EGLN3

From Wikipedia, the free encyclopedia

Egl nine homolog 3 (C. elegans)

Identifiers

EGLN3; FLJ21620; HIFPH3; MGC125998; MGC125999; PHD3

External IDs

OMIM: 606426 MGI: 1932288 HomoloGene: 32531

Gene ontology
Molecular Function:	• iron ion binding • protein 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:	• nucleus
Biological Process:	• apoptosis • protein metabolic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_022073 (mRNA)
NP_071356 (protein)

NM_028133 (mRNA)
NP_082409 (protein)

Location

Chr 14: 33.46 - 33.49 Mb

Chr 12: 55.1 - 55.13 Mb

Pubmed search

[1]

[2]

Egl nine homolog 3 (C. elegans), also known as EGLN3, is a human gene.^[1]

[edit] References

^ Entrez Gene: EGLN3 egl nine homolog 3 (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.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. PMID 8125298.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. PMID 9373149.
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.
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.
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.
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.
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.
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.
Masson N, Appelhoff RJ, Tuckerman JR, et al. (2004). "The HIF prolyl hydroxylase PHD3 is a potential substrate of the TRiC chaperonin.". FEBS Lett. 570 (1-3): 166–70. doi:10.1016/j.febslet.2004.06.040. PMID 15251459.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
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.
Lee S, Nakamura E, Yang H, et al. (2005). "Neuronal apoptosis linked to EglN3 prolyl hydroxylase and familial pheochromocytoma genes: developmental culling and cancer.". Cancer Cell 8 (2): 155–67. doi:10.1016/j.ccr.2005.06.015. PMID 16098468.
Hopfer U, Hopfer H, Jablonski K, et al. (2006). "The novel WD-repeat protein Morg1 acts as a molecular scaffold for hypoxia-inducible factor prolyl hydroxylase 3 (PHD3).". J. Biol. Chem. 281 (13): 8645–55. doi:10.1074/jbc.M513751200. PMID 16407229.
Nakayama K, Gazdoiu S, Abraham R, et al. (2007). "Hypoxia-induced assembly of prolyl hydroxylase PHD3 into complexes: implications for its activity and susceptibility for degradation by the E3 ligase Siah2.". Biochem. J. 401 (1): 217–26. doi:10.1042/BJ20061135. PMID 16958618.