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P25705 (ATPA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 174. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP synthase subunit alpha, mitochondrial
Gene names
Name:ATP5A1
Synonyms:ATP5A, ATP5AL2, ATPM
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length553 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. 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. 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. HAMAP-Rule MF_01346

Acetylated on lysine residues. BLOC1S1 is required for acetylation. Ref.18

Involvement in disease

Mitochondrial complex V deficiency, nuclear 4 (MC5DN4) [MIM:615228]: A mitochondrial disorder with heterogeneous clinical manifestations including dysmorphic features, psychomotor retardation, hypotonia, growth retardation, cardiomyopathy, enlarged liver, hypoplastic kidneys and elevated lactate levels in urine, plasma and cerebrospinal fluid.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.19

Sequence similarities

Belongs to the ATPase alpha/beta chains family.

Ontologies

Keywords
   Biological processATP synthesis
Hydrogen ion transport
Ion transport
Transport
   Cellular componentCell membrane
CF(1)
Membrane
Mitochondrion
Mitochondrion inner membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainTransit peptide
   LigandATP-binding
Nucleotide-binding
   PTMAcetylation
Phosphoprotein
Pyrrolidone carboxylic acid
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processATP biosynthetic process

Non-traceable author statement Ref.1. Source: UniProtKB

ATP catabolic process

Inferred from direct assay PubMed 12110673. Source: GOC

ATP hydrolysis coupled proton transport

Inferred from electronic annotation. Source: InterPro

cellular metabolic process

Traceable author statement. Source: Reactome

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

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentextracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 23376485. Source: UniProt

mitochondrial inner membrane

Inferred from direct assay PubMed 19016746. Source: UniProtKB

mitochondrial matrix

Traceable author statement. Source: Reactome

mitochondrial proton-transporting ATP synthase complex

Inferred from direct assay PubMed 12110673. Source: UniProtKB

mitochondrion

Non-traceable author statement Ref.1. 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_functionATP binding

Inferred from sequence or structural similarity. Source: UniProtKB

MHC class I protein binding

Inferred from direct assay PubMed 17643490. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.13Ref.14. 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

transmembrane transporter activity

Inferred by curator PubMed 12110673. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 3 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.
Isoform 3 (identifier: P25705-3)

The sequence of this isoform differs from the canonical sequence as follows:
     140-161: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4343Mitochondrion Ref.8
Chain44 – 553510ATP synthase subunit alpha, mitochondrial HAMAP-Rule MF_01346
PRO_0000002424

Regions

Nucleotide binding212 – 2198ATP By similarity

Sites

Site4131Required for activity By similarity

Amino acid modifications

Modified residue441Pyrrolidone carboxylic acid By similarity
Modified residue761Phosphoserine By similarity
Modified residue1231N6-acetyllysine By similarity
Modified residue1261N6-acetyllysine By similarity
Modified residue1321N6-acetyllysine By similarity
Modified residue1611N6-acetyllysine; alternate Ref.15
Modified residue1611N6-succinyllysine; alternate By similarity
Modified residue1661Phosphoserine Ref.17
Modified residue1671N6-acetyllysine; alternate By similarity
Modified residue1671N6-succinyllysine; alternate By similarity
Modified residue2301N6-acetyllysine; alternate By similarity
Modified residue2301N6-succinyllysine; alternate By similarity
Modified residue2391N6-acetyllysine; alternate By similarity
Modified residue2391N6-succinyllysine; alternate By similarity
Modified residue2401N6-acetyllysine By similarity
Modified residue2611N6-acetyllysine; alternate Ref.15
Modified residue2611N6-succinyllysine; alternate By similarity
Modified residue3051N6-acetyllysine; alternate By similarity
Modified residue3051N6-succinyllysine; alternate By similarity
Modified residue4271N6-acetyllysine; alternate By similarity
Modified residue4271N6-succinyllysine; alternate By similarity
Modified residue4341N6-acetyllysine Ref.15
Modified residue4981N6-acetyllysine; alternate Ref.15
Modified residue4981N6-succinyllysine; alternate By similarity
Modified residue5061N6-acetyllysine; alternate Ref.15
Modified residue5061N6-succinyllysine; alternate By similarity
Modified residue5311N6-acetyllysine; alternate By similarity
Modified residue5311N6-succinyllysine; alternate By similarity
Modified residue5391N6-acetyllysine; alternate Ref.15
Modified residue5391N6-succinyllysine; alternate By similarity
Modified residue5411N6-acetyllysine By similarity

