Full text data of PTGES3
PTGES3
(P23, TEBP)
[Confidence: low (only semi-automatic identification from reviews)]
Prostaglandin E synthase 3; 5.3.99.3 (Cytosolic prostaglandin E2 synthase; cPGES; Hsp90 co-chaperone; Progesterone receptor complex p23; Telomerase-binding protein p23)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Prostaglandin E synthase 3; 5.3.99.3 (Cytosolic prostaglandin E2 synthase; cPGES; Hsp90 co-chaperone; Progesterone receptor complex p23; Telomerase-binding protein p23)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q15185
ID TEBP_HUMAN Reviewed; 160 AA.
AC Q15185; A8K7D0; Q8WU70;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 135.
DE RecName: Full=Prostaglandin E synthase 3;
DE EC=5.3.99.3;
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RX PubMed=8114727;
RA Johnson J.L., Beito T.G., Krco C.J., Toft D.O.;
RT "Characterization of a novel 23-kilodalton protein of unactive
RT progesterone receptor complexes.";
RL Mol. Cell. Biol. 14:1956-1963(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 13-65; 72-88 AND 96-122, PHOSPHORYLATION AT
RP SER-113, AND MASS SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [6]
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 [7]
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 [8]
RP FUNCTION AS A PROSTAGLANDIN SYNTHASE, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
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
RT is functionally coupled with cyclooxygenase-1 in immediate
RT prostaglandin E2 biosynthesis.";
RL J. Biol. Chem. 275:32775-32782(2000).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-118; SER-148
RP AND SER-151, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND MASS
RP SPECTROMETRY.
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND MASS
RP SPECTROMETRY.
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
RT cancer cells: identification of phosphoproteins in the LNCaP cell
RT line.";
RL Electrophoresis 28:2027-2034(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND MASS
RP SPECTROMETRY.
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
RT sequential IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND MASS
RP SPECTROMETRY.
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-148 AND
RP SER-151, AND MASS SPECTROMETRY.
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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-148 AND
RP SER-151, AND MASS SPECTROMETRY.
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND MASS
RP SPECTROMETRY.
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
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [17]
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND MASS
RP SPECTROMETRY.
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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND MASS
RP SPECTROMETRY.
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 [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-33, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113 AND SER-118, AND
RP MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [22]
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.,
RA Buerckstuemmer T., 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 [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [24]
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [25]
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
RT co-chaperone.";
RL J. Biol. Chem. 275:23045-23052(2000).
CC -!- FUNCTION: Molecular chaperone that localizes to genomic response
CC elements in a hormone-dependent manner and disrupts receptor-
CC mediated transcriptional activation, by promoting disassembly of
CC transcriptional regulatory complexes.
CC -!- CATALYTIC ACTIVITY: (5Z,13E)-(15S)-9-alpha,11-alpha-epidioxy-15-
CC hydroxyprosta-5,13-dienoate = (5Z,13E)-(15S)-11-alpha,15-
CC dihydroxy-9-oxoprosta-5,13-dienoate.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=14 uM for PGH2;
CC Vmax=190 nmol/min/mg enzyme toward PGH2;
CC -!- PATHWAY: Lipid metabolism; prostaglandin biosynthesis.
CC -!- SUBUNIT: Binds to the progesterone receptor. Interacts with TERT;
CC the interaction, together with HSP90AA1, is required for correct
CC assembly and stabilization of the telomerase holoenzyme complex.
CC -!- INTERACTION:
CC P07900:HSP90AA1; NbExp=5; IntAct=EBI-1049387, EBI-296047;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the p23/wos2 family.
CC -!- SIMILARITY: Contains 1 CS domain.
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DR EMBL; L24804; AAA18537.1; -; mRNA.
DR EMBL; AK291945; BAF84634.1; -; mRNA.
DR EMBL; CH471054; EAW96953.1; -; Genomic_DNA.
DR EMBL; BC003005; AAH03005.1; -; mRNA.
DR EMBL; BC021167; AAH21167.1; -; mRNA.
DR PIR; A56211; A56211.
