TEBP_HUMAN
ID TEBP_HUMAN Reviewed; 160 AA.
AC Q15185; A8K7D0; B4DHP2; B4DP11; B4DP21; Q8WU70;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Prostaglandin E synthase 3;
DE EC=5.3.99.3 {ECO:0000269|PubMed:10922363};
DE AltName: Full=Cytosolic prostaglandin E2 synthase;
DE Short=cPGES;
DE AltName: Full=Hsp90 co-chaperone;
DE AltName: Full=Progesterone receptor complex p23;
DE AltName: Full=Telomerase-binding protein p23;
GN Name=PTGES3; Synonyms=P23, TEBP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROGESTERONE RECEPTOR-BINDING.
RC TISSUE=Testis;
RX PubMed=8114727; DOI=10.1128/mcb.14.3.1956-1963.1994;
RA Johnson J.L., Beito T.G., Krco C.J., Toft D.O.;
RT "Characterization of a novel 23-kilodalton protein of unactive progesterone
RT receptor complexes.";
RL Mol. Cell. Biol. 14:1956-1963(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC TISSUE=Caudate nucleus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung, and Urinary bladder;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 13-65; 72-88 AND 96-122, PHOSPHORYLATION AT SER-113,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [7]
RP INTERACTION WITH TERT, AND FUNCTION AS A CO-CHAPERONE IN TELOMERASE
RP HOLOENZYME ASSEMBLY.
RX PubMed=11274138; DOI=10.1074/jbc.c100055200;
RA Forsythe H.L., Jarvis J.L., Turner J.W., Elmore L.W., Holt S.E.;
RT "Stable association of hsp90 and p23, but Not hsp70, with active human
RT telomerase.";
RL J. Biol. Chem. 276:15571-15574(2001).
RN [8]
RP FUNCTION AS A CHAPERONE.
RX PubMed=12077419; DOI=10.1126/science.1073051;
RA Freeman B.C., Yamamoto K.R.;
RT "Disassembly of transcriptional regulatory complexes by molecular
RT chaperones.";
RL Science 296:2232-2235(2002).
RN [9]
RP FUNCTION AS A PROSTAGLANDIN SYNTHASE, BIOPHYSICOCHEMICAL PROPERTIES,
RP CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=10922363; DOI=10.1074/jbc.m003504200;
RA Tanioka T., Nakatani Y., Semmyo N., Murakami M., Kudo I.;
RT "Molecular identification of cytosolic prostaglandin E2 synthase that is
RT functionally coupled with cyclooxygenase-1 in immediate prostaglandin E2
RT biosynthesis.";
RL J. Biol. Chem. 275:32775-32782(2000).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-118; SER-148 AND
RP SER-151, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pituitary;
RX PubMed=16807684; DOI=10.1007/s11102-006-8916-x;
RA Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.;
RT "Phosphoproteomic analysis of the human pituitary.";
RL Pituitary 9:109-120(2006).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Prostate cancer;
RX PubMed=17487921; DOI=10.1002/elps.200600782;
RA Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
RT "Toward a global characterization of the phosphoproteome in prostate cancer
RT cells: identification of phosphoproteins in the LNCaP cell line.";
RL Electrophoresis 28:2027-2034(2007).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-148 AND SER-151, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-148 AND SER-151, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-33, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113 AND SER-118, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [24]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [26]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44; SER-85 AND SER-113, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [28]
RP FUNCTION, AND INTERACTION WITH EGLN1.
RX PubMed=24711448; DOI=10.1074/jbc.m113.541227;
RA Song D., Li L.S., Arsenault P.R., Tan Q., Bigham A.W., Heaton-Johnson K.J.,
RA Master S.R., Lee F.S.;
RT "Defective Tibetan PHD2 binding to p23 links high altitude adaption to
RT altered oxygen sensing.";
RL J. Biol. Chem. 289:14656-14665(2014).
RN [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85; SER-113; SER-148 AND
RP SER-151, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130 (ISOFORM 4), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [30]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [31]
RP INTERACTION WITH HSP90AA1; FLCN; FNIP1 AND FNIP2.
