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Prostaglandin E synthase 3 (EC 5.3.99.3) (Cytosolic prostaglandin E2 synthase) (cPGES) (Hsp90 co-chaperone) (Progesterone receptor complex p23) (Telomerase-binding protein p23)

 TEBP_HUMAN              Reviewed;         160 AA.
Q15185; A8K7D0; B4DHP2; B4DP11; B4DP21; Q8WU70;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
25-OCT-2017, entry version 176.
RecName: Full=Prostaglandin E synthase 3;
EC=5.3.99.3 {ECO:0000269|PubMed:10922363};
AltName: Full=Cytosolic prostaglandin E2 synthase;
Short=cPGES;
AltName: Full=Hsp90 co-chaperone;
AltName: Full=Progesterone receptor complex p23;
AltName: Full=Telomerase-binding protein p23;
Name=PTGES3; Synonyms=P23, TEBP;
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 1), AND PROGESTERONE
RECEPTOR-BINDING.
TISSUE=Testis;
PubMed=8114727; DOI=10.1128/MCB.14.3.1956;
Johnson J.L., Beito T.G., Krco C.J., Toft D.O.;
"Characterization of a novel 23-kilodalton protein of unactive
progesterone receptor complexes.";
Mol. Cell. Biol. 14:1956-1963(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
TISSUE=Caudate nucleus;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[4]
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.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung, and Urinary bladder;
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).
[6]
PROTEIN SEQUENCE OF 13-65; 72-88 AND 96-122, PHOSPHORYLATION AT
SER-113, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Embryonic kidney;
Bienvenut W.V., Waridel P., Quadroni M.;
Submitted (MAR-2009) to UniProtKB.
[7]
INTERACTION WITH TERT, AND FUNCTION AS A CO-CHAPERONE IN TELOMERASE
HOLOENZYME ASSEMBLY.
PubMed=11274138; DOI=10.1074/jbc.C100055200;
Forsythe H.L., Jarvis J.L., Turner J.W., Elmore L.W., Holt S.E.;
"Stable association of hsp90 and p23, but Not hsp70, with active human
telomerase.";
J. Biol. Chem. 276:15571-15574(2001).
[8]
FUNCTION AS A CHAPERONE.
PubMed=12077419; DOI=10.1126/science.1073051;
Freeman B.C., Yamamoto K.R.;
"Disassembly of transcriptional regulatory complexes by molecular
chaperones.";
Science 296:2232-2235(2002).
[9]
FUNCTION AS A PROSTAGLANDIN SYNTHASE, BIOPHYSICOCHEMICAL PROPERTIES,
CATALYTIC ACTIVITY, AND PATHWAY.
PubMed=10922363; DOI=10.1074/jbc.M003504200;
Tanioka T., Nakatani Y., Semmyo N., Murakami M., Kudo I.;
"Molecular identification of cytosolic prostaglandin E2 synthase that
is functionally coupled with cyclooxygenase-1 in immediate
prostaglandin E2 biosynthesis.";
J. Biol. Chem. 275:32775-32782(2000).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-118; SER-148
AND SER-151, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Pituitary;
PubMed=16807684; DOI=10.1007/s11102-006-8916-x;
Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.;
"Phosphoproteomic analysis of the human pituitary.";
Pituitary 9:109-120(2006).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Prostate cancer;
PubMed=17487921; DOI=10.1002/elps.200600782;
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
"Toward a global characterization of the phosphoproteome in prostate
cancer cells: identification of phosphoproteins in the LNCaP cell
line.";
Electrophoresis 28:2027-2034(2007).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=T-cell;
PubMed=19367720; DOI=10.1021/pr800500r;
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
"Phosphorylation analysis of primary human T lymphocytes using
sequential IMAC and titanium oxide enrichment.";
J. Proteome Res. 7:5167-5176(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-148 AND
SER-151, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-148 AND
SER-151, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18318008; DOI=10.1002/pmic.200700884;
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
Zou H., Gu J.;
"Large-scale phosphoproteome analysis of human liver tissue by
enrichment and fractionation of phosphopeptides with strong anion
exchange chromatography.";
Proteomics 8:1346-1361(2008).
[18]
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).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[21]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-33, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113 AND SER-118, 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).
[23]
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).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[25]
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).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44; SER-85 AND SER-113,
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).
[27]
FUNCTION, AND INTERACTION WITH EGLN1.
