Atp5a1

Functionⁱ

Mitochondrial membrane ATP synthase (F₁F₀ 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, F₁ - containing the extramembraneous catalytic core, and F₀ - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F₁ is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F₁. Rotation of the central stalk against the surrounding alpha₃beta₃ subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity).By similarity

Sites

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Siteⁱ	413 – 413	1	Required for activityBy similarity

Regions

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Nucleotide bindingⁱ	212 – 219	8	ATPBy similarity

Enzyme and pathway databases

Reactomeⁱ	R-MMU-163210. Formation of ATP by chemiosmotic coupling.

Reactomeⁱ

R-MMU-163210. Formation of ATP by chemiosmotic coupling.

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: ATP synthase subunit alpha, mitochondrial
Gene namesⁱ	Name:Atp5a1
Organismⁱ	Mus musculus (Mouse)
Taxonomic identifierⁱ	10090 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesⁱ	UP000000589 Componentⁱ: Chromosome 18

Organism-specific databases

MGIⁱ	MGI:88115. Atp5a1.

Subcellular locationⁱ

Mitochondrion inner membrane By similarity
Cell membrane By similarity; Peripheral membrane protein By similarity; Extracellular side By similarity

Note:

Colocalizes with HRG on the cell surface of T-cells.By similarity

GO - Cellular componentⁱ

COP9 signalosome Source: Ensembl
extracellular exosome Source: MGI
membrane
Source: ParkinsonsUK-UCL
Inferred from mutant phenotypeⁱ
- 20080761
mitochondrial inner membrane
Source: MGI
Inferred from direct assayⁱ
- 12865426
mitochondrial proton-transporting ATP synthase complex Source: UniProtKB
mitochondrion
Source: MGI
Inferred from direct assayⁱ
myelin sheath
Source: UniProtKB
Inferred from direct assayⁱ
- 17634366
plasma membrane Source: MGI
proton-transporting ATP synthase complex, catalytic core F(1) Source: UniProtKB-KW

Complete GO annotation...

Keywords - Cellular componentⁱ

Cell membrane, CF(1), Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Transit peptideⁱ	1 – 43	43	MitochondrionBy similarity			Add BLAST
Chainⁱ	44 – 553	510	ATP synthase subunit alpha, mitochondrial		PRO_0000002425	Add BLAST

