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{{Infobox_gene}}
{{PBB_Controls
'''Egl nine homolog 3''' is a [[protein]] that in humans is encoded by the ''EGLN3'' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: EGLN3 egl nine homolog 3 (C. elegans)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=112399| accessdate = }}</ref> ELGN3 is a member of the superfamily of non-haem Fe(II) and [[2-oxoglutarate (2OG)-dependent dioxygenases]].
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== References ==
{{GNF_Protein_box
{{reflist}}
| image = 
| image_source = 
| PDB =
| Name = Egl nine homolog 3 (C. elegans)
| HGNCid = 14661
| Symbol = EGLN3
| AltSymbols =; FLJ21620; HIFPH3; MGC125998; MGC125999; PHD3
| OMIM = 606426
| ECnumber = 
| Homologene = 32531
| MGIid = 1932288
| GeneAtlas_image1 = PBB_GE_EGLN3_219232_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0005515 |text = protein 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: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:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0019538 |text = protein metabolic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 112399
    | Hs_Ensembl = ENSG00000129521
    | Hs_RefseqProtein = NP_071356
    | Hs_RefseqmRNA = NM_022073
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 14
    | Hs_GenLoc_start = 33463174
    | Hs_GenLoc_end = 33490037
    | Hs_Uniprot = Q9H6Z9
    | Mm_EntrezGene = 112407
    | Mm_Ensembl = ENSMUSG00000035105
    | Mm_RefseqmRNA = NM_028133
    | Mm_RefseqProtein = NP_082409
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 12
    | Mm_GenLoc_start = 55100608
    | Mm_GenLoc_end = 55125474
    | Mm_Uniprot = Q91UZ4
  }}
}}
'''Egl nine homolog 3 (C. elegans)''', also known as '''EGLN3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: EGLN3 egl nine homolog 3 (C. elegans)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=112399| accessdate = }}</ref>


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== Further reading ==
{{PBB_Summary
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| summary_text =
}}
 