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).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85; SER-113; SER-148 AND
SER-151, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130 (ISOFORM
4), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[29]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[30]
INTERACTION WITH HSP90AA1; FLCN; FNIP1 AND FNIP2.
PubMed=27353360; DOI=10.1038/ncomms12037;
Woodford M.R., Dunn D.M., Blanden A.R., Capriotti D., Loiselle D.,
Prodromou C., Panaretou B., Hughes P.F., Smith A., Ackerman W.,
Haystead T.A., Loh S.N., Bourboulia D., Schmidt L.S.,
Marston Linehan W., Bratslavsky G., Mollapour M.;
"The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and
enhance drug binding.";
Nat. Commun. 7:12037-12037(2016).
[31]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-35 AND LYS-65, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[32]
X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) OF 1-125.
PubMed=10811660; DOI=10.1074/jbc.M003410200;
Weaver A.J., Sullivan W.P., Felts S.J., Owen B.A.L., Toft D.O.;
"Crystal structure and activity of human p23, a heat shock protein 90
co-chaperone.";
J. Biol. Chem. 275:23045-23052(2000).
-!- FUNCTION: Cytosolic prostaglandin synthase that catalyzes the
oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to
prostaglandin E2 (PGE2) (PubMed:10922363). Molecular chaperone
that localizes to genomic response elements in a hormone-dependent
manner and disrupts receptor-mediated transcriptional activation,
by promoting disassembly of transcriptional regulatory complexes
(PubMed:11274138, PubMed:12077419). Facilitates HIF alpha proteins
hydroxylation via interaction with EGLN1/PHD2, leading to recruit
EGLN1/PHD2 to the HSP90 pathway (PubMed:24711448).
{ECO:0000269|PubMed:10922363, ECO:0000269|PubMed:11274138,
ECO:0000269|PubMed:12077419, ECO:0000269|PubMed:24711448}.
-!- CATALYTIC ACTIVITY: (5Z,13E)-(15S)-9-alpha,11-alpha-epidioxy-15-
hydroxyprosta-5,13-dienoate = (5Z,13E)-(15S)-11-alpha,15-
dihydroxy-9-oxoprosta-5,13-dienoate.
{ECO:0000269|PubMed:10922363}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=14 uM for PGH2 {ECO:0000269|PubMed:10922363};
Vmax=190 nmol/min/mg enzyme toward PGH2
{ECO:0000269|PubMed:10922363};
-!- PATHWAY: Lipid metabolism; prostaglandin biosynthesis.
{ECO:0000269|PubMed:10922363}.
-!- SUBUNIT: Binds to the progesterone receptor (PubMed:8114727).
Interacts with TERT; the interaction, together with HSP90AA1, is
required for correct assembly and stabilization of the telomerase
holoenzyme complex (PubMed:11274138). Interacts (via PXLE motif)
with EGLN1/PHD2, recruiting EGLN1/PHD2 to the HSP90 pathway to
facilitate HIF alpha proteins hydroxylation (PubMed:24711448).
Interacts with HSP90AA1, FLCN, FNIP1 and FNIP2 (PubMed:27353360).
{ECO:0000269|PubMed:11274138, ECO:0000269|PubMed:24711448,
ECO:0000269|PubMed:27353360, ECO:0000269|PubMed:8114727}.
-!- INTERACTION:
Q9UKV8:AGO2; NbExp=3; IntAct=EBI-1049387, EBI-528269;
P07900:HSP90AA1; NbExp=6; IntAct=EBI-1049387, EBI-296047;
P08238:HSP90AB1; NbExp=4; IntAct=EBI-1049387, EBI-352572;
O14654:IRS4; NbExp=2; IntAct=EBI-1049387, EBI-356594;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q3ZBF7}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q15185-1; Sequence=Displayed;
Name=2;
IsoId=Q15185-2; Sequence=VSP_055363;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q15185-3; Sequence=VSP_055364;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q15185-4; Sequence=VSP_055365;
Note=No experimental confirmation available. Contains a
phosphoserine at position 130. {ECO:0000244|PubMed:24275569};
-!- DOMAIN: The PXLE motif mediates interaction with EGLN1/PHD2.
{ECO:0000269|PubMed:24711448}.
-!- SIMILARITY: Belongs to the p23/wos2 family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; L24804; AAA18537.1; -; mRNA.
EMBL; AK291945; BAF84634.1; -; mRNA.
EMBL; AK295208; BAG58204.1; -; mRNA.
EMBL; AK298147; BAG60423.1; -; mRNA.
EMBL; AK298160; BAG60433.1; -; mRNA.
