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P48047

- ATPO_HUMAN

UniProt

P48047 - ATPO_HUMAN

Protein

ATP synthase subunit O, mitochondrial

Gene

ATP5O

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 1 (01 Feb 1996)
      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. Part of the complex F0 domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha3beta3 subcomplex and subunit a/ATP6 static relative to the rotary elements.

    GO - Molecular functioni

    1. drug binding Source: UniProtKB
    2. proton-transporting ATP synthase activity, rotational mechanism Source: InterPro
    3. transmembrane transporter activity Source: UniProtKB
    4. transporter activity Source: ProtInc

    GO - Biological processi

    1. ATP biosynthetic process Source: UniProtKB
    2. ATP catabolic process Source: UniProtKB
    3. cellular metabolic process Source: Reactome
    4. mitochondrial ATP synthesis coupled proton transport Source: UniProtKB
    5. proton transport Source: UniProtKB
    6. respiratory electron transport chain Source: Reactome
    7. small molecule metabolic process Source: Reactome

    Keywords - Biological processi

    ATP synthesis, Hydrogen ion transport, Ion transport, Transport

    Enzyme and pathway databases

    ReactomeiREACT_6759. Formation of ATP by chemiosmotic coupling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATP synthase subunit O, mitochondrial
    Alternative name(s):
    Oligomycin sensitivity conferral protein
    Short name:
    OSCP
    Gene namesi
    Name:ATP5O
    Synonyms:ATPO
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 21

    Organism-specific databases

    HGNCiHGNC:850. ATP5O.

    Subcellular locationi

    Mitochondrion By similarity. Mitochondrion inner membrane By similarity

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion inner membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi162 – 1621K → R: Increased ATP levels. 1 Publication

    Organism-specific databases

    PharmGKBiPA25144.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2323Mitochondrion1 PublicationAdd
    BLAST
    Chaini24 – 213190ATP synthase subunit O, mitochondrialPRO_0000002646Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei54 – 541N6-acetyllysine1 Publication
    Modified residuei60 – 601N6-acetyllysineBy similarity
    Modified residuei70 – 701N6-acetyllysineBy similarity
    Modified residuei73 – 731N6-acetyllysineBy similarity
    Modified residuei90 – 901N6-succinyllysineBy similarity
    Modified residuei158 – 1581N6-acetyllysine; alternateBy similarity
    Modified residuei158 – 1581N6-succinyllysine; alternateBy similarity
    Modified residuei162 – 1621N6-acetyllysine; alternate2 Publications
    Modified residuei162 – 1621N6-succinyllysine; alternateBy similarity
    Modified residuei172 – 1721N6-acetyllysine1 Publication
    Modified residuei176 – 1761N6-acetyllysineBy similarity
    Modified residuei192 – 1921N6-acetyllysine1 Publication
    Modified residuei199 – 1991N6-succinyllysineBy similarity

    Post-translational modificationi

    Acetylation at Lys-162 decreases ATP production. Deacetylated by SIRT3.2 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP48047.
    PaxDbiP48047.
    PeptideAtlasiP48047.
    PRIDEiP48047.

    2D gel databases

    OGPiP48047.
    UCD-2DPAGEP48047.

    PTM databases

    PhosphoSiteiP48047.

    Expressioni

    Gene expression databases

    ArrayExpressiP48047.
    BgeeiP48047.
    CleanExiHS_ATP5O.
    GenevestigatoriP48047.

    Organism-specific databases

    HPAiCAB016209.
    HPA041394.

    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. Component of an ATP synthase complex composed of ATP5F1, ATP5G1, ATP5E, ATP5H, ATP5I, ATP5J, ATP5J2, MT-ATP6, MT-ATP8, ATP5A1, ATP5B, ATP5D, ATP5C1, ATP5O, ATP5L, USMG5 and MP68 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi107021. 23 interactions.
    IntActiP48047. 13 interactions.
    MINTiMINT-5002594.
    STRINGi9606.ENSP00000290299.

    Structurei

    3D structure databases

    ProteinModelPortaliP48047.
    SMRiP48047. Positions 24-212.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ATPase delta chain family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0712.
    HOGENOMiHOG000075825.
    HOVERGENiHBG004309.
    InParanoidiP48047.
    KOiK02137.
    OMAiTKNFLAV.
    PhylomeDBiP48047.
    TreeFamiTF106241.

    Family and domain databases

    Gene3Di1.10.520.20. 1 hit.
    HAMAPiMF_01416. ATP_synth_delta_bact.
    InterProiIPR020781. ATPase_OSCP/d_CS.
    IPR026015. ATPase_OSCP/delta_N.
    IPR000711. ATPase_OSCP/dsu.
    [Graphical view]
    PANTHERiPTHR11910. PTHR11910. 1 hit.
    PfamiPF00213. OSCP. 1 hit.
    [Graphical view]
    PRINTSiPR00125. ATPASEDELTA.
    SUPFAMiSSF47928. SSF47928. 1 hit.
    TIGRFAMsiTIGR01145. ATP_synt_delta. 1 hit.
    PROSITEiPS00389. ATPASE_DELTA. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P48047-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAPAVSGLS RQVRCFSTSV VRPFAKLVRP PVQVYGIEGR YATALYSAAS    50
    KQNKLEQVEK ELLRVAQILK EPKVAASVLN PYVKRSIKVK SLNDITAKER 100
    FSPLTTNLIN LLAENGRLSN TQGVVSAFST MMSVHRGEVP CTVTSASPLE 150
    EATLSELKTV LKSFLSQGQV LKLEAKTDPS ILGGMIVRIG EKYVDMSVKT 200
    KIQKLGRAMR EIV 213
    Length:213
    Mass (Da):23,277
    Last modified:February 1, 1996 - v1
    Checksum:i311F53576A31FC93
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti98 – 981K → R.2 Publications
    Corresponds to variant rs4842 [ dbSNP | Ensembl ].
    VAR_011930

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X83218 mRNA. Translation: CAA58219.1.
    BT019836 mRNA. Translation: AAV38639.1.
    CR456822 mRNA. Translation: CAG33103.1.
    AK222962 mRNA. Translation: BAD96682.1.
    AK311796 mRNA. Translation: BAG34739.1.
    CH471079 Genomic DNA. Translation: EAX09802.1.
    BC021233 mRNA. Translation: AAH21233.1.
    BC022865 mRNA. Translation: AAH22865.1.
    CCDSiCCDS13634.1.
    RefSeqiNP_001688.1. NM_001697.2.
    UniGeneiHs.409140.

