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P25705

- ATPA_HUMAN

UniProt

P25705 - ATPA_HUMAN

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Protein

ATP synthase subunit alpha, mitochondrial

Gene

ATP5A1

Organism
Homo sapiens (Human)
Status
Reviewed - 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 similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei413 – 4131Required for activityBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi212 – 2198ATPBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. MHC class I protein binding Source: UniProtKB
  3. poly(A) RNA binding Source: UniProtKB
  4. proton-transporting ATPase activity, rotational mechanism Source: InterPro
  5. proton-transporting ATP synthase activity, rotational mechanism Source: UniProtKB
  6. transmembrane transporter activity Source: UniProtKB

GO - Biological processi

  1. ATP biosynthetic process Source: UniProtKB
  2. ATP catabolic process Source: GOC
  3. ATP hydrolysis coupled proton transport Source: InterPro
  4. cellular metabolic process Source: Reactome
  5. embryo development Source: UniProtKB
  6. lipid metabolic process Source: UniProtKB
  7. mitochondrial ATP synthesis coupled proton transport Source: UniProtKB
  8. negative regulation of endothelial cell proliferation Source: UniProtKB
  9. respiratory electron transport chain Source: Reactome
  10. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Biological processi

ATP synthesis, Hydrogen ion transport, Ion transport, Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_118595. Mitochondrial protein import.
REACT_6759. 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
ProteomesiUP000005640: Chromosome 18

Organism-specific databases

HGNCiHGNC:823. ATP5A1.

Subcellular locationi

Mitochondrion inner membrane. Cell membrane; Peripheral membrane protein; Extracellular side
Note: Colocalizes with HRG on the cell surface of T-cells.

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProtKB
  2. membrane Source: UniProtKB
  3. mitochondrial inner membrane Source: UniProtKB
  4. mitochondrial matrix Source: Reactome
  5. mitochondrial proton-transporting ATP synthase complex Source: UniProtKB
  6. mitochondrion Source: UniProtKB
  7. plasma membrane Source: UniProtKB
  8. 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

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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti329 – 3291R → C in MC5DN4. 1 Publication
VAR_069769

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi615228. phenotype.
Orphaneti254913. Isolated ATP synthase deficiency.
PharmGKBiPA25115.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4343Mitochondrion1 PublicationAdd
BLAST
Chaini44 – 553510ATP synthase subunit alpha, mitochondrialPRO_0000002424Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei44 – 441Pyrrolidone carboxylic acidBy similarity
Modified residuei76 – 761PhosphoserineBy similarity
Glycosylationi76 – 761O-linked (GlcNAc)By similarity
Modified residuei123 – 1231N6-acetyllysineBy similarity
Modified residuei126 – 1261N6-acetyllysineBy similarity
Modified residuei132 – 1321N6-acetyllysineBy similarity
Modified residuei161 – 1611N6-acetyllysine; alternate1 Publication
Modified residuei161 – 1611N6-succinyllysine; alternateBy similarity
Modified residuei166 – 1661Phosphoserine1 Publication
Modified residuei167 – 1671N6-acetyllysine; alternateBy similarity
Modified residuei167 – 1671N6-succinyllysine; alternateBy similarity
Modified residuei230 – 2301N6-acetyllysine; alternateBy similarity
Modified residuei230 – 2301N6-succinyllysine; alternateBy similarity
Modified residuei239 – 2391N6-acetyllysine; alternateBy similarity
Modified residuei239 – 2391N6-succinyllysine; alternateBy similarity
Modified residuei240 – 2401N6-acetyllysineBy similarity
Modified residuei261 – 2611N6-acetyllysine; alternate1 Publication
Modified residuei261 – 2611N6-succinyllysine; alternateBy similarity
Modified residuei305 – 3051N6-acetyllysine; alternateBy similarity
Modified residuei305 – 3051N6-succinyllysine; alternateBy similarity
Modified residuei427 – 4271N6-acetyllysine; alternateBy similarity
Modified residuei427 – 4271N6-succinyllysine; alternateBy similarity
Modified residuei434 – 4341N6-acetyllysine1 Publication
Modified residuei498 – 4981N6-acetyllysine; alternate1 Publication
Modified residuei498 – 4981N6-succinyllysine; alternateBy similarity
Modified residuei506 – 5061N6-acetyllysine; alternate1 Publication
Modified residuei506 – 5061N6-succinyllysine; alternateBy similarity
Modified residuei531 – 5311N6-acetyllysine; alternateBy similarity
Modified residuei531 – 5311N6-succinyllysine; alternateBy similarity
Modified residuei539 – 5391N6-acetyllysine; alternate1 Publication
Modified residuei539 – 5391N6-succinyllysine; alternateBy similarity
Modified residuei541 – 5411N6-acetyllysineBy similarity

Post-translational modificationi

The N-terminus is blocked.
Acetylated on lysine residues. BLOC1S1 is required for acetylation.2 Publications

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein, Pyrrolidone carboxylic acid

Proteomic databases

MaxQBiP25705.
PaxDbiP25705.
PRIDEiP25705.

2D gel databases

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

PTM databases

PhosphoSiteiP25705.

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

BgeeiP25705.
CleanExiHS_ATP5A1.
ExpressionAtlasiP25705. baseline and differential.
GenevestigatoriP25705.