Amino acid modifications

Feature key	Position(s)	Length	Description
Modified residueⁱ	44 – 44	1	Pyrrolidone carboxylic acidBy similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:P19483 (ATPA_BOVIN)
Modified residueⁱ	53 – 53	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.6 "A tissue-specific atlas of mouse protein phosphorylation and expression." Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P. Cell 143:1174-1189(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53; SER-106 AND SER-521, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	65 – 65	1	PhosphoserineBy similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:P25705 (ATPA_HUMAN)
Modified residueⁱ	76 – 76	1	Phosphoserine; alternateCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.5 "Quantitative analysis of both protein expression and serine / threonine post-translational modifications through stable isotope labeling with dithiothreitol." Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L., Hart G.W., Burlingame A.L. Proteomics 5:388-398(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Glycosylationⁱ	76 – 76	1	O-linked (GlcNAc); alternateBy similarity
Modified residueⁱ	106 – 106	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.6 "A tissue-specific atlas of mouse protein phosphorylation and expression." Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P. Cell 143:1174-1189(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53; SER-106 AND SER-521, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	123 – 123	1	N6-acetyllysineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.8 "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways." Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W. Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-123; LYS-126; LYS-132; LYS-161; LYS-167; LYS-230; LYS-239; LYS-240; LYS-261; LYS-305; LYS-427; LYS-434; LYS-498; LYS-506; LYS-531; LYS-539 AND LYS-541, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	126 – 126	1	N6-acetyllysineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.8 "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways." Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W. Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-123; LYS-126; LYS-132; LYS-161; LYS-167; LYS-230; LYS-239; LYS-240; LYS-261; LYS-305; LYS-427; LYS-434; LYS-498; LYS-506; LYS-531; LYS-539 AND LYS-541, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	132 – 132	1	N6-acetyllysineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.8 "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways." Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W. Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-123; LYS-126; LYS-132; LYS-161; LYS-167; LYS-230; LYS-239; LYS-240; LYS-261; LYS-305; LYS-427; LYS-434; LYS-498; LYS-506; LYS-531; LYS-539 AND LYS-541, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	134 – 134	1	PhosphothreonineBy similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:P15999 (ATPA_RAT)
Modified residueⁱ	161 – 161	1	N6-acetyllysine; alternateCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.8 "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways." Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W. Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-123; LYS-126; LYS-132; LYS-161; LYS-167; LYS-230; LYS-239; LYS-240; LYS-261; LYS-305; LYS-427; LYS-434; LYS-498; LYS-506; LYS-531; LYS-539 AND LYS-541, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	161 – 161	1	N6-succinyllysine; alternateCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.7 "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways." Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y. Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-498; LYS-531 AND LYS-539, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-161; LYS-167; LYS-230; LYS-239; LYS-261; LYS-305; LYS-427; LYS-498; LYS-506; LYS-531 AND LYS-539, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	166 – 166	1	PhosphoserineBy similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:P25705 (ATPA_HUMAN)
Modified residueⁱ	167 – 167	1	N6-acetyllysine; alternateCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.8 "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways." Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W. Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-123; LYS-126; LYS-132; LYS-161; LYS-167; LYS-230; LYS-239; LYS-240; LYS-261; LYS-305; LYS-427; LYS-434; LYS-498; LYS-506; LYS-531; LYS-539 AND LYS-541, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	167 – 167	1	N6-succinyllysine; alternateCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.7 "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways." Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y. Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-498; LYS-531 AND LYS-539, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-161; LYS-167; LYS-230; LYS-239; LYS-261; LYS-305; LYS-427; LYS-498; LYS-506; LYS-531 AND LYS-539, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	184 – 184	1	PhosphoserineBy similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:P25705 (ATPA_HUMAN)
Modified residueⁱ	230 – 230	1	N6-acetyllysine; alternateCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.8 "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways." Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W. Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-123; LYS-126; LYS-132; LYS-161; LYS-167; LYS-230; LYS-239; LYS-240; LYS-261; LYS-305; LYS-427; LYS-434; LYS-498; LYS-506; LYS-531; LYS-539 AND LYS-541, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	230 – 230	1	N6-succinyllysine; alternateCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.7 "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways." Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y. Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-498; LYS-531 AND LYS-539, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-161; LYS-167; LYS-230; LYS-239; LYS-261; LYS-305; LYS-427; LYS-498; LYS-506; LYS-531 AND LYS-539, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	239 – 239	1	N6-acetyllysine; alternateCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.8 "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways." Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W. Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-123; LYS-126; LYS-132; LYS-161; LYS-167; LYS-230; LYS-239; LYS-240; LYS-261; LYS-305; LYS-427; LYS-434; LYS-498; LYS-506; LYS-531; LYS-539 AND LYS-541, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	239 – 239	1	N6-succinyllysine; alternateCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.7 "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways." Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y. Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-498; LYS-531 AND LYS-539, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-161; LYS-167; LYS-230; LYS-239; LYS-261; LYS-305; LYS-427; LYS-498; LYS-506; LYS-531 AND LYS-539, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	240 – 240	1	N6-acetyllysineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.8 "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways." Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W. Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-123; LYS-126; LYS-132; LYS-161; LYS-167; LYS-230; LYS-239; LYS-240; LYS-261; LYS-305; LYS-427; LYS-434; LYS-498; LYS-506; LYS-531; LYS-539 AND LYS-541, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	261 – 261	1	N6-acetyllysine; alternateCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.8 "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways." Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W. Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-123; LYS-126; LYS-132; LYS-161; LYS-167; LYS-230; LYS-239; LYS-240; LYS-261; LYS-305; LYS-427; LYS-434; LYS-498; LYS-506; LYS-531; LYS-539 AND LYS-541, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	261 – 261	1	N6-succinyllysine; alternateCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.7 "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways." Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y. Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-498; LYS-531 AND LYS-539, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-161; LYS-167; LYS-230; LYS-239; LYS-261; LYS-305; LYS-427; LYS-498; LYS-506; LYS-531 AND LYS-539, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	305 – 305	1	N6-acetyllysine; alternateCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.8 "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways." Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W. Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-123; LYS-126; LYS-132; LYS-161; LYS-167; LYS-230; LYS-239; LYS-240; LYS-261; LYS-305; LYS-427; LYS-434; LYS-498; LYS-506; LYS-531; LYS-539 AND LYS-541, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	305 – 305	1	N6-succinyllysine; alternateCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.7 "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways." Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y. Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-498; LYS-531 AND LYS-539, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-161; LYS-167; LYS-230; LYS-239; LYS-261; LYS-305; LYS-427; LYS-498; LYS-506; LYS-531 AND LYS-539, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	427 – 427	1	N6-acetyllysine; alternateCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.8 "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways." Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W. Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-123; LYS-126; LYS-132; LYS-161; LYS-167; LYS-230; LYS-239; LYS-240; LYS-261; LYS-305; LYS-427; LYS-434; LYS-498; LYS-506; LYS-531; LYS-539 AND LYS-541, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	427 – 427	1	N6-succinyllysine; alternateCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.7 "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways." Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y. Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-498; LYS-531 AND LYS-539, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-161; LYS-167; LYS-230; LYS-239; LYS-261; LYS-305; LYS-427; LYS-498; LYS-506; LYS-531 AND LYS-539, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	434 – 434	1	N6-acetyllysineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.8 "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways." Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W. Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-123; LYS-126; LYS-132; LYS-161; LYS-167; LYS-230; LYS-239; LYS-240; LYS-261; LYS-305; LYS-427; LYS-434; LYS-498; LYS-506; LYS-531; LYS-539 AND LYS-541, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	498 – 498	1	N6-acetyllysine; alternateCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.7 "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways." Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y. Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-498; LYS-531 AND LYS-539, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-161; LYS-167; LYS-230; LYS-239; LYS-261; LYS-305; LYS-427; LYS-498; LYS-506; LYS-531 AND LYS-539, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.8 "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways." Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W. Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-123; LYS-126; LYS-132; LYS-161; LYS-167; LYS-230; LYS-239; LYS-240; LYS-261; LYS-305; LYS-427; LYS-434; LYS-498; LYS-506; LYS-531; LYS-539 AND LYS-541, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	498 – 498	1	N6-succinyllysine; alternateCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.7 "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways." Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y. Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-498; LYS-531 AND LYS-539, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-161; LYS-167; LYS-230; LYS-239; LYS-261; LYS-305; LYS-427; LYS-498; LYS-506; LYS-531 AND LYS-539, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	506 – 506	1	N6-acetyllysine; alternateCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.8 "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways." Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W. Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-123; LYS-126; LYS-132; LYS-161; LYS-167; LYS-230; LYS-239; LYS-240; LYS-261; LYS-305; LYS-427; LYS-434; LYS-498; LYS-506; LYS-531; LYS-539 AND LYS-541, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	506 – 506	1	N6-succinyllysine; alternateCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.7 "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways." Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y. Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-498; LYS-531 AND LYS-539, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-161; LYS-167; LYS-230; LYS-239; LYS-261; LYS-305; LYS-427; LYS-498; LYS-506; LYS-531 AND LYS-539, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	521 – 521	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.6 "A tissue-specific atlas of mouse protein phosphorylation and expression." Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P. Cell 143:1174-1189(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53; SER-106 AND SER-521, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	531 – 531	1	N6-acetyllysine; alternateCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.7 "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways." Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y. Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-498; LYS-531 AND LYS-539, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-161; LYS-167; LYS-230; LYS-239; LYS-261; LYS-305; LYS-427; LYS-498; LYS-506; LYS-531 AND LYS-539, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.8 "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways." Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W. Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-123; LYS-126; LYS-132; LYS-161; LYS-167; LYS-230; LYS-239; LYS-240; LYS-261; LYS-305; LYS-427; LYS-434; LYS-498; LYS-506; LYS-531; LYS-539 AND LYS-541, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	531 – 531	1	N6-succinyllysine; alternateCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.7 "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways." Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y. Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-498; LYS-531 AND LYS-539, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-161; LYS-167; LYS-230; LYS-239; LYS-261; LYS-305; LYS-427; LYS-498; LYS-506; LYS-531 AND LYS-539, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	539 – 539	1	N6-acetyllysine; alternateCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.7 "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways." Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y. Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-498; LYS-531 AND LYS-539, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-161; LYS-167; LYS-230; LYS-239; LYS-261; LYS-305; LYS-427; LYS-498; LYS-506; LYS-531 AND LYS-539, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.8 "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways." Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W. Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-123; LYS-126; LYS-132; LYS-161; LYS-167; LYS-230; LYS-239; LYS-240; LYS-261; LYS-305; LYS-427; LYS-434; LYS-498; LYS-506; LYS-531; LYS-539 AND LYS-541, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	539 – 539	1	N6-succinyllysine; alternateCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.7 "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways." Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y. Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-498; LYS-531 AND LYS-539, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-161; LYS-167; LYS-230; LYS-239; LYS-261; LYS-305; LYS-427; LYS-498; LYS-506; LYS-531 AND LYS-539, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	541 – 541	1	N6-acetyllysineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.8 "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways." Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W. Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-123; LYS-126; LYS-132; LYS-161; LYS-167; LYS-230; LYS-239; LYS-240; LYS-261; LYS-305; LYS-427; LYS-434; LYS-498; LYS-506; LYS-531; LYS-539 AND LYS-541, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Post-translational modificationⁱ