    Genome annotation databases

    EnsembliENST00000290299; ENSP00000290299; ENSG00000241837.
    GeneIDi539.
    KEGGihsa:539.
    UCSCiuc002ytl.3. human.

    Polymorphism databases

    DMDMi1352049.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X83218 mRNA. Translation: CAA58219.1 .
    BT019836 mRNA. Translation: AAV38639.1 .
    CR456822 mRNA. Translation: CAG33103.1 .
    AK222962 mRNA. Translation: BAD96682.1 .
    AK311796 mRNA. Translation: BAG34739.1 .
    CH471079 Genomic DNA. Translation: EAX09802.1 .
    BC021233 mRNA. Translation: AAH21233.1 .
    BC022865 mRNA. Translation: AAH22865.1 .
    CCDSi CCDS13634.1.
    RefSeqi NP_001688.1. NM_001697.2.
    UniGenei Hs.409140.

    3D structure databases

    ProteinModelPortali P48047.
    SMRi P48047. Positions 24-212.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107021. 23 interactions.
    IntActi P48047. 13 interactions.
    MINTi MINT-5002594.
    STRINGi 9606.ENSP00000290299.

    PTM databases

    PhosphoSitei P48047.

    Polymorphism databases

    DMDMi 1352049.

    2D gel databases

    OGPi P48047.
    UCD-2DPAGE P48047.

    Proteomic databases

    MaxQBi P48047.
    PaxDbi P48047.
    PeptideAtlasi P48047.
    PRIDEi P48047.

    Protocols and materials databases

    DNASUi 539.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000290299 ; ENSP00000290299 ; ENSG00000241837 .
    GeneIDi 539.
    KEGGi hsa:539.
    UCSCi uc002ytl.3. human.

    Organism-specific databases

    CTDi 539.
    GeneCardsi GC21M035275.
    H-InvDB HIX0158705.
    HGNCi HGNC:850. ATP5O.
    HPAi CAB016209.
    HPA041394.
    MIMi 600828. gene.
    neXtProti NX_P48047.
    PharmGKBi PA25144.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0712.
    HOGENOMi HOG000075825.
    HOVERGENi HBG004309.
    InParanoidi P48047.
    KOi K02137.
    OMAi TKNFLAV.
    PhylomeDBi P48047.
    TreeFami TF106241.

    Enzyme and pathway databases

    Reactomei REACT_6759. Formation of ATP by chemiosmotic coupling.

    Miscellaneous databases

    ChiTaRSi ATP5O. human.
    GeneWikii ATP5O.
    GenomeRNAii 539.
    NextBioi 2235.
    PROi P48047.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P48047.
    Bgeei P48047.
    CleanExi HS_ATP5O.
    Genevestigatori P48047.

    Family and domain databases

    Gene3Di 1.10.520.20. 1 hit.
    HAMAPi MF_01416. ATP_synth_delta_bact.
    InterProi IPR020781. ATPase_OSCP/d_CS.
    IPR026015. ATPase_OSCP/delta_N.
    IPR000711. ATPase_OSCP/dsu.
    [Graphical view ]
    PANTHERi PTHR11910. PTHR11910. 1 hit.
    Pfami PF00213. OSCP. 1 hit.
    [Graphical view ]
    PRINTSi PR00125. ATPASEDELTA.
    SUPFAMi SSF47928. SSF47928. 1 hit.
    TIGRFAMsi TIGR01145. ATP_synt_delta. 1 hit.
    PROSITEi PS00389. ATPASE_DELTA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of the cDNA for the human ATP synthase OSCP subunit (ATP5O) by exon trapping and mapping to chromosome 21q22.1-q22.2."
      Chen H.M., Morris M.A., Rossier C., Blouin J.-L., Antonarakis S.E.
      Genomics 28:470-476(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain and Muscle.
    2. "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 (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ARG-98.
    3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "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].
      Tissue: Testis.
    5. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ARG-98.
      Tissue: Heart.
    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].
      Tissue: Brain.
    8. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 24-40.
      Tissue: Platelet.
    9. "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-54; LYS-162; LYS-172 AND LYS-192, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "SIRT3 deacetylates ATP synthase F1 complex proteins in response to nutrient and exercise-induced stress."
      Vassilopoulos A., Pennington D.J., Andresson T., Rees D., Fearnley I., Ham A., Yan Y., Flynn C.R., Jones K., Kim H.S., Deng C., Walker J., Gius D.
      Antioxid. Redox Signal. 0:0-0(2013)
      Cited for: ACETYLATION AT LYS-162, DEACETYLATION BY SIRT3, MUTAGENESIS OF LYS-162.

    Entry informationi

    Entry nameiATPO_HUMAN
    AccessioniPrimary (citable) accession number: P48047
    Secondary accession number(s): B2R4E2, Q5U042, Q6IBI2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 145 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 21
      Human chromosome 21: 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