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Egl nine homolog 2 (EC 1.14.11.29) (Estrogen-induced tag 6) (HPH-3) (Hypoxia-inducible factor prolyl hydroxylase 1) (HIF-PH1) (HIF-prolyl hydroxylase 1) (HPH-1) (Prolyl hydroxylase domain-containing protein 1) (PHD1)

 EGLN2_HUMAN             Reviewed;         407 AA.
Q96KS0; A8K5S0; Q8WWY4; Q9BV14;
16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
25-OCT-2017, entry version 151.
RecName: Full=Egl nine homolog 2;
EC=1.14.11.29;
AltName: Full=Estrogen-induced tag 6;
AltName: Full=HPH-3;
AltName: Full=Hypoxia-inducible factor prolyl hydroxylase 1;
Short=HIF-PH1;
Short=HIF-prolyl hydroxylase 1;
Short=HPH-1;
AltName: Full=Prolyl hydroxylase domain-containing protein 1;
Short=PHD1;
Name=EGLN2; Synonyms=EIT6;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM P43).
PubMed=11574160; DOI=10.1016/S0378-1119(01)00633-3;
Taylor M.S.;
"Characterization and comparative analysis of the EGLN gene family.";
Gene 275:125-132(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM P43), AND INDUCTION.
TISSUE=Mammary cancer;
PubMed=11850811; DOI=10.1038/sj.onc.1205113;
Seth P., Krop I., Porter D., Polyak K.;
"Novel estrogen and tamoxifen induced genes identified by SAGE (Serial
Analysis of Gene Expression).";
Oncogene 21:836-843(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM P43).
TISSUE=Fetal brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM P43).
TISSUE=Endometrium;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM P43).
TISSUE=Lung, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
REVIEW.
PubMed=11595178; DOI=10.1016/S0092-8674(01)00518-9;
Semenza G.L.;
"HIF-1, O(2), and the 3 PHDs: how animal cells signal hypoxia to the
nucleus.";
Cell 107:1-3(2001).
[9]
FUNCTION, AND MUTAGENESIS OF HIS-358.
PubMed=11595184; DOI=10.1016/S0092-8674(01)00507-4;
Epstein A.C.R., Gleadle J.M., McNeill L.A., Hewitson K.S.,
O'Rourke J., Mole D.R., Mukherji M., Metzen E., Wilson M.I.,
Dhanda A., Tian Y.M., Masson N., Hamilton D.L., Jaakkola P.,
Barstead R., Hodgkin J., Maxwell P.H., Pugh C.W., Schofield C.J.,
Ratcliffe P.J.;
"C. elegans EGL-9 and mammalian homologs define a family of
dioxygenases that regulate HIF by prolyl hydroxylation.";
Cell 107:43-54(2001).
[10]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=12163023; DOI=10.1016/S0006-291X(02)00862-8;
Oehme F., Ellinghaus P., Kolkhof P., Smith T.J., Ramakrishnan S.,
Huetter J., Schramm M., Flamme I.;
"Overexpression of PH-4, a novel putative proline 4-hydroxylase,
modulates activity of hypoxia-inducible transcription factors.";
Biochem. Biophys. Res. Commun. 296:343-349(2002).
[11]
MUTAGENESIS OF HIS-297; ASP-299; HIS-358 AND ARG-367.
PubMed=12039559; DOI=10.1016/S0960-894X(02)00219-6;
McNeill L.A., Hewitson K.S., Gleadle J.M., Horsfall L.E., Oldham N.J.,
Maxwell P.H., Pugh C.W., Ratcliffe P.J., Schofield C.J.;
"The use of dioxygen by HIF prolyl hydroxylase (PHD1).";
Bioorg. Med. Chem. Lett. 12:1547-1550(2002).
[12]
FUNCTION, AND SUBSTRATE RECOGNITION MOTIF.
PubMed=12181324; DOI=10.1074/jbc.M206955200;
Huang J., Zhao Q., Mooney S.M., Lee F.S.;
"Sequence determinants in hypoxia-inducible factor-1alpha for
hydroxylation by the prolyl hydroxylases PHD1, PHD2, and PHD3.";
J. Biol. Chem. 277:39792-39800(2002).
[13]
SUBCELLULAR LOCATION, AND INDUCTION.