RX PubMed=27353360; DOI=10.1038/ncomms12037;
RA Woodford M.R., Dunn D.M., Blanden A.R., Capriotti D., Loiselle D.,
RA Prodromou C., Panaretou B., Hughes P.F., Smith A., Ackerman W.,
RA Haystead T.A., Loh S.N., Bourboulia D., Schmidt L.S., Marston Linehan W.,
RA Bratslavsky G., Mollapour M.;
RT "The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance
RT drug binding.";
RL Nat. Commun. 7:12037-12037(2016).
RN [32]
RP IDENTIFICATION IN A COMPLEX WITH HSP90; HSP70; STIP1; CDC37; PPP5C; TSC1
RP AND TSC2.
RX PubMed=29127155; DOI=10.15252/embj.201796700;
RA Woodford M.R., Sager R.A., Marris E., Dunn D.M., Blanden A.R., Murphy R.L.,
RA Rensing N., Shapiro O., Panaretou B., Prodromou C., Loh S.N., Gutmann D.H.,
RA Bourboulia D., Bratslavsky G., Wong M., Mollapour M.;
RT "Tumor suppressor Tsc1 is a new Hsp90 co-chaperone that facilitates folding
RT of kinase and non-kinase clients.";
RL EMBO J. 36:3650-3665(2017).
RN [33]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-35 AND LYS-65, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [34]
RP X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) OF 1-125.
RX PubMed=10811660; DOI=10.1074/jbc.m003410200;
RA Weaver A.J., Sullivan W.P., Felts S.J., Owen B.A.L., Toft D.O.;
RT "Crystal structure and activity of human p23, a heat shock protein 90 co-
RT chaperone.";
RL J. Biol. Chem. 275:23045-23052(2000).
CC -!- FUNCTION: Cytosolic prostaglandin synthase that catalyzes the
CC oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin
CC E2 (PGE2) (PubMed:10922363). Molecular chaperone that localizes to
CC genomic response elements in a hormone-dependent manner and disrupts
CC receptor-mediated transcriptional activation, by promoting disassembly
CC of transcriptional regulatory complexes (PubMed:11274138,
CC PubMed:12077419). Facilitates HIF alpha proteins hydroxylation via
CC interaction with EGLN1/PHD2, leading to recruit EGLN1/PHD2 to the HSP90
CC pathway (PubMed:24711448). {ECO:0000269|PubMed:10922363,
CC ECO:0000269|PubMed:11274138, ECO:0000269|PubMed:12077419,
CC ECO:0000269|PubMed:24711448}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=prostaglandin H2 = prostaglandin E2; Xref=Rhea:RHEA:12893,
CC ChEBI:CHEBI:57405, ChEBI:CHEBI:606564; EC=5.3.99.3;
CC Evidence={ECO:0000269|PubMed:10922363};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=14 uM for PGH2 {ECO:0000269|PubMed:10922363};
CC Vmax=190 nmol/min/mg enzyme toward PGH2
CC {ECO:0000269|PubMed:10922363};
CC -!- PATHWAY: Lipid metabolism; prostaglandin biosynthesis.
CC {ECO:0000269|PubMed:10922363}.
CC -!- SUBUNIT: Probably forms a complex composed of chaperones HSP90 and
CC HSP70, co-chaperones STIP1/HOP, CDC37, PPP5C, PTGES3/p23, TSC1 and
CC client protein TSC2 (PubMed:29127155). Binds to the progesterone
CC receptor (PubMed:8114727). Interacts with TERT; the interaction,
CC together with HSP90AA1, is required for correct assembly and
CC stabilization of the telomerase holoenzyme complex (PubMed:11274138).
