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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Latest revision as of 21:18, 8 November 2023

Egl nine homolog 2 is a protein that in humans is encoded by the EGLN2 gene.^[5] ELGN2 is an alpha-ketoglutarate-dependent hydroxylase, a superfamily of non-haem iron-containing proteins.

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 hydroxylation. This gene encodes an enzyme responsible for this posttranslational modification. Multiple alternatively spliced variants, encoding the same protein, have been identified.^[5]

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.
^ ^a ^b "Entrez Gene: EGLN2 egl nine homolog 2 (C. elegans)".

Semenza GL (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. S2CID 14922615.
Hartley JL, Temple GF, Brasch MA (2001). "DNA Cloning Using In Vitro Site-Specific Recombination". Genome Res. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
Wiemann S, Weil B, Wellenreuther R, et al. (2001). "Toward a Catalog of Human Genes and Proteins: Sequencing and Analysis of 500 Novel Complete Protein Coding Human cDNAs". Genome Res. 11 (3): 422–35. doi:10.1101/gr.GR1547R. PMC 311072. PMID 11230166.
Jaakkola P, Mole DR, Tian YM, et al. (2001). "Targeting of HIF-alpha to the von Hippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation". Science. 292 (5516): 468–72. Bibcode:2001Sci...292..468J. doi:10.1126/science.1059796. PMID 11292861. S2CID 20914281.
Ivan M, Kondo K, Yang H, et al. (2001). "HIFalpha targeted for VHL-mediated destruction by proline hydroxylation: implications for O2 sensing". Science. 292 (5516): 464–8. Bibcode:2001Sci...292..464I. doi:10.1126/science.1059817. PMID 11292862. S2CID 33725562.
Taylor MS (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, et al. (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. S2CID 18372306.
Bruick RK, McKnight SL (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.
Seth P, Krop I, Porter D, Polyak K (2002). "Novel estrogen and tamoxifen induced genes identified by SAGE (Serial Analysis of Gene Expression)". Oncogene. 21 (5): 836–43. doi:10.1038/sj.onc.1205113. PMID 11850811.
Min JH, Yang H, Ivan M, et al. (2002). "Structure of an HIF-1alpha -pVHL complex: hydroxyproline recognition in signaling". Science. 296 (5574): 1886–9. Bibcode:2002Sci...296.1886M. doi:10.1126/science.1073440. PMID 12004076. S2CID 19641938.
McNeill LA, Hewitson KS, Gleadle JM, et al. (2002). "The use of dioxygen by HIF prolyl hydroxylase (PHD1)". Bioorg. Med. Chem. Lett. 12 (12): 1547–50. doi:10.1016/S0960-894X(02)00219-6. PMID 12039559.
Oehme F, Ellinghaus P, Kolkhof P, et al. (2002). "Overexpression of PH-4, a novel putative proline 4-hydroxylase, modulates activity of hypoxia-inducible transcription factors". Biochem. Biophys. Res. Commun. 296 (2): 343–9. doi:10.1016/S0006-291X(02)00862-8. PMID 12163023.
Ivan M, Haberberger T, Gervasi DC, et al. (2002). "Biochemical purification and pharmacological inhibition of a mammalian prolyl hydroxylase acting on hypoxia-inducible factor". Proc. Natl. Acad. Sci. U.S.A. 99 (21): 13459–64. Bibcode:2002PNAS...9913459I. doi:10.1073/pnas.192342099. PMC 129695. PMID 12351678.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Metzen E, Berchner-Pfannschmidt U, Stengel P, et al. (2003). "Intracellular localisation of human HIF-1 alpha hydroxylases: implications for oxygen sensing". J. Cell Sci. 116 (Pt 7): 1319–26. doi:10.1242/jcs.00318. PMID 12615973.
Cioffi CL, Liu XQ, Kosinski PA, et al. (2003). "Differential regulation of HIF-1 alpha prolyl-4-hydroxylase genes by hypoxia in human cardiovascular cells". Biochem. Biophys. Res. Commun. 303 (3): 947–53. doi:10.1016/S0006-291X(03)00453-4. PMID 12670503.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Aprelikova O, Chandramouli GV, Wood M, et al. (2004). "Regulation of HIF prolyl hydroxylases by hypoxia-inducible factors". J. Cell. Biochem. 92 (3): 491–501. doi:10.1002/jcb.20067. PMID 15156561. S2CID 24455956.
Colland F, Jacq X, Trouplin V, et al. (2004). "Functional Proteomics Mapping of a Human Signaling Pathway". Genome Res. 14 (7): 1324–32. doi:10.1101/gr.2334104. PMC 442148. PMID 15231748.

