P25705 (ATPA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP synthase subunit alpha, mitochondrial

Gene names

Name:	ATP5A1
Synonyms:	ATP5A, ATP5AL2, ATPM

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	553 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.12 Ref.14
Subunit structure	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 By similarity. Interacts with BLOC1S1. Ref.12 Ref.13 Ref.14 Ref.18
Subcellular location	Mitochondrion inner membrane. Cell membrane; Peripheral membrane protein; Extracellular side. Note: Colocalizes with HRG on the cell surface of T-cells. Ref.12 Ref.14
Tissue specificity	Fetal lung, heart, liver, gut and kidney. Expressed at higher levels in the fetal brain, retina and spinal cord. Ref.2
Post-translational modification	The N-terminus is blocked. Acetylated on lysine residues. BLOC1S1 is required for acetylation.
Sequence similarities	Belongs to the ATPase alpha/beta chains family.

Ontologies

Keywords
Biological process	ATP synthesis Hydrogen ion transport Ion transport Transport
Cellular component	CF(1) Cell membrane Membrane Mitochondrion Mitochondrion inner membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Transit peptide
Ligand	ATP-binding Nucleotide-binding
PTM	Acetylation Phosphoprotein Pyrrolidone carboxylic acid
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	ATP hydrolysis coupled proton transport Inferred from electronic annotation. Source: InterPro embryo development Inferred from sequence or structural similarity. Source: UniProtKB lipid metabolic process Inferred from sequence or structural similarity. Source: UniProtKB mitochondrial ATP synthesis coupled proton transport Inferred by curator PubMed 12110673. Source: UniProtKB negative regulation of endothelial cell proliferation Inferred from mutant phenotype Ref.12. Source: UniProtKB respiratory electron transport chain Traceable author statement. Source: Reactome
Cellular_component	mitochondrial matrix Traceable author statement. Source: Reactome mitochondrial proton-transporting ATP synthase complex Inferred from direct assay PubMed 12110673. Source: UniProtKB plasma membrane Inferred from direct assay Ref.12. Source: UniProtKB proton-transporting ATP synthase complex, catalytic core F(1) Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ATP binding Inferred from sequence or structural similarity. Source: UniProtKB MHC class I protein binding Inferred from direct assay PubMed 17643490. Source: UniProtKB eukaryotic cell surface binding Inferred from direct assay Ref.12. Source: UniProtKB proton-transporting ATP synthase activity, rotational mechanism Inferred from sequence or structural similarity. Source: UniProtKB proton-transporting ATPase activity, rotational mechanism Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BLOC1S1	P78537	2	EBI-351437,EBI-348630
SIRT3	Q9NTG7	2	EBI-351437,EBI-724621