CC Interacts (via PXLE motif) with EGLN1/PHD2, recruiting EGLN1/PHD2 to
CC the HSP90 pathway to facilitate HIF alpha proteins hydroxylation
CC (PubMed:24711448). Interacts with HSP90AA1, FLCN, FNIP1 and FNIP2
CC (PubMed:27353360). {ECO:0000269|PubMed:11274138,
CC ECO:0000269|PubMed:24711448, ECO:0000269|PubMed:27353360,
CC ECO:0000269|PubMed:8114727}.
CC -!- INTERACTION:
CC Q15185; Q9UKV8: AGO2; NbExp=3; IntAct=EBI-1049387, EBI-528269;
CC Q15185; P07900: HSP90AA1; NbExp=6; IntAct=EBI-1049387, EBI-296047;
CC Q15185; P08238: HSP90AB1; NbExp=4; IntAct=EBI-1049387, EBI-352572;
CC Q15185; O14654: IRS4; NbExp=2; IntAct=EBI-1049387, EBI-356594;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q3ZBF7}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q15185-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15185-2; Sequence=VSP_055363;
CC Name=3;
CC IsoId=Q15185-3; Sequence=VSP_055364;
CC Name=4;
CC IsoId=Q15185-4; Sequence=VSP_055365;
CC -!- DOMAIN: The PXLE motif mediates interaction with EGLN1/PHD2.
CC {ECO:0000269|PubMed:24711448}.
CC -!- SIMILARITY: Belongs to the p23/wos2 family. {ECO:0000305}.
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DR EMBL; L24804; AAA18537.1; -; mRNA.
DR EMBL; AK291945; BAF84634.1; -; mRNA.
DR EMBL; AK295208; BAG58204.1; -; mRNA.
DR EMBL; AK298147; BAG60423.1; -; mRNA.
DR EMBL; AK298160; BAG60433.1; -; mRNA.
DR EMBL; AC117378; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW96953.1; -; Genomic_DNA.
DR EMBL; CH471054; EAW96958.1; -; Genomic_DNA.
DR EMBL; BC003005; AAH03005.1; -; mRNA.
DR EMBL; BC021167; AAH21167.1; -; mRNA.
DR CCDS; CCDS31836.1; -. [Q15185-1]
DR CCDS; CCDS61158.1; -. [Q15185-2]
DR CCDS; CCDS61159.1; -. [Q15185-3]
DR CCDS; CCDS61160.1; -. [Q15185-4]
DR PIR; A56211; A56211.
DR RefSeq; NP_001269530.1; NM_001282601.1. [Q15185-4]
DR RefSeq; NP_001269531.1; NM_001282602.1. [Q15185-3]
DR RefSeq; NP_001269532.1; NM_001282603.1. [Q15185-2]
DR RefSeq; NP_001269533.1; NM_001282604.1.
DR RefSeq; NP_001269534.1; NM_001282605.1.
DR RefSeq; NP_006592.3; NM_006601.6. [Q15185-1]
DR PDB; 1EJF; X-ray; 2.49 A; A/B=1-125.
DR PDB; 7KRJ; EM; 2.56 A; C=1-160.
DR PDB; 7L7I; EM; 3.30 A; E=1-160.
DR PDB; 7L7J; EM; 3.10 A; C=1-160.
DR PDBsum; 1EJF; -.
DR PDBsum; 7KRJ; -.
DR PDBsum; 7L7I; -.
DR PDBsum; 7L7J; -.
DR AlphaFoldDB; Q15185; -.
DR BMRB; Q15185; -.
DR SASBDB; Q15185; -.
DR SMR; Q15185; -.
DR BioGRID; 115952; 342.
DR CORUM; Q15185; -.
DR DIP; DIP-279N; -.
DR ELM; Q15185; -.
DR IntAct; Q15185; 95.
DR MINT; Q15185; -.
DR STRING; 9606.ENSP00000482075; -.
DR ChEMBL; CHEMBL3341580; -.
DR DrugBank; DB00316; Acetaminophen.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB05036; Grn163l.
DR SwissLipids; SLP:000000831; -.
DR GlyGen; Q15185; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q15185; -.
DR PhosphoSitePlus; Q15185; -.
DR SwissPalm; Q15185; -.
