sujigwak/NVAR huggingface dataset:
UniProt ID: P50219
Variant: R -> G at position 245-245
Variant annotation: in CURRAS
Protein function: Putative transcription factor involved in pancreas development and function.
Reference sequence:
MEKSKNFRIDALLAVDPPRAASAQSAPLALVTSLAAAASGTGGGGGGGGASGGTSGSCSPASSEPPAAPADRLRAESPSPPRLLAAHCALLPKPGFLGAGGGGGGTGGGHGGPHHHAHPGAAAAAAAAAAAAAAGGLALGLHPGGAQGGAGLPAQAALYGHPVYGYSAAAAAAALAGQHPALSYSYPQVQGAHPAHPADPIKLGAGTFQLDQWLRASTAGMILPKMPDFNSQAQSNLLGKCRRPRTAFTSQQLLELEHQFKLNKYLSRPKRFEVATSLMLTETQVKIWFQNRRMKWKRSKKAKEQAAQEAEKQKGGGGGAGKGGAEEPGAEELLGPPAPGDKGSGRRLRDLRDSDPEEDEDEDDEDHFPYSNGASVHAASSDCSSEDDSPPPRPSHQPAPQ
UniProt ID: P50219
Variant: R -> H at position 245-245
Variant annotation: in CURRAS
Protein function: Putative transcription factor involved in pancreas development and function.
Reference sequence:
MEKSKNFRIDALLAVDPPRAASAQSAPLALVTSLAAAASGTGGGGGGGGASGGTSGSCSPASSEPPAAPADRLRAESPSPPRLLAAHCALLPKPGFLGAGGGGGGTGGGHGGPHHHAHPGAAAAAAAAAAAAAAGGLALGLHPGGAQGGAGLPAQAALYGHPVYGYSAAAAAAALAGQHPALSYSYPQVQGAHPAHPADPIKLGAGTFQLDQWLRASTAGMILPKMPDFNSQAQSNLLGKCRRPRTAFTSQQLLELEHQFKLNKYLSRPKRFEVATSLMLTETQVKIWFQNRRMKWKRSKKAKEQAAQEAEKQKGGGGGAGKGGAEEPGAEELLGPPAPGDKGSGRRLRDLRDSDPEEDEDEDDEDHFPYSNGASVHAASSDCSSEDDSPPPRPSHQPAPQ
UniProt ID: P50219
Variant: T -> S at position 246-246
Variant annotation: in CURRAS; dbSNP:rs121912548
Protein function: Putative transcription factor involved in pancreas development and function.
Reference sequence:
MEKSKNFRIDALLAVDPPRAASAQSAPLALVTSLAAAASGTGGGGGGGGASGGTSGSCSPASSEPPAAPADRLRAESPSPPRLLAAHCALLPKPGFLGAGGGGGGTGGGHGGPHHHAHPGAAAAAAAAAAAAAAGGLALGLHPGGAQGGAGLPAQAALYGHPVYGYSAAAAAAALAGQHPALSYSYPQVQGAHPAHPADPIKLGAGTFQLDQWLRASTAGMILPKMPDFNSQAQSNLLGKCRRPRTAFTSQQLLELEHQFKLNKYLSRPKRFEVATSLMLTETQVKIWFQNRRMKWKRSKKAKEQAAQEAEKQKGGGGGAGKGGAEEPGAEELLGPPAPGDKGSGRRLRDLRDSDPEEDEDEDDEDHFPYSNGASVHAASSDCSSEDDSPPPRPSHQPAPQ
UniProt ID: P50219
Variant: W -> G at position 288-288
Variant annotation: in CURRAS
Protein function: Putative transcription factor involved in pancreas development and function.
Reference sequence:
MEKSKNFRIDALLAVDPPRAASAQSAPLALVTSLAAAASGTGGGGGGGGASGGTSGSCSPASSEPPAAPADRLRAESPSPPRLLAAHCALLPKPGFLGAGGGGGGTGGGHGGPHHHAHPGAAAAAAAAAAAAAAGGLALGLHPGGAQGGAGLPAQAALYGHPVYGYSAAAAAAALAGQHPALSYSYPQVQGAHPAHPADPIKLGAGTFQLDQWLRASTAGMILPKMPDFNSQAQSNLLGKCRRPRTAFTSQQLLELEHQFKLNKYLSRPKRFEVATSLMLTETQVKIWFQNRRMKWKRSKKAKEQAAQEAEKQKGGGGGAGKGGAEEPGAEELLGPPAPGDKGSGRRLRDLRDSDPEEDEDEDDEDHFPYSNGASVHAASSDCSSEDDSPPPRPSHQPAPQ
UniProt ID: P50219
Variant: W -> L at position 288-288
Variant annotation: in CURRAS
Protein function: Putative transcription factor involved in pancreas development and function.
