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O75947

- ATP5H_HUMAN

UniProt

O75947 - ATP5H_HUMAN

Protein

ATP synthase subunit d, mitochondrial

Gene

ATP5H

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. 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. hydrogen ion transmembrane transporter activity Source: InterPro
    2. transmembrane transporter activity Source: UniProtKB

    GO - Biological processi

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

    Keywords - Biological processi

    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 d, mitochondrial
    Short name:
    ATPase subunit d
    Gene namesi
    Name:ATP5H
    ORF Names:My032
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:845. ATP5H.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. mitochondrial inner membrane Source: UniProtKB
    3. mitochondrial proton-transporting ATP synthase complex Source: UniProtKB
    4. mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) Source: InterPro
    5. mitochondrion Source: UniProt

    Keywords - Cellular componenti

    CF(0), Membrane, Mitochondrion, Mitochondrion inner membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25135.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 161160ATP synthase subunit d, mitochondrialPRO_0000071673Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei85 – 851N6-acetyllysine1 Publication
    Modified residuei95 – 951N6-acetyllysine1 Publication
    Modified residuei117 – 1171N6-acetyllysine1 Publication
    Modified residuei149 – 1491N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiO75947.
    PaxDbiO75947.
    PeptideAtlasiO75947.
    PRIDEiO75947.

    2D gel databases

    OGPiO75947.
    REPRODUCTION-2DPAGEIPI00456049.
    UCD-2DPAGEO75947.

    PTM databases

    PhosphoSiteiO75947.

    Expressioni

    Gene expression databases

    ArrayExpressiO75947.
    BgeeiO75947.
    CleanExiHS_ATP5H.
    GenevestigatoriO75947.

    Organism-specific databases

    HPAiHPA042777.
    HPA048459.

    Interactioni

    Subunit structurei

    F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. CF0 seems to have nine subunits: a, b, c, d, e, f, g, F6 and 8 (or A6L). 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

    BioGridi115739. 11 interactions.
    IntActiO75947. 6 interactions.
    MINTiMINT-1407327.
    STRINGi9606.ENSP00000301587.

    Structurei

    3D structure databases

    ProteinModelPortaliO75947.
    SMRiO75947. Positions 4-124.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ATPase d subunit family.Curated

    Phylogenomic databases

    eggNOGiNOG307464.
    HOGENOMiHOG000267023.
    HOVERGENiHBG050612.
    InParanoidiO75947.
    KOiK02138.
    OMAiMEDYRDA.
    PhylomeDBiO75947.
    TreeFamiTF314031.

    Family and domain databases

    InterProiIPR008689. ATPase_F0-cplx_dsu_mt.
    [Graphical view]
    PfamiPF05873. Mt_ATP-synt_D. 1 hit.
    [Graphical view]
    PIRSFiPIRSF005514. ATPase_F0_D_mt. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O75947-1) [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

    MAGRKLALKT IDWVAFAEII PQNQKAIASS LKSWNETLTS RLAALPENPP    50
    AIDWAYYKAN VAKAGLVDDF EKKFNALKVP VPEDKYTAQV DAEEKEDVKS 100
    CAEWVSLSKA RIVEYEKEME KMKNLIPFDQ MTIEDLNEAF PETKLDKKKY 150
    PYWPHQPIEN L 161
    Length:161
    Mass (Da):18,491
    Last modified:January 23, 2007 - v3
    Checksum:iE93020ADA1BA1694
    GO
    Isoform 2 (identifier: O75947-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         74-97: Missing.

    Show »
    Length:137
    Mass (Da):15,773
    Checksum:i0796685CD2CC605E
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei74 – 9724Missing in isoform 2. 2 PublicationsVSP_000436Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF087135 mRNA. Translation: AAC36338.1.
    AF070650 mRNA. Translation: AAD20956.1.
    AF061735 mRNA. Translation: AAG43146.1.
    AK312230 mRNA. Translation: BAG35163.1.
    CH471099 Genomic DNA. Translation: EAW89228.1.
    BC032245 mRNA. Translation: AAH32245.1.
    BC038092 mRNA. Translation: AAH38092.1.
    CCDSiCCDS11712.1. [O75947-1]
    CCDS32727.1. [O75947-2]
    RefSeqiNP_001003785.1. NM_001003785.1. [O75947-2]
    NP_006347.1. NM_006356.2. [O75947-1]
    UniGeneiHs.514465.

