EGLN1
Egl nine homolog 1 (C. elegans) | |||||||||||||
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PDB rendering based on 2g19. | |||||||||||||
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Identifiers | |||||||||||||
Symbols | EGLN1 ; C1orf12; DKFZp761F179; ECYT3; HIFPH2; PHD2; SM-20; SM20; ZMYND6 | ||||||||||||
External IDs | Template:OMIM5 HomoloGene: 56936 | ||||||||||||
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RNA expression pattern | |||||||||||||
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Template:GNF Ortholog box | |||||||||||||
Species | Human | Mouse | |||||||||||
Entrez | n/a | n/a | |||||||||||
Ensembl | n/a | n/a | |||||||||||
UniProt | n/a | n/a | |||||||||||
RefSeq (mRNA) | n/a | n/a | |||||||||||
RefSeq (protein) | n/a | n/a | |||||||||||
Location (UCSC) | n/a | n/a | |||||||||||
PubMed search | n/a | n/a |
Egl nine homolog 1 (C. elegans), also known as EGLN1, is a human gene.[1]
References
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.
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