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Egl nine homolog 1 (EC 1.14.11.29) (Hypoxia-inducible factor prolyl hydroxylase 2) (HIF-PH2) (HIF-prolyl hydroxylase 2) (HPH-2) (Prolyl hydroxylase domain-containing protein 2) (PHD2) (SM-20)

 EGLN1_HUMAN             Reviewed;         426 AA.
Q9GZT9; Q8N3M8; Q9BZS8; Q9BZT0;
16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
25-OCT-2017, entry version 165.
RecName: Full=Egl nine homolog 1;
EC=1.14.11.29 {ECO:0000269|PubMed:25129147};
AltName: Full=Hypoxia-inducible factor prolyl hydroxylase 2;
Short=HIF-PH2;
Short=HIF-prolyl hydroxylase 2;
Short=HPH-2;
AltName: Full=Prolyl hydroxylase domain-containing protein 2;
Short=PHD2;
AltName: Full=SM-20;
Name=EGLN1 {ECO:0000312|HGNC:HGNC:1232}; Synonyms=C1orf12;
ORFNames=PNAS-118, PNAS-137;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND TISSUE
SPECIFICITY.
PubMed=11056053; DOI=10.1006/geno.2000.6343;
Dupuy D., Aubert I., Duperat V.G., Petit J., Taine L., Stef M.,
Bloch B., Arveiler B.;
"Mapping, characterization, and expression analysis of the SM-20 human
homologue, C1orf12, and identification of a novel related gene,
SCAND2.";
Genomics 69:348-354(2000).
[2]
NUCLEOTIDE SEQUENCE (ISOFORM 1).
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).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY, AND
SUBSTRATE SPECIFICITY.
TISSUE=Aorta, Colon, and Lung;
PubMed=12788921; DOI=10.1074/jbc.M304982200;
Hirsila M., Koivunen P., Gunzler V., Kivirikko K.I., Myllyharju J.;
"Characterization of the human prolyl 4-hydroxylases that modify the
hypoxia-inducible factor.";
J. Biol. Chem. 278:30772-30780(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 160-426 (ISOFORM 1).
TISSUE=Amygdala;
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=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 136-426 (ISOFORM 2).
TISSUE=Promyelocytic leukemia;
Yu W.-Q., Sun B.-Z., Chai Y.-B., Zhu F., Liu X.-S., Li Z., Lu F.,
Yan W., Yang H., Zhao Z.-L.;
"Human acute promyelocytic leukemia cell line NB4's apoptosis related
genes.";
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
[7]
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).
[8]
FUNCTION.
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).
[9]
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).
[10]
FUNCTION.
PubMed=12351678; DOI=10.1073/pnas.192342099;
Ivan M., Haberberger T., Gervasi D.C., Michelson K.S., Guenzler V.,
Kondo K., Yang H., Sorokina I., Conaway R.C., Conaway J.W.,
Kaelin W.G. Jr.;
"Biochemical purification and pharmacological inhibition of a
mammalian prolyl hydroxylase acting on hypoxia-inducible factor.";
Proc. Natl. Acad. Sci. U.S.A. 99:13459-13464(2002).
[11]
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).
[12]
TISSUE SPECIFICITY, AND ENZYME REGULATION.
PubMed=12670503; DOI=10.1016/S0006-291X(03)00453-4;
Cioffi C.L., Qin Liu X., Kosinski P.A., Garay M., Bowen B.R.;
"Differential regulation of HIF-1alpha prolyl-4-hydroxylase genes by
hypoxia in human cardiovascular cells.";
Biochem. Biophys. Res. Commun. 303:947-953(2003).
[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]
INTERACTION WITH ING4, AND FUNCTION.
PubMed=15897452; DOI=10.1073/pnas.0502716102;
Ozer A., Wu L.C., Bruick R.K.;
"The candidate tumor suppressor ING4 represses activation of the
hypoxia inducible factor (HIF).";
Proc. Natl. Acad. Sci. U.S.A. 102:7481-7486(2005).
[16]
SUBSTRATE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY,
MUTAGENESIS OF 237-ASP--ILE-251, AND DOMAIN.
PubMed=18063574; DOI=10.1074/jbc.M707411200;
Flashman E., Bagg E.A., Chowdhury R., Mecinovic J., Loenarz C.,
McDonough M.A., Hewitson K.S., Schofield C.J.;
"Kinetic rationale for selectivity toward N- and C-terminal oxygen-
dependent degradation domain substrates mediated by a loop region of
hypoxia-inducible factor prolyl hydroxylases.";
J. Biol. Chem. 283:3808-3815(2008).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[18]
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).
[19]
SUBCELLULAR LOCATION, AND FUNCTION.
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).
[20]
INTERACTION WITH EPAS1.
PubMed=19208626; DOI=10.1074/jbc.M808737200;
Furlow P.W., Percy M.J., Sutherland S., Bierl C., McMullin M.F.,
Master S.R., Lappin T.R., Lee F.S.;
"Erythrocytosis-associated HIF-2alpha mutations demonstrate a critical
role for residues C-terminal to the hydroxylacceptor proline.";
J. Biol. Chem. 284:9050-9058(2009).
[21]
ENZYME REGULATION.
PubMed=20840591; DOI=10.1111/j.1742-4658.2010.07804.x;
Flashman E., Hoffart L.M., Hamed R.B., Bollinger J.M. Jr., Krebs C.,
Schofield C.J.;
"Evidence for the slow reaction of hypoxia-inducible factor prolyl
hydroxylase 2 with oxygen.";
FEBS J. 277:4089-4099(2010).