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P25705-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P25705-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-50: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 43	43	Mitochondrion Ref.8
	Chain	44 – 553	510	ATP synthase subunit alpha, mitochondrial		PRO_0000002424
Regions
	Nucleotide binding	212 – 219	8	ATP By similarity
Sites
	Site	413	1	Required for activity By similarity
Amino acid modifications
	Modified residue	44	1	Pyrrolidone carboxylic acid By similarity
	Modified residue	76	1	Phosphoserine By similarity
	Modified residue	132	1	N6-acetyllysine By similarity
	Modified residue	161	1	N6-acetyllysine Ref.15
	Modified residue	166	1	Phosphoserine Ref.17
	Modified residue	230	1	N6-acetyllysine By similarity
	Modified residue	239	1	N6-acetyllysine By similarity
	Modified residue	261	1	N6-acetyllysine Ref.15
	Modified residue	305	1	N6-acetyllysine
	Modified residue	427	1	N6-acetyllysine By similarity
	Modified residue	434	1	N6-acetyllysine Ref.15
	Modified residue	498	1	N6-acetyllysine Ref.15
	Modified residue	506	1	N6-acetyllysine Ref.15
	Modified residue	531	1	N6-acetyllysine By similarity
	Modified residue	539	1	N6-acetyllysine Ref.15
Natural variations
	Alternative sequence	1 – 50	50	Missing in isoform 2.		VSP_045129
	Natural variant	32	1	A → S. Corresponds to variant rs2228437 [ dbSNP | Ensembl ].		VAR_048369
	Natural variant	223	1	I → V. Corresponds to variant rs2228436 [ dbSNP | Ensembl ].		VAR_048370
Experimental info
	Sequence conflict	329	1	R → L in AAH39135. Ref.5
	Sequence conflict	510	1	A → D in AAH11384. Ref.5
	Sequence conflict	529	1	D → E in AAH11384. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 1992. Version 1. Checksum: AA47BBB8EDA77EAC	FASTA	553	59,751
	10 20 30 40 50 60 MLSVRVAAAV VRALPRRAGL VSRNALGSSF IAARNFHASN THLQKTGTAE MSSILEERIL 70 80 90 100 110 120 GADTSVDLEE TGRVLSIGDG IARVHGLRNV QAEEMVEFSS GLKGMSLNLE PDNVGVVVFG 130 140 150 160 170 180 NDKLIKEGDI VKRTGAIVDV PVGEELLGRV VDALGNAIDG KGPIGSKTRR RVGLKAPGII 190 200 210 220 230 240 PRISVREPMQ TGIKAVDSLV PIGRGQRELI IGDRQTGKTS IAIDTIINQK RFNDGSDEKK 250 260 270 280 290 300 KLYCIYVAIG QKRSTVAQLV KRLTDADAMK YTIVVSATAS DAAPLQYLAP YSGCSMGEYF 310 320 330 340 350 360 RDNGKHALII YDDLSKQAVA YRQMSLLLRR PPGREAYPGD VFYLHSRLLE RAAKMNDAFG 370 380 390 400 410 420 GGSLTALPVI ETQAGDVSAY IPTNVISITD GQIFLETELF YKGIRPAINV GLSVSRVGSA 430 440 450 460 470 480 AQTRAMKQVA GTMKLELAQY REVAAFAQFG SDLDAATQQL LSRGVRLTEL LKQGQYSPMA 490 500 510 520 530 540 IEEQVAVIYA GVRGYLDKLE PSKITKFENA FLSHVVSQHQ ALLGTIRADG KISEQSDAKL 550 KEIVTNFLAG FEA
	Isoform 2 [UniParc]. Checksum: 03AE2040A4C147EA	FASTA	503	54,494
	10 20 30 40 50 60 MSSILEERIL GADTSVDLEE TGRVLSIGDG IARVHGLRNV QAEEMVEFSS GLKGMSLNLE 70 80 90 100 110 120 PDNVGVVVFG NDKLIKEGDI VKRTGAIVDV PVGEELLGRV VDALGNAIDG KGPIGSKTRR 130 140 150 160 170 180 RVGLKAPGII PRISVREPMQ TGIKAVDSLV PIGRGQRELI IGDRQTGKTS IAIDTIINQK 190 200 210 220 230 240 RFNDGSDEKK KLYCIYVAIG QKRSTVAQLV KRLTDADAMK YTIVVSATAS DAAPLQYLAP 250 260 270 280 290 300 YSGCSMGEYF RDNGKHALII YDDLSKQAVA YRQMSLLLRR PPGREAYPGD VFYLHSRLLE 310 320 330 340 350 360 RAAKMNDAFG GGSLTALPVI ETQAGDVSAY IPTNVISITD GQIFLETELF YKGIRPAINV 370 380 390 400 410 420 GLSVSRVGSA AQTRAMKQVA GTMKLELAQY REVAAFAQFG SDLDAATQQL LSRGVRLTEL 430 440 450 460 470 480 LKQGQYSPMA IEEQVAVIYA GVRGYLDKLE PSKITKFENA FLSHVVSQHQ ALLGTIRADG 490 500 KISEQSDAKL KEIVTNFLAG FEA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of a cDNA for the alpha subunit of human mitochondrial ATP synthase." Kataoka H., Biswas C. Biochim. Biophys. Acta 1089:393-395(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Lung tumor.
[2]	"Amplification of the gene encoding the alpha-subunit of the mitochondrial ATP synthase complex in a human retinoblastoma cell line." Godbout R., Bisgrove D.A., Honore L.H., Day R.S. III Gene 123:195-201(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY. Tissue: Retinoblastoma.
[3]	"Gene structure and cell type-specific expression of the human ATP synthase alpha subunit." Akiyama S., Endo H., Inohara N., Ohta S., Kagawa Y. Biochim. Biophys. Acta 1219:129-140(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1). Tissue: Colon tumor.
[4]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Small intestine.
[6]	"DNA sequence and analysis of human chromosome 18." Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J. , Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K., Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R., Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S. Nature 437:551-555(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Lung, Retina and Uterus.
[8]	"Global profiling of protease cleavage sites by chemoselective labeling of protein N-termini." Xu G., Shin S.B., Jaffrey S.R. Proc. Natl. Acad. Sci. U.S.A. 106:19310-19315(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 44-59. Tissue: Leukemic T-cell.
[9]	Lubec G., Vishwanath V., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 46-83; 89-103; 134-161; 176-182; 219-230; 242-252; 306-316; 335-347; 403-416; 435-463 AND 507-527, MASS SPECTROMETRY. Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[10]	Bienvenut W.V. Submitted (MAR-2005) to UniProtKB Cited for: PROTEIN SEQUENCE OF 46-73; 104-123; 134-161; 219-230; 232-239; 306-316; 335-347; 403-416; 442-463 AND 507-527, MASS SPECTROMETRY. Tissue: B-cell lymphoma.
