EGLN3

EGLN3
Identifiers
Aliases	EGLN3, HIFP4H3, HIFPH3, PHD3, egl-9 family hypoxia inducible factor 3
External IDs	OMIM: 606426; MGI: 1932288; HomoloGene: 32531; GeneCards: EGLN3; OMA:EGLN3 - orthologs
Gene location (Human) Chr. Chromosome 14 (human) Band 14q13.1 Start 33,924,227 bp End 34,462,774 bp
Gene location (Mouse) Chr. Chromosome 12 (mouse) Band 12|12 C1 Start 54,225,767 bp End 54,250,646 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in skin of leg skin of abdomen apex of heart left ventricle right auricle ventricular zone right uterine tube rectum C1 segment amygdala Top expressed in temporal muscle masseter muscle esophagus mucous cell of stomach conjunctival fornix digastric muscle epithelium of small intestine epithelium of stomach pyloric antrum sternocleidomastoid muscle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function 2-oxoglutarate-dependent dioxygenase activity iron ion binding L-ascorbic acid binding dioxygenase activity metal ion binding protein binding oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen oxidoreductase activity peptidyl-proline 4-dioxygenase activity Cellular component nucleoplasm nucleus cytoplasm cytosol Biological process response to hypoxia regulation of neuron apoptotic process peptidyl-proline hydroxylation to 4-hydroxy-L-proline cellular response to DNA damage stimulus regulation of cell population proliferation regulation of transcription from RNA polymerase II promoter in response to hypoxia activation of cysteine-type endopeptidase activity involved in apoptotic process protein hydroxylation apoptotic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 112399 112407 Ensembl ENSG00000129521 ENSMUSG00000035105 UniProt Q9H6Z9 Q91UZ4 RefSeq (mRNA) NM_001308103 NM_022073 NM_028133 RefSeq (protein) NP_001295032 NP_071356 NP_082409 Location (UCSC) Chr 14: 33.92 – 34.46 Mb Chr 12: 54.23 – 54.25 Mb PubMed search
Wikidata
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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

• Semenza GL (October 2001). "HIF-1, O(2), and the 3 PHDs: how animal cells signal hypoxia to the nucleus". Cell. 107 (1): 1–3. doi:10.1016/S0092-8674(01)00518-9. PMID 11595178.
• Maruyama K, Sugano S (January 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Taylor MS (September 2001). "Characterization and comparative analysis of the EGLN gene family". Gene. 275 (1): 125–32. doi:10.1016/S0378-1119(01)00633-3. PMID 11574160.
• Epstein AC, Gleadle JM, McNeill LA, Hewitson KS, O'Rourke J, Mole DR, Mukherji M, Metzen E, Wilson MI, Dhanda A, Tian YM, Masson N, Hamilton DL, Jaakkola P, Barstead R, Hodgkin J, Maxwell PH, Pugh CW, Schofield CJ, Ratcliffe PJ (October 2001). "C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation". Cell. 107 (1): 43–54. doi:10.1016/S0092-8674(01)00507-4. PMID 11595184.
• Bruick RK, McKnight SL (November 2001). "A conserved family of prolyl-4-hydroxylases that modify HIF". Science. 294 (5545): 1337–40. Bibcode:2001Sci...294.1337B. doi:10.1126/science.1066373. PMID 11598268. S2CID 9695199.
• Oehme F, Ellinghaus P, Kolkhof P, Smith TJ, Ramakrishnan S, Hütter J, Schramm M, Flamme I (August 2002). "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. doi:10.1016/S0006-291X(02)00862-8. PMID 12163023.
• Metzen E, Berchner-Pfannschmidt U, Stengel P, Marxsen JH, Stolze I, Klinger M, Huang WQ, Wotzlaw C, Hellwig-Bürgel T, Jelkmann W, Acker H, Fandrey J (April 2003). "Intracellular localisation of human HIF-1 alpha hydroxylases: implications for oxygen sensing". Journal of Cell Science. 116 (Pt 7): 1319–26. doi:10.1242/jcs.00318. PMID 12615973. S2CID 13698068.
• Cioffi CL, Liu XQ, Kosinski PA, Garay M, Bowen BR (April 2003). "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. doi:10.1016/S0006-291X(03)00453-4. PMID 12670503.
• Aprelikova O, Chandramouli GV, Wood M, Vasselli JR, Riss J, Maranchie JK, Linehan WM, Barrett JC (June 2004). "Regulation of HIF prolyl hydroxylases by hypoxia-inducible factors". Journal of Cellular Biochemistry. 92 (3): 491–501. doi:10.1002/jcb.20067. PMID 15156561. S2CID 24455956.
• Appelhoff RJ, Tian YM, Raval RR, Turley H, Harris AL, Pugh CW, Ratcliffe PJ, Gleadle JM (September 2004). "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. doi:10.1074/jbc.M406026200. PMID 15247232.
• Masson N, Appelhoff RJ, Tuckerman JR, Tian YM, Demol H, Puype M, Vandekerckhove J, Ratcliffe PJ, Pugh CW (July 2004). "The HIF prolyl hydroxylase PHD3 is a potential substrate of the TRiC chaperonin". FEBS Letters. 570 (1–3): 166–70. doi:10.1016/j.febslet.2004.06.040. PMID 15251459.
• Baek JH, Mahon PC, Oh J, Kelly B, Krishnamachary B, Pearson M, Chan DA, Giaccia AJ, Semenza GL (February 2005). "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. doi:10.1016/j.molcel.2005.01.011. PMID 15721254.
• Lee S, Nakamura E, Yang H, Wei W, Linggi MS, Sajan MP, Farese RV, Freeman RS, Carter BD, Kaelin WG, Schlisio S (August 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, Stahl RA, Wolf G (March 2006). "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. doi:10.1074/jbc.M513751200. PMID 16407229.
• Nakayama K, Gazdoiu S, Abraham R, Pan ZQ, Ronai Z (January 2007). "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. doi:10.1042/BJ20061135. PMC 1698661. PMID 16958618.