[22]
POLYMORPHISM.
PubMed=20838600; DOI=10.1371/journal.pgen.1001116;
Bigham A., Bauchet M., Pinto D., Mao X., Akey J.M., Mei R.,
Scherer S.W., Julian C.G., Wilson M.J., Lopez Herraez D.,
Brutsaert T., Parra E.J., Moore L.G., Shriver M.D.;
"Identifying signatures of natural selection in Tibetan and Andean
populations using dense genome scan data.";
PLoS Genet. 6:E1001116-E1001116(2010).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[24]
POLYMORPHISM.
PubMed=20466884; DOI=10.1126/science.1189406;
Simonson T.S., Yang Y., Huff C.D., Yun H., Qin G., Witherspoon D.J.,
Bai Z., Lorenzo F.R., Xing J., Jorde L.B., Prchal J.T., Ge R.;
"Genetic evidence for high-altitude adaptation in Tibet.";
Science 329:72-75(2010).
[25]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[26]
FUNCTION, AND INDUCTION.
PubMed=21792862; DOI=10.1002/cncr.26344;
Su Y., Loos M., Giese N., Metzen E., Buchler M.W., Friess H.,
Kornberg A., Buchler P.;
"Prolyl hydroxylase-2 (PHD2) exerts tumor-suppressive activity in
pancreatic cancer.";
Cancer 118:960-972(2012).
[27]
INTERACTION WITH LIMD1, AND IDENTIFICATION IN A COMPLEX WITH LIMD1;
VHL; ELOB AND CUL2.
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).
[28]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 AND SER-125, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and 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).
[30]
INTERACTION WITH HIF1A.
PubMed=24681946; DOI=10.1038/onc.2014.76;
Seo K.S., Park J.H., Heo J.Y., Jing K., Han J., Min K.N., Kim C.,
Koh G.Y., Lim K., Kang G.Y., Uee Lee J., Yim Y.H., Shong M.,
Kwak T.H., Kweon G.R.;
"SIRT2 regulates tumour hypoxia response by promoting HIF-1alpha
hydroxylation.";
Oncogene 34:1354-1362(2015).
[31]
INTERACTION WITH CBFA2T3 AND HIF1A.
PubMed=25974097; DOI=10.1371/journal.pone.0123725;
Kumar P., Gullberg U., Olsson I., Ajore R.;
"Myeloid translocation gene-16 co-repressor promotes degradation of
hypoxia-inducible factor 1.";
PLoS ONE 10:E0123725-E0123725(2015).
[32]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 181-417 IN COMPLEXES WITH
IRON AND COMPETITIVE INHIBITOR, METAL-BINDING SITES, MUTAGENESIS OF
TYR-303 AND ARG-383, SUBUNIT, AND COFACTOR.
PubMed=16782814; DOI=10.1073/pnas.0601283103;
McDonough M.A., Li V., Flashman E., Chowdhury R., Mohr C.,
Lienard B.M.R., Zondlo J., Oldham N.J., Clifton I.J., Lewis J.,
McNeill L.A., Kurzeja R.J., Hewitson K.S., Yang E., Jordan S.,
Syed R.S., Schofield C.J.;
"Cellular oxygen sensing: crystal structure of hypoxia-inducible
factor prolyl hydroxylase (PHD2).";
Proc. Natl. Acad. Sci. U.S.A. 103:9814-9819(2006).
[33]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 181-426 OF WILD TYPE AND
MUTANTS ALA-252; ALA-254; LYS-254 AND ALA-398 IN COMPLEX WITH HIF1A,
IRON, N-OXALYGLYCINE AND MANGANESE, METAL-BINDING SITES, AND COFACTOR.
PubMed=19604478; DOI=10.1016/j.str.2009.06.002;
Chowdhury R., McDonough M.A., Mecinovic J., Loenarz C., Flashman E.,
Hewitson K.S., Domene C., Schofield C.J.;
"Structural basis for binding of hypoxia-inducible factor to the
oxygen-sensing prolyl hydroxylases.";
Structure 17:981-989(2009).
[34]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 181-426 IN COMPLEX WITH
NITRIC OXIDE OR A NITRIC OXIDE TRANSFER REAGENT, IDENTIFICATION BY
MASS SPECTROMETRY, S-NITROSYLATION AT CYS-201; CYS-208; CYS-302;
CYS-323 AND CYS-326, AND MUTAGENESIS OF CYS-201; CYS-208; CYS-266;
CYS-283; CYS-302; CYS-323 AND CYS-326.
PubMed=21601578; DOI=10.1016/j.jmb.2011.04.075;
Chowdhury R., Flashman E., Mecinovic J., Kramer H.B., Kessler B.M.,
Frapart Y.M., Boucher J.L., Clifton I.J., McDonough M.A.,
Schofield C.J.;
"Studies on the reaction of nitric oxide with the hypoxia-inducible
factor prolyl hydroxylase domain 2 (EGLN1).";
J. Mol. Biol. 410:268-279(2011).
[35]
VARIANT ECYT3 ARG-317, AND CHARACTERIZATION OF VARIANT ECYT3 ARG-317.
PubMed=16407130; DOI=10.1073/pnas.0508423103;
Percy M.J., Zhao Q., Flores A., Harrison C., Lappin T.R.,
Maxwell P.H., McMullin M.F., Lee F.S.;
"A family with erythrocytosis establishes a role for prolyl
hydroxylase domain protein 2 in oxygen homeostasis.";
Proc. Natl. Acad. Sci. U.S.A. 103:654-659(2006).