DR BioMuta; PTGES3; -.
DR EPD; Q15185; -.
DR jPOST; Q15185; -.
DR MassIVE; Q15185; -.
DR MaxQB; Q15185; -.
DR PaxDb; Q15185; -.
DR PeptideAtlas; Q15185; -.
DR PRIDE; Q15185; -.
DR ProteomicsDB; 4234; -.
DR ProteomicsDB; 4741; -.
DR ProteomicsDB; 4744; -.
DR ProteomicsDB; 60486; -. [Q15185-1]
DR TopDownProteomics; Q15185-1; -. [Q15185-1]
DR Antibodypedia; 28360; 764 antibodies from 39 providers.
DR DNASU; 10728; -.
DR Ensembl; ENST00000262033.11; ENSP00000262033.6; ENSG00000110958.16. [Q15185-1]
DR Ensembl; ENST00000414274.7; ENSP00000405299.3; ENSG00000110958.16. [Q15185-3]
DR Ensembl; ENST00000436399.6; ENSP00000402385.2; ENSG00000110958.16. [Q15185-2]
DR Ensembl; ENST00000448157.6; ENSP00000414892.2; ENSG00000110958.16. [Q15185-4]
DR GeneID; 10728; -.
DR KEGG; hsa:10728; -.
DR MANE-Select; ENST00000262033.11; ENSP00000262033.6; NM_006601.7; NP_006592.3.
DR UCSC; uc001slu.6; human. [Q15185-1]
DR CTD; 10728; -.
DR DisGeNET; 10728; -.
DR GeneCards; PTGES3; -.
DR HGNC; HGNC:16049; PTGES3.
DR HPA; ENSG00000110958; Low tissue specificity.
DR MIM; 607061; gene.
DR neXtProt; NX_Q15185; -.
DR OpenTargets; ENSG00000110958; -.
DR PharmGKB; PA142671118; -.
DR VEuPathDB; HostDB:ENSG00000110958; -.
DR eggNOG; KOG3158; Eukaryota.
DR GeneTree; ENSGT00940000154256; -.
DR InParanoid; Q15185; -.
DR PhylomeDB; Q15185; -.
DR TreeFam; TF315077; -.
DR BioCyc; MetaCyc:HS03359-MON; -.
DR PathwayCommons; Q15185; -.
DR Reactome; R-HSA-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
DR Reactome; R-HSA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-HSA-3371511; HSF1 activation.
DR Reactome; R-HSA-3371568; Attenuation phase.
DR Reactome; R-HSA-8937144; Aryl hydrocarbon receptor signalling.
DR Reactome; R-HSA-8939211; ESR-mediated signaling.
DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR Reactome; R-HSA-9679191; Potential therapeutics for SARS.
DR SABIO-RK; Q15185; -.
DR SignaLink; Q15185; -.
DR SIGNOR; Q15185; -.
DR UniPathway; UPA00662; -.
DR BioGRID-ORCS; 10728; 35 hits in 1009 CRISPR screens.
DR ChiTaRS; PTGES3; human.
DR EvolutionaryTrace; Q15185; -.
DR GeneWiki; PTGES3; -.
DR GenomeRNAi; 10728; -.
DR Pharos; Q15185; Tbio.
DR PRO; PR:Q15185; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q15185; protein.
DR Bgee; ENSG00000110958; Expressed in secondary oocyte and 220 other tissues.
DR ExpressionAtlas; Q15185; baseline and differential.
DR Genevisible; Q15185; HS.
DR GO; GO:0101031; C:chaperone complex; IDA:UniProtKB.
DR GO; GO:0000781; C:chromosome, telomeric region; IC:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IMP:CAFA.
DR GO; GO:0005697; C:telomerase holoenzyme complex; IDA:UniProtKB.
DR GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR GO; GO:0070182; F:DNA polymerase binding; IPI:BHF-UCL.
DR GO; GO:0051879; F:Hsp90 protein binding; IPI:CAFA.
