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Literature summary for 1.14.11.2 extracted from

  • Koivunen, P.; Tiainen, P.; Hyvaerinen, J.; Williams, K.E.; Sormunen, R.; Klaus, S.J.; Kivirikko, K.I.; Myllyharju, J.
    An endoplasmic reticulum transmembrane prolyl 4-hydroxylase is induced by hypoxia and acts on hypoxia-inducible factor alpha (2007), J. Biol. Chem., 282, 30544-30552.
    View publication on PubMed
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Protein Variants

Protein Variants Comment Organism
additional information overexpression in cultured neuroblastoma cells reduces levels of hypoxia-induced factor alpha oxygen-dependent degradation domain reporter constructs, whereas depletion by siRNA increases hypoxia-induced factor alpha protein level. Recombinant enzyme hydroxylates the two critical prolines in hypoxia-induced factor alpha oxygen-dependent degradation domain in vitro, but not prolines in recombinant type I procollagen chains Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum prolyl 4-hydroxylase possesses a transmembrane domain, the catalytic site of enzyme is inside the lumen Homo sapiens 5783
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membrane of endoplasmic reticulum, the catalytic site is inside the lumen Homo sapiens 16020
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Organism

Organism UniProt Comment Textmining
Homo sapiens
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-
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Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein enzyme is N-glycosylated Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
hypoxia-induced factor alpha oxygen-dependent degradation domain L-proline + 2-oxoglutarate + O2
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 Homo sapiens hypoxia-induced factor alpha oxygen-dependent degradation domain L-4-hydroxyproline + succinate + CO2 in vitro hydroxylation of two proline residues, with preference for C-terminal proline ?
additional information no substrate: prolines in recombinant type I procollagen chains Homo sapiens ?
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 ?