Reference sequence:
MEKSKNFRIDALLAVDPPRAASAQSAPLALVTSLAAAASGTGGGGGGGGASGGTSGSCSPASSEPPAAPADRLRAESPSPPRLLAAHCALLPKPGFLGAGGGGGGTGGGHGGPHHHAHPGAAAAAAAAAAAAAAGGLALGLHPGGAQGGAGLPAQAALYGHPVYGYSAAAAAAALAGQHPALSYSYPQVQGAHPAHPADPIKLGAGTFQLDQWLRASTAGMILPKMPDFNSQAQSNLLGKCRRPRTAFTSQQLLELEHQFKLNKYLSRPKRFEVATSLMLTETQVKIWFQNRRMKWKRSKKAKEQAAQEAEKQKGGGGGAGKGGAEEPGAEELLGPPAPGDKGSGRRLRDLRDSDPEEDEDEDDEDHFPYSNGASVHAASSDCSSEDDSPPPRPSHQPAPQ
UniProt ID: P50219
Variant: F -> S at position 289-289
Variant annotation: in CURRAS
Protein function: Putative transcription factor involved in pancreas development and function.
Reference sequence:
MEKSKNFRIDALLAVDPPRAASAQSAPLALVTSLAAAASGTGGGGGGGGASGGTSGSCSPASSEPPAAPADRLRAESPSPPRLLAAHCALLPKPGFLGAGGGGGGTGGGHGGPHHHAHPGAAAAAAAAAAAAAAGGLALGLHPGGAQGGAGLPAQAALYGHPVYGYSAAAAAAALAGQHPALSYSYPQVQGAHPAHPADPIKLGAGTFQLDQWLRASTAGMILPKMPDFNSQAQSNLLGKCRRPRTAFTSQQLLELEHQFKLNKYLSRPKRFEVATSLMLTETQVKIWFQNRRMKWKRSKKAKEQAAQEAEKQKGGGGGAGKGGAEEPGAEELLGPPAPGDKGSGRRLRDLRDSDPEEDEDEDDEDHFPYSNGASVHAASSDCSSEDDSPPPRPSHQPAPQ
UniProt ID: P50219
Variant: Q -> P at position 290-290
Variant annotation: in CURRAS
Protein function: Putative transcription factor involved in pancreas development and function.
Reference sequence:
MEKSKNFRIDALLAVDPPRAASAQSAPLALVTSLAAAASGTGGGGGGGGASGGTSGSCSPASSEPPAAPADRLRAESPSPPRLLAAHCALLPKPGFLGAGGGGGGTGGGHGGPHHHAHPGAAAAAAAAAAAAAAGGLALGLHPGGAQGGAGLPAQAALYGHPVYGYSAAAAAAALAGQHPALSYSYPQVQGAHPAHPADPIKLGAGTFQLDQWLRASTAGMILPKMPDFNSQAQSNLLGKCRRPRTAFTSQQLLELEHQFKLNKYLSRPKRFEVATSLMLTETQVKIWFQNRRMKWKRSKKAKEQAAQEAEKQKGGGGGAGKGGAEEPGAEELLGPPAPGDKGSGRRLRDLRDSDPEEDEDEDDEDHFPYSNGASVHAASSDCSSEDDSPPPRPSHQPAPQ
UniProt ID: P50219
Variant: R -> W at position 292-292
Variant annotation: in CURRAS; dbSNP:rs2134838763
Protein function: Putative transcription factor involved in pancreas development and function.
Reference sequence:
MEKSKNFRIDALLAVDPPRAASAQSAPLALVTSLAAAASGTGGGGGGGGASGGTSGSCSPASSEPPAAPADRLRAESPSPPRLLAAHCALLPKPGFLGAGGGGGGTGGGHGGPHHHAHPGAAAAAAAAAAAAAAGGLALGLHPGGAQGGAGLPAQAALYGHPVYGYSAAAAAAALAGQHPALSYSYPQVQGAHPAHPADPIKLGAGTFQLDQWLRASTAGMILPKMPDFNSQAQSNLLGKCRRPRTAFTSQQLLELEHQFKLNKYLSRPKRFEVATSLMLTETQVKIWFQNRRMKWKRSKKAKEQAAQEAEKQKGGGGGAGKGGAEEPGAEELLGPPAPGDKGSGRRLRDLRDSDPEEDEDEDDEDHFPYSNGASVHAASSDCSSEDDSPPPRPSHQPAPQ
UniProt ID: P50219
Variant: R -> Q at position 293-293
Variant annotation: in CURRAS
Protein function: Putative transcription factor involved in pancreas development and function.
