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Protein

ATP synthase subunit alpha, mitochondrial

Gene

ATP5A1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 similarity2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei413Required for activityBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi212 – 219ATPBy similarity8

GO - Molecular functioni

  • ATP binding Source: UniProtKB
  • MHC class I protein binding Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • proton-transporting ATP synthase activity, rotational mechanism Source: UniProtKB
  • transmembrane transporter activity Source: UniProtKB

GO - Biological processi

  • ATP biosynthetic process Source: UniProtKB
  • embryo development Source: UniProtKB
  • lipid metabolic process Source: UniProtKB
  • mitochondrial ATP synthesis coupled proton transport Source: UniProtKB
  • negative regulation of endothelial cell proliferation Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

ATP synthesis, Hydrogen ion transport, Ion transport, Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:HS07800-MONOMER.
ReactomeiR-HSA-1268020. Mitochondrial protein import.
R-HSA-163210. Formation of ATP by chemiosmotic coupling.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit alpha, mitochondrial
Gene namesi
Name:ATP5A1
Synonyms:ATP5A, ATP5AL2, ATPM
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 18

Organism-specific databases

HGNCiHGNC:823. ATP5A1.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • extracellular matrix Source: BHF-UCL
  • membrane Source: UniProtKB
  • mitochondrial inner membrane Source: UniProtKB
  • mitochondrial matrix Source: Reactome
  • mitochondrial proton-transporting ATP synthase complex Source: UniProtKB
  • mitochondrion Source: UniProtKB
  • myelin sheath Source: Ensembl
  • plasma membrane Source: UniProtKB
  • 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

Pathology & Biotechi

Involvement in diseasei

Combined oxidative phosphorylation deficiency 22 (COXPD22)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA mitochondrial disorder characterized by intrauterine growth retardation, microcephaly, hypotonia, pulmonary hypertension, failure to thrive, encephalopathy, and heart failure.
See also OMIM:616045
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_071982321Y → C in COXPD22; reduces mitochondrial membrane potential. 1 PublicationCorresponds to variant rs587777788dbSNPEnsembl.1
Mitochondrial complex V deficiency, nuclear 4 (MC5DN4)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:615228
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_069769329R → C in MC5DN4. 1 PublicationCorresponds to variant rs587776960dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi498.
MalaCardsiATP5A1.
MIMi615228. phenotype.
616045. phenotype.
OpenTargetsiENSG00000152234.
Orphaneti254913. Isolated ATP synthase deficiency.
PharmGKBiPA25115.

Chemistry databases

ChEMBLiCHEMBL2062351.

Polymorphism and mutation databases

BioMutaiATP5A1.
DMDMi114517.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 43Mitochondrion1 PublicationAdd BLAST43
ChainiPRO_000000242444 – 553ATP synthase subunit alpha, mitochondrialAdd BLAST510

