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{{Infobox_gene}}
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'''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| accessdate = }}</ref> ELGN2 is a member of the non-haem Fe(II) and [[2-oxoglutarate (2OG)-dependent dioxygenases]].
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{{GNF_Protein_box
| image = 
| image_source = 
| PDB =
| Name = Egl nine homolog 2 (C. elegans)
| HGNCid = 14660
| Symbol = EGLN2
| AltSymbols =; DKFZp434E026; EIT6; HIFPH1; PHD1
| OMIM = 606424
| ECnumber = 
| Homologene = 14204
| MGIid = 1932287
| GeneAtlas_image1 = PBB_GE_EGLN2_220956_s_at_tn.png
| Function = {{GNF_GO|id=GO:0008198 |text = ferrous iron binding}} {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}} {{GNF_GO|id=GO:0016702 |text = oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen}} {{GNF_GO|id=GO:0016706 |text = 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}} {{GNF_GO|id=GO:0019826 |text = oxygen sensor activity}} {{GNF_GO|id=GO:0031418 |text = L-ascorbic acid binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0001558 |text = regulation of cell growth}} {{GNF_GO|id=GO:0001666 |text = response to hypoxia}} {{GNF_GO|id=GO:0019538 |text = protein metabolic process}} {{GNF_GO|id=GO:0030503 |text = regulation of cell redox homeostasis}} {{GNF_GO|id=GO:0030520 |text = estrogen receptor signaling pathway}} {{GNF_GO|id=GO:0045732 |text = positive regulation of protein catabolic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 112398
    | Hs_Ensembl = ENSG00000171570
    | Hs_RefseqProtein = NP_060025
    | Hs_RefseqmRNA = NM_017555
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 19
    | Hs_GenLoc_start = 45996932
    | Hs_GenLoc_end = 46006176
    | Hs_Uniprot = Q96KS0
    | Mm_EntrezGene = 112406
    | Mm_Ensembl = ENSMUSG00000058709
    | Mm_RefseqmRNA = NM_053208
    | Mm_RefseqProtein = NP_444438
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 7
    | Mm_GenLoc_start = 26867419
    | Mm_GenLoc_end = 26875533
    | Mm_Uniprot = Q3TXL8
  }}
}}
'''Egl nine homolog 2 (C. elegans)''', also known as '''EGLN2''', is a human [[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>


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{{PBB_Summary
| section_title =  
| 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 degration by 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>
| 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" />
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| 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=  }}
*{{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=  }}
*{{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, ''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.154701 }}
*{{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, ''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  | 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, ''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=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=  }}
*{{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, ''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=  }}
*{{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, ''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=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, ''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=  }}
*{{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, ''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=  }}
*{{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, ''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 }}
*{{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, ''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 }}
*{{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, ''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=  }}
*{{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, ''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=  }}
*{{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, ''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=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, ''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  | 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, ''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 }}
*{{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}}
}}
}}
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{{protein-stub}}
{{Dioxygenases}}
{{WikiDoc Sources}}
{{Enzymes}}
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[[Category:Human 2OG oxygenases]]
[[Category:EC 1.14.11]]
 
 
{{gene-19-stub}}

Revision as of 09:31, 23 November 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Egl nine homolog 2 is a protein that in humans is encoded by the EGLN2 gene.[1] ELGN2 is a member of the non-haem Fe(II) and 2-oxoglutarate (2OG)-dependent dioxygenases.

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.[1]

References

  1. ↑ 1.0 1.1 "Entrez Gene: EGLN2 egl nine homolog 2 (C. elegans)".

Further reading


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