sujigwak/NVAR huggingface dataset:
UniProt ID: P38057
Variant: K -> G at position 124-124
Protein function: Inhibits trypsin with a Ki of 7 x 10(-6) M.
Reference sequence:
PAGPFRLPRCRKEFQQAQHLRACQQWLHKQARQSGSGPSPQGPQQRPPLLQQCCNELHQEEPLCVCPTLKGAAKAVKQQIQQQGQQHGQQGQQLQHEIRRIYQTATHLPKVCNIPQVQVCPFNKTMPGPS
UniProt ID: P38057
Variant: M -> V at position 126-126
Protein function: Inhibits trypsin with a Ki of 7 x 10(-6) M.
Reference sequence:
PAGPFRLPRCRKEFQQAQHLRACQQWLHKQARQSGSGPSPQGPQQRPPLLQQCCNELHQEEPLCVCPTLKGAAKAVKQQIQQQGQQHGQQGQQLQHEIRRIYQTATHLPKVCNIPQVQVCPFNKTMPGPS
UniProt ID: P38077
Variant: S -> I at position 207-207
Variant annotation: in strain: D273-10B/A1
Protein function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha(3)beta(3). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
Reference sequence:
MLSRIVSNNATRSVMCHQAQVGILYKTNPVRTYATLKEVEMRLKSIKNIEKITKTMKIVASTRLSKAEKAKISAKKMDEAEQLFYKNAETKNLDVEATETGAPKELIVAITSDKGLCGSIHSQLAKAVRRHLNDQPNADIVTIGDKIKMQLLRTHPNNIKLSINGIGKDAPTFQESALIADKLLSVMKAGTYPKISIFYNDPVSSLSFEPSEKPIFNAKTIEQSPSFGKFEIDTDANVPRDLFEYTLANQMLTAMAQGYAAEISARRNAMDNASKNAGDMINRYSILYNRTRQAVITNELVDIITGASSLG
UniProt ID: P38077
Variant: S -> F at position 308-308
Variant annotation: in allele ATP3a
Protein function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha(3)beta(3). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
Reference sequence:
MLSRIVSNNATRSVMCHQAQVGILYKTNPVRTYATLKEVEMRLKSIKNIEKITKTMKIVASTRLSKAEKAKISAKKMDEAEQLFYKNAETKNLDVEATETGAPKELIVAITSDKGLCGSIHSQLAKAVRRHLNDQPNADIVTIGDKIKMQLLRTHPNNIKLSINGIGKDAPTFQESALIADKLLSVMKAGTYPKISIFYNDPVSSLSFEPSEKPIFNAKTIEQSPSFGKFEIDTDANVPRDLFEYTLANQMLTAMAQGYAAEISARRNAMDNASKNAGDMINRYSILYNRTRQAVITNELVDIITGASSLG
UniProt ID: P38117
Variant: D -> N at position 128-128
Variant annotation: in GA2B; decreased protein stability; dbSNP:rs104894678
Protein function: Heterodimeric electron transfer flavoprotein that accepts electrons from several mitochondrial dehydrogenases, including acyl-CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase . It transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (Probable). Required for normal mitochondrial fatty acid oxidation and normal amino acid metabolism . ETFB binds an AMP molecule that probably has a purely structural role .
Reference sequence:
MAELRVLVAVKRVIDYAVKIRVKPDRTGVVTDGVKHSMNPFCEIAVEEAVRLKEKKLVKEVIAVSCGPAQCQETIRTALAMGADRGIHVEVPPAEAERLGPLQVARVLAKLAEKEKVDLVLLGKQAIDDDCNQTGQMTAGFLDWPQGTFASQVTLEGDKLKVEREIDGGLETLRLKLPAVVTADLRLNEPRYATLPNIMKAKKKKIEVIKPGDLGVDLTSKLSVISVEDPPQRTAGVKVETTEDLVAKLKEIGRI
UniProt ID: P38117
Variant: T -> M at position 154-154
Variant annotation: in dbSNP:rs1130426
Protein function: Heterodimeric electron transfer flavoprotein that accepts electrons from several mitochondrial dehydrogenases, including acyl-CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase . It transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (Probable). Required for normal mitochondrial fatty acid oxidation and normal amino acid metabolism . ETFB binds an AMP molecule that probably has a purely structural role .
