDKMKKMMEQMKKGSDGKPGLSLPRKTKDKRLASISVATEGPVTRSVACQTDVVTESTDPVKKLPLTVPIKPSTGSPLVPTNTKGNVGPSALLIRPGIDRQSSHSDLGPSPPTALPSSANRIEENGPSTGNAPDLSNSTPSTPSSTAPAAAQTPGTAPQNHSQAPTVHSLHSPCANTHPGLNPRIQAARFRFQGNANDPDQNGNNTQSPPSRDVSPTSRDNLVAKQLARNTVTQALSRFTSPQAGASSRLGVSPGGDAGTCPPVGRTGLKTPGAARVDRGNPPPIPPKKPGLSQTPSPPHPQLRASNAGAKVDNKIVASPPSTLPQGTKVVNEENVPKSSSPQLAPKPSIDLTVAPAGCPVSALATSQVGAWPAGTPGLNQPACSDSSLVIPATVAFCSSINPVSASSRSPGASDSLLVAASGWSPSLTPLLMSGGPAPLAGRPTLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFECIELLTAYNANINHSAAGGQTPLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVDSLKLLMYHRVRAHGNSLSSEEPKSGLFSLNGGESPTGPSKPVVPADLINHADKEGWTAAHIAASKGFKNCLEVLCRHGGLEPERRDKCNRTVHDVATDDCKHLLENLNALKIPLRISVGEIQPSNDVSDDFECEHTICTLNIRKQTSWEDFSKAVSQALTNHFQAISSDGWWSLEDG,Cortactin-binding protein 2,"Regulates the dendritic spine distribution of CTTN/cortactin in hippocampal neurons, and thus controls dendritic spinogenesis and dendritic spine maintenance.",Enhanced CTTN-binding; when associated with A-599.,Enhanced CTTN-binding; when associated with A-599.
294,0,0,P32266-A244T,MNASPVRLLILRRQLATHPAILYSSPYIKSPLVHLHSRMSNVHRSAHANALSFVITRRSISHFPKIISKIIRLPIYVGGGMAAAGSYIAYKMEEASSFTKDKLDRIKDLGESMKEKFNKMFSGDKSQDGGHGNDGTVPTATLIAATSLDDDESKRQGDPKDDDDEDDDDEDDENDSVDTTQDEMLNLTKQMIEIRTILNKVDSSSAHLTLPSIVVIGSQSSGKSSVLESIVGREFLPKGSNMVTRRPIELTLVNTPNSNNVTADFPSMRLYNIKDFKEVKRMLMELNMAVPTSEAVSEEPIQLTIKSSRVPDLSLVDLPGYIQVEAADQPIELKTKIRDLCEKYLTAPNIILAISAADVDLANSSALKASKAADPKGLRTIGVITKLDLVDPEKARSILNNKKYPLSMGYVGVITKTPSSINRKHLGLFGEAPSSSLSGIFSKGQHGQSSGEENTNGLKQIVSHQFEKAYFKENKKYFTNCQVSTKKLREKLIKILEISMSNALEPTSTLIQQELDDTSYLFKVEFNDRHLTPKSYLLNNIDVLKLGIKEFQEKFHRNELKSILRAELDQKVLDVLATRYWKDDNLQDLSSSKLESDTDMLYWHKKLELASSGLTKMGIGRLSTMLTTNAILKELDNILESTQLKNHELIKDLVSNTAINVLNSKYYSTADQVENCIKPFKYEIDLEERDWSLARQHSINLIKEELRQCNSRYQAIKNAVGSKKLANVMGYLENESNLQKETLGMSKLLLERGSEAIFLDKRCKVLSFRLKMLKNKCHSTIEKDRCPEVFLSAVSDKLTSTAVLFLNVELLSDFFYNFPIELDRRLTLLGDEQVEMFAKEDPKISRHIELQKRKELLELALEKIDSILVFKKSYKGVSKNL,,-1.0,MNASPVRLLILRRQLATHPAILYSSPYIKSPLVHLHSRMSNVHRSAHANALSFVITRRSISHFPKIISKIIRLPIYVGGGMAAAGSYIAYKMEEASSFTKDKLDRIKDLGESMKEKFNKMFSGDKSQDGGHGNDGTVPTATLIAATSLDDDESKRQGDPKDDDDEDDDDEDDENDSVDTTQDEMLNLTKQMIEIRTILNKVDSSSAHLTLPSIVVIGSQSSGKSSVLESIVGREFLPKGSNMVARRPIELTLVNTPNSNNVTADFPSMRLYNIKDFKEVKRMLMELNMAVPTSEAVSEEPIQLTIKSSRVPDLSLVDLPGYIQVEAADQPIELKTKIRDLCEKYLTAPNIILAISAADVDLANSSALKASKAADPKGLRTIGVITKLDLVDPEKARSILNNKKYPLSMGYVGVITKTPSSINRKHLGLFGEAPSSSLSGIFSKGQHGQSSGEENTNGLKQIVSHQFEKAYFKENKKYFTNCQVSTKKLREKLIKILEISMSNALEPTSTLIQQELDDTSYLFKVEFNDRHLTPKSYLLNNIDVLKLGIKEFQEKFHRNELKSILRAELDQKVLDVLATRYWKDDNLQDLSSSKLESDTDMLYWHKKLELASSGLTKMGIGRLSTMLTTNAILKELDNILESTQLKNHELIKDLVSNTAINVLNSKYYSTADQVENCIKPFKYEIDLEERDWSLARQHSINLIKEELRQCNSRYQAIKNAVGSKKLANVMGYLENESNLQKETLGMSKLLLERGSEAIFLDKRCKVLSFRLKMLKNKCHSTIEKDRCPEVFLSAVSDKLTSTAVLFLNVELLSDFFYNFPIELDRRLTLLGDEQVEMFAKEDPKISRHIELQKRKELLELALEKIDSILVFKKSYKGVSKNL,"Dynamin-like GTPase MGM1, mitochondrial",Dynamin-related GTPase required for mitochondrial fusion. Coordinates interaction between the inner and outer mitochondrial membrane to promote the formation of the double membrane.,Gain of GTPase activity.,Gain of GTPase activity.
295,0,0,Q6UWV6-Q100N,MRGPAVLLTVALATLLAPGAGAPVQSQGSQNKLLLVSFDGFRWNYDQDVDTPNLDAMARDGVKARYMTPAFVTMTSPCHFTLVTGKYIENHGVVHNMYYNTTSKVKLPYHATLGIQRWWDNGSVPIWITAQRQGLRAGSFFYPGGNVTYQGVAVTRSRKEGIAHNYKNETEWRANIDTVMAWFTEEDLDLVTLYFGEPDSTGHRYGPESPERREMVRQVDRTVGYLRESIARNHLTDRLNLIITSDHGMTTVDKRAGDLVEFHKFPNFTFRDIEFELLDYGPNGMLLPKEGRLEKVYDALKDAHPKLHVYKKEAFPEAFHYANNPRVTPLLMYSDLGYVIHGRINVQFNNGEHGFDNKDMDMKTIFRAVGPSFRAGLEVEPFESVHVYELMCRLLGIVPEANDGHLATLLPMLHTESALPPDGRPTLLPKGRSALPPSSRPLLVMGLLGTVILLSEVA,,-1.0,MRGPAVLLTVALATLLAPGAGAPVQSQGSQNKLLLVSFDGFRWNYDQDVDTPNLDAMARDGVKARYMTPAFVTMTSPCHFTLVTGKYIENHGVVHNMYYQTTSKVKLPYHATLGIQRWWDNGSVPIWITAQRQGLRAGSFFYPGGNVTYQGVAVTRSRKEGIAHNYKNETEWRANIDTVMAWFTEEDLDLVTLYFGEPDSTGHRYGPESPERREMVRQVDRTVGYLRESIARNHLTDRLNLIITSDHGMTTVDKRAGDLVEFHKFPNFTFRDIEFELLDYGPNGMLLPKEGRLEKVYDALKDAHPKLHVYKKEAFPEAFHYANNPRVTPLLMYSDLGYVIHGRINVQFNNGEHGFDNKDMDMKTIFRAVGPSFRAGLEVEPFESVHVYELMCRLLGIVPEANDGHLATLLPMLHTESALPPDGRPTLLPKGRSALPPSSRPLLVMGLLGTVILLSEVA,Ectonucleotide pyrophosphatase/phosphodiesterase family member 7,"Choline-specific phosphodiesterase that hydrolyzes sphingomyelin releasing the ceramide and phosphocholine and therefore is involved in sphingomyelin digestion, ceramide formation, and fatty acid (FA) absorption in the gastrointestinal tract. Has also phospholipase C activity and can also cleave phosphocholine from palmitoyl lyso-phosphatidylcholine and platelet-activating factor (PAF) leading to its inactivation. Does not have nucleotide pyrophosphatase activity. May promote cholesterol absorption by affecting the levels of sphingomyelin derived from either diet or endogenous sources, in the intestinal lumen.",Strongly enhances N-glycosylation and enzyme activity; when associated with Q-121; Q-146; Q-168 and Q-267. The mutation in alk-SMase greatly improves its activity.,Strongly enhances N-glycosylation and enzyme activity; when associated with Q-121; Q-146; Q-168 and Q-267. The mutation in alk-SMase greatly improves its activity.
296,0,0,P21926-A79C,MPVKGGTKCIKYLLFGFNFIFWLAGIAVLAIGLWLRFDSQTKSIFEQETNNNNSSFYTGVYILIGAGALMMLVGFLGCCGAVQESQCMLGLFFGFLLVIFAIEIAAAIWGYSHKDEVIKEVQEFYKDTYNKLKTKDEPQRETLKAIHYALNCCGLAGGVEQFISDICPKKDVLETFTVKSCPDAIKEVFDNKFHIIGAVGIGIAVVMIFGMIFSMILCCAIRRNREMV,,-1.0,MPVKGGTKCIKYLLFGFNFIFWLAGIAVLAIGLWLRFDSQTKSIFEQETNNNNSSFYTGVYILIGAGALMMLVGFLGCAGAVQESQCMLGLFFGFLLVIFAIEIAAAIWGYSHKDEVIKEVQEFYKDTYNKLKTKDEPQRETLKAIHYALNCCGLAGGVEQFISDICPKKDVLETFTVKSCPDAIKEVFDNKFHIIGAVGIGIAVVMIFGMIFSMILCCAIRRNREMV,CD9 antigen,"Integral membrane protein associated with integrins, which regulates different processes, such as sperm-egg fusion, platelet activation and aggregation, and cell adhesion. Present at the cell surface of oocytes and plays a key role in sperm-egg fusion, possibly by organizing multiprotein complexes and the morphology of the membrane required for the fusion. In myoblasts, associates with CD81 and PTGFRN and inhibits myotube fusion during muscle regeneration. In macrophages, associates with CD81 and beta-1 and beta-2 integrins, and prevents macrophage fusion into multinucleated giant cells specialized in ingesting complement-opsonized large particles. Also prevents the fusion between mononuclear cell progenitors into osteoclasts in charge of bone resorption. Acts as a receptor for PSG17. Involved in platelet activation and aggregation. Regulates paranodal junction formation. Involved in cell adhesion, cell motility and tumor metastasis.","Loss of depalmitoylation; when associated with A-9; A-78; A-87; A-218 and A-219. The depalmitoylation of CD9 did not influence the partition in detergent-resistant membranes but contributed to the interaction with CD81 and CD53. In particular, the sensitivity of the CD9/CD81 interaction to EDTA, which disrupts other tetraspanin/tetraspanin interactions, was entirely dependent on depalmitoylation.","Loss of depalmitoylation; when associated with A-9; A-78; A-87; A-218 and A-219. The depalmitoylation of CD9 did not influence the partition in detergent-resistant membranes but contributed to the interaction with CD81 and CD53. In particular, the sensitivity of the CD9/CD81 interaction to EDTA, which disrupts other tetraspanin/tetraspanin interactions, was entirely dependent on depalmitoylation."
297,0,0,P25522-N338D,MSDNDTIVAQATPPGRGGVGILRISGFKAREVAETVLGKLPKPRYADYLPFKDADGSVLDQGIALWFPGPNSFTGEDVLELQGHGGPVILDLLLKRILTIPGLRIARPGEFSERAFLNDKLDLAQAEAIADLIDASSEQAARSALNSLQGAFSARVNHLVEALTHLRIYVEAAIDFPDEEIDFLSDGKIEAQLNDVIADLDAVRAEARQGSLLREGMKVVIAGRPNAGKSSLLNALAGREAAIVTDIAGTTRDVLREHIHIDGMPLHIIDTAGLREASDEVERIGIERAWQEIEQADRVLFMVDGTTTDAVDPAEIWPEFIARLPAKLPITVVRNKADITGETLGMSEVNGHALIRLSARTGEGVDVLRNHLKQSMGFDTNMEGGFLARRRHLQALEQAAEHLQQGKAQLLGAWAGELLAEELRLAQQNLSEITGEFTSDDLLGRIFSSFCIGK,,-1.0,MSDNDTIVAQATPPGRGGVGILRISGFKAREVAETVLGKLPKPRYADYLPFKDADGSVLDQGIALWFPGPNSFTGEDVLELQGHGGPVILDLLLKRILTIPGLRIARPGEFSERAFLNDKLDLAQAEAIADLIDASSEQAARSALNSLQGAFSARVNHLVEALTHLRIYVEAAIDFPDEEIDFLSDGKIEAQLNDVIADLDAVRAEARQGSLLREGMKVVIAGRPNAGKSSLLNALAGREAAIVTDIAGTTRDVLREHIHIDGMPLHIIDTAGLREASDEVERIGIERAWQEIEQADRVLFMVDGTTTDAVDPAEIWPEFIARLPAKLPITVVRNKANITGETLGMSEVNGHALIRLSARTGEGVDVLRNHLKQSMGFDTNMEGGFLARRRHLQALEQAAEHLQQGKAQLLGAWAGELLAEELRLAQQNLSEITGEFTSDDLLGRIFSSFCIGK,tRNA modification GTPase MnmE,"Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.","Strong increase in GTP binding. Does not affect hydrolase activity, but has 10-fold lower affinity for XTP than for GTP. Partially enhances tRNA modifying function. The mutational analysis of the GTPase domain indicates that MnmE is closer to GTP-specific metabolic enzymes than to classical GTPases. Therefore, we propose that MnmE uses a conformational stability associated with GTP hydrolysis to promote the tRNA modification reaction, in which the C-terminal C may function as a catalytic residue.","Strong increase in GTP binding. Does not affect hydrolase activity, but has 10-fold lower affinity for XTP than for GTP. Partially enhances tRNA modifying function. The mutational analysis of the GTPase domain indicates that MnmE is closer to GTP-specific metabolic enzymes than to classical GTPases. Therefore, we propose that MnmE uses a conformational stability associated with GTP hydrolysis to promote the tRNA modification reaction, in which the C-terminal C may function as a catalytic residue."
298,0,0,P21926-A218C,MPVKGGTKCIKYLLFGFNFIFWLAGIAVLAIGLWLRFDSQTKSIFEQETNNNNSSFYTGVYILIGAGALMMLVGFLGCCGAVQESQCMLGLFFGFLLVIFAIEIAAAIWGYSHKDEVIKEVQEFYKDTYNKLKTKDEPQRETLKAIHYALNCCGLAGGVEQFISDICPKKDVLETFTVKSCPDAIKEVFDNKFHIIGAVGIGIAVVMIFGMIFSMILCCAIRRNREMV,,-1.0,MPVKGGTKCIKYLLFGFNFIFWLAGIAVLAIGLWLRFDSQTKSIFEQETNNNNSSFYTGVYILIGAGALMMLVGFLGCCGAVQESQCMLGLFFGFLLVIFAIEIAAAIWGYSHKDEVIKEVQEFYKDTYNKLKTKDEPQRETLKAIHYALNCCGLAGGVEQFISDICPKKDVLETFTVKSCPDAIKEVFDNKFHIIGAVGIGIAVVMIFGMIFSMILACAIRRNREMV,CD9 antigen,"Integral membrane protein associated with integrins, which regulates different processes, such as sperm-egg fusion, platelet activation and aggregation, and cell adhesion. Present at the cell surface of oocytes and plays a key role in sperm-egg fusion, possibly by organizing multiprotein complexes and the morphology of the membrane required for the fusion. In myoblasts, associates with CD81 and PTGFRN and inhibits myotube fusion during muscle regeneration. In macrophages, associates with CD81 and beta-1 and beta-2 integrins, and prevents macrophage fusion into multinucleated giant cells specialized in ingesting complement-opsonized large particles. Also prevents the fusion between mononuclear cell progenitors into osteoclasts in charge of bone resorption. Acts as a receptor for PSG17. Involved in platelet activation and aggregation. Regulates paranodal junction formation. Involved in cell adhesion, cell motility and tumor metastasis.",Gain of palmitoylation; when associated with A-9; A-78; A-79; A-87 and A-219.,Gain of palmitoylation; when associated with A-9; A-78; A-79; A-87 and A-219.
299,0,0,Q96AX1-D429K,MAAHLSYGRVNLNVLREAVRRELREFLDKCAGSKAIVWDEYLTGPFGLIAQYSLLKEHEVEKMFTLKGNRLPAADVKNIIFFVRPRLELMDIIAENVLSEDRRGPTRDFHILFVPRRSLLCEQRLKDLGVLGSFIHREEYSLDLIPFDGDLLSMESEGAFKECYLEGDQTSLYHAAKGLMTLQALYGTIPQIFGKGECARQVANMMIRMKREFTGSQNSIFPVFDNLLLLDRNVDLLTPLATQLTYEGLIDEIYGIQNSYVKLPPEKFAPKKQGDGGKDLPTEAKKLQLNSAEELYAEIRDKNFNAVGSVLSKKAKIISAAFEERHNAKTVGEIKQFVSQLPHMQAARGSLANHTSIAELIKDVTTSEDFFDKLTVEQEFMSGIDTDKVNNYIEDCIAQKHSLIKVLRLVCLQSVCNSGLKQKVLDYYKREILQTYGYEHILTLHNLEKAGLLKPQTGGRNNYPTIRKTLRLWMDDVNEQNPTDISYVYSGYAPLSVRLAQLLSRPGWRSIEEVLRILPGPHFEERQPLPTGLQKKRQPGENRVTLIFFLGGVTFAEIAALRFLSQLEDGGTEYVIATTKLMNGTSWIEALMEKPF,,-1.0,MAAHLSYGRVNLNVLREAVRRELREFLDKCAGSKAIVWDEYLTGPFGLIAQYSLLKEHEVEKMFTLKGNRLPAADVKNIIFFVRPRLELMDIIAENVLSEDRRGPTRDFHILFVPRRSLLCEQRLKDLGVLGSFIHREEYSLDLIPFDGDLLSMESEGAFKECYLEGDQTSLYHAAKGLMTLQALYGTIPQIFGKGECARQVANMMIRMKREFTGSQNSIFPVFDNLLLLDRNVDLLTPLATQLTYEGLIDEIYGIQNSYVKLPPEKFAPKKQGDGGKDLPTEAKKLQLNSAEELYAEIRDKNFNAVGSVLSKKAKIISAAFEERHNAKTVGEIKQFVSQLPHMQAARGSLANHTSIAELIKDVTTSEDFFDKLTVEQEFMSGIDTDKVNNYIEDCIAQKHSLIKVLRLVCLQSVCNSGLKQKVLDYYDREILQTYGYEHILTLHNLEKAGLLKPQTGGRNNYPTIRKTLRLWMDDVNEQNPTDISYVYSGYAPLSVRLAQLLSRPGWRSIEEVLRILPGPHFEERQPLPTGLQKKRQPGENRVTLIFFLGGVTFAEIAALRFLSQLEDGGTEYVIATTKLMNGTSWIEALMEKPF,Vacuolar protein sorting-associated protein 33A,"Plays a role in vesicle-mediated protein trafficking to lysosomal compartments including the endocytic membrane transport and autophagic pathways. Believed to act as a core component of the putative HOPS and CORVET endosomal tethering complexes which are proposed to be involved in the Rab5-to-Rab7 endosome conversion probably implicating MON1A/B, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion. The HOPS complex is proposed to be recruited to Rab7 on the late endosomal membrane and to regulate late endocytic, phagocytic and autophagic traffic towards lysosomes. The CORVET complex is proposed to function as a Rab5 effector to mediate early endosome fusion probably in specific endosome subpopulations. Required for fusion of endosomes and autophagosomes with lysosomes; the function is dependent on its association with VPS16 but not VIPAS39. The function in autophagosome-lysosome fusion implicates STX17 but not UVRAG.",Enhances interaction with VPS16. Enhances interaction with VPS18 and promotes endosome-lysosome fusion; when associated with K-438. Enhances interaction with VPS18 and promotes endosome-lysosome fusion; when associated with K-441.,Enhances interaction with VPS16. Enhances interaction with VPS18 and promotes endosome-lysosome fusion; when associated with K-438. Enhances interaction with VPS18 and promotes endosome-lysosome fusion; when associated with K-441.
300,0,0,D5ARH0-N41K,MQAIDIGHVTLERDGTGVFSDLTLRLTERRIGIVGRNGAGKSSLIRLITGLVTPQKGRVVVNGVDVAADRAGALGTVGLLFQNPDHQIIFPVVRDEIAFGLEQKGLKRAAALARAEAVLAAQGRADWGDRLCHTLSQGQRQLLCLMSILAMEPDWILFDEPFNALDLPTALSIEARIAGLAQNVVLVTHDPSRLTGFDRILWLEGGRIEADGPPAEVLPRYIAAMQALARAGAC,,-1.0,MQAIDIGHVTLERDGTGVFSDLTLRLTERRIGIVGRNGAGNSSLIRLITGLVTPQKGRVVVNGVDVAADRAGALGTVGLLFQNPDHQIIFPVVRDEIAFGLEQKGLKRAAALARAEAVLAAQGRADWGDRLCHTLSQGQRQLLCLMSILAMEPDWILFDEPFNALDLPTALSIEARIAGLAQNVVLVTHDPSRLTGFDRILWLEGGRIEADGPPAEVLPRYIAAMQALARAGAC,Biotin transport ATP-binding protein BioM,Required for biotin uptake under very low (pM) biotin concentrations but not under higher (nM) concentrations.,"Enhanced biotin uptake, gain of ATPase activity, BioMNY complexes still form. The mutation in the BioM protein greatly improves the BioMNY-mediated biotin uptake, demonstrating the independence of high-affinity transport on a functional ATPase.","Enhanced biotin uptake, gain of ATPase activity, BioMNY complexes still form. The mutation in the BioM protein greatly improves the BioMNY-mediated biotin uptake, demonstrating the independence of high-affinity transport on a functional ATPase."
301,0,0,Q6MZP7-R536Y,MEVVPAEVNSLLPEEIMDTGITLVDDDSIEAVIVSSPIPMETELEEIVNINSTGDSTATPISTEPITVYSNHTNQVAVNTTITKADSNTTVKPAFPSGLQKLGAQTPVTISANQIILNKVSQTSDLKLGNQTLKPDGQKLILTTLGKSGSPIVLALPHSQLPQAQKVTTQAQSGDAKLPPQQIKVVTIGGRPEVKPVIGVSALTPGSQLINTTTQPSVLQTQQLKTVQIAKKPRTPTSGPVITKLIFAKPINSKAVTGQTTQVSPPVIAGRVLSQSTPGTPSKTITISESGVIGSTLNSTTQTPNKIAISPLKSPNKAVKSTVQTITVGGVSTSQFKTIIPLATAPNVQQIQVPGSKFHYVRLVTATSASSSTQPVSQNPSTNTQPLQQAKPVVVNTTPVRMSVPIVSAQAVKQVVPKPINPTSQIVTTSQPQQRLIMPATPLPQIQPNLTNLPPGTVLAPAPGTGNVGYAVLPAQYVTQLQQSSYVSIASNSTFTGTSGIQTQARLPFNGIIPSESASRPRKPCNCTKSLCLKLYCDCFANGEFCNNCNCTNCYNNLEHENERQKAIKACLDRNPEAFKPKIGKGKEGESDRRHSKGCNCKRSGCLKNYCECYEAKIMCSSICKCIGCKNFEESPERKTLMHLADAAEVRVQQQTAAKTKLSSQISDLLTRPTPALNSGGGKLPFTFVTKEVAEATCNCLLAQAEQADKKGKSKAAAERMILEEFGRCLMSVINSAGKAKSDPCAMNC,,-1.0,MEVVPAEVNSLLPEEIMDTGITLVDDDSIEAVIVSSPIPMETELEEIVNINSTGDSTATPISTEPITVYSNHTNQVAVNTTITKADSNTTVKPAFPSGLQKLGAQTPVTISANQIILNKVSQTSDLKLGNQTLKPDGQKLILTTLGKSGSPIVLALPHSQLPQAQKVTTQAQSGDAKLPPQQIKVVTIGGRPEVKPVIGVSALTPGSQLINTTTQPSVLQTQQLKTVQIAKKPRTPTSGPVITKLIFAKPINSKAVTGQTTQVSPPVIAGRVLSQSTPGTPSKTITISESGVIGSTLNSTTQTPNKIAISPLKSPNKAVKSTVQTITVGGVSTSQFKTIIPLATAPNVQQIQVPGSKFHYVRLVTATSASSSTQPVSQNPSTNTQPLQQAKPVVVNTTPVRMSVPIVSAQAVKQVVPKPINPTSQIVTTSQPQQRLIMPATPLPQIQPNLTNLPPGTVLAPAPGTGNVGYAVLPAQYVTQLQQSSYVSIASNSTFTGTSGIQTQARLPFNGIIPSESASRPRKPCNCTKSLCLKLRCDCFANGEFCNNCNCTNCYNNLEHENERQKAIKACLDRNPEAFKPKIGKGKEGESDRRHSKGCNCKRSGCLKNYCECYEAKIMCSSICKCIGCKNFEESPERKTLMHLADAAEVRVQQQTAAKTKLSSQISDLLTRPTPALNSGGGKLPFTFVTKEVAEATCNCLLAQAEQADKKGKSKAAAERMILEEFGRCLMSVINSAGKAKSDPCAMNC,Protein lin-54 homolog,"Component of the DREAM complex, a multiprotein complex that can both act as a transcription activator or repressor depending on the context. In G0 phase, the complex binds to more than 800 promoters and is required for repression of E2F target genes. In S phase, the complex selectively binds to the promoters of G2/M genes whose products are required for mitosis and participates in their cell cycle dependent activation. In the complex, acts as a DNA-binding protein that binds the promoter of CDK1 in a sequence-specific manner. Specifically recognizes the consensus motif 5'-TTYRAA-3' in target DNA.",Gain of DNA-binding. This mutation enhances the DNA-binding properties of LIN54 and may improve its ability to recognize the CHR sequence. It is unclear how this mutation specifically hinders MuvB recruitment to target promoters or the positioning of downstream nucleosomes.,Gain of DNA-binding. This mutation enhances the DNA-binding properties of LIN54 and may improve its ability to recognize the CHR sequence. It is unclear how this mutation specifically hinders MuvB recruitment to target promoters or the positioning of downstream nucleosomes.
302,0,0,H2KZZ6-P490S,MEDFKDFTEVTQFTNVQYLGCSQLVNNDNDNEMKALMKVLDEQKGAQTINVTLVVPHNISGTVKLIDAQGKVLSSFSLVNIRFCIRGESSTSQNNCFGISFTHKISVGEHNSSDILHQCHVFRTSKAETAAKALYSFSYAFSNKNVSSESNRLEFQFESILEVKENDGTVEKPSWKLCPQHNGVFKVRRDREKKIVVQLRQIDGFLLNIKKCFGMLLAAGRNLRHSDLQLLEMDRNATGTDSAVFVIEANWDPRVHMFEVLNTETPRDTRVFMTVAIDVIVSEISEPIRFSMEAMSRVFHEHERFYKTPQTVVSEEFTLVLEKSCDQSDPNDRKLTFISLESDSDRKRSKQNLGKSPSRMPTQLLHPTGDDESDCDEPLLSGSGKVSQECKEEHLEMWDQLIENWDQQSDRPQKISELVLDGIPDKLRGRVWQLLSNVRILAIDQPDLVEKYHIFLSQPCPSEQVIMRDIHRTFPAHDYFKESQGKGQQSLYKISKVYSLYDEEVSYCQGLSFLAASLLLHMPEEQAFCTLVKIMFNYGLRDLFKLGFDNLHLRFFQLTALLKDYIPDLSHHLEHIGIETHMYASQWFLTLFTAKFPLQMVFFILDLFLSQGMNTIFHISLALLDDAKTDLLQLDFEGTLKYFRVSLPRKYRTEASTKCLIHKAVKFRLNHSKLEVYENEYKRIKELERENEDPVLRMEKEIGRHQANTLRLERENDDLAHELVTSKIELRRKLDVAEDQIETSANAIERLTRQNMDILEENKNLMREYEQIKEMYRRDVLRLEENGSRAEKLLAEYKKLFSERSKRAENEREHFEVQKKAIIARISDCDKCWPAVCEWEKNRSPVHSASTPTGPDLLTKLEEREDHIKNLEIDLAQTKLSLVEAECRNQDLTHQLMAQSESDGKKWFKKTITQLKEVGSSLKHHERSNSSVTP,,-1.0,MEDFKDFTEVTQFTNVQYLGCSQLVNNDNDNEMKALMKVLDEQKGAQTINVTLVVPHNISGTVKLIDAQGKVLSSFSLVNIRFCIRGESSTSQNNCFGISFTHKISVGEHNSSDILHQCHVFRTSKAETAAKALYSFSYAFSNKNVSSESNRLEFQFESILEVKENDGTVEKPSWKLCPQHNGVFKVRRDREKKIVVQLRQIDGFLLNIKKCFGMLLAAGRNLRHSDLQLLEMDRNATGTDSAVFVIEANWDPRVHMFEVLNTETPRDTRVFMTVAIDVIVSEISEPIRFSMEAMSRVFHEHERFYKTPQTVVSEEFTLVLEKSCDQSDPNDRKLTFISLESDSDRKRSKQNLGKSPSRMPTQLLHPTGDDESDCDEPLLSGSGKVSQECKEEHLEMWDQLIENWDQQSDRPQKISELVLDGIPDKLRGRVWQLLSNVRILAIDQPDLVEKYHIFLSQPCPSEQVIMRDIHRTFPAHDYFKESQGKGQQPLYKISKVYSLYDEEVSYCQGLSFLAASLLLHMPEEQAFCTLVKIMFNYGLRDLFKLGFDNLHLRFFQLTALLKDYIPDLSHHLEHIGIETHMYASQWFLTLFTAKFPLQMVFFILDLFLSQGMNTIFHISLALLDDAKTDLLQLDFEGTLKYFRVSLPRKYRTEASTKCLIHKAVKFRLNHSKLEVYENEYKRIKELERENEDPVLRMEKEIGRHQANTLRLERENDDLAHELVTSKIELRRKLDVAEDQIETSANAIERLTRQNMDILEENKNLMREYEQIKEMYRRDVLRLEENGSRAEKLLAEYKKLFSERSKRAENEREHFEVQKKAIIARISDCDKCWPAVCEWEKNRSPVHSASTPTGPDLLTKLEEREDHIKNLEIDLAQTKLSLVEAECRNQDLTHQLMAQSESDGKKWFKKTITQLKEVGSSLKHHERSNSSVTP,Rab GTPase-activating protein tbc-11,Rab GTPase activating protein for the small GTPases rab-6.1 and rab-6.2 (Probable). Probably acts through rab-6.1 and rab-6.2 to play a role in microRNA-mediated gene silencing in different tissue types. Required for seam cell division and alae formation.,"In qbc24; males are fertile. Enhances seam cell division and alae formation. Enhances the localization of alg-1 to endomembranes, and instead alg-1 accumulates in the perinuclear region. Increases the total number of microRNAs and enhances microRNA-mediated gene silencing. Specifically enhances the association of alg-1 with microRNAs. Decreases the expression of lin-41 protein, which is a target for the let-7 microRNA. The seam cell division and alae formation defects are enhanced in a rab-6.1 or rab-6.2 RNAi mutant background. The localization of alg-1 is disrupted in a rab-6.1 RNAi mutant background. The alteration of TBC-11 generates a fraction of ALG-1 that can bind to target mRNAs, leading to defective gene repression.","In qbc24; males are fertile. Enhances seam cell division and alae formation. Enhances the localization of alg-1 to endomembranes, and instead alg-1 accumulates in the perinuclear region. Increases the total number of microRNAs and enhances microRNA-mediated gene silencing. Specifically enhances the association of alg-1 with microRNAs. Decreases the expression of lin-41 protein, which is a target for the let-7 microRNA. The seam cell division and alae formation defects are enhanced in a rab-6.1 or rab-6.2 RNAi mutant background. The localization of alg-1 is disrupted in a rab-6.1 RNAi mutant background. The alteration of TBC-11 generates a fraction of ALG-1 that can bind to target mRNAs, leading to defective gene repression."
303,0,0,Q969S9-Q190R,MLTNLRIFAMSHQTIPSVYINNICCYKIRASLKRLKPHVPLGRNCSSLPGLIGNDIKSLHSIINPPIAKIRNIGIMAHIDAGKTTTTERILYYSGYTRSLGDVDDGDTVTDFMAQERERGITIQSAAVTFDWKGYRVNLIDTPGHVDFTLEVERCLRVLDGAVAVFDASAGVEAQTLTVWRQADKHNIPRICFLNKMDKTGASFKYAVESIREKLKAKPLLLQLPIGEAKTFKGVVDVVMKEKLLWNCNSNDGKDFERKPLLEMNDPELLKETTEARNALIEQVADLDDEFADLVLEEFSENFDLLPAEKLQTAIHRVTLAQTAVPVLCGSALKNKGIQPLLDAVTMYLPSPEERNYEFLQWYKDDLCALAFKVLHDKQRGPLVFMRIYSGTIKPQLAIHNINGNCTERISRLLLPFADQHVEIPSLTAGNIALTVGLKHTATGDTIVSSKSSALAAARRAEREGEKKHRQNNEAERLLLAGVEIPEPVFFCTIEPPSLSKQPDLEHALKCLQREDPSLKVRLDPDSGQTVLCGMGELHIEIIHDRIKREYGLETYLGPLQVAYRETILNSVRATDTLDRTLGDKRHLVTVEVEARPIETSSVMPVIEFEYAESINEGLLKVSQEAIENGIHSACLQGPLLGSPIQDVAITLHSLTIHPGTSTTMISACVSRCVQKALKKADKQVLEPLMNLEVTVARDYLSPVLADLAQRRGNIQEIQTRQDNKVVIGFVPLAEIMGYSTVLRTLTSGSATFALELSTYQAMNPQDQNTLLNRRSGLT,,-1.0,MLTNLRIFAMSHQTIPSVYINNICCYKIRASLKRLKPHVPLGRNCSSLPGLIGNDIKSLHSIINPPIAKIRNIGIMAHIDAGKTTTTERILYYSGYTRSLGDVDDGDTVTDFMAQERERGITIQSAAVTFDWKGYRVNLIDTPGHVDFTLEVERCLRVLDGAVAVFDASAGVEAQTLTVWRQADKHNIPQICFLNKMDKTGASFKYAVESIREKLKAKPLLLQLPIGEAKTFKGVVDVVMKEKLLWNCNSNDGKDFERKPLLEMNDPELLKETTEARNALIEQVADLDDEFADLVLEEFSENFDLLPAEKLQTAIHRVTLAQTAVPVLCGSALKNKGIQPLLDAVTMYLPSPEERNYEFLQWYKDDLCALAFKVLHDKQRGPLVFMRIYSGTIKPQLAIHNINGNCTERISRLLLPFADQHVEIPSLTAGNIALTVGLKHTATGDTIVSSKSSALAAARRAEREGEKKHRQNNEAERLLLAGVEIPEPVFFCTIEPPSLSKQPDLEHALKCLQREDPSLKVRLDPDSGQTVLCGMGELHIEIIHDRIKREYGLETYLGPLQVAYRETILNSVRATDTLDRTLGDKRHLVTVEVEARPIETSSVMPVIEFEYAESINEGLLKVSQEAIENGIHSACLQGPLLGSPIQDVAITLHSLTIHPGTSTTMISACVSRCVQKALKKADKQVLEPLMNLEVTVARDYLSPVLADLAQRRGNIQEIQTRQDNKVVIGFVPLAEIMGYSTVLRTLTSGSATFALELSTYQAMNPQDQNTLLNRRSGLT,"Ribosome-releasing factor 2, mitochondrial",Mitochondrial GTPase that mediates the disassembly of ribosomes from messenger RNA at the termination of mitochondrial protein biosynthesis. Acts in collaboration with MRRF. GTP hydrolysis follows the ribosome disassembly and probably occurs on the ribosome large subunit. Not involved in the GTP-dependent ribosomal translocation step during translation elongation.,"Changes amino acid p. () to a different one in the mtEFG2 protein, resulting in normal mtEFG2 function and absence of clinical symptoms such as global developmental delay and abnormalities on cranial MRI.","Changes amino acid p. () to a different one in the mtEFG2 protein, resulting in normal mtEFG2 function and absence of clinical symptoms such as global developmental delay and abnormalities on cranial MRI."
304,0,0,Q9AQS0-F255Y,MLSGILIAALLMTLWGGWQPDIAHASDEFDALRIKWATLLTGGPALDPADSDIAARTDKLAQDANDYWEDMDLSSSRTYIWYALRGNGTSDNVNAVYERLRTMALAATTVGSSLYGNADLKEDILDALDWLYVNSYNSTRSRSAYNWWHWQLGIPMSLNDIAVLLYDDISAARMATYMDTIDYFTPSIGLTGANRAWQAIVVGVRAVIVKDAVKLAAARNGLSGTGIFPYATGGDGFYADGSFVQHTTFAYTGGYGSSVLETTANLMYLLSGSTWSVSDPNQSNVWQWIYEAYRPLLYKGAMMDMVRGREISRSYAQDHAVGHGIVASIVRLAQFAPAPHAAAFKQIAKRVIQEDTFSSFYGDVSTDTIRLAKAIVDDPSIAPAAAPNLYKQYAAMDRAVLQRPGFALGLALYSTRISSYESINSENGRGWYTGAGATYLYNQDLAQYSEDYWPTVDAYRIPGTTVASGTPIASGTGTSSWTGGVSLAGQYGASGMDLSYGAYNLSARKSWFMFDDEIVALGSGISSTAGIPIETVVDNRKLNGAGDNAWTANGAALSTGLGVAQTLTGVNWVHLAGNTADGSDIGYYFPGGATLQTKREARTGTWKQINNRPATPSTAVTRNYETMWIDHGTNPSGASYGYVLLPNKTSAQVGAYAADPAIEIVVNTSGVQSVKEKTLGLVGANFWTDTTQTADLITSNKKASVMTREIADERLEASVSDPTQANNGTIAIELARSAEGYSADPGITVTQLAPTIKFTVNVNGAKGKSFHASFQLGEDTSGPVDPGEPELPSVIVDNADSAGVTRTGTWKTASTQTDRYGANYLHDDNAGKGTKSVTFTPNLPIAGSYEVYLMWPAHFNREDAVQVDVGHASGTTRTAVDQRSGGGVWHSIGTYEFLAGSGGSVTIRNDALGSPDGYVVADAVKFVAVG,,-1.0,MLSGILIAALLMTLWGGWQPDIAHASDEFDALRIKWATLLTGGPALDPADSDIAARTDKLAQDANDYWEDMDLSSSRTYIWYALRGNGTSDNVNAVYERLRTMALAATTVGSSLYGNADLKEDILDALDWLYVNSYNSTRSRSAYNWWHWQLGIPMSLNDIAVLLYDDISAARMATYMDTIDYFTPSIGLTGANRAWQAIVVGVRAVIVKDAVKLAAARNGLSGTGIFPYATGGDGFYADGSFVQHTTFAYTGGFGSSVLETTANLMYLLSGSTWSVSDPNQSNVWQWIYEAYRPLLYKGAMMDMVRGREISRSYAQDHAVGHGIVASIVRLAQFAPAPHAAAFKQIAKRVIQEDTFSSFYGDVSTDTIRLAKAIVDDPSIAPAAAPNLYKQYAAMDRAVLQRPGFALGLALYSTRISSYESINSENGRGWYTGAGATYLYNQDLAQYSEDYWPTVDAYRIPGTTVASGTPIASGTGTSSWTGGVSLAGQYGASGMDLSYGAYNLSARKSWFMFDDEIVALGSGISSTAGIPIETVVDNRKLNGAGDNAWTANGAALSTGLGVAQTLTGVNWVHLAGNTADGSDIGYYFPGGATLQTKREARTGTWKQINNRPATPSTAVTRNYETMWIDHGTNPSGASYGYVLLPNKTSAQVGAYAADPAIEIVVNTSGVQSVKEKTLGLVGANFWTDTTQTADLITSNKKASVMTREIADERLEASVSDPTQANNGTIAIELARSAEGYSADPGITVTQLAPTIKFTVNVNGAKGKSFHASFQLGEDTSGPVDPGEPELPSVIVDNADSAGVTRTGTWKTASTQTDRYGANYLHDDNAGKGTKSVTFTPNLPIAGSYEVYLMWPAHFNREDAVQVDVGHASGTTRTAVDQRSGGGVWHSIGTYEFLAGSGGSVTIRNDALGSPDGYVVADAVKFVAVG,Xanthan lyase,"Plays a role in xanthan depolymerization pathway by cleaving the linkage between the terminal mannosyl and glucuronyl residues of the side chain of xanthan to liberate pyruvylated mannose. Is highly specific for pyruvylated side-chains of xanthan and is not effective with hyaluronate, chondroitin A, gellan, heparin or pectin.","High increase of activity by 50%. The structure of the mutant-substrate complex showed that the hydroxyl group of Y255 was far from both the C-5 atom of the GlcUA residue and the oxygen atom of the glycosidic bond to be cleaved, suggesting that Y255 likely does not act as a general base that extracts the proton from C-5 of the GlcUA residue and as a general acid that donates the proton to the glycosidic bond.","High increase of activity by 50%. The structure of the mutant-substrate complex showed that the hydroxyl group of Y255 was far from both the C-5 atom of the GlcUA residue and the oxygen atom of the glycosidic bond to be cleaved, suggesting that Y255 likely does not act as a general base that extracts the proton from C-5 of the GlcUA residue and as a general acid that donates the proton to the glycosidic bond."
305,0,0,P51843-C291W,MAGENHQWQGSILYNMLMSAKQTRAAPEAPETRLVDQCWGCSCGDEPGVGREGLLGGRNVALLYRCCFCGKDHPRQGSILYSMLTSAKQTYAAPKAPEATLGPCWGCSCGSDPGVGRAGLPGGRPVALLYRCCFCGEDHPRQGSILYSLLTSSKQTHVAPAAPEARPGGAWWDRSYFAQRPGGKEALPGGRATALLYRCCFCGEDHPQQGSTLYCVPTSTNQAQAAPEERPRAPWWDTSSGALRPVALKSPQVVCEAASAGLLKTLRFVKYLPCFQVLPLDQQLVLVRNCWASLLMLELAQDRLQFETVEVSEPSMLQKILTTRRRETGGNEPLPVPTLQHHLAPPAEARKVPSASQVQAIKCFLSKCWSLNISTKEYAYLKGTVLFNPDVPGLQCVKYIQGLQWGTQQILSEHTRMTHQGPHDRFIELNSTLFLLRFINANVIAELFFRPIIGTVSMDDMMLEMLCTKI,,-1.0,MAGENHQWQGSILYNMLMSAKQTRAAPEAPETRLVDQCWGCSCGDEPGVGREGLLGGRNVALLYRCCFCGKDHPRQGSILYSMLTSAKQTYAAPKAPEATLGPCWGCSCGSDPGVGRAGLPGGRPVALLYRCCFCGEDHPRQGSILYSLLTSSKQTHVAPAAPEARPGGAWWDRSYFAQRPGGKEALPGGRATALLYRCCFCGEDHPQQGSTLYCVPTSTNQAQAAPEERPRAPWWDTSSGALRPVALKSPQVVCEAASAGLLKTLRFVKYLPCFQVLPLDQQLVLVRNCCASLLMLELAQDRLQFETVEVSEPSMLQKILTTRRRETGGNEPLPVPTLQHHLAPPAEARKVPSASQVQAIKCFLSKCWSLNISTKEYAYLKGTVLFNPDVPGLQCVKYIQGLQWGTQQILSEHTRMTHQGPHDRFIELNSTLFLLRFINANVIAELFFRPIIGTVSMDDMMLEMLCTKI,Nuclear receptor subfamily 0 group B member 1,Orphan nuclear receptor. Component of a cascade required for the development of the hypothalamic-pituitary-adrenal-gonadal axis. Acts as a coregulatory protein that inhibits the transcriptional activity of other nuclear receptors through heterodimeric interactions. May also have a role in the development of the embryo and in the maintenance of embryonic stem cell pluripotency.,"In AHC. Cases 4, 5, and 6 showed insertion mutation. In case 6, a de novo insertion mutation was revealed by both northern hybridization and polymerase chain reaction (PCR) of a GGAA tetranucleotide tandem repeat. located in the C-terminal presumptive ligand binding domain, are unimportant to the functional role of the DAX-1 protein in adrenal embryogenesis and/or in hypothalamic-pituitary activity; and 2) molecular analysis of the DAX-1 gene may hinder genetic counseling, even in cases with insertion mutation, because a detection of de novo insertion may include another affected or carrier child.","In AHC. Cases 4, 5, and 6 showed insertion mutation. In case 6, a de novo insertion mutation was revealed by both northern hybridization and polymerase chain reaction (PCR) of a GGAA tetranucleotide tandem repeat. located in the C-terminal presumptive ligand binding domain, are unimportant to the functional role of the DAX-1 protein in adrenal embryogenesis and/or in hypothalamic-pituitary activity; and 2) molecular analysis of the DAX-1 gene may hinder genetic counseling, even in cases with insertion mutation, because a detection of de novo insertion may include another affected or carrier child."