Acetylation of Lys-132, Lys-230 and Lys-498 is observed in liver mitochondria from fasted mice but not from fed mice.

Acetylated on lysine residues. BLOC1S1 is required for acetylation (By similarity).By similarity

Keywords - PTMⁱ

Acetylation, Glycoprotein, Phosphoprotein, Pyrrolidone carboxylic acid

Proteomic databases

EPDⁱ	Q03265.
MaxQBⁱ	Q03265.
PaxDbⁱ	Q03265.
PeptideAtlasⁱ	Q03265.
PRIDEⁱ	Q03265.

2D gel databases

REPRODUCTION-2DPAGE	IPI00130280. Q03265.
SWISS-2DPAGE	Q03265.
UCD-2DPAGE	Q03265.

PTM databases

iPTMnetⁱ	Q03265.
PhosphoSiteⁱ	Q03265.
SwissPalmⁱ	Q03265.

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSMUSG00000025428.
ExpressionAtlasⁱ	Q03265. baseline and differential.
Genevisibleⁱ	Q03265. MM.

Interactionⁱ

Subunit structureⁱ

F-type ATPases have 2 components, CF₁ - the catalytic core - and CF₀ - the membrane proton channel. CF₁ has five subunits: alpha₃, beta₃, gamma₁, delta₁, epsilon₁. CF₀ has three main subunits: a, b and c. Interacts with ATPAF2. Interacts with HRG; the interaction occurs on the surface of T-cells and alters the cell morphology when associated with concanavalin (in vitro). Interacts with PLG (angiostatin peptide); the interaction inhibits most of the angiogenic properties of angiostatin. Component of an ATP synthase complex composed of ATP5F1, ATP5G1, ATP5E, ATP5H, ATP5I, ATP5J, ATP5J2, MT-ATP6, MT-ATP8, ATP5A1, ATP5B, ATP5D, ATP5C1, ATP5O, ATP5L, USMG5 and MP68. Interacts with BLOC1S1. Interacts with BCL2L1 isoform BCL-X(L); the interaction mediates the association of BCL2L1 isoform BCL-X(L) with the mitochondrial membrane F₁F₀ ATP synthase and enhances neurons metabolic efficency (By similarity).By similarity

GO - Molecular functionⁱ

MHC class I protein binding Source: MGI

Protein-protein interaction databases

BioGridⁱ	198253. 22 interactions.
IntActⁱ	Q03265. 32 interactions.
MINTⁱ	MINT-1859704.
STRINGⁱ	10090.ENSMUSP00000026495.