Reference sequence:
MAELRVLVAVKRVIDYAVKIRVKPDRTGVVTDGVKHSMNPFCEIAVEEAVRLKEKKLVKEVIAVSCGPAQCQETIRTALAMGADRGIHVEVPPAEAERLGPLQVARVLAKLAEKEKVDLVLLGKQAIDDDCNQTGQMTAGFLDWPQGTFASQVTLEGDKLKVEREIDGGLETLRLKLPAVVTADLRLNEPRYATLPNIMKAKKKKIEVIKPGDLGVDLTSKLSVISVEDPPQRTAGVKVETTEDLVAKLKEIGRI
UniProt ID: P38117
Variant: R -> Q at position 164-164
Variant annotation: in GA2B; reduced electron transfer activity; dbSNP:rs104894677
Protein function: Heterodimeric electron transfer flavoprotein that accepts electrons from several mitochondrial dehydrogenases, including acyl-CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase . It transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (Probable). Required for normal mitochondrial fatty acid oxidation and normal amino acid metabolism . ETFB binds an AMP molecule that probably has a purely structural role .
Reference sequence:
MAELRVLVAVKRVIDYAVKIRVKPDRTGVVTDGVKHSMNPFCEIAVEEAVRLKEKKLVKEVIAVSCGPAQCQETIRTALAMGADRGIHVEVPPAEAERLGPLQVARVLAKLAEKEKVDLVLLGKQAIDDDCNQTGQMTAGFLDWPQGTFASQVTLEGDKLKVEREIDGGLETLRLKLPAVVTADLRLNEPRYATLPNIMKAKKKKIEVIKPGDLGVDLTSKLSVISVEDPPQRTAGVKVETTEDLVAKLKEIGRI
UniProt ID: P38224
Variant: L -> V at position 153-153
Variant annotation: in strain: CLIB 413 haplotype Ha1
Protein function: Required for efficient mating.
Reference sequence:
MVAISMIWFFTKRMPRIFALAFNLISIFLLIFLLIGCYNPSNQSTFLVKYKFDDNSPFYTIIEKSYEKSNTTLGLEEVIIRSGYMGVCIDNIPSQYSSYNNMTTFSNSICYARKNLSSVPLYRDLEIQLSNIASSSSKTQSSVVLNILKLAQLTSVNVIHPYVLMATVILTILMFLFILYVTVPKLPFKLAVNKFLLLLSSTIVLTWGIGAMWTHVGINASYRLVPSSSMNIITVKKGKKAAVMAWFSFAFLLLDSVVLWLIFLRDRKSLKDEIDNVPCAQNRYNNYSSDSSTLHSKV
UniProt ID: P38224
Variant: I -> L at position 203-203
Variant annotation: in strain: CLIB 630
Protein function: Required for efficient mating.
Reference sequence:
MVAISMIWFFTKRMPRIFALAFNLISIFLLIFLLIGCYNPSNQSTFLVKYKFDDNSPFYTIIEKSYEKSNTTLGLEEVIIRSGYMGVCIDNIPSQYSSYNNMTTFSNSICYARKNLSSVPLYRDLEIQLSNIASSSSKTQSSVVLNILKLAQLTSVNVIHPYVLMATVILTILMFLFILYVTVPKLPFKLAVNKFLLLLSSTIVLTWGIGAMWTHVGINASYRLVPSSSMNIITVKKGKKAAVMAWFSFAFLLLDSVVLWLIFLRDRKSLKDEIDNVPCAQNRYNNYSSDSSTLHSKV
UniProt ID: P38224
Variant: V -> I at position 204-204
Variant annotation: in strain: K1
Protein function: Required for efficient mating.
Reference sequence:
MVAISMIWFFTKRMPRIFALAFNLISIFLLIFLLIGCYNPSNQSTFLVKYKFDDNSPFYTIIEKSYEKSNTTLGLEEVIIRSGYMGVCIDNIPSQYSSYNNMTTFSNSICYARKNLSSVPLYRDLEIQLSNIASSSSKTQSSVVLNILKLAQLTSVNVIHPYVLMATVILTILMFLFILYVTVPKLPFKLAVNKFLLLLSSTIVLTWGIGAMWTHVGINASYRLVPSSSMNIITVKKGKKAAVMAWFSFAFLLLDSVVLWLIFLRDRKSLKDEIDNVPCAQNRYNNYSSDSSTLHSKV
UniProt ID: P38224
Variant: A -> E at position 220-220
Variant annotation: in strain: CLIB 413 haplotype Ha2
Protein function: Required for efficient mating.
Reference sequence:
MVAISMIWFFTKRMPRIFALAFNLISIFLLIFLLIGCYNPSNQSTFLVKYKFDDNSPFYTIIEKSYEKSNTTLGLEEVIIRSGYMGVCIDNIPSQYSSYNNMTTFSNSICYARKNLSSVPLYRDLEIQLSNIASSSSKTQSSVVLNILKLAQLTSVNVIHPYVLMATVILTILMFLFILYVTVPKLPFKLAVNKFLLLLSSTIVLTWGIGAMWTHVGINASYRLVPSSSMNIITVKKGKKAAVMAWFSFAFLLLDSVVLWLIFLRDRKSLKDEIDNVPCAQNRYNNYSSDSSTLHSKV
UniProt ID: P38224
Variant: R -> I at position 223-223
Variant annotation: in strain: CLIB 630
Protein function: Required for efficient mating.