PubMed=12615973; DOI=10.1242/jcs.00318;
Metzen E., Berchner-Pfannschmidt U., Stengel P., Marxsen J.H.,
Stolze I., Klinger M., Huang W.Q., Wotzlaw C., Hellwig-Burgel T.,
Jelkmann W., Acker H., Fandrey J.;
"Intracellular localisation of human HIF-1 alpha hydroxylases:
implications for oxygen sensing.";
J. Cell Sci. 116:1319-1326(2003).
[14]
INDUCTION, AND SUBSTRATE SPECIFICITY.
PubMed=15247232; DOI=10.1074/jbc.M406026200;
Appelhoff R.J., Tian Y.M., Raval R.R., Turley H., Harris A.L.,
Pugh C.W., Ratcliffe P.J., Gleadle J.M.;
"Differential function of the prolyl hydroxylases PHD1, PHD2, and PHD3
in the regulation of hypoxia-inducible factor.";
J. Biol. Chem. 279:38458-38465(2004).
[15]
FUNCTION, INTERACTION WITH SIAH2, ALTERNATIVE INITIATION, INDUCTION,
AND MUTAGENESIS OF MET-1 AND MET-34.
PubMed=16509823; DOI=10.1042/BJ20051996;
Tian Y.M., Mole D.R., Ratcliffe P.J., Gleadle J.M.;
"Characterization of different isoforms of the HIF prolyl hydroxylase
PHD1 generated by alternative initiation.";
Biochem. J. 397:179-186(2006).
[16]
FUNCTION.
PubMed=17114296; DOI=10.1073/pnas.0602235103;
Cummins E.P., Berra E., Comerford K.M., Ginouves A., Fitzgerald K.T.,
Seeballuck F., Godson C., Nielsen J.E., Moynagh P., Pouyssegur J.,
Taylor C.T.;
"Prolyl hydroxylase-1 negatively regulates IkappaB kinase-beta, giving
insight into hypoxia-induced NFkappaB activity.";
Proc. Natl. Acad. Sci. U.S.A. 103:18154-18159(2006).
[17]
SUBCELLULAR LOCATION.
PubMed=19631610; DOI=10.1016/j.bbrc.2009.07.090;
Steinhoff A., Pientka F.K., Mockel S., Kettelhake A., Hartmann E.,
Kohler M., Depping R.;
"Cellular oxygen sensing: Importins and exportins are mediators of
intracellular localisation of prolyl-4-hydroxylases PHD1 and PHD2.";
Biochem. Biophys. Res. Commun. 387:705-711(2009).
[18]
SUBCELLULAR LOCATION, FUNCTION, AND MUTAGENESIS OF LYS-102; ARG-106;
ARG-113; ARG-119 AND ARG-134.
PubMed=19339211; DOI=10.1016/j.bbamcr.2009.01.014;
Yasumoto K., Kowata Y., Yoshida A., Torii S., Sogawa K.;
"Role of the intracellular localization of HIF-prolyl hydroxylases.";
Biochim. Biophys. Acta 1793:792-797(2009).
[19]
SUBSTRATE SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=21410436; DOI=10.1042/BJ20101201;
Pappalardi M.B., McNulty D.E., Martin J.D., Fisher K.E., Jiang Y.,
Burns M.C., Zhao H., Ho T., Sweitzer S., Schwartz B., Annan R.S.,
Copeland R.A., Tummino P.J., Luo L.;
"Biochemical characterization of human HIF hydroxylases using HIF
protein substrates that contain all three hydroxylation sites.";
Biochem. J. 436:363-369(2011).
[20]
INTERACTION WITH LIMD1; WTIP AND AJUBA.
PubMed=22286099; DOI=10.1038/ncb2424;
Foxler D.E., Bridge K.S., James V., Webb T.M., Mee M., Wong S.C.,
Feng Y., Constantin-Teodosiu D., Petursdottir T.E., Bjornsson J.,
Ingvarsson S., Ratcliffe P.J., Longmore G.D., Sharp T.V.;
"The LIMD1 protein bridges an association between the prolyl
hydroxylases and VHL to repress HIF-1 activity.";
Nat. Cell Biol. 14:201-208(2012).
[21]
FUNCTION.
