EGLN2: Difference between revisions

EGLN2
Identifiers
Aliases	EGLN2, EIT6, HIF-PH1, HIFPH1, HPH-1, HPH-3, PHD1, egl-9 family hypoxia inducible factor 2, EIT-6
External IDs	OMIM: 606424; MGI: 1932287; HomoloGene: 14204; GeneCards: EGLN2; OMA:EGLN2 - orthologs
Gene location (Human)
Chr.	Chromosome 19 (human)
End	40,808,434 bp
Gene location (Mouse)
Chr.	Chromosome 7 (mouse)
End	26,866,227 bp
RNA expression pattern
	Top expressed in
	left testis; ; right testis; ; blood; ; spleen; ; right lung; ; apex of heart; ; upper lobe of left lung; ; mucosa of transverse colon; ; primary visual cortex; ; putamen;
	Top expressed in
	seminiferous tubule; ; entorhinal cortex; ; Ileal epithelium; ; perirhinal cortex; ; choroid plexus of fourth ventricle; ; CA3 field; ; spermatid; ; muscle of thigh; ; Paneth cell; ; crypt of lieberkuhn of small intestine;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	2-oxoglutarate-dependent dioxygenase activity; L-ascorbic acid binding; iron ion binding; dioxygenase activity; metal ion binding; protein binding; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; oxidoreductase activity; ferrous iron binding; oxygen gasoreceptor activity; peptidyl-proline 4-dioxygenase activity;
Cellular component	nucleoplasm; nucleus;
Biological process	response to hypoxia; positive regulation of protein catabolic process; regulation of neuron apoptotic process; peptidyl-proline hydroxylation to 4-hydroxy-L-proline; cell redox homeostasis; regulation of cell growth; regulation of transcription from RNA polymerase II promoter in response to hypoxia; intracellular estrogen receptor signaling pathway;
	Sources:Amigo / QuickGO
Orthologs
	112398
	112406
	ENSG00000269858
	ENSMUSG00000058709
	Q96KS0
	Q91YE2
	NM_080732; NM_017555; NM_053046
	NM_053208; NM_001357767
	NP_444274; NP_542770
	NP_444438; NP_001344696
	Wikidata
View/Edit Human	View/Edit Mouse

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Revision as of 05:49, 21 May 2016

Egl nine homolog 2 is a protein that in humans is encoded by the EGLN2 gene.^[5]

Template:PBB Summary

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000269858 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000058709 – 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: EGLN2 egl nine homolog 2 (C. elegans)".