==References==
{{reflist|2}}
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = 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 | date = October 2001 | pmid = 11595178 | doi = 10.1016/S0092-8674(01)00518-9 }}
| citations =
* {{cite journal | vauthors = Maruyama K, Sugano S | title = Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides | journal = Gene | volume = 138 | issue = 1-2 | pages = 171–4 | date = January 1994 | pmid = 8125298 | doi = 10.1016/0378-1119(94)90802-8 }}
*{{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 | vauthors = Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S | title = Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library | journal = Gene | volume = 200 | issue = 1-2 | pages = 149–56 | date = October 1997 | pmid = 9373149 | doi = 10.1016/S0378-1119(97)00411-3 }}
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
* {{cite journal | vauthors = Taylor MS | title = Characterization and comparative analysis of the EGLN gene family | journal = Gene | volume = 275 | issue = 1 | pages = 125–32 | date = September 2001 | pmid = 11574160 | doi = 10.1016/S0378-1119(01)00633-3 }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
* {{cite journal | vauthors = 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 | 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 | date = October 2001 | pmid = 11595184 | doi = 10.1016/S0092-8674(01)00507-4 }}
*{{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 | 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 | date = November 2001 | pmid = 11598268 | doi = 10.1126/science.1066373 }}
*{{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 = Oehme F, Ellinghaus P, Kolkhof P, Smith TJ, Ramakrishnan S, Hütter J, Schramm M, Flamme I | title = Overexpression of PH-4, a novel putative proline 4-hydroxylase, modulates activity of hypoxia-inducible transcription factors | journal = Biochemical and Biophysical Research Communications | volume = 296 | issue = 2 | pages = 343–9 | date = August 2002 | pmid = 12163023 | doi = 10.1016/S0006-291X(02)00862-8 }}
*{{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 = 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 | title = Intracellular localisation of human HIF-1 alpha hydroxylases: implications for oxygen sensing | journal = Journal of Cell Science | volume = 116 | issue = Pt 7 | pages = 1319–26 | date = April 2003 | pmid = 12615973 | doi = 10.1242/jcs.00318 }}
*{{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 = Cioffi CL, Liu XQ, Kosinski PA, Garay M, Bowen BR | title = Differential regulation of HIF-1 alpha prolyl-4-hydroxylase genes by hypoxia in human cardiovascular cells | journal = Biochemical and Biophysical Research Communications | volume = 303 | issue = 3 | pages = 947–53 | date = April 2003 | pmid = 12670503 | doi = 10.1016/S0006-291X(03)00453-4 }}
*{{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 = Aprelikova O, Chandramouli GV, Wood M, Vasselli JR, Riss J, Maranchie JK, Linehan WM, Barrett JC | title = Regulation of HIF prolyl hydroxylases by hypoxia-inducible factors | journal = Journal of Cellular Biochemistry | volume = 92 | issue = 3 | pages = 491–501 | date = June 2004 | pmid = 15156561 | doi = 10.1002/jcb.20067 }}
*{{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 = Appelhoff RJ, Tian YM, Raval RR, Turley H, Harris AL, Pugh CW, Ratcliffe PJ, Gleadle JM | title = Differential function of the prolyl hydroxylases PHD1, PHD2, and PHD3 in the regulation of hypoxia-inducible factor | journal = The Journal of Biological Chemistry | volume = 279 | issue = 37 | pages = 38458–65 | date = September 2004 | pmid = 15247232 | doi = 10.1074/jbc.M406026200 }}
*{{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 = Masson N, Appelhoff RJ, Tuckerman JR, Tian YM, Demol H, Puype M, Vandekerckhove J, Ratcliffe PJ, Pugh CW | title = The HIF prolyl hydroxylase PHD3 is a potential substrate of the TRiC chaperonin | journal = FEBS Letters | volume = 570 | issue = 1-3 | pages = 166–70 | date = July 2004 | pmid = 15251459 | doi = 10.1016/j.febslet.2004.06.040 }}
*{{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 = Baek JH, Mahon PC, Oh J, Kelly B, Krishnamachary B, Pearson M, Chan DA, Giaccia AJ, Semenza GL | title = OS-9 interacts with hypoxia-inducible factor 1alpha and prolyl hydroxylases to promote oxygen-dependent degradation of HIF-1alpha | journal = Molecular Cell | volume = 17 | issue = 4 | pages = 503–12 | date = February 2005 | pmid = 15721254 | doi = 10.1016/j.molcel.2005.01.011 }}
*{{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 = Lee S, Nakamura E, Yang H, Wei W, Linggi MS, Sajan MP, Farese RV, Freeman RS, Carter BD, Kaelin WG, Schlisio S | title = Neuronal apoptosis linked to EglN3 prolyl hydroxylase and familial pheochromocytoma genes: developmental culling and cancer | journal = Cancer Cell | volume = 8 | issue = 2 | pages = 155–67 | date = August 2005 | pmid = 16098468 | doi = 10.1016/j.ccr.2005.06.015 }}
*{{cite journal | author=Appelhoff RJ, Tian YM, Raval RR, ''et al.'' |title=Differential function of the prolyl hydroxylases PHD1, PHD2, and PHD3 in the regulation of hypoxia-inducible factor. |journal=J. Biol. Chem. |volume=279 |issue= 37 |pages= 38458-65 |year= 2004 |pmid= 15247232 |doi= 10.1074/jbc.M406026200 }}
* {{cite journal | vauthors = Hopfer U, Hopfer H, Jablonski K, Stahl RA, Wolf G | title = The novel WD-repeat protein Morg1 acts as a molecular scaffold for hypoxia-inducible factor prolyl hydroxylase 3 (PHD3) | journal = The Journal of Biological Chemistry | volume = 281 | issue = 13 | pages = 8645–55 | date = March 2006 | pmid = 16407229 | doi = 10.1074/jbc.M513751200 }}
*{{cite journal | author=Masson N, Appelhoff RJ, Tuckerman JR, ''et al.'' |title=The HIF prolyl hydroxylase PHD3 is a potential substrate of the TRiC chaperonin. |journal=FEBS Lett. |volume=570 |issue= 1-3 |pages= 166-70 |year= 2004 |pmid= 15251459 |doi= 10.1016/j.febslet.2004.06.040 }}
* {{cite journal | vauthors = Nakayama K, Gazdoiu S, Abraham R, Pan ZQ, Ronai Z | title = Hypoxia-induced assembly of prolyl hydroxylase PHD3 into complexes: implications for its activity and susceptibility for degradation by the E3 ligase Siah2 | journal = The Biochemical Journal | volume = 401 | issue = 1 | pages = 217–26 | date = January 2007 | pmid = 16958618 | pmc = 1698661 | doi = 10.1042/BJ20061135 }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal  | author=Baek JH, Mahon PC, Oh J, ''et al.'' |title=OS-9 interacts with hypoxia-inducible factor 1alpha and prolyl hydroxylases to promote oxygen-dependent degradation of HIF-1alpha. |journal=Mol. Cell |volume=17 |issue= 4 |pages= 503-12 |year= 2005 |pmid= 15721254 |doi= 10.1016/j.molcel.2005.01.011 }}
*{{cite journal | author=Lee S, Nakamura E, Yang H, ''et al.'' |title=Neuronal apoptosis linked to EglN3 prolyl hydroxylase and familial pheochromocytoma genes: developmental culling and cancer. |journal=Cancer Cell |volume=8 |issue= 2 |pages= 155-67 |year= 2005 |pmid= 16098468 |doi= 10.1016/j.ccr.2005.06.015 }}
*{{cite journal | author=Hopfer U, Hopfer H, Jablonski K, ''et al.'' |title=The novel WD-repeat protein Morg1 acts as a molecular scaffold for hypoxia-inducible factor prolyl hydroxylase 3 (PHD3). |journal=J. Biol. Chem. |volume=281 |issue= 13 |pages= 8645-55 |year= 2006 |pmid= 16407229 |doi= 10.1074/jbc.M513751200 }}
*{{cite journal | author=Nakayama K, Gazdoiu S, Abraham R, ''et al.'' |title=Hypoxia-induced assembly of prolyl hydroxylase PHD3 into complexes: implications for its activity and susceptibility for degradation by the E3 ligase Siah2. |journal=Biochem. J. |volume=401 |issue= 1 |pages= 217-26 |year= 2007 |pmid= 16958618 |doi= 10.1042/BJ20061135 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
{{Dioxygenases}}
{{WikiDoc Sources}}
{{Enzymes}}
{{Portal bar|Molecular and Cellular Biology|border=no}}
 
 
[[Category:Human 2OG oxygenases]]
[[Category:EC 1.14.11]]
 
{{gene-14-stub}}

Revision as of 09:32, 23 November 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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n/a

Ensembl

n/a

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UniProt

n/a

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RefSeq (mRNA)

n/a

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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 3 is a protein that in humans is encoded by the EGLN3 gene.[1] ELGN3 is a member of the superfamily of non-haem Fe(II) and 2-oxoglutarate (2OG)-dependent dioxygenases.

References

  1. ↑ "Entrez Gene: EGLN3 egl nine homolog 3 (C. elegans)".

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. 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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