Reference sequence:
MVAISMIWFFTKRMPRIFALAFNLISIFLLIFLLIGCYNPSNQSTFLVKYKFDDNSPFYTIIEKSYEKSNTTLGLEEVIIRSGYMGVCIDNIPSQYSSYNNMTTFSNSICYARKNLSSVPLYRDLEIQLSNIASSSSKTQSSVVLNILKLAQLTSVNVIHPYVLMATVILTILMFLFILYVTVPKLPFKLAVNKFLLLLSSTIVLTWGIGAMWTHVGINASYRLVPSSSMNIITVKKGKKAAVMAWFSFAFLLLDSVVLWLIFLRDRKSLKDEIDNVPCAQNRYNNYSSDSSTLHSKV
UniProt ID: P38224
Variant: K -> N at position 236-236
Variant annotation: in strain: CLIB 219
Protein function: Required for efficient mating.
Reference sequence:
MVAISMIWFFTKRMPRIFALAFNLISIFLLIFLLIGCYNPSNQSTFLVKYKFDDNSPFYTIIEKSYEKSNTTLGLEEVIIRSGYMGVCIDNIPSQYSSYNNMTTFSNSICYARKNLSSVPLYRDLEIQLSNIASSSSKTQSSVVLNILKLAQLTSVNVIHPYVLMATVILTILMFLFILYVTVPKLPFKLAVNKFLLLLSSTIVLTWGIGAMWTHVGINASYRLVPSSSMNIITVKKGKKAAVMAWFSFAFLLLDSVVLWLIFLRDRKSLKDEIDNVPCAQNRYNNYSSDSSTLHSKV
UniProt ID: P38224
Variant: A -> T at position 241-241
Variant annotation: in strain: CLIB 388 haplotype Ha2
Protein function: Required for efficient mating.
Reference sequence:
MVAISMIWFFTKRMPRIFALAFNLISIFLLIFLLIGCYNPSNQSTFLVKYKFDDNSPFYTIIEKSYEKSNTTLGLEEVIIRSGYMGVCIDNIPSQYSSYNNMTTFSNSICYARKNLSSVPLYRDLEIQLSNIASSSSKTQSSVVLNILKLAQLTSVNVIHPYVLMATVILTILMFLFILYVTVPKLPFKLAVNKFLLLLSSTIVLTWGIGAMWTHVGINASYRLVPSSSMNIITVKKGKKAAVMAWFSFAFLLLDSVVLWLIFLRDRKSLKDEIDNVPCAQNRYNNYSSDSSTLHSKV
UniProt ID: P38315
Variant: I -> L at position 7-7
Variant annotation: in strain: W303-1a
Protein function: Involved in oxidative stress response and redox homeostasis. Required for hydrogen peroxide-induced oxidation and nuclear localization (activation) of YAP1. Functions probably in concert with HYP1/GPX3, the actual YAP1 modifying enzyme. YBP1 is not required for HYP1/GPX3-independent, diamide-induced oxidation of YAP1.
Reference sequence:
MEPIDDILFEVTDAFKTQKEDLLELVTLIDIYGEQVNQEGSYEEKTRFIETLNTLLEDNPSTTGEIGWDLPKGLLKFLSKDNVDVNGRLGTNMIVQGVMKCFYAISIQGEPKKCLITGLELLSSLCSKDFSKSDQQNKEDFVDKKANTLPPEGVIENSSNRKDFPSYGESKSSNEFFLKLKSYILFEFIGASLKRISTLFPSKYLGAAVSTIEKFVYSHADTFEDALFLLRRVYTFCRNYIPPDPPKDIQLNEDFTREMFDKVVEEESELQVRLLRRLCTFGISTPIKTVTTNADVKYYCALNQQKFELSAYYTEYLELFCRYYQMAFSLDVDIEGEFQNVIKECRIIYKSVPQEISAVNDEAKLVLERMVYKLAYTFEVQKAAKEKNVGLDYNGVILFSGIHYLETNQHLVKEMNITDAIYLYLRFTTPSLYSKVYYNVAVESVSRYWLWYAITTEPLEDVKKELKNLSVFVTKTLLHVLLQKNCIQVNQQLRMITFTLLTRLLCLIPEKVAFEFILDVLKTSPLPLAKTSVLCVFKDLSRRRISTKDNDSETDLIVEKLSKLKVNDSNKAQQSNIRHYIQLDSSKMKAVHDCCLQTIQDSFTADAKKSDILLLLTYLNIFIVLKKTWDEDLLKIVCSKIDSNLKSVEPDKLPKYKEIVDKNESLNDYFTGIK
UniProt ID: P38315
Variant: F -> V at position 328-328
Variant annotation: in strain: W303-1a
Protein function: Involved in oxidative stress response and redox homeostasis. Required for hydrogen peroxide-induced oxidation and nuclear localization (activation) of YAP1. Functions probably in concert with HYP1/GPX3, the actual YAP1 modifying enzyme. YBP1 is not required for HYP1/GPX3-independent, diamide-induced oxidation of YAP1.