@@ Line 6: / Line 6: @@
 | section_title =
 | summary_text = The [[hypoxia inducible factor]] (HIF) is a transcriptional complex which is involved in [[oxygen homeostasis]]. At normal oxygen levels, the alpha subunit of HIF is targeted for degradation by [[prolyl hydroxylase|prolyl hydroxylation]].
 This gene encodes an enzyme responsible for this posttranslational modification. Multiple alternatively spliced variants, encoding the same protein, have been identified.<ref name="entrez" />
 }}
@@ Line 12: / Line 11: @@
 ==References==
 {{reflist}}
 ==Further reading==
 {{refbegin | 2}}
@@ Line 17: / Line 17: @@
 | citations =
 *{{cite journal  | author=Semenza GL |title=HIF-1, O(2), and the 3 PHDs: how animal cells signal hypoxia to the nucleus |journal=Cell |volume=107 |issue= 1 |pages= 1–3 |year= 2001 |pmid= 11595178 |doi=10.1016/S0092-8674(01)00518-9  }}
-*{{cite journal  | author=Hartley JL, Temple GF, Brasch MA |title=DNA Cloning Using In Vitro Site-Specific Recombination |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788–95 |year= 2001 |pmid= 11076863 |doi=10.1101/gr.143000  | pmc=310948  }}
+*{{cite journal  | vauthors=Hartley JL, Temple GF, Brasch MA |title=DNA Cloning Using In Vitro Site-Specific Recombination |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788–95 |year= 2001 |pmid= 11076863 |doi=10.1101/gr.143000  | pmc=310948  }}
-*{{cite journal  | author=Wiemann S, Weil B, Wellenreuther R |title=Toward a Catalog of Human Genes and Proteins: Sequencing and Analysis of 500 Novel Complete Protein Coding Human cDNAs |journal=Genome Res. |volume=11 |issue= 3 |pages= 422–35 |year= 2001 |pmid= 11230166 |doi= 10.1101/gr.GR1547R  | pmc=311072 |display-authors=etal}}
+*{{cite journal  | vauthors=Wiemann S, Weil B, Wellenreuther R |title=Toward a Catalog of Human Genes and Proteins: Sequencing and Analysis of 500 Novel Complete Protein Coding Human cDNAs |journal=Genome Res. |volume=11 |issue= 3 |pages= 422–35 |year= 2001 |pmid= 11230166 |doi= 10.1101/gr.GR1547R  | pmc=311072 |display-authors=etal}}
-*{{cite journal  | author=Jaakkola P, Mole DR, Tian YM |title=Targeting of HIF-alpha to the von Hippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation |journal=Science |volume=292 |issue= 5516 |pages= 468–72 |year= 2001 |pmid= 11292861 |doi= 10.1126/science.1059796 |display-authors=etal}}
+*{{cite journal  | vauthors=Jaakkola P, Mole DR, Tian YM |title=Targeting of HIF-alpha to the von Hippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation |journal=Science |volume=292 |issue= 5516 |pages= 468–72 |year= 2001 |pmid= 11292861 |doi= 10.1126/science.1059796 |display-authors=etal}}
-*{{cite journal  | author=Ivan M, Kondo K, Yang H |title=HIFalpha targeted for VHL-mediated destruction by proline hydroxylation: implications for O2 sensing |journal=Science |volume=292 |issue= 5516 |pages= 464–8 |year= 2001 |pmid= 11292862 |doi= 10.1126/science.1059817 |display-authors=etal}}
+*{{cite journal  | vauthors=Ivan M, Kondo K, Yang H |title=HIFalpha targeted for VHL-mediated destruction by proline hydroxylation: implications for O2 sensing |journal=Science |volume=292 |issue= 5516 |pages= 464–8 |year= 2001 |pmid= 11292862 |doi= 10.1126/science.1059817 |display-authors=etal}}
 *{{cite journal  | author=Taylor MS |title=Characterization and comparative analysis of the EGLN gene family |journal=Gene |volume=275 |issue= 1 |pages= 125–32 |year= 2001 |pmid= 11574160 |doi=10.1016/S0378-1119(01)00633-3  }}
-*{{cite journal  | author=Epstein AC, Gleadle JM, McNeill LA |title=C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation |journal=Cell |volume=107 |issue= 1 |pages= 43–54 |year= 2001 |pmid= 11595184 |doi=10.1016/S0092-8674(01)00507-4  |display-authors=etal}}