DR RefSeq; NP_001269530.1; NM_001282601.1.
DR RefSeq; NP_001269531.1; NM_001282602.1.
DR RefSeq; NP_001269532.1; NM_001282603.1.
DR RefSeq; NP_001269533.1; NM_001282604.1.
DR RefSeq; NP_001269534.1; NM_001282605.1.
DR RefSeq; NP_006592.3; NM_006601.6.
DR UniGene; Hs.50425; -.
DR PDB; 1EJF; X-ray; 2.49 A; A/B=1-125.
DR PDB; 1LG0; Model; -; A=1-110.
DR PDBsum; 1EJF; -.
DR PDBsum; 1LG0; -.
DR DisProt; DP00358; -.
DR ProteinModelPortal; Q15185; -.
DR SMR; Q15185; 1-110.
DR DIP; DIP-279N; -.
DR IntAct; Q15185; 10.
DR MINT; MINT-5000397; -.
DR STRING; 9606.ENSP00000262033; -.
DR PhosphoSite; Q15185; -.
DR DMDM; 8928247; -.
DR PaxDb; Q15185; -.
DR PRIDE; Q15185; -.
DR DNASU; 10728; -.
DR Ensembl; ENST00000262033; ENSP00000262033; ENSG00000110958.
DR GeneID; 10728; -.
DR KEGG; hsa:10728; -.
DR UCSC; uc001slu.4; human.
DR CTD; 10728; -.
DR GeneCards; GC12M057057; -.
DR HGNC; HGNC:16049; PTGES3.
DR HPA; CAB034319; -.
DR HPA; HPA038672; -.
DR HPA; HPA038673; -.
DR MIM; 607061; gene.
DR neXtProt; NX_Q15185; -.
DR PharmGKB; PA142671118; -.
DR eggNOG; NOG283591; -.
DR HOVERGEN; HBG002143; -.
DR InParanoid; Q15185; -.
DR KO; K15730; -.
DR OMA; VTENSFT; -.
DR OrthoDB; EOG77HDGK; -.
DR BioCyc; MetaCyc:HS03359-MONOMER; -.
DR Reactome; REACT_111217; Metabolism.
DR UniPathway; UPA00662; -.
DR ChiTaRS; PTGES3; human.
DR EvolutionaryTrace; Q15185; -.
DR GeneWiki; PTGES3; -.
DR GenomeRNAi; 10728; -.
DR NextBio; 40728; -.
DR PRO; PR:Q15185; -.
DR ArrayExpress; Q15185; -.
DR Bgee; Q15185; -.
DR CleanEx; HS_PTGES3; -.
DR Genevestigator; Q15185; -.
DR GO; GO:0000781; C:chromosome, telomeric region; IC:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005697; C:telomerase holoenzyme complex; IDA:UniProtKB.
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:0070389; P:chaperone cofactor-dependent protein refolding; IDA:UniProtKB.
DR GO; GO:0019371; P:cyclooxygenase pathway; TAS:Reactome.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0000723; P:telomere maintenance; TAS:UniProtKB.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
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; Chaperone; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Fatty acid biosynthesis;
KW Fatty acid metabolism; Isomerase; Lipid biosynthesis;
KW Lipid metabolism; Phosphoprotein; Prostaglandin biosynthesis;
KW Prostaglandin metabolism; Reference proteome.
FT CHAIN 1 160 Prostaglandin E synthase 3.
FT /FTId=PRO_0000218952.
FT DOMAIN 1 90 CS.
FT COMPBIAS 108 160 Asp/Glu-rich.
FT MOD_RES 33 33 N6-acetyllysine.
FT MOD_RES 113 113 Phosphoserine.
FT MOD_RES 118 118 Phosphoserine.
FT MOD_RES 148 148 Phosphoserine.
FT MOD_RES 151 151 Phosphoserine.