Reference sequence:
MEPIDDILFEVTDAFKTQKEDLLELVTLIDIYGEQVNQEGSYEEKTRFIETLNTLLEDNPSTTGEIGWDLPKGLLKFLSKDNVDVNGRLGTNMIVQGVMKCFYAISIQGEPKKCLITGLELLSSLCSKDFSKSDQQNKEDFVDKKANTLPPEGVIENSSNRKDFPSYGESKSSNEFFLKLKSYILFEFIGASLKRISTLFPSKYLGAAVSTIEKFVYSHADTFEDALFLLRRVYTFCRNYIPPDPPKDIQLNEDFTREMFDKVVEEESELQVRLLRRLCTFGISTPIKTVTTNADVKYYCALNQQKFELSAYYTEYLELFCRYYQMAFSLDVDIEGEFQNVIKECRIIYKSVPQEISAVNDEAKLVLERMVYKLAYTFEVQKAAKEKNVGLDYNGVILFSGIHYLETNQHLVKEMNITDAIYLYLRFTTPSLYSKVYYNVAVESVSRYWLWYAITTEPLEDVKKELKNLSVFVTKTLLHVLLQKNCIQVNQQLRMITFTLLTRLLCLIPEKVAFEFILDVLKTSPLPLAKTSVLCVFKDLSRRRISTKDNDSETDLIVEKLSKLKVNDSNKAQQSNIRHYIQLDSSKMKAVHDCCLQTIQDSFTADAKKSDILLLLTYLNIFIVLKKTWDEDLLKIVCSKIDSNLKSVEPDKLPKYKEIVDKNESLNDYFTGIK
UniProt ID: P38315
Variant: K -> E at position 343-343
Variant annotation: in strain: W303-1a
Protein function: Involved in oxidative stress response and redox homeostasis. Required for hydrogen peroxide-induced oxidation and nuclear localization (activation) of YAP1. Functions probably in concert with HYP1/GPX3, the actual YAP1 modifying enzyme. YBP1 is not required for HYP1/GPX3-independent, diamide-induced oxidation of YAP1.
Reference sequence:
MEPIDDILFEVTDAFKTQKEDLLELVTLIDIYGEQVNQEGSYEEKTRFIETLNTLLEDNPSTTGEIGWDLPKGLLKFLSKDNVDVNGRLGTNMIVQGVMKCFYAISIQGEPKKCLITGLELLSSLCSKDFSKSDQQNKEDFVDKKANTLPPEGVIENSSNRKDFPSYGESKSSNEFFLKLKSYILFEFIGASLKRISTLFPSKYLGAAVSTIEKFVYSHADTFEDALFLLRRVYTFCRNYIPPDPPKDIQLNEDFTREMFDKVVEEESELQVRLLRRLCTFGISTPIKTVTTNADVKYYCALNQQKFELSAYYTEYLELFCRYYQMAFSLDVDIEGEFQNVIKECRIIYKSVPQEISAVNDEAKLVLERMVYKLAYTFEVQKAAKEKNVGLDYNGVILFSGIHYLETNQHLVKEMNITDAIYLYLRFTTPSLYSKVYYNVAVESVSRYWLWYAITTEPLEDVKKELKNLSVFVTKTLLHVLLQKNCIQVNQQLRMITFTLLTRLLCLIPEKVAFEFILDVLKTSPLPLAKTSVLCVFKDLSRRRISTKDNDSETDLIVEKLSKLKVNDSNKAQQSNIRHYIQLDSSKMKAVHDCCLQTIQDSFTADAKKSDILLLLTYLNIFIVLKKTWDEDLLKIVCSKIDSNLKSVEPDKLPKYKEIVDKNESLNDYFTGIK
UniProt ID: P38315
Variant: N -> D at position 570-570
Variant annotation: in strain: W303-1a
Protein function: Involved in oxidative stress response and redox homeostasis. Required for hydrogen peroxide-induced oxidation and nuclear localization (activation) of YAP1. Functions probably in concert with HYP1/GPX3, the actual YAP1 modifying enzyme. YBP1 is not required for HYP1/GPX3-independent, diamide-induced oxidation of YAP1.