Reference sequence:
MEKSKNFRIDALLAVDPPRAASAQSAPLALVTSLAAAASGTGGGGGGGGASGGTSGSCSPASSEPPAAPADRLRAESPSPPRLLAAHCALLPKPGFLGAGGGGGGTGGGHGGPHHHAHPGAAAAAAAAAAAAAAGGLALGLHPGGAQGGAGLPAQAALYGHPVYGYSAAAAAAALAGQHPALSYSYPQVQGAHPAHPADPIKLGAGTFQLDQWLRASTAGMILPKMPDFNSQAQSNLLGKCRRPRTAFTSQQLLELEHQFKLNKYLSRPKRFEVATSLMLTETQVKIWFQNRRMKWKRSKKAKEQAAQEAEKQKGGGGGAGKGGAEEPGAEELLGPPAPGDKGSGRRLRDLRDSDPEEDEDEDDEDHFPYSNGASVHAASSDCSSEDDSPPPRPSHQPAPQ
UniProt ID: P50219
Variant: R -> W at position 293-293
Variant annotation: in CURRAS
Protein function: Putative transcription factor involved in pancreas development and function.
Reference sequence:
MEKSKNFRIDALLAVDPPRAASAQSAPLALVTSLAAAASGTGGGGGGGGASGGTSGSCSPASSEPPAAPADRLRAESPSPPRLLAAHCALLPKPGFLGAGGGGGGTGGGHGGPHHHAHPGAAAAAAAAAAAAAAGGLALGLHPGGAQGGAGLPAQAALYGHPVYGYSAAAAAAALAGQHPALSYSYPQVQGAHPAHPADPIKLGAGTFQLDQWLRASTAGMILPKMPDFNSQAQSNLLGKCRRPRTAFTSQQLLELEHQFKLNKYLSRPKRFEVATSLMLTETQVKIWFQNRRMKWKRSKKAKEQAAQEAEKQKGGGGGAGKGGAEEPGAEELLGPPAPGDKGSGRRLRDLRDSDPEEDEDEDDEDHFPYSNGASVHAASSDCSSEDDSPPPRPSHQPAPQ
UniProt ID: P50221
Variant: S -> L at position 27-27
Variant annotation: in dbSNP:rs9898682
Protein function: Mesodermal transcription factor that plays a key role in somitogenesis and is specifically required for sclerotome development. Required for maintenance of the sclerotome polarity and formation of the cranio-cervical joints . Binds specifically to the promoter of target genes and regulates their expression. Activates expression of NKX3-2 in the sclerotome. Activates expression of CDKN1A and CDKN2A in endothelial cells, acting as a regulator of vascular cell proliferation. While it activates CDKN1A in a DNA-dependent manner, it activates CDKN2A in a DNA-independent manner. Required for hematopoietic stem cell (HSCs) induction via its role in somitogenesis: specification of HSCs occurs via the deployment of a specific endothelial precursor population, which arises within a sub-compartment of the somite named endotome.