FT STRAND 6 10
FT STRAND 12 19
FT STRAND 24 32
FT STRAND 35 42
FT TURN 43 46
FT STRAND 47 57
FT STRAND 59 68
FT STRAND 73 81
FT STRAND 87 92
FT STRAND 99 101
FT TURN 103 105
SQ SEQUENCE 160 AA; 18697 MW; 23538BB9D7AFD73F CRC64;
MQPASAKWYD RRDYVFIEFC VEDSKDVNVN FEKSKLTFSC LGGSDNFKHL NEIDLFHCID
PNDSKHKRTD RSILCCLRKG ESGQSWPRLT KERAKLNWLS VDFNNWKDWE DDSDEDMSNF
DRFSEMMNNM GGDEDVDLPE VDGADDDSQD SDDEKMPDLE
//
ID TEBP_HUMAN Reviewed; 160 AA.
AC Q15185; A8K7D0; Q8WU70;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 135.
DE RecName: Full=Prostaglandin E synthase 3;
DE EC=5.3.99.3;
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RX PubMed=8114727;
RA Johnson J.L., Beito T.G., Krco C.J., Toft D.O.;
RT "Characterization of a novel 23-kilodalton protein of unactive
RT progesterone receptor complexes.";
RL Mol. Cell. Biol. 14:1956-1963(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 13-65; 72-88 AND 96-122, PHOSPHORYLATION AT
RP SER-113, AND MASS SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [6]
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 [7]
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 [8]
RP FUNCTION AS A PROSTAGLANDIN SYNTHASE, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
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
RT is functionally coupled with cyclooxygenase-1 in immediate
RT prostaglandin E2 biosynthesis.";
RL J. Biol. Chem. 275:32775-32782(2000).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-118; SER-148
RP AND SER-151, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND MASS
RP SPECTROMETRY.
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND MASS
RP SPECTROMETRY.
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
RT cancer cells: identification of phosphoproteins in the LNCaP cell
RT line.";
RL Electrophoresis 28:2027-2034(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND MASS
RP SPECTROMETRY.
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
RT sequential IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND MASS
RP SPECTROMETRY.
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-148 AND
RP SER-151, AND MASS SPECTROMETRY.
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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-148 AND
RP SER-151, AND MASS SPECTROMETRY.
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND MASS
RP SPECTROMETRY.
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
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [17]
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND MASS
RP SPECTROMETRY.
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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND MASS
RP SPECTROMETRY.
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 [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-33, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113 AND SER-118, AND
RP MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [22]
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.,
RA Buerckstuemmer T., 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 [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [24]
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [25]
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
RT co-chaperone.";
RL J. Biol. Chem. 275:23045-23052(2000).
CC -!- FUNCTION: Molecular chaperone that localizes to genomic response
CC elements in a hormone-dependent manner and disrupts receptor-
CC mediated transcriptional activation, by promoting disassembly of
CC transcriptional regulatory complexes.
CC -!- CATALYTIC ACTIVITY: (5Z,13E)-(15S)-9-alpha,11-alpha-epidioxy-15-
CC hydroxyprosta-5,13-dienoate = (5Z,13E)-(15S)-11-alpha,15-
CC dihydroxy-9-oxoprosta-5,13-dienoate.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=14 uM for PGH2;
CC Vmax=190 nmol/min/mg enzyme toward PGH2;
CC -!- PATHWAY: Lipid metabolism; prostaglandin biosynthesis.
CC -!- SUBUNIT: Binds to the progesterone receptor. Interacts with TERT;
CC the interaction, together with HSP90AA1, is required for correct
CC assembly and stabilization of the telomerase holoenzyme complex.
CC -!- INTERACTION:
CC P07900:HSP90AA1; NbExp=5; IntAct=EBI-1049387, EBI-296047;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the p23/wos2 family.
CC -!- SIMILARITY: Contains 1 CS domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; L24804; AAA18537.1; -; mRNA.
DR EMBL; AK291945; BAF84634.1; -; mRNA.
DR EMBL; CH471054; EAW96953.1; -; Genomic_DNA.
DR EMBL; BC003005; AAH03005.1; -; mRNA.
DR EMBL; BC021167; AAH21167.1; -; mRNA.
DR PIR; A56211; A56211.
DR RefSeq; NP_001269530.1; NM_001282601.1.
