HUMAN:ATPA

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	ATP5A1 (synonyms: ATP5A, ATP5AL2, ATPM)
Protein Name(s)	ATP synthase subunit alpha, mitochondrial
External Links
UniProt	P25705
EMBL	X59066 X65460 D14710 D28126 BT007209 AK092735 AK289457 AK302272 AC012569 BC003119 BC007299 BC008028 BC011384 BC016046 BC019310 BC039135 BC064562 BC067385
CCDS	CCDS11927.1 CCDS58620.1 CCDS59315.1
PIR	S17193
RefSeq	NP_001001935.1 NP_001001937.1 NP_001244263.1 NP_001244264.1 NP_004037.1
UniGene	Hs.298280
ProteinModelPortal	P25705
SMR	P25705
BioGrid	106987
DIP	DIP-32871N
IntAct	P25705
MINT	MINT-1163289
STRING	9606.ENSP00000282050
ChEMBL	CHEMBL2062351
PhosphoSite	P25705
DMDM	114517
OGP	P25705
REPRODUCTION-2DPAGE	P25705
UCD-2DPAGE	P25705
MaxQB	P25705
PaxDb	P25705
PRIDE	P25705
DNASU	498
Ensembl	ENST00000282050 ENST00000398752 ENST00000590665 ENST00000593152
GeneID	498
KEGG	hsa:498
UCSC	uc002lbr.2
CTD	498
GeneCards	GC18M043664
HGNC	HGNC:823
HPA	CAB013067
MIM	164360 615228
neXtProt	NX_P25705
Orphanet	254913
PharmGKB	PA25115
eggNOG	COG0056
GeneTree	ENSGT00550000074846
HOVERGEN	HBG001536
InParanoid	P25705
KO	K02132
OMA	LQHIKTS
OrthoDB	EOG773XFP
PhylomeDB	P25705
TreeFam	TF300321
Reactome	REACT_118595 REACT_6759
ChiTaRS	ATP5A1
GenomeRNAi	498
NextBio	2089
PMAP-CutDB	P25705
PRO	PR:P25705
Proteomes	UP000005640
Bgee	P25705
CleanEx	HS_ATP5A1
ExpressionAtlas	P25705
Genevestigator	P25705
GO	GO:0070062 GO:0016020 GO:0005743 GO:0005759 GO:0005753 GO:0005739 GO:0005886 GO:0045261 GO:0005524 GO:0042288 GO:0044822 GO:0046933 GO:0046961 GO:0022857 GO:0006754 GO:0006200 GO:0015991 GO:0044237 GO:0009790 GO:0006629 GO:0042776 GO:0001937 GO:0022904 GO:0044281
Gene3D	2.40.30.20 3.40.50.300
HAMAP	MF_01346
InterPro	IPR020003 IPR023366 IPR005294 IPR000793 IPR000194 IPR004100 IPR027417
Pfam	PF00006 PF00306 PF02874
SUPFAM	SSF47917 SSF50615 SSF52540
TIGRFAMs	TIGR00962
PROSITE	PS00152