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei44Pyrrolidone carboxylic acidBy similarity1
Modified residuei53PhosphoserineCombined sources1
Modified residuei65PhosphoserineCombined sources1
Modified residuei76Phosphoserine; alternateCombined sources1
Glycosylationi76O-linked (GlcNAc); alternateBy similarity1
Modified residuei106PhosphoserineBy similarity1
Modified residuei123N6-acetyllysineBy similarity1
Modified residuei126N6-acetyllysineBy similarity1
Modified residuei132N6-acetyllysineBy similarity1
Modified residuei134PhosphothreonineBy similarity1
Modified residuei161N6-acetyllysine; alternateCombined sources1
Modified residuei161N6-succinyllysine; alternateBy similarity1
Modified residuei166PhosphoserineCombined sources1
Modified residuei167N6-acetyllysine; alternateBy similarity1
Modified residuei167N6-succinyllysine; alternateBy similarity1
Modified residuei184PhosphoserineCombined sources1
Modified residuei204Omega-N-methylarginineBy similarity1
Modified residuei230N6-acetyllysine; alternateBy similarity1
Modified residuei230N6-succinyllysine; alternateBy similarity1
Modified residuei239N6-acetyllysine; alternateBy similarity1
Modified residuei239N6-succinyllysine; alternateBy similarity1
Modified residuei240N6-acetyllysineBy similarity1
Modified residuei261N6-acetyllysine; alternateCombined sources1
Modified residuei261N6-succinyllysine; alternateBy similarity1
Modified residuei305N6-acetyllysine; alternateBy similarity1
Modified residuei305N6-succinyllysine; alternateBy similarity1
Modified residuei427N6-acetyllysine; alternateBy similarity1
Modified residuei427N6-succinyllysine; alternateBy similarity1
Modified residuei434N6-acetyllysineCombined sources1
Modified residuei498N6-acetyllysine; alternateCombined sources1
Modified residuei498N6-succinyllysine; alternateBy similarity1
Modified residuei506N6-acetyllysine; alternateCombined sources1
Modified residuei506N6-succinyllysine; alternateBy similarity1
Modified residuei531N6-acetyllysine; alternateBy similarity1
Modified residuei531N6-succinyllysine; alternateBy similarity1
Modified residuei539N6-acetyllysine; alternateCombined sources1
Modified residuei539N6-succinyllysine; alternateBy similarity1
Modified residuei541N6-acetyllysineBy similarity1

Post-translational modificationi

The N-terminus is blocked.
Acetylated on lysine residues. BLOC1S1 is required for acetylation.1 Publication

Keywords - PTMi

Acetylation, Glycoprotein, Methylation, Phosphoprotein, Pyrrolidone carboxylic acid

Proteomic databases

EPDiP25705.
PaxDbiP25705.
PeptideAtlasiP25705.
PRIDEiP25705.
TopDownProteomicsiP25705-1. [P25705-1]

2D gel databases

OGPiP25705.
REPRODUCTION-2DPAGEP25705.
UCD-2DPAGEP25705.

PTM databases

iPTMnetiP25705.
PhosphoSitePlusiP25705.
SwissPalmiP25705.

Miscellaneous databases

PMAP-CutDBP25705.

Expressioni

Tissue specificityi

Fetal lung, heart, liver, gut and kidney. Expressed at higher levels in the fetal brain, retina and spinal cord.1 Publication

Gene expression databases

BgeeiENSG00000152234.
CleanExiHS_ATP5A1.
ExpressionAtlasiP25705. baseline and differential.
GenevisibleiP25705. HS.

Organism-specific databases

HPAiCAB013067.
HPA040622.
HPA044202.

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 (PubMed:11410595). Interacts with HRG; the interaction occurs on the surface of T-cells and alters the cell morphology when associated with concanavalin (in vitro) (PubMed:19285951). Interacts with PLG (angiostatin peptide); the interaction inhibits most of the angiogenic properties of angiostatin (PubMed:10077593). 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 (PubMed:22309213). 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. Interacts with CLN5 and PPT1 (By similarity).By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BLOC1S1P785372EBI-351437,EBI-348630
SIRT3Q9NTG72EBI-351437,EBI-724621
YWHAZP631043EBI-351437,EBI-347088

GO - Molecular functioni

  • MHC class I protein binding Source: UniProtKB

Protein-protein interaction databases

BioGridi106987. 167 interactors.
DIPiDIP-32871N.
IntActiP25705. 61 interactors.
MINTiMINT-1163289.
STRINGi9606.ENSP00000282050.

Structurei

3D structure databases

ProteinModelPortaliP25705.
SMRiP25705.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase alpha/beta chains family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1353. Eukaryota.
COG0056. LUCA.
GeneTreeiENSGT00550000074846.
HOVERGENiHBG001536.
InParanoidiP25705.
KOiK02132.
OMAiKRFNEAQ.
OrthoDBiEOG091G0D1M.
PhylomeDBiP25705.
TreeFamiTF300321.

