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Description for Protein ATP5I

ATP synthase, H+ transporting, mitochondrial Fo complex, subunit E
No Interacting Proteins
Icon Book Platelet Evidence (proteome studies/others : 2/0)
(membrane: 1; platelet: 1)
Summary:
Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. It is composed of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, Fo, which comprises the proton channel. The F1 complex consists of 5 different subunits (alpha, beta, gamma, delta, and epsilon) assembled in a ratio of 3 alpha, 3 beta, and a single representative of the other 3. The Fo seems to have nine subunits (a, b, c, d, e, f, g, F6 and 8). This gene encodes the e subunit of the Fo complex. Alternative splicing results in multiple transcript variants. (PubMed Links)
Domains and Motifs:
  • CC: Coiled Coil
    • Gene Ontology:
    Gene Ontology Annotations
    KEGG - Enzyme ID(s):
    3.6.3.14
    KEGG - Orthology:
    K02129
    KEGG - Pathway(s):
    hsa00190; hsa01100
    (The yellow boxes represents platelet proteins)
    Nomenclature / Alternative Names:
    ATP synthase, H+ transporting, mitochondrial F0 complex, subunit E; F1F0-ATP synthase, e subunit gene; ATP5K; ATP synthase e chain, mitochondrial; MGC12532; EC 3.6.3.14
    Approved Symbol:
    ATP5I
    (De-) Phosphorylations:
    Total (de-) phosphorylation sites: 2
    Human (de-) phosphorylation sites: 2; No platelet phosphorylation sites
    Phosphorylation Targets:
    Total phosphorylation targets: 0
    Human phosphorylation targets: 0;Predicted platelet targets: 0
    		Protein Characteristics:
    Isoform-specific Information
    Icon DrugsAssociated Drugs (DrugBank Accession):

    None Available

    Associated Genetic Diseases:

    None Available
    		Predicted Transmembrane Domains:
  • Isoform 1 : 0
    • Additional Identifiers:

    HPRD: 03308 Entrez Gene ID: 521 OMIM ID: 601519 Swissprot Accession: P56385;