Biology:EGLN3

Short description: Protein-coding gene in the species Homo sapiens

Generic protein structure example

Egl nine homolog 3 is a protein that in humans is encoded by the EGLN3 gene. ELGN3 is a member of the superfamily of alpha-ketoglutarate-dependent hydroxylases, which are non-haem iron-containing proteins.

Further reading

• "HIF-1, O(2), and the 3 PHDs: how animal cells signal hypoxia to the nucleus". Cell 107 (1): 1–3. October 2001. doi:10.1016/S0092-8674(01)00518-9. PMID 11595178. 
• "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4. January 1994. doi:10.1016/0378-1119(94)90802-8. PMID 8125298. 
• "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. October 1997. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149. 
• "Characterization and comparative analysis of the EGLN gene family". Gene 275 (1): 125–32. September 2001. doi:10.1016/S0378-1119(01)00633-3. PMID 11574160. 
• "C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation". Cell 107 (1): 43–54. October 2001. doi:10.1016/S0092-8674(01)00507-4. PMID 11595184. 
• "A conserved family of prolyl-4-hydroxylases that modify HIF". Science 294 (5545): 1337–40. November 2001. doi:10.1126/science.1066373. PMID 11598268. Bibcode: 2001Sci...294.1337B. 
• "Overexpression of PH-4, a novel putative proline 4-hydroxylase, modulates activity of hypoxia-inducible transcription factors". Biochemical and Biophysical Research Communications 296 (2): 343–9. August 2002. doi:10.1016/S0006-291X(02)00862-8. PMID 12163023. 
• "Intracellular localisation of human HIF-1 alpha hydroxylases: implications for oxygen sensing". Journal of Cell Science 116 (Pt 7): 1319–26. April 2003. doi:10.1242/jcs.00318. PMID 12615973. 
• "Differential regulation of HIF-1 alpha prolyl-4-hydroxylase genes by hypoxia in human cardiovascular cells". Biochemical and Biophysical Research Communications 303 (3): 947–53. April 2003. doi:10.1016/S0006-291X(03)00453-4. PMID 12670503. 
• "Regulation of HIF prolyl hydroxylases by hypoxia-inducible factors". Journal of Cellular Biochemistry 92 (3): 491–501. June 2004. doi:10.1002/jcb.20067. PMID 15156561. https://zenodo.org/record/1229216. 
• "Differential function of the prolyl hydroxylases PHD1, PHD2, and PHD3 in the regulation of hypoxia-inducible factor". The Journal of Biological Chemistry 279 (37): 38458–65. September 2004. doi:10.1074/jbc.M406026200. PMID 15247232. 
• "The HIF prolyl hydroxylase PHD3 is a potential substrate of the TRiC chaperonin". FEBS Letters 570 (1–3): 166–70. July 2004. doi:10.1016/j.febslet.2004.06.040. PMID 15251459. 
• "OS-9 interacts with hypoxia-inducible factor 1alpha and prolyl hydroxylases to promote oxygen-dependent degradation of HIF-1alpha". Molecular Cell 17 (4): 503–12. February 2005. doi:10.1016/j.molcel.2005.01.011. PMID 15721254. 
• "Neuronal apoptosis linked to EglN3 prolyl hydroxylase and familial pheochromocytoma genes: developmental culling and cancer". Cancer Cell 8 (2): 155–67. August 2005. doi:10.1016/j.ccr.2005.06.015. PMID 16098468. 
• "The novel WD-repeat protein Morg1 acts as a molecular scaffold for hypoxia-inducible factor prolyl hydroxylase 3 (PHD3)". The Journal of Biological Chemistry 281 (13): 8645–55. March 2006. doi:10.1074/jbc.M513751200. PMID 16407229. 
• "Hypoxia-induced assembly of prolyl hydroxylase PHD3 into complexes: implications for its activity and susceptibility for degradation by the E3 ligase Siah2". The Biochemical Journal 401 (1): 217–26. January 2007. doi:10.1042/BJ20061135. PMID 16958618.