Natural variations

Alternative sequence1 – 5050Missing in isoform 2.
VSP_045129
Alternative sequence140 – 16122Missing in isoform 3.
VSP_054688
Natural variant321A → S.
Corresponds to variant rs2228437 [ dbSNP | Ensembl ].
VAR_048369
Natural variant2231I → V.
Corresponds to variant rs2228436 [ dbSNP | Ensembl ].
VAR_048370
Natural variant3291R → C in MC5DN4. Ref.19
VAR_069769

Experimental info

Sequence conflict1621G → V in BAG63618. Ref.5
Sequence conflict1831I → T in BAG63618. Ref.5
Sequence conflict3291R → L in AAH39135. Ref.5
Sequence conflict3561N → D in BAG63618. Ref.5
Sequence conflict5101A → D in AAH11384. Ref.5
Sequence conflict5291D → E in AAH11384. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: AA47BBB8EDA77EAC

FASTA55359,751
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 03AE2040A4C147EA
Show »

FASTA50354,494
Isoform 3 [UniParc].

Checksum: 616061583D30DF52
Show »

FASTA53157,547

References

« Hide '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. expand/collapse author list , 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] (ISOFORMS 2 AND 3).
Tissue: Small intestine and Testis.
[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. expand/collapse author list , 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, IDENTIFICATION BY 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, IDENTIFICATION BY 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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.
[19]"A complex V ATP5A1 defect causes fatal neonatal mitochondrial encephalopathy."
Jonckheere A.I., Renkema G.H., Bras M., van den Heuvel L.P., Hoischen A., Gilissen C., Nabuurs S.B., Huynen M.A., de Vries M.C., Smeitink J.A., Rodenburg R.J.
Brain 136:1544-1554(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MC5DN4 CYS-329.
+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.
AK302272 mRNA. Translation: BAG63618.1.
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.
CCDSCCDS11927.1. [P25705-1]
CCDS58620.1. [P25705-2]
PIRPWHUA. S17193.
RefSeqNP_001001935.1. NM_001001935.2. [P25705-2]
NP_001001937.1. NM_001001937.1. [P25705-1]
NP_001244263.1. NM_001257334.1. [P25705-3]
NP_001244264.1. NM_001257335.1. [P25705-2]
NP_004037.1. NM_004046.5. [P25705-1]
UniGeneHs.298280.

3D structure databases

ProteinModelPortalP25705.
SMRP25705. Positions 56-553.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106987. 84 interactions.
DIPDIP-32871N.
IntActP25705. 31 interactions.
MINTMINT-1163289.
STRING9606.ENSP00000282050.

Chemistry

ChEMBLCHEMBL2062351.

PTM databases

PhosphoSiteP25705.

Polymorphism databases

DMDM114517.

2D gel databases

OGPP25705.
REPRODUCTION-2DPAGEP25705.
UCD-2DPAGEP25705.

Proteomic databases

MaxQBP25705.
PaxDbP25705.
PRIDEP25705.

Protocols and materials databases

DNASU498.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000282050; ENSP00000282050; ENSG00000152234. [P25705-1]
ENST00000398752; ENSP00000381736; ENSG00000152234. [P25705-1]
ENST00000590665; ENSP00000467037; ENSG00000152234.
ENST00000593152; ENSP00000465477; ENSG00000152234. [P25705-2]
GeneID498.
KEGGhsa:498.
UCSCuc002lbr.2. human. [P25705-1]

Organism-specific databases

CTD498.
GeneCardsGC18M043664.
HGNCHGNC:823. ATP5A1.
HPACAB013067.
MIM164360. gene.
615228. phenotype.
neXtProtNX_P25705.
Orphanet254913. Isolated ATP synthase deficiency.
PharmGKBPA25115.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0056.
HOVERGENHBG001536.
InParanoidP25705.
KOK02132.
OMAKEPMLTG.
OrthoDBEOG773XFP.
PhylomeDBP25705.
TreeFamTF300321.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressP25705.
BgeeP25705.
CleanExHS_ATP5A1.
GenevestigatorP25705.

Family and domain databases

Gene3D2.40.30.20. 1 hit.
3.40.50.300. 1 hit.
HAMAPMF_01346. ATP_synth_alpha_bact.
InterProIPR020003. 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.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
SUPFAMSSF47917. SSF47917. 1 hit.
SSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00962. atpA. 1 hit.
PROSITEPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSATP5A1. human.
GenomeRNAi498.
NextBio2089.
PMAP-CutDBP25705.
PROP25705.
SOURCESearch...

Entry information

Entry nameATPA_HUMAN
AccessionPrimary (citable) accession number: P25705
Secondary accession number(s): A8K092 expand/collapse secondary AC list , B4DY56, K7ENP3, Q53XX6, Q8IXV2, Q96FB4, Q96HW2, Q96IR6, Q9BTV8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: July 9, 2014
This is version 174 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 18

Human chromosome 18: entries, gene names and cross-references to MIM