sujigwak/NVAR huggingface dataset:
UniProt ID: Q53T94
Variant: R -> H at position 292-292
Variant annotation: in dbSNP:rs16867223
Protein function: Component of RNA polymerase I core factor complex that acts as a GTF2B/TFIIB-like factor and plays a key role in multiple steps during transcription initiation such as pre-initiation complex (PIC) assembly and postpolymerase recruitment events in polymerase I (Pol I) transcription. Binds rDNA promoters and plays a role in Pol I recruitment as a component of the SL1/TIF-IB complex and, possibly, directly through its interaction with RRN3.
Reference sequence:
MDLEEAEEFKERCTQCAAVSWGLTDEGKYYCTSCHNVTERYQEVTNTDLIPNTQIKALNRGLKKKNNTEKGWDWYVCEGFQYILYQQAEALKNLGVGPELKNDVLHNFWKRYLQKSKQAYCKNPVYTTGRKPTVLEDNLSHSDWASEPELLSDVSCPPFLESGAESQSDIHTRKPFPVSKASQSETSVCSGSLDGVEYSQRKEKGIVKMTMPQTLAFCYLSLLWQREAITLSDLLRFVEEDHIPYINAFQHFPEQMKLYGRDRGIFGIESWPDYEDIYKKTVEVGTFLDLPRFPDITEDCYLHPNILCMKYLMEVNLPDEMHSLTCHVVKMTGMGEVDFLTFDPIAKMAKTVKYDVQAVAIIVVVLKLLFLLDDSFEWSLSNLAEKHNEKNKKDKPWFDFRKWYQIMKKAFDEKKQKWEEARAKYLWKSEKPLYYSFVDKPVAYKKREMVVNLQKQFSTLVESTATAGKKSPSSFQFNWTEEDTDRTCFHGHSLQGVLKEKGQSLLTKNSLYWLSTQKFCRCYCTHVTTYEESNYSLSYQFILNLFSFLLRIKTSLLHEEVSLVEKKLFEKKYSVKRKKSRSKKVRRH
UniProt ID: Q53T94
Variant: T -> A at position 351-351
Variant annotation: in dbSNP:rs1054565
Protein function: Component of RNA polymerase I core factor complex that acts as a GTF2B/TFIIB-like factor and plays a key role in multiple steps during transcription initiation such as pre-initiation complex (PIC) assembly and postpolymerase recruitment events in polymerase I (Pol I) transcription. Binds rDNA promoters and plays a role in Pol I recruitment as a component of the SL1/TIF-IB complex and, possibly, directly through its interaction with RRN3.
Reference sequence:
MDLEEAEEFKERCTQCAAVSWGLTDEGKYYCTSCHNVTERYQEVTNTDLIPNTQIKALNRGLKKKNNTEKGWDWYVCEGFQYILYQQAEALKNLGVGPELKNDVLHNFWKRYLQKSKQAYCKNPVYTTGRKPTVLEDNLSHSDWASEPELLSDVSCPPFLESGAESQSDIHTRKPFPVSKASQSETSVCSGSLDGVEYSQRKEKGIVKMTMPQTLAFCYLSLLWQREAITLSDLLRFVEEDHIPYINAFQHFPEQMKLYGRDRGIFGIESWPDYEDIYKKTVEVGTFLDLPRFPDITEDCYLHPNILCMKYLMEVNLPDEMHSLTCHVVKMTGMGEVDFLTFDPIAKMAKTVKYDVQAVAIIVVVLKLLFLLDDSFEWSLSNLAEKHNEKNKKDKPWFDFRKWYQIMKKAFDEKKQKWEEARAKYLWKSEKPLYYSFVDKPVAYKKREMVVNLQKQFSTLVESTATAGKKSPSSFQFNWTEEDTDRTCFHGHSLQGVLKEKGQSLLTKNSLYWLSTQKFCRCYCTHVTTYEESNYSLSYQFILNLFSFLLRIKTSLLHEEVSLVEKKLFEKKYSVKRKKSRSKKVRRH
UniProt ID: Q53T94
Variant: E -> D at position 462-462
Variant annotation: in dbSNP:rs1820965
Protein function: Component of RNA polymerase I core factor complex that acts as a GTF2B/TFIIB-like factor and plays a key role in multiple steps during transcription initiation such as pre-initiation complex (PIC) assembly and postpolymerase recruitment events in polymerase I (Pol I) transcription. Binds rDNA promoters and plays a role in Pol I recruitment as a component of the SL1/TIF-IB complex and, possibly, directly through its interaction with RRN3.