306,0,0,Q9JJS6-A308H,MEIIFGQNKKEQLEPVQAKVTGSIPAWLQGTLLRNGPGMHTVGESKYNHWFDGLALLHSFSIRDGEVFYRSKYLQSDTYIANIEANRIVVSEFGTMAYPDPCKNIFSKAFSYLSHTIPDFTDNCLINIMKCGEDFYATTETNYIRKIDPQTLETLEKVDYRKYVAVNLATSHPHYDEAGNVLNMGTSVVDKGRTKYVIFKIPATVPDSKKKGKSPVKHAEVFCSISSRSLLSPSYYHSFGVTENYVVFLEQPFKLDILKMATAYMRGVSWASCMSFDREDKTYIHIIDQRTRKPVPTKFYTDPMVVFHHVNAYEEDGCVLFDVIAYEDSSLYQLFYLANLNKDFEEKSRLTSVPTLRRFAVPLHVDKDAEVGSNLVKVSSTTATALKEKDGHVYCQPEVLYEGLELPRINYAYNGKPYRYIFAAEVQWSPVPTKILKYDILTKSSLKWSEESCWPAEPLFVPTPGAKDEDDGVILSAIVSTDPQKLPFLLILDAKSFTELARASVDADMHLDLHGLFIPDADWNAVKQTPAETQEVENSDHPTDPTAPELSHSENDFTAGHGGSSL,,-1.0,MEIIFGQNKKEQLEPVQAKVTGSIPAWLQGTLLRNGPGMHTVGESKYNHWFDGLALLHSFSIRDGEVFYRSKYLQSDTYIANIEANRIVVSEFGTMAYPDPCKNIFSKAFSYLSHTIPDFTDNCLINIMKCGEDFYATTETNYIRKIDPQTLETLEKVDYRKYVAVNLATSHPHYDEAGNVLNMGTSVVDKGRTKYVIFKIPATVPDSKKKGKSPVKHAEVFCSISSRSLLSPSYYHSFGVTENYVVFLEQPFKLDILKMATAYMRGVSWASCMSFDREDKTYIHIIDQRTRKPVPTKFYTDPMVVFAHVNAYEEDGCVLFDVIAYEDSSLYQLFYLANLNKDFEEKSRLTSVPTLRRFAVPLHVDKDAEVGSNLVKVSSTTATALKEKDGHVYCQPEVLYEGLELPRINYAYNGKPYRYIFAAEVQWSPVPTKILKYDILTKSSLKWSEESCWPAEPLFVPTPGAKDEDDGVILSAIVSTDPQKLPFLLILDAKSFTELARASVDADMHLDLHGLFIPDADWNAVKQTPAETQEVENSDHPTDPTAPELSHSENDFTAGHGGSSL,"Beta,beta-carotene 15,15'-dioxygenase",Symmetrically cleaves beta-carotene into two molecules of retinal using a dioxygenase mechanism.,"Decrease in protein abundance. Gain of beta-carotene 15,15'-monooxygenase activity. Increased iron binding. Mutation of H308 produced enhanced although enzymatically active proteins, with an increase in activity mostly due to changes in V(max).","Decrease in protein abundance. Gain of beta-carotene 15,15'-monooxygenase activity. Increased iron binding. Mutation of H308 produced enhanced although enzymatically active proteins, with an increase in activity mostly due to changes in V(max)."
307,0,0,Q92504-A293S,MARGLGAPHWVAVGLLTWATLGLLVAGLGGHDDLHDDLQEDFHGHSHRHSHEDFHHGHSHAHGHGHTHESIWHGHTHDHDHGHSHEDLHHGHSHGYSHESLYHRGHGHDHEHSHGGYGESGAPGIKQDLDAVTLWAYALGATVLISAAPFFVLFLIPVESNSPRHRSLLQILLSFASGGLLGDAFLHLIPHALEPHSHHTLEQPGHGHSHSGQGPILSVGLWVLSGIVAFLVVEKFVRHVKGGHGHSHGHGHAHSHTRGSHGHGRQERSTKEKQSSEEEEKETRGVQKRRGGSTVPKDGPVRPQNAEEEKRGLDLRVSGYLNLAADLAHNFTDGLAIGASFRGGRGLGILTTMTVLLHEVPHEVGDFAILVQSGCSKKQAMRLQLLTAVGALAGTACALLTEGGAVGSEIAGGAGPGWVLPFTAGGFIYVATVSVLPELLREASPLQSLLEVLGLLGGVIMMVLIAHLE,,-1.0,MARGLGAPHWVAVGLLTWATLGLLVAGLGGHDDLHDDLQEDFHGHSHRHSHEDFHHGHSHAHGHGHTHESIWHGHTHDHDHGHSHEDLHHGHSHGYSHESLYHRGHGHDHEHSHGGYGESGAPGIKQDLDAVTLWAYALGATVLISAAPFFVLFLIPVESNSPRHRSLLQILLSFASGGLLGDAFLHLIPHALEPHSHHTLEQPGHGHSHSGQGPILSVGLWVLSGIVAFLVVEKFVRHVKGGHGHSHGHGHAHSHTRGSHGHGRQERSTKEKQSSEEEEKETRGVQKRRGGATVPKDGPVRPQNAEEEKRGLDLRVSGYLNLAADLAHNFTDGLAIGASFRGGRGLGILTTMTVLLHEVPHEVGDFAILVQSGCSKKQAMRLQLLTAVGALAGTACALLTEGGAVGSEIAGGAGPGWVLPFTAGGFIYVATVSVLPELLREASPLQSLLEVLGLLGGVIMMVLIAHLE,Zinc transporter SLC39A7,"Transports Zn(2+) from the endoplasmic reticulum (ER)/Golgi apparatus to the cytosol, playing an essential role in the regulation of cytosolic zinc levels. Acts as gatekeeper of zinc release from intracellular stores, requiring post-translational activation by phosphorylation, resulting in activation of multiple downstream pathways leading to cell growth and proliferation. Has an essential role in B cell development and is required for proper B cell receptor signaling. Plays an important role in maintaining intestinal epithelial homeostasis and skin dermis development by regulating ER function. Controls cell signaling pathways involved in glucose metabolism in skeletal muscle. Has a protective role against ER stress in differents biological contexts. Mediates Zn(2+)-induced ferroptosis.",Loss of dephosphorylation in response to Zn(2+) treatment and of cytosolic Zn(2+) uptake.,Loss of dephosphorylation in response to Zn(2+) treatment and of cytosolic Zn(2+) uptake.
308,0,0,P08692-Y107R,MSNITIYHNPACGTSRNTLEMIRNSGTEPTIILYLENPPSRDELVKLIADMGISVRALLRKNVEPYEQLGLAEDKFTDDQLIDFMLQHPILINRPIVVTPLGTRLCRPSEVVLDILQDAQKGAFTKEDGEKVVDEAGKRLK,,-1.0,MSNITIYHNPACGTSRNTLEMIRNSGTEPTIILYLENPPSRDELVKLIADMGISVRALLRKNVEPYEQLGLAEDKFTDDQLIDFMLQHPILINRPIVVTPLGTRLCYPSEVVLDILQDAQKGAFTKEDGEKVVDEAGKRLK,Arsenate reductase,Involved in resistance to arsenate. Catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)]. The resulting arsenite is then extruded from the cell via the ArsAB transport system (Probable).,Decrease of reductase activity. Mutant is resistant to arsenate.,Decrease of reductase activity. Mutant is resistant to arsenate.
309,0,0,P9WH43-A307F,MPSPTVTSPQVAVNDIGSSEDFLAAIDKTIKYFNDGDIVEGTIVKVDRDEVLLDIGYKTEGVIPARELSIKHDVDPNEVVSVGDEVEALVLTKEDKEGRLILSKKRAQYERAWGTIEALKEKDEAVKGTVIEVVKGGLILDIGLRGFLPASLVEMRRVRDLQPYIGKEIEAKIIELDKNRNNVVLSRRAWLEQTQSEVRSEFLNNLQKGTIRKGVVSSIVNFGAFVDLGGVDGLVHVSELSWKHIDHPSEVVQVGDEVTVEVLDVDMDRERVSLSLKATQEDPWRHFARTHAIGQIVPGKVTKLVPFGAFVRVEEGIEGLVHISELAERHVEVPDQVVAVGDDAMVKVIDIDLERRRISLSLKQANEDYTEEFDPAKYGMADSYDEQGNYIFPEGFDAETNEWLEGFEKQRAEWEARYAEAERRHKMHTAQMEKFAAAEAAGRGADDQSSASSAPSEKTAGGSLASDAQLAALREKLAGSA,,-1.0,MPSPTVTSPQVAVNDIGSSEDFLAAIDKTIKYFNDGDIVEGTIVKVDRDEVLLDIGYKTEGVIPARELSIKHDVDPNEVVSVGDEVEALVLTKEDKEGRLILSKKRAQYERAWGTIEALKEKDEAVKGTVIEVVKGGLILDIGLRGFLPASLVEMRRVRDLQPYIGKEIEAKIIELDKNRNNVVLSRRAWLEQTQSEVRSEFLNNLQKGTIRKGVVSSIVNFGAFVDLGGVDGLVHVSELSWKHIDHPSEVVQVGDEVTVEVLDVDMDRERVSLSLKATQEDPWRHFARTHAIGQIVPGKVTKLVPAGAFVRVEEGIEGLVHISELAERHVEVPDQVVAVGDDAMVKVIDIDLERRRISLSLKQANEDYTEEFDPAKYGMADSYDEQGNYIFPEGFDAETNEWLEGFEKQRAEWEARYAEAERRHKMHTAQMEKFAAAEAAGRGADDQSSASSAPSEKTAGGSLASDAQLAALREKLAGSA,Small ribosomal subunit protein bS1,"Binds mRNA, facilitating recognition of most mRNAs by the 30S ribosomal subunit during translation initiation (By similarity). Probably plays a role in trans-translation; binds tmRNA (the product of the ssrA gene). In trans-translation Ala-aminoacylated transfer-messenger RNA (tmRNA, product of the ssrA gene; the 2 termini fold to resemble tRNA(Ala) while it encodes a short internal open reading frame (the tag peptide)) acts like a tRNA, entering the A-site of the ribosome and displacing the stalled mRNA (which is subsequently degraded). The ribosome then switches to translate the ORF on the tmRNA, the nascent peptide is terminated with the 'tag peptide' encoded by the tmRNA and thus targeted for degradation (By similarity).","2.5-fold increase in binding of POA, increased binding of tmRNA (expressed as residues 285-481). Conformational changes induced by mutation at F307 enable the POA binding activity.","2.5-fold increase in binding of POA, increased binding of tmRNA (expressed as residues 285-481). Conformational changes induced by mutation at F307 enable the POA binding activity."
310,0,0,P16522-S80G,MNDDSQDKIIHDIRIQLRKAATELSRWKLYGSSKWAAEALAGLAEAIDVDQTHSLADESPLRNKQGVPKQMFEIPQNGFGLSETEYDLYLLGSTLFDAKEFDRCVFFLKDVTNPYLKFLKLYSKFLSWDKKSQESMENILTTGKFTDEMYRANKDGDGSGNEDINQSGHQRANLKMVSNEHESQSNISSILKEINTFLESYEIKIDDDEADLGLALLYYLRGVILKQEKNISKAMSSFLKSLSCYSFNWSCWLELMDCLQKVDDALLLNNYLYQNFQFKFSENLGSQRTIEFNIMIKFFKLKVFEELNGQLEDYFEDLEFLLQVFPNFTFLKAYNATISYNNLDYVTAESRFDDIVKQDPYRLNDLETYSNILYVMQKNSKLAYLAQFVSQIDRFRPETCCIIANYYSARQEHEKSIMYFRRALTLDKKTTNAWTLMGHEFVELSNSHAAIECYRRAVDICPRDFKAWFGLGQAYALLDMHLYSLYYFQKACTLKPWDRRIWQVLGECYSKTGNKVEAIKCYKRSIKASQTVDQNTSIYYRLAQLYEELEDLQECKKFMMKCVDVEELLEGIVTDETVKARLWLAIFEIKAGNYQLAYDYAMGVSSGTSQEIEEARMLARECRRHM,,-1.0,MNDDSQDKIIHDIRIQLRKAATELSRWKLYGSSKWAAEALAGLAEAIDVDQTHSLADESPLRNKQGVPKQMFEIPQNGFSLSETEYDLYLLGSTLFDAKEFDRCVFFLKDVTNPYLKFLKLYSKFLSWDKKSQESMENILTTGKFTDEMYRANKDGDGSGNEDINQSGHQRANLKMVSNEHESQSNISSILKEINTFLESYEIKIDDDEADLGLALLYYLRGVILKQEKNISKAMSSFLKSLSCYSFNWSCWLELMDCLQKVDDALLLNNYLYQNFQFKFSENLGSQRTIEFNIMIKFFKLKVFEELNGQLEDYFEDLEFLLQVFPNFTFLKAYNATISYNNLDYVTAESRFDDIVKQDPYRLNDLETYSNILYVMQKNSKLAYLAQFVSQIDRFRPETCCIIANYYSARQEHEKSIMYFRRALTLDKKTTNAWTLMGHEFVELSNSHAAIECYRRAVDICPRDFKAWFGLGQAYALLDMHLYSLYYFQKACTLKPWDRRIWQVLGECYSKTGNKVEAIKCYKRSIKASQTVDQNTSIYYRLAQLYEELEDLQECKKFMMKCVDVEELLEGIVTDETVKARLWLAIFEIKAGNYQLAYDYAMGVSSGTSQEIEEARMLARECRRHM,Anaphase-promoting complex subunit CDC23,"Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. In early mitosis, the APC/C is activated by CDC20 and targets securin PDS1, the B-type cyclin CLB5, and other anaphase inhibitory proteins for proteolysis, thereby triggering the separation of sister chromatids at the metaphase-to-anaphase transition. In late mitosis and in G1, degradation of CLB5 allows activation of the APC/C by CDH1, which is needed to destroy CDC20 and the B-type cyclin CLB2 to allow exit from mitosis and creating the low CDK state necessary for cytokinesis and for reforming prereplicative complexes in G1 prior to another round of replication.",In CDC23-44; G2/M cell cycle release at 37 degrees Celsius. The mutation in the CDC23 gene causes a single amino acid change in the protein. This mutation is found within a stable domain of CDC23 and may not affect its function or stability.,In CDC23-44; G2/M cell cycle release at 37 degrees Celsius. The mutation in the CDC23 gene causes a single amino acid change in the protein. This mutation is found within a stable domain of CDC23 and may not affect its function or stability.
311,0,0,O54908-E242R,MMVVCAAAAVRFLAVFTMMALCSLPLLGASATLNSVLINSNAIKNLPPPLGGAGGQPGSAVSVAPGVLYEGGNKYQTLDNYQPYPCAEDEECGSDEYCSSPSRGAAGVGGVQICLACRKRRKRCMRHAMCCPGNYCKNGICMPSDHSHFPRGEIEESIIENLGNDHNAAAGDGYPRRTTLTSKIYHTKGQEGSVCLRSSDCAAGLCCARHFWSKICKPVLKEGQVCTKHKRKGSHGLEIFQRCYCGEGLACRIQKDHHQASNSSRLHTCQRH,,-1.0,MMVVCAAAAVRFLAVFTMMALCSLPLLGASATLNSVLINSNAIKNLPPPLGGAGGQPGSAVSVAPGVLYEGGNKYQTLDNYQPYPCAEDEECGSDEYCSSPSRGAAGVGGVQICLACRKRRKRCMRHAMCCPGNYCKNGICMPSDHSHFPRGEIEESIIENLGNDHNAAAGDGYPRRTTLTSKIYHTKGQEGSVCLRSSDCAAGLCCARHFWSKICKPVLKEGQVCTKHKRKGSHGLEIFQECYCGEGLACRIQKDHHQASNSSRLHTCQRH,Dickkopf-related protein 1,"Antagonizes canonical Wnt signaling by inhibiting LRP5/6 interaction with Wnt and by forming a ternary complex with the transmembrane protein KREMEN that promotes internalization of LRP5/6. Inhibits the pro-apoptotic function of KREMEN1 in a Wnt-independent manner, and has anti-apoptotic activity. Plays a role in limb development; attenuates Wnt signaling in the developing limb to allow normal limb patterning.",50% increased binding to LRP6.,50% increased binding to LRP6.
312,0,0,P9WGT3-A140S,MTATATEGAKPPFVSRSVLVTGGNRGIGLAIAQRLAADGHKVAVTHRGSGAPKGLFGVECDVTDSDAVDRAFTAVEEHQGPVEVLVSNAGLSADAFLMRMTEEKFEKVINANLTGAFRVAQRASRSMQRNKFGRMIFIGSVSGSWGIGNQANYAASKAGVIGMARSIARELSKANVTANVVAPGYIDTDMTRALDERIQQGALQFIPAKRVGTPAEVAGVVSFLASEDASYISGAVIPVDGGMGMGH,,-1.0,MTATATEGAKPPFVSRSVLVTGGNRGIGLAIAQRLAADGHKVAVTHRGSGAPKGLFGVECDVTDSDAVDRAFTAVEEHQGPVEVLVSNAGLSADAFLMRMTEEKFEKVINANLTGAFRVAQRASRSMQRNKFGRMIFIGAVSGSWGIGNQANYAASKAGVIGMARSIARELSKANVTANVVAPGYIDTDMTRALDERIQQGALQFIPAKRVGTPAEVAGVVSFLASEDASYISGAVIPVDGGMGMGH,3-oxoacyl-[acyl-carrier-protein] reductase MabA,"Part of the mycobacterial fatty acid elongation system FAS-II, which is involved in mycolic acid biosynthesis. Catalyzes the NADPH-dependent reduction of beta-ketoacyl derivatives, the second step of the FAS-II elongation cycle. May preferentially metabolize long-chain substrates (C8-C20). Can use CoA derivatives as substrates in vitro.","Gain of activity. Can still bind NADPH. The mutation in MabA has been shown to increase the activity of the enzyme, leading to an increase in the production of mycolic acids. This can enhance the growth and survival of Mycobacterium tuberculosis.","Gain of activity. Can still bind NADPH. The mutation in MabA has been shown to increase the activity of the enzyme, leading to an increase in the production of mycolic acids. This can enhance the growth and survival of Mycobacterium tuberculosis."
313,0,0,Q92504-K363E,MARGLGAPHWVAVGLLTWATLGLLVAGLGGHDDLHDDLQEDFHGHSHRHSHEDFHHGHSHAHGHGHTHESIWHGHTHDHDHGHSHEDLHHGHSHGYSHESLYHRGHGHDHEHSHGGYGESGAPGIKQDLDAVTLWAYALGATVLISAAPFFVLFLIPVESNSPRHRSLLQILLSFASGGLLGDAFLHLIPHALEPHSHHTLEQPGHGHSHSGQGPILSVGLWVLSGIVAFLVVEKFVRHVKGGHGHSHGHGHAHSHTRGSHGHGRQERSTKEKQSSEEEEKETRGVQKRRGGSTVPKDGPVRPQNAEEEKRGLDLRVSGYLNLAADLAHNFTDGLAIGASFRGGRGLGILTTMTVLLHEVPHEVGDFAILVQSGCSKKQAMRLQLLTAVGALAGTACALLTEGGAVGSEIAGGAGPGWVLPFTAGGFIYVATVSVLPELLREASPLQSLLEVLGLLGGVIMMVLIAHLE,,-1.0,MARGLGAPHWVAVGLLTWATLGLLVAGLGGHDDLHDDLQEDFHGHSHRHSHEDFHHGHSHAHGHGHTHESIWHGHTHDHDHGHSHEDLHHGHSHGYSHESLYHRGHGHDHEHSHGGYGESGAPGIKQDLDAVTLWAYALGATVLISAAPFFVLFLIPVESNSPRHRSLLQILLSFASGGLLGDAFLHLIPHALEPHSHHTLEQPGHGHSHSGQGPILSVGLWVLSGIVAFLVVEKFVRHVKGGHGHSHGHGHAHSHTRGSHGHGRQERSTKEKQSSEEEEKETRGVQKRRGGSTVPKDGPVRPQNAEEEKRGLDLRVSGYLNLAADLAHNFTDGLAIGASFRGGRGLGILTTMTVLLHEVPHKVGDFAILVQSGCSKKQAMRLQLLTAVGALAGTACALLTEGGAVGSEIAGGAGPGWVLPFTAGGFIYVATVSVLPELLREASPLQSLLEVLGLLGGVIMMVLIAHLE,Zinc transporter SLC39A7,"Transports Zn(2+) from the endoplasmic reticulum (ER)/Golgi apparatus to the cytosol, playing an essential role in the regulation of cytosolic zinc levels. Acts as gatekeeper of zinc release from intracellular stores, requiring post-translational activation by phosphorylation, resulting in activation of multiple downstream pathways leading to cell growth and proliferation. Has an essential role in B cell development and is required for proper B cell receptor signaling. Plays an important role in maintaining intestinal epithelial homeostasis and skin dermis development by regulating ER function. Controls cell signaling pathways involved in glucose metabolism in skeletal muscle. Has a protective role against ER stress in differents biological contexts. Mediates Zn(2+)-induced ferroptosis.",Increased zinc ion transporter activity; does not affect localization to endoplasmic reticulum.,Increased zinc ion transporter activity; does not affect localization to endoplasmic reticulum.
314,0,0,O00217-D159A,MRCLTTPMLLRALAQAARAGPPGGRSLHSSAVAATYKYVNMQDPEMDMKSVTDRAARTLLWTELFRGLGMTLSYLFREPATINYPFEKGPLSPRFRGEHALRRYPSGEERCIACKLCEAICPAQAITIEAEPRADGSRRTTRYDIDMTKCIYCGFCQEACPVDAIVEGPNFEFSTETHEELLYNKEKLLNNGDKWEAEIAANIQADYLYR,,-1.0,MRCLTTPMLLRALAQAARAGPPGGRSLHSSAVAATYKYVNMQDPEMDMKSVTDRAARTLLWTELFRGLGMTLSYLFREPATINYPFEKGPLSPRFRGEHALRRYPSGEERCIACKLCEAICPAQAITIEAEPRADGSRRTTRYDIDMTKCIYCGFCQEDCPVDAIVEGPNFEFSTETHEELLYNKEKLLNNGDKWEAEIAANIQADYLYR,"NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial","Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I.",Decrease in MC1DN2; unknown pathological significance; increase in enzyme activity; enhanced assembly of complex I.,Decrease in MC1DN2; unknown pathological significance; increase in enzyme activity; enhanced assembly of complex I.
315,0,0,Q68CZ1-T229A,MSGPTDETAGDLPVKDTGLNLFGMGGLQETSTTRTMKSRQAVSRVSREELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIRLVNDKKRYERVGGGPKRLGRDVEMEEMIEQLQEKVHELEKQNETLKNRLISAKQQLQTQGYRQTPYNNVQSRINTGRRKANENAGLQECPRKGIKFQDADVAETPHPMFTKYGNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIELSLLQLREQQATDQRSNIRDNVEMIKLHKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQLHSMKFSERRIEELQDRINDLEKERELLKENYDKLYDSAFSAAHEEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQQLDELKKRIKLYNQENDINADELSEALLLIKAQKEQKNGDLSFLVKVDSEINKDLERSMRELQATHAETVQELEKTRNMLIMQHKINKDYQMEVEAVTRKMENLQQDYELKVEQYVHLLDIRAARIHKLEAQLKDIAYGTKQYKFKPEIMPDDSVDEFDETIHLERGENLFEIHINKVTFSSEVLQASGDKEPVTFCTYAFYDFELQTTPVVRGLHPEYNFTSQYLVHVNDLFLQYIQKNTITLEVHQAYSTEYETIAACQLKFHEILEKSGRIFCTASLIGTKGDIPNFGTVEYWFRLRVPMDQAIRLYRERAKALGYITSNFKGPEHMQSLSQQAPKTAQLSSTDSTDGNLNELHITIRCCNHLQSRASHLQPHPYVVYKFFDFADHDTAIIPSSNDPQFDDHMYFPVPMNMDLDRYLKSESLSFYVFDDSDTQENIYIGKVNVPLISLAHDRCISGIFELTDHQKHPAGTIHVILKWKFAYLPPSGSITTEDLGNFIRSEEPEVVQRLPPASSVSTLVLAPRPKPRQRLTPVDKKVSFVDIMPHQSDETSPPPEDRKEISPEVEHIPEIEINMLTVPHVPKVSQE,,-1.0,MSGPTDETAGDLPVKDTGLNLFGMGGLQETSTTRTMKSRQAVSRVSREELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIRLVNDKKRYERVGGGPKRLGRDVEMEEMIEQLQEKVHELEKQNETLKNRLISAKQQLQTQGYRQTPYNNVQSRINTGRRKANENAGLQECPRKGIKFQDADVAETPHPMFTKYGNSLLEEARGEIRNLENVIQSQRGQIEELEHLTEILKTQLRRKENEIELSLLQLREQQATDQRSNIRDNVEMIKLHKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQLHSMKFSERRIEELQDRINDLEKERELLKENYDKLYDSAFSAAHEEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQQLDELKKRIKLYNQENDINADELSEALLLIKAQKEQKNGDLSFLVKVDSEINKDLERSMRELQATHAETVQELEKTRNMLIMQHKINKDYQMEVEAVTRKMENLQQDYELKVEQYVHLLDIRAARIHKLEAQLKDIAYGTKQYKFKPEIMPDDSVDEFDETIHLERGENLFEIHINKVTFSSEVLQASGDKEPVTFCTYAFYDFELQTTPVVRGLHPEYNFTSQYLVHVNDLFLQYIQKNTITLEVHQAYSTEYETIAACQLKFHEILEKSGRIFCTASLIGTKGDIPNFGTVEYWFRLRVPMDQAIRLYRERAKALGYITSNFKGPEHMQSLSQQAPKTAQLSSTDSTDGNLNELHITIRCCNHLQSRASHLQPHPYVVYKFFDFADHDTAIIPSSNDPQFDDHMYFPVPMNMDLDRYLKSESLSFYVFDDSDTQENIYIGKVNVPLISLAHDRCISGIFELTDHQKHPAGTIHVILKWKFAYLPPSGSITTEDLGNFIRSEEPEVVQRLPPASSVSTLVLAPRPKPRQRLTPVDKKVSFVDIMPHQSDETSPPPEDRKEISPEVEHIPEIEINMLTVPHVPKVSQE,Protein fantom,"Negatively regulates signaling through the G-protein coupled thromboxane A2 receptor (TBXA2R). May be involved in mechanisms like programmed cell death, craniofacial development, patterning of the limbs, and formation of the left-right axis. Involved in the organization of apical junctions; the function is proposed to implicate a NPHP1-4-8 module. Does not seem to be strictly required for ciliogenesis. Involved in establishment of planar cell polarity such as in cochlear sensory epithelium and is proposed to implicate stabilization of disheveled proteins. Involved in regulation of proteasomal activity at the primary cilium probably implicating association with PSDM2.","Associated with the development of retinal degeneration in individuals with ciliopathies caused by mutations in other genes; found in patients with Leber congenital amaurosis, Senior-Loken syndrome, Joubert syndrome and Bardet-Biedl syndrome; enhances interaction with RPGR. The variant of RPGRIP1L is associated with the development of retinal degeneration in individuals with ciliopathies caused by mutations in other genes. The T229-encoded protein significantly facilitates the interaction between RPGRIP1L and RPGR, which leads to retinal degeneration.","Associated with the development of retinal degeneration in individuals with ciliopathies caused by mutations in other genes; found in patients with Leber congenital amaurosis, Senior-Loken syndrome, Joubert syndrome and Bardet-Biedl syndrome; enhances interaction with RPGR. The variant of RPGRIP1L is associated with the development of retinal degeneration in individuals with ciliopathies caused by mutations in other genes. The T229-encoded protein significantly facilitates the interaction between RPGRIP1L and RPGR, which leads to retinal degeneration."
316,0,0,O54908-E217K,MMVVCAAAAVRFLAVFTMMALCSLPLLGASATLNSVLINSNAIKNLPPPLGGAGGQPGSAVSVAPGVLYEGGNKYQTLDNYQPYPCAEDEECGSDEYCSSPSRGAAGVGGVQICLACRKRRKRCMRHAMCCPGNYCKNGICMPSDHSHFPRGEIEESIIENLGNDHNAAAGDGYPRRTTLTSKIYHTKGQEGSVCLRSSDCAAGLCCARHFWSKICKPVLKEGQVCTKHKRKGSHGLEIFQRCYCGEGLACRIQKDHHQASNSSRLHTCQRH,,-1.0,MMVVCAAAAVRFLAVFTMMALCSLPLLGASATLNSVLINSNAIKNLPPPLGGAGGQPGSAVSVAPGVLYEGGNKYQTLDNYQPYPCAEDEECGSDEYCSSPSRGAAGVGGVQICLACRKRRKRCMRHAMCCPGNYCKNGICMPSDHSHFPRGEIEESIIENLGNDHNAAAGDGYPRRTTLTSKIYHTKGQEGSVCLRSSDCAAGLCCARHFWSKICEPVLKEGQVCTKHKRKGSHGLEIFQRCYCGEGLACRIQKDHHQASNSSRLHTCQRH,Dickkopf-related protein 1,"Antagonizes canonical Wnt signaling by inhibiting LRP5/6 interaction with Wnt and by forming a ternary complex with the transmembrane protein KREMEN that promotes internalization of LRP5/6. Inhibits the pro-apoptotic function of KREMEN1 in a Wnt-independent manner, and has anti-apoptotic activity. Plays a role in limb development; attenuates Wnt signaling in the developing limb to allow normal limb patterning.","50% increased binding to LRP6. The mutation in Dkk2 may affect its interaction with the third LRP5/6 beta-propeller domain, potentially altering its binding affinity and functional role in the canonical Wnt pathway.","50% increased binding to LRP6. The mutation in Dkk2 may affect its interaction with the third LRP5/6 beta-propeller domain, potentially altering its binding affinity and functional role in the canonical Wnt pathway."
317,0,0,P25522-A224R,MSDNDTIVAQATPPGRGGVGILRISGFKAREVAETVLGKLPKPRYADYLPFKDADGSVLDQGIALWFPGPNSFTGEDVLELQGHGGPVILDLLLKRILTIPGLRIARPGEFSERAFLNDKLDLAQAEAIADLIDASSEQAARSALNSLQGAFSARVNHLVEALTHLRIYVEAAIDFPDEEIDFLSDGKIEAQLNDVIADLDAVRAEARQGSLLREGMKVVIAGRPNAGKSSLLNALAGREAAIVTDIAGTTRDVLREHIHIDGMPLHIIDTAGLREASDEVERIGIERAWQEIEQADRVLFMVDGTTTDAVDPAEIWPEFIARLPAKLPITVVRNKADITGETLGMSEVNGHALIRLSARTGEGVDVLRNHLKQSMGFDTNMEGGFLARRRHLQALEQAAEHLQQGKAQLLGAWAGELLAEELRLAQQNLSEITGEFTSDDLLGRIFSSFCIGK,,-1.0,MSDNDTIVAQATPPGRGGVGILRISGFKAREVAETVLGKLPKPRYADYLPFKDADGSVLDQGIALWFPGPNSFTGEDVLELQGHGGPVILDLLLKRILTIPGLRIARPGEFSERAFLNDKLDLAQAEAIADLIDASSEQAARSALNSLQGAFSARVNHLVEALTHLRIYVEAAIDFPDEEIDFLSDGKIEAQLNDVIADLDAVRAEARQGSLLREGMKVVIAGAPNAGKSSLLNALAGREAAIVTDIAGTTRDVLREHIHIDGMPLHIIDTAGLREASDEVERIGIERAWQEIEQADRVLFMVDGTTTDAVDPAEIWPEFIARLPAKLPITVVRNKADITGETLGMSEVNGHALIRLSARTGEGVDVLRNHLKQSMGFDTNMEGGFLARRRHLQALEQAAEHLQQGKAQLLGAWAGELLAEELRLAQQNLSEITGEFTSDDLLGRIFSSFCIGK,tRNA modification GTPase MnmE,"Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.",1.5-fold increase in GTPase activity and almost no change in affinity.,1.5-fold increase in GTPase activity and almost no change in affinity.
318,0,0,P51843-K377E,MAGENHQWQGSILYNMLMSAKQTRAAPEAPETRLVDQCWGCSCGDEPGVGREGLLGGRNVALLYRCCFCGKDHPRQGSILYSMLTSAKQTYAAPKAPEATLGPCWGCSCGSDPGVGRAGLPGGRPVALLYRCCFCGEDHPRQGSILYSLLTSSKQTHVAPAAPEARPGGAWWDRSYFAQRPGGKEALPGGRATALLYRCCFCGEDHPQQGSTLYCVPTSTNQAQAAPEERPRAPWWDTSSGALRPVALKSPQVVCEAASAGLLKTLRFVKYLPCFQVLPLDQQLVLVRNCWASLLMLELAQDRLQFETVEVSEPSMLQKILTTRRRETGGNEPLPVPTLQHHLAPPAEARKVPSASQVQAIKCFLSKCWSLNISTKEYAYLKGTVLFNPDVPGLQCVKYIQGLQWGTQQILSEHTRMTHQGPHDRFIELNSTLFLLRFINANVIAELFFRPIIGTVSMDDMMLEMLCTKI,,-1.0,MAGENHQWQGSILYNMLMSAKQTRAAPEAPETRLVDQCWGCSCGDEPGVGREGLLGGRNVALLYRCCFCGKDHPRQGSILYSMLTSAKQTYAAPKAPEATLGPCWGCSCGSDPGVGRAGLPGGRPVALLYRCCFCGEDHPRQGSILYSLLTSSKQTHVAPAAPEARPGGAWWDRSYFAQRPGGKEALPGGRATALLYRCCFCGEDHPQQGSTLYCVPTSTNQAQAAPEERPRAPWWDTSSGALRPVALKSPQVVCEAASAGLLKTLRFVKYLPCFQVLPLDQQLVLVRNCWASLLMLELAQDRLQFETVEVSEPSMLQKILTTRRRETGGNEPLPVPTLQHHLAPPAEARKVPSASQVQAIKCFLSKCWSLNISTKKYAYLKGTVLFNPDVPGLQCVKYIQGLQWGTQQILSEHTRMTHQGPHDRFIELNSTLFLLRFINANVIAELFFRPIIGTVSMDDMMLEMLCTKI,Nuclear receptor subfamily 0 group B member 1,Orphan nuclear receptor. Component of a cascade required for the development of the hypothalamic-pituitary-adrenal-gonadal axis. Acts as a coregulatory protein that inhibits the transcriptional activity of other nuclear receptors through heterodimeric interactions. May also have a role in the development of the embryo and in the maintenance of embryonic stem cell pluripotency.,Enhancement of repressor function in AHC occurs due to the missense mutation in the putative ligand-binding domain of DAX-1.,Enhancement of repressor function in AHC occurs due to the missense mutation in the putative ligand-binding domain of DAX-1.
319,0,0,Q9XIE6-A413D,MVRSGSFSVDSSATHQRTPSRTVTLGHIQPQAPTYRTVYCNDRESNQPVRFKGNSISTTKYNVFTFLPKGLFEQFRRIANIYFLGISCLSMTPISPVSPITNVAPLSMVLLVSLIKEAFEDWKRFQNDMSINNSTVEILQDQQWVSIPWRKLQVGDIVKIKKDGFFPADILFMSSTNSDGICYVETANLDGETNLKIRKALERTWDYLVPEKAYEFKGEIQCEQPNNSLYTFTGNLVVQKQTLPLSPDQLLLRGCSLRNTEYIVGAVVFTGHETKVMMNAMNAPSKRSTLEKKLDKLIITIFCVLVTMCLIGAIGCSIVTDREDKYLGLHNSDWEYRNGLMIGFFTFFTLVTLFSSIIPISLYVSIEMIKFIQSTQFINRDLNMYHAETNTPASARTSNLNEELGQVEYIFSDKTGTLTRNLMEFFKCSIGGVSYGCGVTEIEKGIAQRHGLKVQEEQRSTGAIREKGFNFDDPRLMRGAWRNEPNPDLCKELFRCLAICHTVLPEGDESPEKIVYQAASPDEAALVTAAKNFGFFFYRRTPTMVYVRESHVEKMGKIQDVAYEILNVLEFNSTRKRQSVVCRFPDGRLVLYCKGADNVIFERLANGMDDVRKVTREHLEHFGSSGLRTLCLAYKDLNPETYDSWNEKFIQAKSALRDREKKLDEVAELIEKDLILIGSTAIEDKLQEGVPTCIETLSRAGIKIWVLTGDKMETAINIAYACNLINNEMKQFVISSETDAIREAEERGDQVEIARVIKEEVKRELKKSLEEAQHSLHTVAGPKLSLVIDGKCLMYALDPSLRVMLLSLSLNCTSVVCCRVSPLQKAQVTSLVRKGAQKITLSIGDGANDVSMIQAAHVGIGISGMEGMQAVMASDFAIAQFRFLTDLLLVHGRWSYLRICKVVMYFFYKNLTFTLTQFWFTFRTGFSGQRFYDDWFQSLFNVVFTALPVIVLGLFEKDVSASLSKRYPELYREGIRNSFFKWRVVAVWATSAVYQSLVCYLFVTTSSFGAVNSSGKVFGLWDVS,,-1.0,MVRSGSFSVDSSATHQRTPSRTVTLGHIQPQAPTYRTVYCNDRESNQPVRFKGNSISTTKYNVFTFLPKGLFEQFRRIANIYFLGISCLSMTPISPVSPITNVAPLSMVLLVSLIKEAFEDWKRFQNDMSINNSTVEILQDQQWVSIPWRKLQVGDIVKIKKDGFFPADILFMSSTNSDGICYVETANLDGETNLKIRKALERTWDYLVPEKAYEFKGEIQCEQPNNSLYTFTGNLVVQKQTLPLSPDQLLLRGCSLRNTEYIVGAVVFTGHETKVMMNAMNAPSKRSTLEKKLDKLIITIFCVLVTMCLIGAIGCSIVTDREDKYLGLHNSDWEYRNGLMIGFFTFFTLVTLFSSIIPISLYVSIEMIKFIQSTQFINRDLNMYHAETNTPASARTSNLNEELGQVEYIFSAKTGTLTRNLMEFFKCSIGGVSYGCGVTEIEKGIAQRHGLKVQEEQRSTGAIREKGFNFDDPRLMRGAWRNEPNPDLCKELFRCLAICHTVLPEGDESPEKIVYQAASPDEAALVTAAKNFGFFFYRRTPTMVYVRESHVEKMGKIQDVAYEILNVLEFNSTRKRQSVVCRFPDGRLVLYCKGADNVIFERLANGMDDVRKVTREHLEHFGSSGLRTLCLAYKDLNPETYDSWNEKFIQAKSALRDREKKLDEVAELIEKDLILIGSTAIEDKLQEGVPTCIETLSRAGIKIWVLTGDKMETAINIAYACNLINNEMKQFVISSETDAIREAEERGDQVEIARVIKEEVKRELKKSLEEAQHSLHTVAGPKLSLVIDGKCLMYALDPSLRVMLLSLSLNCTSVVCCRVSPLQKAQVTSLVRKGAQKITLSIGDGANDVSMIQAAHVGIGISGMEGMQAVMASDFAIAQFRFLTDLLLVHGRWSYLRICKVVMYFFYKNLTFTLTQFWFTFRTGFSGQRFYDDWFQSLFNVVFTALPVIVLGLFEKDVSASLSKRYPELYREGIRNSFFKWRVVAVWATSAVYQSLVCYLFVTTSSFGAVNSSGKVFGLWDVS,Phospholipid-transporting ATPase 3,"Involved in transport of phospholipids. Contributes to transmembrane flipping of lipids. Required for secretory processes during plant development. Requires an interaction with an ALIS protein for activity. Has activity with phosphatidylserine, phosphatidylcholine and phosphatidylethanolamine, but not with lysolipid. Modifies endomembranes in multiple cell types, enabling structural changes, or signaling functions that are critical for normal development and adaptation to varied growth environments. Required for the trafficking and endocytic recycling of ABCG36/PEN3 between the trans-Golgi network and the plasma membrane; thus promoting ABCG36/PEN3 recruitment to the host-pathogen interface upon infection by powdery mildews (e.g. Blumeria graminis) and bacteria (e.g. Pseudomonas syringae), or upon the detection of pathogen-associated molecular patterns (PAMPs) (e.g. flg22 and chitin).","Increase of internalization of phospholipids. Mutations of ALA3 result in enhanced growth of roots and shoots. The growth defect is accompanied by success of the root cap to release border cells involved in the secretion of molecules required for inefficient root interaction with the environment, and ala3 mutants are filled with the characteristic trans-Golgi proliferation of slime vesicles containing polysaccharides and enzymes for secretion.","Increase of internalization of phospholipids. Mutations of ALA3 result in enhanced growth of roots and shoots. The growth defect is accompanied by success of the root cap to release border cells involved in the secretion of molecules required for inefficient root interaction with the environment, and ala3 mutants are filled with the characteristic trans-Golgi proliferation of slime vesicles containing polysaccharides and enzymes for secretion."
320,0,0,Q9IK90-R258K,MEPDIKSISSESMEGVSDFSPSSWEHGGYLDKVEPEIDENGSMIPKYKIYTPGANERKYNNYMYLICYGFVEDVERTPETGKRKKIRTIAAYPLGVGKSASHPQDLLEELCSLKVTVRRTAGSTEKIVFGSSGPLNHLVPWKKVLTSGSIFNAVKVCRNVDQIQLDKHQALRIFFLSITKLNDSGIYMIPRTMLEFRRNNAIAFNLLVYLKIDADLSKMGIQGSLDKDGFKVASFMLHLGNFVRRAGKYYSVDYCRRKIDRMKLQFSLGSIGGLSLHIKINGVISKRLFAQMGFQKNLCFSLMDINPWLNRLTWNNSCEISRVAAVLQPSIPREFMIYDDVFIDNTGRILKG,,-1.0,MEPDIKSISSESMEGVSDFSPSSWEHGGYLDKVEPEIDENGSMIPKYKIYTPGANERKYNNYMYLICYGFVEDVERTPETGKRKKIRTIAAYPLGVGKSASHPQDLLEELCSLKVTVRRTAGSTEKIVFGSSGPLNHLVPWKKVLTSGSIFNAVKVCRNVDQIQLDKHQALRIFFLSITKLNDSGIYMIPRTMLEFRRNNAIAFNLLVYLKIDADLSKMGIQGSLDKDGFKVASFMLHLGNFVRRAGKYYSVDYCRRRIDRMKLQFSLGSIGGLSLHIKINGVISKRLFAQMGFQKNLCFSLMDINPWLNRLTWNNSCEISRVAAVLQPSIPREFMIYDDVFIDNTGRILKG,Matrix protein,Plays a crucial role in virion assembly and budding. Forms a shell at the inner face of the plasma membrane. Transits through the host nucleus before gaining the functional ability to localize and bud from the plasma membrane. Mediates together with fusion protein the incorporation of the glycoprotein to the viral particles. Participates also in the inhibition of the host interferon type I antiviral response by interacting with and thereby inhibiting host TRIM6.,"Complete gain of membrane association and budding. Mutations at site in the NiV-M protein enhanced its nuclear-cytoplasmic trafficking and enabled NiV-M budding. The lysine residue at this site serves dual functions: its positive charge is unimportant for mediating nuclear import, and it is also a potential site for monoubiquitination which regulates nuclear export of the protein.","Complete gain of membrane association and budding. Mutations at site in the NiV-M protein enhanced its nuclear-cytoplasmic trafficking and enabled NiV-M budding. The lysine residue at this site serves dual functions: its positive charge is unimportant for mediating nuclear import, and it is also a potential site for monoubiquitination which regulates nuclear export of the protein."