Reference sequence:
MEPIDDILFEVTDAFKTQKEDLLELVTLIDIYGEQVNQEGSYEEKTRFIETLNTLLEDNPSTTGEIGWDLPKGLLKFLSKDNVDVNGRLGTNMIVQGVMKCFYAISIQGEPKKCLITGLELLSSLCSKDFSKSDQQNKEDFVDKKANTLPPEGVIENSSNRKDFPSYGESKSSNEFFLKLKSYILFEFIGASLKRISTLFPSKYLGAAVSTIEKFVYSHADTFEDALFLLRRVYTFCRNYIPPDPPKDIQLNEDFTREMFDKVVEEESELQVRLLRRLCTFGISTPIKTVTTNADVKYYCALNQQKFELSAYYTEYLELFCRYYQMAFSLDVDIEGEFQNVIKECRIIYKSVPQEISAVNDEAKLVLERMVYKLAYTFEVQKAAKEKNVGLDYNGVILFSGIHYLETNQHLVKEMNITDAIYLYLRFTTPSLYSKVYYNVAVESVSRYWLWYAITTEPLEDVKKELKNLSVFVTKTLLHVLLQKNCIQVNQQLRMITFTLLTRLLCLIPEKVAFEFILDVLKTSPLPLAKTSVLCVFKDLSRRRISTKDNDSETDLIVEKLSKLKVNDSNKAQQSNIRHYIQLDSSKMKAVHDCCLQTIQDSFTADAKKSDILLLLTYLNIFIVLKKTWDEDLLKIVCSKIDSNLKSVEPDKLPKYKEIVDKNESLNDYFTGIK
UniProt ID: P38365
Variant: A -> E at position 56-56
Variant annotation: in A2
Protein function: Variable subunit of the ferredoxin-thioredoxin reductase (FTR), which catalyzes the two-electron reduction of thioredoxins by the electrons provided by reduced ferredoxin.
Reference sequence:
MTTGVAVMSSATAASTATATAAATARIPLFLSRNNSSATVCSTLRCRTITRTRTRARLAICCEVALKSDSSTGFDSSSSSPPEEDEELKKNLEKVGCKVKVKSPLKVYHVPKLPEVELTPDMVGVIKQYVGFWKGKYISPNYPFKVEYRIDVPDRGSVKLVVHLKEEEFEIIAE
UniProt ID: P38365
Variant: S -> SS at position 80-80
Variant annotation: in A2
Protein function: Variable subunit of the ferredoxin-thioredoxin reductase (FTR), which catalyzes the two-electron reduction of thioredoxins by the electrons provided by reduced ferredoxin.
Reference sequence:
MTTGVAVMSSATAASTATATAAATARIPLFLSRNNSSATVCSTLRCRTITRTRTRARLAICCEVALKSDSSTGFDSSSSSPPEEDEELKKNLEKVGCKVKVKSPLKVYHVPKLPEVELTPDMVGVIKQYVGFWKGKYISPNYPFKVEYRIDVPDRGSVKLVVHLKEEEFEIIAE
UniProt ID: P38393
Variant: F -> C at position 51-51
Variant annotation: in strain: B
Protein function: Causes inhibition of cell division. At high levels of expression, can also abolish the rod shape of the cells. Division inhibition by KilR can be relieved by overexpression of the cell division protein FtsZ.
Reference sequence:
MIAHHFGTDEIPRQCVTPGDYVLHEGRTYIASANNIKKRKLYIRNLTTKTFITDRMIKVFLGRDGLPVKAESW
UniProt ID: P38405
Variant: V -> F at position 16-16
Variant annotation: in dbSNP:rs1039372506
Protein function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. G(olf) alpha mediates signal transduction within the olfactory neuroepithelium and the basal ganglia. May be involved in some aspect of visual transduction, and in mediating the effect of one or more hormones/neurotransmitters.
Reference sequence:
MGCLGGNSKTTEDQGVDEKERREANKKIEKQLQKERLAYKATHRLLLLGAGESGKSTIVKQMRILHVNGFNPEEKKQKILDIRKNVKDAIVTIVSAMSTIIPPVPLANPENQFRSDYIKSIAPITDFEYSQEFFDHVKKLWDDEGVKACFERSNEYQLIDCAQYFLERIDSVSLVDYTPTDQDLLRCRVLTSGIFETRFQVDKVNFHMFDVGGQRDERRKWIQCFNDVTAIIYVAACSSYNMVIREDNNTNRLRESLDLFESIWNNRWLRTISIILFLNKQDMLAEKVLAGKSKIEDYFPEYANYTVPEDATPDAGEDPKVTRAKFFIRDLFLRISTATGDGKHYCYPHFTCAVDTENIRRVFNDCRDIIQRMHLKQYELL
UniProt ID: P38405
Variant: V -> M at position 137-137
Variant annotation: in DYT25; loss of function mutation; dbSNP:rs398122923
Effect: loss
Target: function mutation
Protein function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. G(olf) alpha mediates signal transduction within the olfactory neuroepithelium and the basal ganglia. May be involved in some aspect of visual transduction, and in mediating the effect of one or more hormones/neurotransmitters.