Reference sequence:
MDLEEAEEFKERCTQCAAVSWGLTDEGKYYCTSCHNVTERYQEVTNTDLIPNTQIKALNRGLKKKNNTEKGWDWYVCEGFQYILYQQAEALKNLGVGPELKNDVLHNFWKRYLQKSKQAYCKNPVYTTGRKPTVLEDNLSHSDWASEPELLSDVSCPPFLESGAESQSDIHTRKPFPVSKASQSETSVCSGSLDGVEYSQRKEKGIVKMTMPQTLAFCYLSLLWQREAITLSDLLRFVEEDHIPYINAFQHFPEQMKLYGRDRGIFGIESWPDYEDIYKKTVEVGTFLDLPRFPDITEDCYLHPNILCMKYLMEVNLPDEMHSLTCHVVKMTGMGEVDFLTFDPIAKMAKTVKYDVQAVAIIVVVLKLLFLLDDSFEWSLSNLAEKHNEKNKKDKPWFDFRKWYQIMKKAFDEKKQKWEEARAKYLWKSEKPLYYSFVDKPVAYKKREMVVNLQKQFSTLVESTATAGKKSPSSFQFNWTEEDTDRTCFHGHSLQGVLKEKGQSLLTKNSLYWLSTQKFCRCYCTHVTTYEESNYSLSYQFILNLFSFLLRIKTSLLHEEVSLVEKKLFEKKYSVKRKKSRSKKVRRH
UniProt ID: Q53T94
Variant: T -> M at position 487-487
Variant annotation: in dbSNP:rs16867245
Protein function: Component of RNA polymerase I core factor complex that acts as a GTF2B/TFIIB-like factor and plays a key role in multiple steps during transcription initiation such as pre-initiation complex (PIC) assembly and postpolymerase recruitment events in polymerase I (Pol I) transcription. Binds rDNA promoters and plays a role in Pol I recruitment as a component of the SL1/TIF-IB complex and, possibly, directly through its interaction with RRN3.
Reference sequence:
MDLEEAEEFKERCTQCAAVSWGLTDEGKYYCTSCHNVTERYQEVTNTDLIPNTQIKALNRGLKKKNNTEKGWDWYVCEGFQYILYQQAEALKNLGVGPELKNDVLHNFWKRYLQKSKQAYCKNPVYTTGRKPTVLEDNLSHSDWASEPELLSDVSCPPFLESGAESQSDIHTRKPFPVSKASQSETSVCSGSLDGVEYSQRKEKGIVKMTMPQTLAFCYLSLLWQREAITLSDLLRFVEEDHIPYINAFQHFPEQMKLYGRDRGIFGIESWPDYEDIYKKTVEVGTFLDLPRFPDITEDCYLHPNILCMKYLMEVNLPDEMHSLTCHVVKMTGMGEVDFLTFDPIAKMAKTVKYDVQAVAIIVVVLKLLFLLDDSFEWSLSNLAEKHNEKNKKDKPWFDFRKWYQIMKKAFDEKKQKWEEARAKYLWKSEKPLYYSFVDKPVAYKKREMVVNLQKQFSTLVESTATAGKKSPSSFQFNWTEEDTDRTCFHGHSLQGVLKEKGQSLLTKNSLYWLSTQKFCRCYCTHVTTYEESNYSLSYQFILNLFSFLLRIKTSLLHEEVSLVEKKLFEKKYSVKRKKSRSKKVRRH
UniProt ID: Q54518
Variant: A -> V at position 226-226
Variant annotation: in strain: NCTC 11906
Protein function: Dephosphorylates CpsD. Involved in the regulation of capsular polysaccharide biosynthesis.
Reference sequence:
MIDIHSHIVFDVDDGPKSREESKALLAESYRQGVRTIVSTSHRRKGMFETPEEKIAENFLQVREIAKEVADDLVIAYGAEIYYTLDALEKLEKKEIPTLNDSRYALIEFSMHTSYRQIHTGLSNILMLGITPVIAHIERYDALENNEKRVRELIDMGCYTQINSYHVSKPKFFGEKYKFMKKRARYFLERDLVHVVASDMHNLDSRPPYMQQAYDIIAKKYGAKKAKELFVDNPRKIIMDQLI
UniProt ID: Q54520
Variant: I -> V at position 14-14
Variant annotation: in strain: NCTC 11906 and PO-329
Protein function: Involved in the regulation of capsular polysaccharide biosynthesis. Autophosphorylation of CpsD attenuates its activity and reduces the level of encapsulation. May be part of a complex that directs the coordinated polymerization and export to the cell surface of the capsular polysaccharide.