PubMed=23932902; DOI=10.1016/j.devcel.2013.06.014;
Moser S.C., Bensaddek D., Ortmann B., Maure J.F., Mudie S., Blow J.J.,
Lamond A.I., Swedlow J.R., Rocha S.;
"PHD1 links cell-cycle progression to oxygen sensing through
hydroxylation of the centrosomal protein Cep192.";
Dev. Cell 26:381-392(2013).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
-!- FUNCTION: Cellular oxygen sensor that catalyzes, under normoxic
conditions, the post-translational formation of 4-hydroxyproline
in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a
specific proline found in each of the oxygen-dependent degradation
(ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A.
Also hydroxylates HIF2A. Has a preference for the CODD site for
both HIF1A and HIF2A. Hydroxylated HIFs are then targeted for
proteasomal degradation via the von Hippel-Lindau ubiquitination
complex. Under hypoxic conditions, the hydroxylation reaction is
attenuated allowing HIFs to escape degradation resulting in their
translocation to the nucleus, heterodimerization with HIF1B, and
increased expression of hypoxy-inducible genes. EGLN2 is involved
in regulating hypoxia tolerance and apoptosis in cardiac and
skeletal muscle. Also regulates susceptibility to normoxic
oxidative neuronal death. Links oxygen sensing to cell cycle and
primary cilia formation by hydroxylating the critical centrosome
component CEP192 which promotes its ubiquitination and subsequent
proteasomal degradation. Hydroxylates IKBKB, mediating NF-kappaB
activation in hypoxic conditions. Target proteins are
preferentially recognized via a LXXLAP motif.
{ECO:0000269|PubMed:11595184, ECO:0000269|PubMed:12181324,
ECO:0000269|PubMed:16509823, ECO:0000269|PubMed:17114296,
ECO:0000269|PubMed:19339211, ECO:0000269|PubMed:23932902}.
-!- CATALYTIC ACTIVITY: Hypoxia-inducible factor-L-proline + 2-
oxoglutarate + O(2) = hypoxia-inducible factor-trans-4-hydroxy-L-
proline + succinate + CO(2).
-!- COFACTOR:
Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
Note=Binds 1 Fe(2+) ion per subunit.;
-!- COFACTOR:
Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
-!- SUBUNIT: Interacts (preferably isoform p40) with SIAH2; the
interaction targets both SIAH2 isoforms for proteasomal
degradation in vitro. Interacts with LIMD1, WTIP and AJUBA.
{ECO:0000269|PubMed:16509823, ECO:0000269|PubMed:22286099}.
-!- INTERACTION:
Q16665:HIF1A; NbExp=2; IntAct=EBI-726614, EBI-447269;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12163023,
ECO:0000269|PubMed:12615973, ECO:0000269|PubMed:19339211,
ECO:0000269|PubMed:19631610}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=2;
Name=p43; Synonyms=PHD1p43;
IsoId=Q96KS0-1; Sequence=Displayed;
Name=p40; Synonyms=PHD1p40;
IsoId=Q96KS0-2; Sequence=VSP_038836;
-!- TISSUE SPECIFICITY: Expressed in adult and fetal heart, brain,
liver, lung, skeletal muscle, and kidney. Also expressed in testis
and placenta. Highest levels in adult brain, placenta, lung,
kidney, and testis. Expressed in hormone responsive tissues,
including normal and cancerous mammary, ovarian and prostate
epithelium. {ECO:0000269|PubMed:12163023}.
-!- INDUCTION: By estrogen. Isoform p43 is induced by hypoxia leading
to protein stability. Isoform p40 repressed by hypoxia. Both
isoforms are induced by proteasomal inhibitor MG132 (at protein
level). {ECO:0000269|PubMed:11850811, ECO:0000269|PubMed:12615973,
ECO:0000269|PubMed:15247232, ECO:0000269|PubMed:16509823}.
-!- DOMAIN: The Beta(2)beta(3) 'finger-like' loop domain is important
for substrate (HIFs' CODD/NODD) selectivity. {ECO:0000250}.
-!- SEQUENCE CAUTION:
Sequence=AAH01723.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AJ310544; CAC42510.1; -; mRNA.
EMBL; AY040565; AAK82943.1; -; mRNA.
EMBL; AK291385; BAF84074.1; -; mRNA.
EMBL; AL832506; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AC008537; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471126; EAW57008.1; -; Genomic_DNA.