Reference sequence:
MGCLGGNSKTTEDQGVDEKERREANKKIEKQLQKERLAYKATHRLLLLGAGESGKSTIVKQMRILHVNGFNPEEKKQKILDIRKNVKDAIVTIVSAMSTIIPPVPLANPENQFRSDYIKSIAPITDFEYSQEFFDHVKKLWDDEGVKACFERSNEYQLIDCAQYFLERIDSVSLVDYTPTDQDLLRCRVLTSGIFETRFQVDKVNFHMFDVGGQRDERRKWIQCFNDVTAIIYVAACSSYNMVIREDNNTNRLRESLDLFESIWNNRWLRTISIILFLNKQDMLAEKVLAGKSKIEDYFPEYANYTVPEDATPDAGEDPKVTRAKFFIRDLFLRISTATGDGKHYCYPHFTCAVDTENIRRVFNDCRDIIQRMHLKQYELL
UniProt ID: P38405
Variant: E -> K at position 155-155
Variant annotation: in DYT25; loss of function mutation; dbSNP:rs398122925
Effect: loss
Target: function mutation
Protein function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. G(olf) alpha mediates signal transduction within the olfactory neuroepithelium and the basal ganglia. May be involved in some aspect of visual transduction, and in mediating the effect of one or more hormones/neurotransmitters.
Reference sequence:
MGCLGGNSKTTEDQGVDEKERREANKKIEKQLQKERLAYKATHRLLLLGAGESGKSTIVKQMRILHVNGFNPEEKKQKILDIRKNVKDAIVTIVSAMSTIIPPVPLANPENQFRSDYIKSIAPITDFEYSQEFFDHVKKLWDDEGVKACFERSNEYQLIDCAQYFLERIDSVSLVDYTPTDQDLLRCRVLTSGIFETRFQVDKVNFHMFDVGGQRDERRKWIQCFNDVTAIIYVAACSSYNMVIREDNNTNRLRESLDLFESIWNNRWLRTISIILFLNKQDMLAEKVLAGKSKIEDYFPEYANYTVPEDATPDAGEDPKVTRAKFFIRDLFLRISTATGDGKHYCYPHFTCAVDTENIRRVFNDCRDIIQRMHLKQYELL
UniProt ID: P38420
Variant: I -> N at position 787-787
Protein function: Essential for the completion of the three rounds of mitosis in female megaspores required for the development of mature gametophytes .
Reference sequence:
MEYNEYEPEPQYVEDDDDEEITQEDAWAVISAYFEEKGLVRQQLDSFDEFIQNTMQEIVDESADIEIRPESQHNPGHQSDFAETIYKISFGQIYLSKPMMTESDGETATLFPKAARLRNLTYSAPLYVDVTKRVIKKGHDGEEVTETQDFTKVFIGKVPIMLRSSYCTLFQNSEKDLTELGECPYDQGGYFIINGSEKVLIAQEKMSTNHVYVFKKRQPNKYAYVGEVRSMAENQNRPPSTMFVRMLARASAKGGSSGQYIRCTLPYIRTEIPIIIVFRALGFVADKDILEHICYDFADTQMMELLRPSLEEAFVIQNQLVALDYIGKRGATVGVTKEKRIKYARDILQKEMLPHVGIGEHCETKKAYYFGYIIHRLLLCALGRRPEDDRDHYGNKRLDLAGPLLGGLFRMLFRKLTRDVRSYVQKCVDNGKEVNLQFAIKAKTITSGLKYSLATGNWGQANAAGTRAGVSQVLNRLTYASTLSHLRRLNSPIGREGKLAKPRQLHNSQWGMMCPAETPEGQACGLVKNLALMVYITVGSAAYPILEFLEEWGTENFEEISPSVIPQATKIFVNGMWVGVHRDPDMLVKTLRRLRRRVDVNTEVGVVRDIRLKELRIYTDYGRCSRPLFIVDNQKLLIKKRDIYALQQRESAEEDGWHHLVAKGFIEYIDTEEEETTMISMTISDLVQARLRPEEAYTENYTHCEIHPSLILGVCASIIPFPDHNQSPRNTYQSAMGKQAMGIYVTNYQFRMDTLAYVLYYPQKPLVTTRAMEHLHFRQLPAGINAIVAISCYSGYNQEDSVIMNQSSIDRGFFRSLFFRSYRDEEKKMGTLVKEDFGRPDRGSTMGMRHGSYDKLDDDGLAPPGTRVSGEDVIIGKTTPISQDEAQGQSSRYTRRDHSISLRHSETGMVDQVLLTTNADGLRFVKVRVRSVRIPQIGDKFSSRHGQKGTVGMTYTQEDMPWTIEGVTPDIIVNPHAIPSRMTIGQLIECIMGKVAAHMGKEGDATPFTDVTVDNISKALHKCGYQMRGFERMYNGHTGRPLTAMIFLGPTYYQRLKHMVDDKIHSRGRGPVQILTRQPAEGRSRDGGLRFGEMERDCMIAHGAAHFLKERLFDQSDAYRVHVCEVCGLIAIANLKKNSFECRGCKNKTDIVQVYIPYACKLLFQELMSMAIAPRMLTKHLKSAKGRQ
UniProt ID: P38435
Variant: F -> S at position 299-299
Variant annotation: in PXEL-MCFD; dbSNP:rs121909677
Protein function: Mediates the vitamin K-dependent carboxylation of glutamate residues to calcium-binding gamma-carboxyglutamate (Gla) residues with the concomitant conversion of the reduced hydroquinone form of vitamin K to vitamin K epoxide.