Reference sequence:
MPTLEIAQKKLEFIKKAEEYYNALCTNIQLSGDKLKVISVTSVNPGEGKTTTSVNIARSFARAGYKTLLIDGDTRNSVMSGFFKSREKITGLTEFLSGTADLSHGLCDTNIENLFVVQSGTVSPNPTALLQSKNFNDMIETLRKYFDYIIVDTAPIGIVIDAAIITQKCDASILVTATGEVNKRDVQKAKQQLEQTGKLFLGVVFNKLDISVDKYGVYGFYGNYGKK
UniProt ID: Q54520
Variant: T -> I at position 74-74
Variant annotation: in strain: NCTC 11906 and PO-329
Protein function: Involved in the regulation of capsular polysaccharide biosynthesis. Autophosphorylation of CpsD attenuates its activity and reduces the level of encapsulation. May be part of a complex that directs the coordinated polymerization and export to the cell surface of the capsular polysaccharide.
Reference sequence:
MPTLEIAQKKLEFIKKAEEYYNALCTNIQLSGDKLKVISVTSVNPGEGKTTTSVNIARSFARAGYKTLLIDGDTRNSVMSGFFKSREKITGLTEFLSGTADLSHGLCDTNIENLFVVQSGTVSPNPTALLQSKNFNDMIETLRKYFDYIIVDTAPIGIVIDAAIITQKCDASILVTATGEVNKRDVQKAKQQLEQTGKLFLGVVFNKLDISVDKYGVYGFYGNYGKK
UniProt ID: Q564N8
Variant: H -> R at position 313-313
Variant annotation: in strain: Isolate Y6
Protein function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
Reference sequence:
MTNIRKTHPLIKIVNHSFIDLPTPSNISAWWNFGSLLGFCLIIQIVTGLFLAMHYTSDTMTAFSSVTHICRDVNYGWLIRYMHANGASMFFICLFLHVGRGLYYGSYTYLETWNIGVILLFAVMATAFMGYVLPRGQMSFWGATVITNLLSAIPYIGTTLVEWIWGGFSVDKATLTRFFAFHFVLPFVIAALAMIHLLFLHETGSNNPSGLVSDSDKIPFHPYFSIKDLLGALILLLAFMNLVLFTPDLLGDPDNYIPANPLNTPPHIKPEWYFLFAYTILRSIPNKLGGVLALVFSILILMLFPILHMSKQHSMMFRPLSQCFFWILVADLFTLTWIGGQPVEYPFITIGQVASILYFTIILIILPSISLLENKLLKW
UniProt ID: Q564N8
Variant: R -> W at position 318-318
Variant annotation: in strain: Isolate Y6
Protein function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
Reference sequence:
MTNIRKTHPLIKIVNHSFIDLPTPSNISAWWNFGSLLGFCLIIQIVTGLFLAMHYTSDTMTAFSSVTHICRDVNYGWLIRYMHANGASMFFICLFLHVGRGLYYGSYTYLETWNIGVILLFAVMATAFMGYVLPRGQMSFWGATVITNLLSAIPYIGTTLVEWIWGGFSVDKATLTRFFAFHFVLPFVIAALAMIHLLFLHETGSNNPSGLVSDSDKIPFHPYFSIKDLLGALILLLAFMNLVLFTPDLLGDPDNYIPANPLNTPPHIKPEWYFLFAYTILRSIPNKLGGVLALVFSILILMLFPILHMSKQHSMMFRPLSQCFFWILVADLFTLTWIGGQPVEYPFITIGQVASILYFTIILIILPSISLLENKLLKW
UniProt ID: Q564P1
Variant: L -> P at position 253-253
Variant annotation: in strain: Isolate SP802 and Isolate SP805
Protein function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
Reference sequence:
MTNIRKTHPLIKIVNSSFIDLPTPSNISAWWNFGSLLGLCLIIQIVTGLFLAMHYTSDTMTAFSSVTHICRDVNYGWLIRYMHANGASMFFICLFLHVGRGLYYGSYTYFETWNIGVILLFAVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTTLVEWIWGGFSVDKATLTRFFAFHFILPFIIAALAMVHLLFLHETGSNNPSGLISDSDKIPFHPYFSIKDILGFLILIMLFMTLVLFTPDLLGDLDNYTPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALVFSILILMLFPILHMAKQRSMMFRPLSQCIFWILVADLFTLTWIGGQPVEYPFIIMGQMASILYFTIILIIFPSISLLENKLLKW
UniProt ID: Q567U6
Variant: R -> C at position 179-179
Variant annotation: in dbSNP:rs33975708
Protein function: (Microbial infection) The CCC complex, in collaboration with the heterotrimeric retriever complex, mediates the exit of human papillomavirus to the cell surface.