Family and domain databases

CDDicd01132. F1_ATPase_alpha. 1 hit.
Gene3Di2.40.30.20. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_01346. ATP_synth_alpha_bact. 1 hit.
InterProiIPR023366. ATP_synth_asu-like.
IPR000793. ATP_synth_asu_C.
IPR033732. ATP_synth_F1_a.
IPR005294. ATP_synth_F1_asu.
IPR020003. ATPase_a/bsu_AS.
IPR004100. ATPase_F1/V1/A1_a/bsu_N.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR15184:SF3. PTHR15184:SF3. 1 hit.
PfamiPF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
PIRSFiPIRSF039088. F_ATPase_subunit_alpha. 1 hit.
SUPFAMiSSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00962. atpA. 1 hit.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P25705-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MLSVRVAAAV VRALPRRAGL VSRNALGSSF IAARNFHASN THLQKTGTAE
60 70 80 90 100
MSSILEERIL GADTSVDLEE TGRVLSIGDG IARVHGLRNV QAEEMVEFSS
110 120 130 140 150
GLKGMSLNLE PDNVGVVVFG NDKLIKEGDI VKRTGAIVDV PVGEELLGRV
160 170 180 190 200
VDALGNAIDG KGPIGSKTRR RVGLKAPGII PRISVREPMQ TGIKAVDSLV
210 220 230 240 250
PIGRGQRELI IGDRQTGKTS IAIDTIINQK RFNDGSDEKK 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
RAAKMNDAFG 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 FLSHVVSQHQ ALLGTIRADG KISEQSDAKL KEIVTNFLAG

FEA
Length:553
Mass (Da):59,751
Last modified:May 1, 1992 - v1
Checksum:iAA47BBB8EDA77EAC
GO
Isoform 2 (identifier: P25705-2) [UniParc]FASTAAdd to basket

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

Show »
Length:503
Mass (Da):54,494
Checksum:i03AE2040A4C147EA
GO
Isoform 3 (identifier: P25705-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     140-161: Missing.

Note: No experimental confirmation available.
Show »
Length:531
Mass (Da):57,547
Checksum:i616061583D30DF52
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti162G → V in BAG63618 (PubMed:14702039).Curated1
Sequence conflicti183I → T in BAG63618 (PubMed:14702039).Curated1
Sequence conflicti329R → L in AAH39135 (PubMed:14702039).Curated1
Sequence conflicti356N → D in BAG63618 (PubMed:14702039).Curated1
Sequence conflicti510A → D in AAH11384 (PubMed:14702039).Curated1
Sequence conflicti529D → E in AAH11384 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04836932A → S.Corresponds to variant rs2228437dbSNPEnsembl.1
Natural variantiVAR_048370223I → V.Corresponds to variant rs2228436dbSNPEnsembl.1
Natural variantiVAR_071982321Y → C in COXPD22; reduces mitochondrial membrane potential. 1 PublicationCorresponds to variant rs587777788dbSNPEnsembl.1
Natural variantiVAR_069769329R → C in MC5DN4. 1 PublicationCorresponds to variant rs587776960dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0451291 – 50Missing in isoform 2. 1 PublicationAdd BLAST50
Alternative sequenceiVSP_054688140 – 161Missing in isoform 3. 1 PublicationAdd BLAST22

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS11927.1. [P25705-1]
CCDS58620.1. [P25705-2]
CCDS59315.1. [P25705-3]
PIRiS17193. PWHUA.
RefSeqiNP_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]
UniGeneiHs.298280.

Genome annotation databases

EnsembliENST00000282050; ENSP00000282050; ENSG00000152234. [P25705-1]
ENST00000398752; ENSP00000381736; ENSG00000152234. [P25705-1]
ENST00000590665; ENSP00000467037; ENSG00000152234. [P25705-3]
ENST00000593152; ENSP00000465477; ENSG00000152234. [P25705-2]
GeneIDi498.
KEGGihsa:498.
UCSCiuc010dnl.2. human. [P25705-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS11927.1. [P25705-1]
CCDS58620.1. [P25705-2]
CCDS59315.1. [P25705-3]
PIRiS17193. PWHUA.
RefSeqiNP_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]
UniGeneiHs.298280.