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	Q03265.
SMRⁱ	Q03265. Positions 56-552.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the ATPase alpha/beta chains family.Curated

Keywords - Domainⁱ

Transit peptide

Phylogenomic databases

eggNOGⁱ	KOG1353. Eukaryota. COG0056. LUCA.
GeneTreeⁱ	ENSGT00550000074846.
HOVERGENⁱ	HBG001536.
InParanoidⁱ	Q03265.
KOⁱ	K02132.
OMAⁱ	MVQDIRR.
OrthoDBⁱ	EOG091G0D1M.
PhylomeDBⁱ	Q03265.
TreeFamⁱ	TF300321.

Family and domain databases

CDDⁱ	cd01132. F1_ATPase_alpha. 1 hit.
Gene3Dⁱ	2.40.30.20. 1 hit. 3.40.50.300. 1 hit.
HAMAPⁱ	MF_01346. ATP_synth_alpha_bact. 1 hit.
InterProⁱ	IPR020003. ATPase_a/bsu_AS. IPR023366. ATPase_asu-like. IPR005294. ATPase_F1-cplx_asu. IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C. IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd. IPR004100. ATPase_F1_a/bsu_N. IPR033732. F1_ATPase_alpha. IPR027417. P-loop_NTPase. [Graphical view]
PANTHERⁱ	PTHR15184:SF3. PTHR15184:SF3. 1 hit.
Pfamⁱ	PF00006. ATP-synt_ab. 1 hit. PF00306. ATP-synt_ab_C. 1 hit. PF02874. ATP-synt_ab_N. 1 hit. [Graphical view]
PIRSFⁱ	PIRSF039088. F_ATPase_subunit_alpha. 1 hit.
SUPFAMⁱ	SSF47917. SSF47917. 1 hit. SSF50615. SSF50615. 1 hit. SSF52540. SSF52540. 1 hit.
TIGRFAMsⁱ	TIGR00962. atpA. 1 hit.
PROSITEⁱ	PS00152. ATPASE_ALPHA_BETA. 1 hit. [Graphical view]

Sequenceⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

Q03265-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MLSVRVAAAV ARALPRRAGL VSKNALGSSF VGARNLHASN TRLQKTGTAE 
        60         70         80         90        100
MSSILEERIL GADTSVDLEE TGRVLSIGDG IARVHGLRNV QAEEMVEFSS 
       110        120        130        140        150
GLKGMSLNLE PDNVGVVVFG NDKLIKEGDV VKRTGAIVDV PVGEELLGRV 
       160        170        180        190        200
VDALGNAIDG KGPIGSKTRR RVGLKAPGII PRISVREPMQ TGIKAVDSLV 
       210        220        230        240        250
PIGRGQRELI IGDRQTGKTS IAIDTIINQK RFNDGTDEKK KLYCIYVAIG 
       260        270        280        290        300
QKRSTVAQLV KRLTDADAMK YTIVVSATAS DAAPLQYLAP YSGCSMGEYF 
       310        320        330        340        350
RDNGKHALII YDDLSKQAVA YRQMSLLLRR PPGREAYPGD VFYLHSRLLE 
       360        370        380        390        400
RAAKMNDSFG GGSLTALPVI ETQAGDVSAY IPTNVISITD GQIFLETELF 
       410        420        430        440        450
YKGIRPAINV GLSVSRVGSA AQTRAMKQVA GTMKLELAQY REVAAFAQFG 
       460        470        480        490        500
SDLDAATQQL LSRGVRLTEL LKQGQYSPMA IEEQVAVIYA GVRGYLDKLE 
       510        520        530        540        550
PSKITKFENA FLSHVISQHQ SLLGNIRSDG KISEQSDAKL KEIVTNFLAG 