Reference sequence:
MAVSAGSARTSPSSDKVQKDKAELISGPRQDSRIGKLLGFEWTDLSSWRRLVTLLNRPTDPASLAVFRFLFGFLMVLDIPQERGLSSLDRKYLDGLDVCRFPLLDALRPLPLDWMYLVYTIMFLGALGMMLGLCYRISCVLFLLPYWYVFLLDKTSWNNHSYLYGLLAFQLTFMDANHYWSVDGLLNAHRRNAHVPLWNYAVLRGQIFIVYFIAGVKKLDADWVEGYSMEYLSRHWLFSPFKLLLSEELTSLLVVHWGGLLLDLSAGFLLFFDVSRSIGLFFVSYFHCMNSQLFSIGMFSYVMLASSPLFCSPEWPRKLVSYCPRRLQQLLPLKAAPQPSVSCVYKRSRGKSGQKPGLRHQLGAAFTLLYLLEQLFLPYSHFLTQGYNNWTNGLYGYSWDMMVHSRSHQHVKITYRDGRTGELGYLNPGVFTQSRRWKDHADMLKQYATCLSRLLPKYNVTEPQIYFDIWVSINDRFQQRIFDPRVDIVQAAWSPFQRTSWVQPLLMDLSPWRAKLQEIKSSLDNHTEVVFIADFPGLHLENFVSEDLGNTSIQLLQGEVTVELVAEQKNQTLREGEKMQLPAGEYHKVYTTSPSPSCYMYVYVNTTELALEQDLAYLQELKEKVENGSETGPLPPELQPLLEGEVKGGPEPTPLVQTFLRRQQRLQEIERRRNTPFHERFFRFLLRKLYVFRRSFLMTCISLRNLILGRPSLEQLAQEVTYANLRPFEAVGELNPSNTDSSHSNPPESNPDPVHSEF
UniProt ID: P38435
Variant: R -> Q at position 325-325
Variant annotation: in dbSNP:rs699664
Protein function: Mediates the vitamin K-dependent carboxylation of glutamate residues to calcium-binding gamma-carboxyglutamate (Gla) residues with the concomitant conversion of the reduced hydroquinone form of vitamin K to vitamin K epoxide.
Reference sequence:
MAVSAGSARTSPSSDKVQKDKAELISGPRQDSRIGKLLGFEWTDLSSWRRLVTLLNRPTDPASLAVFRFLFGFLMVLDIPQERGLSSLDRKYLDGLDVCRFPLLDALRPLPLDWMYLVYTIMFLGALGMMLGLCYRISCVLFLLPYWYVFLLDKTSWNNHSYLYGLLAFQLTFMDANHYWSVDGLLNAHRRNAHVPLWNYAVLRGQIFIVYFIAGVKKLDADWVEGYSMEYLSRHWLFSPFKLLLSEELTSLLVVHWGGLLLDLSAGFLLFFDVSRSIGLFFVSYFHCMNSQLFSIGMFSYVMLASSPLFCSPEWPRKLVSYCPRRLQQLLPLKAAPQPSVSCVYKRSRGKSGQKPGLRHQLGAAFTLLYLLEQLFLPYSHFLTQGYNNWTNGLYGYSWDMMVHSRSHQHVKITYRDGRTGELGYLNPGVFTQSRRWKDHADMLKQYATCLSRLLPKYNVTEPQIYFDIWVSINDRFQQRIFDPRVDIVQAAWSPFQRTSWVQPLLMDLSPWRAKLQEIKSSLDNHTEVVFIADFPGLHLENFVSEDLGNTSIQLLQGEVTVELVAEQKNQTLREGEKMQLPAGEYHKVYTTSPSPSCYMYVYVNTTELALEQDLAYLQELKEKVENGSETGPLPPELQPLLEGEVKGGPEPTPLVQTFLRRQQRLQEIERRRNTPFHERFFRFLLRKLYVFRRSFLMTCISLRNLILGRPSLEQLAQEVTYANLRPFEAVGELNPSNTDSSHSNPPESNPDPVHSEF
UniProt ID: P38435
Variant: L -> R at position 394-394
Variant annotation: in VKCFD1; affects glutamate binding; dbSNP:rs121909675
Protein function: Mediates the vitamin K-dependent carboxylation of glutamate residues to calcium-binding gamma-carboxyglutamate (Gla) residues with the concomitant conversion of the reduced hydroquinone form of vitamin K to vitamin K epoxide.