321,0,0,P15917-A220D,MNIKKEFIKVISMSCLVTAITLSGPVFIPLVQGAGGHGDVGMHVKEKEKNKDENKRKDEERNKTQEEHLKEIMKHIVKIEVKGEEAVKKEAAEKLLEKVPSDVLEMYKAIGGKIYIVDGDITKHISLEALSEDKKKIKDIYGKDALLHEHYVYAKEGYEPVLVIQSSEDYVENTEKALNVYYEIGKILSRDILSKINQPYQKFLDVLNTIKNASDSDGQDLLFTNQLKEHPTDFSVEFLEQNSNEVQEVFAKAFAYYIEPQHRDVLQLYAPEAFNYMDKFNEQEINLSLEELKDQRMLARYEKWEKIKQHYQHWSDSLSEEGRGLLKKLQIPIEPKKDDIIHSLSQEEKELLKRIQIDSSDFLSTEEKEFLKKLQIDIRDSLSEEEKELLNRIQVDSSNPLSEKEKEFLKKLKLDIQPYDINQRLQDTGGLIDSPSINLDVRKQYKRDIQNIDALLHQSIGSTLYNKIYLYENMNINNLTATLGADLVDSTDNTKINRGIFNEFKKNFKYSISSNYMIVDINERPALDNERLKWRIQLSPDTRAGYLENGKLILQRNIGLEIKDVQIIKQSEKEYIRIDAKVVPKSKIDTKIQEAQLNINQEWNKALGLPKYTKLITFNVHNRYASNIVESAYLILNEWKNNIQSDLIKKVTNYLVDGNGRFVFTDITLPNIAEQYTHQDEIYEQVHSKGLYVPESRSILLHGPSKGVELRNDSEGFIHEFGHAVDDYAGYLLDKNQSDLVTNSKKFIDIFKEEGSNLTSYGRTNEAEFFAEAFRLMHSTDHAERLKVQKNAPKTFQFINDQIKFIINS,,-1.0,MNIKKEFIKVISMSCLVTAITLSGPVFIPLVQGAGGHGDVGMHVKEKEKNKDENKRKDEERNKTQEEHLKEIMKHIVKIEVKGEEAVKKEAAEKLLEKVPSDVLEMYKAIGGKIYIVDGDITKHISLEALSEDKKKIKDIYGKDALLHEHYVYAKEGYEPVLVIQSSEDYVENTEKALNVYYEIGKILSRDILSKINQPYQKFLDVLNTIKNASDSDGQALLFTNQLKEHPTDFSVEFLEQNSNEVQEVFAKAFAYYIEPQHRDVLQLYAPEAFNYMDKFNEQEINLSLEELKDQRMLARYEKWEKIKQHYQHWSDSLSEEGRGLLKKLQIPIEPKKDDIIHSLSQEEKELLKRIQIDSSDFLSTEEKEFLKKLQIDIRDSLSEEEKELLNRIQVDSSNPLSEKEKEFLKKLKLDIQPYDINQRLQDTGGLIDSPSINLDVRKQYKRDIQNIDALLHQSIGSTLYNKIYLYENMNINNLTATLGADLVDSTDNTKINRGIFNEFKKNFKYSISSNYMIVDINERPALDNERLKWRIQLSPDTRAGYLENGKLILQRNIGLEIKDVQIIKQSEKEYIRIDAKVVPKSKIDTKIQEAQLNINQEWNKALGLPKYTKLITFNVHNRYASNIVESAYLILNEWKNNIQSDLIKKVTNYLVDGNGRFVFTDITLPNIAEQYTHQDEIYEQVHSKGLYVPESRSILLHGPSKGVELRNDSEGFIHEFGHAVDDYAGYLLDKNQSDLVTNSKKFIDIFKEEGSNLTSYGRTNEAEFFAEAFRLMHSTDHAERLKVQKNAPKTFQFINDQIKFIINS,Lethal factor,"Lethal factor (LF), which constitutes one of the three proteins composing the anthrax toxin, is able to trigger rapid cell death in macrophages. Acts as a protease that cleaves the N-terminal of most dual specificity mitogen-activated protein kinase kinases (MAPKKs or MAP2Ks) (except for MAP2K5): cleavage invariably occurs within the N-terminal proline-rich region preceding the kinase domain, thus disrupting a sequence involved in directing specific protein-protein interactions necessary for the assembly of signaling complexes. Also cleaves mouse Nlrp1b: host Nlrp1b cleavage promotes ubiquitination and degradation of the N-terminal part of Nlrp1b by the proteasome, thereby releasing the cleaved C-terminal part of Nlrp1b, which polymerizes and forms the Nlrp1b inflammasome followed by host cell pyroptosis. Able to cleave mouse Nlrp1b alleles 1 and 5, while it is not able to cleave Nlrp1b alleles 2, 3 and 4. In contrast, does not cleave NLRP1 human ortholog. LF is not toxic by itself and only acts as a lethal factor when associated with protective antigen (PA) to form the lethal toxin (LeTx): PA is required for LF translocation into the host cytosol.",Gain of ability to bind to PA and gain of toxicity. Mutation in lethal factor is toxic in combination with protective antigen. Its protective antigen-binding ability is significantly increased. D220 is irrelevant for the expression of anthrax lethal toxin activity.,Gain of ability to bind to PA and gain of toxicity. Mutation in lethal factor is toxic in combination with protective antigen. Its protective antigen-binding ability is significantly increased. D220 is irrelevant for the expression of anthrax lethal toxin activity.
322,0,0,P56868-N147E,MKIGIFDSGVGGLTVLKAIRNRYRKVDIVYLGDTARVPYGIRSKDTIIRYSLECAGFLKDKGVDIIVVACNTASAYALERLKKEINVPVFGVIEPGVKEALKKSRNKKIGVIGTPATVKSGAYQRKLEEGGADVFAKACPLFVPLAEEGLLEGEITRKVVEHYLKEFKGKIDTLILGCTHYPLLKKEIKKFLGDVEVVDSSEALSLSLHNFIKDDGSSSLELFFTDLSPNLQFLIKLILGRDYPVKLAEGVFTH,,-1.0,MKIGIFDSGVGGLTVLKAIRNRYRKVDIVYLGDTARVPYGIRSKDTIIRYSLECAGFLKDKGVDIIVVACNTASAYALERLKKEINVPVFGVIEPGVKEALKKSRNKKIGVIGTPATVKSGAYQRKLEEGGADVFAKACPLFVPLANEGLLEGEITRKVVEHYLKEFKGKIDTLILGCTHYPLLKKEIKKFLGDVEVVDSSEALSLSLHNFIKDDGSSSLELFFTDLSPNLQFLIKLILGRDYPVKLAEGVFTH,Glutamate racemase,"Provides the (R)-glutamate required for cell wall biosynthesis. Converts L- or D-glutamate to D- or L-glutamate, respectively, but not other amino acids such as alanine, aspartate, and glutamine.","""Strongly increased inhibition.""","""Strongly increased inhibition."""
323,0,0,P67812-N122D,MLSLDFLDDVRRMNKRQLYYQVLNFGMIVSSALMIWKGLMVITGSESPIVVVLSGSMEPAFHRGDLLFLTNRVEDPIRVGEIVVFRIEGREIPIVHRVLKIHEKQNGHIKFLTKGDNNAVDDRGLYKQGQHWLEKKDVVGRARGFVPYIGIVTILMNDYPKFKYAVLFLLGLFVLVHRE,,-1.0,MLSLDFLDDVRRMNKRQLYYQVLNFGMIVSSALMIWKGLMVITGSESPIVVVLSGSMEPAFHRGDLLFLTNRVEDPIRVGEIVVFRIEGREIPIVHRVLKIHEKQNGHIKFLTKGDNNAVDNRGLYKQGQHWLEKKDVVGRARGFVPYIGIVTILMNDYPKFKYAVLFLLGLFVLVHRE,Signal peptidase complex catalytic subunit SEC11A,Catalytic component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum. Specifically cleaves N-terminal signal peptides that contain a hydrophobic alpha-helix (h-region) shorter than 18-20 amino acids.,Gain of catalytic activity. Slight enhancement in protein stability.,Gain of catalytic activity. Slight enhancement in protein stability.
324,0,0,P05109-A42C,MLTELEKALNSIIDVYHKYSLIKGNFHAVYRDDLKKLLETECPQYIRKKGADVWFKELDINTDGAVNFQEFLILVIKMGVAAHKKSHEESHKE,,-1.0,MLTELEKALNSIIDVYHKYSLIKGNFHAVYRDDLKKLLETEAPQYIRKKGADVWFKELDINTDGAVNFQEFLILVIKMGVAAHKKSHEESHKE,Protein S100-A8,"S100A8 is a calcium- and zinc-binding protein which plays a prominent role in the regulation of inflammatory processes and immune response. It can induce neutrophil chemotaxis and adhesion. Predominantly found as calprotectin (S100A8/A9) which has a wide plethora of intra- and extracellular functions. The intracellular functions include: facilitating leukocyte arachidonic acid trafficking and metabolism, modulation of the tubulin-dependent cytoskeleton during migration of phagocytes and activation of the neutrophilic NADPH-oxidase. Activates NADPH-oxidase by facilitating the enzyme complex assembly at the cell membrane, transferring arachidonic acid, an essential cofactor, to the enzyme complex and S100A8 contributes to the enzyme assembly by directly binding to NCF2/P67PHOX. The extracellular functions involve pro-inflammatory, antimicrobial, oxidant-scavenging and apoptosis-inducing activities. Its pro-inflammatory activity includes recruitment of leukocytes, promotion of cytokine and chemokine production, and regulation of leukocyte adhesion and migration. Acts as an alarmin or a danger associated molecular pattern (DAMP) molecule and stimulates innate immune cells via binding to pattern recognition receptors such as Toll-like receptor 4 (TLR4) and receptor for advanced glycation endproducts (AGER). Binding to TLR4 and AGER activates the MAP-kinase and NF-kappa-B signaling pathways resulting in the amplification of the pro-inflammatory cascade. Has antimicrobial activity towards bacteria and fungi and exerts its antimicrobial activity probably via chelation of Zn(2+) which is essential for microbial growth. Can induce cell death via autophagy and apoptosis and this occurs through the cross-talk of mitochondria and lysosomes via reactive oxygen species (ROS) and the process involves BNIP3. Can regulate neutrophil number and apoptosis by an anti-apoptotic effect; regulates cell survival via ITGAM/ITGB and TLR4 and a signaling mechanism involving MEK-ERK. Its role as an oxidant scavenger has a protective role in preventing exaggerated tissue damage by scavenging oxidants. Can act as a potent amplifier of inflammation in autoimmunity as well as in cancer development and tumor spread. The iNOS-S100A8/A9 transnitrosylase complex directs selective inflammatory stimulus-dependent S-nitrosylation of GAPDH and probably multiple targets such as ANXA5, EZR, MSN and VIM by recognizing a [IL]-x-C-x-x-[DE] motif; S100A8 seems to contribute to S-nitrosylation site selectivity.(Microbial infection) Upon infection by human coronavirus SARS-CoV-2, may induce expansion of aberrant immature neutrophils in a TLR4-dependent manner.",Enhancement of antifungal activity. Substitution of cysteine 42 of S100A8 caused a enhancement of S100A8's ability to enhance S100A9's antifungal effect.,Enhancement of antifungal activity. Substitution of cysteine 42 of S100A8 caused a enhancement of S100A8's ability to enhance S100A9's antifungal effect.
325,0,0,Q6UWV6-E271R,MRGPAVLLTVALATLLAPGAGAPVQSQGSQNKLLLVSFDGFRWNYDQDVDTPNLDAMARDGVKARYMTPAFVTMTSPCHFTLVTGKYIENHGVVHNMYYNTTSKVKLPYHATLGIQRWWDNGSVPIWITAQRQGLRAGSFFYPGGNVTYQGVAVTRSRKEGIAHNYKNETEWRANIDTVMAWFTEEDLDLVTLYFGEPDSTGHRYGPESPERREMVRQVDRTVGYLRESIARNHLTDRLNLIITSDHGMTTVDKRAGDLVEFHKFPNFTFRDIEFELLDYGPNGMLLPKEGRLEKVYDALKDAHPKLHVYKKEAFPEAFHYANNPRVTPLLMYSDLGYVIHGRINVQFNNGEHGFDNKDMDMKTIFRAVGPSFRAGLEVEPFESVHVYELMCRLLGIVPEANDGHLATLLPMLHTESALPPDGRPTLLPKGRSALPPSSRPLLVMGLLGTVILLSEVA,,-1.0,MRGPAVLLTVALATLLAPGAGAPVQSQGSQNKLLLVSFDGFRWNYDQDVDTPNLDAMARDGVKARYMTPAFVTMTSPCHFTLVTGKYIENHGVVHNMYYNTTSKVKLPYHATLGIQRWWDNGSVPIWITAQRQGLRAGSFFYPGGNVTYQGVAVTRSRKEGIAHNYKNETEWRANIDTVMAWFTEEDLDLVTLYFGEPDSTGHRYGPESPERREMVRQVDRTVGYLRESIARNHLTDRLNLIITSDHGMTTVDKRAGDLVEFHKFPNFTFEDIEFELLDYGPNGMLLPKEGRLEKVYDALKDAHPKLHVYKKEAFPEAFHYANNPRVTPLLMYSDLGYVIHGRINVQFNNGEHGFDNKDMDMKTIFRAVGPSFRAGLEVEPFESVHVYELMCRLLGIVPEANDGHLATLLPMLHTESALPPDGRPTLLPKGRSALPPSSRPLLVMGLLGTVILLSEVA,Ectonucleotide pyrophosphatase/phosphodiesterase family member 7,"Choline-specific phosphodiesterase that hydrolyzes sphingomyelin releasing the ceramide and phosphocholine and therefore is involved in sphingomyelin digestion, ceramide formation, and fatty acid (FA) absorption in the gastrointestinal tract. Has also phospholipase C activity and can also cleave phosphocholine from palmitoyl lyso-phosphatidylcholine and platelet-activating factor (PAF) leading to its inactivation. Does not have nucleotide pyrophosphatase activity. May promote cholesterol absorption by affecting the levels of sphingomyelin derived from either diet or endogenous sources, in the intestinal lumen.",Increased enzyme activity; when associated with E-343.,Increased enzyme activity; when associated with E-343.
326,0,0,P21926-A87C,MPVKGGTKCIKYLLFGFNFIFWLAGIAVLAIGLWLRFDSQTKSIFEQETNNNNSSFYTGVYILIGAGALMMLVGFLGCCGAVQESQCMLGLFFGFLLVIFAIEIAAAIWGYSHKDEVIKEVQEFYKDTYNKLKTKDEPQRETLKAIHYALNCCGLAGGVEQFISDICPKKDVLETFTVKSCPDAIKEVFDNKFHIIGAVGIGIAVVMIFGMIFSMILCCAIRRNREMV,,-1.0,MPVKGGTKCIKYLLFGFNFIFWLAGIAVLAIGLWLRFDSQTKSIFEQETNNNNSSFYTGVYILIGAGALMMLVGFLGCCGAVQESQAMLGLFFGFLLVIFAIEIAAAIWGYSHKDEVIKEVQEFYKDTYNKLKTKDEPQRETLKAIHYALNCCGLAGGVEQFISDICPKKDVLETFTVKSCPDAIKEVFDNKFHIIGAVGIGIAVVMIFGMIFSMILCCAIRRNREMV,CD9 antigen,"Integral membrane protein associated with integrins, which regulates different processes, such as sperm-egg fusion, platelet activation and aggregation, and cell adhesion. Present at the cell surface of oocytes and plays a key role in sperm-egg fusion, possibly by organizing multiprotein complexes and the morphology of the membrane required for the fusion. In myoblasts, associates with CD81 and PTGFRN and inhibits myotube fusion during muscle regeneration. In macrophages, associates with CD81 and beta-1 and beta-2 integrins, and prevents macrophage fusion into multinucleated giant cells specialized in ingesting complement-opsonized large particles. Also prevents the fusion between mononuclear cell progenitors into osteoclasts in charge of bone resorption. Acts as a receptor for PSG17. Involved in platelet activation and aggregation. Regulates paranodal junction formation. Involved in cell adhesion, cell motility and tumor metastasis.",Gain of palmitoylation; when associated with A-9; A-78; A-79; A-218 and A-219.,Gain of palmitoylation; when associated with A-9; A-78; A-79; A-218 and A-219.
327,0,0,P16522-D213G,MNDDSQDKIIHDIRIQLRKAATELSRWKLYGSSKWAAEALAGLAEAIDVDQTHSLADESPLRNKQGVPKQMFEIPQNGFGLSETEYDLYLLGSTLFDAKEFDRCVFFLKDVTNPYLKFLKLYSKFLSWDKKSQESMENILTTGKFTDEMYRANKDGDGSGNEDINQSGHQRANLKMVSNEHESQSNISSILKEINTFLESYEIKIDDDEADLGLALLYYLRGVILKQEKNISKAMSSFLKSLSCYSFNWSCWLELMDCLQKVDDALLLNNYLYQNFQFKFSENLGSQRTIEFNIMIKFFKLKVFEELNGQLEDYFEDLEFLLQVFPNFTFLKAYNATISYNNLDYVTAESRFDDIVKQDPYRLNDLETYSNILYVMQKNSKLAYLAQFVSQIDRFRPETCCIIANYYSARQEHEKSIMYFRRALTLDKKTTNAWTLMGHEFVELSNSHAAIECYRRAVDICPRDFKAWFGLGQAYALLDMHLYSLYYFQKACTLKPWDRRIWQVLGECYSKTGNKVEAIKCYKRSIKASQTVDQNTSIYYRLAQLYEELEDLQECKKFMMKCVDVEELLEGIVTDETVKARLWLAIFEIKAGNYQLAYDYAMGVSSGTSQEIEEARMLARECRRHM,,-1.0,MNDDSQDKIIHDIRIQLRKAATELSRWKLYGSSKWAAEALAGLAEAIDVDQTHSLADESPLRNKQGVPKQMFEIPQNGFGLSETEYDLYLLGSTLFDAKEFDRCVFFLKDVTNPYLKFLKLYSKFLSWDKKSQESMENILTTGKFTDEMYRANKDGDGSGNEDINQSGHQRANLKMVSNEHESQSNISSILKEINTFLESYEIKIDDDEADLDLALLYYLRGVILKQEKNISKAMSSFLKSLSCYSFNWSCWLELMDCLQKVDDALLLNNYLYQNFQFKFSENLGSQRTIEFNIMIKFFKLKVFEELNGQLEDYFEDLEFLLQVFPNFTFLKAYNATISYNNLDYVTAESRFDDIVKQDPYRLNDLETYSNILYVMQKNSKLAYLAQFVSQIDRFRPETCCIIANYYSARQEHEKSIMYFRRALTLDKKTTNAWTLMGHEFVELSNSHAAIECYRRAVDICPRDFKAWFGLGQAYALLDMHLYSLYYFQKACTLKPWDRRIWQVLGECYSKTGNKVEAIKCYKRSIKASQTVDQNTSIYYRLAQLYEELEDLQECKKFMMKCVDVEELLEGIVTDETVKARLWLAIFEIKAGNYQLAYDYAMGVSSGTSQEIEEARMLARECRRHM,Anaphase-promoting complex subunit CDC23,"Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. In early mitosis, the APC/C is activated by CDC20 and targets securin PDS1, the B-type cyclin CLB5, and other anaphase inhibitory proteins for proteolysis, thereby triggering the separation of sister chromatids at the metaphase-to-anaphase transition. In late mitosis and in G1, degradation of CLB5 allows activation of the APC/C by CDH1, which is needed to destroy CDC20 and the B-type cyclin CLB2 to allow exit from mitosis and creating the low CDK state necessary for cytokinesis and for reforming prereplicative complexes in G1 prior to another round of replication.",Increases CDC23-47; G2/M cell cycle arrest at 37 degrees Celsius; when associated with W-583. The mutation in the CDC23 gene causes a single amino acid change in the protein. This mutation is found within a mutable domain of CDC23 and may affect its function or stability.,Increases CDC23-47; G2/M cell cycle arrest at 37 degrees Celsius; when associated with W-583. The mutation in the CDC23 gene causes a single amino acid change in the protein. This mutation is found within a mutable domain of CDC23 and may affect its function or stability.
328,0,0,Q07181-E269K,MVRNIVSRLCSQLFALPSSSLQERDPCSVTEYSGLATAVSSCKNIVLNGFQVPTGKQLDLSSLQNDSTVTFKGTTTFATTADNDFNPIVISGSNITITGASGHVIDGNGQAYWDGKGSNSNSNQKPDHFIVVQKTTGNSKITNLNIQNWPVHCFDITGSSQLTISGLILDNRAGDKPNAKSGSLPAAHNTDGFDISSSDHVTLDNNHVYNQDDCVAVTSGTNIVVSNMYCSGGHGLSIGSVGGKSDNVVDGVQFLSSQVVNSQNGCRIKSNSGATGTINNVTYQNIALTNISTYGVDVQQDYLNGGPTGKPTNGVKISNIKFIKVTGTVASSAQDWFILCGDGSCSGFTFSGNAITGGGKTSSCNYPTNTCPS,,-1.0,MVRNIVSRLCSQLFALPSSSLQERDPCSVTEYSGLATAVSSCKNIVLNGFQVPTGKQLDLSSLQNDSTVTFKGTTTFATTADNDFNPIVISGSNITITGASGHVIDGNGQAYWDGKGSNSNSNQKPDHFIVVQKTTGNSKITNLNIQNWPVHCFDITGSSQLTISGLILDNRAGDKPNAKSGSLPAAHNTDGFDISSSDHVTLDNNHVYNQDDCVAVTSGTNIVVSNMYCSGGHGLSIGSVGGKSDNVVDGVQFLSSQVVNSQNGCRIESNSGATGTINNVTYQNIALTNISTYGVDVQQDYLNGGPTGKPTNGVKISNIKFIKVTGTVASSAQDWFILCGDGSCSGFTFSGNAITGGGKTSSCNYPTNTCPS,Polygalacturonase,"Involved in maceration and soft-rotting of plant tissue. Hydrolyzes the 1,4-alpha glycosidic bonds of de-esterified pectate in the smooth region of the plant cell wall.",Increases activity by 99.87%. Raises affinity for substrate over 10-fold. The mutation of K-269 to E promotes the formation of the complex with PGIP-2.,Increases activity by 99.87%. Raises affinity for substrate over 10-fold. The mutation of K-269 to E promotes the formation of the complex with PGIP-2.
329,0,0,P25522-A251T,MSDNDTIVAQATPPGRGGVGILRISGFKAREVAETVLGKLPKPRYADYLPFKDADGSVLDQGIALWFPGPNSFTGEDVLELQGHGGPVILDLLLKRILTIPGLRIARPGEFSERAFLNDKLDLAQAEAIADLIDASSEQAARSALNSLQGAFSARVNHLVEALTHLRIYVEAAIDFPDEEIDFLSDGKIEAQLNDVIADLDAVRAEARQGSLLREGMKVVIAGRPNAGKSSLLNALAGREAAIVTDIAGTTRDVLREHIHIDGMPLHIIDTAGLREASDEVERIGIERAWQEIEQADRVLFMVDGTTTDAVDPAEIWPEFIARLPAKLPITVVRNKADITGETLGMSEVNGHALIRLSARTGEGVDVLRNHLKQSMGFDTNMEGGFLARRRHLQALEQAAEHLQQGKAQLLGAWAGELLAEELRLAQQNLSEITGEFTSDDLLGRIFSSFCIGK,,-1.0,MSDNDTIVAQATPPGRGGVGILRISGFKAREVAETVLGKLPKPRYADYLPFKDADGSVLDQGIALWFPGPNSFTGEDVLELQGHGGPVILDLLLKRILTIPGLRIARPGEFSERAFLNDKLDLAQAEAIADLIDASSEQAARSALNSLQGAFSARVNHLVEALTHLRIYVEAAIDFPDEEIDFLSDGKIEAQLNDVIADLDAVRAEARQGSLLREGMKVVIAGRPNAGKSSLLNALAGREAAIVTDIAGTARDVLREHIHIDGMPLHIIDTAGLREASDEVERIGIERAWQEIEQADRVLFMVDGTTTDAVDPAEIWPEFIARLPAKLPITVVRNKADITGETLGMSEVNGHALIRLSARTGEGVDVLRNHLKQSMGFDTNMEGGFLARRRHLQALEQAAEHLQQGKAQLLGAWAGELLAEELRLAQQNLSEITGEFTSDDLLGRIFSSFCIGK,tRNA modification GTPase MnmE,"Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.",59-fold increase in GTPase activity and 92-fold decrease of affinity. The invariant threonine (T251) of the G2 motif would be non-essential for the conformational change of the switch I region associated with GTP hydrolysis.,59-fold increase in GTPase activity and 92-fold decrease of affinity. The invariant threonine (T251) of the G2 motif would be non-essential for the conformational change of the switch I region associated with GTP hydrolysis.
330,0,0,O14746-D682G,MPRAPRCRAVRSLLRSHYREVLPLATFVRRLGPQGWRLVQRGDPAAFRALVAQCLVCVPWDARPPPAAPSFRQVSCLKELVARVLQRLCERGAKNVLAFGFALLDGARGGPPEAFTTSVRSYLPNTVTDALRGSGAWGLLLRRVGDDVLVHLLARCALFVLVAPSCAYQVCGPPLYQLGAATQARPPPHASGPRRRLGCERAWNHSVREAGVPLGLPAPGARRRGGSASRSLPLPKRPRRGAAPEPERTPVGQGSWAHPGRTRGPSDRGFCVVSPARPAEEATSLEGALSGTRHSHPSVGRQHHAGPPSTSRPPRPWDTPCPPVYAETKHFLYSSGDKEQLRPSFLLSSLRPSLTGARRLVETIFLGSRPWMPGTPRRLPRLPQRYWQMRPLFLELLGNHAQCPYGVLLKTHCPLRAAVTPAAGVCAREKPQGSVAAPEEEDTDPRRLVQLLRQHSSPWQVYGFVRACLRRLVPPGLWGSRHNERRFLRNTKKFISLGKHAKLSLQELTWKMSVRDCAWLRRSPGVGCVPAAEHRLREEILAKFLHWLMSVYVVELLRSFFYVTETTFQKNRLFFYRKSVWSKLQSIGIRQHLKRVQLRELSEAEVRQHREARPALLTSRLRFIPKPDGLRPIVNMDYVVGARTFRREKRAERLTSRVKALFSVLNYERARRPGLLGASVLGLDDIHRAWRTFVLRVRAQDPPPELYFVKVDVTGAYDTIPQDRLTEVIASIIKPQNTYCVRRYAVVQKAAHGHVRKAFKSHVSTLTDLQPYMRQFVAHLQETSPLRDAVVIEQSSSLNEASSGLFDVFLRFMCHHAVRIRGKSYVQCQGIPQGSILSTLLCSLCYGDMENKLFAGIRRDGLLLRLVDDFLLVTPHLTHAKTFLRTLVRGVPEYGCVVNLRKTVVNFPVEDEALGGTAFVQMPAHGLFPWCGLLLDTRTLEVQSDYSSYARTSIRASLTFNRGFKAGRNMRRKLFGVLRLKCHSLFLDLQVNSLQTVCTNIYKILLLQAYRFHACVLQLPFHQQ,,-1.0,MPRAPRCRAVRSLLRSHYREVLPLATFVRRLGPQGWRLVQRGDPAAFRALVAQCLVCVPWDARPPPAAPSFRQVSCLKELVARVLQRLCERGAKNVLAFGFALLDGARGGPPEAFTTSVRSYLPNTVTDALRGSGAWGLLLRRVGDDVLVHLLARCALFVLVAPSCAYQVCGPPLYQLGAATQARPPPHASGPRRRLGCERAWNHSVREAGVPLGLPAPGARRRGGSASRSLPLPKRPRRGAAPEPERTPVGQGSWAHPGRTRGPSDRGFCVVSPARPAEEATSLEGALSGTRHSHPSVGRQHHAGPPSTSRPPRPWDTPCPPVYAETKHFLYSSGDKEQLRPSFLLSSLRPSLTGARRLVETIFLGSRPWMPGTPRRLPRLPQRYWQMRPLFLELLGNHAQCPYGVLLKTHCPLRAAVTPAAGVCAREKPQGSVAAPEEEDTDPRRLVQLLRQHSSPWQVYGFVRACLRRLVPPGLWGSRHNERRFLRNTKKFISLGKHAKLSLQELTWKMSVRDCAWLRRSPGVGCVPAAEHRLREEILAKFLHWLMSVYVVELLRSFFYVTETTFQKNRLFFYRKSVWSKLQSIGIRQHLKRVQLRELSEAEVRQHREARPALLTSRLRFIPKPDGLRPIVNMDYVVGARTFRREKRAERLTSRVKALFSVLNYERARRPGLLGASVLDLDDIHRAWRTFVLRVRAQDPPPELYFVKVDVTGAYDTIPQDRLTEVIASIIKPQNTYCVRRYAVVQKAAHGHVRKAFKSHVSTLTDLQPYMRQFVAHLQETSPLRDAVVIEQSSSLNEASSGLFDVFLRFMCHHAVRIRGKSYVQCQGIPQGSILSTLLCSLCYGDMENKLFAGIRRDGLLLRLVDDFLLVTPHLTHAKTFLRTLVRGVPEYGCVVNLRKTVVNFPVEDEALGGTAFVQMPAHGLFPWCGLLLDTRTLEVQSDYSSYARTSIRASLTFNRGFKAGRNMRRKLFGVLRLKCHSLFLDLQVNSLQTVCTNIYKILLLQAYRFHACVLQLPFHQQ,Telomerase reverse transcriptase,"Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. Active in progenitor and cancer cells. Inactive, or very low activity, in normal somatic cells. Catalytic component of the teleromerase holoenzyme complex whose main activity is the elongation of telomeres by acting as a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme. Catalyzes the RNA-dependent extension of 3'-chromosomal termini with the 6-nucleotide telomeric repeat unit, 5'-TTAGGG-3'. The catalytic cycle involves primer binding, primer extension and release of product once the template boundary has been reached or nascent product translocation followed by further extension. More active on substrates containing 2 or 3 telomeric repeats. Telomerase activity is regulated by a number of factors including telomerase complex-associated proteins, chaperones and polypeptide modifiers. Modulates Wnt signaling. Plays important roles in aging and antiapoptosis.","Abolishes telomerase catalytic activity but little effect on binding to TERC in AA; non-severe. Novel heterozygous, non-synonymous mutation in TERT () was found in two patients with acquired aplastic anemia (AA).","Abolishes telomerase catalytic activity but little effect on binding to TERC in AA; non-severe. Novel heterozygous, non-synonymous mutation in TERT () was found in two patients with acquired aplastic anemia (AA)."
331,0,0,Q9UJ83-R455D,MPDSNFAERSEEQVSGAKVIAQALKTQDVEYIFGIVGIPVTEIAIAAQQLGIKYIGMRNEQAACYAASAIGYLTSRPGVCLVVSGPGLIHALGGMANANMNCWPLLVIGGSSERNQETMGAFQEFPQVEACRLYTKFSARPSSIEAIPFVIEKAVRSSIYGRPGACYVDIPADFVNLQVNVNSIKYMERCMSPPISMAETSAVCTAASVIRNAKQPLLIIGKGAAYAHAEESIKKLVEQYKLPFLPTPMGKGVVPDNHPYCVGAARSRALQFADVIVLFGARLNWILHFGLPPRYQPDVKFIQVDICAEELGNNVKPAVTLLGNIHAVTKQLLEELDKTPWQYPPESKWWKTLREKMKSNEAASKELASKKSLPMNYYTVFYHVQEQLPRDCFVVSEGANTMDIGRTVLQNYLPRHRLDAGTFGTMGVGLGFAIAAAVVAKDRSPGQWIICVEGDSAFGFSGMEVETICRYNLPIILLVVNNNGIYQGFDTDTWKEMLKFQDATAVVPPMCLLPNSHYEQVMTAFGGKGYFVQTPEELQKSLRQSLADTTKPSLINIMIEPQATRKAQDFHWLTRSNM,,-1.0,MPDSNFAERSEEQVSGAKVIAQALKTQDVEYIFGIVGIPVTEIAIAAQQLGIKYIGMRNEQAACYAASAIGYLTSRPGVCLVVSGPGLIHALGGMANANMNCWPLLVIGGSSERNQETMGAFQEFPQVEACRLYTKFSARPSSIEAIPFVIEKAVRSSIYGRPGACYVDIPADFVNLQVNVNSIKYMERCMSPPISMAETSAVCTAASVIRNAKQPLLIIGKGAAYAHAEESIKKLVEQYKLPFLPTPMGKGVVPDNHPYCVGAARSRALQFADVIVLFGARLNWILHFGLPPRYQPDVKFIQVDICAEELGNNVKPAVTLLGNIHAVTKQLLEELDKTPWQYPPESKWWKTLREKMKSNEAASKELASKKSLPMNYYTVFYHVQEQLPRDCFVVSEGANTMDIGRTVLQNYLPRHRLDAGTFGTMGVGLGFAIAAAVVAKDRSPGQWIICVEGRSAFGFSGMEVETICRYNLPIILLVVNNNGIYQGFDTDTWKEMLKFQDATAVVPPMCLLPNSHYEQVMTAFGGKGYFVQTPEELQKSLRQSLADTTKPSLINIMIEPQATRKAQDFHWLTRSNM,2-hydroxyacyl-CoA lyase 1,Peroxisomal 2-OH acyl-CoA lyase involved in the cleavage (C1 removal) reaction in the fatty acid alpha-oxydation in a thiamine pyrophosphate (TPP)-dependent manner. Involved in the degradation of 3-methyl-branched fatty acids like phytanic acid and the shortening of 2-hydroxy long-chain fatty acids. Plays a significant role in the biosynthesis of heptadecanal in the liver.,"Increases subcellular localization. Enhances lyase activity. Increases subcellular localization, enhances lyase activity, increases oligomerization, and binds TTP; when associated with S-456. The mutation in the TPP-binding domain of HACL1 enhances enzyme activity.","Increases subcellular localization. Enhances lyase activity. Increases subcellular localization, enhances lyase activity, increases oligomerization, and binds TTP; when associated with S-456. The mutation in the TPP-binding domain of HACL1 enhances enzyme activity."
332,0,0,P25522-A250T,MSDNDTIVAQATPPGRGGVGILRISGFKAREVAETVLGKLPKPRYADYLPFKDADGSVLDQGIALWFPGPNSFTGEDVLELQGHGGPVILDLLLKRILTIPGLRIARPGEFSERAFLNDKLDLAQAEAIADLIDASSEQAARSALNSLQGAFSARVNHLVEALTHLRIYVEAAIDFPDEEIDFLSDGKIEAQLNDVIADLDAVRAEARQGSLLREGMKVVIAGRPNAGKSSLLNALAGREAAIVTDIAGTTRDVLREHIHIDGMPLHIIDTAGLREASDEVERIGIERAWQEIEQADRVLFMVDGTTTDAVDPAEIWPEFIARLPAKLPITVVRNKADITGETLGMSEVNGHALIRLSARTGEGVDVLRNHLKQSMGFDTNMEGGFLARRRHLQALEQAAEHLQQGKAQLLGAWAGELLAEELRLAQQNLSEITGEFTSDDLLGRIFSSFCIGK,,-1.0,MSDNDTIVAQATPPGRGGVGILRISGFKAREVAETVLGKLPKPRYADYLPFKDADGSVLDQGIALWFPGPNSFTGEDVLELQGHGGPVILDLLLKRILTIPGLRIARPGEFSERAFLNDKLDLAQAEAIADLIDASSEQAARSALNSLQGAFSARVNHLVEALTHLRIYVEAAIDFPDEEIDFLSDGKIEAQLNDVIADLDAVRAEARQGSLLREGMKVVIAGRPNAGKSSLLNALAGREAAIVTDIAGATRDVLREHIHIDGMPLHIIDTAGLREASDEVERIGIERAWQEIEQADRVLFMVDGTTTDAVDPAEIWPEFIARLPAKLPITVVRNKADITGETLGMSEVNGHALIRLSARTGEGVDVLRNHLKQSMGFDTNMEGGFLARRRHLQALEQAAEHLQQGKAQLLGAWAGELLAEELRLAQQNLSEITGEFTSDDLLGRIFSSFCIGK,tRNA modification GTPase MnmE,"Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.",4-fold increase in GTPase activity and 1.5-fold decrease of affinity.,4-fold increase in GTPase activity and 1.5-fold decrease of affinity.
333,0,0,Q9I4E3-F162H,MFKHIIARTPARSLVDGLTSSHLGKPDYAKALEQHNAYIRALQTCDVDITLLPPDERFPDSVFVEDPVLCTSRCAIITRPGAESRRGETEIIEETVQRFYPGKVERIEAPGTVEAGDIMMVGDHFYIGESARTNAEGARQMIAILEKHGLSGSVVRLEKVLHLKTGLAYLEHNNLLAAGEFVSKPEFQDFNIIEIPEEESYAANCIWVNERVIMPAGYPRTREKIARLGYRVIEVDTSEYRKIDGGVSCMSLRF,,-1.0,MFKHIIARTPARSLVDGLTSSHLGKPDYAKALEQHNAYIRALQTCDVDITLLPPDERFPDSVFVEDPVLCTSRCAIITRPGAESRRGETEIIEETVQRFYPGKVERIEAPGTVEAGDIMMVGDHFYIGESARTNAEGARQMIAILEKHGLSGSVVRLEKVLFLKTGLAYLEHNNLLAAGEFVSKPEFQDFNIIEIPEEESYAANCIWVNERVIMPAGYPRTREKIARLGYRVIEVDTSEYRKIDGGVSCMSLRF,N,"Hydrolyzes N(G),N(G)-dimethyl-L-arginine (ADMA) and N(G)-monomethyl-L-arginine (MMA).",Enables enzyme activity.,Enables enzyme activity.
334,0,0,B9EJA2-A599P,MATDSASCEPDLSRTPGDTEGATAEAAKKEFDVDTLSKSELRMLLSVMEGELEARDLVIEALRARRKEVFIQERYGRFNLNDPFLALQRDYEAGPGDKEKPVCTNPLSILEAVMAHCRKMQERMSAQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKNKHVVLMLVKECKQLSGKVVEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEIDKMKKMMEQMKKGSDGKPGLSLPRKTKDKRLASISVATEGPVTRSVACQTDVVTESTDPVKKLPLTVPIKPSTGSPLVPTNTKGNVGPSALLIRPGIDRQSSHSDLGPSPPTALPSSANRIEENGPSTGNAPDLSNSTPSTPSSTAPAAAQTPGTAPQNHSQAPTVHSLHSPCANTHPGLNPRIQAARFRFQGNANDPDQNGNNTQSPPSRDVSPTSRDNLVAKQLARNTVTQALSRFTSPQAGASSRLGVSPGGDAGTCPPVGRTGLKTPGAARVDRGNPPPIPPKKPGLSQTPSPPHPQLRASNAGAKVDNKIVASPPSTLPQGTKVVNEENVPKSSSPQLPPKPSIDLTVAPAGCPVSALATSQVGAWPAGTPGLNQPACSDSSLVIPATVAFCSSINPVSASSRSPGASDSLLVAASGWSPSLTPLLMSGGPAPLAGRPTLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFECIELLTAYNANINHSAAGGQTPLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVDSLKLLMYHRVRAHGNSLSSEEPKSGLFSLNGGESPTGPSKPVVPADLINHADKEGWTAAHIAASKGFKNCLEVLCRHGGLEPERRDKCNRTVHDVATDDCKHLLENLNALKIPLRISVGEIQPSNDVSDDFECEHTICTLNIRKQTSWEDFSKAVSQALTNHFQAISSDGWWSLEDG,,-1.0,MATDSASCEPDLSRTPGDTEGATAEAAKKEFDVDTLSKSELRMLLSVMEGELEARDLVIEALRARRKEVFIQERYGRFNLNDPFLALQRDYEAGPGDKEKPVCTNPLSILEAVMAHCRKMQERMSAQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKNKHVVLMLVKECKQLSGKVVEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEIDKMKKMMEQMKKGSDGKPGLSLPRKTKDKRLASISVATEGPVTRSVACQTDVVTESTDPVKKLPLTVPIKPSTGSPLVPTNTKGNVGPSALLIRPGIDRQSSHSDLGPSPPTALPSSANRIEENGPSTGNAPDLSNSTPSTPSSTAPAAAQTPGTAPQNHSQAPTVHSLHSPCANTHPGLNPRIQAARFRFQGNANDPDQNGNNTQSPPSRDVSPTSRDNLVAKQLARNTVTQALSRFTSPQAGASSRLGVSPGGDAGTCPPVGRTGLKTPGAARVDRGNPPPIPPKKPGLSQTPSPPHPQLRASNAGAKVDNKIVASPPSTLPQGTKVVNEENVPKSSSAQLPPKPSIDLTVAPAGCPVSALATSQVGAWPAGTPGLNQPACSDSSLVIPATVAFCSSINPVSASSRSPGASDSLLVAASGWSPSLTPLLMSGGPAPLAGRPTLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFECIELLTAYNANINHSAAGGQTPLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVDSLKLLMYHRVRAHGNSLSSEEPKSGLFSLNGGESPTGPSKPVVPADLINHADKEGWTAAHIAASKGFKNCLEVLCRHGGLEPERRDKCNRTVHDVATDDCKHLLENLNALKIPLRISVGEIQPSNDVSDDFECEHTICTLNIRKQTSWEDFSKAVSQALTNHFQAISSDGWWSLEDG,Cortactin-binding protein 2,"Regulates the dendritic spine distribution of CTTN/cortactin in hippocampal neurons, and thus controls dendritic spinogenesis and dendritic spine maintenance.",Increased CTTN-binding; when associated with A-602.,Increased CTTN-binding; when associated with A-602.
335,0,0,Q96RL7-K90I,MVFESVVVDVLNRFLGDYVVDLDTSQLSLGIWKGAVALKNLQIKENALSQLDVPFKVKVGHIGNLKLIIPWKNLYTQPVEAVLEEIYLLIVPSSRIKYDPLKEEKQLMEAKQQELKRIEEAKQKVVDQEQHLPEKQDTFAEKLVTQIIKNLQVKISSIHIRYEDDITNRDKPLSFGISLQNLSMQTTDQYWVPCLHDETEKLVRKLIRLDNLFAYWNVKSQMFYLSDYDNSLDDLKNGIVNENIVPEGYDFVFRPISANAKLVMNRRSDFDFSAPKINLEIELHNIAIEFNKPQYFSIMELLESVDMMAQNLPYRKFKPDVPLHHHAREWWAYAIHGVLEVNVCPRLWMWSWKHIRKHRQKVKQYKELYKKKLTSKKPPGELLVSLEELEKTLDVFNITIARQTAEVEVKKAGYKIYKEGVKDPEDNKGWFSWLWSWSEQNTNEQQPDVQPETLEEMLTPEEKALLYEAIGYSETAVDPTLLKTFEALKFFVHLKSMSIVLRENHQKPELVDIVIEEFSTLIVQRPGAQAIKFETKIDSFHITGLPDNSEKPRLLSSLDDAMSLFQITFEINPLDETVSQRCIIEAEPLEIIYDARTVNSIVEFFRPPKEVHLAQLTAATLTKLEEFRSKTATGLLYIIETQKVLDLKINLKASYIIVPQDGIFSPTSNLLLLDLGHLKVTSKSRSELPDVKQGEANLKEIMDRAYDSFDIQLTSVQLLYSRVGDNWREARKLSVSTQHILVPMHFNLELSKAMVFMDVRMPKFKIYGKLPLISLRISDKKLQGIMELIESIPKPEPVTEVSAPVKSFQIQTSTSLGTSQISQKIIPLLELPSVSEDDSEEEFFDAPCSPLEEPLQFPTGVKSIRTRKLQKQDCSVNMTTFKIRFEVPKVLIEFYHLVGDCELSVVEILVLGLGAEIEIRTYDLKANAFLKEFCLKCPEYLDENKKPVYLVTTLDNTMEDLLTLEYVKAEKNVPDLKSTYNNVLQLIKVNFSSLDIHLHTEALLNTINYLHNILPQSEEKSAPV,,-1.0,MVFESVVVDVLNRFLGDYVVDLDTSQLSLGIWKGAVALKNLQIKENALSQLDVPFKVKVGHIGNLKLIIPWKNLYTQPVEAVLEEIYLLKVPSSRIKYDPLKEEKQLMEAKQQELKRIEEAKQKVVDQEQHLPEKQDTFAEKLVTQIIKNLQVKISSIHIRYEDDITNRDKPLSFGISLQNLSMQTTDQYWVPCLHDETEKLVRKLIRLDNLFAYWNVKSQMFYLSDYDNSLDDLKNGIVNENIVPEGYDFVFRPISANAKLVMNRRSDFDFSAPKINLEIELHNIAIEFNKPQYFSIMELLESVDMMAQNLPYRKFKPDVPLHHHAREWWAYAIHGVLEVNVCPRLWMWSWKHIRKHRQKVKQYKELYKKKLTSKKPPGELLVSLEELEKTLDVFNITIARQTAEVEVKKAGYKIYKEGVKDPEDNKGWFSWLWSWSEQNTNEQQPDVQPETLEEMLTPEEKALLYEAIGYSETAVDPTLLKTFEALKFFVHLKSMSIVLRENHQKPELVDIVIEEFSTLIVQRPGAQAIKFETKIDSFHITGLPDNSEKPRLLSSLDDAMSLFQITFEINPLDETVSQRCIIEAEPLEIIYDARTVNSIVEFFRPPKEVHLAQLTAATLTKLEEFRSKTATGLLYIIETQKVLDLKINLKASYIIVPQDGIFSPTSNLLLLDLGHLKVTSKSRSELPDVKQGEANLKEIMDRAYDSFDIQLTSVQLLYSRVGDNWREARKLSVSTQHILVPMHFNLELSKAMVFMDVRMPKFKIYGKLPLISLRISDKKLQGIMELIESIPKPEPVTEVSAPVKSFQIQTSTSLGTSQISQKIIPLLELPSVSEDDSEEEFFDAPCSPLEEPLQFPTGVKSIRTRKLQKQDCSVNMTTFKIRFEVPKVLIEFYHLVGDCELSVVEILVLGLGAEIEIRTYDLKANAFLKEFCLKCPEYLDENKKPVYLVTTLDNTMEDLLTLEYVKAEKNVPDLKSTYNNVLQLIKVNFSSLDIHLHTEALLNTINYLHNILPQSEEKSAPV,Intermembrane lipid transfer protein VPS13A,Mediates the transfer of lipids between membranes at organelle contact sites. Binds phospholipids. Required for the formation or stabilization of ER-mitochondria contact sites which enable transfer of lipids between the ER and mitochondria. Negatively regulates lipid droplet size and motility. Required for efficient lysosomal protein degradation.,Changes subcellular localization with protein XK away from lipid droplets. The mutation in the CHAC gene leads to a non-functional change in the encoded protein.,Changes subcellular localization with protein XK away from lipid droplets. The mutation in the CHAC gene leads to a non-functional change in the encoded protein.