[36]
VARIANT ECYT3 HIS-371, AND CHARACTERIZATION OF VARIANT EXCYT3 HIS-371.
PubMed=17579185; DOI=10.1182/blood-2007-04-084434;
Percy M.J., Furlow P.W., Beer P.A., Lappin T.R.J., McMullin M.F.,
Lee F.S.;
"A novel erythrocytosis-associated PHD2 mutation suggests the location
of a HIF binding groove.";
Blood 110:2193-2196(2007).
[37]
VARIANTS GLU-4 AND SER-127, POLYMORPHISM, INTERACTION WITH PTGES3, AND
CHARACTERIZATION OF VARIANTS GLU-4 AND SER-127.
PubMed=24711448; DOI=10.1074/jbc.M113.541227;
Song D., Li L.S., Arsenault P.R., Tan Q., Bigham A.W.,
Heaton-Johnson K.J., Master S.R., Lee F.S.;
"Defective Tibetan PHD2 binding to p23 links high altitude adaption to
altered oxygen sensing.";
J. Biol. Chem. 289:14656-14665(2014).
[38]
VARIANTS GLU-4 AND SER-127, FUNCTION, CATALYTIC ACTIVITY,
BIOPHYSICOCHEMICAL PROPERTIES, POLYMORPHISM, AND CHARACTERIZATION OF
VARIANTS GLU-4 AND SER-127.
PubMed=25129147; DOI=10.1038/ng.3067;
Lorenzo F.R., Huff C., Myllymaeki M., Olenchock B., Swierczek S.,
Tashi T., Gordeuk V., Wuren T., Ri-Li G., McClain D.A., Khan T.M.,
Koul P.A., Guchhait P., Salama M.E., Xing J., Semenza G.L.,
Liberzon E., Wilson A., Simonson T.S., Jorde L.B., Kaelin W.G. Jr.,
Koivunen P., Prchal J.T.;
"A genetic mechanism for Tibetan high-altitude adaptation.";
Nat. Genet. 46:951-956(2014).
-!- 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 HIF1B. 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. EGLN1 is the most
important isozyme under normoxia and, through regulating the
stability of HIF1, involved in various hypoxia-influenced
processes such as angiogenesis in retinal and cardiac
functionality. Target proteins are preferentially recognized via a
LXXLAP motif. {ECO:0000269|PubMed:11595184,
ECO:0000269|PubMed:12181324, ECO:0000269|PubMed:12351678,
ECO:0000269|PubMed:15897452, ECO:0000269|PubMed:19339211,
ECO:0000269|PubMed:21792862, ECO:0000269|PubMed:25129147}.
-!- CATALYTIC ACTIVITY: Hypoxia-inducible factor-L-proline + 2-
oxoglutarate + O(2) = hypoxia-inducible factor-trans-4-hydroxy-L-
proline + succinate + CO(2). {ECO:0000269|PubMed:25129147}.
-!- COFACTOR:
Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
Evidence={ECO:0000255|PROSITE-ProRule:PRU00805,
ECO:0000269|PubMed:16782814, ECO:0000269|PubMed:19604478};
Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
ProRule:PRU00805, ECO:0000269|PubMed:16782814,
ECO:0000269|PubMed:19604478};
-!- COFACTOR:
Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
Evidence={ECO:0000269|PubMed:19604478};
-!- ENZYME REGULATION: Following exposure to hypoxia, activated in
HeLa cells but not in cardiovascular cells.
{ECO:0000269|PubMed:12670503, ECO:0000269|PubMed:20840591}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=70 nM for HIF2A {ECO:0000269|PubMed:25129147};
KM=150 uM for O(2) {ECO:0000269|PubMed:25129147};
KM=1.3 uM for 2-oxoglutarate {ECO:0000269|PubMed:25129147};
-!- SUBUNIT: Monomer. Interacts with ING4; the interaction inhibits
the hydroxylation of HIF alpha proteins. Interacts with PTGES3
(via PXLE motif); thereby recruiting EGLN1 to the HSP90 pathway to
facilitate HIF alpha proteins hydroxylation. Interacts with LIMD1.
Found in a complex composed of LIMD1, VHL, EGLN1/PHD2, ELOB and
CUL2. Interacts with EPAS1. Interacts with CBFA2T3
(PubMed:25974097). Interacts with HIF1A (PubMed:25974097).
{ECO:0000269|PubMed:15897452, ECO:0000269|PubMed:16782814,
ECO:0000269|PubMed:19208626, ECO:0000269|PubMed:19604478,
ECO:0000269|PubMed:21601578, ECO:0000269|PubMed:22286099,
ECO:0000269|PubMed:24681946, ECO:0000269|PubMed:25974097}.