3D structure databases

ProteinModelPortaliP25705.
SMRiP25705.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106987. 167 interactors.
DIPiDIP-32871N.
IntActiP25705. 61 interactors.
MINTiMINT-1163289.
STRINGi9606.ENSP00000282050.

Chemistry databases

ChEMBLiCHEMBL2062351.

PTM databases

iPTMnetiP25705.
PhosphoSitePlusiP25705.
SwissPalmiP25705.

Polymorphism and mutation databases

BioMutaiATP5A1.
DMDMi114517.

2D gel databases

OGPiP25705.
REPRODUCTION-2DPAGEP25705.
UCD-2DPAGEP25705.

Proteomic databases

EPDiP25705.
PaxDbiP25705.
PeptideAtlasiP25705.
PRIDEiP25705.
TopDownProteomicsiP25705-1. [P25705-1]

Protocols and materials databases

DNASUi498.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000282050; ENSP00000282050; ENSG00000152234. [P25705-1]
ENST00000398752; ENSP00000381736; ENSG00000152234. [P25705-1]
ENST00000590665; ENSP00000467037; ENSG00000152234. [P25705-3]
ENST00000593152; ENSP00000465477; ENSG00000152234. [P25705-2]
GeneIDi498.
KEGGihsa:498.
UCSCiuc010dnl.2. human. [P25705-1]

Organism-specific databases

CTDi498.
DisGeNETi498.
GeneCardsiATP5A1.
HGNCiHGNC:823. ATP5A1.
HPAiCAB013067.
HPA040622.
HPA044202.
MalaCardsiATP5A1.
MIMi164360. gene.
615228. phenotype.
616045. phenotype.
neXtProtiNX_P25705.
OpenTargetsiENSG00000152234.
Orphaneti254913. Isolated ATP synthase deficiency.
PharmGKBiPA25115.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1353. Eukaryota.
COG0056. LUCA.
GeneTreeiENSGT00550000074846.
HOVERGENiHBG001536.
InParanoidiP25705.
KOiK02132.
OMAiKRFNEAQ.
OrthoDBiEOG091G0D1M.
PhylomeDBiP25705.
TreeFamiTF300321.

Enzyme and pathway databases

BioCyciZFISH:HS07800-MONOMER.
ReactomeiR-HSA-1268020. Mitochondrial protein import.
R-HSA-163210. Formation of ATP by chemiosmotic coupling.

Miscellaneous databases

ChiTaRSiATP5A1. human.
GenomeRNAii498.
PMAP-CutDBP25705.
PROiP25705.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000152234.
CleanExiHS_ATP5A1.
ExpressionAtlasiP25705. baseline and differential.
GenevisibleiP25705. HS.

Family and domain databases

CDDicd01132. F1_ATPase_alpha. 1 hit.
Gene3Di2.40.30.20. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_01346. ATP_synth_alpha_bact. 1 hit.
InterProiIPR023366. ATP_synth_asu-like.
IPR000793. ATP_synth_asu_C.
IPR033732. ATP_synth_F1_a.
IPR005294. ATP_synth_F1_asu.
IPR020003. ATPase_a/bsu_AS.
IPR004100. ATPase_F1/V1/A1_a/bsu_N.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR15184:SF3. PTHR15184:SF3. 1 hit.
PfamiPF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
PIRSFiPIRSF039088. F_ATPase_subunit_alpha. 1 hit.
SUPFAMiSSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00962. atpA. 1 hit.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiATPA_HUMAN
AccessioniPrimary (citable) accession number: P25705
Secondary accession number(s): A8K092
, B4DY56, K7ENP3, Q53XX6, Q8IXV2, Q96FB4, Q96HW2, Q96IR6, Q9BTV8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: November 30, 2016
This is version 200 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 18
    Human chromosome 18: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.