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P25705

- ATPA_HUMAN

UniProt

P25705 - ATPA_HUMAN

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
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    • History
      Entry version 176 (01 Oct 2014)
      Sequence version 1 (01 May 1992)
      Previous versions | rss
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    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. protein binding Source: UniProtKB
    5. proton-transporting ATPase activity, rotational mechanism Source: InterPro
    6. proton-transporting ATP synthase activity, rotational mechanism Source: UniProtKB
    7. 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

    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: UniProt
    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

    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; alternate2 Publications
    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; alternate2 Publications
    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-acetyllysine2 Publications
    Modified residuei498 – 4981N6-acetyllysine; alternate2 Publications
    Modified residuei498 – 4981N6-succinyllysine; alternateBy similarity
    Modified residuei506 – 5061N6-acetyllysine; alternate2 Publications
    Modified residuei506 – 5061N6-succinyllysine; alternateBy similarity
    Modified residuei531 – 5311N6-acetyllysine; alternateBy similarity
    Modified residuei531 – 5311N6-succinyllysine; alternateBy similarity
    Modified residuei539 – 5391N6-acetyllysine; alternate2 Publications
    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

    ArrayExpressiP25705.
    BgeeiP25705.
    CleanExiHS_ATP5A1.
    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. 76 interactions.
    DIPiDIP-32871N.
    IntActiP25705. 34 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.
    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

    MLSVRVAAAV VRALPRRAGL VSRNALGSSF IAARNFHASN THLQKTGTAE    50
    MSSILEERIL GADTSVDLEE TGRVLSIGDG IARVHGLRNV QAEEMVEFSS 100
    GLKGMSLNLE PDNVGVVVFG NDKLIKEGDI VKRTGAIVDV PVGEELLGRV 150
    VDALGNAIDG KGPIGSKTRR RVGLKAPGII PRISVREPMQ TGIKAVDSLV 200
    PIGRGQRELI IGDRQTGKTS IAIDTIINQK RFNDGSDEKK KLYCIYVAIG 250
    QKRSTVAQLV KRLTDADAMK YTIVVSATAS DAAPLQYLAP YSGCSMGEYF 300
    RDNGKHALII YDDLSKQAVA YRQMSLLLRR PPGREAYPGD VFYLHSRLLE 350
    RAAKMNDAFG GGSLTALPVI ETQAGDVSAY IPTNVISITD GQIFLETELF 400
    YKGIRPAINV GLSVSRVGSA AQTRAMKQVA GTMKLELAQY REVAAFAQFG 450
    SDLDAATQQL LSRGVRLTEL LKQGQYSPMA IEEQVAVIYA GVRGYLDKLE 500
    PSKITKFENA FLSHVVSQHQ ALLGTIRADG KISEQSDAKL KEIVTNFLAG 550
    FEA 553
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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. 76 interactions.
    DIPi DIP-32871N.
    IntActi P25705. 34 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.
    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

    ArrayExpressi P25705.
    Bgeei P25705.
    CleanExi HS_ATP5A1.
    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

    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 1, 2014
    This is version 176 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