+*{{cite journal  | vauthors=Epstein AC, Gleadle JM, McNeill LA |title=C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation |journal=Cell |volume=107 |issue= 1 |pages= 43–54 |year= 2001 |pmid= 11595184 |doi=10.1016/S0092-8674(01)00507-4  |display-authors=etal}}
-*{{cite journal  | author=Bruick RK, McKnight SL |title=A conserved family of prolyl-4-hydroxylases that modify HIF |journal=Science |volume=294 |issue= 5545 |pages= 1337–40 |year= 2001 |pmid= 11598268 |doi= 10.1126/science.1066373 }}
+*{{cite journal  | vauthors=Bruick RK, McKnight SL |title=A conserved family of prolyl-4-hydroxylases that modify HIF |journal=Science |volume=294 |issue= 5545 |pages= 1337–40 |year= 2001 |pmid= 11598268 |doi= 10.1126/science.1066373 }}
-*{{cite journal  | author=Seth P, Krop I, Porter D, Polyak K |title=Novel estrogen and tamoxifen induced genes identified by SAGE (Serial Analysis of Gene Expression) |journal=Oncogene |volume=21 |issue= 5 |pages= 836–43 |year= 2002 |pmid= 11850811 |doi= 10.1038/sj.onc.1205113 }}
+*{{cite journal  | vauthors=Seth P, Krop I, Porter D, Polyak K |title=Novel estrogen and tamoxifen induced genes identified by SAGE (Serial Analysis of Gene Expression) |journal=Oncogene |volume=21 |issue= 5 |pages= 836–43 |year= 2002 |pmid= 11850811 |doi= 10.1038/sj.onc.1205113 }}
-*{{cite journal  | author=Min JH, Yang H, Ivan M |title=Structure of an HIF-1alpha -pVHL complex: hydroxyproline recognition in signaling |journal=Science |volume=296 |issue= 5574 |pages= 1886–9 |year= 2002 |pmid= 12004076 |doi= 10.1126/science.1073440 |display-authors=etal}}
+*{{cite journal  | vauthors=Min JH, Yang H, Ivan M |title=Structure of an HIF-1alpha -pVHL complex: hydroxyproline recognition in signaling |journal=Science |volume=296 |issue= 5574 |pages= 1886–9 |year= 2002 |pmid= 12004076 |doi= 10.1126/science.1073440 |display-authors=etal}}
-*{{cite journal  | author=McNeill LA, Hewitson KS, Gleadle JM |title=The use of dioxygen by HIF prolyl hydroxylase (PHD1) |journal=Bioorg. Med. Chem. Lett. |volume=12 |issue= 12 |pages= 1547–50 |year= 2002 |pmid= 12039559 |doi=10.1016/S0960-894X(02)00219-6  |display-authors=etal}}
+*{{cite journal  | vauthors=McNeill LA, Hewitson KS, Gleadle JM |title=The use of dioxygen by HIF prolyl hydroxylase (PHD1) |journal=Bioorg. Med. Chem. Lett. |volume=12 |issue= 12 |pages= 1547–50 |year= 2002 |pmid= 12039559 |doi=10.1016/S0960-894X(02)00219-6  |display-authors=etal}}
-*{{cite journal  | author=Oehme F, Ellinghaus P, Kolkhof P |title=Overexpression of PH-4, a novel putative proline 4-hydroxylase, modulates activity of hypoxia-inducible transcription factors |journal=Biochem. Biophys. Res. Commun. |volume=296 |issue= 2 |pages= 343–9 |year= 2002 |pmid= 12163023 |doi=10.1016/S0006-291X(02)00862-8  |display-authors=etal}}
+*{{cite journal  | vauthors=Oehme F, Ellinghaus P, Kolkhof P |title=Overexpression of PH-4, a novel putative proline 4-hydroxylase, modulates activity of hypoxia-inducible transcription factors |journal=Biochem. Biophys. Res. Commun. |volume=296 |issue= 2 |pages= 343–9 |year= 2002 |pmid= 12163023 |doi=10.1016/S0006-291X(02)00862-8  |display-authors=etal}}
-*{{cite journal  | author=Ivan M, Haberberger T, Gervasi DC |title=Biochemical purification and pharmacological inhibition of a mammalian prolyl hydroxylase acting on hypoxia-inducible factor |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 21 |pages= 13459–64 |year= 2002 |pmid= 12351678 |doi= 10.1073/pnas.192342099  | pmc=129695 |display-authors=etal}}
+*{{cite journal  | vauthors=Ivan M, Haberberger T, Gervasi DC |title=Biochemical purification and pharmacological inhibition of a mammalian prolyl hydroxylase acting on hypoxia-inducible factor |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 21 |pages= 13459–64 |year= 2002 |pmid= 12351678 |doi= 10.1073/pnas.192342099  | pmc=129695 |display-authors=etal}}