FEP

Length:553

Mass (Da):59,753

Last modified:October 1, 1993 - v1

Checksum:ⁱCF35B4FBA7ED431D

GO

Experimental Info

Feature key	Position(s)	Length	Description	Actions
Sequence conflictⁱ	3 – 3	1	S → T in BAE37632 (PubMed:16141072).Curated
Sequence conflictⁱ	63 – 63	1	D → Y in BAE34114 (PubMed:16141072).Curated
Sequence conflictⁱ	119 – 119	1	F → L in BAE34114 (PubMed:16141072).Curated
Sequence conflictⁱ	126 – 126	1	K → N in BAE34114 (PubMed:16141072).Curated
Sequence conflictⁱ	315 – 315	1	S → Y in BAE34114 (PubMed:16141072).Curated
Sequence conflictⁱ	321 – 321	1	Y → C in BAE40868 (PubMed:16141072).Curated
Sequence conflictⁱ	422 – 456	35	Missing in BAE27439 (PubMed:16141072).Curated	Add BLAST
Sequence conflictⁱ	486 – 486	1	A → T in BAE40158 (PubMed:16141072).Curated

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	L01062 mRNA. Translation: AAA37271.1. AK043976 mRNA. Translation: BAC31722.1. AK076572 mRNA. Translation: BAC36399.1. AK146797 mRNA. Translation: BAE27439.1. AK150426 mRNA. Translation: BAE29549.1. AK150843 mRNA. Translation: BAE29901.1. AK151004 mRNA. Translation: BAE30027.1. AK151128 mRNA. Translation: BAE30136.1. AK151224 mRNA. Translation: BAE30216.1. AK151920 mRNA. Translation: BAE30798.1. AK152054 mRNA. Translation: BAE30910.1. AK152890 mRNA. Translation: BAE31573.1. AK157529 mRNA. Translation: BAE34114.1. AK159540 mRNA. Translation: BAE35167.1. AK159491 mRNA. Translation: BAE35125.1. AK159758 mRNA. Translation: BAE35349.1. AK160043 mRNA. Translation: BAE35585.1. AK164110 mRNA. Translation: BAE37632.1. AK164193 mRNA. Translation: BAE37675.1. AK166709 mRNA. Translation: BAE38962.1. AK166812 mRNA. Translation: BAE39039.1. AK167159 mRNA. Translation: BAE39300.1. AK167863 mRNA. Translation: BAE39881.1. AK168198 mRNA. Translation: BAE40158.1. AK168617 mRNA. Translation: BAE40482.1. AK168879 mRNA. Translation: BAE40697.1. AK168890 mRNA. Translation: BAE40707.1. AK168932 mRNA. Translation: BAE40744.1. AK169080 mRNA. Translation: BAE40864.1. AK169084 mRNA. Translation: BAE40868.1. AK169105 mRNA. Translation: BAE40887.1. AK169142 mRNA. Translation: BAE40921.1. AK169300 mRNA. Translation: BAE41056.1. AK169308 mRNA. Translation: BAE41063.1. AK169414 mRNA. Translation: BAE41160.1. BC014854 mRNA. Translation: AAH14854.1.
CCDSⁱ	CCDS29358.1.
PIRⁱ	JC1473.
RefSeqⁱ	NP_031531.1. NM_007505.2.
UniGeneⁱ	Mm.276137.

Genome annotation databases

Ensemblⁱ	ENSMUST00000026495; ENSMUSP00000026495; ENSMUSG00000025428.
GeneIDⁱ	11946.
KEGGⁱ	mmu:11946.
UCSCⁱ	uc008fru.1. mouse.

