EGLN2

Identifiers

EGLN2, EIT6, HIF-PH1, HIFPH1, HPH-1, HPH-3, PHD1, egl-9 family hypoxia inducible factor 2

External IDs

MGI: 1932287 HomoloGene: 14204 GeneCards: EGLN2

Gene ontology
Molecular function	• 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 • L-ascorbic acid binding • iron ion binding • dioxygenase activity • metal ion binding • protein binding • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen • oxidoreductase activity • ferrous iron binding • oxygen sensor activity • peptidyl-proline 4-dioxygenase activity
Cellular component	• nucleoplasm • nucleus
Biological process	• response to hypoxia • positive regulation of protein catabolic process • regulation of neuron apoptotic process • peptidyl-proline hydroxylation to 4-hydroxy-L-proline • cell redox homeostasis • regulation of cell growth • regulation of transcription from RNA polymerase II promoter in response to hypoxia • oxidation-reduction process • intracellular estrogen receptor signaling pathway
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_080732 NM_017555 NM_053046


NM_053208

RefSeq (protein)


NP_444274 NP_542770


NP_444438

Location (UCSC)

Chr 19: 40.8 – 40.81 Mb

Chr 7: 27.16 – 27.17 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

Egl nine homolog 2 is a protein that in humans is encoded by the EGLN2 gene.^[3]

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.^[3]

References

Semenza GL (2001). "HIF-1, O(2), and the 3 PHDs: how animal cells signal hypoxia to the nucleus". Cell. 107 (1): 1–3. PMID 11595178. doi:10.1016/S0092-8674(01)00518-9.
Hartley JL, Temple GF, Brasch MA (2001). "DNA Cloning Using In Vitro Site-Specific Recombination". Genome Res. 10 (11): 1788–95. PMC 310948 . PMID 11076863. doi:10.1101/gr.143000.
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. PMC 311072 . PMID 11230166. doi:10.1101/gr.GR1547R.
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. PMID 11292861. doi:10.1126/science.1059796.
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. PMID 11292862. doi:10.1126/science.1059817.
Taylor MS (2001). "Characterization and comparative analysis of the EGLN gene family". Gene. 275 (1): 125–32. PMID 11574160. doi:10.1016/S0378-1119(01)00633-3.
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. PMID 11595184. doi:10.1016/S0092-8674(01)00507-4.
Bruick RK, McKnight SL (2001). "A conserved family of prolyl-4-hydroxylases that modify HIF". Science. 294 (5545): 1337–40. PMID 11598268. doi:10.1126/science.1066373.
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. PMID 11850811. doi:10.1038/sj.onc.1205113.
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. PMID 12004076. doi:10.1126/science.1073440.
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. PMID 12039559. doi:10.1016/S0960-894X(02)00219-6.
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. PMID 12163023. doi:10.1016/S0006-291X(02)00862-8.
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. PMC 129695 . PMID 12351678. doi:10.1073/pnas.192342099.
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. PMC 139241 . PMID 12477932. doi:10.1073/pnas.242603899.
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. PMID 12615973. doi:10.1242/jcs.00318.
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. PMID 12670503. doi:10.1016/S0006-291X(03)00453-4.
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. PMID 14702039. doi:10.1038/ng1285.
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. PMID 15156561. doi:10.1002/jcb.20067.
Colland F, Jacq X, Trouplin V, et al. (2004). "Functional Proteomics Mapping of a Human Signaling Pathway". Genome Res. 14 (7): 1324–32. PMC 442148 . PMID 15231748. doi:10.1101/gr.2334104.

Oxidoreductases: dioxygenases, including steroid hydroxylases (EC 1.14)
1.14.11: 2-oxoglutarate	Prolyl hydroxylase Lysyl hydroxylase
1.14.13: NADH or NADPH	Flavin-containing monooxygenase FMO1 FMO2 FMO3 FMO4 FMO5 Nitric oxide synthase NOS1 NOS2 NOS3 Cholesterol 7 alpha-hydroxylase Methane monooxygenase 3A4 Lanosterol 14 alpha-demethylase 24-hydroxycholesterol 7α-hydroxylase
1.14.14: reduced flavin or flavoprotein	19A1 2D6 2E1
1.14.15: reduced iron-sulfur protein	11B1 11B2 11A1
1.14.16: reduced pteridine (BH4 dependent)	Phenylalanine hydroxylase Tyrosine hydroxylase Tryptophan hydroxylase
1.14.17: reduced ascorbate	Dopamine beta-hydroxylase
1.14.18-19: other	Tyrosinase Stearoyl-CoA desaturase-1
1.14.99 - miscellaneous	Cyclooxygenase Heme oxygenase (HMOX1) Squalene monooxygenase 17A1 21A2

Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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EGLN2

References

Further reading