EGLN2

Egl-9 family hypoxia-inducible factor 2
Identifiers
Symbols	EGLN2 ; EIT6; HIF-PH1; HIFPH1; HPH-1; HPH-3; PHD1
External IDs	OMIM: 606424 MGI: 1932287 HomoloGene: 14204 ChEMBL: 3028 GeneCards: EGLN2 Gene
EC number	1.14.11.29
Gene ontology Molecular function • protein binding • ferrous iron binding • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors • oxygen sensor activity • L-ascorbic acid binding • peptidyl-proline 4-dioxygenase activity Cellular component • nucleus • nucleoplasm • cytosol Biological process • regulation of cell growth • response to hypoxia • peptidyl-proline hydroxylation to 4-hydroxy-L-proline • intracellular estrogen receptor signaling pathway • regulation of neuron apoptotic process • cell redox homeostasis • positive regulation of protein catabolic process • oxidation-reduction process • regulation of transcription from RNA polymerase II promoter in response to hypoxia • cellular response to hypoxia Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	112398	112406
Ensembl	ENSG00000269858	ENSMUSG00000058709
UniProt	Q96KS0	Q91YE2
RefSeq (mRNA)	NM_017555	NM_053208
RefSeq (protein)	NP_444274	NP_444438
Location (UCSC)	Chr 19: 40.8 – 40.81 Mb	Chr 7: 27.16 – 27.17 Mb
PubMed search

Egl nine homolog 2 is a protein that in humans is encoded by the EGLN2 gene.^[1]

The hypoxia inducible factor (HIF) is a transcriptional complex which is involved in oxygen homeostasis. At normal oxygen levels, the alpha subunit of HIF is targeted for degradation by prolyl hydroxylation.

This gene encodes an enzyme responsible for this posttranslational modification. Multiple alternatively spliced variants, encoding the same protein, have been identified.^[1]

References

1. "Entrez Gene: EGLN2 egl nine homolog 2 (C. elegans)".

Further reading

• Semenza GL (2001). "HIF-1, O(2), and the 3 PHDs: how animal cells signal hypoxia to the nucleus". Cell 107 (1): 1–3. doi:10.1016/S0092-8674(01)00518-9. PMID 11595178.
• Hartley JL, Temple GF, Brasch MA (2001). "DNA Cloning Using In Vitro Site-Specific Recombination". Genome Res. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
• Wiemann S, Weil B, Wellenreuther R; et al. (2001). "Toward a Catalog of Human Genes and Proteins: Sequencing and Analysis of 500 Novel Complete Protein Coding Human cDNAs". Genome Res. 11 (3): 422–35. doi:10.1101/gr.GR1547R. PMC 311072. PMID 11230166.
• Jaakkola P, Mole DR, Tian YM; et al. (2001). "Targeting of HIF-alpha to the von Hippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation". Science 292 (5516): 468–72. doi:10.1126/science.1059796. PMID 11292861.
• Ivan M, Kondo K, Yang H; et al. (2001). "HIFalpha targeted for VHL-mediated destruction by proline hydroxylation: implications for O2 sensing". Science 292 (5516): 464–8. doi:10.1126/science.1059817. PMID 11292862.
• Taylor MS (2001). "Characterization and comparative analysis of the EGLN gene family". Gene 275 (1): 125–32. doi:10.1016/S0378-1119(01)00633-3. PMID 11574160.
• Epstein AC, Gleadle JM, McNeill LA; et al. (2001). "C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation". Cell 107 (1): 43–54. doi:10.1016/S0092-8674(01)00507-4. PMID 11595184.
• Bruick RK, McKnight SL (2001). "A conserved family of prolyl-4-hydroxylases that modify HIF". Science 294 (5545): 1337–40. doi:10.1126/science.1066373. PMID 11598268.
• Seth P, Krop I, Porter D, Polyak K (2002). "Novel estrogen and tamoxifen induced genes identified by SAGE (Serial Analysis of Gene Expression)". Oncogene 21 (5): 836–43. doi:10.1038/sj.onc.1205113. PMID 11850811.
• Min JH, Yang H, Ivan M; et al. (2002). "Structure of an HIF-1alpha -pVHL complex: hydroxyproline recognition in signaling". Science 296 (5574): 1886–9. doi:10.1126/science.1073440. PMID 12004076.
• McNeill LA, Hewitson KS, Gleadle JM; et al. (2002). "The use of dioxygen by HIF prolyl hydroxylase (PHD1)". Bioorg. Med. Chem. Lett. 12 (12): 1547–50. doi:10.1016/S0960-894X(02)00219-6. PMID 12039559.
• Oehme F, Ellinghaus P, Kolkhof P; et al. (2002). "Overexpression of PH-4, a novel putative proline 4-hydroxylase, modulates activity of hypoxia-inducible transcription factors". Biochem. Biophys. Res. Commun. 296 (2): 343–9. doi:10.1016/S0006-291X(02)00862-8. PMID 12163023.
• Ivan M, Haberberger T, Gervasi DC; et al. (2002). "Biochemical purification and pharmacological inhibition of a mammalian prolyl hydroxylase acting on hypoxia-inducible factor". Proc. Natl. Acad. Sci. U.S.A. 99 (21): 13459–64. doi:10.1073/pnas.192342099. PMC 129695. PMID 12351678.
• Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Metzen E, Berchner-Pfannschmidt U, Stengel P; et al. (2003). "Intracellular localisation of human HIF-1 alpha hydroxylases: implications for oxygen sensing". J. Cell. Sci. 116 (Pt 7): 1319–26. doi:10.1242/jcs.00318. PMID 12615973.
• Cioffi CL, Liu XQ, Kosinski PA; et al. (2003). "Differential regulation of HIF-1 alpha prolyl-4-hydroxylase genes by hypoxia in human cardiovascular cells". Biochem. Biophys. Res. Commun. 303 (3): 947–53. doi:10.1016/S0006-291X(03)00453-4. PMID 12670503.
• Ota T, Suzuki Y, Nishikawa T; et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• Aprelikova O, Chandramouli GV, Wood M; et al. (2004). "Regulation of HIF prolyl hydroxylases by hypoxia-inducible factors". J. Cell. Biochem. 92 (3): 491–501. doi:10.1002/jcb.20067. PMID 15156561.
• Colland F, Jacq X, Trouplin V; et al. (2004). "Functional Proteomics Mapping of a Human Signaling Pathway". Genome Res. 14 (7): 1324–32. doi:10.1101/gr.2334104. PMC 442148. PMID 15231748.