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	L01062 mRNA. Translation: AAA37271.1. AK043976 mRNA. Translation: BAC31722.1. AK076572 mRNA. Translation: BAC36399.1. AK146797 mRNA. Translation: BAE27439.1. AK150426 mRNA. Translation: BAE29549.1. AK150843 mRNA. Translation: BAE29901.1. AK151004 mRNA. Translation: BAE30027.1. AK151128 mRNA. Translation: BAE30136.1. AK151224 mRNA. Translation: BAE30216.1. AK151920 mRNA. Translation: BAE30798.1. AK152054 mRNA. Translation: BAE30910.1. AK152890 mRNA. Translation: BAE31573.1. AK157529 mRNA. Translation: BAE34114.1. AK159540 mRNA. Translation: BAE35167.1. AK159491 mRNA. Translation: BAE35125.1. AK159758 mRNA. Translation: BAE35349.1. AK160043 mRNA. Translation: BAE35585.1. AK164110 mRNA. Translation: BAE37632.1. AK164193 mRNA. Translation: BAE37675.1. AK166709 mRNA. Translation: BAE38962.1. AK166812 mRNA. Translation: BAE39039.1. AK167159 mRNA. Translation: BAE39300.1. AK167863 mRNA. Translation: BAE39881.1. AK168198 mRNA. Translation: BAE40158.1. AK168617 mRNA. Translation: BAE40482.1. AK168879 mRNA. Translation: BAE40697.1. AK168890 mRNA. Translation: BAE40707.1. AK168932 mRNA. Translation: BAE40744.1. AK169080 mRNA. Translation: BAE40864.1. AK169084 mRNA. Translation: BAE40868.1. AK169105 mRNA. Translation: BAE40887.1. AK169142 mRNA. Translation: BAE40921.1. AK169300 mRNA. Translation: BAE41056.1. AK169308 mRNA. Translation: BAE41063.1. AK169414 mRNA. Translation: BAE41160.1. BC014854 mRNA. Translation: AAH14854.1.
CCDSⁱ	CCDS29358.1.
PIRⁱ	JC1473.
RefSeqⁱ	NP_031531.1. NM_007505.2.
UniGeneⁱ	Mm.276137.

3D structure databases

ProteinModelPortalⁱ	Q03265.
SMRⁱ	Q03265. Positions 56-552.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	198253. 22 interactions.
IntActⁱ	Q03265. 32 interactions.
MINTⁱ	MINT-1859704.
STRINGⁱ	10090.ENSMUSP00000026495.

PTM databases

iPTMnetⁱ	Q03265.
PhosphoSiteⁱ	Q03265.
SwissPalmⁱ	Q03265.

2D gel databases

REPRODUCTION-2DPAGE	IPI00130280. Q03265.
SWISS-2DPAGE	Q03265.
UCD-2DPAGE	Q03265.

Proteomic databases

EPDⁱ	Q03265.
MaxQBⁱ	Q03265.
PaxDbⁱ	Q03265.
PeptideAtlasⁱ	Q03265.
PRIDEⁱ	Q03265.

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

Ensemblⁱ	ENSMUST00000026495; ENSMUSP00000026495; ENSMUSG00000025428.
GeneIDⁱ	11946.
KEGGⁱ	mmu:11946.
UCSCⁱ	uc008fru.1. mouse.

Organism-specific databases

CTDⁱ	498.
MGIⁱ	MGI:88115. Atp5a1.

Phylogenomic databases

eggNOGⁱ	KOG1353. Eukaryota. COG0056. LUCA.
GeneTreeⁱ	ENSGT00550000074846.
HOVERGENⁱ	HBG001536.
InParanoidⁱ	Q03265.
KOⁱ	K02132.
OMAⁱ	MVQDIRR.
OrthoDBⁱ	EOG091G0D1M.
PhylomeDBⁱ	Q03265.
TreeFamⁱ	TF300321.