Reference sequence:
MGLPRGPEGQGLPEVETREDEEQNVKLTEILELLVAAGYFRARIKGLSPFDKVVGGMTWCITTCNFDVDVDLLFQENSTIGQKIALSEKIVSVLPRMKCPHQLEPHQIQGMDFIHIFPVVQWLVKRAIETKEEMGDYIRSYSVSQFQKTYSLPEDDDFIKRKEKAIKTVVDLSEVYKPRRKYKRHQGAEELLDEESRIHATLLEYGRRYGFSRQSKMEKAEDKKTALPAGLSATEKADAHEEDELRAAEEQRIQSLMTKMTAMANEESRLTASSVGQIVGLCSAEIKQIVSEYAEKQSELSAEESPEKLGTSQLHRRKVISLNKQIAQKTKHLEELRASHTSLQARYNEAKKTLTELKTYSEKLDKEQAALEKIESKADPSILQNLRALVAMNENLKSQEQEFKAHCREEMTRLQQEIENLKAERAPRGDEKTLSSGEPPGTLTSAMTHDEDLDRRYNMEKEKLYKIRLLQARRNREIAILHRKIDEVPSRAELIQYQKRFIELYRQISAVHKETKQFFTLYNTLDDKKVYLEKEISLLNSIHENFSQAMASPAARDQFLRQMEQIVEGIKQSRMKMEKKKQENKMRRDQLNDQYLELLEKQRLYFKTVKEFKEEGRKNEMLLSKVKAKAS
UniProt ID: Q567U6
Variant: R -> C at position 213-213
Variant annotation: in dbSNP:rs34095554
Protein function: (Microbial infection) The CCC complex, in collaboration with the heterotrimeric retriever complex, mediates the exit of human papillomavirus to the cell surface.
Reference sequence:
MGLPRGPEGQGLPEVETREDEEQNVKLTEILELLVAAGYFRARIKGLSPFDKVVGGMTWCITTCNFDVDVDLLFQENSTIGQKIALSEKIVSVLPRMKCPHQLEPHQIQGMDFIHIFPVVQWLVKRAIETKEEMGDYIRSYSVSQFQKTYSLPEDDDFIKRKEKAIKTVVDLSEVYKPRRKYKRHQGAEELLDEESRIHATLLEYGRRYGFSRQSKMEKAEDKKTALPAGLSATEKADAHEEDELRAAEEQRIQSLMTKMTAMANEESRLTASSVGQIVGLCSAEIKQIVSEYAEKQSELSAEESPEKLGTSQLHRRKVISLNKQIAQKTKHLEELRASHTSLQARYNEAKKTLTELKTYSEKLDKEQAALEKIESKADPSILQNLRALVAMNENLKSQEQEFKAHCREEMTRLQQEIENLKAERAPRGDEKTLSSGEPPGTLTSAMTHDEDLDRRYNMEKEKLYKIRLLQARRNREIAILHRKIDEVPSRAELIQYQKRFIELYRQISAVHKETKQFFTLYNTLDDKKVYLEKEISLLNSIHENFSQAMASPAARDQFLRQMEQIVEGIKQSRMKMEKKKQENKMRRDQLNDQYLELLEKQRLYFKTVKEFKEEGRKNEMLLSKVKAKAS
UniProt ID: Q567U6
Variant: P -> L at position 228-228
Variant annotation: in dbSNP:rs17512204
Protein function: (Microbial infection) The CCC complex, in collaboration with the heterotrimeric retriever complex, mediates the exit of human papillomavirus to the cell surface.
Reference sequence:
MGLPRGPEGQGLPEVETREDEEQNVKLTEILELLVAAGYFRARIKGLSPFDKVVGGMTWCITTCNFDVDVDLLFQENSTIGQKIALSEKIVSVLPRMKCPHQLEPHQIQGMDFIHIFPVVQWLVKRAIETKEEMGDYIRSYSVSQFQKTYSLPEDDDFIKRKEKAIKTVVDLSEVYKPRRKYKRHQGAEELLDEESRIHATLLEYGRRYGFSRQSKMEKAEDKKTALPAGLSATEKADAHEEDELRAAEEQRIQSLMTKMTAMANEESRLTASSVGQIVGLCSAEIKQIVSEYAEKQSELSAEESPEKLGTSQLHRRKVISLNKQIAQKTKHLEELRASHTSLQARYNEAKKTLTELKTYSEKLDKEQAALEKIESKADPSILQNLRALVAMNENLKSQEQEFKAHCREEMTRLQQEIENLKAERAPRGDEKTLSSGEPPGTLTSAMTHDEDLDRRYNMEKEKLYKIRLLQARRNREIAILHRKIDEVPSRAELIQYQKRFIELYRQISAVHKETKQFFTLYNTLDDKKVYLEKEISLLNSIHENFSQAMASPAARDQFLRQMEQIVEGIKQSRMKMEKKKQENKMRRDQLNDQYLELLEKQRLYFKTVKEFKEEGRKNEMLLSKVKAKAS
UniProt ID: Q567U6
Variant: H -> R at position 315-315
Variant annotation: in a colorectal cancer sample; somatic mutation; dbSNP:rs1679285734
Protein function: (Microbial infection) The CCC complex, in collaboration with the heterotrimeric retriever complex, mediates the exit of human papillomavirus to the cell surface.