Reference sequence:
MDPAASSCMRSLQPPAPVWGCLRNPHSEGNGASGLPHYPPTPFSFHQKPDFLATATAAYPDFSASCLAATPHSLPQEEHIFTEQHPAFPQSPNWHFPVSDARRRPNSGPAGGSKEMGTSSLGLVDTTGGPGDDYGVLGSTANETEKKSSRRRKESSDNQENRGKPEGSSKARKERTAFTKEQLRELEAEFAHHNYLTRLRRYEIAVNLDLSERQVKVWFQNRRMKWKRVKGGQPISPNGQDPEDGDSTASPSSE
UniProt ID: P50253
Variant: D -> A at position 25-25
Variant annotation: in strain: 14021-0251.0
Protein function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Reference sequence:
MSTWANLGLQDSASPLMEQLIFFHDHALLILVMITVLVGYLMFMLFFNNYVNRFLLHGQLIEMIWTILPAIILLFIALPSLRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELTTDGFRLLDVDNRVILPMNSQIRILVTAADVIHSWTVPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESVPVNHFIKWISSNNS
UniProt ID: P50253
Variant: N -> S at position 115-115
Variant annotation: in strain: HW00, HW09, NC37, NC48, TT00 and TT01
Protein function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Reference sequence:
MSTWANLGLQDSASPLMEQLIFFHDHALLILVMITVLVGYLMFMLFFNNYVNRFLLHGQLIEMIWTILPAIILLFIALPSLRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELTTDGFRLLDVDNRVILPMNSQIRILVTAADVIHSWTVPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESVPVNHFIKWISSNNS
UniProt ID: P50253
Variant: F -> Y at position 118-118
Variant annotation: in strain: MD106, MD225 and RU35
Protein function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Reference sequence:
MSTWANLGLQDSASPLMEQLIFFHDHALLILVMITVLVGYLMFMLFFNNYVNRFLLHGQLIEMIWTILPAIILLFIALPSLRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELTTDGFRLLDVDNRVILPMNSQIRILVTAADVIHSWTVPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESVPVNHFIKWISSNNS
UniProt ID: P50253
Variant: T -> S at position 129-129
Variant annotation: in strain: 14021-0251.0, C167, AU023, DSR, DSW, KY007, KY045, KY201, KY215, MD106, MD111, MD112, MD199, MD221, MD225, MDW86, RU00, RU01, RU07, RU35, RU259 and Sc00
Protein function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Reference sequence:
MSTWANLGLQDSASPLMEQLIFFHDHALLILVMITVLVGYLMFMLFFNNYVNRFLLHGQLIEMIWTILPAIILLFIALPSLRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELTTDGFRLLDVDNRVILPMNSQIRILVTAADVIHSWTVPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESVPVNHFIKWISSNNS
UniProt ID: P50253
Variant: T -> I at position 130-130
Variant annotation: in strain: 14021-0251.0, C167, AU023, DSR, DSW, KY007, KY045, KY201, KY215, MD106, MD111, MD112, MD199, MD221, MD225, MDW86, RU00, RU01, RU07, RU35, RU259 and Sc00
Protein function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Reference sequence:
MSTWANLGLQDSASPLMEQLIFFHDHALLILVMITVLVGYLMFMLFFNNYVNRFLLHGQLIEMIWTILPAIILLFIALPSLRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELTTDGFRLLDVDNRVILPMNSQIRILVTAADVIHSWTVPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESVPVNHFIKWISSNNS
UniProt ID: P50253
Variant: V -> I at position 165-165
Variant annotation: in strain: AU023, C167, DSR, DSW, KY007, KY045, KY201, KY215, MD106, MD111, MD112, MD199, MD221, MD225, MDW86, RU00, RU01, RU07, RU35, RU259 and Sc00
Protein function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Reference sequence:
MSTWANLGLQDSASPLMEQLIFFHDHALLILVMITVLVGYLMFMLFFNNYVNRFLLHGQLIEMIWTILPAIILLFIALPSLRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELTTDGFRLLDVDNRVILPMNSQIRILVTAADVIHSWTVPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESVPVNHFIKWISSNNS
UniProt ID: P50253
Variant: H -> N at position 218-218
Variant annotation: in strain: 14021-0251.0