This article on a gene on human chromosome 19 is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000269858 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000058709 – 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: EGLN2 egl nine homolog 2 (C. elegans)".

[1]

[2]

[3]

[4]

[5]

@@ Line 1: / Line 1: @@
+{{Short description|Protein-coding gene in the species Homo sapiens}}
-{{PBB|geneid=112398}}
+{{Infobox_gene}}
-'''Egl nine homolog 2''' is a [[protein]] that in humans is encoded by the ''EGLN2'' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: EGLN2 egl nine homolog 2 (C. elegans)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=112398| accessdate = }}</ref>
+'''Egl nine homolog 2''' is a [[protein]] that in humans is encoded by the ''EGLN2'' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: EGLN2 egl nine homolog 2 (C. elegans)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=112398}}</ref> ELGN2 is an [[alpha-ketoglutarate-dependent hydroxylase]], a superfamily of non-haem iron-containing proteins.
+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]].
-<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
+This gene encodes an enzyme responsible for this posttranslational modification. Multiple alternatively spliced variants, encoding the same protein, have been identified.<ref name="entrez" />
-{{PBB_Summary
-| 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">{{cite web | title = Entrez Gene: EGLN2 egl nine homolog 2 (C. elegans)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=112398| accessdate = }}</ref>
-}}
 ==References==
 {{reflist}}
 ==Further reading==
 {{refbegin | 2}}
+*{{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  |s2cid=14922615 |doi-access=free }}
-{{PBB_Further_reading
+*{{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  }}
-| 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  | 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=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=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|bibcode=2001Sci...292..468J |s2cid=20914281 |doi-access=free }}
-*{{cite journal  | author=Wiemann S, Weil B, Wellenreuther R, ''et al.'' |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 }}
+*{{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|bibcode=2001Sci...292..464I |s2cid=33725562 |doi-access=free }}
-*{{cite journal  | author=Jaakkola P, Mole DR, Tian YM, ''et al.'' |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 }}
+*{{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=Ivan M, Kondo K, Yang H, ''et al.'' |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 }}
+*{{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  |s2cid=18372306 |display-authors=etal|doi-access=free }}
-*{{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  | 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 |bibcode=2001Sci...294.1337B |s2cid=9695199 }}
-*{{cite journal  | author=Epstein AC, Gleadle JM, McNeill LA, ''et al.'' |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  }}
+*{{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 |doi-access= free }}
-*{{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=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|bibcode=2002Sci...296.1886M |s2cid=19641938 |doi-access=free }}
-*{{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=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=Min JH, Yang H, Ivan M, ''et al.'' |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 }}
+*{{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=McNeill LA, Hewitson KS, Gleadle JM, ''et al.'' |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  }}
+*{{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|bibcode=2002PNAS...9913459I |doi-access=free }}
-*{{cite journal  | author=Oehme F, Ellinghaus P, Kolkhof P, ''et al.'' |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  }}
+*{{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 |bibcode=2002PNAS...9916899M|doi-access=free }}
-*{{cite journal  | author=Ivan M, Haberberger T, Gervasi DC, ''et al.'' |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 }}
+*{{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|doi-access=free }}
-*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |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 }}
+*{{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=Metzen E, Berchner-Pfannschmidt U, Stengel P, ''et al.'' |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  }}
+*{{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|doi-access=free }}
-*{{cite journal  | author=Cioffi CL, Liu XQ, Kosinski PA, ''et al.'' |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  }}
+*{{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 |s2cid=24455956 |display-authors=etal|url=https://zenodo.org/record/1229216 }}
-*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |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 }}
+*{{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}}
-*{{cite journal  | author=Aprelikova O, Chandramouli GV, Wood M, ''et al.'' |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 }}
-*{{cite journal  | author=Colland F, Jacq X, Trouplin V, ''et al.'' |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 }}
-}}
 {{refend}}
-{{gene-19-stub}}
+{{Dioxygenases}}
+{{Enzymes}}
+{{Portal bar|Biology|border=no}}
 [[Category:Human 2OG oxygenases]]
 [[Category:EC 1.14.11]]
-<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
+{{gene-19-stub}}
-{{PBB_Controls
-| update_page = yes
-| require_manual_inspection = no
-| update_protein_box = yes
-| update_summary = yes
-| update_citations = yes
-}}

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)