EMBL; AC117378; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471054; EAW96953.1; -; Genomic_DNA.
EMBL; CH471054; EAW96958.1; -; Genomic_DNA.
EMBL; BC003005; AAH03005.1; -; mRNA.
EMBL; BC021167; AAH21167.1; -; mRNA.
CCDS; CCDS31836.1; -. [Q15185-1]
CCDS; CCDS61158.1; -. [Q15185-2]
CCDS; CCDS61159.1; -. [Q15185-3]
CCDS; CCDS61160.1; -. [Q15185-4]
PIR; A56211; A56211.
RefSeq; NP_001269530.1; NM_001282601.1. [Q15185-4]
RefSeq; NP_001269531.1; NM_001282602.1. [Q15185-3]
RefSeq; NP_001269532.1; NM_001282603.1. [Q15185-2]
RefSeq; NP_001269533.1; NM_001282604.1.
RefSeq; NP_001269534.1; NM_001282605.1.
RefSeq; NP_006592.3; NM_006601.6. [Q15185-1]
UniGene; Hs.50425; -.
PDB; 1EJF; X-ray; 2.49 A; A/B=1-125.
PDB; 1LG0; Model; -; A=1-110.
PDBsum; 1EJF; -.
PDBsum; 1LG0; -.
DisProt; DP00358; -.
ProteinModelPortal; Q15185; -.
SMR; Q15185; -.
BioGrid; 115952; 103.
CORUM; Q15185; -.
DIP; DIP-279N; -.
ELM; Q15185; -.
IntAct; Q15185; 49.
MINT; MINT-5000397; -.
STRING; 9606.ENSP00000262033; -.
ChEMBL; CHEMBL3341580; -.
DrugBank; DB05036; Grn163l.
SwissLipids; SLP:000000831; -.
iPTMnet; Q15185; -.
PhosphoSitePlus; Q15185; -.
SwissPalm; Q15185; -.
EPD; Q15185; -.
MaxQB; Q15185; -.
PaxDb; Q15185; -.
PeptideAtlas; Q15185; -.
PRIDE; Q15185; -.
TopDownProteomics; Q15185-1; -. [Q15185-1]
DNASU; 10728; -.
Ensembl; ENST00000262033; ENSP00000262033; ENSG00000110958. [Q15185-1]
Ensembl; ENST00000414274; ENSP00000405299; ENSG00000110958. [Q15185-3]
Ensembl; ENST00000436399; ENSP00000402385; ENSG00000110958. [Q15185-2]
Ensembl; ENST00000448157; ENSP00000414892; ENSG00000110958. [Q15185-4]
GeneID; 10728; -.
KEGG; hsa:10728; -.
UCSC; uc001slu.6; human. [Q15185-1]
CTD; 10728; -.
DisGeNET; 10728; -.
EuPathDB; HostDB:ENSG00000110958.15; -.
GeneCards; PTGES3; -.
HGNC; HGNC:16049; PTGES3.
HPA; CAB034319; -.
HPA; HPA038672; -.
HPA; HPA038673; -.
MIM; 607061; gene.
neXtProt; NX_Q15185; -.
OpenTargets; ENSG00000110958; -.
PharmGKB; PA142671118; -.
eggNOG; KOG3158; Eukaryota.
eggNOG; ENOG41121RT; LUCA.
GeneTree; ENSGT00510000046493; -.
HOGENOM; HOG000177563; -.
HOVERGEN; HBG002143; -.
InParanoid; Q15185; -.
KO; K15730; -.
PhylomeDB; Q15185; -.
TreeFam; TF315077; -.
BioCyc; MetaCyc:HS03359-MONOMER; -.
Reactome; R-HSA-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
Reactome; R-HSA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR).
Reactome; R-HSA-3371511; HSF1 activation.
Reactome; R-HSA-3371568; Attenuation phase.
Reactome; R-HSA-8937144; Aryl hydrocarbon receptor signalling.
SIGNOR; Q15185; -.
UniPathway; UPA00662; -.
ChiTaRS; PTGES3; human.
EvolutionaryTrace; Q15185; -.
GeneWiki; PTGES3; -.
GenomeRNAi; 10728; -.
PRO; PR:Q15185; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000110958; -.
CleanEx; HS_PTGES3; -.
ExpressionAtlas; Q15185; baseline and differential.
Genevisible; Q15185; HS.
GO; GO:0000781; C:chromosome, telomeric region; IC:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IMP:CAFA.
