| Post Translational Modifications | S-nitrosylation inhibits the enzyme activity up to 60% under aerobic conditions. Chelation of Fe(2+) has no effect on the S-nitrosylation. It is uncertain whether nitrosylation occurs on Cys-323 or Cys-326. |
| Function | Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. Also hydroxylates HIF2A. Has a preference for the CODD site for both HIF1A and HIF1B. Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes. EGLN1 is the most important isozyme under normoxia and, through regulating the stability of HIF1, involved in various hypoxia-influenced processes such as angiogenesis in retinal and cardiac functionality. Target proteins are preferentially recognized via a LXXLAP motif. |
| Protein Name | Egl Nine Homolog 1Hypoxia-Inducible Factor Prolyl Hydroxylase 2Hif-Ph2Hif-Prolyl Hydroxylase 2Hph-2Prolyl Hydroxylase Domain-Containing Protein 2Phd2Sm-20 |
| Database Links | Reactome: R-HSA-1234176 |
| Cellular Localisation | CytoplasmNucleusMainly CytoplasmicShuttles Between The Nucleus And CytoplasmNuclear Export Requires Functional Xpo1 |
| Alternative Protein Names | Egl Nine Homolog 1 proteinHypoxia-Inducible Factor Prolyl Hydroxylase 2 proteinHif-Ph2 proteinHif-Prolyl Hydroxylase 2 proteinHph-2 proteinProlyl Hydroxylase Domain-Containing Protein 2 proteinPhd2 proteinSm-20 proteinEGLN1 proteinC1orf12 proteinPNAS-118 proteinPNAS-137 protein |
Information sourced from Uniprot.org