-!- INTERACTION:
Q9WMX2:- (xeno); NbExp=3; IntAct=EBI-1174818, EBI-6863748;
Q99814:EPAS1; NbExp=2; IntAct=EBI-1174818, EBI-447470;
Q14318:FKBP8; NbExp=6; IntAct=EBI-1174818, EBI-724839;
Q16665:HIF1A; NbExp=4; IntAct=EBI-1174818, EBI-447269;
Q13438:OS9; NbExp=4; IntAct=EBI-1174818, EBI-725454;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12615973,
ECO:0000269|PubMed:19339211, ECO:0000269|PubMed:19631610}. Nucleus
{ECO:0000269|PubMed:12615973, ECO:0000269|PubMed:19339211,
ECO:0000269|PubMed:19631610}. Note=Mainly cytoplasmic. Shuttles
between the nucleus and cytoplasm (PubMed:19631610). Nuclear
export requires functional XPO1. {ECO:0000269|PubMed:19339211,
ECO:0000269|PubMed:19631610}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9GZT9-1; Sequence=Displayed;
Name=2;
IsoId=Q9GZT9-2; Sequence=VSP_007569;
Note=Inactive isoform.;
Name=3;
IsoId=Q9GZT9-3; Sequence=VSP_042191;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: According to PubMed:11056053, widely expressed
with highest levels in skeletal muscle and heart, moderate levels
in pancreas, brain (dopaminergic neurons of adult and fetal
substantia nigra) and kidney, and lower levels in lung and liver.
According to PubMed:12351678 widely expressed with highest levels
in brain, kidney and adrenal gland. Expressed in cardiac myocytes,
aortic endothelial cells and coronary artery smooth muscle.
According to PubMed:12788921; expressed in adult and fetal heart,
brain, liver, lung, skeletal muscle and kidney. Also expressed in
placenta. Highest levels in adult heart, brain, lung and liver and
fetal brain, heart spleen and skeletal muscle.
{ECO:0000269|PubMed:11056053, ECO:0000269|PubMed:12163023,
ECO:0000269|PubMed:12351678, ECO:0000269|PubMed:12670503,
ECO:0000269|PubMed:12788921}.
-!- DOMAIN: The beta(2)beta(3) 'finger-like' loop domain is important
for substrate (HIFs' CODD/NODD) selectivity.
{ECO:0000269|PubMed:18063574}.
-!- PTM: S-nitrosylation inhibits the enzyme activity up to 60% under
aerobic conditions. Chelation of Fe(2+) has no effect on the S-
nitrosylation. It is uncertain whether nitrosylation occurs on
Cys-323 or Cys-326. {ECO:0000269|PubMed:21601578}.
-!- POLYMORPHISM: Variations in EGLN1 are associated with adaptation
to high altitude (PubMed:20838600, PubMed:20466884,
PubMed:24711448, PubMed:25129147). High-altitude hypoxia (reduced
inspired oxygen tension due to decreased barometric pressure)
exerts severe physiological stress on the human body and leads to
an elevation of hematocrit levels and an increased number of
erythrocytes (polycythemia) in non-adapted individuals. Genetic
variations in EGLN1 contribute to adaptation to high altitute by
maintaining hematocrit levels comparable to those for populations
living at sea level and are present in two high-altitude regions
where humans have lived for millennia, the Andean Altiplano and
the Tibetan Plateau (PubMed:20838600, PubMed:20466884). Variants
Glu-4 and Ser-127, which are frequently associated together and
are present in the majority of Tibetan populations, participate in
adaptation to high altitude (PubMed:24711448, PubMed:25129147).
Molecular mechanisms explaining this adaptation are however
unclear. According to a report, variants Glu-4 and Ser-127 lead to
decreased interaction with PTGES3 and subsequent decrease of HIF
alpha proteins degradation (PubMed:24711448). According to a
second report, Glu-4 and Ser-127 haplotype enhances the catalytic
activity under hypoxic conditions, promoting increased HIF alpha
proteins degradation, thereby abrogating hypoxia-induced and HIF
alpha-mediated augmentation of erythropoiesis and protecting
Tibetans from polycythemia at high altitude (PubMed:25129147).
{ECO:0000269|PubMed:20466884, ECO:0000269|PubMed:20838600,
ECO:0000269|PubMed:24711448, ECO:0000269|PubMed:25129147,
ECO:0000305}.
-!- DISEASE: Erythrocytosis, familial, 3 (ECYT3) [MIM:609820]: An
autosomal dominant disorder characterized by increased serum red
blood cell mass, elevated serum hemoglobin and hematocrit, and
normal serum erythropoietin levels. {ECO:0000269|PubMed:16407130,
ECO:0000269|PubMed:17579185}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- CAUTION: It was previously reported that this protein was the
ortholog of rat SM-20. However, EGLN3 is now considered the true
ortholog of rat SM-20 since it shows substantially greater
similarity. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAK07534.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAK07536.1; Type=Frameshift; Positions=239; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/EGLN1ID44140ch1q42.html";
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AF246631; AAG34568.1; -; Genomic_DNA.
EMBL; AF246630; AAG34568.1; JOINED; Genomic_DNA.
EMBL; AF229245; AAG33965.1; -; mRNA.
EMBL; AJ310543; CAC42509.1; -; mRNA.
EMBL; AL833885; CAD38741.2; -; mRNA.
EMBL; AF277174; AAK07534.1; ALT_INIT; mRNA.
EMBL; AF277176; AAK07536.1; ALT_FRAME; mRNA.
EMBL; AL117352; CAI23092.1; -; Genomic_DNA.
EMBL; AL445524; CAI23092.1; JOINED; Genomic_DNA.
EMBL; AL445524; CAH72105.1; -; Genomic_DNA.
EMBL; AL117352; CAH72105.1; JOINED; Genomic_DNA.
CCDS; CCDS1595.1; -. [Q9GZT9-1]
RefSeq; NP_071334.1; NM_022051.2. [Q9GZT9-1]
UniGene; Hs.444450; -.
PDB; 2G19; X-ray; 1.70 A; A=181-417.
PDB; 2G1M; X-ray; 2.20 A; A=181-426.
PDB; 2HBT; X-ray; 1.60 A; A=188-426.
