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Literature summary for 1.14.11.2 extracted from

  • Qi, H.H.; Ongusaha, P.P.; Myllyharju, J.; Cheng, D.; Pakkanen, O.; Shi, Y.; Lee, S.W.; Peng, J.; Shi, Y.
    Prolyl 4-hydroxylation regulates Argonaute 2 stability (2008), Nature, 455, 421-424.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.14.11.2

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
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 Homo sapiens 5737
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Argonaute 2 + 2-oxoglutarate + O2 Homo sapiens regulation of Ago 2 protein activity via substrate protein stability involving Ago Pro700 residue, the Ago protein mutant P700A is destabilized, overview 4-hydroxyproline-Argonaute 2 + succinate + CO2
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 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
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 three isoforms I, II, III of the alpha-subunit
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Source Tissue

Source Tissue Comment Organism Textmining
293ET cell
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 Homo sapiens
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HeLa cell
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 Homo sapiens
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Argonaute 2 + 2-oxoglutarate + O2 regulation of Ago 2 protein activity via substrate protein stability involving Ago Pro700 residue, the Ago protein mutant P700A is destabilized, overview Homo sapiens 4-hydroxyproline-Argonaute 2 + succinate + CO2
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 ?
Argonaute protein + 2-oxoglutarate + O2 i.e. GERp95 or Golgi endoplasmic reticulum protein 95 kDa. Recombinant substrate proteins expressed in HeLa S3 cells. Ago2 is a cytoplasmically exposed, peripheral membrane protein that exists in a protease-resistant complex. Hydroxylation of Pro700, which is important for Ago2 stability, but not of Ago1 or Ago3 stability, identification by mass spectrometric analysis. In vitro, both Ago2 and Ago4 seem to be more efficiently hydroxylated than Ago1 and Ago3 by recombinant human isozyme C-P4H(I) Homo sapiens 4-hydroxyproline-Argonaute protein + succinate + CO2
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 ?
additional information C-P4H catalyses proline hydroxylation of collagens in the X-Pro-Gly (X-P-G) triplets Homo sapiens ?
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Synonyms

Synonyms Comment Organism
P4H
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 Homo sapiens
prolyl 4-hydroxylase
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 Homo sapiens

General Information

General Information Comment Organism
malfunction reduced enzyme activity leads to reduced steady-state level of Ago2 protein. Hydroxylation has an impact on Ago2 P-body and stress granule localization, depletion of the C-P4H-I subunits by RNAi or genetic ablation of P4H-alphaI in MEF cells reduced Ago2 P-body localization Homo sapiens
physiological function P4H regulates the localization and action of Argonaute proteins, i.e. Ago proteins, essential components of the RNA-induced silencing complexes. Proteins such as Dicer, TRBP, MOV10, RHA, RCK/p54 and KIAA1093 associate with Ago proteins and participate in small RNA processing, RISC loading and localization of Ago proteins in the cytoplasmic messenger RNA processing bodies, mechanism, overview Homo sapiens