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
involved_in	GO:0006754	ATP biosynthetic process	PMID:21106936^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	occurs_in:(CL:0002618) has_direct_input:(UniProtKB:P62328) regulates:(GO:0043534)	Seeded From UniProt	complete
enables	GO:0046933	proton-transporting ATP synthase activity, rotational mechanism	PMID:21106936^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	occurs_in:(CL:0002618) has_direct_input:(UniProtKB:P62328) regulates:(GO:0043534)	Seeded From UniProt	complete
part_of	GO:0045259	proton-transporting ATP synthase complex	PMID:21106936^[1]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0002618)	Seeded From UniProt	complete
involved_in	GO:0043536	positive regulation of blood vessel endothelial cell migration	PMID:21106936^[1]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:P62328	P	regulates_o_results_in_movement_of:(CL:0002618)	Seeded From UniProt	complete
enables	GO:0043532	angiostatin binding	PMID:21106936^[1]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P00747:PRO_0000028057	F		Seeded From UniProt	complete
part_of	GO:0016020	membrane	PMID:21106936^[1]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0002618)	Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:23533145^[2]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0016020	membrane	PMID:19946888^[3]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:19056867^[4]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001088)	Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:20833797^[5]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001134)	Seeded From UniProt	complete
enables	GO:0046933	proton-transporting ATP synthase activity, rotational mechanism	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q03265	F		Seeded From UniProt	complete
enables	GO:0003723	RNA binding	PMID:22658674^[6]	ECO:0007005	high throughput direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0042776	mitochondrial ATP synthesis coupled proton transport	PMID:12110673^[7]	ECO:0000305	curator inference used in manual assertion	GO:0005753	P		Seeded From UniProt	complete
enables	GO:0042288	MHC class I protein binding	PMID:17643490^[8]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0022857	transmembrane transporter activity	PMID:12110673^[7]	ECO:0000305	curator inference used in manual assertion	GO:0005753	F		Seeded From UniProt	complete
contributes_to	GO:0016887	ATPase activity	PMID:12110673^[7]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
colocalizes_with	GO:0008180	COP9 signalosome	PMID:18850735^[9]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0006754	ATP biosynthetic process	PMID:12110673^[7]	ECO:0000305	curator inference used in manual assertion	GO:0016887	P		Seeded From UniProt	complete
involved_in	GO:0006754	ATP biosynthetic process	PMID:1830491^[10]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006629	lipid metabolic process	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q03265	P		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:10077593^[11]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005753	mitochondrial proton-transporting ATP synthase complex	PMID:12110673^[7]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005743	mitochondrial inner membrane	PMID:19016746^[12]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:1830491^[10]	ECO:0000303	author statement without traceable support used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q03265	F		Seeded From UniProt	complete
involved_in	GO:0001937	negative regulation of endothelial cell proliferation	PMID:10077593^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0046933	proton-transporting ATP synthase activity, rotational mechanism	PMID:21873635^[13]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:88115 PANTHER:PTN000389891 UniProtKB:P25705	F		Seeded From UniProt	complete
enables	GO:0046933	proton-transporting ATP synthase activity, rotational mechanism	PMID:21873635^[13]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:88115 PANTHER:PTN000389891 SGD:S000000195 UniProtKB:P25705	F		Seeded From UniProt	complete
enables	GO:0043531	ADP binding	PMID:21873635^[13]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000389891 RGD:619993	F		Seeded From UniProt	complete
contributes_to	GO:0016887	ATPase activity	PMID:21873635^[13]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000389891 RGD:619993 SGD:S000000195 UniProtKB:P25705	F		Seeded From UniProt	complete
involved_in	GO:0015986	ATP synthesis coupled proton transport	PMID:21873635^[13]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10098 PANTHER:PTN000389891 SGD:S000000195	P		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	PMID:21873635^[13]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:88115 PANTHER:PTN000389891 RGD:619993	F		Seeded From UniProt	complete
part_of	GO:0000275	mitochondrial proton-transporting ATP synthase complex, catalytic core F(1)	PMID:21873635^[13]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002875162 RGD:619993	C		Seeded From UniProt	complete
involved_in	GO:0099132	ATP hydrolysis coupled cation transmembrane transport	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0046933	P		Seeded From UniProt	complete
involved_in	GO:0099132	ATP hydrolysis coupled cation transmembrane transport	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0046933	P		Seeded From UniProt	complete
involved_in	GO:0099132	ATP hydrolysis coupled cation transmembrane transport	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0046933	P		Seeded From UniProt	complete
involved_in	GO:0099132	ATP hydrolysis coupled cation transmembrane transport	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0046933	P		Seeded From UniProt	complete
involved_in	GO:0099132	ATP hydrolysis coupled cation transmembrane transport	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0046933	P		Seeded From UniProt	complete
involved_in	GO:0099132	ATP hydrolysis coupled cation transmembrane transport	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0046933	P		Seeded From UniProt	complete
enables	GO:0046933	proton-transporting ATP synthase activity, rotational mechanism	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q03265 ensembl:ENSMUSP00000026495	F		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q03265 ensembl:ENSMUSP00000026495	C		Seeded From UniProt	complete
involved_in	GO:0006629	lipid metabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q03265 ensembl:ENSMUSP00000026495	P		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q03265 ensembl:ENSMUSP00000026495	C		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q03265 ensembl:ENSMUSP00000026495	F		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000194 InterPro:IPR020003	F		Seeded From UniProt	complete
involved_in	GO:0015986	ATP synthesis coupled proton transport	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000793 InterPro:IPR005294	P		Seeded From UniProt	complete
enables	GO:0032559	adenyl ribonucleotide binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR033732	F		Seeded From UniProt	complete
part_of	GO:0045261	proton-transporting ATP synthase complex, catalytic core F(1)	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR005294	C		Seeded From UniProt	complete
involved_in	GO:0046034	ATP metabolic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR004100 InterPro:IPR036121	P		Seeded From UniProt	complete
enables	GO:0046933	proton-transporting ATP synthase activity, rotational mechanism	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR005294	F		Seeded From UniProt	complete
involved_in	GO:1902600	proton transmembrane transport	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR004100 InterPro:IPR036121	P		Seeded From UniProt	complete
involved_in	GO:0042776	mitochondrial ATP synthesis coupled proton transport	Reactome:R-HSA-164834	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0042407	cristae formation	Reactome:R-HSA-8949613	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006754	ATP biosynthetic process	Reactome:R-HSA-164840 Reactome:R-HSA-164832	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005759	mitochondrial matrix	Reactome:R-HSA-8949580 Reactome:R-HSA-164840 Reactome:R-HSA-164834 Reactome:R-HSA-164832	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	F		Seeded From UniProt	complete
part_of	GO:0045261	proton-transporting ATP synthase complex, catalytic core F(1)	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0139	C		Seeded From UniProt	complete
involved_in	GO:0006811	ion transport	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0406	P		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C		Seeded From UniProt	complete
part_of	GO:0005743	mitochondrial inner membrane	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0999 UniProtKB-SubCell:SL-0168	C		Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1003 UniProtKB-SubCell:SL-0039	C		Seeded From UniProt	complete
involved_in	GO:0006754	ATP biosynthetic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0066	P		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0496 UniProtKB-SubCell:SL-0173	C		Seeded From UniProt	complete
edit table

Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 ^1.3 ^1.4 ^1.5 Freeman, KW et al. (2011) Regenerative protein thymosin beta-4 is a novel regulator of purinergic signaling. FASEB J. 25 907-15 PubMed GONUTS page
↑ Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page
↑ Ghosh, D et al. (2010) Defining the membrane proteome of NK cells. J Mass Spectrom 45 1-25 PubMed GONUTS page
↑ Gonzales, PA et al. (2009) Large-scale proteomics and phosphoproteomics of urinary exosomes. J. Am. Soc. Nephrol. 20 363-79 PubMed GONUTS page
↑ Zhao, X et al. (2011) Phosphoproteome analysis of functional mitochondria isolated from resting human muscle reveals extensive phosphorylation of inner membrane protein complexes and enzymes. Mol. Cell Proteomics 10 M110.000299 PubMed GONUTS page
↑ Castello, A et al. (2012) Insights into RNA biology from an atlas of mammalian mRNA-binding proteins. Cell 149 1393-406 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 ^7.3 ^7.4 Aggeler, R et al. (2002) A functionally active human F1F0 ATPase can be purified by immunocapture from heart tissue and fibroblast cell lines. Subunit structure and activity studies. J. Biol. Chem. 277 33906-12 PubMed GONUTS page
↑ Vantourout, P et al. (2008) Ecto-F1-ATPase and MHC-class I close association on cell membranes. Mol. Immunol. 45 485-92 PubMed GONUTS page
↑ Fang, L et al. (2008) Characterization of the human COP9 signalosome complex using affinity purification and mass spectrometry. J. Proteome Res. 7 4914-25 PubMed GONUTS page
↑ ^10.0 ^10.1 Kataoka, H & Biswas, C (1991) Nucleotide sequence of a cDNA for the alpha subunit of human mitochondrial ATP synthase. Biochim. Biophys. Acta 1089 393-5 PubMed GONUTS page
↑ ^11.0 ^11.1 Moser, TL et al. (1999) Angiostatin binds ATP synthase on the surface of human endothelial cells. Proc. Natl. Acad. Sci. U.S.A. 96 2811-6 PubMed GONUTS page
↑ Kim, DW et al. (2008) Identification of mitochondrial F(1)F(0)-ATP synthase interacting with galectin-3 in colon cancer cells. Cancer Sci. 99 1884-91 PubMed GONUTS page
↑ ^13.0 ^13.1 ^13.2 ^13.3 ^13.4 ^13.5 ^13.6 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:21106936-1] 1.0 ^1.1 ^1.2 ^1.3 ^1.4 ^1.5 Freeman, KW et al. (2011) Regenerative protein thymosin beta-4 is a novel regulator of purinergic signaling. FASEB J. 25 907-15 PubMed GONUTS page

