EGLN1

From Wikipedia, the free encyclopedia

Egl nine homolog 1 (C. elegans)

PDB rendering based on 2g19.

Available structures: 2g19, 2g1m, 2hbt, 2hbu

Identifiers

Symbol(s)

EGLN1; C1orf12; DKFZp761F179; ECYT3; HIFPH2; PHD2; SM-20; SM20; ZMYND6

External IDs

OMIM: 606425 HomoloGene: 56936

Gene ontology
Molecular Function:	• iron ion binding • protein binding • zinc ion binding • oxidoreductase activity • oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen • 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 • metal ion binding
Cellular Component:	• cytosol
Biological Process:	• protein metabolic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

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Refseq

NM_022051 (mRNA)
NP_071334 (protein)

n/a (mRNA)
n/a (protein)

Location

Chr 1: 229.57 - 229.63 Mb

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Pubmed search

[1]

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Egl nine homolog 1 (C. elegans), also known as EGLN1, is a human gene.^[1]

[edit] References

^ Entrez Gene: EGLN1 egl nine homolog 1 (C. elegans).

[edit] 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. PMID 11595178.
Wax SD, Tsao L, Lieb ME, et al. (1996). "SM-20 is a novel 40-kd protein whose expression in the arterial wall is restricted to smooth muscle.". Lab. Invest. 74 (4): 797–808. PMID 8606489.
Dupuy D, Aubert I, Dupérat VG, et al. (2001). "Mapping, characterization, and expression analysis of the SM-20 human homologue, c1orf12, and identification of a novel related gene, SCAND2.". Genomics 69 (3): 348–54. doi:10.1006/geno.2000.6343. PMID 11056053.
Taylor MS (2001). "Characterization and comparative analysis of the EGLN gene family.". Gene 275 (1): 125–32. 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. PMID 11595184.
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.
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. 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. 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. 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. PMID 12670503.
Berra E, Benizri E, Ginouvès A, et al. (2003). "HIF prolyl-hydroxylase 2 is the key oxygen sensor setting low steady-state levels of HIF-1alpha in normoxia.". EMBO J. 22 (16): 4082–90. doi:10.1093/emboj/cdg392. PMID 12912907.
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.
Appelhoff RJ, Tian YM, Raval RR, et al. (2004). "Differential function of the prolyl hydroxylases PHD1, PHD2, and PHD3 in the regulation of hypoxia-inducible factor.". J. Biol. Chem. 279 (37): 38458–65. doi:10.1074/jbc.M406026200. PMID 15247232.
Metzen E, Stiehl DP, Doege K, et al. (2006). "Regulation of the prolyl hydroxylase domain protein 2 (phd2/egln-1) gene: identification of a functional hypoxia-responsive element.". Biochem. J. 387 (Pt 3): 711–7. doi:10.1042/BJ20041736. PMID 15563275.
Baek JH, Mahon PC, Oh J, et al. (2005). "OS-9 interacts with hypoxia-inducible factor 1alpha and prolyl hydroxylases to promote oxygen-dependent degradation of HIF-1alpha.". Mol. Cell 17 (4): 503–12. doi:10.1016/j.molcel.2005.01.011. PMID 15721254.
Ozer A, Wu LC, Bruick RK (2005). "The candidate tumor suppressor ING4 represses activation of the hypoxia inducible factor (HIF).". Proc. Natl. Acad. Sci. U.S.A. 102 (21): 7481–6. doi:10.1073/pnas.0502716102. PMID 15897452.
Choi KO, Lee T, Lee N, et al. (2006). "Inhibition of the catalytic activity of hypoxia-inducible factor-1alpha-prolyl-hydroxylase 2 by a MYND-type zinc finger.". Mol. Pharmacol. 68 (6): 1803–9. doi:10.1124/mol.105.015271. PMID 16155211.
To KK, Huang LE (2006). "Suppression of hypoxia-inducible factor 1alpha (HIF-1alpha) transcriptional activity by the HIF prolyl hydroxylase EGLN1.". J. Biol. Chem. 280 (45): 38102–7. doi:10.1074/jbc.M504342200. PMID 16157596.
Kato H, Inoue T, Asanoma K, et al. (2006). "Induction of human endometrial cancer cell senescence through modulation of HIF-1alpha activity by EGLN1.". Int. J. Cancer 118 (5): 1144–53. doi:10.1002/ijc.21488. PMID 16161047.