Reference sequence:
MGLPRGPEGQGLPEVETREDEEQNVKLTEILELLVAAGYFRARIKGLSPFDKVVGGMTWCITTCNFDVDVDLLFQENSTIGQKIALSEKIVSVLPRMKCPHQLEPHQIQGMDFIHIFPVVQWLVKRAIETKEEMGDYIRSYSVSQFQKTYSLPEDDDFIKRKEKAIKTVVDLSEVYKPRRKYKRHQGAEELLDEESRIHATLLEYGRRYGFSRQSKMEKAEDKKTALPAGLSATEKADAHEEDELRAAEEQRIQSLMTKMTAMANEESRLTASSVGQIVGLCSAEIKQIVSEYAEKQSELSAEESPEKLGTSQLHRRKVISLNKQIAQKTKHLEELRASHTSLQARYNEAKKTLTELKTYSEKLDKEQAALEKIESKADPSILQNLRALVAMNENLKSQEQEFKAHCREEMTRLQQEIENLKAERAPRGDEKTLSSGEPPGTLTSAMTHDEDLDRRYNMEKEKLYKIRLLQARRNREIAILHRKIDEVPSRAELIQYQKRFIELYRQISAVHKETKQFFTLYNTLDDKKVYLEKEISLLNSIHENFSQAMASPAARDQFLRQMEQIVEGIKQSRMKMEKKKQENKMRRDQLNDQYLELLEKQRLYFKTVKEFKEEGRKNEMLLSKVKAKAS
UniProt ID: Q567U6
Variant: Y -> H at position 465-465
Variant annotation: in dbSNP:rs17047557
Protein function: (Microbial infection) The CCC complex, in collaboration with the heterotrimeric retriever complex, mediates the exit of human papillomavirus to the cell surface.
Reference sequence:
MGLPRGPEGQGLPEVETREDEEQNVKLTEILELLVAAGYFRARIKGLSPFDKVVGGMTWCITTCNFDVDVDLLFQENSTIGQKIALSEKIVSVLPRMKCPHQLEPHQIQGMDFIHIFPVVQWLVKRAIETKEEMGDYIRSYSVSQFQKTYSLPEDDDFIKRKEKAIKTVVDLSEVYKPRRKYKRHQGAEELLDEESRIHATLLEYGRRYGFSRQSKMEKAEDKKTALPAGLSATEKADAHEEDELRAAEEQRIQSLMTKMTAMANEESRLTASSVGQIVGLCSAEIKQIVSEYAEKQSELSAEESPEKLGTSQLHRRKVISLNKQIAQKTKHLEELRASHTSLQARYNEAKKTLTELKTYSEKLDKEQAALEKIESKADPSILQNLRALVAMNENLKSQEQEFKAHCREEMTRLQQEIENLKAERAPRGDEKTLSSGEPPGTLTSAMTHDEDLDRRYNMEKEKLYKIRLLQARRNREIAILHRKIDEVPSRAELIQYQKRFIELYRQISAVHKETKQFFTLYNTLDDKKVYLEKEISLLNSIHENFSQAMASPAARDQFLRQMEQIVEGIKQSRMKMEKKKQENKMRRDQLNDQYLELLEKQRLYFKTVKEFKEEGRKNEMLLSKVKAKAS
UniProt ID: Q567V2
Variant: M -> V at position 72-72
Variant annotation: in dbSNP:rs874628
Protein function: Required for the assembly and stability of the mitochondrial ribosome . Is a positive regulator of mitochondrial protein synthesis .