[PMID:23533145-2] Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page

[PMID:19946888-3] Ghosh, D et al. (2010) Defining the membrane proteome of NK cells. J Mass Spectrom 45 1-25 PubMed GONUTS page

[PMID:19056867-4] Gonzales, PA et al. (2009) Large-scale proteomics and phosphoproteomics of urinary exosomes. J. Am. Soc. Nephrol. 20 363-79 PubMed GONUTS page

[PMID:20833797-5] Zhao, X et al. (2011) Phosphoproteome analysis of functional mitochondria isolated from resting human muscle reveals extensive phosphorylation of inner membrane protein complexes and enzymes. Mol. Cell Proteomics 10 M110.000299 PubMed GONUTS page

[PMID:22658674-6] Castello, A et al. (2012) Insights into RNA biology from an atlas of mammalian mRNA-binding proteins. Cell 149 1393-406 PubMed GONUTS page

[PMID:12110673-7] 7.0 ^7.1 ^7.2 ^7.3 ^7.4 Aggeler, R et al. (2002) A functionally active human F1F0 ATPase can be purified by immunocapture from heart tissue and fibroblast cell lines. Subunit structure and activity studies. J. Biol. Chem. 277 33906-12 PubMed GONUTS page

[PMID:17643490-8] Vantourout, P et al. (2008) Ecto-F1-ATPase and MHC-class I close association on cell membranes. Mol. Immunol. 45 485-92 PubMed GONUTS page

[PMID:18850735-9] Fang, L et al. (2008) Characterization of the human COP9 signalosome complex using affinity purification and mass spectrometry. J. Proteome Res. 7 4914-25 PubMed GONUTS page

[PMID:1830491-10] 10.0 ^10.1 Kataoka, H & Biswas, C (1991) Nucleotide sequence of a cDNA for the alpha subunit of human mitochondrial ATP synthase. Biochim. Biophys. Acta 1089 393-5 PubMed GONUTS page

[PMID:10077593-11] 11.0 ^11.1 Moser, TL et al. (1999) Angiostatin binds ATP synthase on the surface of human endothelial cells. Proc. Natl. Acad. Sci. U.S.A. 96 2811-6 PubMed GONUTS page

[PMID:19016746-12] Kim, DW et al. (2008) Identification of mitochondrial F(1)F(0)-ATP synthase interacting with galectin-3 in colon cancer cells. Cancer Sci. 99 1884-91 PubMed GONUTS page

[PMID:21873635-13] 13.0 ^13.1 ^13.2 ^13.3 ^13.4 ^13.5 ^13.6 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[1]

[2]

[3]

[4]

[5]

[6]

[7]

[8]

[9]

[10]

[11]

[12]

[13]

HUMAN:ATPA

Contents

Annotations

Notes

References

a

b

c

e

h

l

m

n

o

p

r

t

v

Navigation menu

Personal tools

Namespaces

Variants

Views

More

Search

Navigation

Cacao

Links

Tools