Protein function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Reference sequence:
MSTWANLGLQDSASPLMEQLIFFHDHALLILVMITVLVGYLMFMLFFNNYVNRFLLHGQLIEMIWTILPAIILLFIALPSLRLLYLLDEINEPSVTLKSIGHQWYWSYEYSDFNNIEFDSYMIPTNELTTDGFRLLDVDNRVILPMNSQIRILVTAADVIHSWTVPALGVKVDGTPGRLNQTNFFINRPGLFYGQCSEICGANHSFMPIVIESVPVNHFIKWISSNNS
UniProt ID: P50269
Variant: L -> I at position 28-28
Variant annotation: in strain: HW00, HW09, NC37, NC48, TT00 and TT01
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. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Reference sequence:
MMTNLFSVFDPSAIFNLSLNWLSTFLGLLMIPSIYWLMPSRYNIVWNSILLTLHKEFKTLLGPSGHNGSTFIFISLFSLILFNNFMGLFPYIFTSTSHLTLTLSLALPLWLCFMLYGWINHTQHMFAHLVPQGTPAILMPFMVCIETISNIIRPGTLAVRLTANMIAGHLLLTLLGNTGPSMSYLLVTFLLTAQIALLVLESAVAMIQSYVFAVLSTLYSSEVN
UniProt ID: P50269
Variant: L -> M at position 115-115
Variant annotation: in strain: HW00, HW09, NC37, NC48, TT00 and TT01
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. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Reference sequence:
MMTNLFSVFDPSAIFNLSLNWLSTFLGLLMIPSIYWLMPSRYNIVWNSILLTLHKEFKTLLGPSGHNGSTFIFISLFSLILFNNFMGLFPYIFTSTSHLTLTLSLALPLWLCFMLYGWINHTQHMFAHLVPQGTPAILMPFMVCIETISNIIRPGTLAVRLTANMIAGHLLLTLLGNTGPSMSYLLVTFLLTAQIALLVLESAVAMIQSYVFAVLSTLYSSEVN
UniProt ID: P50269
Variant: I -> F at position 119-119
Variant annotation: in strain: C167
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. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Reference sequence:
MMTNLFSVFDPSAIFNLSLNWLSTFLGLLMIPSIYWLMPSRYNIVWNSILLTLHKEFKTLLGPSGHNGSTFIFISLFSLILFNNFMGLFPYIFTSTSHLTLTLSLALPLWLCFMLYGWINHTQHMFAHLVPQGTPAILMPFMVCIETISNIIRPGTLAVRLTANMIAGHLLLTLLGNTGPSMSYLLVTFLLTAQIALLVLESAVAMIQSYVFAVLSTLYSSEVN
UniProt ID: P50269
Variant: I -> V at position 137-137
Variant annotation: in strain: HW00, HW09, NC37, NC48, TT00 and TT01
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. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Reference sequence:
MMTNLFSVFDPSAIFNLSLNWLSTFLGLLMIPSIYWLMPSRYNIVWNSILLTLHKEFKTLLGPSGHNGSTFIFISLFSLILFNNFMGLFPYIFTSTSHLTLTLSLALPLWLCFMLYGWINHTQHMFAHLVPQGTPAILMPFMVCIETISNIIRPGTLAVRLTANMIAGHLLLTLLGNTGPSMSYLLVTFLLTAQIALLVLESAVAMIQSYVFAVLSTLYSSEVN
UniProt ID: P50269
Variant: V -> I at position 187-187
Variant annotation: in strain: HW09
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. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Reference sequence:
MMTNLFSVFDPSAIFNLSLNWLSTFLGLLMIPSIYWLMPSRYNIVWNSILLTLHKEFKTLLGPSGHNGSTFIFISLFSLILFNNFMGLFPYIFTSTSHLTLTLSLALPLWLCFMLYGWINHTQHMFAHLVPQGTPAILMPFMVCIETISNIIRPGTLAVRLTANMIAGHLLLTLLGNTGPSMSYLLVTFLLTAQIALLVLESAVAMIQSYVFAVLSTLYSSEVN
UniProt ID: P50277
Variant: K -> E at position 229-229
Variant annotation: in strain: ATCC 28383 and ATCC 204626
Protein function: Catalyzes the transfer of the alpha-amino group from S-adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA) . It is the only aminotransferase known to utilize SAM as an amino donor .
Reference sequence:
MSQEISYTPDVAELLDFDKKHIWHPYTSLSSPLNVYPVKSAHGCKLVLDTDSPVDVEVIDAMSSWWCVIHGYNNPELNEALTKQMLKFSHVLLGGFTHKGAVNLVQKLLKVIDEPSLQYCFLADSGSVAVEVALKMALQSNMSGEATKNRTKFLTIKNGYHGDTFGAMSVCDPENSMHHIYNDRLSENIFAQAPSIVDGLPTSQNGFEDHWNAEEVTDLKKQFELHSDKICAVILEPILQGAGGLRPYHPQFLIEVQKLCNQYDVLFIMDEIATGFGRTGEIFAFKHCQKYQDQHGISPSDQIKVVPDILCVGKGLTSGYMTMSAVVVNDKVASRISSPNSPTGGCFMHGPTFMGNALACSVAEKSMDILLRGEWRKQVSAIENQIYRELYQYIKNPDNGLIGTVVKRVSVIGAVGIVELYKKTDPEWFQKKFISKGVHIRPFNCLCYIMPPYVITTEELTKVNQVLIEVLHEWKSHINQ