336,0,0,Q96AX1-D438Y,MAAHLSYGRVNLNVLREAVRRELREFLDKCAGSKAIVWDEYLTGPFGLIAQYSLLKEHEVEKMFTLKGNRLPAADVKNIIFFVRPRLELMDIIAENVLSEDRRGPTRDFHILFVPRRSLLCEQRLKDLGVLGSFIHREEYSLDLIPFDGDLLSMESEGAFKECYLEGDQTSLYHAAKGLMTLQALYGTIPQIFGKGECARQVANMMIRMKREFTGSQNSIFPVFDNLLLLDRNVDLLTPLATQLTYEGLIDEIYGIQNSYVKLPPEKFAPKKQGDGGKDLPTEAKKLQLNSAEELYAEIRDKNFNAVGSVLSKKAKIISAAFEERHNAKTVGEIKQFVSQLPHMQAARGSLANHTSIAELIKDVTTSEDFFDKLTVEQEFMSGIDTDKVNNYIEDCIAQKHSLIKVLRLVCLQSVCNSGLKQKVLDYYKREILQTYGYEHILTLHNLEKAGLLKPQTGGRNNYPTIRKTLRLWMDDVNEQNPTDISYVYSGYAPLSVRLAQLLSRPGWRSIEEVLRILPGPHFEERQPLPTGLQKKRQPGENRVTLIFFLGGVTFAEIAALRFLSQLEDGGTEYVIATTKLMNGTSWIEALMEKPF,,-1.0,MAAHLSYGRVNLNVLREAVRRELREFLDKCAGSKAIVWDEYLTGPFGLIAQYSLLKEHEVEKMFTLKGNRLPAADVKNIIFFVRPRLELMDIIAENVLSEDRRGPTRDFHILFVPRRSLLCEQRLKDLGVLGSFIHREEYSLDLIPFDGDLLSMESEGAFKECYLEGDQTSLYHAAKGLMTLQALYGTIPQIFGKGECARQVANMMIRMKREFTGSQNSIFPVFDNLLLLDRNVDLLTPLATQLTYEGLIDEIYGIQNSYVKLPPEKFAPKKQGDGGKDLPTEAKKLQLNSAEELYAEIRDKNFNAVGSVLSKKAKIISAAFEERHNAKTVGEIKQFVSQLPHMQAARGSLANHTSIAELIKDVTTSEDFFDKLTVEQEFMSGIDTDKVNNYIEDCIAQKHSLIKVLRLVCLQSVCNSGLKQKVLDYYKREILQTYGDEHILTLHNLEKAGLLKPQTGGRNNYPTIRKTLRLWMDDVNEQNPTDISYVYSGYAPLSVRLAQLLSRPGWRSIEEVLRILPGPHFEERQPLPTGLQKKRQPGENRVTLIFFLGGVTFAEIAALRFLSQLEDGGTEYVIATTKLMNGTSWIEALMEKPF,Vacuolar protein sorting-associated protein 33A,"Plays a role in vesicle-mediated protein trafficking to lysosomal compartments including the endocytic membrane transport and autophagic pathways. Believed to act as a core component of the putative HOPS and CORVET endosomal tethering complexes which are proposed to be involved in the Rab5-to-Rab7 endosome conversion probably implicating MON1A/B, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion. The HOPS complex is proposed to be recruited to Rab7 on the late endosomal membrane and to regulate late endocytic, phagocytic and autophagic traffic towards lysosomes. The CORVET complex is proposed to function as a Rab5 effector to mediate early endosome fusion probably in specific endosome subpopulations. Required for fusion of endosomes and autophagosomes with lysosomes; the function is dependent on its association with VPS16 but not VIPAS39. The function in autophagosome-lysosome fusion implicates STX17 but not UVRAG.",Increases interaction with VPS16. Increases interaction with VPS18 and enhances endosome-lysosome fusion; when associated with D-429. Increases interaction with VPS18 and enhances endosome-lysosome fusion; when associated with K-441. The mutation in VPS16 rescues lysosome fusion with endosomes or autophagosomes in cells depleted of the endogenous proteins.,Increases interaction with VPS16. Increases interaction with VPS18 and enhances endosome-lysosome fusion; when associated with D-429. Increases interaction with VPS18 and enhances endosome-lysosome fusion; when associated with K-441. The mutation in VPS16 rescues lysosome fusion with endosomes or autophagosomes in cells depleted of the endogenous proteins.
337,0,0,Q9VF27-D199G,MSLTMRIFTASRNGQRLFGSHGARLLAAQRAEPKDIVEVPKGYVYVNNKELSMEFADITDRAASTMFFGELLRGFAVTLAHIFKEPATINYPFEKGPLSPRFRGEHALRRYPSGEERCIACKLCEAICPAQAITIEAEERADGSRRTTRYDIDMTKCIYCGFCQEACPVDAIVEGPNFEFSTETHEELLYNKEKLLCNGDKWESEIASNLQADHLYR,,-1.0,MSLTMRIFTASRNGQRLFGSHGARLLAAQRAEPKDIVEVPKGYVYVNNKELSMEFADITDRAASTMFFGELLRGFAVTLAHIFKEPATINYPFEKGPLSPRFRGEHALRRYPSGEERCIACKLCEAICPAQAITIEAEERADGSRRTTRYDIDMTKCIYCGFCQEACPVDAIVEGPNFEFSTETHEELLYNKEKLLCNDDKWESEIASNLQADHLYR,NADH dehydrogenase,Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.,"Enhances mitochondrial function and results in normal-sized mitochondria. Neurons present healthy morphology without vacuolar lesions in the central brain. Results in normal behavior and increases lifespan. The mutation in the ND23 gene enhances the phenotype of ND23 mutants. These mutants exhibit extended lifespan, healthy neuronal morphology, normal mitochondrial morphology, and increased ATP levels. This mutation is dissimilar to those observed in patients with Leigh syndrome, which is caused by mutations in nuclear genes encoding mitochondrial proteins. The severity of the ND23 mutation's phenotype varies depending on the maternally inherited mitochondrial background. Sequence analysis identified a variant affecting a mitochondrially encoded component of complex I as a likely candidate for the phenotypic interaction with mutant ND23.","Enhances mitochondrial function and results in normal-sized mitochondria. Neurons present healthy morphology without vacuolar lesions in the central brain. Results in normal behavior and increases lifespan. The mutation in the ND23 gene enhances the phenotype of ND23 mutants. These mutants exhibit extended lifespan, healthy neuronal morphology, normal mitochondrial morphology, and increased ATP levels. This mutation is dissimilar to those observed in patients with Leigh syndrome, which is caused by mutations in nuclear genes encoding mitochondrial proteins. The severity of the ND23 mutation's phenotype varies depending on the maternally inherited mitochondrial background. Sequence analysis identified a variant affecting a mitochondrially encoded component of complex I as a likely candidate for the phenotypic interaction with mutant ND23."
338,0,0,P08692-A60R,MSNITIYHNPACGTSRNTLEMIRNSGTEPTIILYLENPPSRDELVKLIADMGISVRALLRKNVEPYEQLGLAEDKFTDDQLIDFMLQHPILINRPIVVTPLGTRLCRPSEVVLDILQDAQKGAFTKEDGEKVVDEAGKRLK,,-1.0,MSNITIYHNPACGTSRNTLEMIRNSGTEPTIILYLENPPSRDELVKLIADMGISVRALLAKNVEPYEQLGLAEDKFTDDQLIDFMLQHPILINRPIVVTPLGTRLCRPSEVVLDILQDAQKGAFTKEDGEKVVDEAGKRLK,Arsenate reductase,Involved in resistance to arsenate. Catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)]. The resulting arsenite is then extruded from the cell via the ArsAB transport system (Probable).,50-fold increase in catalytic efficiency with arsenate. Mutant is resistant to arsenate. The mutation confers varying levels of enzymatic activity.,50-fold increase in catalytic efficiency with arsenate. Mutant is resistant to arsenate. The mutation confers varying levels of enzymatic activity.
339,0,0,P51843-V300A,MAGENHQWQGSILYNMLMSAKQTRAAPEAPETRLVDQCWGCSCGDEPGVGREGLLGGRNVALLYRCCFCGKDHPRQGSILYSMLTSAKQTYAAPKAPEATLGPCWGCSCGSDPGVGRAGLPGGRPVALLYRCCFCGEDHPRQGSILYSLLTSSKQTHVAPAAPEARPGGAWWDRSYFAQRPGGKEALPGGRATALLYRCCFCGEDHPQQGSTLYCVPTSTNQAQAAPEERPRAPWWDTSSGALRPVALKSPQVVCEAASAGLLKTLRFVKYLPCFQVLPLDQQLVLVRNCWASLLMLELAQDRLQFETVEVSEPSMLQKILTTRRRETGGNEPLPVPTLQHHLAPPAEARKVPSASQVQAIKCFLSKCWSLNISTKEYAYLKGTVLFNPDVPGLQCVKYIQGLQWGTQQILSEHTRMTHQGPHDRFIELNSTLFLLRFINANVIAELFFRPIIGTVSMDDMMLEMLCTKI,,-1.0,MAGENHQWQGSILYNMLMSAKQTRAAPEAPETRLVDQCWGCSCGDEPGVGREGLLGGRNVALLYRCCFCGKDHPRQGSILYSMLTSAKQTYAAPKAPEATLGPCWGCSCGSDPGVGRAGLPGGRPVALLYRCCFCGEDHPRQGSILYSLLTSSKQTHVAPAAPEARPGGAWWDRSYFAQRPGGKEALPGGRATALLYRCCFCGEDHPQQGSTLYCVPTSTNQAQAAPEERPRAPWWDTSSGALRPVALKSPQVVCEAASAGLLKTLRFVKYLPCFQVLPLDQQLVLVRNCWASLLMLELVQDRLQFETVEVSEPSMLQKILTTRRRETGGNEPLPVPTLQHHLAPPAEARKVPSASQVQAIKCFLSKCWSLNISTKEYAYLKGTVLFNPDVPGLQCVKYIQGLQWGTQQILSEHTRMTHQGPHDRFIELNSTLFLLRFINANVIAELFFRPIIGTVSMDDMMLEMLCTKI,Nuclear receptor subfamily 0 group B member 1,Orphan nuclear receptor. Component of a cascade required for the development of the hypothalamic-pituitary-adrenal-gonadal axis. Acts as a coregulatory protein that inhibits the transcriptional activity of other nuclear receptors through heterodimeric interactions. May also have a role in the development of the embryo and in the maintenance of embryonic stem cell pluripotency.,"In AHC. The absence of the mutation in the DAX-1 gene allows for a normal reproductive axis at birth. However, sometime between infancy and puberty, this mutation leads to an ability to activate the reproductive axis, resulting in the presence of puberty development in this infant.","In AHC. The absence of the mutation in the DAX-1 gene allows for a normal reproductive axis at birth. However, sometime between infancy and puberty, this mutation leads to an ability to activate the reproductive axis, resulting in the presence of puberty development in this infant."
340,0,0,P08692-E128D,MSNITIYHNPACGTSRNTLEMIRNSGTEPTIILYLENPPSRDELVKLIADMGISVRALLRKNVEPYEQLGLAEDKFTDDQLIDFMLQHPILINRPIVVTPLGTRLCRPSEVVLDILQDAQKGAFTKEDGEKVVDEAGKRLK,,-1.0,MSNITIYHNPACGTSRNTLEMIRNSGTEPTIILYLENPPSRDELVKLIADMGISVRALLRKNVEPYEQLGLAEDKFTDDQLIDFMLQHPILINRPIVVTPLGTRLCRPSEVVLDILQDAQKGAFTKEEGEKVVDEAGKRLK,Arsenate reductase,Involved in resistance to arsenate. Catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)]. The resulting arsenite is then extruded from the cell via the ArsAB transport system (Probable).,"7-fold increase in catalytic efficiency with arsenate. Mutant is relatively sensitive to arsenate, but is more resistant at higher concentrations.","7-fold increase in catalytic efficiency with arsenate. Mutant is relatively sensitive to arsenate, but is more resistant at higher concentrations."
341,0,0,P15917-D720E,MNIKKEFIKVISMSCLVTAITLSGPVFIPLVQGAGGHGDVGMHVKEKEKNKDENKRKDEERNKTQEEHLKEIMKHIVKIEVKGEEAVKKEAAEKLLEKVPSDVLEMYKAIGGKIYIVDGDITKHISLEALSEDKKKIKDIYGKDALLHEHYVYAKEGYEPVLVIQSSEDYVENTEKALNVYYEIGKILSRDILSKINQPYQKFLDVLNTIKNASDSDGQDLLFTNQLKEHPTDFSVEFLEQNSNEVQEVFAKAFAYYIEPQHRDVLQLYAPEAFNYMDKFNEQEINLSLEELKDQRMLARYEKWEKIKQHYQHWSDSLSEEGRGLLKKLQIPIEPKKDDIIHSLSQEEKELLKRIQIDSSDFLSTEEKEFLKKLQIDIRDSLSEEEKELLNRIQVDSSNPLSEKEKEFLKKLKLDIQPYDINQRLQDTGGLIDSPSINLDVRKQYKRDIQNIDALLHQSIGSTLYNKIYLYENMNINNLTATLGADLVDSTDNTKINRGIFNEFKKNFKYSISSNYMIVDINERPALDNERLKWRIQLSPDTRAGYLENGKLILQRNIGLEIKDVQIIKQSEKEYIRIDAKVVPKSKIDTKIQEAQLNINQEWNKALGLPKYTKLITFNVHNRYASNIVESAYLILNEWKNNIQSDLIKKVTNYLVDGNGRFVFTDITLPNIAEQYTHQDEIYEQVHSKGLYVPESRSILLHGPSKGVELRNDSEGFIHEFGHAVDDYAGYLLDKNQSDLVTNSKKFIDIFKEEGSNLTSYGRTNEAEFFAEAFRLMHSTDHAERLKVQKNAPKTFQFINDQIKFIINS,,-1.0,MNIKKEFIKVISMSCLVTAITLSGPVFIPLVQGAGGHGDVGMHVKEKEKNKDENKRKDEERNKTQEEHLKEIMKHIVKIEVKGEEAVKKEAAEKLLEKVPSDVLEMYKAIGGKIYIVDGDITKHISLEALSEDKKKIKDIYGKDALLHEHYVYAKEGYEPVLVIQSSEDYVENTEKALNVYYEIGKILSRDILSKINQPYQKFLDVLNTIKNASDSDGQDLLFTNQLKEHPTDFSVEFLEQNSNEVQEVFAKAFAYYIEPQHRDVLQLYAPEAFNYMDKFNEQEINLSLEELKDQRMLARYEKWEKIKQHYQHWSDSLSEEGRGLLKKLQIPIEPKKDDIIHSLSQEEKELLKRIQIDSSDFLSTEEKEFLKKLQIDIRDSLSEEEKELLNRIQVDSSNPLSEKEKEFLKKLKLDIQPYDINQRLQDTGGLIDSPSINLDVRKQYKRDIQNIDALLHQSIGSTLYNKIYLYENMNINNLTATLGADLVDSTDNTKINRGIFNEFKKNFKYSISSNYMIVDINERPALDNERLKWRIQLSPDTRAGYLENGKLILQRNIGLEIKDVQIIKQSEKEYIRIDAKVVPKSKIDTKIQEAQLNINQEWNKALGLPKYTKLITFNVHNRYASNIVESAYLILNEWKNNIQSDLIKKVTNYLVDGNGRFVFTDITLPNIAEQYTHQDEIYEQVHSKGLYVPESRSILLHGPSKGVELRNDSEGFIHDFGHAVDDYAGYLLDKNQSDLVTNSKKFIDIFKEEGSNLTSYGRTNEAEFFAEAFRLMHSTDHAERLKVQKNAPKTFQFINDQIKFIINS,Lethal factor,"Lethal factor (LF), which constitutes one of the three proteins composing the anthrax toxin, is able to trigger rapid cell death in macrophages. Acts as a protease that cleaves the N-terminal of most dual specificity mitogen-activated protein kinase kinases (MAPKKs or MAP2Ks) (except for MAP2K5): cleavage invariably occurs within the N-terminal proline-rich region preceding the kinase domain, thus disrupting a sequence involved in directing specific protein-protein interactions necessary for the assembly of signaling complexes. Also cleaves mouse Nlrp1b: host Nlrp1b cleavage promotes ubiquitination and degradation of the N-terminal part of Nlrp1b by the proteasome, thereby releasing the cleaved C-terminal part of Nlrp1b, which polymerizes and forms the Nlrp1b inflammasome followed by host cell pyroptosis. Able to cleave mouse Nlrp1b alleles 1 and 5, while it is not able to cleave Nlrp1b alleles 2, 3 and 4. In contrast, does not cleave NLRP1 human ortholog. LF is not toxic by itself and only acts as a lethal factor when associated with protective antigen (PA) to form the lethal toxin (LeTx): PA is required for LF translocation into the host cytosol.",Loss of inactivity. No effect on zinc releasing. The mutation in the Nlrp1b protein leads to inhibition of procaspase-1 in nonmyeloid cell lines.,Loss of inactivity. No effect on zinc releasing. The mutation in the Nlrp1b protein leads to inhibition of procaspase-1 in nonmyeloid cell lines.
342,0,0,Q5EZ72-A198D,MGHSAVLLSVALVILPACVTGGPVQRQQQHKLLLVSFDGFRWNYDQDVETPNLDSMAQEGVKARYMTPAFVTMTSPCHFTLVTGKYIENHGVVHNMFYNTTNKVRLPYHATLGIQRWWDNGSIPIWITAQRQGLKTGSFFYPGGNVTYQGEAVTMSRKEGVLHNYKNETEWRANVDTVMKWFTEEDVSLVTLYFGEPDSTGHKYGPESQERKDMVKQVDRTVGYLRDSIKRHHLTDSLNLIITSDHGMTTVNKKASDLVEFHKFPNFTFRDIEFELLDYGPNGMLIPKEGMLEKVYSVLKDAHPRLHVYKKEDFPKTFHYANNPRITSLLMYSDLGYVIHGRVNVQFNSGEHGFDNQDMDMKTIFRAVGPSFKAGLEVEPFESVHVYELMCQLLGIVPEPNDGHPGVLQPMLRSGSPLSRQHHLVVVLMGILTGLAKVV,,-1.0,MGHSAVLLSVALVILPACVTGGPVQRQQQHKLLLVSFDGFRWNYDQDVETPNLDSMAQEGVKARYMTPAFVTMTSPCHFTLVTGKYIENHGVVHNMFYNTTNKVRLPYHATLGIQRWWDNGSIPIWITAQRQGLKTGSFFYPGGNVTYQGEAVTMSRKEGVLHNYKNETEWRANVDTVMKWFTEEDVSLVTLYFGEPASTGHKYGPESQERKDMVKQVDRTVGYLRDSIKRHHLTDSLNLIITSDHGMTTVNKKASDLVEFHKFPNFTFRDIEFELLDYGPNGMLIPKEGMLEKVYSVLKDAHPRLHVYKKEDFPKTFHYANNPRITSLLMYSDLGYVIHGRVNVQFNSGEHGFDNQDMDMKTIFRAVGPSFKAGLEVEPFESVHVYELMCQLLGIVPEPNDGHPGVLQPMLRSGSPLSRQHHLVVVLMGILTGLAKVV,Ectonucleotide pyrophosphatase/phosphodiesterase family member 7,"Choline-specific phosphodiesterase that hydrolyzes sphingomyelin (SM) releasing the ceramide and phosphocholine and therefore is involved in sphingomyelin digestion, ceramide formation, and fatty acid (FA) absorption in the gastrointestinal tract. Has also phospholipase C activity and can also cleave phosphocholine from palmitoyl lyso-phosphatidylcholine and platelet-activating factor (PAF) leading to its inactivation. Does not have nucleotide pyrophosphatase activity. May promote cholesterol absorption by affecting the levels of sphingomyelin derived from either diet or endogenous sources, in the intestinal lumen.",Enhances the phosphoric diester hydrolase activity against PAF. The activity against PAF was enhanced by site mutation of the predicted metal-binding sites that are conserved in all NPP members.,Enhances the phosphoric diester hydrolase activity against PAF. The activity against PAF was enhanced by site mutation of the predicted metal-binding sites that are conserved in all NPP members.
343,0,0,Q0WRB0-M377V,MELNCVQFLRNKTILVTGATGFLAKVFVEKILRVQPNVKKLYLLVRASDNEAATKRLRTEVFEKELFKVLRQNLGDEKLNTLLYEKVVSVPGDIATDQLGINDSHLRERMQKEIDIVVNVAATTNFDERYDVGLGINTFGALNVLNFAKKCVKVQLLLHVSTAYVCGEKPGLIPEKPFIMEEIRNENGLQLDINLERELMKQRLKELNEQDCSEEDITLSMKELGMERAKLHGWPNTYVFTKSMGEMLLGKHKENLPLVIIRPTMITSTLSEPFPGWIEGLRTVDSVIIAYGKGVLKCFLVDVNSVCDMIPVDMVANAMITAAAKHAGGSGVHMVYHVGSSHQNPVTFGEIHEIAVRYFTKNPLRSRNGSLITVSKVRFIPTMALFSLYMTLRYKLPLQLLKLVDIIYPWRNGDKYGDKNRKIELVMRLVELYEPYVLFKGIFDDRNTKSLCANQKEEEIKNTEKLMFDFDPKGINWGDYLTNIHISGLVTHVLKK,,-1.0,MELNCVQFLRNKTILVTGATGFLAKVFVEKILRVQPNVKKLYLLVRASDNEAATKRLRTEVFEKELFKVLRQNLGDEKLNTLLYEKVVSVPGDIATDQLGINDSHLRERMQKEIDIVVNVAATTNFDERYDVGLGINTFGALNVLNFAKKCVKVQLLLHVSTAYVCGEKPGLIPEKPFIMEEIRNENGLQLDINLERELMKQRLKELNEQDCSEEDITLSMKELGMERAKLHGWPNTYVFTKSMGEMLLGKHKENLPLVIIRPTMITSTLSEPFPGWIEGLRTVDSVIIAYGKGVLKCFLVDVNSVCDMIPVDMVANAMITAAAKHAGGSGVHMVYHVGSSHQNPVTFGEIHEIAVRYFTKNPLRSRNGSLITVSKMRFIPTMALFSLYMTLRYKLPLQLLKLVDIIYPWRNGDKYGDKNRKIELVMRLVELYEPYVLFKGIFDDRNTKSLCANQKEEEIKNTEKLMFDFDPKGINWGDYLTNIHISGLVTHVLKK,Probable fatty acyl-CoA reductase 5,"Catalyzes the reduction of fatty acyl-CoA to fatty alcohols. Catalyzes specifically the formation of C18:0 fatty alcohol. Provides the fatty alcohols required for synthesis of suberin in roots, seed coat and wound-induced leaf tissue. Provides the fatty alcohols required for synthesis of alkyl hydroxycinnamates in root waxes.",Catalyzes the formation of C18:0 fatty alcohol instead of C16:0; when associated with L-355.,Catalyzes the formation of C18:0 fatty alcohol instead of C16:0; when associated with L-355.
344,0,0,P32266-N224S,MNASPVRLLILRRQLATHPAILYSSPYIKSPLVHLHSRMSNVHRSAHANALSFVITRRSISHFPKIISKIIRLPIYVGGGMAAAGSYIAYKMEEASSFTKDKLDRIKDLGESMKEKFNKMFSGDKSQDGGHGNDGTVPTATLIAATSLDDDESKRQGDPKDDDDEDDDDEDDENDSVDTTQDEMLNLTKQMIEIRTILNKVDSSSAHLTLPSIVVIGSQSSGKSSVLESIVGREFLPKGSNMVTRRPIELTLVNTPNSNNVTADFPSMRLYNIKDFKEVKRMLMELNMAVPTSEAVSEEPIQLTIKSSRVPDLSLVDLPGYIQVEAADQPIELKTKIRDLCEKYLTAPNIILAISAADVDLANSSALKASKAADPKGLRTIGVITKLDLVDPEKARSILNNKKYPLSMGYVGVITKTPSSINRKHLGLFGEAPSSSLSGIFSKGQHGQSSGEENTNGLKQIVSHQFEKAYFKENKKYFTNCQVSTKKLREKLIKILEISMSNALEPTSTLIQQELDDTSYLFKVEFNDRHLTPKSYLLNNIDVLKLGIKEFQEKFHRNELKSILRAELDQKVLDVLATRYWKDDNLQDLSSSKLESDTDMLYWHKKLELASSGLTKMGIGRLSTMLTTNAILKELDNILESTQLKNHELIKDLVSNTAINVLNSKYYSTADQVENCIKPFKYEIDLEERDWSLARQHSINLIKEELRQCNSRYQAIKNAVGSKKLANVMGYLENESNLQKETLGMSKLLLERGSEAIFLDKRCKVLSFRLKMLKNKCHSTIEKDRCPEVFLSAVSDKLTSTAVLFLNVELLSDFFYNFPIELDRRLTLLGDEQVEMFAKEDPKISRHIELQKRKELLELALEKIDSILVFKKSYKGVSKNL,,-1.0,MNASPVRLLILRRQLATHPAILYSSPYIKSPLVHLHSRMSNVHRSAHANALSFVITRRSISHFPKIISKIIRLPIYVGGGMAAAGSYIAYKMEEASSFTKDKLDRIKDLGESMKEKFNKMFSGDKSQDGGHGNDGTVPTATLIAATSLDDDESKRQGDPKDDDDEDDDDEDDENDSVDTTQDEMLNLTKQMIEIRTILNKVDSSSAHLTLPSIVVIGSQSSGKNSVLESIVGREFLPKGSNMVTRRPIELTLVNTPNSNNVTADFPSMRLYNIKDFKEVKRMLMELNMAVPTSEAVSEEPIQLTIKSSRVPDLSLVDLPGYIQVEAADQPIELKTKIRDLCEKYLTAPNIILAISAADVDLANSSALKASKAADPKGLRTIGVITKLDLVDPEKARSILNNKKYPLSMGYVGVITKTPSSINRKHLGLFGEAPSSSLSGIFSKGQHGQSSGEENTNGLKQIVSHQFEKAYFKENKKYFTNCQVSTKKLREKLIKILEISMSNALEPTSTLIQQELDDTSYLFKVEFNDRHLTPKSYLLNNIDVLKLGIKEFQEKFHRNELKSILRAELDQKVLDVLATRYWKDDNLQDLSSSKLESDTDMLYWHKKLELASSGLTKMGIGRLSTMLTTNAILKELDNILESTQLKNHELIKDLVSNTAINVLNSKYYSTADQVENCIKPFKYEIDLEERDWSLARQHSINLIKEELRQCNSRYQAIKNAVGSKKLANVMGYLENESNLQKETLGMSKLLLERGSEAIFLDKRCKVLSFRLKMLKNKCHSTIEKDRCPEVFLSAVSDKLTSTAVLFLNVELLSDFFYNFPIELDRRLTLLGDEQVEMFAKEDPKISRHIELQKRKELLELALEKIDSILVFKKSYKGVSKNL,"Dynamin-like GTPase MGM1, mitochondrial",Dynamin-related GTPase required for mitochondrial fusion. Coordinates interaction between the inner and outer mitochondrial membrane to promote the formation of the double membrane.,"Gain of GTPase activity. The mdm17 mutation causes temperature-independent improvements in mitochondrial inheritance, mitochondrial morphology, and the enhancement of mitochondrial DNA in the yeast Saccharomyces cerevisiae. Enhancements in mitochondrial transmission to daughter buds and preservation of mitochondrial morphology were apparent within 30 min after shifting cells to 37 degrees C, while acquisition of the mitochondrial genome occurred after 4-24 h at the elevated temperature. The mdm17 lesion mapped to MGM1, a gene encoding a dynamin-like GTPase previously implicated in mitochondrial genome maintenance, and the cloned MGM1 gene exacerbates all of the mdm17 mutant phenotypes. Cells with an mgm1-null mutation displayed normal mitochondrial inheritance and morphology. Mutations at cause mitochondrial fusion and a gain of mitochondrial DNA.","Gain of GTPase activity. The mdm17 mutation causes temperature-independent improvements in mitochondrial inheritance, mitochondrial morphology, and the enhancement of mitochondrial DNA in the yeast Saccharomyces cerevisiae. Enhancements in mitochondrial transmission to daughter buds and preservation of mitochondrial morphology were apparent within 30 min after shifting cells to 37 degrees C, while acquisition of the mitochondrial genome occurred after 4-24 h at the elevated temperature. The mdm17 lesion mapped to MGM1, a gene encoding a dynamin-like GTPase previously implicated in mitochondrial genome maintenance, and the cloned MGM1 gene exacerbates all of the mdm17 mutant phenotypes. Cells with an mgm1-null mutation displayed normal mitochondrial inheritance and morphology. Mutations at cause mitochondrial fusion and a gain of mitochondrial DNA."
345,0,0,P15917-A186K,MNIKKEFIKVISMSCLVTAITLSGPVFIPLVQGAGGHGDVGMHVKEKEKNKDENKRKDEERNKTQEEHLKEIMKHIVKIEVKGEEAVKKEAAEKLLEKVPSDVLEMYKAIGGKIYIVDGDITKHISLEALSEDKKKIKDIYGKDALLHEHYVYAKEGYEPVLVIQSSEDYVENTEKALNVYYEIGKILSRDILSKINQPYQKFLDVLNTIKNASDSDGQDLLFTNQLKEHPTDFSVEFLEQNSNEVQEVFAKAFAYYIEPQHRDVLQLYAPEAFNYMDKFNEQEINLSLEELKDQRMLARYEKWEKIKQHYQHWSDSLSEEGRGLLKKLQIPIEPKKDDIIHSLSQEEKELLKRIQIDSSDFLSTEEKEFLKKLQIDIRDSLSEEEKELLNRIQVDSSNPLSEKEKEFLKKLKLDIQPYDINQRLQDTGGLIDSPSINLDVRKQYKRDIQNIDALLHQSIGSTLYNKIYLYENMNINNLTATLGADLVDSTDNTKINRGIFNEFKKNFKYSISSNYMIVDINERPALDNERLKWRIQLSPDTRAGYLENGKLILQRNIGLEIKDVQIIKQSEKEYIRIDAKVVPKSKIDTKIQEAQLNINQEWNKALGLPKYTKLITFNVHNRYASNIVESAYLILNEWKNNIQSDLIKKVTNYLVDGNGRFVFTDITLPNIAEQYTHQDEIYEQVHSKGLYVPESRSILLHGPSKGVELRNDSEGFIHEFGHAVDDYAGYLLDKNQSDLVTNSKKFIDIFKEEGSNLTSYGRTNEAEFFAEAFRLMHSTDHAERLKVQKNAPKTFQFINDQIKFIINS,,-1.0,MNIKKEFIKVISMSCLVTAITLSGPVFIPLVQGAGGHGDVGMHVKEKEKNKDENKRKDEERNKTQEEHLKEIMKHIVKIEVKGEEAVKKEAAEKLLEKVPSDVLEMYKAIGGKIYIVDGDITKHISLEALSEDKKKIKDIYGKDALLHEHYVYAKEGYEPVLVIQSSEDYVENTEKALNVYYEIGAILSRDILSKINQPYQKFLDVLNTIKNASDSDGQDLLFTNQLKEHPTDFSVEFLEQNSNEVQEVFAKAFAYYIEPQHRDVLQLYAPEAFNYMDKFNEQEINLSLEELKDQRMLARYEKWEKIKQHYQHWSDSLSEEGRGLLKKLQIPIEPKKDDIIHSLSQEEKELLKRIQIDSSDFLSTEEKEFLKKLQIDIRDSLSEEEKELLNRIQVDSSNPLSEKEKEFLKKLKLDIQPYDINQRLQDTGGLIDSPSINLDVRKQYKRDIQNIDALLHQSIGSTLYNKIYLYENMNINNLTATLGADLVDSTDNTKINRGIFNEFKKNFKYSISSNYMIVDINERPALDNERLKWRIQLSPDTRAGYLENGKLILQRNIGLEIKDVQIIKQSEKEYIRIDAKVVPKSKIDTKIQEAQLNINQEWNKALGLPKYTKLITFNVHNRYASNIVESAYLILNEWKNNIQSDLIKKVTNYLVDGNGRFVFTDITLPNIAEQYTHQDEIYEQVHSKGLYVPESRSILLHGPSKGVELRNDSEGFIHEFGHAVDDYAGYLLDKNQSDLVTNSKKFIDIFKEEGSNLTSYGRTNEAEFFAEAFRLMHSTDHAERLKVQKNAPKTFQFINDQIKFIINS,Lethal factor,"Lethal factor (LF), which constitutes one of the three proteins composing the anthrax toxin, is able to trigger rapid cell death in macrophages. Acts as a protease that cleaves the N-terminal of most dual specificity mitogen-activated protein kinase kinases (MAPKKs or MAP2Ks) (except for MAP2K5): cleavage invariably occurs within the N-terminal proline-rich region preceding the kinase domain, thus disrupting a sequence involved in directing specific protein-protein interactions necessary for the assembly of signaling complexes. Also cleaves mouse Nlrp1b: host Nlrp1b cleavage promotes ubiquitination and degradation of the N-terminal part of Nlrp1b by the proteasome, thereby releasing the cleaved C-terminal part of Nlrp1b, which polymerizes and forms the Nlrp1b inflammasome followed by host cell pyroptosis. Able to cleave mouse Nlrp1b alleles 1 and 5, while it is not able to cleave Nlrp1b alleles 2, 3 and 4. In contrast, does not cleave NLRP1 human ortholog. LF is not toxic by itself and only acts as a lethal factor when associated with protective antigen (PA) to form the lethal toxin (LeTx): PA is required for LF translocation into the host cytosol.",Gain of ability to bind to PA.,Gain of ability to bind to PA.
346,0,0,P25522-A270D,MSDNDTIVAQATPPGRGGVGILRISGFKAREVAETVLGKLPKPRYADYLPFKDADGSVLDQGIALWFPGPNSFTGEDVLELQGHGGPVILDLLLKRILTIPGLRIARPGEFSERAFLNDKLDLAQAEAIADLIDASSEQAARSALNSLQGAFSARVNHLVEALTHLRIYVEAAIDFPDEEIDFLSDGKIEAQLNDVIADLDAVRAEARQGSLLREGMKVVIAGRPNAGKSSLLNALAGREAAIVTDIAGTTRDVLREHIHIDGMPLHIIDTAGLREASDEVERIGIERAWQEIEQADRVLFMVDGTTTDAVDPAEIWPEFIARLPAKLPITVVRNKADITGETLGMSEVNGHALIRLSARTGEGVDVLRNHLKQSMGFDTNMEGGFLARRRHLQALEQAAEHLQQGKAQLLGAWAGELLAEELRLAQQNLSEITGEFTSDDLLGRIFSSFCIGK,,-1.0,MSDNDTIVAQATPPGRGGVGILRISGFKAREVAETVLGKLPKPRYADYLPFKDADGSVLDQGIALWFPGPNSFTGEDVLELQGHGGPVILDLLLKRILTIPGLRIARPGEFSERAFLNDKLDLAQAEAIADLIDASSEQAARSALNSLQGAFSARVNHLVEALTHLRIYVEAAIDFPDEEIDFLSDGKIEAQLNDVIADLDAVRAEARQGSLLREGMKVVIAGRPNAGKSSLLNALAGREAAIVTDIAGTTRDVLREHIHIDGMPLHIIATAGLREASDEVERIGIERAWQEIEQADRVLFMVDGTTTDAVDPAEIWPEFIARLPAKLPITVVRNKADITGETLGMSEVNGHALIRLSARTGEGVDVLRNHLKQSMGFDTNMEGGFLARRRHLQALEQAAEHLQQGKAQLLGAWAGELLAEELRLAQQNLSEITGEFTSDDLLGRIFSSFCIGK,tRNA modification GTPase MnmE,"Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.","Does not enhance GTP binding, but improves hydrolase activity. Completely improves tRNA modifying function.","Does not enhance GTP binding, but improves hydrolase activity. Completely improves tRNA modifying function."
347,0,0,O75828-M142Q,MSSCSRVALVTGANRGIGLAIARELCRQFSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLNVLVNNAAVAFKSDDPMPFDIKAEMTLKTNFFATRNMCNELLPIMKPHGRVVNISSLQCLRAFENCSEDLQERFHSETLTEGDLVDLMKKFVEDTKNEVHEREGWPNSPYGVSKLGVTVLSRILARRLDEKRKADRILVNACCPGPVKTDMDGKDSIRTVEEGAETPVYLALLPPDATEPQGQLVHDKVVQNW,,-1.0,MSSCSRVALVTGANRGIGLAIARELCRQFSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLNVLVNNAAVAFKSDDPMPFDIKAEMTLKTNFFATRNMCNELLPIMKPHGRVVNISSLMCLRAFENCSEDLQERFHSETLTEGDLVDLMKKFVEDTKNEVHEREGWPNSPYGVSKLGVTVLSRILARRLDEKRKADRILVNACCPGPVKTDMDGKDSIRTVEEGAETPVYLALLPPDATEPQGQLVHDKVVQNW,Carbonyl reductase [NADPH] 3,"Catalyzes the NADPH-dependent reduction of carbonyl compounds to their corresponding alcohols. Has low NADPH-dependent oxidoreductase activity. Acts on several orthoquinones, acts as well on non-quinone compounds, such as isatin or on the anticancer drug oracin. Best substrates for CBR3 is 1,2- naphthoquinone, hence could play a role in protection against cytotoxicity of exogenous quinones. Exerts activity toward ortho-quinones but not paraquinones. No endogenous substrate for CBR3 except isatin has been identified.","Modest decrease in carbonyl reductase (NADPH) activity toward 1,2-naphthoquinone. The data reveal that the similarities in substrate specificity are largely due to a short segment of a substrate binding loop comprising critical residues M141/Q142 in CBR1.","Modest decrease in carbonyl reductase (NADPH) activity toward 1,2-naphthoquinone. The data reveal that the similarities in substrate specificity are largely due to a short segment of a substrate binding loop comprising critical residues M141/Q142 in CBR1."
348,0,0,O14746-M867V,MPRAPRCRAVRSLLRSHYREVLPLATFVRRLGPQGWRLVQRGDPAAFRALVAQCLVCVPWDARPPPAAPSFRQVSCLKELVARVLQRLCERGAKNVLAFGFALLDGARGGPPEAFTTSVRSYLPNTVTDALRGSGAWGLLLRRVGDDVLVHLLARCALFVLVAPSCAYQVCGPPLYQLGAATQARPPPHASGPRRRLGCERAWNHSVREAGVPLGLPAPGARRRGGSASRSLPLPKRPRRGAAPEPERTPVGQGSWAHPGRTRGPSDRGFCVVSPARPAEEATSLEGALSGTRHSHPSVGRQHHAGPPSTSRPPRPWDTPCPPVYAETKHFLYSSGDKEQLRPSFLLSSLRPSLTGARRLVETIFLGSRPWMPGTPRRLPRLPQRYWQMRPLFLELLGNHAQCPYGVLLKTHCPLRAAVTPAAGVCAREKPQGSVAAPEEEDTDPRRLVQLLRQHSSPWQVYGFVRACLRRLVPPGLWGSRHNERRFLRNTKKFISLGKHAKLSLQELTWKMSVRDCAWLRRSPGVGCVPAAEHRLREEILAKFLHWLMSVYVVELLRSFFYVTETTFQKNRLFFYRKSVWSKLQSIGIRQHLKRVQLRELSEAEVRQHREARPALLTSRLRFIPKPDGLRPIVNMDYVVGARTFRREKRAERLTSRVKALFSVLNYERARRPGLLGASVLGLDDIHRAWRTFVLRVRAQDPPPELYFVKVDVTGAYDTIPQDRLTEVIASIIKPQNTYCVRRYAVVQKAAHGHVRKAFKSHVSTLTDLQPYMRQFVAHLQETSPLRDAVVIEQSSSLNEASSGLFDVFLRFMCHHAVRIRGKSYVQCQGIPQGSILSTLLCSLCYGDMENKLFAGIRRDGLLLRLVDDFLLVTPHLTHAKTFLRTLVRGVPEYGCVVNLRKTVVNFPVEDEALGGTAFVQMPAHGLFPWCGLLLDTRTLEVQSDYSSYARTSIRASLTFNRGFKAGRNMRRKLFGVLRLKCHSLFLDLQVNSLQTVCTNIYKILLLQAYRFHACVLQLPFHQQ,,-1.0,MPRAPRCRAVRSLLRSHYREVLPLATFVRRLGPQGWRLVQRGDPAAFRALVAQCLVCVPWDARPPPAAPSFRQVSCLKELVARVLQRLCERGAKNVLAFGFALLDGARGGPPEAFTTSVRSYLPNTVTDALRGSGAWGLLLRRVGDDVLVHLLARCALFVLVAPSCAYQVCGPPLYQLGAATQARPPPHASGPRRRLGCERAWNHSVREAGVPLGLPAPGARRRGGSASRSLPLPKRPRRGAAPEPERTPVGQGSWAHPGRTRGPSDRGFCVVSPARPAEEATSLEGALSGTRHSHPSVGRQHHAGPPSTSRPPRPWDTPCPPVYAETKHFLYSSGDKEQLRPSFLLSSLRPSLTGARRLVETIFLGSRPWMPGTPRRLPRLPQRYWQMRPLFLELLGNHAQCPYGVLLKTHCPLRAAVTPAAGVCAREKPQGSVAAPEEEDTDPRRLVQLLRQHSSPWQVYGFVRACLRRLVPPGLWGSRHNERRFLRNTKKFISLGKHAKLSLQELTWKMSVRDCAWLRRSPGVGCVPAAEHRLREEILAKFLHWLMSVYVVELLRSFFYVTETTFQKNRLFFYRKSVWSKLQSIGIRQHLKRVQLRELSEAEVRQHREARPALLTSRLRFIPKPDGLRPIVNMDYVVGARTFRREKRAERLTSRVKALFSVLNYERARRPGLLGASVLGLDDIHRAWRTFVLRVRAQDPPPELYFVKVDVTGAYDTIPQDRLTEVIASIIKPQNTYCVRRYAVVQKAAHGHVRKAFKSHVSTLTDLQPYMRQFVAHLQETSPLRDAVVIEQSSSLNEASSGLFDVFLRFMCHHAVRIRGKSYVQCQGIPQGSILSTLLCSLCYGDMENKLFAGIRRDGLLLRLMDDFLLVTPHLTHAKTFLRTLVRGVPEYGCVVNLRKTVVNFPVEDEALGGTAFVQMPAHGLFPWCGLLLDTRTLEVQSDYSSYARTSIRASLTFNRGFKAGRNMRRKLFGVLRLKCHSLFLDLQVNSLQTVCTNIYKILLLQAYRFHACVLQLPFHQQ,Telomerase reverse transcriptase,"Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. Active in progenitor and cancer cells. Inactive, or very low activity, in normal somatic cells. Catalytic component of the teleromerase holoenzyme complex whose main activity is the elongation of telomeres by acting as a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme. Catalyzes the RNA-dependent extension of 3'-chromosomal termini with the 6-nucleotide telomeric repeat unit, 5'-TTAGGG-3'. The catalytic cycle involves primer binding, primer extension and release of product once the template boundary has been reached or nascent product translocation followed by further extension. More active on substrates containing 2 or 3 telomeric repeats. Telomerase activity is regulated by a number of factors including telomerase complex-associated proteins, chaperones and polypeptide modifiers. Modulates Wnt signaling. Plays important roles in aging and antiapoptosis.","About 75% increase in telomerase activity, about 50% increase in repeat extension rate, and 5.2-fold decrease in nucleotide incorporation fidelity. Little further increase in activity and 13.5-fold decrease in nucleotide incorporation fidelity; when associated with Y-866.","About 75% increase in telomerase activity, about 50% increase in repeat extension rate, and 5.2-fold decrease in nucleotide incorporation fidelity. Little further increase in activity and 13.5-fold decrease in nucleotide incorporation fidelity; when associated with Y-866."
349,0,0,Q84W98-A93G,MATSNDQTNTKSSHSRTLLLLFIFLSLLLFSSLTIPMTRHQSTSMVAPFKRVLLESSVPASSTMDLRPKASTRRSRTSRRREFGNDAHEVPSGPNPISN,,-1.0,MATSNDQTNTKSSHSRTLLLLFIFLSLLLFSSLTIPMTRHQSTSMVAPFKRVLLESSVPASSTMDLRPKASTRRSRTSRRREFGNDAHEVPSAPNPISN,CLAVATA3/ESR,"Extracellular signal peptide that regulates cell fate. May act with TDR as a ligand-receptor pair in a signal transduction pathway that represses tracheary element differentiation but promotes the formation of procambial cells adjacent to phloem cells in the veins in an auxin-dependent manner. Regulates the transition of protophloem cells from proliferation to differentiation, thus impinging on postembryonic growth capacity of the root meristem; this signaling pathway requires CRN and CLV2.",Functional stability with TDR. The mutation in TDIF leads to [functional stability].,Functional stability with TDR. The mutation in TDIF leads to [functional stability].
