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
Gene location (Human)
Chr.	Chromosome 14 (human)[1]
End	34,462,774 bp[1]
Gene location (Mouse)
Chr.	Chromosome 12 (mouse)[2]
End	54,203,860 bp[2]
RNA expression pattern
	More reference expression data
Gene ontology
Molecular function	• 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; • iron ion binding; • L-ascorbic acid binding; • dioxygenase activity; • metal ion binding; • GO:0001948 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; • cell 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 proliferation; • regulation of transcription from RNA polymerase II promoter in response to hypoxia; • activation of cysteine-type endopeptidase activity involved in apoptotic process; • oxidation-reduction process; • protein hydroxylation; • apoptotic process;
	Sources:Amigo / QuickGO
Orthologs
	112399
	112407
	ENSG00000129521
	ENSMUSG00000035105
	Q9H6Z9
	Q91UZ4
	NM_001308103; NM_022073
	NM_028133
	NP_001295032; NP_071356
	NP_082409
	Wikidata
View/Edit Human	View/Edit Mouse

Egl nine homolog 3 is a protein that in humans is encoded by the EGLN3 gene.[5] ELGN3 is a member of the superfamily of alpha-ketoglutarate-dependent hydroxylases, which are non-haem iron-containing proteins.

References

GRCh38: Ensembl release 89: ENSG00000129521 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000035105 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Entrez Gene: EGLN3 egl nine homolog 3 (C. elegans)".

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. doi:10.1126/science.1066373. PMID 11598268.
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.
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.
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.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000129521 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000035105 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[entrez-5] "Entrez Gene: EGLN3 egl nine homolog 3 (C. elegans)".

Oxidoreductases: dioxygenases, including steroid hydroxylases (EC 1.14)
1.14.11: 2-oxoglutarate	Prolyl hydroxylase HIF prolyl-hydroxylase EGLN1 EGLN2 EGLN3 P4HTM Lysyl hydroxylase
1.14.13: NADH or NADPH	Flavin-containing monooxygenase FMO1 FMO2 FMO3 FMO4 FMO5 Nitric oxide synthase NOS1 NOS2 NOS3 Cholesterol 7 alpha-hydroxylase Methane monooxygenase 3A4 14α-demethylase 24-hydroxycholesterol 7α-hydroxylase
1.14.14: reduced flavin or flavoprotein	19A1 2D6 2E1
1.14.15: reduced iron-sulfur protein	11B1 11B2 11A1
1.14.16: reduced pteridine (BH4 dependent)	Phenylalanine hydroxylase Tyrosine hydroxylase Tryptophan hydroxylase
1.14.17: reduced ascorbate	Dopamine beta-hydroxylase
1.14.18-19: other	Tyrosinase Stearoyl-CoA desaturase-1
1.14.99 - miscellaneous	Cyclooxygenase Heme oxygenase (HMOX1) Squalene monooxygenase 17A1 21A2 Ecdysone 20-monooxygenase

Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

EGLN3

References

Further reading