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 33,924,227bp End 34,462,774bp
Gene location (Mouse) Chr. Chromosome 12 (mouse) Band 12|12 C1 Start 54,225,767bp End 54,250,646bp
RNA expressionpattern 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 PubMedsearch
Wikidata
View/Edit Human View/Edit Mouse

Egl nine homolog 3is aproteinthat in humans is encoded by theEGLN3gene.ELGN3 is a member of the superfamily ofAlpha -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.PMID11595178.
• 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.PMID8125298.
• 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.PMID9373149.
• 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.PMID11574160.
• 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.PMID11595184.
• 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.PMID11598268.S2CID9695199.
• 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.PMID12163023.
• 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.PMID12615973.S2CID13698068.
• 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.PMID12670503.
• 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.PMID15156561.S2CID24455956.
• 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.PMID15247232.
• 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.PMID15251459.
• 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 1 Alpha and prolyl hydroxylases to promote oxygen-dependent degradation of HIF-1 Alpha".Molecular Cell.17(4): 503–12.doi:10.1016/j.molcel.2005.01.011.PMID15721254.
• 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.PMID16098468.
• 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.PMID16407229.
• 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.PMC1698661.PMID16958618.