Organism-specific databases

HPAiCAB013067.

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.4 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi106987. 82 interactions.
DIPiDIP-32871N.
IntActiP25705. 35 interactions.
MINTiMINT-1163289.
STRINGi9606.ENSP00000282050.

Structurei

3D structure databases

ProteinModelPortaliP25705.
SMRiP25705. Positions 56-553.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase alpha/beta chains family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0056.
GeneTreeiENSGT00550000074846.
HOVERGENiHBG001536.
InParanoidiP25705.
KOiK02132.
OMAiKEPMLTG.
OrthoDBiEOG773XFP.
PhylomeDBiP25705.
TreeFamiTF300321.

Family and domain databases

Gene3Di2.40.30.20. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_01346. ATP_synth_alpha_bact.
InterProiIPR020003. 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]
PfamiPF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
SUPFAMiSSF47917. SSF47917. 1 hit.
SSF50615. 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. Align

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti162 – 1621G → V in BAG63618. (PubMed:14702039)Curated
Sequence conflicti183 – 1831I → T in BAG63618. (PubMed:14702039)Curated
Sequence conflicti329 – 3291R → L in AAH39135. (PubMed:14702039)Curated
Sequence conflicti356 – 3561N → D in BAG63618. (PubMed:14702039)Curated
Sequence conflicti510 – 5101A → D in AAH11384. (PubMed:14702039)Curated
Sequence conflicti529 – 5291D → E in AAH11384. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti32 – 321A → S.
Corresponds to variant rs2228437 [ dbSNP | Ensembl ].
VAR_048369
Natural varianti223 – 2231I → V.
Corresponds to variant rs2228436 [ dbSNP | Ensembl ].
VAR_048370
Natural varianti329 – 3291R → C in MC5DN4. 1 Publication
VAR_069769

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5050Missing in isoform 2. 1 PublicationVSP_045129Add
BLAST
Alternative sequencei140 – 16122Missing in isoform 3. 1 PublicationVSP_054688Add
BLAST

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.
UCSCiuc002lbr.2. human. [P25705-1]

Polymorphism databases

DMDMi114517.

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 .
CCDSi CCDS11927.1. [P25705-1 ]
CCDS58620.1. [P25705-2 ]
CCDS59315.1. [P25705-3 ]
PIRi S17193. PWHUA.
RefSeqi NP_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 ]
UniGenei Hs.298280.

3D structure databases

ProteinModelPortali P25705.
SMRi P25705. Positions 56-553.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106987. 82 interactions.
DIPi DIP-32871N.
IntActi P25705. 35 interactions.
MINTi MINT-1163289.
STRINGi 9606.ENSP00000282050.

Chemistry

ChEMBLi CHEMBL2062351.

PTM databases

PhosphoSitei P25705.

Polymorphism databases

DMDMi 114517.

2D gel databases

OGPi P25705.
REPRODUCTION-2DPAGE P25705.
UCD-2DPAGE P25705.

Proteomic databases

MaxQBi P25705.
PaxDbi P25705.
PRIDEi P25705.

Protocols and materials databases

DNASUi 498.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000282050 ; ENSP00000282050 ; ENSG00000152234 . [P25705-1 ]
ENST00000398752 ; ENSP00000381736 ; ENSG00000152234 . [P25705-1 ]
ENST00000590665 ; ENSP00000467037 ; ENSG00000152234 . [P25705-3 ]
ENST00000593152 ; ENSP00000465477 ; ENSG00000152234 . [P25705-2 ]
GeneIDi 498.
KEGGi hsa:498.
UCSCi uc002lbr.2. human. [P25705-1 ]

Organism-specific databases

CTDi 498.
GeneCardsi GC18M043664.
HGNCi HGNC:823. ATP5A1.
HPAi CAB013067.
MIMi 164360. gene.
615228. phenotype.
neXtProti NX_P25705.
Orphaneti 254913. Isolated ATP synthase deficiency.
PharmGKBi PA25115.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0056.
GeneTreei ENSGT00550000074846.
HOVERGENi HBG001536.
InParanoidi P25705.
KOi K02132.
OMAi KEPMLTG.
OrthoDBi EOG773XFP.
PhylomeDBi P25705.
TreeFami TF300321.

Enzyme and pathway databases

Reactomei REACT_118595. Mitochondrial protein import.
REACT_6759. Formation of ATP by chemiosmotic coupling.

Miscellaneous databases

ChiTaRSi ATP5A1. human.
GenomeRNAii 498.
NextBioi 2089.
PMAP-CutDB P25705.
PROi P25705.
SOURCEi Search...

Gene expression databases

Bgeei P25705.
CleanExi HS_ATP5A1.
ExpressionAtlasi P25705. baseline and differential.
Genevestigatori P25705.

Family and domain databases

Gene3Di 2.40.30.20. 1 hit.
3.40.50.300. 1 hit.
HAMAPi MF_01346. ATP_synth_alpha_bact.
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.
IPR027417. P-loop_NTPase.
[Graphical view ]
Pfami PF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view ]
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...

Publicationsi

« Hide 'large scale' publications
  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] (ISOFORMS 2 AND 3).
    Tissue: Small intestine and Testis.
  6. 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. 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. 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. Cited for: VARIANT MC5DN4 CYS-329.

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: October 29, 2014
This is version 177 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

External Data

Dasty 3