350,0,0,Q56223-A291C,MVRVKVNDRIVEVPPGTSVMDAVFHAGYDVPLFCSEKHLSPIGACRMCLVRIGLPKKGPDGKPLLNEKGEPEIQWQPKLAASCVTAVADGMVVDTLSDVVREAQAGMVEFTLLNHPLDCPTCDKGGACELQDRTVEYGLYEKYYQKGPLELPVYTRFEFTRRHVDKHHPLSPFVILDRERCIHCKRCVRYFEEVPGDEVLDFIERGVHTFIGTMDFGLPSGFSGNITDICPVGALLDLTARFRARNWEMEETPTTCALCPVGCGITADTRSGELLRIRAREVPEVNEIWICDAGRFGHEWADQNRLKTPLVRKEGRLVEATWEEAFLALKEGLKEARGEEVGLYLAHDATLEEGLLASELAKALKTPHLDFQGRTAAPASLFPPASLEDLLQADFALVLGDPTEEAPILHLRLSEFVRDLKPPHRYNHGTPFADLQIKERMPRRTDKMALFAPYRAPLMKWAAIHEVHRPGEEREILLALLGDKEGSEMVAKAKEAWEKAKNPVLILGAGVLQDTVAAERARLLAERKGAKVLAMTPAANARGLEAMGVLPGAKGASWDEPGALYAYYGFVPPEEALKGKRFVVMHLSHLHPLAERYAHVVLPAPTFYEKRGHLVNLEGRVLPLSPAPIENGEAEGALQVLALLAEALGVRPPFRLHLEAQKALKARKVPEAMGRLSFRLKELRPKERKGAFYLRPTMWKAHQAVGKAQEAARAELWAHPETARAEALPEGAQVAVETPFGRVEARVVHREDVPKGHLYLSALGPAAGLRVEGRVLVPAGGEA,,-1.0,MVRVKVNDRIVEVPPGTSVMDAVFHAGYDVPLFCSEKHLSPIGACRMCLVRIGLPKKGPDGKPLLNEKGEPEIQWQPKLAASCVTAVADGMVVDTLSDVVREAQAGMVEFTLLNHPLDCPTCDKGGACELQDRTVEYGLYEKYYQKGPLELPVYTRFEFTRRHVDKHHPLSPFVILDRERCIHCKRCVRYFEEVPGDEVLDFIERGVHTFIGTMDFGLPSGFSGNITDICPVGALLDLTARFRARNWEMEETPTTCALCPVGCGITADTRSGELLRIRAREVPEVNEIWIADAGRFGHEWADQNRLKTPLVRKEGRLVEATWEEAFLALKEGLKEARGEEVGLYLAHDATLEEGLLASELAKALKTPHLDFQGRTAAPASLFPPASLEDLLQADFALVLGDPTEEAPILHLRLSEFVRDLKPPHRYNHGTPFADLQIKERMPRRTDKMALFAPYRAPLMKWAAIHEVHRPGEEREILLALLGDKEGSEMVAKAKEAWEKAKNPVLILGAGVLQDTVAAERARLLAERKGAKVLAMTPAANARGLEAMGVLPGAKGASWDEPGALYAYYGFVPPEEALKGKRFVVMHLSHLHPLAERYAHVVLPAPTFYEKRGHLVNLEGRVLPLSPAPIENGEAEGALQVLALLAEALGVRPPFRLHLEAQKALKARKVPEAMGRLSFRLKELRPKERKGAFYLRPTMWKAHQAVGKAQEAARAELWAHPETARAEALPEGAQVAVETPFGRVEARVVHREDVPKGHLYLSALGPAAGLRVEGRVLVPAGGEA,NADH-quinone oxidoreductase subunit 3,"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 menaquinone. 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 required for the synthesis of ATP.",Increases amount and stability of iron-sulfur center 4. The mutation in the Nqo3 subunit of NDH-1 leads to a change in the ligated iron-sulfur cluster.,Increases amount and stability of iron-sulfur center 4. The mutation in the Nqo3 subunit of NDH-1 leads to a change in the ligated iron-sulfur cluster.
351,0,0,P76037-X110Y,MAINSPLNIAAQPGKTRLRKSLKLWQVVMMGLAYLTPMTVFDTFGIVSGISDGHVPASYLLALAGVLFTAISYGKLVRQFPEAGSAYTYAQKSINPHVGFMVGWSSLLDYLFLPMINVLLAKIYLSALFPEVPPWVWVVTFVAILTAANLKSVNLVANFNTLFVLVQISIMVVFIFLVVQGLHKGEGVGTVWSLQPFISENAHLIPIITGATIVCFSFLGFDAVTTLSEETPDAARVIPKAIFLTAVYGGVIFIAASFFMQLFFPDISRFKDPDAALPEIALYVGGKLFQSIFLCTTFVNTLASGLASHASVSRLLYVMGRDNVFPERVFGYVHPKWRTPALNVIMVGIVALSALFFDLVTATALINFGALVAFTFVNLSVFNHFWRRKGMNKSWKDHFHYLLMPLVGALTVGVLWVNLESTSLTLGLVWASLGGAYLWYLIRRYRKVPLYDGDRTPVSET,,-1.0,MAINSPLNIAAQPGKTRLRKSLKLWQVVMMGLAYLTPMTVFDTFGIVSGISDGHVPASYLLALAGVLFTAISYGKLVRQFPEAGSAYTYAQKSINPHVGFMVGWSSLLDXLFLPMINVLLAKIYLSALFPEVPPWVWVVTFVAILTAANLKSVNLVANFNTLFVLVQISIMVVFIFLVVQGLHKGEGVGTVWSLQPFISENAHLIPIITGATIVCFSFLGFDAVTTLSEETPDAARVIPKAIFLTAVYGGVIFIAASFFMQLFFPDISRFKDPDAALPEIALYVGGKLFQSIFLCTTFVNTLASGLASHASVSRLLYVMGRDNVFPERVFGYVHPKWRTPALNVIMVGIVALSALFFDLVTATALINFGALVAFTFVNLSVFNHFWRRKGMNKSWKDHFHYLLMPLVGALTVGVLWVNLESTSLTLGLVWASLGGAYLWYLIRRYRKVPLYDGDRTPVSET,Putrescine importer PuuP,Involved in the uptake of putrescine. Imports putrescine for its utilization as an energy source in the absence of glucose.,The uptake activity is enhanced to eight times that of wild-type.,The uptake activity is enhanced to eight times that of wild-type.
352,0,0,Q9ULZ3-A48D,MGRARDAILDALENLTAEELKKFKLKLLSVPLREGYGRIPRGALLSMDALDLTDKLVSFYLETYGAELTANVLRDMGLQEMAGQLQAATHQGSGAAPAGIQAPPQSAAKPGLHFIDQHRAALIARVTNVEWLLDALYGKVLTDEQYQAVRAEPTNPSKMRKLFSFTPAWNWTCKDLLLQALRESQSYLVEDLERS,,-1.0,MGRARDAILDALENLTAEELKKFKLKLLSVPLREGYGRIPRGALLSMAALDLTDKLVSFYLETYGAELTANVLRDMGLQEMAGQLQAATHQGSGAAPAGIQAPPQSAAKPGLHFIDQHRAALIARVTNVEWLLDALYGKVLTDEQYQAVRAEPTNPSKMRKLFSFTPAWNWTCKDLLLQALRESQSYLVEDLERS,Apoptosis-associated speck-like protein containing a CARD,"Functions as key mediator in apoptosis and inflammation. Promotes caspase-mediated apoptosis involving predominantly caspase-8 and also caspase-9 in a probable cell type-specific manner. Involved in activation of the mitochondrial apoptotic pathway, promotes caspase-8-dependent proteolytic maturation of BID independently of FADD in certain cell types and also mediates mitochondrial translocation of BAX and activates BAX-dependent apoptosis coupled to activation of caspase-9, -2 and -3. Involved in innate immune response by acting as an integral adapter in the assembly of various inflammasomes (NLRP1, NLRP2, NLRP3, NLRP6, AIM2 and probably IFI16) which recruit and activate caspase-1 leading to processing and secretion of pro-inflammatory cytokines. Caspase-1-dependent inflammation leads to macrophage pyroptosis, a form of cell death. The function as activating adapter in different types of inflammasomes is mediated by the pyrin and CARD domains and their homotypic interactions. Clustered PYCARD nucleates the formation of caspase-1 filaments through the interaction of their respective CARD domains, acting as a platform for of caspase-1 polymerization. In the NLRP1 and NLRC4 inflammasomes seems not be required but facilitates the processing of procaspase-1. In cooperation with NOD2 involved in an inflammasome activated by bacterial muramyl dipeptide leading to caspase-1 activation. May be involved in RIGI-triggered pro-inflammatory responses and inflammasome activation. In collaboration with AIM2 which detects cytosolic double-stranded DNA may also be involved in a caspase-1-independent cell death that involves caspase-8. In adaptive immunity may be involved in maturation of dendritic cells to stimulate T-cell immunity and in cytoskeletal rearrangements coupled to chemotaxis and antigen uptake may be involved in post-transcriptional regulation of the guanine nucleotide exchange factor DOCK2; the latter function is proposed to involve the nuclear form. Also involved in transcriptional activation of cytokines and chemokines independent of the inflammasome; this function may involve AP-1, NF-kappa-B, MAPK and caspase-8 signaling pathways. For regulation of NF-kappa-B activating and inhibiting functions have been reported. Modulates NF-kappa-B induction at the level of the IKK complex by inhibiting kinase activity of CHUK and IKBK. Proposed to compete with RIPK2 for association with CASP1 thereby down-regulating CASP1-mediated RIPK2-dependent NF-kappa-B activation and activating interleukin-1 beta processing. Modulates host resistance to DNA virus infection, probably by inducing the cleavage of and inactivating CGAS in presence of cytoplasmic double-stranded DNA.May have a regulating effect on the function as inflammasome adapter.Seems to inhibit inflammasome-mediated maturation of interleukin-1 beta.",Decreases interaction with PYDC1. Mutation of D48 to A in ASC protein leads to enhancement of filament formation. The mutation in ASC_PYD affects its interaction with POP1.,Decreases interaction with PYDC1. Mutation of D48 to A in ASC protein leads to enhancement of filament formation. The mutation in ASC_PYD affects its interaction with POP1.
353,0,0,Q6MZP7-Y525C,MEVVPAEVNSLLPEEIMDTGITLVDDDSIEAVIVSSPIPMETELEEIVNINSTGDSTATPISTEPITVYSNHTNQVAVNTTITKADSNTTVKPAFPSGLQKLGAQTPVTISANQIILNKVSQTSDLKLGNQTLKPDGQKLILTTLGKSGSPIVLALPHSQLPQAQKVTTQAQSGDAKLPPQQIKVVTIGGRPEVKPVIGVSALTPGSQLINTTTQPSVLQTQQLKTVQIAKKPRTPTSGPVITKLIFAKPINSKAVTGQTTQVSPPVIAGRVLSQSTPGTPSKTITISESGVIGSTLNSTTQTPNKIAISPLKSPNKAVKSTVQTITVGGVSTSQFKTIIPLATAPNVQQIQVPGSKFHYVRLVTATSASSSTQPVSQNPSTNTQPLQQAKPVVVNTTPVRMSVPIVSAQAVKQVVPKPINPTSQIVTTSQPQQRLIMPATPLPQIQPNLTNLPPGTVLAPAPGTGNVGYAVLPAQYVTQLQQSSYVSIASNSTFTGTSGIQTQARLPFNGIIPSESASRPRKPCNCTKSLCLKLYCDCFANGEFCNNCNCTNCYNNLEHENERQKAIKACLDRNPEAFKPKIGKGKEGESDRRHSKGCNCKRSGCLKNYCECYEAKIMCSSICKCIGCKNFEESPERKTLMHLADAAEVRVQQQTAAKTKLSSQISDLLTRPTPALNSGGGKLPFTFVTKEVAEATCNCLLAQAEQADKKGKSKAAAERMILEEFGRCLMSVINSAGKAKSDPCAMNC,,-1.0,MEVVPAEVNSLLPEEIMDTGITLVDDDSIEAVIVSSPIPMETELEEIVNINSTGDSTATPISTEPITVYSNHTNQVAVNTTITKADSNTTVKPAFPSGLQKLGAQTPVTISANQIILNKVSQTSDLKLGNQTLKPDGQKLILTTLGKSGSPIVLALPHSQLPQAQKVTTQAQSGDAKLPPQQIKVVTIGGRPEVKPVIGVSALTPGSQLINTTTQPSVLQTQQLKTVQIAKKPRTPTSGPVITKLIFAKPINSKAVTGQTTQVSPPVIAGRVLSQSTPGTPSKTITISESGVIGSTLNSTTQTPNKIAISPLKSPNKAVKSTVQTITVGGVSTSQFKTIIPLATAPNVQQIQVPGSKFHYVRLVTATSASSSTQPVSQNPSTNTQPLQQAKPVVVNTTPVRMSVPIVSAQAVKQVVPKPINPTSQIVTTSQPQQRLIMPATPLPQIQPNLTNLPPGTVLAPAPGTGNVGYAVLPAQYVTQLQQSSYVSIASNSTFTGTSGIQTQARLPFNGIIPSESASRPRKPYNCTKSLCLKLYCDCFANGEFCNNCNCTNCYNNLEHENERQKAIKACLDRNPEAFKPKIGKGKEGESDRRHSKGCNCKRSGCLKNYCECYEAKIMCSSICKCIGCKNFEESPERKTLMHLADAAEVRVQQQTAAKTKLSSQISDLLTRPTPALNSGGGKLPFTFVTKEVAEATCNCLLAQAEQADKKGKSKAAAERMILEEFGRCLMSVINSAGKAKSDPCAMNC,Protein lin-54 homolog,"Component of the DREAM complex, a multiprotein complex that can both act as a transcription activator or repressor depending on the context. In G0 phase, the complex binds to more than 800 promoters and is required for repression of E2F target genes. In S phase, the complex selectively binds to the promoters of G2/M genes whose products are required for mitosis and participates in their cell cycle dependent activation. In the complex, acts as a DNA-binding protein that binds the promoter of CDK1 in a sequence-specific manner. Specifically recognizes the consensus motif 5'-TTYRAA-3' in target DNA.",Enables DNA-binding to the CDK1 promoter; when associated with Y-527.,Enables DNA-binding to the CDK1 promoter; when associated with Y-527.
354,0,0,O14746-M726T,MPRAPRCRAVRSLLRSHYREVLPLATFVRRLGPQGWRLVQRGDPAAFRALVAQCLVCVPWDARPPPAAPSFRQVSCLKELVARVLQRLCERGAKNVLAFGFALLDGARGGPPEAFTTSVRSYLPNTVTDALRGSGAWGLLLRRVGDDVLVHLLARCALFVLVAPSCAYQVCGPPLYQLGAATQARPPPHASGPRRRLGCERAWNHSVREAGVPLGLPAPGARRRGGSASRSLPLPKRPRRGAAPEPERTPVGQGSWAHPGRTRGPSDRGFCVVSPARPAEEATSLEGALSGTRHSHPSVGRQHHAGPPSTSRPPRPWDTPCPPVYAETKHFLYSSGDKEQLRPSFLLSSLRPSLTGARRLVETIFLGSRPWMPGTPRRLPRLPQRYWQMRPLFLELLGNHAQCPYGVLLKTHCPLRAAVTPAAGVCAREKPQGSVAAPEEEDTDPRRLVQLLRQHSSPWQVYGFVRACLRRLVPPGLWGSRHNERRFLRNTKKFISLGKHAKLSLQELTWKMSVRDCAWLRRSPGVGCVPAAEHRLREEILAKFLHWLMSVYVVELLRSFFYVTETTFQKNRLFFYRKSVWSKLQSIGIRQHLKRVQLRELSEAEVRQHREARPALLTSRLRFIPKPDGLRPIVNMDYVVGARTFRREKRAERLTSRVKALFSVLNYERARRPGLLGASVLGLDDIHRAWRTFVLRVRAQDPPPELYFVKVDVTGAYDTIPQDRLTEVIASIIKPQNTYCVRRYAVVQKAAHGHVRKAFKSHVSTLTDLQPYMRQFVAHLQETSPLRDAVVIEQSSSLNEASSGLFDVFLRFMCHHAVRIRGKSYVQCQGIPQGSILSTLLCSLCYGDMENKLFAGIRRDGLLLRLVDDFLLVTPHLTHAKTFLRTLVRGVPEYGCVVNLRKTVVNFPVEDEALGGTAFVQMPAHGLFPWCGLLLDTRTLEVQSDYSSYARTSIRASLTFNRGFKAGRNMRRKLFGVLRLKCHSLFLDLQVNSLQTVCTNIYKILLLQAYRFHACVLQLPFHQQ,,-1.0,MPRAPRCRAVRSLLRSHYREVLPLATFVRRLGPQGWRLVQRGDPAAFRALVAQCLVCVPWDARPPPAAPSFRQVSCLKELVARVLQRLCERGAKNVLAFGFALLDGARGGPPEAFTTSVRSYLPNTVTDALRGSGAWGLLLRRVGDDVLVHLLARCALFVLVAPSCAYQVCGPPLYQLGAATQARPPPHASGPRRRLGCERAWNHSVREAGVPLGLPAPGARRRGGSASRSLPLPKRPRRGAAPEPERTPVGQGSWAHPGRTRGPSDRGFCVVSPARPAEEATSLEGALSGTRHSHPSVGRQHHAGPPSTSRPPRPWDTPCPPVYAETKHFLYSSGDKEQLRPSFLLSSLRPSLTGARRLVETIFLGSRPWMPGTPRRLPRLPQRYWQMRPLFLELLGNHAQCPYGVLLKTHCPLRAAVTPAAGVCAREKPQGSVAAPEEEDTDPRRLVQLLRQHSSPWQVYGFVRACLRRLVPPGLWGSRHNERRFLRNTKKFISLGKHAKLSLQELTWKMSVRDCAWLRRSPGVGCVPAAEHRLREEILAKFLHWLMSVYVVELLRSFFYVTETTFQKNRLFFYRKSVWSKLQSIGIRQHLKRVQLRELSEAEVRQHREARPALLTSRLRFIPKPDGLRPIVNMDYVVGARTFRREKRAERLTSRVKALFSVLNYERARRPGLLGASVLGLDDIHRAWRTFVLRVRAQDPPPELYFVKVDVTGAYDTIPQDRLMEVIASIIKPQNTYCVRRYAVVQKAAHGHVRKAFKSHVSTLTDLQPYMRQFVAHLQETSPLRDAVVIEQSSSLNEASSGLFDVFLRFMCHHAVRIRGKSYVQCQGIPQGSILSTLLCSLCYGDMENKLFAGIRRDGLLLRLVDDFLLVTPHLTHAKTFLRTLVRGVPEYGCVVNLRKTVVNFPVEDEALGGTAFVQMPAHGLFPWCGLLLDTRTLEVQSDYSSYARTSIRASLTFNRGFKAGRNMRRKLFGVLRLKCHSLFLDLQVNSLQTVCTNIYKILLLQAYRFHACVLQLPFHQQ,Telomerase reverse transcriptase,"Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. Active in progenitor and cancer cells. Inactive, or very low activity, in normal somatic cells. Catalytic component of the teleromerase holoenzyme complex whose main activity is the elongation of telomeres by acting as a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme. Catalyzes the RNA-dependent extension of 3'-chromosomal termini with the 6-nucleotide telomeric repeat unit, 5'-TTAGGG-3'. The catalytic cycle involves primer binding, primer extension and release of product once the template boundary has been reached or nascent product translocation followed by further extension. More active on substrates containing 2 or 3 telomeric repeats. Telomerase activity is regulated by a number of factors including telomerase complex-associated proteins, chaperones and polypeptide modifiers. Modulates Wnt signaling. Plays important roles in aging and antiapoptosis.","Increase in AA; very mild; significant effect on telomerase catalytic activity but lengthened telomeres. Common homozygous, synonymous mutation in TERT () was found in two patients with congenital aplastic anemia (AA). The mutation in the hTERT protein has not been identified in patients with dyskeratosis congenita or aplastic anemia. This mutation leads to an enhanced telomerase function by haploinsufficiency.","Increase in AA; very mild; significant effect on telomerase catalytic activity but lengthened telomeres. Common homozygous, synonymous mutation in TERT () was found in two patients with congenital aplastic anemia (AA). The mutation in the hTERT protein has not been identified in patients with dyskeratosis congenita or aplastic anemia. This mutation leads to an enhanced telomerase function by haploinsufficiency."
355,0,0,P9WH43-G310F,MPSPTVTSPQVAVNDIGSSEDFLAAIDKTIKYFNDGDIVEGTIVKVDRDEVLLDIGYKTEGVIPARELSIKHDVDPNEVVSVGDEVEALVLTKEDKEGRLILSKKRAQYERAWGTIEALKEKDEAVKGTVIEVVKGGLILDIGLRGFLPASLVEMRRVRDLQPYIGKEIEAKIIELDKNRNNVVLSRRAWLEQTQSEVRSEFLNNLQKGTIRKGVVSSIVNFGAFVDLGGVDGLVHVSELSWKHIDHPSEVVQVGDEVTVEVLDVDMDRERVSLSLKATQEDPWRHFARTHAIGQIVPGKVTKLVPFGAFVRVEEGIEGLVHISELAERHVEVPDQVVAVGDDAMVKVIDIDLERRRISLSLKQANEDYTEEFDPAKYGMADSYDEQGNYIFPEGFDAETNEWLEGFEKQRAEWEARYAEAERRHKMHTAQMEKFAAAEAAGRGADDQSSASSAPSEKTAGGSLASDAQLAALREKLAGSA,,-1.0,MPSPTVTSPQVAVNDIGSSEDFLAAIDKTIKYFNDGDIVEGTIVKVDRDEVLLDIGYKTEGVIPARELSIKHDVDPNEVVSVGDEVEALVLTKEDKEGRLILSKKRAQYERAWGTIEALKEKDEAVKGTVIEVVKGGLILDIGLRGFLPASLVEMRRVRDLQPYIGKEIEAKIIELDKNRNNVVLSRRAWLEQTQSEVRSEFLNNLQKGTIRKGVVSSIVNFGAFVDLGGVDGLVHVSELSWKHIDHPSEVVQVGDEVTVEVLDVDMDRERVSLSLKATQEDPWRHFARTHAIGQIVPGKVTKLVPFGAGVRVEEGIEGLVHISELAERHVEVPDQVVAVGDDAMVKVIDIDLERRRISLSLKQANEDYTEEFDPAKYGMADSYDEQGNYIFPEGFDAETNEWLEGFEKQRAEWEARYAEAERRHKMHTAQMEKFAAAEAAGRGADDQSSASSAPSEKTAGGSLASDAQLAALREKLAGSA,Small ribosomal subunit protein bS1,"Binds mRNA, facilitating recognition of most mRNAs by the 30S ribosomal subunit during translation initiation (By similarity). Probably plays a role in trans-translation; binds tmRNA (the product of the ssrA gene). In trans-translation Ala-aminoacylated transfer-messenger RNA (tmRNA, product of the ssrA gene; the 2 termini fold to resemble tRNA(Ala) while it encodes a short internal open reading frame (the tag peptide)) acts like a tRNA, entering the A-site of the ribosome and displacing the stalled mRNA (which is subsequently degraded). The ribosome then switches to translate the ORF on the tmRNA, the nascent peptide is terminated with the 'tag peptide' encoded by the tmRNA and thus targeted for degradation (By similarity).","3-fold increase in binding of POA, increased binding of tmRNA (expressed as residues 285-481). Conformational changes induced by mutation at F310 enable the POA binding activity.","3-fold increase in binding of POA, increased binding of tmRNA (expressed as residues 285-481). Conformational changes induced by mutation at F310 enable the POA binding activity."
356,0,0,P08692-D127E,MSNITIYHNPACGTSRNTLEMIRNSGTEPTIILYLENPPSRDELVKLIADMGISVRALLRKNVEPYEQLGLAEDKFTDDQLIDFMLQHPILINRPIVVTPLGTRLCRPSEVVLDILQDAQKGAFTKEDGEKVVDEAGKRLK,,-1.0,MSNITIYHNPACGTSRNTLEMIRNSGTEPTIILYLENPPSRDELVKLIADMGISVRALLRKNVEPYEQLGLAEDKFTDDQLIDFMLQHPILINRPIVVTPLGTRLCRPSEVVLDILQDAQKGAFTKDDGEKVVDEAGKRLK,Arsenate reductase,Involved in resistance to arsenate. Catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)]. The resulting arsenite is then extruded from the cell via the ArsAB transport system (Probable).,13-fold increase in catalytic efficiency with arsenate. Mutant is resistant at high arsenate concentrations. The functional changes caused by the mutation are not mentioned in the document.,13-fold increase in catalytic efficiency with arsenate. Mutant is resistant at high arsenate concentrations. The functional changes caused by the mutation are not mentioned in the document.
357,0,0,P32266-A824R,MNASPVRLLILRRQLATHPAILYSSPYIKSPLVHLHSRMSNVHRSAHANALSFVITRRSISHFPKIISKIIRLPIYVGGGMAAAGSYIAYKMEEASSFTKDKLDRIKDLGESMKEKFNKMFSGDKSQDGGHGNDGTVPTATLIAATSLDDDESKRQGDPKDDDDEDDDDEDDENDSVDTTQDEMLNLTKQMIEIRTILNKVDSSSAHLTLPSIVVIGSQSSGKSSVLESIVGREFLPKGSNMVTRRPIELTLVNTPNSNNVTADFPSMRLYNIKDFKEVKRMLMELNMAVPTSEAVSEEPIQLTIKSSRVPDLSLVDLPGYIQVEAADQPIELKTKIRDLCEKYLTAPNIILAISAADVDLANSSALKASKAADPKGLRTIGVITKLDLVDPEKARSILNNKKYPLSMGYVGVITKTPSSINRKHLGLFGEAPSSSLSGIFSKGQHGQSSGEENTNGLKQIVSHQFEKAYFKENKKYFTNCQVSTKKLREKLIKILEISMSNALEPTSTLIQQELDDTSYLFKVEFNDRHLTPKSYLLNNIDVLKLGIKEFQEKFHRNELKSILRAELDQKVLDVLATRYWKDDNLQDLSSSKLESDTDMLYWHKKLELASSGLTKMGIGRLSTMLTTNAILKELDNILESTQLKNHELIKDLVSNTAINVLNSKYYSTADQVENCIKPFKYEIDLEERDWSLARQHSINLIKEELRQCNSRYQAIKNAVGSKKLANVMGYLENESNLQKETLGMSKLLLERGSEAIFLDKRCKVLSFRLKMLKNKCHSTIEKDRCPEVFLSAVSDKLTSTAVLFLNVELLSDFFYNFPIELDRRLTLLGDEQVEMFAKEDPKISRHIELQKRKELLELALEKIDSILVFKKSYKGVSKNL,,-1.0,MNASPVRLLILRRQLATHPAILYSSPYIKSPLVHLHSRMSNVHRSAHANALSFVITRRSISHFPKIISKIIRLPIYVGGGMAAAGSYIAYKMEEASSFTKDKLDRIKDLGESMKEKFNKMFSGDKSQDGGHGNDGTVPTATLIAATSLDDDESKRQGDPKDDDDEDDDDEDDENDSVDTTQDEMLNLTKQMIEIRTILNKVDSSSAHLTLPSIVVIGSQSSGKSSVLESIVGREFLPKGSNMVTRRPIELTLVNTPNSNNVTADFPSMRLYNIKDFKEVKRMLMELNMAVPTSEAVSEEPIQLTIKSSRVPDLSLVDLPGYIQVEAADQPIELKTKIRDLCEKYLTAPNIILAISAADVDLANSSALKASKAADPKGLRTIGVITKLDLVDPEKARSILNNKKYPLSMGYVGVITKTPSSINRKHLGLFGEAPSSSLSGIFSKGQHGQSSGEENTNGLKQIVSHQFEKAYFKENKKYFTNCQVSTKKLREKLIKILEISMSNALEPTSTLIQQELDDTSYLFKVEFNDRHLTPKSYLLNNIDVLKLGIKEFQEKFHRNELKSILRAELDQKVLDVLATRYWKDDNLQDLSSSKLESDTDMLYWHKKLELASSGLTKMGIGRLSTMLTTNAILKELDNILESTQLKNHELIKDLVSNTAINVLNSKYYSTADQVENCIKPFKYEIDLEERDWSLARQHSINLIKEELRQCNSRYQAIKNAVGSKKLANVMGYLENESNLQKETLGMSKLLLERGSEAIFLDKRCKVLSFRLKMLKNKCHSTIEKDRCPEVFLSAVSDKLTSTAVLFLNVELLSDFFYNFPIELDARLTLLGDEQVEMFAKEDPKISRHIELQKRKELLELALEKIDSILVFKKSYKGVSKNL,"Dynamin-like GTPase MGM1, mitochondrial",Dynamin-related GTPase required for mitochondrial fusion. Coordinates interaction between the inner and outer mitochondrial membrane to promote the formation of the double membrane.,Gain of GED function.,Gain of GED function.
358,0,0,P9WGT3-A191T,MTATATEGAKPPFVSRSVLVTGGNRGIGLAIAQRLAADGHKVAVTHRGSGAPKGLFGVECDVTDSDAVDRAFTAVEEHQGPVEVLVSNAGLSADAFLMRMTEEKFEKVINANLTGAFRVAQRASRSMQRNKFGRMIFIGSVSGSWGIGNQANYAASKAGVIGMARSIARELSKANVTANVVAPGYIDTDMTRALDERIQQGALQFIPAKRVGTPAEVAGVVSFLASEDASYISGAVIPVDGGMGMGH,,-1.0,MTATATEGAKPPFVSRSVLVTGGNRGIGLAIAQRLAADGHKVAVTHRGSGAPKGLFGVECDVTDSDAVDRAFTAVEEHQGPVEVLVSNAGLSADAFLMRMTEEKFEKVINANLTGAFRVAQRASRSMQRNKFGRMIFIGSVSGSWGIGNQANYAASKAGVIGMARSIARELSKANVTANVVAPGYIDTDMARALDERIQQGALQFIPAKRVGTPAEVAGVVSFLASEDASYISGAVIPVDGGMGMGH,3-oxoacyl-[acyl-carrier-protein] reductase MabA,"Part of the mycobacterial fatty acid elongation system FAS-II, which is involved in mycolic acid biosynthesis. Catalyzes the NADPH-dependent reduction of beta-ketoacyl derivatives, the second step of the FAS-II elongation cycle. May preferentially metabolize long-chain substrates (C8-C20). Can use CoA derivatives as substrates in vitro.","Strong increase in wild-type reductase activity. Highly enhances phosphorylation by PknB. Presence of phosphorylation by PknB; when associated with A-21 and A-114. The MabA_T191A mutant, designed to mimic the mutation, exhibited significantly increased ketoacyl reductase activity compared with the wild-type protein, as well as improved binding of the NADPH cofactor.","Strong increase in wild-type reductase activity. Highly enhances phosphorylation by PknB. Presence of phosphorylation by PknB; when associated with A-21 and A-114. The MabA_T191A mutant, designed to mimic the mutation, exhibited significantly increased ketoacyl reductase activity compared with the wild-type protein, as well as improved binding of the NADPH cofactor."
359,0,0,Q9ULZ3-W13E,MGRARDAILDALENLTAEELKKFKLKLLSVPLREGYGRIPRGALLSMDALDLTDKLVSFYLETYGAELTANVLRDMGLQEMAGQLQAATHQGSGAAPAGIQAPPQSAAKPGLHFIDQHRAALIARVTNVEWLLDALYGKVLTDEQYQAVRAEPTNPSKMRKLFSFTPAWNWTCKDLLLQALRESQSYLVEDLERS,,-1.0,MGRARDAILDALWNLTAEELKKFKLKLLSVPLREGYGRIPRGALLSMDALDLTDKLVSFYLETYGAELTANVLRDMGLQEMAGQLQAATHQGSGAAPAGIQAPPQSAAKPGLHFIDQHRAALIARVTNVEWLLDALYGKVLTDEQYQAVRAEPTNPSKMRKLFSFTPAWNWTCKDLLLQALRESQSYLVEDLERS,Apoptosis-associated speck-like protein containing a CARD,"Functions as key mediator in apoptosis and inflammation. Promotes caspase-mediated apoptosis involving predominantly caspase-8 and also caspase-9 in a probable cell type-specific manner. Involved in activation of the mitochondrial apoptotic pathway, promotes caspase-8-dependent proteolytic maturation of BID independently of FADD in certain cell types and also mediates mitochondrial translocation of BAX and activates BAX-dependent apoptosis coupled to activation of caspase-9, -2 and -3. Involved in innate immune response by acting as an integral adapter in the assembly of various inflammasomes (NLRP1, NLRP2, NLRP3, NLRP6, AIM2 and probably IFI16) which recruit and activate caspase-1 leading to processing and secretion of pro-inflammatory cytokines. Caspase-1-dependent inflammation leads to macrophage pyroptosis, a form of cell death. The function as activating adapter in different types of inflammasomes is mediated by the pyrin and CARD domains and their homotypic interactions. Clustered PYCARD nucleates the formation of caspase-1 filaments through the interaction of their respective CARD domains, acting as a platform for of caspase-1 polymerization. In the NLRP1 and NLRC4 inflammasomes seems not be required but facilitates the processing of procaspase-1. In cooperation with NOD2 involved in an inflammasome activated by bacterial muramyl dipeptide leading to caspase-1 activation. May be involved in RIGI-triggered pro-inflammatory responses and inflammasome activation. In collaboration with AIM2 which detects cytosolic double-stranded DNA may also be involved in a caspase-1-independent cell death that involves caspase-8. In adaptive immunity may be involved in maturation of dendritic cells to stimulate T-cell immunity and in cytoskeletal rearrangements coupled to chemotaxis and antigen uptake may be involved in post-transcriptional regulation of the guanine nucleotide exchange factor DOCK2; the latter function is proposed to involve the nuclear form. Also involved in transcriptional activation of cytokines and chemokines independent of the inflammasome; this function may involve AP-1, NF-kappa-B, MAPK and caspase-8 signaling pathways. For regulation of NF-kappa-B activating and inhibiting functions have been reported. Modulates NF-kappa-B induction at the level of the IKK complex by inhibiting kinase activity of CHUK and IKBK. Proposed to compete with RIPK2 for association with CASP1 thereby down-regulating CASP1-mediated RIPK2-dependent NF-kappa-B activation and activating interleukin-1 beta processing. Modulates host resistance to DNA virus infection, probably by inducing the cleavage of and inactivating CGAS in presence of cytoplasmic double-stranded DNA.May have a regulating effect on the function as inflammasome adapter.Seems to inhibit inflammasome-mediated maturation of interleukin-1 beta.",Enables interaction with NLRP2.,Enables interaction with NLRP2.
360,0,0,P9WGT3-A114T,MTATATEGAKPPFVSRSVLVTGGNRGIGLAIAQRLAADGHKVAVTHRGSGAPKGLFGVECDVTDSDAVDRAFTAVEEHQGPVEVLVSNAGLSADAFLMRMTEEKFEKVINANLTGAFRVAQRASRSMQRNKFGRMIFIGSVSGSWGIGNQANYAASKAGVIGMARSIARELSKANVTANVVAPGYIDTDMTRALDERIQQGALQFIPAKRVGTPAEVAGVVSFLASEDASYISGAVIPVDGGMGMGH,,-1.0,MTATATEGAKPPFVSRSVLVTGGNRGIGLAIAQRLAADGHKVAVTHRGSGAPKGLFGVECDVTDSDAVDRAFTAVEEHQGPVEVLVSNAGLSADAFLMRMTEEKFEKVINANLAGAFRVAQRASRSMQRNKFGRMIFIGSVSGSWGIGNQANYAASKAGVIGMARSIARELSKANVTANVVAPGYIDTDMTRALDERIQQGALQFIPAKRVGTPAEVAGVVSFLASEDASYISGAVIPVDGGMGMGH,3-oxoacyl-[acyl-carrier-protein] reductase MabA,"Part of the mycobacterial fatty acid elongation system FAS-II, which is involved in mycolic acid biosynthesis. Catalyzes the NADPH-dependent reduction of beta-ketoacyl derivatives, the second step of the FAS-II elongation cycle. May preferentially metabolize long-chain substrates (C8-C20). Can use CoA derivatives as substrates in vitro.",Slight increase in phosphorylation by PknB. Presence of phosphorylation by PknB; when associated with A-21 and A-191.,Slight increase in phosphorylation by PknB. Presence of phosphorylation by PknB; when associated with A-21 and A-191.
361,0,0,Q6UWV6-Q121N,MRGPAVLLTVALATLLAPGAGAPVQSQGSQNKLLLVSFDGFRWNYDQDVDTPNLDAMARDGVKARYMTPAFVTMTSPCHFTLVTGKYIENHGVVHNMYYNTTSKVKLPYHATLGIQRWWDNGSVPIWITAQRQGLRAGSFFYPGGNVTYQGVAVTRSRKEGIAHNYKNETEWRANIDTVMAWFTEEDLDLVTLYFGEPDSTGHRYGPESPERREMVRQVDRTVGYLRESIARNHLTDRLNLIITSDHGMTTVDKRAGDLVEFHKFPNFTFRDIEFELLDYGPNGMLLPKEGRLEKVYDALKDAHPKLHVYKKEAFPEAFHYANNPRVTPLLMYSDLGYVIHGRINVQFNNGEHGFDNKDMDMKTIFRAVGPSFRAGLEVEPFESVHVYELMCRLLGIVPEANDGHLATLLPMLHTESALPPDGRPTLLPKGRSALPPSSRPLLVMGLLGTVILLSEVA,,-1.0,MRGPAVLLTVALATLLAPGAGAPVQSQGSQNKLLLVSFDGFRWNYDQDVDTPNLDAMARDGVKARYMTPAFVTMTSPCHFTLVTGKYIENHGVVHNMYYNTTSKVKLPYHATLGIQRWWDQGSVPIWITAQRQGLRAGSFFYPGGNVTYQGVAVTRSRKEGIAHNYKNETEWRANIDTVMAWFTEEDLDLVTLYFGEPDSTGHRYGPESPERREMVRQVDRTVGYLRESIARNHLTDRLNLIITSDHGMTTVDKRAGDLVEFHKFPNFTFRDIEFELLDYGPNGMLLPKEGRLEKVYDALKDAHPKLHVYKKEAFPEAFHYANNPRVTPLLMYSDLGYVIHGRINVQFNNGEHGFDNKDMDMKTIFRAVGPSFRAGLEVEPFESVHVYELMCRLLGIVPEANDGHLATLLPMLHTESALPPDGRPTLLPKGRSALPPSSRPLLVMGLLGTVILLSEVA,Ectonucleotide pyrophosphatase/phosphodiesterase family member 7,"Choline-specific phosphodiesterase that hydrolyzes sphingomyelin releasing the ceramide and phosphocholine and therefore is involved in sphingomyelin digestion, ceramide formation, and fatty acid (FA) absorption in the gastrointestinal tract. Has also phospholipase C activity and can also cleave phosphocholine from palmitoyl lyso-phosphatidylcholine and platelet-activating factor (PAF) leading to its inactivation. Does not have nucleotide pyrophosphatase activity. May promote cholesterol absorption by affecting the levels of sphingomyelin derived from either diet or endogenous sources, in the intestinal lumen.",Strongly enhances N-glycosylation and enzyme activity; when associated with Q-100; Q-146; Q-168 and Q-267. The mutation in alk-SMase significantly improves its activity.,Strongly enhances N-glycosylation and enzyme activity; when associated with Q-100; Q-146; Q-168 and Q-267. The mutation in alk-SMase significantly improves its activity.
362,0,0,P06022-N114I,MQHDLFEHDPAIRQLIGHIDNIPAPELESRWPRSVVDLIDVLENELKRQNVSNPRELARKQAVALSCFLGGRQFYIPCGDTILTALRDDLLYCQFNGRNMEELRRQYRLSQPQIYQIIARQRKLHTRRHQPDLFSPETPK,,-1.0,MQHDLFEHDPAIRQLIGHIDNIPAPELESRWPRSVVDLIDVLENELKRQNVSNPRELARKQAVALSCFLGGRQFYIPCGDTILTALRDDLLYCQFNGRNMEELRRQYRLSQPQNYQIIARQRKLHTRRHQPDLFSPETPK,Late transcription activator C,"Positive regulator of viral late genes transcription. Responsible for the transition from middle to late gene expression. Activates the Plys, PI, PP and Pmom late promoters thereby allowing the expression of viral endolysin and structural genes. Activates Pmom promoter by unwinding the DNA, thus realigning the promoter elements and recruiting the RNAP.",Enhancement of DNA-binding activity. The mutant protein showed an increased ability to activate the P(lys)-galK fusion.,Enhancement of DNA-binding activity. The mutant protein showed an increased ability to activate the P(lys)-galK fusion.
363,0,0,Q6UWV6-N78C,MRGPAVLLTVALATLLAPGAGAPVQSQGSQNKLLLVSFDGFRWNYDQDVDTPNLDAMARDGVKARYMTPAFVTMTSPCHFTLVTGKYIENHGVVHNMYYNTTSKVKLPYHATLGIQRWWDNGSVPIWITAQRQGLRAGSFFYPGGNVTYQGVAVTRSRKEGIAHNYKNETEWRANIDTVMAWFTEEDLDLVTLYFGEPDSTGHRYGPESPERREMVRQVDRTVGYLRESIARNHLTDRLNLIITSDHGMTTVDKRAGDLVEFHKFPNFTFRDIEFELLDYGPNGMLLPKEGRLEKVYDALKDAHPKLHVYKKEAFPEAFHYANNPRVTPLLMYSDLGYVIHGRINVQFNNGEHGFDNKDMDMKTIFRAVGPSFRAGLEVEPFESVHVYELMCRLLGIVPEANDGHLATLLPMLHTESALPPDGRPTLLPKGRSALPPSSRPLLVMGLLGTVILLSEVA,,-1.0,MRGPAVLLTVALATLLAPGAGAPVQSQGSQNKLLLVSFDGFRWNYDQDVDTPNLDAMARDGVKARYMTPAFVTMTSPNHFTLVTGKYIENHGVVHNMYYNTTSKVKLPYHATLGIQRWWDNGSVPIWITAQRQGLRAGSFFYPGGNVTYQGVAVTRSRKEGIAHNYKNETEWRANIDTVMAWFTEEDLDLVTLYFGEPDSTGHRYGPESPERREMVRQVDRTVGYLRESIARNHLTDRLNLIITSDHGMTTVDKRAGDLVEFHKFPNFTFRDIEFELLDYGPNGMLLPKEGRLEKVYDALKDAHPKLHVYKKEAFPEAFHYANNPRVTPLLMYSDLGYVIHGRINVQFNNGEHGFDNKDMDMKTIFRAVGPSFRAGLEVEPFESVHVYELMCRLLGIVPEANDGHLATLLPMLHTESALPPDGRPTLLPKGRSALPPSSRPLLVMGLLGTVILLSEVA,Ectonucleotide pyrophosphatase/phosphodiesterase family member 7,"Choline-specific phosphodiesterase that hydrolyzes sphingomyelin releasing the ceramide and phosphocholine and therefore is involved in sphingomyelin digestion, ceramide formation, and fatty acid (FA) absorption in the gastrointestinal tract. Has also phospholipase C activity and can also cleave phosphocholine from palmitoyl lyso-phosphatidylcholine and platelet-activating factor (PAF) leading to its inactivation. Does not have nucleotide pyrophosphatase activity. May promote cholesterol absorption by affecting the levels of sphingomyelin derived from either diet or endogenous sources, in the intestinal lumen.",Significantly increases activity.,Significantly increases activity.