GO; GO:0005697; C:telomerase holoenzyme complex; IDA:UniProtKB.
GO; GO:0070182; F:DNA polymerase binding; IPI:BHF-UCL.
GO; GO:0051879; F:Hsp90 protein binding; IPI:CAFA.
GO; GO:0050220; F:prostaglandin-E synthase activity; IDA:UniProtKB.
GO; GO:0003720; F:telomerase activity; IDA:UniProtKB.
GO; GO:0051082; F:unfolded protein binding; IDA:UniProtKB.
GO; GO:0070389; P:chaperone cofactor-dependent protein refolding; IDA:UniProtKB.
GO; GO:0051131; P:chaperone-mediated protein complex assembly; IMP:CAFA.
GO; GO:0019371; P:cyclooxygenase pathway; TAS:Reactome.
GO; GO:0042327; P:positive regulation of phosphorylation; IDA:BHF-UCL.
GO; GO:0051973; P:positive regulation of telomerase activity; IDA:BHF-UCL.
GO; GO:0001516; P:prostaglandin biosynthetic process; IDA:UniProtKB.
GO; GO:0050821; P:protein stabilization; IMP:CAFA.
GO; GO:1900034; P:regulation of cellular response to heat; TAS:Reactome.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:1905323; P:telomerase holoenzyme complex assembly; IDA:BHF-UCL.
GO; GO:0000723; P:telomere maintenance; TAS:UniProtKB.
GO; GO:0007004; P:telomere maintenance via telomerase; IDA:BHF-UCL.
GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome.
Gene3D; 2.60.40.790; -; 1.
InterPro; IPR007052; CS_dom.
InterPro; IPR008978; HSP20-like_chaperone.
Pfam; PF04969; CS; 1.
SUPFAM; SSF49764; SSF49764; 1.
PROSITE; PS51203; CS; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Chaperone;
Complete proteome; Cytoplasm; Direct protein sequencing;
Fatty acid biosynthesis; Fatty acid metabolism; Isomerase;
Isopeptide bond; Lipid biosynthesis; Lipid metabolism; Phosphoprotein;
Prostaglandin biosynthesis; Prostaglandin metabolism;
Reference proteome; Ubl conjugation.
CHAIN 1 160 Prostaglandin E synthase 3.
/FTId=PRO_0000218952.
DOMAIN 1 90 CS. {ECO:0000255|PROSITE-
ProRule:PRU00547}.
MOTIF 157 160 PXLE motif.
{ECO:0000303|PubMed:24711448}.
COMPBIAS 108 160 Asp/Glu-rich.
MOD_RES 33 33 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 44 44 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 85 85 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 100 100 Phosphoserine.
{ECO:0000250|UniProtKB:Q9R0Q7}.
MOD_RES 113 113 Phosphoserine.
{ECO:0000244|PubMed:16807684,
ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:17487921,
ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:18318008,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19367720,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|Ref.6}.
MOD_RES 118 118 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231}.
MOD_RES 148 148 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:24275569}.
MOD_RES 151 151 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:24275569}.
CROSSLNK 35 35 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 65 65 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 63 95 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055363.
VAR_SEQ 96 125 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055364.
VAR_SEQ 126 146 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055365.
STRAND 6 10 {ECO:0000244|PDB:1EJF}.
STRAND 12 19 {ECO:0000244|PDB:1EJF}.
STRAND 24 32 {ECO:0000244|PDB:1EJF}.
STRAND 35 42 {ECO:0000244|PDB:1EJF}.
TURN 43 46 {ECO:0000244|PDB:1EJF}.
STRAND 47 57 {ECO:0000244|PDB:1EJF}.
STRAND 59 68 {ECO:0000244|PDB:1EJF}.
STRAND 73 81 {ECO:0000244|PDB:1EJF}.
STRAND 87 92 {ECO:0000244|PDB:1EJF}.
STRAND 99 101 {ECO:0000244|PDB:1EJF}.
TURN 103 105 {ECO:0000244|PDB:1EJF}.
SEQUENCE 160 AA; 18697 MW; 23538BB9D7AFD73F CRC64;
MQPASAKWYD RRDYVFIEFC VEDSKDVNVN FEKSKLTFSC LGGSDNFKHL NEIDLFHCID
PNDSKHKRTD RSILCCLRKG ESGQSWPRLT KERAKLNWLS VDFNNWKDWE DDSDEDMSNF
DRFSEMMNNM GGDEDVDLPE VDGADDDSQD SDDEKMPDLE


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