Reference sequence:
MARGGWRRLRRLLSAGQLLFQGRALLVTNTLGCGALMAAGDGVRQSWEIRARPGQVFDPRRSASMFAVGCSMGPFLHYWYLSLDRLFPASGLRGFPNVLKKVLVDQLVASPLLGVWYFLGLGCLEGQTVGESCQELREKFWEFYKADWCVWPAAQFVNFLFVPPQFRVTYINGLTLGWDTYLSYLKYRSPVPLTPPGCVALDTRAD
UniProt ID: Q569H4
Variant: P -> T at position 110-110
Variant annotation: in dbSNP:rs17853861
Protein function: Regulator of cell size that promotes cell size increase independently of mTOR and Hippo signaling pathways. Acts by stimulating the translation of specific mRNAs, including those encoding proteins affecting mitochondrial functions. Increases mitochondrial mass and respiration.
Reference sequence:
MSAKSKGNPSSSCPAEGPPAASKTKVKEQIKIIVEDLELVLGDLKDVAKELKEVVDQIDTLTSDLQLEDEMTDSSKTDTLNSSSSGTTASSLEKIKVQANAPLIKPPAHPSAILTVLRKPNPPPPPPRLTPVKCEDPKRVVPTANPVKTNGTLLRNGGLPGGPNKIPNGDICCIPNSNLDKAPVQLLMHRPEKDRCPQAGPRERVRFNEKVQYHGYCPDCDTRYNIKNREVHLHSEPVHPPGKIPHQGPPLPPTPHLPPFPLENGGMGISHSNSFPPIRPATVPPPTAPKPQKTILRKSTTTTV
UniProt ID: Q569K4
Variant: S -> G at position 242-242
Variant annotation: in dbSNP:rs2271761
Protein function: May play a role in p53/TP53-mediated apoptosis.
Reference sequence:
MNMANFLRGFEEKGIKNDRPEDQLSKEKKKILFSFCEVCNIQLNSAAQAQVHSNGKSHRKRVKQLSDGQPPPPAQASPSSNSSTGSTCHTTTLPALVRTPTLMMQPSLDIKPFMSFPVDSSSAVGLFPNFNTMDPVQKAVINHTFGVSIPPKKKQVISCNVCQLRFNSDSQAEAHYKGSKHAKKVKALDATKNKPKMVPSKDSAKANPSCSITPITGNNSDKSEDKGKLKASSSSQPSSSESGSFLLKSGTTPLPPGAATSPSKSTNGAPGTVVESEEEKAKKLLYCSLCKVAVNSLSQLEAHNTGSKHKTMVEARNGAGPIKSYPRPGSRLKMQNGSKGSGLQNKTFHCEICDVHVNSEIQLKQHISSRRHKDRVAGKPLKPKYSPYNKLQRSPSILAAKLAFQKDMMKPLAPAFLSSPLAAAAAVSSALSLPPRPSASLFQAPAIPPALLRPGHGPIRATPASILFAPY
UniProt ID: Q569K4
Variant: F -> Y at position 416-416
Protein function: May play a role in p53/TP53-mediated apoptosis.
Reference sequence:
MNMANFLRGFEEKGIKNDRPEDQLSKEKKKILFSFCEVCNIQLNSAAQAQVHSNGKSHRKRVKQLSDGQPPPPAQASPSSNSSTGSTCHTTTLPALVRTPTLMMQPSLDIKPFMSFPVDSSSAVGLFPNFNTMDPVQKAVINHTFGVSIPPKKKQVISCNVCQLRFNSDSQAEAHYKGSKHAKKVKALDATKNKPKMVPSKDSAKANPSCSITPITGNNSDKSEDKGKLKASSSSQPSSSESGSFLLKSGTTPLPPGAATSPSKSTNGAPGTVVESEEEKAKKLLYCSLCKVAVNSLSQLEAHNTGSKHKTMVEARNGAGPIKSYPRPGSRLKMQNGSKGSGLQNKTFHCEICDVHVNSEIQLKQHISSRRHKDRVAGKPLKPKYSPYNKLQRSPSILAAKLAFQKDMMKPLAPAFLSSPLAAAAAVSSALSLPPRPSASLFQAPAIPPALLRPGHGPIRATPASILFAPY
UniProt ID: Q56EB1
Variant: S -> P at position 31-31
Protein function: This potent antithrombotic agent acts in a calcium-independent manner. Exerts its anticoagulant effect by two distinct mechanisms. It binds to activated thrombin through exosite 1, blocking fibrinogen clotting, platelet activation, factor V activation and other effects, and it interacts with prothrombin (F2), decreasing its proteolytic activation -especially in the presence of factor Va. In vivo, intravenous injection before thrombosis induction causes a significant decrease in thrombus weight. Furthermore, BJC shows a prolonged effect by remaining in the plasma bound to prothrombin for at least 12 hours.