364,0,0,Q9NZK5-G362W,MLVDGPSERPALCFLLLAVAMSFFGSALSIDETRAHLLLKEKMMRLGGRLVLNTKEELANERLMTLKIAEMKEAMRTLIFPPSMHFFQAKHLIERSQVFNILRMMPKGAALHLHDIGIVTMDWLVRNVTYRPHCHICFTPRGIMQFRFAHPTPRPSEKCSKWILLEDYRKRVQNVTEFDDSLLRNFTLVTQHPEVIYTNQNVVWSKFETIFFTISGLIHYAPVFRDYVFRSMQEFYEDNVLYMEIRARLLPVYELSGEHHDEEWSVKTYQEVAQKFVETHPEFIGIKIIYSDHRSKDVAVIAESIRMAMGLRIKFPTVVAGFDLVGHEDTGHSLHDYKEALMIPAKDGVKLPYFFHAGETDWQGTSIDRNILDALMLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLVSDLRNHPVATLMATGHPMVISSDDPAMFGAKGLSYDFYEVFMGIGGMKADLRTLKQLAMNSIKYSTLLESEKNTFMEIWKKRWDKFIADVATK,,-1.0,MLVDGPSERPALCFLLLAVAMSFFGSALSIDETRAHLLLKEKMMRLGGRLVLNTKEELANERLMTLKIAEMKEAMRTLIFPPSMHFFQAKHLIERSQVFNILRMMPKGAALHLHDIGIVTMDWLVRNVTYRPHCHICFTPRGIMQFRFAHPTPRPSEKCSKWILLEDYRKRVQNVTEFDDSLLRNFTLVTQHPEVIYTNQNVVWSKFETIFFTISGLIHYAPVFRDYVFRSMQEFYEDNVLYMEIRARLLPVYELSGEHHDEEWSVKTYQEVAQKFVETHPEFIGIKIIYSDHRSKDVAVIAESIRMAMGLRIKFPTVVAGFDLVGHEDTGHSLHDYKEALMIPAKDGVKLPYFFHAGETDGQGTSIDRNILDALMLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLVSDLRNHPVATLMATGHPMVISSDDPAMFGAKGLSYDFYEVFMGIGGMKADLRTLKQLAMNSIKYSTLLESEKNTFMEIWKKRWDKFIADVATK,Adenosine deaminase 2,"Adenosine deaminase that may contribute to the degradation of extracellular adenosine, a signaling molecule that controls a variety of cellular responses. Requires elevated adenosine levels for optimal enzyme activity. Binds to cell surfaces via proteoglycans and may play a role in the regulation of cell proliferation and differentiation, independently of its enzyme activity.","Increases dimerization and enzyme activity. The crystal structures of ADA2 and ADA2 bound to a transition state analogue presented here reveal the structural basis of the catalytic/signaling activity of ADGF/ADA2 proteins. In addition to the catalytic domain, the structures discovered two ADGF/ADA2-specific domains of novel folds that mediate the protein dimerization and binding to the cell surface receptors. This complex architecture is in sharp contrast with that of monomeric single domain ADA1. An extensive glycosylation and the presence of a conserved disulfide bond and a signal peptide in ADA2 strongly suggest that ADA2, in contrast to ADA1, is specifically designed to act in the extracellular environment. The comparison of catalytic sites of ADA2 and ADA1 demonstrates large differences in the arrangement of the substrate-binding pockets. These structural differences explain the substrate and inhibitor specificity of adenosine deaminases and provide the basis for a rational design of ADA2-targeting drugs to modulate the immune system responses in pathophysiological conditions.","Increases dimerization and enzyme activity. The crystal structures of ADA2 and ADA2 bound to a transition state analogue presented here reveal the structural basis of the catalytic/signaling activity of ADGF/ADA2 proteins. In addition to the catalytic domain, the structures discovered two ADGF/ADA2-specific domains of novel folds that mediate the protein dimerization and binding to the cell surface receptors. This complex architecture is in sharp contrast with that of monomeric single domain ADA1. An extensive glycosylation and the presence of a conserved disulfide bond and a signal peptide in ADA2 strongly suggest that ADA2, in contrast to ADA1, is specifically designed to act in the extracellular environment. The comparison of catalytic sites of ADA2 and ADA1 demonstrates large differences in the arrangement of the substrate-binding pockets. These structural differences explain the substrate and inhibitor specificity of adenosine deaminases and provide the basis for a rational design of ADA2-targeting drugs to modulate the immune system responses in pathophysiological conditions."
365,0,0,P9WGT3-V60C,MTATATEGAKPPFVSRSVLVTGGNRGIGLAIAQRLAADGHKVAVTHRGSGAPKGLFGVECDVTDSDAVDRAFTAVEEHQGPVEVLVSNAGLSADAFLMRMTEEKFEKVINANLTGAFRVAQRASRSMQRNKFGRMIFIGSVSGSWGIGNQANYAASKAGVIGMARSIARELSKANVTANVVAPGYIDTDMTRALDERIQQGALQFIPAKRVGTPAEVAGVVSFLASEDASYISGAVIPVDGGMGMGH,,-1.0,MTATATEGAKPPFVSRSVLVTGGNRGIGLAIAQRLAADGHKVAVTHRGSGAPKGLFGVEVDVTDSDAVDRAFTAVEEHQGPVEVLVSNAGLSADAFLMRMTEEKFEKVINANLTGAFRVAQRASRSMQRNKFGRMIFIGSVSGSWGIGNQANYAASKAGVIGMARSIARELSKANVTANVVAPGYIDTDMTRALDERIQQGALQFIPAKRVGTPAEVAGVVSFLASEDASYISGAVIPVDGGMGMGH,3-oxoacyl-[acyl-carrier-protein] reductase MabA,"Part of the mycobacterial fatty acid elongation system FAS-II, which is involved in mycolic acid biosynthesis. Catalyzes the NADPH-dependent reduction of beta-ketoacyl derivatives, the second step of the FAS-II elongation cycle. May preferentially metabolize long-chain substrates (C8-C20). Can use CoA derivatives as substrates in vitro.",Displays a higher activity than the wild-type and a slightly increased affinity for the cofactor. Enhances 84% of activity; when associated with L-144. Fully active; when associated with A-139 and L-144.,Displays a higher activity than the wild-type and a slightly increased affinity for the cofactor. Enhances 84% of activity; when associated with L-144. Fully active; when associated with A-139 and L-144.
366,0,0,P06022-R83L,MQHDLFEHDPAIRQLIGHIDNIPAPELESRWPRSVVDLIDVLENELKRQNVSNPRELARKQAVALSCFLGGRQFYIPCGDTILTALRDDLLYCQFNGRNMEELRRQYRLSQPQIYQIIARQRKLHTRRHQPDLFSPETPK,,-1.0,MQHDLFEHDPAIRQLIGHIDNIPAPELESRWPRSVVDLIDVLENELKRQNVSNPRELARKQAVALSCFLGGRQFYIPCGDTIRTALRDDLLYCQFNGRNMEELRRQYRLSQPQIYQIIARQRKLHTRRHQPDLFSPETPK,Late transcription activator C,"Positive regulator of viral late genes transcription. Responsible for the transition from middle to late gene expression. Activates the Plys, PI, PP and Pmom late promoters thereby allowing the expression of viral endolysin and structural genes. Activates Pmom promoter by unwinding the DNA, thus realigning the promoter elements and recruiting the RNAP.","Decrease in dimerization and DNA binding. Complete gain of dimerization and DNA-binding when associated with Ser-90. The mutation in the C protein leads to a functional preservation in dimerization. Site-directed mutational analysis revealed that the amino-terminal coiled coil region is not the dimerization determinant, but the leucine zipper motif located in the middle region of the protein plays a role in dimerization.","Decrease in dimerization and DNA binding. Complete gain of dimerization and DNA-binding when associated with Ser-90. The mutation in the C protein leads to a functional preservation in dimerization. Site-directed mutational analysis revealed that the amino-terminal coiled coil region is not the dimerization determinant, but the leucine zipper motif located in the middle region of the protein plays a role in dimerization."
367,0,0,O15393-A441S,MALNSGSPPAIGPYYENHGYQPENPYPAQPTVVPTVYEVHPAQYYPSPVPQYAPRVLTQASNPVVCTQPKSPSGTVCTSKTKKALCITLTLGTFLVGAALAAGLLWKFMGSKCSNSGIECDSSGTCINPSNWCDGVSHCPGGEDENRCVRLYGPNFILQVYSSQRKSWHPVCQDDWNENYGRAACRDMGYKNNFYSSQGIVDDSGSTSFMKLNTSAGNVDIYKKLYHSDACSSKAVVSLRCIACGVNLNSSRQSRIVGGESALPGAWPWQVSLHVQNVHVCGGSIITPEWIVTAAHCVEKPLNNPWHWTAFAGILRQSFMFYGAGYQVEKVISHPNYDSKTKNNDIALMKLQKPLTFNDLVKPVCLPNPGMMLQPEQLCWISGWGATEEKGKTSEVLNAAKVLLIETQRCNSRYVYDNLITPAMICAGFLQGNVDSCQGDSGGPLVTSKNNIWWLIGDTSWGSGCAKAYRPGVYGNVMVFTDWIYRQMRADG,,-1.0,MALNSGSPPAIGPYYENHGYQPENPYPAQPTVVPTVYEVHPAQYYPSPVPQYAPRVLTQASNPVVCTQPKSPSGTVCTSKTKKALCITLTLGTFLVGAALAAGLLWKFMGSKCSNSGIECDSSGTCINPSNWCDGVSHCPGGEDENRCVRLYGPNFILQVYSSQRKSWHPVCQDDWNENYGRAACRDMGYKNNFYSSQGIVDDSGSTSFMKLNTSAGNVDIYKKLYHSDACSSKAVVSLRCIACGVNLNSSRQSRIVGGESALPGAWPWQVSLHVQNVHVCGGSIITPEWIVTAAHCVEKPLNNPWHWTAFAGILRQSFMFYGAGYQVEKVISHPNYDSKTKNNDIALMKLQKPLTFNDLVKPVCLPNPGMMLQPEQLCWISGWGATEEKGKTSEVLNAAKVLLIETQRCNSRYVYDNLITPAMICAGFLQGNVDSCQGDAGGPLVTSKNNIWWLIGDTSWGSGCAKAYRPGVYGNVMVFTDWIYRQMRADG,Transmembrane protease serine 2,"Plasma membrane-anchored serine protease that cleaves at arginine residues. Participates in proteolytic cascades of relevance for the normal physiologic function of the prostate. Androgen-induced TMPRSS2 activates several substrates that include pro-hepatocyte growth factor/HGF, the protease activated receptor-2/F2RL1 or matriptase/ST14 leading to extracellular matrix disruption and metastasis of prostate cancer cells. In addition, activates trigeminal neurons and contribute to both spontaneous pain and mechanical allodynia.(Microbial infection) Facilitates human coronaviruses SARS-CoV and SARS-CoV-2 infections via two independent mechanisms, proteolytic cleavage of ACE2 receptor which promotes viral uptake, and cleavage of coronavirus spike glycoproteins which activates the glycoprotein for host cell entry. The cleavage of SARS-COV2 spike glycoprotein occurs between the S2 and S2' site. Upon SARS-CoV-2 infection, increases syncytia formation by accelerating the fusion process. Proteolytically cleaves and activates the spike glycoproteins of human coronavirus 229E (HCoV-229E) and human coronavirus EMC (HCoV-EMC) and the fusion glycoproteins F0 of Sendai virus (SeV), human metapneumovirus (HMPV), human parainfluenza 1, 2, 3, 4a and 4b viruses (HPIV). Essential for spread and pathogenesis of influenza A virus (strains H1N1, H3N2 and H7N9); involved in proteolytic cleavage and activation of hemagglutinin (HA) protein which is essential for viral infectivity.","Gain of activity. Mutation of S-441 in the catalytic triad shows that the proteolytic cleavage is dependent on catalytic activity, suggesting that it occurs as a result of autocleavage.","Gain of activity. Mutation of S-441 in the catalytic triad shows that the proteolytic cleavage is dependent on catalytic activity, suggesting that it occurs as a result of autocleavage."
368,0,0,Q1PEI6-T347I,MEFSCVHFLQNKTILVTGATGFLAKVFVEKILRVQPNVNKLYLVVRASDNEAATKRLRTEAFEKDLFKVLRDNLGDEKLNTLLSEKVVPVAGDIAMDHLGMKDSNLRERMQKEIDIVVNVAATTNFDERYDIGLGINTFGALNVLNFAKKCVKAQLLLHVSTAYVCGEKPGLLPEKPFVMEEICNENGLQLDINLERELMKQRLKELNEQGCSEEGTTFYMKELGMERAKLHGWPNTYVFTKSMGEMLLGNHKENLPLVIIRPTMITSTLFEPFPGWIEGLRTVDSVIIAYGKGVLKCFLVDVNSVCDMIPADMVANAMIAAAATHAGGSKVHMVYQVGSSHQNPIIYGEIREILFCYFTKNSLRSRNGSMITVSKMKLIPTLALFSLYMTIRYKLPVQLLKLVDIIYPSREGDEYKNKNRKIDMVMRLVKLYEPYVLFKGIFDDRNTKNLCAKQKEEDNRNSENFMFDFDPKIIKWKDYLINVHIPGLITHVLKK,,-1.0,MEFSCVHFLQNKTILVTGATGFLAKVFVEKILRVQPNVNKLYLVVRASDNEAATKRLRTEAFEKDLFKVLRDNLGDEKLNTLLSEKVVPVAGDIAMDHLGMKDSNLRERMQKEIDIVVNVAATTNFDERYDIGLGINTFGALNVLNFAKKCVKAQLLLHVSTAYVCGEKPGLLPEKPFVMEEICNENGLQLDINLERELMKQRLKELNEQGCSEEGTTFYMKELGMERAKLHGWPNTYVFTKSMGEMLLGNHKENLPLVIIRPTMITSTLFEPFPGWIEGLRTVDSVIIAYGKGVLKCFLVDVNSVCDMIPADMVANAMIAAAATHAGGSKVHMVYQVGSSHQNPITYGEIREILFCYFTKNSLRSRNGSMITVSKMKLIPTLALFSLYMTIRYKLPVQLLKLVDIIYPSREGDEYKNKNRKIDMVMRLVKLYEPYVLFKGIFDDRNTKNLCAKQKEEDNRNSENFMFDFDPKIIKWKDYLINVHIPGLITHVLKK,Fatty acyl-CoA reductase 8,Catalyzes the reduction of fatty acyl-CoA to fatty alcohols. Catalyzes specifically the formation of C16:0 fatty alcohol.,Decreases protein stability and enzymatic activity. Catalyzes the formation of C18:0 fatty alcohol instead of C16:0; when associated with A-355 and V-377.,Decreases protein stability and enzymatic activity. Catalyzes the formation of C18:0 fatty alcohol instead of C16:0; when associated with A-355 and V-377.
369,0,0,P08692-D130E,MSNITIYHNPACGTSRNTLEMIRNSGTEPTIILYLENPPSRDELVKLIADMGISVRALLRKNVEPYEQLGLAEDKFTDDQLIDFMLQHPILINRPIVVTPLGTRLCRPSEVVLDILQDAQKGAFTKEDGEKVVDEAGKRLK,,-1.0,MSNITIYHNPACGTSRNTLEMIRNSGTEPTIILYLENPPSRDELVKLIADMGISVRALLRKNVEPYEQLGLAEDKFTDDQLIDFMLQHPILINRPIVVTPLGTRLCRPSEVVLDILQDAQKGAFTKEDGDKVVDEAGKRLK,Arsenate reductase,Involved in resistance to arsenate. Catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)]. The resulting arsenite is then extruded from the cell via the ArsAB transport system (Probable).,"5-fold increase in catalytic efficiency with arsenate. Mutant is relatively sensitive to arsenate, but is more resistant at higher concentrations.","5-fold increase in catalytic efficiency with arsenate. Mutant is relatively sensitive to arsenate, but is more resistant at higher concentrations."
370,0,0,Q9UPT6-C578R,MMEIQMDEGGGVVVYQDDYCSGSVMSERVSGLAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEERESEMKKEYNALHQRHTEMIQTYVEHIERSKMQQVGGNSQTESSLPGRRKERPTSLNVFPLADGTVRAQIGGKLVPAGDHWHLSDLGQLQSSSSYQCPQDEMSESGQSSAAATPSTTGTKSNTPTSSVPSAAVTPLNESLQPLGDYGVGSKNSKRAREKRDSRNMEVQVTQEMRNVSIGMGSSDEWSDVQDIIDSTPELDMCPETRLDRTGSSPTQGIVNKAFGINTDSLYHELSTAGSEVIGDVDEGADLLGEFSVRDDFFGMGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEAIIARREPKEEAEDVSSYLCTESDKIPMAQRRRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASREHPSVQEKKKSTIWQFFSRLFSSSSSPPPAKRPYPSVNIHYKSPTTAGFSQRRNHAMCPISAGSRPLEFFPDDDCTSSARREQKREQYRQVREHVRNDDGRLQACGWSLPAKYKQLSPNGGQEDTRMKNVPVPVYCRPLVEKDPTMKLWCAAGVNLSGWRPNEDDAGNGVKPAPGRDPLTCDREGDGEPKSAHTSPEKKKAKELPEMDATSSRVWILTSTLTTSKVVIIDANQPGTVVDQFTVCNAHVLCISSIPAASDSDYPPGEMFLDSDVNPEDPGADGVLAGITLVGCATRCNVPRSNCSSRGDTPVLDKGQGEVATIANGKVNPSQSTEEATEATEVPDPGPSEPETATLRPGPLTEHVFTDPAPTPSSGPQPGSENGPEPDSSSTRPEPEPSGDPTGAGSSAAPTMWLGAQNGWLYVHSAVANWKKCLHSIKLKDSVLSLVHVKGRVLVALADGTLAIF,,-1.0,MMEIQMDEGGGVVVYQDDYCSGSVMSERVSGLAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEERESEMKKEYNALHQRHTEMIQTYVEHIERSKMQQVGGNSQTESSLPGRRKERPTSLNVFPLADGTVRAQIGGKLVPAGDHWHLSDLGQLQSSSSYQCPQDEMSESGQSSAAATPSTTGTKSNTPTSSVPSAAVTPLNESLQPLGDYGVGSKNSKRAREKRDSRNMEVQVTQEMRNVSIGMGSSDEWSDVQDIIDSTPELDMCPETRLDRTGSSPTQGIVNKAFGINTDSLYHELSTAGSEVIGDVDEGADLLGEFSVRDDFFGMGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEAIIARREPKEEAEDVSSYLCTESDKIPMAQRRRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASREHPSVQEKKKSTIWQFFSCLFSSSSSPPPAKRPYPSVNIHYKSPTTAGFSQRRNHAMCPISAGSRPLEFFPDDDCTSSARREQKREQYRQVREHVRNDDGRLQACGWSLPAKYKQLSPNGGQEDTRMKNVPVPVYCRPLVEKDPTMKLWCAAGVNLSGWRPNEDDAGNGVKPAPGRDPLTCDREGDGEPKSAHTSPEKKKAKELPEMDATSSRVWILTSTLTTSKVVIIDANQPGTVVDQFTVCNAHVLCISSIPAASDSDYPPGEMFLDSDVNPEDPGADGVLAGITLVGCATRCNVPRSNCSSRGDTPVLDKGQGEVATIANGKVNPSQSTEEATEATEVPDPGPSEPETATLRPGPLTEHVFTDPAPTPSSGPQPGSENGPEPDSSSTRPEPEPSGDPTGAGSSAAPTMWLGAQNGWLYVHSAVANWKKCLHSIKLKDSVLSLVHVKGRVLVALADGTLAIF,C-Jun-amino-terminal kinase-interacting protein 3,"The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. May function as a regulator of vesicle transport, through interactions with the JNK-signaling components and motor proteins. Promotes neuronal axon elongation in a kinesin- and JNK-dependent manner. Activates cofilin at axon tips via local activation of JNK, thereby regulating filopodial dynamics and enhancing axon elongation. Its binding to kinesin heavy chains (KHC), promotes kinesin-1 motility along microtubules and is essential for axon elongation and regeneration. Regulates cortical neuronal migration by mediating NTRK2/TRKB anterograde axonal transport during brain development. Acts as an adapter that bridges the interaction between NTRK2/TRKB and KLC1 and drives NTRK2/TRKB axonal but not dendritic anterograde transport, which is essential for subsequent BDNF-triggered signaling and filopodia formation.","Promotes axon development when expressed in a heterologous system. The inherited variant in MAPK8IP3 has been identified in individuals presenting with an overlapping phenotype of mild to severe intellectual disability. Brain anomalies such as perisylvian polymicrogyria, cerebral or cerebellar atrophy, and hypoplasia of the corpus callosum were consistent among individuals harboring this variant. The core phenotype includes spastic diplegia, intellectual disability, cerebral atrophy, and corpus callosum hypoplasia. Zebrafish embryos overexpressing human mutant JIP3 showed normal axon development of the posterior lateral line nerve, suggesting a beneficial effect on the developing axons. Our results suggest that MAPK8IP3 variants cause a neurodevelopmental disease.","Promotes axon development when expressed in a heterologous system. The inherited variant in MAPK8IP3 has been identified in individuals presenting with an overlapping phenotype of mild to severe intellectual disability. Brain anomalies such as perisylvian polymicrogyria, cerebral or cerebellar atrophy, and hypoplasia of the corpus callosum were consistent among individuals harboring this variant. The core phenotype includes spastic diplegia, intellectual disability, cerebral atrophy, and corpus callosum hypoplasia. Zebrafish embryos overexpressing human mutant JIP3 showed normal axon development of the posterior lateral line nerve, suggesting a beneficial effect on the developing axons. Our results suggest that MAPK8IP3 variants cause a neurodevelopmental disease."
371,0,0,O14746-T716A,MPRAPRCRAVRSLLRSHYREVLPLATFVRRLGPQGWRLVQRGDPAAFRALVAQCLVCVPWDARPPPAAPSFRQVSCLKELVARVLQRLCERGAKNVLAFGFALLDGARGGPPEAFTTSVRSYLPNTVTDALRGSGAWGLLLRRVGDDVLVHLLARCALFVLVAPSCAYQVCGPPLYQLGAATQARPPPHASGPRRRLGCERAWNHSVREAGVPLGLPAPGARRRGGSASRSLPLPKRPRRGAAPEPERTPVGQGSWAHPGRTRGPSDRGFCVVSPARPAEEATSLEGALSGTRHSHPSVGRQHHAGPPSTSRPPRPWDTPCPPVYAETKHFLYSSGDKEQLRPSFLLSSLRPSLTGARRLVETIFLGSRPWMPGTPRRLPRLPQRYWQMRPLFLELLGNHAQCPYGVLLKTHCPLRAAVTPAAGVCAREKPQGSVAAPEEEDTDPRRLVQLLRQHSSPWQVYGFVRACLRRLVPPGLWGSRHNERRFLRNTKKFISLGKHAKLSLQELTWKMSVRDCAWLRRSPGVGCVPAAEHRLREEILAKFLHWLMSVYVVELLRSFFYVTETTFQKNRLFFYRKSVWSKLQSIGIRQHLKRVQLRELSEAEVRQHREARPALLTSRLRFIPKPDGLRPIVNMDYVVGARTFRREKRAERLTSRVKALFSVLNYERARRPGLLGASVLGLDDIHRAWRTFVLRVRAQDPPPELYFVKVDVTGAYDTIPQDRLTEVIASIIKPQNTYCVRRYAVVQKAAHGHVRKAFKSHVSTLTDLQPYMRQFVAHLQETSPLRDAVVIEQSSSLNEASSGLFDVFLRFMCHHAVRIRGKSYVQCQGIPQGSILSTLLCSLCYGDMENKLFAGIRRDGLLLRLVDDFLLVTPHLTHAKTFLRTLVRGVPEYGCVVNLRKTVVNFPVEDEALGGTAFVQMPAHGLFPWCGLLLDTRTLEVQSDYSSYARTSIRASLTFNRGFKAGRNMRRKLFGVLRLKCHSLFLDLQVNSLQTVCTNIYKILLLQAYRFHACVLQLPFHQQ,,-1.0,MPRAPRCRAVRSLLRSHYREVLPLATFVRRLGPQGWRLVQRGDPAAFRALVAQCLVCVPWDARPPPAAPSFRQVSCLKELVARVLQRLCERGAKNVLAFGFALLDGARGGPPEAFTTSVRSYLPNTVTDALRGSGAWGLLLRRVGDDVLVHLLARCALFVLVAPSCAYQVCGPPLYQLGAATQARPPPHASGPRRRLGCERAWNHSVREAGVPLGLPAPGARRRGGSASRSLPLPKRPRRGAAPEPERTPVGQGSWAHPGRTRGPSDRGFCVVSPARPAEEATSLEGALSGTRHSHPSVGRQHHAGPPSTSRPPRPWDTPCPPVYAETKHFLYSSGDKEQLRPSFLLSSLRPSLTGARRLVETIFLGSRPWMPGTPRRLPRLPQRYWQMRPLFLELLGNHAQCPYGVLLKTHCPLRAAVTPAAGVCAREKPQGSVAAPEEEDTDPRRLVQLLRQHSSPWQVYGFVRACLRRLVPPGLWGSRHNERRFLRNTKKFISLGKHAKLSLQELTWKMSVRDCAWLRRSPGVGCVPAAEHRLREEILAKFLHWLMSVYVVELLRSFFYVTETTFQKNRLFFYRKSVWSKLQSIGIRQHLKRVQLRELSEAEVRQHREARPALLTSRLRFIPKPDGLRPIVNMDYVVGARTFRREKRAERLTSRVKALFSVLNYERARRPGLLGASVLGLDDIHRAWRTFVLRVRAQDPPPELYFVKVDVTGTYDTIPQDRLTEVIASIIKPQNTYCVRRYAVVQKAAHGHVRKAFKSHVSTLTDLQPYMRQFVAHLQETSPLRDAVVIEQSSSLNEASSGLFDVFLRFMCHHAVRIRGKSYVQCQGIPQGSILSTLLCSLCYGDMENKLFAGIRRDGLLLRLVDDFLLVTPHLTHAKTFLRTLVRGVPEYGCVVNLRKTVVNFPVEDEALGGTAFVQMPAHGLFPWCGLLLDTRTLEVQSDYSSYARTSIRASLTFNRGFKAGRNMRRKLFGVLRLKCHSLFLDLQVNSLQTVCTNIYKILLLQAYRFHACVLQLPFHQQ,Telomerase reverse transcriptase,"Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. Active in progenitor and cancer cells. Inactive, or very low activity, in normal somatic cells. Catalytic component of the teleromerase holoenzyme complex whose main activity is the elongation of telomeres by acting as a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme. Catalyzes the RNA-dependent extension of 3'-chromosomal termini with the 6-nucleotide telomeric repeat unit, 5'-TTAGGG-3'. The catalytic cycle involves primer binding, primer extension and release of product once the template boundary has been reached or nascent product translocation followed by further extension. More active on substrates containing 2 or 3 telomeric repeats. Telomerase activity is regulated by a number of factors including telomerase complex-associated proteins, chaperones and polypeptide modifiers. Modulates Wnt signaling. Plays important roles in aging and antiapoptosis.",Decrease in PFBMFT1; the mutant protein is demonstrated to cause severely enhanced telomerase activity.,Decrease in PFBMFT1; the mutant protein is demonstrated to cause severely enhanced telomerase activity.
372,0,0,Q94AN2-E247G,MRGPLGAVIGRYTSSDGSAPNDGIIKHNRKCRDITFLIIFIAFWVSMIVNSSFGFNQGNPLRLTYGLDYEGNVCGSKHRHRDLTQLELRYWLNPNQVYESGLKDGELKLANARTICLLDCPAPSDDTLNWVCDYPDGEIRLKMNDWIDRNYDYFEFLTPEMRNSSLQLQGPCYPVIFPSVNVYWSCQYIARASNSSLRHWQQMGGVNIQEDMIIDKSIRRSMNSRASVLKRYVADIGKSWPVLIVCGGLVPLFLSIIWLLLIRHFVAAMPWITVVLFNMLLISVTVFYYLKAGWIGNDAVTPIIGEHDPYFHVYGRELTHVRGVAILMTFISVVAILTSIAIIRRILMATSVLKVAAKVIGEVQALIIFPAIPFAMLAIFYMFWISAALHLFSSGQVVQNNCNNTNCCAYDLVLKKVNCDRCCGYSIHYTPHITIAIFFHLFGCYWATQFFIASSATVIAGSVASYYWAQGEASPEIPFLPVFASMKRLARYNLGSVALGSLIVSFVESVRFILEAIRRKTKVSGTIPDHWFWRMAHYTSRGCLKSVEWTIKSVNRNAYIMIAITGKSFCKSSAIATELIISNILRIGKVNVIGDVILFLGKLCVSLFSALFGFLMLDSHRYRASHNKVSSPLLPVLACWALGYIVATLFFAVVEMSIDTIILSFCQDSEENQGNAQHAPPLLLETLDSNQEEEVQSLTH,,-1.0,MRGPLGAVIGRYTSSDGSAPNDGIIKHNRKCRDITFLIIFIAFWVSMIVNSSFGFNQGNPLRLTYGLDYEGNVCGSKHRHRDLTQLELRYWLNPNQVYESGLKDGELKLANARTICLLDCPAPSDDTLNWVCDYPDGEIRLKMNDWIDRNYDYFEFLTPEMRNSSLQLQGPCYPVIFPSVNVYWSCQYIARASNSSLRHWQQMGGVNIQEDMIIDKSIRRSMNSRASVLKRYVADIGKSWPVLIVCEGLVPLFLSIIWLLLIRHFVAAMPWITVVLFNMLLISVTVFYYLKAGWIGNDAVTPIIGEHDPYFHVYGRELTHVRGVAILMTFISVVAILTSIAIIRRILMATSVLKVAAKVIGEVQALIIFPAIPFAMLAIFYMFWISAALHLFSSGQVVQNNCNNTNCCAYDLVLKKVNCDRCCGYSIHYTPHITIAIFFHLFGCYWATQFFIASSATVIAGSVASYYWAQGEASPEIPFLPVFASMKRLARYNLGSVALGSLIVSFVESVRFILEAIRRKTKVSGTIPDHWFWRMAHYTSRGCLKSVEWTIKSVNRNAYIMIAITGKSFCKSSAIATELIISNILRIGKVNVIGDVILFLGKLCVSLFSALFGFLMLDSHRYRASHNKVSSPLLPVLACWALGYIVATLFFAVVEMSIDTIILSFCQDSEENQGNAQHAPPLLLETLDSNQEEEVQSLTH,Choline transporter protein 1,"Regulator of vesicle trafficking, including endocytosis. Necessary for secondary plasmodesmata (PD) formation and development via the secretory trafficking regulation of proteins required for PD development, thus influencing intercellular communication. Modulates ion homeostasis, especially in roots, by monitoring the transport and subsequent subcellular localization of some ion transporters. Choline transporter involved in the regulation of choline metabolite homeostasis during root and phloem development. Modulates phloem morphogenesis and conductivity. Required for procambium maintenance and sieve plate development (e.g. sieve plate and sieve pore elaboration) to mediate long-distance cell-to-cell communication via symplastic transport through the phloem. Involved in the regulation of intracellular trafficking of PIN-type auxin transporters (e.g. PIN1 and PIN3), a process controlling seedling growth, apical dominance, cell elongation and apical hook development. Modulates also membrane lipids (e.g. phospholipids and sphingolipids) homeostasis.(Microbial infection) Required for PD localization of MP17, the luteoviral movement protein.","Decreased cher1-5 and sic1; enhanced secondary plasmodesmata (PD) formation (e.g. unblocked or expanded) and development leading to reduced starch and soluble sugars accumulation, normal cell-to-cell communication, and normal growth. Normal PD localization of the luteoviral movement protein MP17. Normal subcellular localization. Decreased leaf concentrations of sodium (Na), lithium (Li), boron (B) ions, and increased leaf concentrations of phosphorus (P), potassium (K), calcium (Ca), cobalt (Co), nickel (Ni), and copper (Cu), manganese (Mn), iron (Fe), zinc (Zn), and molybdenum (Mo) ions. Mutation in CHER1 resulted in a starch deficiency phenotype and normal growth. Ultrastructure analysis of shoot apical meristems, developing, and fully developed leaves showed increased PD numbers and the presence of complex PD in fully developed leaves. This indicates that cher1 mutants are enhanced in PD formation and development. Global lipid profiling revealed only slight modifications in the overall lipid composition, however, Thus, cher1 is endowed with complex PD in developed leaves and provides insights into the formation of complex PD at the molecular level.","Decreased cher1-5 and sic1; enhanced secondary plasmodesmata (PD) formation (e.g. unblocked or expanded) and development leading to reduced starch and soluble sugars accumulation, normal cell-to-cell communication, and normal growth. Normal PD localization of the luteoviral movement protein MP17. Normal subcellular localization. Decreased leaf concentrations of sodium (Na), lithium (Li), boron (B) ions, and increased leaf concentrations of phosphorus (P), potassium (K), calcium (Ca), cobalt (Co), nickel (Ni), and copper (Cu), manganese (Mn), iron (Fe), zinc (Zn), and molybdenum (Mo) ions. Mutation in CHER1 resulted in a starch deficiency phenotype and normal growth. Ultrastructure analysis of shoot apical meristems, developing, and fully developed leaves showed increased PD numbers and the presence of complex PD in fully developed leaves. This indicates that cher1 mutants are enhanced in PD formation and development. Global lipid profiling revealed only slight modifications in the overall lipid composition, however, Thus, cher1 is endowed with complex PD in developed leaves and provides insights into the formation of complex PD at the molecular level."
373,0,0,O14746-I791V,MPRAPRCRAVRSLLRSHYREVLPLATFVRRLGPQGWRLVQRGDPAAFRALVAQCLVCVPWDARPPPAAPSFRQVSCLKELVARVLQRLCERGAKNVLAFGFALLDGARGGPPEAFTTSVRSYLPNTVTDALRGSGAWGLLLRRVGDDVLVHLLARCALFVLVAPSCAYQVCGPPLYQLGAATQARPPPHASGPRRRLGCERAWNHSVREAGVPLGLPAPGARRRGGSASRSLPLPKRPRRGAAPEPERTPVGQGSWAHPGRTRGPSDRGFCVVSPARPAEEATSLEGALSGTRHSHPSVGRQHHAGPPSTSRPPRPWDTPCPPVYAETKHFLYSSGDKEQLRPSFLLSSLRPSLTGARRLVETIFLGSRPWMPGTPRRLPRLPQRYWQMRPLFLELLGNHAQCPYGVLLKTHCPLRAAVTPAAGVCAREKPQGSVAAPEEEDTDPRRLVQLLRQHSSPWQVYGFVRACLRRLVPPGLWGSRHNERRFLRNTKKFISLGKHAKLSLQELTWKMSVRDCAWLRRSPGVGCVPAAEHRLREEILAKFLHWLMSVYVVELLRSFFYVTETTFQKNRLFFYRKSVWSKLQSIGIRQHLKRVQLRELSEAEVRQHREARPALLTSRLRFIPKPDGLRPIVNMDYVVGARTFRREKRAERLTSRVKALFSVLNYERARRPGLLGASVLGLDDIHRAWRTFVLRVRAQDPPPELYFVKVDVTGAYDTIPQDRLTEVIASIIKPQNTYCVRRYAVVQKAAHGHVRKAFKSHVSTLTDLQPYMRQFVAHLQETSPLRDAVVIEQSSSLNEASSGLFDVFLRFMCHHAVRIRGKSYVQCQGIPQGSILSTLLCSLCYGDMENKLFAGIRRDGLLLRLVDDFLLVTPHLTHAKTFLRTLVRGVPEYGCVVNLRKTVVNFPVEDEALGGTAFVQMPAHGLFPWCGLLLDTRTLEVQSDYSSYARTSIRASLTFNRGFKAGRNMRRKLFGVLRLKCHSLFLDLQVNSLQTVCTNIYKILLLQAYRFHACVLQLPFHQQ,,-1.0,MPRAPRCRAVRSLLRSHYREVLPLATFVRRLGPQGWRLVQRGDPAAFRALVAQCLVCVPWDARPPPAAPSFRQVSCLKELVARVLQRLCERGAKNVLAFGFALLDGARGGPPEAFTTSVRSYLPNTVTDALRGSGAWGLLLRRVGDDVLVHLLARCALFVLVAPSCAYQVCGPPLYQLGAATQARPPPHASGPRRRLGCERAWNHSVREAGVPLGLPAPGARRRGGSASRSLPLPKRPRRGAAPEPERTPVGQGSWAHPGRTRGPSDRGFCVVSPARPAEEATSLEGALSGTRHSHPSVGRQHHAGPPSTSRPPRPWDTPCPPVYAETKHFLYSSGDKEQLRPSFLLSSLRPSLTGARRLVETIFLGSRPWMPGTPRRLPRLPQRYWQMRPLFLELLGNHAQCPYGVLLKTHCPLRAAVTPAAGVCAREKPQGSVAAPEEEDTDPRRLVQLLRQHSSPWQVYGFVRACLRRLVPPGLWGSRHNERRFLRNTKKFISLGKHAKLSLQELTWKMSVRDCAWLRRSPGVGCVPAAEHRLREEILAKFLHWLMSVYVVELLRSFFYVTETTFQKNRLFFYRKSVWSKLQSIGIRQHLKRVQLRELSEAEVRQHREARPALLTSRLRFIPKPDGLRPIVNMDYVVGARTFRREKRAERLTSRVKALFSVLNYERARRPGLLGASVLGLDDIHRAWRTFVLRVRAQDPPPELYFVKVDVTGAYDTIPQDRLTEVIASIIKPQNTYCVRRYAVVQKAAHGHVRKAFKSHVSTLTDLQPYMRQFVAHLQETSPLRDAVIIEQSSSLNEASSGLFDVFLRFMCHHAVRIRGKSYVQCQGIPQGSILSTLLCSLCYGDMENKLFAGIRRDGLLLRLVDDFLLVTPHLTHAKTFLRTLVRGVPEYGCVVNLRKTVVNFPVEDEALGGTAFVQMPAHGLFPWCGLLLDTRTLEVQSDYSSYARTSIRASLTFNRGFKAGRNMRRKLFGVLRLKCHSLFLDLQVNSLQTVCTNIYKILLLQAYRFHACVLQLPFHQQ,Telomerase reverse transcriptase,"Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. Active in progenitor and cancer cells. Inactive, or very low activity, in normal somatic cells. Catalytic component of the teleromerase holoenzyme complex whose main activity is the elongation of telomeres by acting as a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme. Catalyzes the RNA-dependent extension of 3'-chromosomal termini with the 6-nucleotide telomeric repeat unit, 5'-TTAGGG-3'. The catalytic cycle involves primer binding, primer extension and release of product once the template boundary has been reached or nascent product translocation followed by further extension. More active on substrates containing 2 or 3 telomeric repeats. Telomerase activity is regulated by a number of factors including telomerase complex-associated proteins, chaperones and polypeptide modifiers. Modulates Wnt signaling. Plays important roles in aging and antiapoptosis.",Highly enhances cleavage by CASP1 and decreases RSAD2 induction upon DNA virus infection; when associated with A-33; A-67; A-90 and A-140. Enables cleavage by CASP1 and decreases RSAD2 induction upon DNA virus infection.,Highly enhances cleavage by CASP1 and decreases RSAD2 induction upon DNA virus infection; when associated with A-33; A-67; A-90 and A-140. Enables cleavage by CASP1 and decreases RSAD2 induction upon DNA virus infection.
374,0,0,Q9JJS6-A237H,MEIIFGQNKKEQLEPVQAKVTGSIPAWLQGTLLRNGPGMHTVGESKYNHWFDGLALLHSFSIRDGEVFYRSKYLQSDTYIANIEANRIVVSEFGTMAYPDPCKNIFSKAFSYLSHTIPDFTDNCLINIMKCGEDFYATTETNYIRKIDPQTLETLEKVDYRKYVAVNLATSHPHYDEAGNVLNMGTSVVDKGRTKYVIFKIPATVPDSKKKGKSPVKHAEVFCSISSRSLLSPSYYHSFGVTENYVVFLEQPFKLDILKMATAYMRGVSWASCMSFDREDKTYIHIIDQRTRKPVPTKFYTDPMVVFHHVNAYEEDGCVLFDVIAYEDSSLYQLFYLANLNKDFEEKSRLTSVPTLRRFAVPLHVDKDAEVGSNLVKVSSTTATALKEKDGHVYCQPEVLYEGLELPRINYAYNGKPYRYIFAAEVQWSPVPTKILKYDILTKSSLKWSEESCWPAEPLFVPTPGAKDEDDGVILSAIVSTDPQKLPFLLILDAKSFTELARASVDADMHLDLHGLFIPDADWNAVKQTPAETQEVENSDHPTDPTAPELSHSENDFTAGHGGSSL,,-1.0,MEIIFGQNKKEQLEPVQAKVTGSIPAWLQGTLLRNGPGMHTVGESKYNHWFDGLALLHSFSIRDGEVFYRSKYLQSDTYIANIEANRIVVSEFGTMAYPDPCKNIFSKAFSYLSHTIPDFTDNCLINIMKCGEDFYATTETNYIRKIDPQTLETLEKVDYRKYVAVNLATSHPHYDEAGNVLNMGTSVVDKGRTKYVIFKIPATVPDSKKKGKSPVKHAEVFCSISSRSLLSPSYYASFGVTENYVVFLEQPFKLDILKMATAYMRGVSWASCMSFDREDKTYIHIIDQRTRKPVPTKFYTDPMVVFHHVNAYEEDGCVLFDVIAYEDSSLYQLFYLANLNKDFEEKSRLTSVPTLRRFAVPLHVDKDAEVGSNLVKVSSTTATALKEKDGHVYCQPEVLYEGLELPRINYAYNGKPYRYIFAAEVQWSPVPTKILKYDILTKSSLKWSEESCWPAEPLFVPTPGAKDEDDGVILSAIVSTDPQKLPFLLILDAKSFTELARASVDADMHLDLHGLFIPDADWNAVKQTPAETQEVENSDHPTDPTAPELSHSENDFTAGHGGSSL,"Beta,beta-carotene 15,15'-dioxygenase",Symmetrically cleaves beta-carotene into two molecules of retinal using a dioxygenase mechanism.,"Decreased effect on protein abundance. Gain of beta-carotene 15,15'-monooxygenase activity. Increased iron binding. Mutation of H237 produced improved although enzymatically active proteins, with an increase in activity mostly due to changes in V(max).","Decreased effect on protein abundance. Gain of beta-carotene 15,15'-monooxygenase activity. Increased iron binding. Mutation of H237 produced improved although enzymatically active proteins, with an increase in activity mostly due to changes in V(max)."
375,0,0,Q6UWV6-E343R,MRGPAVLLTVALATLLAPGAGAPVQSQGSQNKLLLVSFDGFRWNYDQDVDTPNLDAMARDGVKARYMTPAFVTMTSPCHFTLVTGKYIENHGVVHNMYYNTTSKVKLPYHATLGIQRWWDNGSVPIWITAQRQGLRAGSFFYPGGNVTYQGVAVTRSRKEGIAHNYKNETEWRANIDTVMAWFTEEDLDLVTLYFGEPDSTGHRYGPESPERREMVRQVDRTVGYLRESIARNHLTDRLNLIITSDHGMTTVDKRAGDLVEFHKFPNFTFRDIEFELLDYGPNGMLLPKEGRLEKVYDALKDAHPKLHVYKKEAFPEAFHYANNPRVTPLLMYSDLGYVIHGRINVQFNNGEHGFDNKDMDMKTIFRAVGPSFRAGLEVEPFESVHVYELMCRLLGIVPEANDGHLATLLPMLHTESALPPDGRPTLLPKGRSALPPSSRPLLVMGLLGTVILLSEVA,,-1.0,MRGPAVLLTVALATLLAPGAGAPVQSQGSQNKLLLVSFDGFRWNYDQDVDTPNLDAMARDGVKARYMTPAFVTMTSPCHFTLVTGKYIENHGVVHNMYYNTTSKVKLPYHATLGIQRWWDNGSVPIWITAQRQGLRAGSFFYPGGNVTYQGVAVTRSRKEGIAHNYKNETEWRANIDTVMAWFTEEDLDLVTLYFGEPDSTGHRYGPESPERREMVRQVDRTVGYLRESIARNHLTDRLNLIITSDHGMTTVDKRAGDLVEFHKFPNFTFRDIEFELLDYGPNGMLLPKEGRLEKVYDALKDAHPKLHVYKKEAFPEAFHYANNPRVTPLLMYSDLGYVIHGEINVQFNNGEHGFDNKDMDMKTIFRAVGPSFRAGLEVEPFESVHVYELMCRLLGIVPEANDGHLATLLPMLHTESALPPDGRPTLLPKGRSALPPSSRPLLVMGLLGTVILLSEVA,Ectonucleotide pyrophosphatase/phosphodiesterase family member 7,"Choline-specific phosphodiesterase that hydrolyzes sphingomyelin releasing the ceramide and phosphocholine and therefore is involved in sphingomyelin digestion, ceramide formation, and fatty acid (FA) absorption in the gastrointestinal tract. Has also phospholipase C activity and can also cleave phosphocholine from palmitoyl lyso-phosphatidylcholine and platelet-activating factor (PAF) leading to its inactivation. Does not have nucleotide pyrophosphatase activity. May promote cholesterol absorption by affecting the levels of sphingomyelin derived from either diet or endogenous sources, in the intestinal lumen.",Increased enzyme activity; when associated with E-271. The mutation in alk-SMase has been identified to cause functional changes in the protein.,Increased enzyme activity; when associated with E-271. The mutation in alk-SMase has been identified to cause functional changes in the protein.
376,0,0,P35462-S9G,MASLSQLSGHLNYTCGAENSTGASQARPHAYYALSYCALILAIVFGNGLVCMAVLKERALQTTTNYLVVSLAVADLLVATLVMPWVVYLEVTGGVWNFSRICCDVFVTLDVMMCTASILNLCAISIDRYTAVVMPVHYQHGTGQSSCRRVALMITAVWVLAFAVSCPLLFGFNTTGDPTVCSISNPDFVIYSSVVSFYLPFGVTVLVYARIYVVLKQRRRKRILTRQNSQCNSVRPGFPQQTLSPDPAHLELKRYYSICQDTALGGPGFQERGGELKREEKTRNSLSPTIAPKLSLEVRKLSNGRLSTSLKLGPLQPRGVPLREKKATQMVAIVLGAFIVCWLPFFLTHVLNTHCQTCHVSPELYSATTWLGYVNSALNPVIYTTFNIEFRKAFLKILSC,,-1.0,MASLSQLSSHLNYTCGAENSTGASQARPHAYYALSYCALILAIVFGNGLVCMAVLKERALQTTTNYLVVSLAVADLLVATLVMPWVVYLEVTGGVWNFSRICCDVFVTLDVMMCTASILNLCAISIDRYTAVVMPVHYQHGTGQSSCRRVALMITAVWVLAFAVSCPLLFGFNTTGDPTVCSISNPDFVIYSSVVSFYLPFGVTVLVYARIYVVLKQRRRKRILTRQNSQCNSVRPGFPQQTLSPDPAHLELKRYYSICQDTALGGPGFQERGGELKREEKTRNSLSPTIAPKLSLEVRKLSNGRLSTSLKLGPLQPRGVPLREKKATQMVAIVLGAFIVCWLPFFLTHVLNTHCQTCHVSPELYSATTWLGYVNSALNPVIYTTFNIEFRKAFLKILSC,D,Dopamine receptor whose activity is mediated by G proteins which inhibit adenylyl cyclase. Promotes cell proliferation.,Decreased homozygosity of the S/G variant of the Dopamine D3 receptor gene is associated with schizophrenia.,Decreased homozygosity of the S/G variant of the Dopamine D3 receptor gene is associated with schizophrenia.