EMBL; BC001723; AAH01723.1; ALT_INIT; mRNA.
EMBL; BC036051; AAH36051.1; -; mRNA.
CCDS; CCDS12567.1; -. [Q96KS0-1]
RefSeq; NP_444274.1; NM_053046.3. [Q96KS0-1]
RefSeq; NP_542770.2; NM_080732.3. [Q96KS0-1]
UniGene; Hs.515417; -.
UniGene; Hs.631539; -.
UniGene; Hs.730737; -.
PDB; 5V1B; X-ray; 2.49 A; A=167-403.
PDBsum; 5V1B; -.
ProteinModelPortal; Q96KS0; -.
SMR; Q96KS0; -.
BioGrid; 125184; 23.
IntAct; Q96KS0; 6.
MINT; MINT-1186497; -.
STRING; 9606.ENSP00000307080; -.
BindingDB; Q96KS0; -.
ChEMBL; CHEMBL3028; -.
DrugBank; DB04847; FG-4592.
DrugBank; DB00126; Vitamin C.
GuidetoPHARMACOLOGY; 2832; -.
iPTMnet; Q96KS0; -.
PhosphoSitePlus; Q96KS0; -.
BioMuta; EGLN2; -.
DMDM; 32129513; -.
MaxQB; Q96KS0; -.
PaxDb; Q96KS0; -.
PeptideAtlas; Q96KS0; -.
PRIDE; Q96KS0; -.
DNASU; 112398; -.
Ensembl; ENST00000303961; ENSP00000307080; ENSG00000269858. [Q96KS0-1]
Ensembl; ENST00000406058; ENSP00000385253; ENSG00000269858. [Q96KS0-1]
Ensembl; ENST00000593726; ENSP00000469686; ENSG00000269858. [Q96KS0-1]
GeneID; 112398; -.
KEGG; hsa:112398; -.
UCSC; uc002opg.5; human. [Q96KS0-1]
CTD; 112398; -.
DisGeNET; 112398; -.
EuPathDB; HostDB:ENSG00000269858.5; -.
GeneCards; EGLN2; -.
HGNC; HGNC:14660; EGLN2.
HPA; HPA056649; -.
MIM; 606424; gene.
neXtProt; NX_Q96KS0; -.
OpenTargets; ENSG00000269858; -.
PharmGKB; PA27671; -.
eggNOG; KOG3710; Eukaryota.
eggNOG; ENOG410ZHZN; LUCA.
GeneTree; ENSGT00390000001936; -.
HOGENOM; HOG000013099; -.
HOVERGEN; HBG051456; -.
InParanoid; Q96KS0; -.
KO; K09592; -.
OMA; GMSCGCS; -.
OrthoDB; EOG091G03SP; -.
PhylomeDB; Q96KS0; -.
TreeFam; TF314595; -.
BioCyc; MetaCyc:ENSG00000171570-MONOMER; -.
BRENDA; 1.14.11.2; 2681.
BRENDA; 1.14.11.29; 2681.
Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
SIGNOR; Q96KS0; -.
ChiTaRS; EGLN2; human.
GeneWiki; EGLN2; -.
GenomeRNAi; 112398; -.
PRO; PR:Q96KS0; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000269858; -.
CleanEx; HS_EGLN2; -.
ExpressionAtlas; Q96KS0; baseline and differential.
Genevisible; Q96KS0; HS.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0008198; F:ferrous iron binding; NAS:UniProtKB.
GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
GO; GO:0016706; F: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; IDA:UniProtKB.
GO; GO:0019826; F:oxygen sensor activity; IDA:UniProtKB.
GO; GO:0031545; F:peptidyl-proline 4-dioxygenase activity; IDA:FlyBase.
GO; GO:0045454; P:cell redox homeostasis; IDA:UniProtKB.
GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; NAS:UniProtKB.
GO; GO:0018401; P:peptidyl-proline hydroxylation to 4-hydroxy-L-proline; IDA:FlyBase.
GO; GO:0045732; P:positive regulation of protein catabolic process; IDA:UniProtKB.
GO; GO:0001558; P:regulation of cell growth; NAS:UniProtKB.
GO; GO:0043523; P:regulation of neuron apoptotic process; IMP:UniProtKB.
GO; GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; TAS:Reactome.