DR GO; GO:0050220; F:prostaglandin-E synthase activity; IDA:UniProtKB.
DR GO; GO:0003720; F:telomerase activity; IDA:UniProtKB.
DR GO; GO:0051082; F:unfolded protein binding; IDA:UniProtKB.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IDA:UniProtKB.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; IMP:CAFA.
DR GO; GO:0019371; P:cyclooxygenase pathway; TAS:Reactome.
DR GO; GO:0048144; P:fibroblast proliferation; IEA:Ensembl.
DR GO; GO:0042921; P:glucocorticoid receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:Ensembl.
DR GO; GO:0060430; P:lung saccule development; IEA:Ensembl.
DR GO; GO:0042327; P:positive regulation of phosphorylation; IDA:BHF-UCL.
DR GO; GO:0051973; P:positive regulation of telomerase activity; IDA:BHF-UCL.
DR GO; GO:0001516; P:prostaglandin biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0050821; P:protein stabilization; IMP:CAFA.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0043588; P:skin development; IEA:Ensembl.
DR GO; GO:1905323; P:telomerase holoenzyme complex assembly; IDA:BHF-UCL.
DR GO; GO:0000723; P:telomere maintenance; TAS:UniProtKB.
DR GO; GO:0007004; P:telomere maintenance via telomerase; IDA:BHF-UCL.
DR DisProt; DP00358; -.
DR Gene3D; 2.60.40.790; -; 1.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR InterPro; IPR045250; p23-like.
DR PANTHER; PTHR22932; PTHR22932; 1.
DR Pfam; PF04969; CS; 1.
DR SUPFAM; SSF49764; SSF49764; 1.
DR PROSITE; PS51203; CS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Chaperone; Cytoplasm;
KW Direct protein sequencing; Fatty acid biosynthesis; Fatty acid metabolism;
KW Isomerase; Isopeptide bond; Lipid biosynthesis; Lipid metabolism;
KW Phosphoprotein; Prostaglandin biosynthesis; Prostaglandin metabolism;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..160
FT /note="Prostaglandin E synthase 3"
FT /id="PRO_0000218952"
FT DOMAIN 1..90
FT /note="CS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00547"
FT REGION 124..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 157..160
FT /note="PXLE motif"
FT /evidence="ECO:0000303|PubMed:24711448"
FT COMPBIAS 135..160
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 33
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9R0Q7"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:16807684,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:17487921,
FT ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18318008,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19367720, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:24275569"
FT CROSSLNK 35
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 65
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 63..95
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055363"
FT VAR_SEQ 96..125
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055364"
FT VAR_SEQ 126..146
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055365"
FT STRAND 6..10
FT /evidence="ECO:0007829|PDB:1EJF"
FT STRAND 12..19
FT /evidence="ECO:0007829|PDB:1EJF"
FT STRAND 24..32
FT /evidence="ECO:0007829|PDB:1EJF"
FT STRAND 35..42
FT /evidence="ECO:0007829|PDB:1EJF"
FT TURN 43..46
FT /evidence="ECO:0007829|PDB:1EJF"
FT STRAND 47..57
FT /evidence="ECO:0007829|PDB:1EJF"
FT STRAND 59..68
FT /evidence="ECO:0007829|PDB:1EJF"
FT STRAND 73..81
FT /evidence="ECO:0007829|PDB:1EJF"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:1EJF"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:1EJF"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:1EJF"
FT HELIX 120..130
FT /evidence="ECO:0007829|PDB:7KRJ"
FT MOD_RES Q15185-4:130
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
SQ SEQUENCE 160 AA; 18697 MW; 23538BB9D7AFD73F CRC64;
MQPASAKWYD RRDYVFIEFC VEDSKDVNVN FEKSKLTFSC LGGSDNFKHL NEIDLFHCID
PNDSKHKRTD RSILCCLRKG ESGQSWPRLT KERAKLNWLS VDFNNWKDWE DDSDEDMSNF
DRFSEMMNNM GGDEDVDLPE VDGADDDSQD SDDEKMPDLE