-*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241 |display-authors=etal}}
+*{{cite journal  | vauthors=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241 |display-authors=etal}}
-*{{cite journal  | author=Metzen E, Berchner-Pfannschmidt U, Stengel P |title=Intracellular localisation of human HIF-1 alpha hydroxylases: implications for oxygen sensing |journal=J. Cell. Sci. |volume=116 |issue= Pt 7 |pages= 1319–26 |year= 2003 |pmid= 12615973 |doi=10.1242/jcs.00318  |display-authors=etal}}
+*{{cite journal  | vauthors=Metzen E, Berchner-Pfannschmidt U, Stengel P |title=Intracellular localisation of human HIF-1 alpha hydroxylases: implications for oxygen sensing |journal=J. Cell. Sci. |volume=116 |issue= Pt 7 |pages= 1319–26 |year= 2003 |pmid= 12615973 |doi=10.1242/jcs.00318  |display-authors=etal}}
-*{{cite journal  | author=Cioffi CL, Liu XQ, Kosinski PA |title=Differential regulation of HIF-1 alpha prolyl-4-hydroxylase genes by hypoxia in human cardiovascular cells |journal=Biochem. Biophys. Res. Commun. |volume=303 |issue= 3 |pages= 947–53 |year= 2003 |pmid= 12670503 |doi=10.1016/S0006-291X(03)00453-4  |display-authors=etal}}
+*{{cite journal  | vauthors=Cioffi CL, Liu XQ, Kosinski PA |title=Differential regulation of HIF-1 alpha prolyl-4-hydroxylase genes by hypoxia in human cardiovascular cells |journal=Biochem. Biophys. Res. Commun. |volume=303 |issue= 3 |pages= 947–53 |year= 2003 |pmid= 12670503 |doi=10.1016/S0006-291X(03)00453-4  |display-authors=etal}}
-*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T |title=Complete sequencing and characterization of 21,243 full-length human cDNAs |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 |display-authors=etal}}
+*{{cite journal  | vauthors=Ota T, Suzuki Y, Nishikawa T |title=Complete sequencing and characterization of 21,243 full-length human cDNAs |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 |display-authors=etal}}
-*{{cite journal  | author=Aprelikova O, Chandramouli GV, Wood M |title=Regulation of HIF prolyl hydroxylases by hypoxia-inducible factors |journal=J. Cell. Biochem. |volume=92 |issue= 3 |pages= 491–501 |year= 2004 |pmid= 15156561 |doi= 10.1002/jcb.20067 |display-authors=etal}}
+*{{cite journal  | vauthors=Aprelikova O, Chandramouli GV, Wood M |title=Regulation of HIF prolyl hydroxylases by hypoxia-inducible factors |journal=J. Cell. Biochem. |volume=92 |issue= 3 |pages= 491–501 |year= 2004 |pmid= 15156561 |doi= 10.1002/jcb.20067 |display-authors=etal}}
-*{{cite journal  | author=Colland F, Jacq X, Trouplin V |title=Functional Proteomics Mapping of a Human Signaling Pathway |journal=Genome Res. |volume=14 |issue= 7 |pages= 1324–32 |year= 2004 |pmid= 15231748 |doi= 10.1101/gr.2334104  | pmc=442148 |display-authors=etal}}
+*{{cite journal  | vauthors=Colland F, Jacq X, Trouplin V |title=Functional Proteomics Mapping of a Human Signaling Pathway |journal=Genome Res. |volume=14 |issue= 7 |pages= 1324–32 |year= 2004 |pmid= 15231748 |doi= 10.1101/gr.2334104  | pmc=442148 |display-authors=etal}}
 }}
 {{refend}}
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 {{Enzymes}}
 {{Portal bar|Molecular and Cellular Biology|border=no}}
-{{gene-19-stub}}
-[[Category:Human 2OG oxygenases]]
-[[Category:EC 1.14.11]]
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+[[Category:Human 2OG oxygenases]]
+[[Category:EC 1.14.11]]
+{{gene-19-stub}}

v t e Oxidoreductases: dioxygenases, including steroid hydroxylases (EC 1.14)
1.14.11: 2-oxoglutarate	Prolyl hydroxylase HIF prolyl-hydroxylase EGLN1 EGLN2 EGLN3 P4HTM Lysyl hydroxylase AlkB ALKBH1 FTO
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 Deoxyhypusine monooxygenase

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme 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)