PDB; 2HBU; X-ray; 1.85 A; A=188-426.
PDB; 2Y33; X-ray; 2.00 A; A=181-426.
PDB; 2Y34; X-ray; 2.01 A; A=181-426.
PDB; 3HQR; X-ray; 2.00 A; A=181-426.
PDB; 3HQU; X-ray; 2.30 A; A=181-426.
PDB; 3OUH; X-ray; 2.51 A; A=181-416.
PDB; 3OUI; X-ray; 1.70 A; A=181-392.
PDB; 3OUJ; X-ray; 2.30 A; A=181-416.
PDB; 4BQW; X-ray; 1.79 A; A=181-426.
PDB; 4BQX; X-ray; 1.79 A; A=181-426.
PDB; 4BQY; X-ray; 1.53 A; A=181-426.
PDB; 4JZR; X-ray; 2.10 A; A=189-399.
PDB; 4KBZ; X-ray; 2.15 A; A=184-419.
PDB; 4UWD; X-ray; 1.72 A; A=181-426.
PDB; 5A3U; X-ray; 3.30 A; A/B/C=181-426.
PDB; 5L9B; X-ray; 1.95 A; A/B=181-426.
PDB; 5L9R; X-ray; 1.81 A; A=181-426.
PDB; 5L9V; X-ray; 1.83 A; A/B=181-426.
PDB; 5LA9; X-ray; 2.81 A; A/B=181-426.
PDB; 5LAS; X-ray; 2.10 A; A/B=181-426.
PDB; 5LAT; X-ray; 1.90 A; A=181-426.
PDB; 5LB6; X-ray; 1.70 A; A=181-426.
PDB; 5LBB; X-ray; 1.70 A; A=181-426.
PDB; 5LBC; X-ray; 1.82 A; A=181-426.
PDB; 5LBE; X-ray; 1.75 A; A=181-426.
PDB; 5LBF; X-ray; 1.90 A; A=181-426.
PDB; 5V18; X-ray; 2.15 A; A=181-416.
PDBsum; 2G19; -.
PDBsum; 2G1M; -.
PDBsum; 2HBT; -.
PDBsum; 2HBU; -.
PDBsum; 2Y33; -.
PDBsum; 2Y34; -.
PDBsum; 3HQR; -.
PDBsum; 3HQU; -.
PDBsum; 3OUH; -.
PDBsum; 3OUI; -.
PDBsum; 3OUJ; -.
PDBsum; 4BQW; -.
PDBsum; 4BQX; -.
PDBsum; 4BQY; -.
PDBsum; 4JZR; -.
PDBsum; 4KBZ; -.
PDBsum; 4UWD; -.
PDBsum; 5A3U; -.
PDBsum; 5L9B; -.
PDBsum; 5L9R; -.
PDBsum; 5L9V; -.
PDBsum; 5LA9; -.
PDBsum; 5LAS; -.
PDBsum; 5LAT; -.
PDBsum; 5LB6; -.
PDBsum; 5LBB; -.
PDBsum; 5LBC; -.
PDBsum; 5LBE; -.
PDBsum; 5LBF; -.
PDBsum; 5V18; -.
ProteinModelPortal; Q9GZT9; -.
SMR; Q9GZT9; -.
BioGrid; 120060; 37.
CORUM; Q9GZT9; -.
DIP; DIP-37495N; -.
ELM; Q9GZT9; -.
IntAct; Q9GZT9; 14.
MINT; MINT-1206232; -.
STRING; 9606.ENSP00000355601; -.
BindingDB; Q9GZT9; -.
ChEMBL; CHEMBL5697; -.
DrugBank; DB04847; FG-4592.
DrugBank; DB08687; N-[(1-CHLORO-4-HYDROXYISOQUINOLIN-3-YL)CARBONYL]GLYCINE.
DrugBank; DB07112; N-[(4-HYDROXY-8-IODOISOQUINOLIN-3-YL)CARBONYL]GLYCINE.
DrugBank; DB00126; Vitamin C.
GuidetoPHARMACOLOGY; 2833; -.
iPTMnet; Q9GZT9; -.
PhosphoSitePlus; Q9GZT9; -.
BioMuta; EGLN1; -.
DMDM; 32129514; -.
EPD; Q9GZT9; -.
PaxDb; Q9GZT9; -.
PeptideAtlas; Q9GZT9; -.
PRIDE; Q9GZT9; -.
Ensembl; ENST00000366641; ENSP00000355601; ENSG00000135766. [Q9GZT9-1]
GeneID; 54583; -.
KEGG; hsa:54583; -.
CTD; 54583; -.
DisGeNET; 54583; -.
EuPathDB; HostDB:ENSG00000135766.8; -.
GeneCards; EGLN1; -.
H-InvDB; HIX0159985; -.
HGNC; HGNC:1232; EGLN1.
HPA; HPA022129; -.
MalaCards; EGLN1; -.
MIM; 606425; gene.
MIM; 609820; phenotype.
neXtProt; NX_Q9GZT9; -.
OpenTargets; ENSG00000135766; -.
Orphanet; 247511; Autosomal dominant secondary polycythemia.
PharmGKB; PA27670; -.
eggNOG; KOG3710; Eukaryota.
eggNOG; ENOG410ZHZN; LUCA.
GeneTree; ENSGT00390000001936; -.
HOGENOM; HOG000004818; -.
HOVERGEN; HBG051455; -.
InParanoid; Q9GZT9; -.
KO; K09592; -.
OMA; KANLYPP; -.