Enzyme and pathway databases

Reactomeⁱ	R-MMU-163210. Formation of ATP by chemiosmotic coupling.

Reactomeⁱ

R-MMU-163210. Formation of ATP by chemiosmotic coupling.

Miscellaneous databases

ChiTaRSⁱ	Atp5a1. mouse.
PROⁱ	Q03265.
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSMUSG00000025428.
ExpressionAtlasⁱ	Q03265. baseline and differential.
Genevisibleⁱ	Q03265. MM.

Family and domain databases

CDDⁱ	cd01132. F1_ATPase_alpha. 1 hit.
Gene3Dⁱ	2.40.30.20. 1 hit. 3.40.50.300. 1 hit.
HAMAPⁱ	MF_01346. ATP_synth_alpha_bact. 1 hit.
InterProⁱ	IPR020003. ATPase_a/bsu_AS. IPR023366. ATPase_asu-like. IPR005294. ATPase_F1-cplx_asu. IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C. IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd. IPR004100. ATPase_F1_a/bsu_N. IPR033732. F1_ATPase_alpha. IPR027417. P-loop_NTPase. [Graphical view]
PANTHERⁱ	PTHR15184:SF3. PTHR15184:SF3. 1 hit.
Pfamⁱ	PF00006. ATP-synt_ab. 1 hit. PF00306. ATP-synt_ab_C. 1 hit. PF02874. ATP-synt_ab_N. 1 hit. [Graphical view]
PIRSFⁱ	PIRSF039088. F_ATPase_subunit_alpha. 1 hit.
SUPFAMⁱ	SSF47917. SSF47917. 1 hit. SSF50615. SSF50615. 1 hit. SSF52540. SSF52540. 1 hit.
TIGRFAMsⁱ	TIGR00962. atpA. 1 hit.
PROSITEⁱ	PS00152. ATPASE_ALPHA_BETA. 1 hit. [Graphical view]
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ

ATPA_MOUSE

Accessionⁱ

Primary (citable) accession number: Q03265
Secondary accession number(s): Q3TFN0

Q543Y6

Entry historyⁱ

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	September 7, 2016
This is version 170 of the entry and version 1 of the sequence. [Complete history]

Entry statusⁱ

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

Complete proteome, Direct protein sequencing, Reference proteome

Documents

MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
SIMILARITY comments
Index of protein domains and families

Similar proteinsⁱ

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:

100%	UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%	UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%	UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q03265 (ATPA_MOUSE)

UniProt

Q03265 - ATPA_MOUSE

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ATP synthase subunit alpha, mitochondrial

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<p>Provides any useful information about the protein, mostly biological knowledge.</p><p><a href='../manual/function_section' target='_top'>More...</a></p>Functioni

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Enzyme and pathway databases

<p>Provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.</p><p><a href='../manual/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>Provides information on the location and the topology of the mature protein in the cell.</p><p><a href='../manual/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Cellular componenti

<p>Describes post-translational modifications (PTMs) and/or processing events.</p><p><a href='../manual/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Proteomic databases

2D gel databases

PTM databases

<p>Provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.</p><p><a href='../manual/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

<p>Provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.</p><p><a href='../manual/interaction_section' target='_top'>More...</a></p>Interactioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Protein-protein interaction databases

<p>Provides information on the tertiary and secondary structure of a protein.</p><p><a href='../manual/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>Provides information on sequence similarities with other proteins and the domain(s) present in a protein.</p><p><a href='../manual/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>Provides information about the sequence similarity with other proteins.</p><p><a href='../manual/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>Displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including length and molecular weight.</p><p><a href='../manual/sequences_section' target='_top'>More...</a></p>Sequencei

Experimental Info

Sequence databases

Genome annotation databases

<p>Is used to point to information related to entries and found in data collections other than UniProtKB.</p><p><a href='../manual/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>Provides general information on the entry.</p><p><a href='../manual/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>Contains any relevant information that doesn’t fit in any other defined sections</p><p><a href='../manual/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequenceⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