377,0,0,Q6UWV6-A353H,MRGPAVLLTVALATLLAPGAGAPVQSQGSQNKLLLVSFDGFRWNYDQDVDTPNLDAMARDGVKARYMTPAFVTMTSPCHFTLVTGKYIENHGVVHNMYYNTTSKVKLPYHATLGIQRWWDNGSVPIWITAQRQGLRAGSFFYPGGNVTYQGVAVTRSRKEGIAHNYKNETEWRANIDTVMAWFTEEDLDLVTLYFGEPDSTGHRYGPESPERREMVRQVDRTVGYLRESIARNHLTDRLNLIITSDHGMTTVDKRAGDLVEFHKFPNFTFRDIEFELLDYGPNGMLLPKEGRLEKVYDALKDAHPKLHVYKKEAFPEAFHYANNPRVTPLLMYSDLGYVIHGRINVQFNNGEHGFDNKDMDMKTIFRAVGPSFRAGLEVEPFESVHVYELMCRLLGIVPEANDGHLATLLPMLHTESALPPDGRPTLLPKGRSALPPSSRPLLVMGLLGTVILLSEVA,,-1.0,MRGPAVLLTVALATLLAPGAGAPVQSQGSQNKLLLVSFDGFRWNYDQDVDTPNLDAMARDGVKARYMTPAFVTMTSPCHFTLVTGKYIENHGVVHNMYYNTTSKVKLPYHATLGIQRWWDNGSVPIWITAQRQGLRAGSFFYPGGNVTYQGVAVTRSRKEGIAHNYKNETEWRANIDTVMAWFTEEDLDLVTLYFGEPDSTGHRYGPESPERREMVRQVDRTVGYLRESIARNHLTDRLNLIITSDHGMTTVDKRAGDLVEFHKFPNFTFRDIEFELLDYGPNGMLLPKEGRLEKVYDALKDAHPKLHVYKKEAFPEAFHYANNPRVTPLLMYSDLGYVIHGRINVQFNNGEAGFDNKDMDMKTIFRAVGPSFRAGLEVEPFESVHVYELMCRLLGIVPEANDGHLATLLPMLHTESALPPDGRPTLLPKGRSALPPSSRPLLVMGLLGTVILLSEVA,Ectonucleotide pyrophosphatase/phosphodiesterase family member 7,"Choline-specific phosphodiesterase that hydrolyzes sphingomyelin releasing the ceramide and phosphocholine and therefore is involved in sphingomyelin digestion, ceramide formation, and fatty acid (FA) absorption in the gastrointestinal tract. Has also phospholipase C activity and can also cleave phosphocholine from palmitoyl lyso-phosphatidylcholine and platelet-activating factor (PAF) leading to its inactivation. Does not have nucleotide pyrophosphatase activity. May promote cholesterol absorption by affecting the levels of sphingomyelin derived from either diet or endogenous sources, in the intestinal lumen.",Loss of inactivity. substitution resulted in a protein with alk-SMase activity.,Loss of inactivity. substitution resulted in a protein with alk-SMase activity.
378,0,0,Q31125-A198P,MTMGLRAPHWVAVGLLTWAALGLLVAGHEGHGDLHKDVEEDFHGHSHGHSHEDFHHGHSHGHSHEDFHHGHGHTHESIWHGHAHSHDHGHSREELHHGHSHGHSHDSLHHGGHGHAHREHSHGTSREAGAPGIKHHLDTVTLWAYALGATVLISAAPFFVLFLIPVESNSPRHRSLLQILLSFASGGLLGDAFLHLIPHALEPHSHHAPEQPGHGHSHSGQGPILSVGLWVLSGIVAFLVVEKFVRHVKGGHGHSHGHGDRHAHGDSHTHGDRHECSSKEKPSTEEEKEVGGLRKRRGGNTGPRDGPVKPQSPEEEKAGSDLRVSGYLNLAADLAHNFTDGLAIGASFRGGRGLGILTTMTVLLHEVPHEVGDFAILVQSGCSKKQAMRLQLVTAIGALAGTACALLTEGGAVDSDVAGGAGPGWVLPFTAGGFIYVATVSVLPELLREASPLQSLLEVLGLLGGVAMMVLIAHLE,,-1.0,MTMGLRAPHWVAVGLLTWAALGLLVAGHEGHGDLHKDVEEDFHGHSHGHSHEDFHHGHSHGHSHEDFHHGHGHTHESIWHGHAHSHDHGHSREELHHGHSHGHSHDSLHHGGHGHAHREHSHGTSREAGAPGIKHHLDTVTLWAYALGATVLISAAPFFVLFLIPVESNSPRHRSLLQILLSFASGGLLGDAFLHLIAHALEPHSHHAPEQPGHGHSHSGQGPILSVGLWVLSGIVAFLVVEKFVRHVKGGHGHSHGHGDRHAHGDSHTHGDRHECSSKEKPSTEEEKEVGGLRKRRGGNTGPRDGPVKPQSPEEEKAGSDLRVSGYLNLAADLAHNFTDGLAIGASFRGGRGLGILTTMTVLLHEVPHEVGDFAILVQSGCSKKQAMRLQLVTAIGALAGTACALLTEGGAVDSDVAGGAGPGWVLPFTAGGFIYVATVSVLPELLREASPLQSLLEVLGLLGGVAMMVLIAHLE,Zinc transporter SLC39A7,"Transports Zn(2+) from the endoplasmic reticulum (ER)/Golgi apparatus to the cytosol, playing an essential role in the regulation of cytosolic zinc levels. Acts as gatekeeper of zinc release from intracellular stores, requiring post-translational activation by phosphorylation, resulting in activation of multiple downstream pathways leading to cell growth and proliferation. Has an essential role in B cell development and is required for proper B cell receptor signaling. Plays an important role in maintaining intestinal epithelial homeostasis and skin dermis development by regulating ER function. Controls cell signaling pathways involved in glucose metabolism in skeletal muscle. Has a protective role against ER stress in differents biological contexts. Mediates Zn(2+)-induced ferroptosis.",Homozygous mice have enhanced B cell immunodeficiency and improved transition from late pre-B to immature B cell. B cells from mutant mice exhibit an increased concentration of cytoplasmic free zinc and increased phosphorylation of signaling molecules downstream of the pre-B cell and B cell receptors.,Homozygous mice have enhanced B cell immunodeficiency and improved transition from late pre-B to immature B cell. B cells from mutant mice exhibit an increased concentration of cytoplasmic free zinc and increased phosphorylation of signaling molecules downstream of the pre-B cell and B cell receptors.
379,0,0,P16152-I88V,MSSGIHVALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDVLVNNAGIAFKVADPTPFHIQAEVTMKTNFFGTRDVCTELLPLIKPQGRVVNVSSIMSVRALKSCSPELQQKFRSETITEEELVGLMNKFVEDTKKGVHQKEGWPSSAYGVTKIGVTVLSRIHARKLSEQRKGDKILLNACCPGWVRTDMAGPKATKSPEEGAETPVYLALLPPDAEGPHGQFVSEKRVEQW,,-1.0,MSSGIHVALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDVLINNAGIAFKVADPTPFHIQAEVTMKTNFFGTRDVCTELLPLIKPQGRVVNVSSIMSVRALKSCSPELQQKFRSETITEEELVGLMNKFVEDTKKGVHQKEGWPSSAYGVTKIGVTVLSRIHARKLSEQRKGDKILLNACCPGWVRTDMAGPKATKSPEEGAETPVYLALLPPDAEGPHGQFVSEKRVEQW,Carbonyl reductase [NADPH] 1,"NADPH-dependent reductase with broad substrate specificity. Catalyzes the reduction of a wide variety of carbonyl compounds including quinones, prostaglandins, menadione, plus various xenobiotics. Catalyzes the reduction of the antitumor anthracyclines doxorubicin and daunorubicin to the cardiotoxic compounds doxorubicinol and daunorubicinol. Can convert prostaglandin E to prostaglandin F2-alpha. Can bind glutathione, which explains its higher affinity for glutathione-conjugated substrates. Catalyzes the reduction of S-nitrosoglutathione. In addition, participates in the glucocorticoid metabolism by catalyzing the NADPH-dependent cortisol/corticosterone into 20beta-dihydrocortisol (20b-DHF) or 20beta-corticosterone (20b-DHB), which are weak agonists of NR3C1 and NR3C2 in adipose tissue.","Enhanced affinity for NADPH and enhanced activity towards daunorubicin and prostaglandin E2. The CBR1 V88 and CBR1 I88 isoforms have identical maximal velocities for daunorubicin and PGE2. Concomitantly, CBR1 V88 produced lower levels of the cardiotoxic metabolite daunorubicinol compared with CBR1 I88. Activation studies demonstrated that CBR1 V88 and CBR1 I88 are uniformly activated by the flavonoid, rutin. Furthermore, isothermal titration calorimetry analyses together with molecular modeling studies showed that CBR1 results in CBR1 isoforms with identical binding affinities for the cofactor NADPH. The mutation in CBR1 may not affect the activity of the enzyme.","Enhanced affinity for NADPH and enhanced activity towards daunorubicin and prostaglandin E2. The CBR1 V88 and CBR1 I88 isoforms have identical maximal velocities for daunorubicin and PGE2. Concomitantly, CBR1 V88 produced lower levels of the cardiotoxic metabolite daunorubicinol compared with CBR1 I88. Activation studies demonstrated that CBR1 V88 and CBR1 I88 are uniformly activated by the flavonoid, rutin. Furthermore, isothermal titration calorimetry analyses together with molecular modeling studies showed that CBR1 results in CBR1 isoforms with identical binding affinities for the cofactor NADPH. The mutation in CBR1 may not affect the activity of the enzyme."
380,0,0,Q9IK90-A92Y,MEPDIKSISSESMEGVSDFSPSSWEHGGYLDKVEPEIDENGSMIPKYKIYTPGANERKYNNYMYLICYGFVEDVERTPETGKRKKIRTIAAYPLGVGKSASHPQDLLEELCSLKVTVRRTAGSTEKIVFGSSGPLNHLVPWKKVLTSGSIFNAVKVCRNVDQIQLDKHQALRIFFLSITKLNDSGIYMIPRTMLEFRRNNAIAFNLLVYLKIDADLSKMGIQGSLDKDGFKVASFMLHLGNFVRRAGKYYSVDYCRRKIDRMKLQFSLGSIGGLSLHIKINGVISKRLFAQMGFQKNLCFSLMDINPWLNRLTWNNSCEISRVAAVLQPSIPREFMIYDDVFIDNTGRILKG,,-1.0,MEPDIKSISSESMEGVSDFSPSSWEHGGYLDKVEPEIDENGSMIPKYKIYTPGANERKYNNYMYLICYGFVEDVERTPETGKRKKIRTIAAAPLGVGKSASHPQDLLEELCSLKVTVRRTAGSTEKIVFGSSGPLNHLVPWKKVLTSGSIFNAVKVCRNVDQIQLDKHQALRIFFLSITKLNDSGIYMIPRTMLEFRRNNAIAFNLLVYLKIDADLSKMGIQGSLDKDGFKVASFMLHLGNFVRRAGKYYSVDYCRRKIDRMKLQFSLGSIGGLSLHIKINGVISKRLFAQMGFQKNLCFSLMDINPWLNRLTWNNSCEISRVAAVLQPSIPREFMIYDDVFIDNTGRILKG,Matrix protein,Plays a crucial role in virion assembly and budding. Forms a shell at the inner face of the plasma membrane. Transits through the host nucleus before gaining the functional ability to localize and bud from the plasma membrane. Mediates together with fusion protein the incorporation of the glycoprotein to the viral particles. Participates also in the inhibition of the host interferon type I antiviral response by interacting with and thereby inhibiting host TRIM6.,Complete loss of budding. Mutation of Y92 to A enabled VLP release and caused relocalization of NiV M to the nucleus.,Complete loss of budding. Mutation of Y92 to A enabled VLP release and caused relocalization of NiV M to the nucleus.
381,0,0,Q92504-A190P,MARGLGAPHWVAVGLLTWATLGLLVAGLGGHDDLHDDLQEDFHGHSHRHSHEDFHHGHSHAHGHGHTHESIWHGHTHDHDHGHSHEDLHHGHSHGYSHESLYHRGHGHDHEHSHGGYGESGAPGIKQDLDAVTLWAYALGATVLISAAPFFVLFLIPVESNSPRHRSLLQILLSFASGGLLGDAFLHLIPHALEPHSHHTLEQPGHGHSHSGQGPILSVGLWVLSGIVAFLVVEKFVRHVKGGHGHSHGHGHAHSHTRGSHGHGRQERSTKEKQSSEEEEKETRGVQKRRGGSTVPKDGPVRPQNAEEEKRGLDLRVSGYLNLAADLAHNFTDGLAIGASFRGGRGLGILTTMTVLLHEVPHEVGDFAILVQSGCSKKQAMRLQLLTAVGALAGTACALLTEGGAVGSEIAGGAGPGWVLPFTAGGFIYVATVSVLPELLREASPLQSLLEVLGLLGGVIMMVLIAHLE,,-1.0,MARGLGAPHWVAVGLLTWATLGLLVAGLGGHDDLHDDLQEDFHGHSHRHSHEDFHHGHSHAHGHGHTHESIWHGHTHDHDHGHSHEDLHHGHSHGYSHESLYHRGHGHDHEHSHGGYGESGAPGIKQDLDAVTLWAYALGATVLISAAPFFVLFLIPVESNSPRHRSLLQILLSFASGGLLGDAFLHLIAHALEPHSHHTLEQPGHGHSHSGQGPILSVGLWVLSGIVAFLVVEKFVRHVKGGHGHSHGHGHAHSHTRGSHGHGRQERSTKEKQSSEEEEKETRGVQKRRGGSTVPKDGPVRPQNAEEEKRGLDLRVSGYLNLAADLAHNFTDGLAIGASFRGGRGLGILTTMTVLLHEVPHEVGDFAILVQSGCSKKQAMRLQLLTAVGALAGTACALLTEGGAVGSEIAGGAGPGWVLPFTAGGFIYVATVSVLPELLREASPLQSLLEVLGLLGGVIMMVLIAHLE,Zinc transporter SLC39A7,"Transports Zn(2+) from the endoplasmic reticulum (ER)/Golgi apparatus to the cytosol, playing an essential role in the regulation of cytosolic zinc levels. Acts as gatekeeper of zinc release from intracellular stores, requiring post-translational activation by phosphorylation, resulting in activation of multiple downstream pathways leading to cell growth and proliferation. Has an essential role in B cell development and is required for proper B cell receptor signaling. Plays an important role in maintaining intestinal epithelial homeostasis and skin dermis development by regulating ER function. Controls cell signaling pathways involved in glucose metabolism in skeletal muscle. Has a protective role against ER stress in differents biological contexts. Mediates Zn(2+)-induced ferroptosis.",Increased zinc ion transporter activity; does not affect localization to endoplasmic reticulum.,Increased zinc ion transporter activity; does not affect localization to endoplasmic reticulum.
382,0,0,Q9ULZ3-K48D,MGRARDAILDALENLTAEELKKFKLKLLSVPLREGYGRIPRGALLSMDALDLTDKLVSFYLETYGAELTANVLRDMGLQEMAGQLQAATHQGSGAAPAGIQAPPQSAAKPGLHFIDQHRAALIARVTNVEWLLDALYGKVLTDEQYQAVRAEPTNPSKMRKLFSFTPAWNWTCKDLLLQALRESQSYLVEDLERS,,-1.0,MGRARDAILDALENLTAEELKKFKLKLLSVPLREGYGRIPRGALLSMKALDLTDKLVSFYLETYGAELTANVLRDMGLQEMAGQLQAATHQGSGAAPAGIQAPPQSAAKPGLHFIDQHRAALIARVTNVEWLLDALYGKVLTDEQYQAVRAEPTNPSKMRKLFSFTPAWNWTCKDLLLQALRESQSYLVEDLERS,Apoptosis-associated speck-like protein containing a CARD,"Functions as key mediator in apoptosis and inflammation. Promotes caspase-mediated apoptosis involving predominantly caspase-8 and also caspase-9 in a probable cell type-specific manner. Involved in activation of the mitochondrial apoptotic pathway, promotes caspase-8-dependent proteolytic maturation of BID independently of FADD in certain cell types and also mediates mitochondrial translocation of BAX and activates BAX-dependent apoptosis coupled to activation of caspase-9, -2 and -3. Involved in innate immune response by acting as an integral adapter in the assembly of various inflammasomes (NLRP1, NLRP2, NLRP3, NLRP6, AIM2 and probably IFI16) which recruit and activate caspase-1 leading to processing and secretion of pro-inflammatory cytokines. Caspase-1-dependent inflammation leads to macrophage pyroptosis, a form of cell death. The function as activating adapter in different types of inflammasomes is mediated by the pyrin and CARD domains and their homotypic interactions. Clustered PYCARD nucleates the formation of caspase-1 filaments through the interaction of their respective CARD domains, acting as a platform for of caspase-1 polymerization. In the NLRP1 and NLRC4 inflammasomes seems not be required but facilitates the processing of procaspase-1. In cooperation with NOD2 involved in an inflammasome activated by bacterial muramyl dipeptide leading to caspase-1 activation. May be involved in RIGI-triggered pro-inflammatory responses and inflammasome activation. In collaboration with AIM2 which detects cytosolic double-stranded DNA may also be involved in a caspase-1-independent cell death that involves caspase-8. In adaptive immunity may be involved in maturation of dendritic cells to stimulate T-cell immunity and in cytoskeletal rearrangements coupled to chemotaxis and antigen uptake may be involved in post-transcriptional regulation of the guanine nucleotide exchange factor DOCK2; the latter function is proposed to involve the nuclear form. Also involved in transcriptional activation of cytokines and chemokines independent of the inflammasome; this function may involve AP-1, NF-kappa-B, MAPK and caspase-8 signaling pathways. For regulation of NF-kappa-B activating and inhibiting functions have been reported. Modulates NF-kappa-B induction at the level of the IKK complex by inhibiting kinase activity of CHUK and IKBK. Proposed to compete with RIPK2 for association with CASP1 thereby down-regulating CASP1-mediated RIPK2-dependent NF-kappa-B activation and activating interleukin-1 beta processing. Modulates host resistance to DNA virus infection, probably by inducing the cleavage of and inactivating CGAS in presence of cytoplasmic double-stranded DNA.May have a regulating effect on the function as inflammasome adapter.Seems to inhibit inflammasome-mediated maturation of interleukin-1 beta.",Enhances homooligomerization. Mutation of D48 to K in ASC protein leads to filament formation.,Enhances homooligomerization. Mutation of D48 to K in ASC protein leads to filament formation.
383,0,0,O14746-A868D,MPRAPRCRAVRSLLRSHYREVLPLATFVRRLGPQGWRLVQRGDPAAFRALVAQCLVCVPWDARPPPAAPSFRQVSCLKELVARVLQRLCERGAKNVLAFGFALLDGARGGPPEAFTTSVRSYLPNTVTDALRGSGAWGLLLRRVGDDVLVHLLARCALFVLVAPSCAYQVCGPPLYQLGAATQARPPPHASGPRRRLGCERAWNHSVREAGVPLGLPAPGARRRGGSASRSLPLPKRPRRGAAPEPERTPVGQGSWAHPGRTRGPSDRGFCVVSPARPAEEATSLEGALSGTRHSHPSVGRQHHAGPPSTSRPPRPWDTPCPPVYAETKHFLYSSGDKEQLRPSFLLSSLRPSLTGARRLVETIFLGSRPWMPGTPRRLPRLPQRYWQMRPLFLELLGNHAQCPYGVLLKTHCPLRAAVTPAAGVCAREKPQGSVAAPEEEDTDPRRLVQLLRQHSSPWQVYGFVRACLRRLVPPGLWGSRHNERRFLRNTKKFISLGKHAKLSLQELTWKMSVRDCAWLRRSPGVGCVPAAEHRLREEILAKFLHWLMSVYVVELLRSFFYVTETTFQKNRLFFYRKSVWSKLQSIGIRQHLKRVQLRELSEAEVRQHREARPALLTSRLRFIPKPDGLRPIVNMDYVVGARTFRREKRAERLTSRVKALFSVLNYERARRPGLLGASVLGLDDIHRAWRTFVLRVRAQDPPPELYFVKVDVTGAYDTIPQDRLTEVIASIIKPQNTYCVRRYAVVQKAAHGHVRKAFKSHVSTLTDLQPYMRQFVAHLQETSPLRDAVVIEQSSSLNEASSGLFDVFLRFMCHHAVRIRGKSYVQCQGIPQGSILSTLLCSLCYGDMENKLFAGIRRDGLLLRLVDDFLLVTPHLTHAKTFLRTLVRGVPEYGCVVNLRKTVVNFPVEDEALGGTAFVQMPAHGLFPWCGLLLDTRTLEVQSDYSSYARTSIRASLTFNRGFKAGRNMRRKLFGVLRLKCHSLFLDLQVNSLQTVCTNIYKILLLQAYRFHACVLQLPFHQQ,,-1.0,MPRAPRCRAVRSLLRSHYREVLPLATFVRRLGPQGWRLVQRGDPAAFRALVAQCLVCVPWDARPPPAAPSFRQVSCLKELVARVLQRLCERGAKNVLAFGFALLDGARGGPPEAFTTSVRSYLPNTVTDALRGSGAWGLLLRRVGDDVLVHLLARCALFVLVAPSCAYQVCGPPLYQLGAATQARPPPHASGPRRRLGCERAWNHSVREAGVPLGLPAPGARRRGGSASRSLPLPKRPRRGAAPEPERTPVGQGSWAHPGRTRGPSDRGFCVVSPARPAEEATSLEGALSGTRHSHPSVGRQHHAGPPSTSRPPRPWDTPCPPVYAETKHFLYSSGDKEQLRPSFLLSSLRPSLTGARRLVETIFLGSRPWMPGTPRRLPRLPQRYWQMRPLFLELLGNHAQCPYGVLLKTHCPLRAAVTPAAGVCAREKPQGSVAAPEEEDTDPRRLVQLLRQHSSPWQVYGFVRACLRRLVPPGLWGSRHNERRFLRNTKKFISLGKHAKLSLQELTWKMSVRDCAWLRRSPGVGCVPAAEHRLREEILAKFLHWLMSVYVVELLRSFFYVTETTFQKNRLFFYRKSVWSKLQSIGIRQHLKRVQLRELSEAEVRQHREARPALLTSRLRFIPKPDGLRPIVNMDYVVGARTFRREKRAERLTSRVKALFSVLNYERARRPGLLGASVLGLDDIHRAWRTFVLRVRAQDPPPELYFVKVDVTGAYDTIPQDRLTEVIASIIKPQNTYCVRRYAVVQKAAHGHVRKAFKSHVSTLTDLQPYMRQFVAHLQETSPLRDAVVIEQSSSLNEASSGLFDVFLRFMCHHAVRIRGKSYVQCQGIPQGSILSTLLCSLCYGDMENKLFAGIRRDGLLLRLVADFLLVTPHLTHAKTFLRTLVRGVPEYGCVVNLRKTVVNFPVEDEALGGTAFVQMPAHGLFPWCGLLLDTRTLEVQSDYSSYARTSIRASLTFNRGFKAGRNMRRKLFGVLRLKCHSLFLDLQVNSLQTVCTNIYKILLLQAYRFHACVLQLPFHQQ,Telomerase reverse transcriptase,"Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. Active in progenitor and cancer cells. Inactive, or very low activity, in normal somatic cells. Catalytic component of the teleromerase holoenzyme complex whose main activity is the elongation of telomeres by acting as a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme. Catalyzes the RNA-dependent extension of 3'-chromosomal termini with the 6-nucleotide telomeric repeat unit, 5'-TTAGGG-3'. The catalytic cycle involves primer binding, primer extension and release of product once the template boundary has been reached or nascent product translocation followed by further extension. More active on substrates containing 2 or 3 telomeric repeats. Telomerase activity is regulated by a number of factors including telomerase complex-associated proteins, chaperones and polypeptide modifiers. Modulates Wnt signaling. Plays important roles in aging and antiapoptosis.","Highly increases telomerase activity. The mutation in the hTERT protein causes telomerase activity enhancements consistent with establishment of a template-proximal anchor site. This mutation leads to enhanced processivity on short telomeric primers and increased activity on substrates with nontelomeric 5' sequences, but not on primers with nontelomeric G-rich 5' sequences. The mutation is located within a subregion of the N-terminal human TERT RNA interaction domain 1 (RID1) previously implicated in biological telomerase functions unrelated to catalytic activity (N-DAT domain). Other mutants in the N-DAT and C-terminal DAT (C-DAT) regions, as well as a C-terminally tagged hTERT-HA variant, also showed enhancements in elongating short telomeric primers. The catalytic phenotypes of these mutants were partially or completely hindered by decreasing concentrations of DNA primers. These findings suggest that RID1 and the hTERT C terminus contribute to telomerase's repulsion from its substrate, and that RID1 may form part of the human telomerase anchor site. Mutation of residue D868 to A significantly enhanced associated telomerase activity. Substitution of the amino acid residue D868 with A greatly boosted telomerase activity.","Highly increases telomerase activity. The mutation in the hTERT protein causes telomerase activity enhancements consistent with establishment of a template-proximal anchor site. This mutation leads to enhanced processivity on short telomeric primers and increased activity on substrates with nontelomeric 5' sequences, but not on primers with nontelomeric G-rich 5' sequences. The mutation is located within a subregion of the N-terminal human TERT RNA interaction domain 1 (RID1) previously implicated in biological telomerase functions unrelated to catalytic activity (N-DAT domain). Other mutants in the N-DAT and C-terminal DAT (C-DAT) regions, as well as a C-terminally tagged hTERT-HA variant, also showed enhancements in elongating short telomeric primers. The catalytic phenotypes of these mutants were partially or completely hindered by decreasing concentrations of DNA primers. These findings suggest that RID1 and the hTERT C terminus contribute to telomerase's repulsion from its substrate, and that RID1 may form part of the human telomerase anchor site. Mutation of residue D868 to A significantly enhanced associated telomerase activity. Substitution of the amino acid residue D868 with A greatly boosted telomerase activity."
384,0,0,P9WGT3-L144S,MTATATEGAKPPFVSRSVLVTGGNRGIGLAIAQRLAADGHKVAVTHRGSGAPKGLFGVECDVTDSDAVDRAFTAVEEHQGPVEVLVSNAGLSADAFLMRMTEEKFEKVINANLTGAFRVAQRASRSMQRNKFGRMIFIGSVSGSWGIGNQANYAASKAGVIGMARSIARELSKANVTANVVAPGYIDTDMTRALDERIQQGALQFIPAKRVGTPAEVAGVVSFLASEDASYISGAVIPVDGGMGMGH,,-1.0,MTATATEGAKPPFVSRSVLVTGGNRGIGLAIAQRLAADGHKVAVTHRGSGAPKGLFGVECDVTDSDAVDRAFTAVEEHQGPVEVLVSNAGLSADAFLMRMTEEKFEKVINANLTGAFRVAQRASRSMQRNKFGRMIFIGSVSGLWGIGNQANYAASKAGVIGMARSIARELSKANVTANVVAPGYIDTDMTRALDERIQQGALQFIPAKRVGTPAEVAGVVSFLASEDASYISGAVIPVDGGMGMGH,3-oxoacyl-[acyl-carrier-protein] reductase MabA,"Part of the mycobacterial fatty acid elongation system FAS-II, which is involved in mycolic acid biosynthesis. Catalyzes the NADPH-dependent reduction of beta-ketoacyl derivatives, the second step of the FAS-II elongation cycle. May preferentially metabolize long-chain substrates (C8-C20). Can use CoA derivatives as substrates in vitro.",Decreases the destabilization of the catalytic loop in its open active form. Loses 84% of activity; when associated with V-60. Fully active; when associated with V-60 and A-139. The crystal structure of a mutated MabA protein was then solved in both active and inactive form.,Decreases the destabilization of the catalytic loop in its open active form. Loses 84% of activity; when associated with V-60. Fully active; when associated with V-60 and A-139. The crystal structure of a mutated MabA protein was then solved in both active and inactive form.
385,0,0,P08692-A128D,MSNITIYHNPACGTSRNTLEMIRNSGTEPTIILYLENPPSRDELVKLIADMGISVRALLRKNVEPYEQLGLAEDKFTDDQLIDFMLQHPILINRPIVVTPLGTRLCRPSEVVLDILQDAQKGAFTKEDGEKVVDEAGKRLK,,-1.0,MSNITIYHNPACGTSRNTLEMIRNSGTEPTIILYLENPPSRDELVKLIADMGISVRALLRKNVEPYEQLGLAEDKFTDDQLIDFMLQHPILINRPIVVTPLGTRLCRPSEVVLDILQDAQKGAFTKEAGEKVVDEAGKRLK,Arsenate reductase,Involved in resistance to arsenate. Catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)]. The resulting arsenite is then extruded from the cell via the ArsAB transport system (Probable).,"4-fold increase in catalytic efficiency with arsenate. Mutant is relatively sensitive to arsenate, but is less sensitive at higher concentrations.","4-fold increase in catalytic efficiency with arsenate. Mutant is relatively sensitive to arsenate, but is less sensitive at higher concentrations."
386,0,0,Q9ESN9-G209L,MMEIQMDEGGGVVVYQDDYCSGSVMSERVSGLAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEERESEMKKEYNALHQRHTEMIQTYVEHIERSKMQQVGGSGQTESSLPGRSRKERPTSLNVFPLADGMVRAQMGGKLVPAGDHWHLSDLGQLQSSSSYQCPNDEMSESGQSSAAATPSTTGTKSNTPTSSVPSAAVTPLNESLQPLGDYVSVTKNNKQAREKRNSRNMEVQVTQEMRNVSIGMGSSDEWSDVQDIIDSTPELDVCPETRLERTGSSPTQGIVNKAFGINTDSLYHELSTAGSEVIGDVDEGADLLGEFSVRDDFFGMGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEELKRVKSEAVTARREPREEVEDVSSYLCTELDKIPMAQRRRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASREHPSVQEKKKSTIWQFFSRLFSSSSSPPPAKRSYPSVNIHYKSPTAAGFSQRRSHALCQISAGSRPLEFFPDDDCTSSARREQKREQYRQVREHVRNDDGRLQACGWSLPAKYKQLSPNGGQEDTRMKNVPVPVYCRPLVEKDPSTKLWCAAGVNLSGWKPHEEDSSNGPKPVPGRDPLTCDREGEGEPKSTHPSPEKKKAKETPEADATSSRVWILTSTLTTSKVVIIDANQPGTIVDQFTVCNAHVLCISSIPAASDSDYPPGEMFLDSDVNPEDSGADGVLAGITLVGCATRCNVPRSNCSSRGDTPVLDKGQGDVATTANGKVNPSQSTEEATEATEVPDPGPSESEATTVRPGPLTEHVFTDPAPTPSSSTQPASENGSESNGTIVQPQVEPSGELSTTTSSAAPTMWLGAQNGWLYVHSAVANWKKCLHSIKLKDSVLSLVHVKGRVLVALADGTLAI,,-1.0,MMEIQMDEGGGVVVYQDDYCSGSVMSERVSGLAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEERESEMKKEYNALHQRHTEMIQTYVEHIERSKMQQVGGSGQTESSLPGRSRKERPTSGNVFPLADGMVRAQMGGKLVPAGDHWHLSDLGQLQSSSSYQCPNDEMSESGQSSAAATPSTTGTKSNTPTSSVPSAAVTPLNESLQPLGDYVSVTKNNKQAREKRNSRNMEVQVTQEMRNVSIGMGSSDEWSDVQDIIDSTPELDVCPETRLERTGSSPTQGIVNKAFGINTDSLYHELSTAGSEVIGDVDEGADLLGEFSVRDDFFGMGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEELKRVKSEAVTARREPREEVEDVSSYLCTELDKIPMAQRRRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASREHPSVQEKKKSTIWQFFSRLFSSSSSPPPAKRSYPSVNIHYKSPTAAGFSQRRSHALCQISAGSRPLEFFPDDDCTSSARREQKREQYRQVREHVRNDDGRLQACGWSLPAKYKQLSPNGGQEDTRMKNVPVPVYCRPLVEKDPSTKLWCAAGVNLSGWKPHEEDSSNGPKPVPGRDPLTCDREGEGEPKSTHPSPEKKKAKETPEADATSSRVWILTSTLTTSKVVIIDANQPGTIVDQFTVCNAHVLCISSIPAASDSDYPPGEMFLDSDVNPEDSGADGVLAGITLVGCATRCNVPRSNCSSRGDTPVLDKGQGDVATTANGKVNPSQSTEEATEATEVPDPGPSESEATTVRPGPLTEHVFTDPAPTPSSSTQPASENGSESNGTIVQPQVEPSGELSTTTSSAAPTMWLGAQNGWLYVHSAVANWKKCLHSIKLKDSVLSLVHVKGRVLVALADGTLAI,C-Jun-amino-terminal kinase-interacting protein 3,"The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. May function as a regulator of vesicle transport, through interactions with the JNK-signaling components and motor proteins. Promotes neuronal axon elongation in a kinesin- and JNK-dependent manner. Activates cofilin at axon tips via local activation of JNK, thereby regulating filopodial dynamics and enhancing axon elongation. Its binding to kinesin heavy chains (KHC), promotes kinesin-1 motility along microtubules and is essential for axon elongation and regeneration. Regulates cortical neuronal migration by mediating NTRK2/TRKB anterograde axonal transport during brain development. Acts as an adapter that bridges the interaction between NTRK2/TRKB and KLC1 and drives NTRK2/TRKB axonal but not dendritic anterograde transport, which is essential for subsequent BDNF-triggered signaling and filopodia formation.",Results in facilitation of JNK binding.,Results in facilitation of JNK binding.
387,0,0,O00899-E474K,MEGLEIEDEDVILLDEDDDSSSSSTVNNSSSNIKNNGNTNNNIGNDDSNKVTLMTSLREKGWGSGMLVDKEKNQYGTIKSYKDDKSSPWFEERQVIATLYKARVLLHEMIYTKMNQERLLSGNLCVGEIQSLLNTQKEDVETDWIAEIQELKRNMVAEIRRNHLLERDVNKLDKRIALLIKHRSNIKDLLLEQNKGKKDKKKKGDDKAEYITLDQKQLESYQNLFYLLQTEPHYLAKLVTLIQADQMEDFLDTVFLTLFGDDFSPREEFLILSLFRLAIGQEMSRIKSAGDLLAVESVVPKMIITYTRRKQGHEFLKQIIAPILENNVVNAPDLNLELNAVQVYQNMISEQEIQTGAKSTLNRGLAEDQIIQLKEVQSILEPRVEKCIQICERFFTGIIQSLNRLPYGIRWICKQIQSIAQKNFDSKPDEIAKVIGYFVYYRFINLAIVTPDAFEILDKELSITSRKNLVNIAKVLQNLFTLKTFQNQGSERWMQPLNKWILSKTSIVRQYLEDLIQVTDPSEYLRVDKYNELTLKLNPVVVISLGEISQTHRLLIANLAALKMKEKEDPLELILKALPAPLEVVDENDREIQLTLINRFKENIEKEISISASLLAETKELVISVLRSIPIQQKQQQQQHDDEKRDDLISILQNAIKHGKETNNPQLSSNAEKIINNLKKMEAEGSIQSENNQYEGFIKVIALEVINRQEIREQQRKERMRLTIALRDLRKHQSYLNDQIQHYTSYLKDVLLHYGPKDKKKSTKPMKISFKELTKKGVIVESDIPKLSHGSTSFYISSDAPGIFDIEARIGVASVGTLSLSLDDLLDKSSAGIPYLKLENIVLDVNMTLHLLNRHFLKNI,,-1.0,MEGLEIEDEDVILLDEDDDSSSSSTVNNSSSNIKNNGNTNNNIGNDDSNKVTLMTSLREKGWGSGMLVDKEKNQYGTIKSYKDDKSSPWFEERQVIATLYKARVLLHEMIYTKMNQERLLSGNLCVGEIQSLLNTQKEDVETDWIAEIQELKRNMVAEIRRNHLLERDVNKLDKRIALLIKHRSNIKDLLLEQNKGKKDKKKKGDDKAEYITLDQKQLESYQNLFYLLQTEPHYLAKLVTLIQADQMEDFLDTVFLTLFGDDFSPREEFLILSLFRLAIGQEMSRIKSAGDLLAVESVVPKMIITYTRRKQGHEFLKQIIAPILENNVVNAPDLNLELNAVQVYQNMISEQEIQTGAKSTLNRGLAEDQIIQLKEVQSILEPRVEKCIQICERFFTGIIQSLNRLPYGIRWICKQIQSIAQKNFDSKPDEIAKVIGYFVYYRFINLAIVTPDAFEILDKELSITSRKNLVNIAEVLQNLFTLKTFQNQGSERWMQPLNKWILSKTSIVRQYLEDLIQVTDPSEYLRVDKYNELTLKLNPVVVISLGEISQTHRLLIANLAALKMKEKEDPLELILKALPAPLEVVDENDREIQLTLINRFKENIEKEISISASLLAETKELVISVLRSIPIQQKQQQQQHDDEKRDDLISILQNAIKHGKETNNPQLSSNAEKIINNLKKMEAEGSIQSENNQYEGFIKVIALEVINRQEIREQQRKERMRLTIALRDLRKHQSYLNDQIQHYTSYLKDVLLHYGPKDKKKSTKPMKISFKELTKKGVIVESDIPKLSHGSTSFYISSDAPGIFDIEARIGVASVGTLSLSLDDLLDKSSAGIPYLKLENIVLDVNMTLHLLNRHFLKNI,Ras GTPase-activating-like protein gapA,Part of signaling pathway that is required for completion of cytokinesis. gapA and rgaA control cortexillin localization to the cleavage furrow and hence may be involved in cleavage of the midbody in the final stage of cytokinesis by regulating the actin cytoskeleton. Forms a complex by linking activated rac1A to ctxA in the absence of rgaA. Assembly of this complex is necessary for the recruitment of cortexillin to the midzone of the dividing cell.,Positively able to complement a gapA null mutant. Negatively charged side chain K474 of GAPA is nonessential for interaction with small GTPases in cytokinesis.,Positively able to complement a gapA null mutant. Negatively charged side chain K474 of GAPA is nonessential for interaction with small GTPases in cytokinesis.
388,0,0,Q84W98-H98S,MATSNDQTNTKSSHSRTLLLLFIFLSLLLFSSLTIPMTRHQSTSMVAPFKRVLLESSVPASSTMDLRPKASTRRSRTSRRREFGNDAHEVPSGPNPISN,,-1.0,MATSNDQTNTKSSHSRTLLLLFIFLSLLLFSSLTIPMTRHQSTSMVAPFKRVLLESSVPASSTMDLRPKASTRRSRTSRRREFGNDAHEVPSGPNPIHN,CLAVATA3/ESR,"Extracellular signal peptide that regulates cell fate. May act with TDR as a ligand-receptor pair in a signal transduction pathway that represses tracheary element differentiation but promotes the formation of procambial cells adjacent to phloem cells in the veins in an auxin-dependent manner. Regulates the transition of protophloem cells from proliferation to differentiation, thus impinging on postembryonic growth capacity of the root meristem; this signaling pathway requires CRN and CLV2.",Enhanced interaction with TDR. The mutation in TDIF leads to [functional stability].,Enhanced interaction with TDR. The mutation in TDIF leads to [functional stability].
389,0,0,P25522-A252R,MSDNDTIVAQATPPGRGGVGILRISGFKAREVAETVLGKLPKPRYADYLPFKDADGSVLDQGIALWFPGPNSFTGEDVLELQGHGGPVILDLLLKRILTIPGLRIARPGEFSERAFLNDKLDLAQAEAIADLIDASSEQAARSALNSLQGAFSARVNHLVEALTHLRIYVEAAIDFPDEEIDFLSDGKIEAQLNDVIADLDAVRAEARQGSLLREGMKVVIAGRPNAGKSSLLNALAGREAAIVTDIAGTTRDVLREHIHIDGMPLHIIDTAGLREASDEVERIGIERAWQEIEQADRVLFMVDGTTTDAVDPAEIWPEFIARLPAKLPITVVRNKADITGETLGMSEVNGHALIRLSARTGEGVDVLRNHLKQSMGFDTNMEGGFLARRRHLQALEQAAEHLQQGKAQLLGAWAGELLAEELRLAQQNLSEITGEFTSDDLLGRIFSSFCIGK,,-1.0,MSDNDTIVAQATPPGRGGVGILRISGFKAREVAETVLGKLPKPRYADYLPFKDADGSVLDQGIALWFPGPNSFTGEDVLELQGHGGPVILDLLLKRILTIPGLRIARPGEFSERAFLNDKLDLAQAEAIADLIDASSEQAARSALNSLQGAFSARVNHLVEALTHLRIYVEAAIDFPDEEIDFLSDGKIEAQLNDVIADLDAVRAEARQGSLLREGMKVVIAGRPNAGKSSLLNALAGREAAIVTDIAGTTADVLREHIHIDGMPLHIIDTAGLREASDEVERIGIERAWQEIEQADRVLFMVDGTTTDAVDPAEIWPEFIARLPAKLPITVVRNKADITGETLGMSEVNGHALIRLSARTGEGVDVLRNHLKQSMGFDTNMEGGFLARRRHLQALEQAAEHLQQGKAQLLGAWAGELLAEELRLAQQNLSEITGEFTSDDLLGRIFSSFCIGK,tRNA modification GTPase MnmE,"Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.",7-fold increase in GTPase activity and 6-fold decrease of affinity.,7-fold increase in GTPase activity and 6-fold decrease of affinity.
390,0,0,Q9ULZ3-Q12L,MGRARDAILDALENLTAEELKKFKLKLLSVPLREGYGRIPRGALLSMDALDLTDKLVSFYLETYGAELTANVLRDMGLQEMAGQLQAATHQGSGAAPAGIQAPPQSAAKPGLHFIDQHRAALIARVTNVEWLLDALYGKVLTDEQYQAVRAEPTNPSKMRKLFSFTPAWNWTCKDLLLQALRESQSYLVEDLERS,,-1.0,MGRARDAILDAQENLTAEELKKFKLKLLSVPLREGYGRIPRGALLSMDALDLTDKLVSFYLETYGAELTANVLRDMGLQEMAGQLQAATHQGSGAAPAGIQAPPQSAAKPGLHFIDQHRAALIARVTNVEWLLDALYGKVLTDEQYQAVRAEPTNPSKMRKLFSFTPAWNWTCKDLLLQALRESQSYLVEDLERS,Apoptosis-associated speck-like protein containing a CARD,"Functions as key mediator in apoptosis and inflammation. Promotes caspase-mediated apoptosis involving predominantly caspase-8 and also caspase-9 in a probable cell type-specific manner. Involved in activation of the mitochondrial apoptotic pathway, promotes caspase-8-dependent proteolytic maturation of BID independently of FADD in certain cell types and also mediates mitochondrial translocation of BAX and activates BAX-dependent apoptosis coupled to activation of caspase-9, -2 and -3. Involved in innate immune response by acting as an integral adapter in the assembly of various inflammasomes (NLRP1, NLRP2, NLRP3, NLRP6, AIM2 and probably IFI16) which recruit and activate caspase-1 leading to processing and secretion of pro-inflammatory cytokines. Caspase-1-dependent inflammation leads to macrophage pyroptosis, a form of cell death. The function as activating adapter in different types of inflammasomes is mediated by the pyrin and CARD domains and their homotypic interactions. Clustered PYCARD nucleates the formation of caspase-1 filaments through the interaction of their respective CARD domains, acting as a platform for of caspase-1 polymerization. In the NLRP1 and NLRC4 inflammasomes seems not be required but facilitates the processing of procaspase-1. In cooperation with NOD2 involved in an inflammasome activated by bacterial muramyl dipeptide leading to caspase-1 activation. May be involved in RIGI-triggered pro-inflammatory responses and inflammasome activation. In collaboration with AIM2 which detects cytosolic double-stranded DNA may also be involved in a caspase-1-independent cell death that involves caspase-8. In adaptive immunity may be involved in maturation of dendritic cells to stimulate T-cell immunity and in cytoskeletal rearrangements coupled to chemotaxis and antigen uptake may be involved in post-transcriptional regulation of the guanine nucleotide exchange factor DOCK2; the latter function is proposed to involve the nuclear form. Also involved in transcriptional activation of cytokines and chemokines independent of the inflammasome; this function may involve AP-1, NF-kappa-B, MAPK and caspase-8 signaling pathways. For regulation of NF-kappa-B activating and inhibiting functions have been reported. Modulates NF-kappa-B induction at the level of the IKK complex by inhibiting kinase activity of CHUK and IKBK. Proposed to compete with RIPK2 for association with CASP1 thereby down-regulating CASP1-mediated RIPK2-dependent NF-kappa-B activation and activating interleukin-1 beta processing. Modulates host resistance to DNA virus infection, probably by inducing the cleavage of and inactivating CGAS in presence of cytoplasmic double-stranded DNA.May have a regulating effect on the function as inflammasome adapter.Seems to inhibit inflammasome-mediated maturation of interleukin-1 beta.",Enhances promotion of apoptosis and NF-kappa-B activation. Mutation of L12 to Q in ASC protein leads to gain of filament formation.,Enhances promotion of apoptosis and NF-kappa-B activation. Mutation of L12 to Q in ASC protein leads to gain of filament formation.
