Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cytoplasm | - |
Homo sapiens | 5737 | - |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
three isoforms I, II, III of the alpha-subunit | - |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
293ET cell | - |
Homo sapiens | - |
HeLa cell | - |
Homo sapiens | - |
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 | - |
? | |
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 | - |
? | |
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 | Comment | Organism |
---|---|---|
P4H | - |
Homo sapiens |
prolyl 4-hydroxylase | - |
Homo sapiens |
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 |