OrthoDB; EOG091G03SP; -.
PhylomeDB; Q9GZT9; -.
TreeFam; TF314595; -.
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.
ChiTaRS; EGLN1; human.
EvolutionaryTrace; Q9GZT9; -.
GeneWiki; EGLN1; -.
GenomeRNAi; 54583; -.
PRO; PR:Q9GZT9; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000135766; -.
CleanEx; HS_EGLN1; -.
ExpressionAtlas; Q9GZT9; baseline and differential.
Genevisible; Q9GZT9; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0019899; F:enzyme binding; ISS:BHF-UCL.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
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:MGI.
GO; GO:0031545; F:peptidyl-proline 4-dioxygenase activity; IDA:FlyBase.
GO; GO:0031543; F:peptidyl-proline dioxygenase activity; TAS:HGNC.
GO; GO:0055008; P:cardiac muscle tissue morphogenesis; IEA:Ensembl.
GO; GO:0006879; P:cellular iron ion homeostasis; IEA:Ensembl.
GO; GO:0060347; P:heart trabecula formation; IEA:Ensembl.
GO; GO:0060711; P:labyrinthine layer development; IEA:Ensembl.
GO; GO:0030821; P:negative regulation of cAMP catabolic process; ISS:BHF-UCL.
GO; GO:0051344; P:negative regulation of cyclic-nucleotide phosphodiesterase activity; ISS:BHF-UCL.
GO; GO:0043433; P:negative regulation of sequence-specific DNA binding transcription factor activity; IDA:HGNC.
GO; GO:0032364; P:oxygen homeostasis; IDA:HGNC.
GO; GO:0018401; P:peptidyl-proline hydroxylation to 4-hydroxy-L-proline; IDA:FlyBase.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0045765; P:regulation of angiogenesis; ISS:UniProtKB.
GO; GO:1901214; P:regulation of neuron death; IEA:Ensembl.
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:HGNC.
GO; GO:0071731; P:response to nitric oxide; IDA:UniProtKB.
GO; GO:0060412; P:ventricular septum morphogenesis; IEA:Ensembl.
InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
InterPro; IPR006620; Pro_4_hyd_alph.
InterPro; IPR002893; Znf_MYND.
Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
Pfam; PF01753; zf-MYND; 1.
SMART; SM00702; P4Hc; 1.
PROSITE; PS51471; FE2OG_OXY; 1.
PROSITE; PS01360; ZF_MYND_1; 1.
PROSITE; PS50865; ZF_MYND_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Congenital erythrocytosis; Cytoplasm; Dioxygenase; Disease mutation;
Iron; Metal-binding; Nucleus; Oxidoreductase; Phosphoprotein;
Polymorphism; Reference proteome; S-nitrosylation; Vitamin C; Zinc;
Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22814378}.
CHAIN 2 426 Egl nine homolog 1.
/FTId=PRO_0000206661.
DOMAIN 291 392 Fe2OG dioxygenase. {ECO:0000255|PROSITE-
ProRule:PRU00805}.
ZN_FING 21 58 MYND-type. {ECO:0000255|PROSITE-
ProRule:PRU00134}.
REGION 6 20 Required for nuclear export.
REGION 241 251 Beta(2)beta(3) 'finger-like' loop.
{ECO:0000269|PubMed:18063574}.
METAL 313 313 Iron. {ECO:0000269|PubMed:16782814,
ECO:0000269|PubMed:19604478}.
METAL 315 315 Iron. {ECO:0000269|PubMed:16782814,
ECO:0000269|PubMed:19604478}.
METAL 374 374 Iron. {ECO:0000269|PubMed:16782814,
ECO:0000269|PubMed:19604478}.
BINDING 383 383 2-oxoglutarate.
{ECO:0000305|PubMed:19604478}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22814378}.
MOD_RES 12 12 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 125 125 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 201 201 S-nitrosocysteine.
{ECO:0000269|PubMed:21601578}.
MOD_RES 208 208 S-nitrosocysteine.
{ECO:0000269|PubMed:21601578}.
MOD_RES 302 302 S-nitrosocysteine.
{ECO:0000269|PubMed:21601578}.
MOD_RES 323 323 S-nitrosocysteine.
{ECO:0000269|PubMed:21601578}.
MOD_RES 326 326 S-nitrosocysteine.
{ECO:0000269|PubMed:21601578}.
VAR_SEQ 58 175 CQGSEGALGHGVGPHQHSGPAPPAAVPPPRAGAREPRKAAA
RRDNASGDAAKGKVKAKPPADPAAAASPCRAAAGGQGSAVA
AEAEPGKEEPPARSSLFQEKANLYPPSNTPGDALSP -> L
LGGYRFAFSWNSDERA (in isoform 3).
{ECO:0000303|PubMed:12788921}.
/FTId=VSP_042191.
VAR_SEQ 338 359 Missing (in isoform 2).
{ECO:0000303|Ref.6}.
/FTId=VSP_007569.
VARIANT 4 4 D -> E (polymorphism present in the
majority of Tibetans; increased
protection from polycythemia at high
altitude; when associated with S-127;
dbSNP:rs186996510).
{ECO:0000269|PubMed:24711448,
ECO:0000269|PubMed:25129147}.
/FTId=VAR_071858.
VARIANT 127 127 C -> S (polymorphism present in the
majority of Tibetans; increased
protection from polycythemia at high
altitude; when associated with E-4;
dbSNP:rs12097901).
{ECO:0000269|PubMed:24711448,
ECO:0000269|PubMed:25129147}.