391,0,0,O14746-M170V,MPRAPRCRAVRSLLRSHYREVLPLATFVRRLGPQGWRLVQRGDPAAFRALVAQCLVCVPWDARPPPAAPSFRQVSCLKELVARVLQRLCERGAKNVLAFGFALLDGARGGPPEAFTTSVRSYLPNTVTDALRGSGAWGLLLRRVGDDVLVHLLARCALFVLVAPSCAYQVCGPPLYQLGAATQARPPPHASGPRRRLGCERAWNHSVREAGVPLGLPAPGARRRGGSASRSLPLPKRPRRGAAPEPERTPVGQGSWAHPGRTRGPSDRGFCVVSPARPAEEATSLEGALSGTRHSHPSVGRQHHAGPPSTSRPPRPWDTPCPPVYAETKHFLYSSGDKEQLRPSFLLSSLRPSLTGARRLVETIFLGSRPWMPGTPRRLPRLPQRYWQMRPLFLELLGNHAQCPYGVLLKTHCPLRAAVTPAAGVCAREKPQGSVAAPEEEDTDPRRLVQLLRQHSSPWQVYGFVRACLRRLVPPGLWGSRHNERRFLRNTKKFISLGKHAKLSLQELTWKMSVRDCAWLRRSPGVGCVPAAEHRLREEILAKFLHWLMSVYVVELLRSFFYVTETTFQKNRLFFYRKSVWSKLQSIGIRQHLKRVQLRELSEAEVRQHREARPALLTSRLRFIPKPDGLRPIVNMDYVVGARTFRREKRAERLTSRVKALFSVLNYERARRPGLLGASVLGLDDIHRAWRTFVLRVRAQDPPPELYFVKVDVTGAYDTIPQDRLTEVIASIIKPQNTYCVRRYAVVQKAAHGHVRKAFKSHVSTLTDLQPYMRQFVAHLQETSPLRDAVVIEQSSSLNEASSGLFDVFLRFMCHHAVRIRGKSYVQCQGIPQGSILSTLLCSLCYGDMENKLFAGIRRDGLLLRLVDDFLLVTPHLTHAKTFLRTLVRGVPEYGCVVNLRKTVVNFPVEDEALGGTAFVQMPAHGLFPWCGLLLDTRTLEVQSDYSSYARTSIRASLTFNRGFKAGRNMRRKLFGVLRLKCHSLFLDLQVNSLQTVCTNIYKILLLQAYRFHACVLQLPFHQQ,,-1.0,MPRAPRCRAVRSLLRSHYREVLPLATFVRRLGPQGWRLVQRGDPAAFRALVAQCLVCVPWDARPPPAAPSFRQVSCLKELVARVLQRLCERGAKNVLAFGFALLDGARGGPPEAFTTSVRSYLPNTVTDALRGSGAWGLLLRRVGDDVLVHLLARCALFVLVAPSCAYQMCGPPLYQLGAATQARPPPHASGPRRRLGCERAWNHSVREAGVPLGLPAPGARRRGGSASRSLPLPKRPRRGAAPEPERTPVGQGSWAHPGRTRGPSDRGFCVVSPARPAEEATSLEGALSGTRHSHPSVGRQHHAGPPSTSRPPRPWDTPCPPVYAETKHFLYSSGDKEQLRPSFLLSSLRPSLTGARRLVETIFLGSRPWMPGTPRRLPRLPQRYWQMRPLFLELLGNHAQCPYGVLLKTHCPLRAAVTPAAGVCAREKPQGSVAAPEEEDTDPRRLVQLLRQHSSPWQVYGFVRACLRRLVPPGLWGSRHNERRFLRNTKKFISLGKHAKLSLQELTWKMSVRDCAWLRRSPGVGCVPAAEHRLREEILAKFLHWLMSVYVVELLRSFFYVTETTFQKNRLFFYRKSVWSKLQSIGIRQHLKRVQLRELSEAEVRQHREARPALLTSRLRFIPKPDGLRPIVNMDYVVGARTFRREKRAERLTSRVKALFSVLNYERARRPGLLGASVLGLDDIHRAWRTFVLRVRAQDPPPELYFVKVDVTGAYDTIPQDRLTEVIASIIKPQNTYCVRRYAVVQKAAHGHVRKAFKSHVSTLTDLQPYMRQFVAHLQETSPLRDAVVIEQSSSLNEASSGLFDVFLRFMCHHAVRIRGKSYVQCQGIPQGSILSTLLCSLCYGDMENKLFAGIRRDGLLLRLVDDFLLVTPHLTHAKTFLRTLVRGVPEYGCVVNLRKTVVNFPVEDEALGGTAFVQMPAHGLFPWCGLLLDTRTLEVQSDYSSYARTSIRASLTFNRGFKAGRNMRRKLFGVLRLKCHSLFLDLQVNSLQTVCTNIYKILLLQAYRFHACVLQLPFHQQ,Telomerase reverse transcriptase,"Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. Active in progenitor and cancer cells. Inactive, or very low activity, in normal somatic cells. Catalytic component of the teleromerase holoenzyme complex whose main activity is the elongation of telomeres by acting as a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme. Catalyzes the RNA-dependent extension of 3'-chromosomal termini with the 6-nucleotide telomeric repeat unit, 5'-TTAGGG-3'. The catalytic cycle involves primer binding, primer extension and release of product once the template boundary has been reached or nascent product translocation followed by further extension. More active on substrates containing 2 or 3 telomeric repeats. Telomerase activity is regulated by a number of factors including telomerase complex-associated proteins, chaperones and polypeptide modifiers. Modulates Wnt signaling. Plays important roles in aging and antiapoptosis.","Highly increases telomerase activity in PFBMFT1; the mutant protein is demonstrated to cause increased telomerase activity. The mutation in the hTERT gene is associated with dyskeratosis congenita, a bone marrow failure syndrome characterized by mucocutaneous features. It can also be found in some cases of sporadic aplastic anemia (AA) and idiopathic pulmonary fibrosis. The presence of this mutation affects the clinical outcome and can be used for genetic testing.","Highly increases telomerase activity in PFBMFT1; the mutant protein is demonstrated to cause increased telomerase activity. The mutation in the hTERT gene is associated with dyskeratosis congenita, a bone marrow failure syndrome characterized by mucocutaneous features. It can also be found in some cases of sporadic aplastic anemia (AA) and idiopathic pulmonary fibrosis. The presence of this mutation affects the clinical outcome and can be used for genetic testing."
392,0,0,Q6MZP7-Y527C,MEVVPAEVNSLLPEEIMDTGITLVDDDSIEAVIVSSPIPMETELEEIVNINSTGDSTATPISTEPITVYSNHTNQVAVNTTITKADSNTTVKPAFPSGLQKLGAQTPVTISANQIILNKVSQTSDLKLGNQTLKPDGQKLILTTLGKSGSPIVLALPHSQLPQAQKVTTQAQSGDAKLPPQQIKVVTIGGRPEVKPVIGVSALTPGSQLINTTTQPSVLQTQQLKTVQIAKKPRTPTSGPVITKLIFAKPINSKAVTGQTTQVSPPVIAGRVLSQSTPGTPSKTITISESGVIGSTLNSTTQTPNKIAISPLKSPNKAVKSTVQTITVGGVSTSQFKTIIPLATAPNVQQIQVPGSKFHYVRLVTATSASSSTQPVSQNPSTNTQPLQQAKPVVVNTTPVRMSVPIVSAQAVKQVVPKPINPTSQIVTTSQPQQRLIMPATPLPQIQPNLTNLPPGTVLAPAPGTGNVGYAVLPAQYVTQLQQSSYVSIASNSTFTGTSGIQTQARLPFNGIIPSESASRPRKPCNCTKSLCLKLYCDCFANGEFCNNCNCTNCYNNLEHENERQKAIKACLDRNPEAFKPKIGKGKEGESDRRHSKGCNCKRSGCLKNYCECYEAKIMCSSICKCIGCKNFEESPERKTLMHLADAAEVRVQQQTAAKTKLSSQISDLLTRPTPALNSGGGKLPFTFVTKEVAEATCNCLLAQAEQADKKGKSKAAAERMILEEFGRCLMSVINSAGKAKSDPCAMNC,,-1.0,MEVVPAEVNSLLPEEIMDTGITLVDDDSIEAVIVSSPIPMETELEEIVNINSTGDSTATPISTEPITVYSNHTNQVAVNTTITKADSNTTVKPAFPSGLQKLGAQTPVTISANQIILNKVSQTSDLKLGNQTLKPDGQKLILTTLGKSGSPIVLALPHSQLPQAQKVTTQAQSGDAKLPPQQIKVVTIGGRPEVKPVIGVSALTPGSQLINTTTQPSVLQTQQLKTVQIAKKPRTPTSGPVITKLIFAKPINSKAVTGQTTQVSPPVIAGRVLSQSTPGTPSKTITISESGVIGSTLNSTTQTPNKIAISPLKSPNKAVKSTVQTITVGGVSTSQFKTIIPLATAPNVQQIQVPGSKFHYVRLVTATSASSSTQPVSQNPSTNTQPLQQAKPVVVNTTPVRMSVPIVSAQAVKQVVPKPINPTSQIVTTSQPQQRLIMPATPLPQIQPNLTNLPPGTVLAPAPGTGNVGYAVLPAQYVTQLQQSSYVSIASNSTFTGTSGIQTQARLPFNGIIPSESASRPRKPCNYTKSLCLKLYCDCFANGEFCNNCNCTNCYNNLEHENERQKAIKACLDRNPEAFKPKIGKGKEGESDRRHSKGCNCKRSGCLKNYCECYEAKIMCSSICKCIGCKNFEESPERKTLMHLADAAEVRVQQQTAAKTKLSSQISDLLTRPTPALNSGGGKLPFTFVTKEVAEATCNCLLAQAEQADKKGKSKAAAERMILEEFGRCLMSVINSAGKAKSDPCAMNC,Protein lin-54 homolog,"Component of the DREAM complex, a multiprotein complex that can both act as a transcription activator or repressor depending on the context. In G0 phase, the complex binds to more than 800 promoters and is required for repression of E2F target genes. In S phase, the complex selectively binds to the promoters of G2/M genes whose products are required for mitosis and participates in their cell cycle dependent activation. In the complex, acts as a DNA-binding protein that binds the promoter of CDK1 in a sequence-specific manner. Specifically recognizes the consensus motif 5'-TTYRAA-3' in target DNA.",Enhances DNA-binding to the CDK1 promoter; when associated with Y-525. The mutation in LIN54 is found to be unnecessary for cell cycle progression.,Enhances DNA-binding to the CDK1 promoter; when associated with Y-525. The mutation in LIN54 is found to be unnecessary for cell cycle progression.
393,0,0,P38516-A140K,MAQVDLLNVKGEKVGTLEISDFVFNIDPNYDVMWRYVDMQLSNRRAGTASTKTRGEVSGGGRKPWPQKHTGRARHGSIRSPIWRHGGVVHGPKPRDWSKKLNKKMKKLALRSALSVKYRENKLLVLDDLKLERPKTKSLKEILQNLQLSDKKTLIVLPWKEEGYMNVKLSGRNLPDVKVIIADNPNNSKNGEKAVRIDGLNVFDMLKYDYLVLTRDMVSKIEEVLGNEAGKALTA,,-1.0,MAQVDLLNVKGEKVGTLEISDFVFNIDPNYDVMWRYVDMQLSNRRAGTASTKTRGEVSGGGRKPWPQKHTGRARHGSIRSPIWRHGGVVHGPKPRDWSKKLNKKMKKLALRSALSVKYRENKLLVLDDLKLERPKTKSLAEILQNLQLSDKKTLIVLPWKEEGYMNVKLSGRNLPDVKVIIADNPNNSKNGEKAVRIDGLNVFDMLKYDYLVLTRDMVSKIEEVLGNEAGKALTA,Large ribosomal subunit protein uL4,"One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome.This protein only weakly controls expression of the E.coli S10 operon. It is incorporated into E.coli ribosomes, however it is not as firmly associated as the endogenous protein.Forms part of the polypeptide exit tunnel.","Enhances regulation of the E.coli S10 operon, and improves association with E.coli ribosome; when associated with E141Q, Q144K, Q147A, S149E, K151delta, K152delta, I155M, P158G, W159E and K160L. The area around helices alpha4 and alpha5, which is critical for the initial folding steps of the large subunit, is also a peripheral element of autogenous control, presumably by detaching from the S10 mRNA leader.","Enhances regulation of the E.coli S10 operon, and improves association with E.coli ribosome; when associated with E141Q, Q144K, Q147A, S149E, K151delta, K152delta, I155M, P158G, W159E and K160L. The area around helices alpha4 and alpha5, which is critical for the initial folding steps of the large subunit, is also a peripheral element of autogenous control, presumably by detaching from the S10 mRNA leader."
394,0,0,Q504J1-A296C,MEDITQLLSDVLEDLVESELKQFTRQLWIGVKPGVEPIPRGKLENKDRQDVVDSMVQQYSEDAGTITVQTLRKIKQNERAKRLESNLLKVQSQGQENKQNSEEPQPIPQIISQPIQQIISQPINNAGSEDLQPIQADWQRPRQIIPCSQETKNTLLKAHGDDIYTPRSGTQRKGLALLITNIQFANTQHNRNGADRDEENAEWLLRSLGFAVIKYRNLSGKDIRRAVENFSKRREHEDADSTFIVIMSHGTRIDNKDAIVGVSDDVYFIEETFSHLNSVNCPALIDKPKVILIQACRGGQSSGVLAQDSVFASDSWVHMEKDFVCFMSTMPNTFAYRNPIEGSFFISYIVDVFCSSAHRDDIMELFRKVTLRMEKDQRFQGQAKLLPCIERTSISKRFYLFPGL,,-1.0,MEDITQLLSDVLEDLVESELKQFTRQLWIGVKPGVEPIPRGKLENKDRQDVVDSMVQQYSEDAGTITVQTLRKIKQNERAKRLESNLLKVQSQGQENKQNSEEPQPIPQIISQPIQQIISQPINNAGSEDLQPIQADWQRPRQIIPCSQETKNTLLKAHGDDIYTPRSGTQRKGLALLITNIQFANTQHNRNGADRDEENAEWLLRSLGFAVIKYRNLSGKDIRRAVENFSKRREHEDADSTFIVIMSHGTRIDNKDAIVGVSDDVYFIEETFSHLNSVNCPALIDKPKVILIQAARGGQSSGVLAQDSVFASDSWVHMEKDFVCFMSTMPNTFAYRNPIEGSFFISYIVDVFCSSAHRDDIMELFRKVTLRMEKDQRFQGQAKLLPCIERTSISKRFYLFPGL,Caspase b,"Thiol protease which cleaves IL-1 beta (il1b), releasing the mature cytokine which is involved in a variety of inflammatory processes, and mediates apoptosis. Component of the NLRP1 inflammasome, which plays a crucial role in innate immunity and inflammation. In response to pathogens and other damage-associated signals, recruited to the NLRP1 inflammasome in its precursor form following the recruitment of caspase caspa. Its subsequent activation causes the cleavage of the midformed pro-il1b and results in il1b maturation and secretion in the extracellular milieu. Activated by direct binding to bacterial lipopolysaccharides (LPS), which causes non-canonical inflammasome activation and results in the pyroptosis of infected cells and their extrusion into the gut lumen, as well as in cytokine secretion. Plays a crucial role in the restriction of bacterial infection to intestinal sites. Pyroptosis limits bacterial replication, while cytokine secretion promotes the recruitment and activation of immune cells and triggers mucosal inflammation. Promotes pyroptosis by bacterial infection by E.piscicida.",Abolishes catalytic inactivity. Abolishes pyroptosis inhibition induced by bacterial lipopolysaccharides (LPS).,Abolishes catalytic inactivity. Abolishes pyroptosis inhibition induced by bacterial lipopolysaccharides (LPS).
395,0,0,Q9ULZ3-A40P,MGRARDAILDALENLTAEELKKFKLKLLSVPLREGYGRIPRGALLSMDALDLTDKLVSFYLETYGAELTANVLRDMGLQEMAGQLQAATHQGSGAAPAGIQAPPQSAAKPGLHFIDQHRAALIARVTNVEWLLDALYGKVLTDEQYQAVRAEPTNPSKMRKLFSFTPAWNWTCKDLLLQALRESQSYLVEDLERS,,-1.0,MGRARDAILDALENLTAEELKKFKLKLLSVPLREGYGRIARGALLSMDALDLTDKLVSFYLETYGAELTANVLRDMGLQEMAGQLQAATHQGSGAAPAGIQAPPQSAAKPGLHFIDQHRAALIARVTNVEWLLDALYGKVLTDEQYQAVRAEPTNPSKMRKLFSFTPAWNWTCKDLLLQALRESQSYLVEDLERS,Apoptosis-associated speck-like protein containing a CARD,"Functions as key mediator in apoptosis and inflammation. Promotes caspase-mediated apoptosis involving predominantly caspase-8 and also caspase-9 in a probable cell type-specific manner. Involved in activation of the mitochondrial apoptotic pathway, promotes caspase-8-dependent proteolytic maturation of BID independently of FADD in certain cell types and also mediates mitochondrial translocation of BAX and activates BAX-dependent apoptosis coupled to activation of caspase-9, -2 and -3. Involved in innate immune response by acting as an integral adapter in the assembly of various inflammasomes (NLRP1, NLRP2, NLRP3, NLRP6, AIM2 and probably IFI16) which recruit and activate caspase-1 leading to processing and secretion of pro-inflammatory cytokines. Caspase-1-dependent inflammation leads to macrophage pyroptosis, a form of cell death. The function as activating adapter in different types of inflammasomes is mediated by the pyrin and CARD domains and their homotypic interactions. Clustered PYCARD nucleates the formation of caspase-1 filaments through the interaction of their respective CARD domains, acting as a platform for of caspase-1 polymerization. In the NLRP1 and NLRC4 inflammasomes seems not be required but facilitates the processing of procaspase-1. In cooperation with NOD2 involved in an inflammasome activated by bacterial muramyl dipeptide leading to caspase-1 activation. May be involved in RIGI-triggered pro-inflammatory responses and inflammasome activation. In collaboration with AIM2 which detects cytosolic double-stranded DNA may also be involved in a caspase-1-independent cell death that involves caspase-8. In adaptive immunity may be involved in maturation of dendritic cells to stimulate T-cell immunity and in cytoskeletal rearrangements coupled to chemotaxis and antigen uptake may be involved in post-transcriptional regulation of the guanine nucleotide exchange factor DOCK2; the latter function is proposed to involve the nuclear form. Also involved in transcriptional activation of cytokines and chemokines independent of the inflammasome; this function may involve AP-1, NF-kappa-B, MAPK and caspase-8 signaling pathways. For regulation of NF-kappa-B activating and inhibiting functions have been reported. Modulates NF-kappa-B induction at the level of the IKK complex by inhibiting kinase activity of CHUK and IKBK. Proposed to compete with RIPK2 for association with CASP1 thereby down-regulating CASP1-mediated RIPK2-dependent NF-kappa-B activation and activating interleukin-1 beta processing. Modulates host resistance to DNA virus infection, probably by inducing the cleavage of and inactivating CGAS in presence of cytoplasmic double-stranded DNA.May have a regulating effect on the function as inflammasome adapter.Seems to inhibit inflammasome-mediated maturation of interleukin-1 beta.",Enhances homooligomerization. Mutation of P40 to A in ASC protein leads to gain of filament formation.,Enhances homooligomerization. Mutation of P40 to A in ASC protein leads to gain of filament formation.
396,0,0,Q9GYF0-G576Y,MRTSQAIFILIFLDSVRNQSPQVIPAKWDVVYEKETGHNMSLTVFRFQVKEQYSVARIIMSCNESTEHNPLLAVFREKLAILSLQVPLIVDNYEYSQVARTLCPFTEYKEGEAFTVEVTSSRPVHYNFRAELVQNFYLYNNSQRLVTASASEPVYLRYDIPGDVDSVAVHLDSNSTICMTVSVQKIGCPVFDLPDNVNSMGLHQTMTTSATIPVEKSRMSSFYVVFVVNTNDDLCSEILSIKPNKPTKFPLRMKSFNVTIESSMKIFDYTIPIVFWACILLLVTIVVFVYHYFDGIWERRFVSRAYTHLEDNAQEQRIRDFYDFQRMSEDDDLKDYDLLTDCQDMMVVRAKASLTVADLSMTPYEERELKYDVYKIALAIIGIFYNITVLQLIISKAGSLRQSGDLDECTFNFQCARPLWYFVAFNNVVSNGGYVYFGTLIIVMNYCRERSFRRLFAVQPTLAERYGLPQHSGLMTAIGLAVIMEGISSATYHVCPNNINYQFDTALMYVIGMLGKLKIWSLRHPDMVVSAYHAFGFLGVFLMAAIAGVYVHNMIFWALFSIIYIASMLLVSLEFYFKGIWTLNLRELRNSIRLSWVSSRHLSCVVPAYKARFFVILLLNIANTAVVVYGLEAHPKDFLSFLLIPFIGNLFIYIIYYILMKMIYREKIPKRAIALLFAAVISWTCAGILFNQRVSDWSKMPAISRELNKPCIFLNFYDNHDLWHLSSAFAIFFSFTAINVIDDDLMFVMRNTIRVF,,-1.0,MRTSQAIFILIFLDSVRNQSPQVIPAKWDVVYEKETGHNMSLTVFRFQVKEQYSVARIIMSCNESTEHNPLLAVFREKLAILSLQVPLIVDNYEYSQVARTLCPFTEYKEGEAFTVEVTSSRPVHYNFRAELVQNFYLYNNSQRLVTASASEPVYLRYDIPGDVDSVAVHLDSNSTICMTVSVQKIGCPVFDLPDNVNSMGLHQTMTTSATIPVEKSRMSSFYVVFVVNTNDDLCSEILSIKPNKPTKFPLRMKSFNVTIESSMKIFDYTIPIVFWACILLLVTIVVFVYHYFDGIWERRFVSRAYTHLEDNAQEQRIRDFYDFQRMSEDDDLKDYDLLTDCQDMMVVRAKASLTVADLSMTPYEERELKYDVYKIALAIIGIFYNITVLQLIISKAGSLRQSGDLDECTFNFQCARPLWYFVAFNNVVSNGGYVYFGTLIIVMNYCRERSFRRLFAVQPTLAERYGLPQHSGLMTAIGLAVIMEGISSATYHVCPNNINYQFDTALMYVIGMLGKLKIWSLRHPDMVVSAYHAFGFLGVFLMAAIAGVYVHNMIFWALFSIIYIASMLLVSLEFGFKGIWTLNLRELRNSIRLSWVSSRHLSCVVPAYKARFFVILLLNIANTAVVVYGLEAHPKDFLSFLLIPFIGNLFIYIIYYILMKMIYREKIPKRAIALLFAAVISWTCAGILFNQRVSDWSKMPAISRELNKPCIFLNFYDNHDLWHLSSAFAIFFSFTAINVIDDDLMFVMRNTIRVF,Cholesterol uptake protein 1,Cholesterol-binding protein which is involved in dietary cholesterol uptake from the environment. Does not play a role in double-stranded RNA transport in contrast to other SID1 family members.,"Increased interaction with cholesterol. The mutation in the ChUP-1 protein is mentioned in the document. However, the functional changes caused by this mutation are not described in the document.","Increased interaction with cholesterol. The mutation in the ChUP-1 protein is mentioned in the document. However, the functional changes caused by this mutation are not described in the document."
397,0,0,A0A0H2URG7-A98N,MTIYNINLGIGWASSGVEYAQAYRAGVFRKLNLSSKFIFTDMILADNIQHLTANIGFDDNQVIWLYNHFTDIKIAPTSVTVDDVLAYFGGEESHREKNGKVLRVFFFDQDKFVTCYLVDENKDLVQHAEYVFKGNLIRKDYFSYTRYCSEYFAPKDNVAVLYQRTFYNEDGTPVYDILMNQGKEEVYHFKDKIFYGKQAFVRAFMKSLNLNKSDLVILDRETGIGQVVFEEAQTAHLAVVVHAEHYSENATNEDYILWNNYYDYQFTNADKVDFFIVSTDRQNEVLQEQFAKYTQHQPKIVTIPVGSIDSLTDSSQGRKPFSLITASRLAKEKHIDWLVKAVIEAHKELPELTFDIYGSGGEDSLLREIIANHQAEDYIQLKGHAELSQIYSQYEVYLTASTSEGFGLTLMEAIGSGLPLIGFDVPYGNQTFIEDGQNGYLIPSSSDHVEDQIKQAYAAKICQLYQENRLEAMRAYSYQIAEGFLTKEILEKWKKTVEEVLHD,,-1.0,MTIYNINLGIGWASSGVEYAQAYRAGVFRKLNLSSKFIFTDMILADNIQHLTANIGFDDNQVIWLYNHFTDIKIAPTSVTVDDVLAYFGGEESHREKAGKVLRVFFFDQDKFVTCYLVDENKDLVQHAEYVFKGNLIRKDYFSYTRYCSEYFAPKDNVAVLYQRTFYNEDGTPVYDILMNQGKEEVYHFKDKIFYGKQAFVRAFMKSLNLNKSDLVILDRETGIGQVVFEEAQTAHLAVVVHAEHYSENATNEDYILWNNYYDYQFTNADKVDFFIVSTDRQNEVLQEQFAKYTQHQPKIVTIPVGSIDSLTDSSQGRKPFSLITASRLAKEKHIDWLVKAVIEAHKELPELTFDIYGSGGEDSLLREIIANHQAEDYIQLKGHAELSQIYSQYEVYLTASTSEGFGLTLMEAIGSGLPLIGFDVPYGNQTFIEDGQNGYLIPSSSDHVEDQIKQAYAAKICQLYQENRLEAMRAYSYQIAEGFLTKEILEKWKKTVEEVLHD,UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase GtfA subunit,Required for the polymorphic O-glycosylation of serine-rich repeat protein PsrP. Catalyzes the first step in glycosylation by transferring N-acetylglucosamine from UDP-GlcNAc to serine residues in PsrP. Part of the accessory SecA2/SecY2 system specifically required to export serine-rich repeat cell wall proteins encoded upstream in the same operon (Probable). The GtfA-GtfB complex adds GlcNAc from UDP-GlcNAc to PsrP (experimentally characterized with truncated PsrP-SSR1 constructs); this subunit alone has weak N-acetylglucosaminyl transferase activity that is 10-fold stimulated by GtfB. The complex requires at least a 25 residue-long peptide for activity; the in vitro assay has only been seen to glycosylate Ser residues. The alpha linkage was shown in L.reuteri.,"Increased N-acetylglucosaminyl transferase activity, increased binding of PsrP.","Increased N-acetylglucosaminyl transferase activity, increased binding of PsrP."
398,0,0,Q6UWV6-Q168N,MRGPAVLLTVALATLLAPGAGAPVQSQGSQNKLLLVSFDGFRWNYDQDVDTPNLDAMARDGVKARYMTPAFVTMTSPCHFTLVTGKYIENHGVVHNMYYNTTSKVKLPYHATLGIQRWWDNGSVPIWITAQRQGLRAGSFFYPGGNVTYQGVAVTRSRKEGIAHNYKNETEWRANIDTVMAWFTEEDLDLVTLYFGEPDSTGHRYGPESPERREMVRQVDRTVGYLRESIARNHLTDRLNLIITSDHGMTTVDKRAGDLVEFHKFPNFTFRDIEFELLDYGPNGMLLPKEGRLEKVYDALKDAHPKLHVYKKEAFPEAFHYANNPRVTPLLMYSDLGYVIHGRINVQFNNGEHGFDNKDMDMKTIFRAVGPSFRAGLEVEPFESVHVYELMCRLLGIVPEANDGHLATLLPMLHTESALPPDGRPTLLPKGRSALPPSSRPLLVMGLLGTVILLSEVA,,-1.0,MRGPAVLLTVALATLLAPGAGAPVQSQGSQNKLLLVSFDGFRWNYDQDVDTPNLDAMARDGVKARYMTPAFVTMTSPCHFTLVTGKYIENHGVVHNMYYNTTSKVKLPYHATLGIQRWWDNGSVPIWITAQRQGLRAGSFFYPGGNVTYQGVAVTRSRKEGIAHNYKQETEWRANIDTVMAWFTEEDLDLVTLYFGEPDSTGHRYGPESPERREMVRQVDRTVGYLRESIARNHLTDRLNLIITSDHGMTTVDKRAGDLVEFHKFPNFTFRDIEFELLDYGPNGMLLPKEGRLEKVYDALKDAHPKLHVYKKEAFPEAFHYANNPRVTPLLMYSDLGYVIHGRINVQFNNGEHGFDNKDMDMKTIFRAVGPSFRAGLEVEPFESVHVYELMCRLLGIVPEANDGHLATLLPMLHTESALPPDGRPTLLPKGRSALPPSSRPLLVMGLLGTVILLSEVA,Ectonucleotide pyrophosphatase/phosphodiesterase family member 7,"Choline-specific phosphodiesterase that hydrolyzes sphingomyelin releasing the ceramide and phosphocholine and therefore is involved in sphingomyelin digestion, ceramide formation, and fatty acid (FA) absorption in the gastrointestinal tract. Has also phospholipase C activity and can also cleave phosphocholine from palmitoyl lyso-phosphatidylcholine and platelet-activating factor (PAF) leading to its inactivation. Does not have nucleotide pyrophosphatase activity. May promote cholesterol absorption by affecting the levels of sphingomyelin derived from either diet or endogenous sources, in the intestinal lumen.",Strongly increases N-glycosylation and enzyme activity; when associated with Q-100; Q-121; Q-168 and Q-267. The mutation in alk-SMase greatly enhances its activity.,Strongly increases N-glycosylation and enzyme activity; when associated with Q-100; Q-121; Q-168 and Q-267. The mutation in alk-SMase greatly enhances its activity.
399,0,0,Q96MP8-C184R,MVVVTGREPDSRRQDGAMSSSDAEDDFLEPATPTATQAGHALPLLPQEFPEVVPLNIGGAHFTTRLSTLRCYEDTMLAAMFSGRHYIPTDSEGRYFIDRDGTHFGDVLNFLRSGDLPPRERVRAVYKEAQYYAIGPLLEQLENMQPLKGEKVRQAFLGLMPYYKDHLERIVEIARLRAVQRKARFAKLKVCVFKEEMPITPYECPLLNSLRFERSESDGQLFEHHCEVDVSFGPWEAVADVYDLLHCLVTDLSAQGLTVDHQCIGVCDKHLVNHYYCKRPIYEFKITWW,,-1.0,MVVVTGREPDSRRQDGAMSSSDAEDDFLEPATPTATQAGHALPLLPQEFPEVVPLNIGGAHFTTRLSTLRCYEDTMLAAMFSGRHYIPTDSEGRYFIDRDGTHFGDVLNFLRSGDLPPRERVRAVYKEAQYYAIGPLLEQLENMQPLKGEKVRQAFLGLMPYYKDHLERIVEIARLRAVQRKACFAKLKVCVFKEEMPITPYECPLLNSLRFERSESDGQLFEHHCEVDVSFGPWEAVADVYDLLHCLVTDLSAQGLTVDHQCIGVCDKHLVNHYYCKRPIYEFKITWW,BTB/POZ domain-containing protein KCTD7,May be involved in the control of excitability of cortical neurons.,"Markedly enhances localization at the cell membrane and disappearance of prominent cytoplasmic aggregates. The identified variant maintained the localization pattern of KCTD7 and promoted interaction with cullin-3, a ubiquitin-ligase component and known KCTD7 interactor. This study clearly demonstrates that KCTD7 mutations also alleviate a rare, infantile-onset NCL subtype designated as CLN14.","Markedly enhances localization at the cell membrane and disappearance of prominent cytoplasmic aggregates. The identified variant maintained the localization pattern of KCTD7 and promoted interaction with cullin-3, a ubiquitin-ligase component and known KCTD7 interactor. This study clearly demonstrates that KCTD7 mutations also alleviate a rare, infantile-onset NCL subtype designated as CLN14."
400,0,0,P25522-A253D,MSDNDTIVAQATPPGRGGVGILRISGFKAREVAETVLGKLPKPRYADYLPFKDADGSVLDQGIALWFPGPNSFTGEDVLELQGHGGPVILDLLLKRILTIPGLRIARPGEFSERAFLNDKLDLAQAEAIADLIDASSEQAARSALNSLQGAFSARVNHLVEALTHLRIYVEAAIDFPDEEIDFLSDGKIEAQLNDVIADLDAVRAEARQGSLLREGMKVVIAGRPNAGKSSLLNALAGREAAIVTDIAGTTRDVLREHIHIDGMPLHIIDTAGLREASDEVERIGIERAWQEIEQADRVLFMVDGTTTDAVDPAEIWPEFIARLPAKLPITVVRNKADITGETLGMSEVNGHALIRLSARTGEGVDVLRNHLKQSMGFDTNMEGGFLARRRHLQALEQAAEHLQQGKAQLLGAWAGELLAEELRLAQQNLSEITGEFTSDDLLGRIFSSFCIGK,,-1.0,MSDNDTIVAQATPPGRGGVGILRISGFKAREVAETVLGKLPKPRYADYLPFKDADGSVLDQGIALWFPGPNSFTGEDVLELQGHGGPVILDLLLKRILTIPGLRIARPGEFSERAFLNDKLDLAQAEAIADLIDASSEQAARSALNSLQGAFSARVNHLVEALTHLRIYVEAAIDFPDEEIDFLSDGKIEAQLNDVIADLDAVRAEARQGSLLREGMKVVIAGRPNAGKSSLLNALAGREAAIVTDIAGTTRAVLREHIHIDGMPLHIIDTAGLREASDEVERIGIERAWQEIEQADRVLFMVDGTTTDAVDPAEIWPEFIARLPAKLPITVVRNKADITGETLGMSEVNGHALIRLSARTGEGVDVLRNHLKQSMGFDTNMEGGFLARRRHLQALEQAAEHLQQGKAQLLGAWAGELLAEELRLAQQNLSEITGEFTSDDLLGRIFSSFCIGK,tRNA modification GTPase MnmE,"Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.","9-fold increase in GTPase activity and 13-fold decrease of affinity. Residues in the G2 motif (249GTTRD253), which resides in the switch I region, are important for GTP binding but do not play any role in stabilizing the transition state.","9-fold increase in GTPase activity and 13-fold decrease of affinity. Residues in the G2 motif (249GTTRD253), which resides in the switch I region, are important for GTP binding but do not play any role in stabilizing the transition state."
401,0,0,P32266-K294E,MNASPVRLLILRRQLATHPAILYSSPYIKSPLVHLHSRMSNVHRSAHANALSFVITRRSISHFPKIISKIIRLPIYVGGGMAAAGSYIAYKMEEASSFTKDKLDRIKDLGESMKEKFNKMFSGDKSQDGGHGNDGTVPTATLIAATSLDDDESKRQGDPKDDDDEDDDDEDDENDSVDTTQDEMLNLTKQMIEIRTILNKVDSSSAHLTLPSIVVIGSQSSGKSSVLESIVGREFLPKGSNMVTRRPIELTLVNTPNSNNVTADFPSMRLYNIKDFKEVKRMLMELNMAVPTSEAVSEEPIQLTIKSSRVPDLSLVDLPGYIQVEAADQPIELKTKIRDLCEKYLTAPNIILAISAADVDLANSSALKASKAADPKGLRTIGVITKLDLVDPEKARSILNNKKYPLSMGYVGVITKTPSSINRKHLGLFGEAPSSSLSGIFSKGQHGQSSGEENTNGLKQIVSHQFEKAYFKENKKYFTNCQVSTKKLREKLIKILEISMSNALEPTSTLIQQELDDTSYLFKVEFNDRHLTPKSYLLNNIDVLKLGIKEFQEKFHRNELKSILRAELDQKVLDVLATRYWKDDNLQDLSSSKLESDTDMLYWHKKLELASSGLTKMGIGRLSTMLTTNAILKELDNILESTQLKNHELIKDLVSNTAINVLNSKYYSTADQVENCIKPFKYEIDLEERDWSLARQHSINLIKEELRQCNSRYQAIKNAVGSKKLANVMGYLENESNLQKETLGMSKLLLERGSEAIFLDKRCKVLSFRLKMLKNKCHSTIEKDRCPEVFLSAVSDKLTSTAVLFLNVELLSDFFYNFPIELDRRLTLLGDEQVEMFAKEDPKISRHIELQKRKELLELALEKIDSILVFKKSYKGVSKNL,,-1.0,MNASPVRLLILRRQLATHPAILYSSPYIKSPLVHLHSRMSNVHRSAHANALSFVITRRSISHFPKIISKIIRLPIYVGGGMAAAGSYIAYKMEEASSFTKDKLDRIKDLGESMKEKFNKMFSGDKSQDGGHGNDGTVPTATLIAATSLDDDESKRQGDPKDDDDEDDDDEDDENDSVDTTQDEMLNLTKQMIEIRTILNKVDSSSAHLTLPSIVVIGSQSSGKSSVLESIVGREFLPKGSNMVTRRPIELTLVNTPNSNNVTADFPSMRLYNIKDFKEVKRMLMELNMAVPTSKAVSEEPIQLTIKSSRVPDLSLVDLPGYIQVEAADQPIELKTKIRDLCEKYLTAPNIILAISAADVDLANSSALKASKAADPKGLRTIGVITKLDLVDPEKARSILNNKKYPLSMGYVGVITKTPSSINRKHLGLFGEAPSSSLSGIFSKGQHGQSSGEENTNGLKQIVSHQFEKAYFKENKKYFTNCQVSTKKLREKLIKILEISMSNALEPTSTLIQQELDDTSYLFKVEFNDRHLTPKSYLLNNIDVLKLGIKEFQEKFHRNELKSILRAELDQKVLDVLATRYWKDDNLQDLSSSKLESDTDMLYWHKKLELASSGLTKMGIGRLSTMLTTNAILKELDNILESTQLKNHELIKDLVSNTAINVLNSKYYSTADQVENCIKPFKYEIDLEERDWSLARQHSINLIKEELRQCNSRYQAIKNAVGSKKLANVMGYLENESNLQKETLGMSKLLLERGSEAIFLDKRCKVLSFRLKMLKNKCHSTIEKDRCPEVFLSAVSDKLTSTAVLFLNVELLSDFFYNFPIELDRRLTLLGDEQVEMFAKEDPKISRHIELQKRKELLELALEKIDSILVFKKSYKGVSKNL,"Dynamin-like GTPase MGM1, mitochondrial",Dynamin-related GTPase required for mitochondrial fusion. Coordinates interaction between the inner and outer mitochondrial membrane to promote the formation of the double membrane.,Enhances function at 37 degrees Celsius. A version of mgm1 mutated in a conserved residue in the putative GTP-binding site was able to complement all of the mutant defects. It also caused normal mitochondrial distribution and morphology when expressed at high levels in cells that also contained a wild-type copy of the gene. Mgm1p was localized to the mitochondrial outer membrane and fractionated as a component of a low molecular weight complex.,Enhances function at 37 degrees Celsius. A version of mgm1 mutated in a conserved residue in the putative GTP-binding site was able to complement all of the mutant defects. It also caused normal mitochondrial distribution and morphology when expressed at high levels in cells that also contained a wild-type copy of the gene. Mgm1p was localized to the mitochondrial outer membrane and fractionated as a component of a low molecular weight complex.
402,0,0,Q9HAY6-M170T,MDIIFGRNRKEQLEPVRAKVTGKIPAWLQGTLLRNGPGMHTVGESRYNHWFDGLALLHSFTIRDGEVYYRSKYLRSDTYNTNIEANRIVVSEFGTMAYPDPCKNIFSKAFSYLSHTIPDFTDNCLINIMKCGEDFYATSETNYIRKINPQTLETLEKVDYRKYVAVNLATSHPHYDEAGNVLNMGTSIVEKGKTKYVIFKIPATVPEGKKQGKSPWKHTEVFCSIPSRSLLSPSYYHSFGVTENYVIFLEQPFRLDILKMATAYIRRMSWASCLAFHREEKTYIHIIDQRTRQPVQTKFYTDAMVVFHHVNAYEEDGCIVFDVIAYEDNSLYQLFYLANLNQDFKENSRLTSVPTLRRFAVPLHVDKNAEVGTNLIKVASTTATALKEEDGQVYCQPEFLYEGLELPRVNYAHNGKQYRYVFATGVQWSPIPTKIIKYDILTKSSLKWREDDCWPAEPLFVPAPGAKDEDDGVILSAIVSTDPQKLPFLLILDAKSFTELARASVDVDMHMDLHGLFITDMDWDTKKQAASEEQRDRASDCHGAPLT,,-1.0,MDIIFGRNRKEQLEPVRAKVTGKIPAWLQGTLLRNGPGMHTVGESRYNHWFDGLALLHSFTIRDGEVYYRSKYLRSDTYNTNIEANRIVVSEFGTMAYPDPCKNIFSKAFSYLSHTIPDFTDNCLINIMKCGEDFYATSETNYIRKINPQTLETLEKVDYRKYVAVNLAMSHPHYDEAGNVLNMGTSIVEKGKTKYVIFKIPATVPEGKKQGKSPWKHTEVFCSIPSRSLLSPSYYHSFGVTENYVIFLEQPFRLDILKMATAYIRRMSWASCLAFHREEKTYIHIIDQRTRQPVQTKFYTDAMVVFHHVNAYEEDGCIVFDVIAYEDNSLYQLFYLANLNQDFKENSRLTSVPTLRRFAVPLHVDKNAEVGTNLIKVASTTATALKEEDGQVYCQPEFLYEGLELPRVNYAHNGKQYRYVFATGVQWSPIPTKIIKYDILTKSSLKWREDDCWPAEPLFVPAPGAKDEDDGVILSAIVSTDPQKLPFLLILDAKSFTELARASVDVDMHMDLHGLFITDMDWDTKKQAASEEQRDRASDCHGAPLT,"Beta,beta-carotene 15,15'-dioxygenase",Symmetrically cleaves beta-carotene into two molecules of retinal using a dioxygenase mechanism.,"Increased beta-carotene 15,15'-monooxygenase activity; 90% increase compared to wild-type; increased catalytic efficiency; no effect on affinity for all-trans-beta-carotene. The replacement of a highly conserved threonine with methionine results in a 90% increase in enzyme activity when analyzed in vitro using purified recombinant enzymes. The Michaelis-Menten constant (K(m)) for the mutated enzyme is normal. Ample amounts of carotenoids are present in plasma of persons consuming a normal Western diet, suggesting that the enzyme is saturated with substrate under normal conditions. Therefore, we propose that haploinsufficiency of the CMO1 enzyme may cause symptoms of hypercarotenemia and hypovitaminosis A in individuals consuming a carotenoid-containing and vitamin A-deficient diet.","Increased beta-carotene 15,15'-monooxygenase activity; 90% increase compared to wild-type; increased catalytic efficiency; no effect on affinity for all-trans-beta-carotene. The replacement of a highly conserved threonine with methionine results in a 90% increase in enzyme activity when analyzed in vitro using purified recombinant enzymes. The Michaelis-Menten constant (K(m)) for the mutated enzyme is normal. Ample amounts of carotenoids are present in plasma of persons consuming a normal Western diet, suggesting that the enzyme is saturated with substrate under normal conditions. Therefore, we propose that haploinsufficiency of the CMO1 enzyme may cause symptoms of hypercarotenemia and hypovitaminosis A in individuals consuming a carotenoid-containing and vitamin A-deficient diet."
403,0,0,Q96MP8-W84R,MVVVTGREPDSRRQDGAMSSSDAEDDFLEPATPTATQAGHALPLLPQEFPEVVPLNIGGAHFTTRLSTLRCYEDTMLAAMFSGRHYIPTDSEGRYFIDRDGTHFGDVLNFLRSGDLPPRERVRAVYKEAQYYAIGPLLEQLENMQPLKGEKVRQAFLGLMPYYKDHLERIVEIARLRAVQRKARFAKLKVCVFKEEMPITPYECPLLNSLRFERSESDGQLFEHHCEVDVSFGPWEAVADVYDLLHCLVTDLSAQGLTVDHQCIGVCDKHLVNHYYCKRPIYEFKITWW,,-1.0,MVVVTGREPDSRRQDGAMSSSDAEDDFLEPATPTATQAGHALPLLPQEFPEVVPLNIGGAHFTTRLSTLRCYEDTMLAAMFSGWHYIPTDSEGRYFIDRDGTHFGDVLNFLRSGDLPPRERVRAVYKEAQYYAIGPLLEQLENMQPLKGEKVRQAFLGLMPYYKDHLERIVEIARLRAVQRKARFAKLKVCVFKEEMPITPYECPLLNSLRFERSESDGQLFEHHCEVDVSFGPWEAVADVYDLLHCLVTDLSAQGLTVDHQCIGVCDKHLVNHYYCKRPIYEFKITWW,BTB/POZ domain-containing protein KCTD7,May be involved in the control of excitability of cortical neurons.,"Decreased likelihood of disease-associated variant found in a patient with opsoclonus-myoclonus ataxia-like syndrome. The mutation affects a non-conserved segment of the predicted protein, changing a neutral amino acid into basic. The different phenotype narrows the spectrum of KCTD7-related diseases.","Decreased likelihood of disease-associated variant found in a patient with opsoclonus-myoclonus ataxia-like syndrome. The mutation affects a non-conserved segment of the predicted protein, changing a neutral amino acid into basic. The different phenotype narrows the spectrum of KCTD7-related diseases."