Reference sequence:
MAVSAGSARTSPSSDKVQKDKAELISGPRQDSRIGKLLGFEWTDLSSWRRLVTLLNRPTDPASLAVFRFLFGFLMVLDIPQERGLSSLDRKYLDGLDVCRFPLLDALRPLPLDWMYLVYTIMFLGALGMMLGLCYRISCVLFLLPYWYVFLLDKTSWNNHSYLYGLLAFQLTFMDANHYWSVDGLLNAHRRNAHVPLWNYAVLRGQIFIVYFIAGVKKLDADWVEGYSMEYLSRHWLFSPFKLLLSEELTSLLVVHWGGLLLDLSAGFLLFFDVSRSIGLFFVSYFHCMNSQLFSIGMFSYVMLASSPLFCSPEWPRKLVSYCPRRLQQLLPLKAAPQPSVSCVYKRSRGKSGQKPGLRHQLGAAFTLLYLLEQLFLPYSHFLTQGYNNWTNGLYGYSWDMMVHSRSHQHVKITYRDGRTGELGYLNPGVFTQSRRWKDHADMLKQYATCLSRLLPKYNVTEPQIYFDIWVSINDRFQQRIFDPRVDIVQAAWSPFQRTSWVQPLLMDLSPWRAKLQEIKSSLDNHTEVVFIADFPGLHLENFVSEDLGNTSIQLLQGEVTVELVAEQKNQTLREGEKMQLPAGEYHKVYTTSPSPSCYMYVYVNTTELALEQDLAYLQELKEKVENGSETGPLPPELQPLLEGEVKGGPEPTPLVQTFLRRQQRLQEIERRRNTPFHERFFRFLLRKLYVFRRSFLMTCISLRNLILGRPSLEQLAQEVTYANLRPFEAVGELNPSNTDSSHSNPPESNPDPVHSEF
UniProt ID: P38435
Variant: R -> C at position 476-476
Variant annotation: in PXEL-MCFD; dbSNP:rs121909681
Protein function: Mediates the vitamin K-dependent carboxylation of glutamate residues to calcium-binding gamma-carboxyglutamate (Gla) residues with the concomitant conversion of the reduced hydroquinone form of vitamin K to vitamin K epoxide.
Reference sequence:
MAVSAGSARTSPSSDKVQKDKAELISGPRQDSRIGKLLGFEWTDLSSWRRLVTLLNRPTDPASLAVFRFLFGFLMVLDIPQERGLSSLDRKYLDGLDVCRFPLLDALRPLPLDWMYLVYTIMFLGALGMMLGLCYRISCVLFLLPYWYVFLLDKTSWNNHSYLYGLLAFQLTFMDANHYWSVDGLLNAHRRNAHVPLWNYAVLRGQIFIVYFIAGVKKLDADWVEGYSMEYLSRHWLFSPFKLLLSEELTSLLVVHWGGLLLDLSAGFLLFFDVSRSIGLFFVSYFHCMNSQLFSIGMFSYVMLASSPLFCSPEWPRKLVSYCPRRLQQLLPLKAAPQPSVSCVYKRSRGKSGQKPGLRHQLGAAFTLLYLLEQLFLPYSHFLTQGYNNWTNGLYGYSWDMMVHSRSHQHVKITYRDGRTGELGYLNPGVFTQSRRWKDHADMLKQYATCLSRLLPKYNVTEPQIYFDIWVSINDRFQQRIFDPRVDIVQAAWSPFQRTSWVQPLLMDLSPWRAKLQEIKSSLDNHTEVVFIADFPGLHLENFVSEDLGNTSIQLLQGEVTVELVAEQKNQTLREGEKMQLPAGEYHKVYTTSPSPSCYMYVYVNTTELALEQDLAYLQELKEKVENGSETGPLPPELQPLLEGEVKGGPEPTPLVQTFLRRQQRLQEIERRRNTPFHERFFRFLLRKLYVFRRSFLMTCISLRNLILGRPSLEQLAQEVTYANLRPFEAVGELNPSNTDSSHSNPPESNPDPVHSEF