/FTId=VAR_071859.
VARIANT 317 317 P -> R (in ECYT3; marked decrease in
enzyme activity; dbSNP:rs80358193).
{ECO:0000269|PubMed:16407130}.
/FTId=VAR_027371.
VARIANT 371 371 R -> H (in ECYT3; decreased interaction
with HIF1A and HIF2A and decreased enzyme
activity; dbSNP:rs119476044).
{ECO:0000269|PubMed:17579185}.
/FTId=VAR_045902.
MUTAGEN 201 201 C->A: Little change in enzyme activity.
{ECO:0000269|PubMed:21601578}.
MUTAGEN 208 208 C->A: Little change in enzyme activity.
{ECO:0000269|PubMed:21601578}.
MUTAGEN 252 252 R->A: Reduced C-terminal ODD domain
(CODD) hydroxylation of HIF1A.
MUTAGEN 254 254 D->A,K: Reduced C-terminal ODD domain
(CODD) hxdroxylation of HIF1A.
MUTAGEN 266 266 C->A: Little change in enzyme activity.
{ECO:0000269|PubMed:21601578}.
MUTAGEN 283 283 C->A: Little change in enzyme activity.
{ECO:0000269|PubMed:21601578}.
MUTAGEN 302 302 C->A: Slight increase in enzyme activity.
{ECO:0000269|PubMed:21601578}.
MUTAGEN 303 303 Y->F: No effect.
{ECO:0000269|PubMed:16782814}.
MUTAGEN 323 323 C->A: Little change in enzyme activity.
{ECO:0000269|PubMed:21601578}.
MUTAGEN 326 326 C->A: Slight increase in enzyme activity.
{ECO:0000269|PubMed:21601578}.
MUTAGEN 383 383 R->A: Reduces enzyme activity by 95%.
{ECO:0000269|PubMed:16782814}.
HELIX 190 196 {ECO:0000244|PDB:4BQY}.
HELIX 198 205 {ECO:0000244|PDB:4BQY}.
STRAND 206 214 {ECO:0000244|PDB:4BQY}.
HELIX 216 231 {ECO:0000244|PDB:4BQY}.
STRAND 240 242 {ECO:0000244|PDB:4BQY}.
HELIX 247 249 {ECO:0000244|PDB:4BQY}.
STRAND 255 259 {ECO:0000244|PDB:4BQY}.
HELIX 267 283 {ECO:0000244|PDB:4BQY}.
TURN 284 286 {ECO:0000244|PDB:4BQY}.
STRAND 287 289 {ECO:0000244|PDB:2G1M}.
STRAND 292 295 {ECO:0000244|PDB:4BQY}.
STRAND 298 303 {ECO:0000244|PDB:4BQY}.
STRAND 305 313 {ECO:0000244|PDB:4BQY}.
STRAND 315 318 {ECO:0000244|PDB:5LBB}.
STRAND 321 329 {ECO:0000244|PDB:4BQY}.
STRAND 331 333 {ECO:0000244|PDB:4KBZ}.
HELIX 336 339 {ECO:0000244|PDB:4BQY}.
STRAND 343 345 {ECO:0000244|PDB:4BQY}.
STRAND 348 351 {ECO:0000244|PDB:3OUH}.
STRAND 354 356 {ECO:0000244|PDB:4BQY}.
STRAND 362 367 {ECO:0000244|PDB:4BQY}.
STRAND 374 381 {ECO:0000244|PDB:4BQY}.
STRAND 383 392 {ECO:0000244|PDB:4BQY}.
HELIX 393 402 {ECO:0000244|PDB:4BQY}.
HELIX 407 409 {ECO:0000244|PDB:3OUJ}.
SEQUENCE 426 AA; 46021 MW; 81A97FF772CAA14C CRC64;
MANDSGGPGG PSPSERDRQY CELCGKMENL LRCSRCRSSF YCCKEHQRQD WKKHKLVCQG
SEGALGHGVG PHQHSGPAPP AAVPPPRAGA REPRKAAARR DNASGDAAKG KVKAKPPADP
AAAASPCRAA AGGQGSAVAA EAEPGKEEPP ARSSLFQEKA NLYPPSNTPG DALSPGGGLR
PNGQTKPLPA LKLALEYIVP CMNKHGICVV DDFLGKETGQ QIGDEVRALH DTGKFTDGQL
VSQKSDSSKD IRGDKITWIE GKEPGCETIG LLMSSMDDLI RHCNGKLGSY KINGRTKAMV
ACYPGNGTGY VRHVDNPNGD GRCVTCIYYL NKDWDAKVSG GILRIFPEGK AQFADIEPKF
DRLLFFWSDR RNPHEVQPAY ATRYAITVWY FDADERARAK VKYLTGEKGV RVELNKPSDS
VGKDVF


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EIAAB12617 Egl nine homolog 2,EGLN2,EIT6,Estrogen-induced tag 6,HIF-PH1,HIF-prolyl hydroxylase 1,Homo sapiens,HPH-1,HPH-3,Human,Hypoxia-inducible factor prolyl hydroxylase 1,PHD1,Prolyl hydroxylase domain-contai
EIAAB29551 HIF-PH4,HIF-prolyl hydroxylase 4,Homo sapiens,HPH-4,Human,Hypoxia-inducible factor prolyl hydroxylase 4,P4HTM,P4H-TM,PH4,Transmembrane prolyl 4-hydroxylase
EIAAB29550 HIF-PH4,HIF-prolyl hydroxylase 4,HPH-4,Hypoxia-inducible factor prolyl hydroxylase 4,Mouse,Mus musculus,P4htm,P4H-TM,Ph4,Transmembrane prolyl 4-hydroxylase
EIAAB12618 Egl nine homolog 2,Egln2,Falkor,HIF-PH1,HIF-prolyl hydroxylase 1,HPH-1,Hypoxia-inducible factor prolyl hydroxylase 1,Mouse,Mus musculus