[11]	"The major protein expression profile and two-dimensional protein database of human heart." Kovalyov L.I., Shishkin S.S., Efimochkin A.S., Kovalyova M.A., Ershova E.S., Egorov T.A., Musalyamov A.K. Electrophoresis 16:1160-1169(1995) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 134-141 AND 335-339. Tissue: Heart.
[12]	"Angiostatin binds ATP synthase on the surface of human endothelial cells." Moser T.L., Stack M.S., Asplin I., Enghild J.J., Hojrup P., Everitt L., Hubchak S., Schnaper H.W., Pizzo S.V. Proc. Natl. Acad. Sci. U.S.A. 96:2811-2816(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PLG, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, FUNCTION.
[13]	"Atp11p and Atp12p are assembly factors for the F(1)-ATPase in human mitochondria." Wang Z.-G., White P.S., Ackerman S.H. J. Biol. Chem. 276:30773-30778(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ATPAF2.
[14]	"High affinity interaction between histidine-rich glycoprotein and the cell surface type ATP synthase on T-cells." Ohta T., Ikemoto Y., Usami A., Koide T., Wakabayashi S. Biochim. Biophys. Acta 1788:1099-1107(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HRG, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, FUNCTION.
[15]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-161; LYS-261; LYS-434; LYS-498; LYS-506 AND LYS-539, MASS SPECTROMETRY.
[16]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166, MASS SPECTROMETRY.
[18]	"Identification of a molecular component of the mitochondrial acetyl transferase program; a novel role for GCN5L1." Scott I., Webster B.R., Li J.H., Sack M.N. Biochem. J. 443:655-661(2012) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH BLOC1S1, ACETYLATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X59066 mRNA. Translation: CAA41789.1. X65460 mRNA. Translation: CAA46452.1. D14710 mRNA. Translation: BAA03531.1. D28126 Genomic DNA. Translation: BAA05672.1. BT007209 mRNA. Translation: AAP35873.1. AK092735 mRNA. Translation: BAG52604.1. AK289457 mRNA. Translation: BAF82146.1. AC012569 Genomic DNA. No translation available. BC003119 mRNA. Translation: AAH03119.1. BC007299 mRNA. Translation: AAH07299.1. BC008028 mRNA. Translation: AAH08028.2. BC011384 mRNA. Translation: AAH11384.1. BC016046 mRNA. Translation: AAH16046.1. BC019310 mRNA. Translation: AAH19310.1. BC039135 mRNA. Translation: AAH39135.2. BC064562 mRNA. Translation: AAH64562.1. BC067385 mRNA. Translation: AAH67385.1.
IPI	IPI00440493.
PIR	PWHUA. S17193.
RefSeq	NP_001001935.1. NM_001001935.2. NP_001001937.1. NM_001001937.1. NP_001244263.1. NM_001257334.1. NP_001244264.1. NM_001257335.1. NP_004037.1. NM_004046.5.
UniGene	Hs.298280.
3D structure databases
ProteinModelPortal	P25705.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-32871N.
IntAct	P25705. 25 interactions.
MINT	MINT-1163289.
STRING	9606.ENSP00000282050.
PTM databases
PhosphoSite	P25705.
Polymorphism databases
DMDM	114517.
2D gel databases
OGP	P25705.
REPRODUCTION-2DPAGE	P25705.
UCD-2DPAGE	P25705.
Proteomic databases
PaxDb	P25705.
PRIDE	P25705.
Protocols and materials databases
DNASU	498.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000282050; ENSP00000282050; ENSG00000152234. ENST00000398752; ENSP00000381736; ENSG00000152234. ENST00000586592; ENSP00000466275; ENSG00000152234.
GeneID	498.
KEGG	hsa:498.
UCSC	uc002lbr.1. human.
Organism-specific databases
CTD	498.
GeneCards	GC18M043664.
HGNC	HGNC:823. ATP5A1.
HPA	CAB013067.
MIM	164360. gene.
neXtProt	NX_P25705.
PharmGKB	PA25115.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0056.
HOVERGEN	HBG001536.
InParanoid	P25705.
KO	K02132.
OMA	DSGRHAL.
OrthoDB	EOG4ZCT48.
PhylomeDB	P25705.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism. REACT_17015. Metabolism of proteins.
Gene expression databases
ArrayExpress	P25705.
Bgee	P25705.
CleanEx	HS_ATP5A1.
Genevestigator	P25705.
GermOnline	ENSG00000152234. Homo sapiens.
Family and domain databases
Gene3D	2.40.30.20. 1 hit.
InterPro	IPR020003. ATPase_a/bsu_AS. IPR004100. ATPase_a/bsu_N. IPR005294. ATPase_F1-cplx_asu. IPR023366. ATPase_F1/A1-cplx_a_su_N. IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C. IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd. [Graphical view]
Pfam	PF00006. ATP-synt_ab. 1 hit. PF00306. ATP-synt_ab_C. 1 hit. PF02874. ATP-synt_ab_N. 1 hit. [Graphical view]
SUPFAM	SSF47917. ATPase_a/b_C. 1 hit. SSF50615. ATPase_a/b_N. 1 hit.
TIGRFAMs	TIGR00962. atpA. 1 hit.
PROSITE	PS00152. ATPASE_ALPHA_BETA. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ATP5A1. human.
GenomeRNAi	498.
NextBio	2089.
PMAP-CutDB	P25705.
SOURCE	Search...

Entry information

Entry name

ATPA_HUMAN

Accession

Primary (citable) accession number: P25705
Secondary accession number(s): A8K092 , Q53XX6, Q8IXV2, Q96FB4, Q96HW2, Q96IR6, Q9BTV8

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	May 1, 1992
Last modified:	May 1, 2013
This is version 160 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.