Reference sequence:
MGRFLFVSFGLLVVFLSLSGTAADCPSDWSSHEGHCYKFFQQKMNWADAERFCSEQAKGGHLVSFQSDGETDFVVNLVTEKIQSTDLYAWIGLRVQNKEKQCSSKWSDGSSVSYENVVGRTVKKCFALEKEQEFFVWINIYCGQQNPFVCKSPPP
UniProt ID: Q56EB1
Variant: G -> Q at position 34-34
Protein function: This potent antithrombotic agent acts in a calcium-independent manner. Exerts its anticoagulant effect by two distinct mechanisms. It binds to activated thrombin through exosite 1, blocking fibrinogen clotting, platelet activation, factor V activation and other effects, and it interacts with prothrombin (F2), decreasing its proteolytic activation -especially in the presence of factor Va. In vivo, intravenous injection before thrombosis induction causes a significant decrease in thrombus weight. Furthermore, BJC shows a prolonged effect by remaining in the plasma bound to prothrombin for at least 12 hours.
Reference sequence:
MGRFLFVSFGLLVVFLSLSGTAADCPSDWSSHEGHCYKFFQQKMNWADAERFCSEQAKGGHLVSFQSDGETDFVVNLVTEKIQSTDLYAWIGLRVQNKEKQCSSKWSDGSSVSYENVVGRTVKKCFALEKEQEFFVWINIYCGQQNPFVCKSPPP
UniProt ID: Q56EB1
Variant: H -> Q at position 35-35
Protein function: This potent antithrombotic agent acts in a calcium-independent manner. Exerts its anticoagulant effect by two distinct mechanisms. It binds to activated thrombin through exosite 1, blocking fibrinogen clotting, platelet activation, factor V activation and other effects, and it interacts with prothrombin (F2), decreasing its proteolytic activation -especially in the presence of factor Va. In vivo, intravenous injection before thrombosis induction causes a significant decrease in thrombus weight. Furthermore, BJC shows a prolonged effect by remaining in the plasma bound to prothrombin for at least 12 hours.
Reference sequence:
MGRFLFVSFGLLVVFLSLSGTAADCPSDWSSHEGHCYKFFQQKMNWADAERFCSEQAKGGHLVSFQSDGETDFVVNLVTEKIQSTDLYAWIGLRVQNKEKQCSSKWSDGSSVSYENVVGRTVKKCFALEKEQEFFVWINIYCGQQNPFVCKSPPP
UniProt ID: Q56EB1
Variant: F -> V at position 40-40
Protein function: This potent antithrombotic agent acts in a calcium-independent manner. Exerts its anticoagulant effect by two distinct mechanisms. It binds to activated thrombin through exosite 1, blocking fibrinogen clotting, platelet activation, factor V activation and other effects, and it interacts with prothrombin (F2), decreasing its proteolytic activation -especially in the presence of factor Va. In vivo, intravenous injection before thrombosis induction causes a significant decrease in thrombus weight. Furthermore, BJC shows a prolonged effect by remaining in the plasma bound to prothrombin for at least 12 hours.
Reference sequence:
MGRFLFVSFGLLVVFLSLSGTAADCPSDWSSHEGHCYKFFQQKMNWADAERFCSEQAKGGHLVSFQSDGETDFVVNLVTEKIQSTDLYAWIGLRVQNKEKQCSSKWSDGSSVSYENVVGRTVKKCFALEKEQEFFVWINIYCGQQNPFVCKSPPP
UniProt ID: Q56EB1
Variant: K -> E at position 43-43
Protein function: This potent antithrombotic agent acts in a calcium-independent manner. Exerts its anticoagulant effect by two distinct mechanisms. It binds to activated thrombin through exosite 1, blocking fibrinogen clotting, platelet activation, factor V activation and other effects, and it interacts with prothrombin (F2), decreasing its proteolytic activation -especially in the presence of factor Va. In vivo, intravenous injection before thrombosis induction causes a significant decrease in thrombus weight. Furthermore, BJC shows a prolonged effect by remaining in the plasma bound to prothrombin for at least 12 hours.