GO; GO:0001666; P:response to hypoxia; IDA:UniProtKB.
InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
InterPro; IPR006620; Pro_4_hyd_alph.
Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
SMART; SM00702; P4Hc; 1.
PROSITE; PS51471; FE2OG_OXY; 1.
1: Evidence at protein level;
3D-structure; Alternative initiation; Complete proteome; Dioxygenase;
Iron; Metal-binding; Nucleus; Oxidoreductase; Phosphoprotein;
Reference proteome; Vitamin C.
CHAIN 1 407 Egl nine homolog 2.
/FTId=PRO_0000206664.
DOMAIN 278 376 Fe2OG dioxygenase. {ECO:0000255|PROSITE-
ProRule:PRU00805}.
REGION 225 235 Beta(2)beta(3) 'finger-like' loop.
MOTIF 89 134 Bipartite nuclear localization signal.
METAL 297 297 Iron. {ECO:0000255|PROSITE-
ProRule:PRU00805}.
METAL 299 299 Iron. {ECO:0000255|PROSITE-
ProRule:PRU00805}.
METAL 358 358 Iron. {ECO:0000255|PROSITE-
ProRule:PRU00805}.
BINDING 367 367 2-oxoglutarate. {ECO:0000255|PROSITE-
ProRule:PRU00805}.
MOD_RES 130 130 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 33 Missing (in isoform p40). {ECO:0000305}.
/FTId=VSP_038836.
MUTAGEN 1 1 M->A: Leads to expression of isoform p40
only. {ECO:0000269|PubMed:16509823}.
MUTAGEN 34 34 M->A: Leads to expression of isoform p43
only. {ECO:0000269|PubMed:16509823}.
MUTAGEN 102 102 K->A: Retained in the nucleus.
{ECO:0000269|PubMed:19339211}.
MUTAGEN 106 106 R->A: Retained in the nucleus.
{ECO:0000269|PubMed:19339211}.
MUTAGEN 113 113 R->A: Retained in the nucleus.
{ECO:0000269|PubMed:19339211}.
MUTAGEN 119 119 R->A: Cytoplasmic and nuclear
localization. Reduced transcriptional
activity of HIF1A as for wild type.
{ECO:0000269|PubMed:19339211}.
MUTAGEN 134 134 R->A: Retained in the nucleus.
{ECO:0000269|PubMed:19339211}.
MUTAGEN 297 297 H->A: Eliminates hydroxylase activity.
{ECO:0000269|PubMed:12039559}.
MUTAGEN 299 299 D->A: Eliminates hydroxylase activity.
{ECO:0000269|PubMed:12039559}.
MUTAGEN 358 358 H->A: Eliminates hydroxylase activity.
{ECO:0000269|PubMed:11595184,
ECO:0000269|PubMed:12039559}.
MUTAGEN 367 367 R->A: Eliminates hydroxylase activity.
{ECO:0000269|PubMed:12039559}.
MUTAGEN 367 367 R->K: Eliminates hydroxylase activity on
a HIF1A peptide.
{ECO:0000269|PubMed:12039559}.
CONFLICT 176 176 R -> P (in Ref. 2; AAK82943).
{ECO:0000305}.
SEQUENCE 407 AA; 43650 MW; F172E9B0482C9CF3 CRC64;
MDSPCQPQPL SQALPQLPGS SSEPLEPEPG RARMGVESYL PCPLLPSYHC PGVPSEASAG
SGTPRATATS TTASPLRDGF GGQDGGELRP LQSEGAAALV TKGCQRLAAQ GARPEAPKRK
WAEDGGDAPS PSKRPWARQE NQEAEREGGM SCSCSSGSGE ASAGLMEEAL PSAPERLALD
YIVPCMRYYG ICVKDSFLGA ALGGRVLAEV EALKRGGRLR DGQLVSQRAI PPRSIRGDQI
AWVEGHEPGC RSIGALMAHV DAVIRHCAGR LGSYVINGRT KAMVACYPGN GLGYVRHVDN
PHGDGRCITC IYYLNQNWDV KVHGGLLQIF PEGRPVVANI EPLFDRLLIF WSDRRNPHEV
KPAYATRYAI TVWYFDAKER AAAKDKYQLA SGQKGVQVPV SQPPTPT


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