    Genome annotation databases

    EnsembliENST00000301587; ENSP00000301587; ENSG00000167863. [O75947-1]
    ENST00000344546; ENSP00000344230; ENSG00000167863. [O75947-2]
    GeneIDi10476.
    KEGGihsa:10476.
    UCSCiuc002jmn.1. human. [O75947-1]
    uc002jmo.1. human. [O75947-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF087135 mRNA. Translation: AAC36338.1 .
    AF070650 mRNA. Translation: AAD20956.1 .
    AF061735 mRNA. Translation: AAG43146.1 .
    AK312230 mRNA. Translation: BAG35163.1 .
    CH471099 Genomic DNA. Translation: EAW89228.1 .
    BC032245 mRNA. Translation: AAH32245.1 .
    BC038092 mRNA. Translation: AAH38092.1 .
    CCDSi CCDS11712.1. [O75947-1 ]
    CCDS32727.1. [O75947-2 ]
    RefSeqi NP_001003785.1. NM_001003785.1. [O75947-2 ]
    NP_006347.1. NM_006356.2. [O75947-1 ]
    UniGenei Hs.514465.

    3D structure databases

    ProteinModelPortali O75947.
    SMRi O75947. Positions 4-124.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115739. 11 interactions.
    IntActi O75947. 6 interactions.
    MINTi MINT-1407327.
    STRINGi 9606.ENSP00000301587.

    PTM databases

    PhosphoSitei O75947.

    2D gel databases

    OGPi O75947.
    REPRODUCTION-2DPAGE IPI00456049.
    UCD-2DPAGE O75947.

    Proteomic databases

    MaxQBi O75947.
    PaxDbi O75947.
    PeptideAtlasi O75947.
    PRIDEi O75947.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000301587 ; ENSP00000301587 ; ENSG00000167863 . [O75947-1 ]
    ENST00000344546 ; ENSP00000344230 ; ENSG00000167863 . [O75947-2 ]
    GeneIDi 10476.
    KEGGi hsa:10476.
    UCSCi uc002jmn.1. human. [O75947-1 ]
    uc002jmo.1. human. [O75947-2 ]

    Organism-specific databases

    CTDi 10476.
    GeneCardsi GC17M073034.
    HGNCi HGNC:845. ATP5H.
    HPAi HPA042777.
    HPA048459.
    neXtProti NX_O75947.
    PharmGKBi PA25135.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG307464.
    HOGENOMi HOG000267023.
    HOVERGENi HBG050612.
    InParanoidi O75947.
    KOi K02138.
    OMAi MEDYRDA.
    PhylomeDBi O75947.
    TreeFami TF314031.

    Enzyme and pathway databases

    Reactomei REACT_6759. Formation of ATP by chemiosmotic coupling.

    Miscellaneous databases

    GeneWikii ATP5H.
    GenomeRNAii 10476.
    NextBioi 39734.
    PROi O75947.

    Gene expression databases

    ArrayExpressi O75947.
    Bgeei O75947.
    CleanExi HS_ATP5H.
    Genevestigatori O75947.

    Family and domain databases

    InterProi IPR008689. ATPase_F0-cplx_dsu_mt.
    [Graphical view ]
    Pfami PF05873. Mt_ATP-synt_D. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF005514. ATPase_F0_D_mt. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "cDNA cloning, and chromosomal localization of a human F1F0-type ATPase subunit d."
      Lee H.C., Park D.S., Lee C.M., Cho W.K., Ahn H.J., Lee M.Y., Hwang M.Y., Jin S.W., Sohn U.I.K.
      Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Thymus.
    2. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
      Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
      , Gu J., Chen S.-J., Chen Z.
      Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Umbilical cord blood.
    3. Mao Y.M., Xie Y., Ying K.
      Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Fetal brain.
    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] (ISOFORM 1).
      Tissue: Uterus.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORMS 1 AND 2).
      Tissue: Brain and Pancreas.
    7. Lubec G., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 10-25; 33-58; 64-72; 79-109 AND 124-144.
      Tissue: Fetal brain cortex.
    8. "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-85; LYS-95; LYS-117 AND LYS-149, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiATP5H_HUMAN
    AccessioniPrimary (citable) accession number: O75947
    Secondary accession number(s): B2R5L6, Q9H3J4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 137 of the entry and version 3 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 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3