Reference sequence:
MGRFLFVSFGLLVVFLSLSGTAADCPSDWSSHEGHCYKFFQQKMNWADAERFCSEQAKGGHLVSFQSDGETDFVVNLVTEKIQSTDLYAWIGLRVQNKEKQCSSKWSDGSSVSYENVVGRTVKKCFALEKEQEFFVWINIYCGQQNPFVCKSPPP
UniProt ID: Q56EB1
Variant: K -> Q at position 43-43
Protein function: This potent antithrombotic agent acts in a calcium-independent manner. Exerts its anticoagulant effect by two distinct mechanisms. It binds to activated thrombin through exosite 1, blocking fibrinogen clotting, platelet activation, factor V activation and other effects, and it interacts with prothrombin (F2), decreasing its proteolytic activation -especially in the presence of factor Va. In vivo, intravenous injection before thrombosis induction causes a significant decrease in thrombus weight. Furthermore, BJC shows a prolonged effect by remaining in the plasma bound to prothrombin for at least 12 hours.
Reference sequence:
MGRFLFVSFGLLVVFLSLSGTAADCPSDWSSHEGHCYKFFQQKMNWADAERFCSEQAKGGHLVSFQSDGETDFVVNLVTEKIQSTDLYAWIGLRVQNKEKQCSSKWSDGSSVSYENVVGRTVKKCFALEKEQEFFVWINIYCGQQNPFVCKSPPP
UniProt ID: Q56EB1
Variant: W -> H at position 46-46
Protein function: This potent antithrombotic agent acts in a calcium-independent manner. Exerts its anticoagulant effect by two distinct mechanisms. It binds to activated thrombin through exosite 1, blocking fibrinogen clotting, platelet activation, factor V activation and other effects, and it interacts with prothrombin (F2), decreasing its proteolytic activation -especially in the presence of factor Va. In vivo, intravenous injection before thrombosis induction causes a significant decrease in thrombus weight. Furthermore, BJC shows a prolonged effect by remaining in the plasma bound to prothrombin for at least 12 hours.
Reference sequence:
MGRFLFVSFGLLVVFLSLSGTAADCPSDWSSHEGHCYKFFQQKMNWADAERFCSEQAKGGHLVSFQSDGETDFVVNLVTEKIQSTDLYAWIGLRVQNKEKQCSSKWSDGSSVSYENVVGRTVKKCFALEKEQEFFVWINIYCGQQNPFVCKSPPP
UniProt ID: Q56EB1
Variant: W -> N at position 46-46
Protein function: This potent antithrombotic agent acts in a calcium-independent manner. Exerts its anticoagulant effect by two distinct mechanisms. It binds to activated thrombin through exosite 1, blocking fibrinogen clotting, platelet activation, factor V activation and other effects, and it interacts with prothrombin (F2), decreasing its proteolytic activation -especially in the presence of factor Va. In vivo, intravenous injection before thrombosis induction causes a significant decrease in thrombus weight. Furthermore, BJC shows a prolonged effect by remaining in the plasma bound to prothrombin for at least 12 hours.
Reference sequence:
MGRFLFVSFGLLVVFLSLSGTAADCPSDWSSHEGHCYKFFQQKMNWADAERFCSEQAKGGHLVSFQSDGETDFVVNLVTEKIQSTDLYAWIGLRVQNKEKQCSSKWSDGSSVSYENVVGRTVKKCFALEKEQEFFVWINIYCGQQNPFVCKSPPP
UniProt ID: Q56EB1
Variant: R -> Y at position 51-51
Protein function: This potent antithrombotic agent acts in a calcium-independent manner. Exerts its anticoagulant effect by two distinct mechanisms. It binds to activated thrombin through exosite 1, blocking fibrinogen clotting, platelet activation, factor V activation and other effects, and it interacts with prothrombin (F2), decreasing its proteolytic activation -especially in the presence of factor Va. In vivo, intravenous injection before thrombosis induction causes a significant decrease in thrombus weight. Furthermore, BJC shows a prolonged effect by remaining in the plasma bound to prothrombin for at least 12 hours.
Reference sequence:
MGRFLFVSFGLLVVFLSLSGTAADCPSDWSSHEGHCYKFFQQKMNWADAERFCSEQAKGGHLVSFQSDGETDFVVNLVTEKIQSTDLYAWIGLRVQNKEKQCSSKWSDGSSVSYENVVGRTVKKCFALEKEQEFFVWINIYCGQQNPFVCKSPPP
UniProt ID: Q56P42
Variant: Q -> R at position 81-81
Variant annotation: in dbSNP:rs293833
Protein function: May play a role in innate immunity by disrupting the interaction between PYCARD and NLRP3, thereby regulating the NLRP3 inflammasome . May also inhibit NF-kappa-B signaling distally by affecting the nuclear accumulation of RELA .
Reference sequence:
MASSAELDFNLQALLEQLSQDELSKFKSLIRTISLGKELQTVPQTEVDKANGKQLVEIFTSHSCSYWAGMAAIQVFEKMNQTHLSGRADEHCVMPPP