EIAAB12619 Egl nine homolog 3, mitochondrial,Egln3,HIF-PH3,HIF-prolyl hydroxylase 3,HPH-3,Hypoxia-inducible factor prolyl hydroxylase 3,Rat,Rattus norvegicus,Sm20,SM-20
EIAAB12615 Egl nine homolog 1,Egln1,HIF-PH2,HIF-prolyl hydroxylase 2,HPH-2,Hypoxia-inducible factor prolyl hydroxylase 2,Rat,Rattus norvegicus
EIAAB12616 Egl nine homolog 1,Egln1,HIF-PH2,HIF-prolyl hydroxylase 2,HPH-2,Hypoxia-inducible factor prolyl hydroxylase 2,Mouse,Mus musculus,SM-20
EIAAB12621 Egl nine homolog 3,Egln3,HIF-PH3,HIF-prolyl hydroxylase 3,HPH-3,Hypoxia-inducible factor prolyl hydroxylase 3,Mouse,Mus musculus,SM-20
SCH-MCA2890P MOUSE ANTI HUMAN PROLYL HYDROXYLASE 3 HRP, Product Type Monoclonal Antibody, Specificity PROLYL HYDROXYLASE 3, Target Species Human, Host Mouse, Format HRP, Isotypes IgG1, Applications C, WB, C 0.1 mg
MCA2888P MOUSE ANTI HUMAN PROLYL HYDROXYLASE 1 HRP, Product Type Monoclonal Antibody, Specificity PROLYL HYDROXYLASE 1, Target Species Human, Host Mouse, Format HRP, Isotypes IgG2a, Applications P*, WB, 0.1 mg
SCH-MCA2888P MOUSE ANTI HUMAN PROLYL HYDROXYLASE 1 HRP, Product Type Monoclonal Antibody, Specificity PROLYL HYDROXYLASE 1, Target Species Human, Host Mouse, Format HRP, Isotypes IgG2a, Applications P*, WB, 0.1 mg
SCH-MCA2889P MOUSE ANTI HUMAN PROLYL HYDROXYLASE 2 HRP, Product Type Monoclonal Antibody, Specificity PROLYL HYDROXYLASE 2, Target Species Human, Host Mouse, Format HRP, Isotypes IgG1, Applications P, WB, C 0.1 mg
MCA2889P MOUSE ANTI HUMAN PROLYL HYDROXYLASE 2 HRP, Product Type Monoclonal Antibody, Specificity PROLYL HYDROXYLASE 2, Target Species Human, Host Mouse, Format HRP, Isotypes IgG1, Applications P, WB, C 0.1 mg
MCA2890P MOUSE ANTI HUMAN PROLYL HYDROXYLASE 3 HRP, Product Type Monoclonal Antibody, Specificity PROLYL HYDROXYLASE 3, Target Species Human, Host Mouse, Format HRP, Isotypes IgG1, Applications C, WB, C 0.1 mg
MCA2889GA MOUSE ANTI HUMAN PROLYL HYDROXYLASE 2, Product Type Monoclonal Antibody, Specificity PROLYL HYDROXYLASE 2, Target Species Human, Host Mouse, Format Purified, Isotypes IgG1, Applications P, WB, 0.1 mg
MCA2889 MOUSE ANTI HUMAN PROLYL HYDROXYLASE 2, Product Type Monoclonal Antibody, Specificity PROLYL HYDROXYLASE 2, Target Species Human, Host Mouse, Format Purified, Isotypes IgG1, Applications P, WB, 0.2 mg
SCH-MCA2888GA MOUSE ANTI HUMAN PROLYL HYDROXYLASE 1, Product Type Monoclonal Antibody, Specificity PROLYL HYDROXYLASE 1, Target Species Human, Host Mouse, Format Purified, Isotypes IgG2a, Applications P*, WB 0.1 mg
SCH-MCA2890GA MOUSE ANTI HUMAN PROLYL HYDROXYLASE 3, Product Type Monoclonal Antibody, Specificity PROLYL HYDROXYLASE 3, Target Species Human, Host Mouse, Format Purified, Isotypes IgG1, Applications C, WB, 0.1 mg
MCA2888GA MOUSE ANTI HUMAN PROLYL HYDROXYLASE 1, Product Type Monoclonal Antibody, Specificity PROLYL HYDROXYLASE 1, Target Species Human, Host Mouse, Format Purified, Isotypes IgG2a, Applications P*, WB 0.1 mg
MCA2888 MOUSE ANTI HUMAN PROLYL HYDROXYLASE 1, Product Type Monoclonal Antibody, Specificity PROLYL HYDROXYLASE 1, Target Species Human, Host Mouse, Format Purified, Isotypes IgG2a, Applications P*, WB 0.2 mg
SCH-MCA2889GA MOUSE ANTI HUMAN PROLYL HYDROXYLASE 2, Product Type Monoclonal Antibody, Specificity PROLYL HYDROXYLASE 2, Target Species Human, Host Mouse, Format Purified, Isotypes IgG1, Applications P, WB, 0.1 mg


 

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