DR RefSeq; NP_001269531.1; NM_001282602.1.
DR RefSeq; NP_001269532.1; NM_001282603.1.
DR RefSeq; NP_001269533.1; NM_001282604.1.
DR RefSeq; NP_001269534.1; NM_001282605.1.
DR RefSeq; NP_006592.3; NM_006601.6.
DR UniGene; Hs.50425; -.
DR PDB; 1EJF; X-ray; 2.49 A; A/B=1-125.
DR PDB; 1LG0; Model; -; A=1-110.
DR PDBsum; 1EJF; -.
DR PDBsum; 1LG0; -.
DR DisProt; DP00358; -.
DR ProteinModelPortal; Q15185; -.
DR SMR; Q15185; 1-110.
DR DIP; DIP-279N; -.
DR IntAct; Q15185; 10.
DR MINT; MINT-5000397; -.
DR STRING; 9606.ENSP00000262033; -.
DR PhosphoSite; Q15185; -.
DR DMDM; 8928247; -.
DR PaxDb; Q15185; -.
DR PRIDE; Q15185; -.
DR DNASU; 10728; -.
DR Ensembl; ENST00000262033; ENSP00000262033; ENSG00000110958.
DR GeneID; 10728; -.
DR KEGG; hsa:10728; -.
DR UCSC; uc001slu.4; human.
DR CTD; 10728; -.
DR GeneCards; GC12M057057; -.
DR HGNC; HGNC:16049; PTGES3.
DR HPA; CAB034319; -.
DR HPA; HPA038672; -.
DR HPA; HPA038673; -.
DR MIM; 607061; gene.
DR neXtProt; NX_Q15185; -.
DR PharmGKB; PA142671118; -.
DR eggNOG; NOG283591; -.
DR HOVERGEN; HBG002143; -.
DR InParanoid; Q15185; -.
DR KO; K15730; -.
DR OMA; VTENSFT; -.
DR OrthoDB; EOG77HDGK; -.
DR BioCyc; MetaCyc:HS03359-MONOMER; -.
DR Reactome; REACT_111217; Metabolism.
DR UniPathway; UPA00662; -.
DR ChiTaRS; PTGES3; human.
DR EvolutionaryTrace; Q15185; -.
DR GeneWiki; PTGES3; -.
DR GenomeRNAi; 10728; -.
DR NextBio; 40728; -.
DR PRO; PR:Q15185; -.
DR ArrayExpress; Q15185; -.
DR Bgee; Q15185; -.
DR CleanEx; HS_PTGES3; -.
DR Genevestigator; Q15185; -.
DR GO; GO:0000781; C:chromosome, telomeric region; IC:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005697; C:telomerase holoenzyme complex; IDA:UniProtKB.
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:0070389; P:chaperone cofactor-dependent protein refolding; IDA:UniProtKB.
DR GO; GO:0019371; P:cyclooxygenase pathway; TAS:Reactome.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0000723; P:telomere maintenance; TAS:UniProtKB.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
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; Chaperone; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Fatty acid biosynthesis;
KW Fatty acid metabolism; Isomerase; Lipid biosynthesis;
KW Lipid metabolism; Phosphoprotein; Prostaglandin biosynthesis;
KW Prostaglandin metabolism; Reference proteome.
FT CHAIN 1 160 Prostaglandin E synthase 3.
FT /FTId=PRO_0000218952.
FT DOMAIN 1 90 CS.
FT COMPBIAS 108 160 Asp/Glu-rich.
FT MOD_RES 33 33 N6-acetyllysine.
FT MOD_RES 113 113 Phosphoserine.
FT MOD_RES 118 118 Phosphoserine.
FT MOD_RES 148 148 Phosphoserine.
FT MOD_RES 151 151 Phosphoserine.
FT STRAND 6 10
FT STRAND 12 19
FT STRAND 24 32
FT STRAND 35 42
FT TURN 43 46
FT STRAND 47 57
FT STRAND 59 68
FT STRAND 73 81
FT STRAND 87 92
FT STRAND 99 101
FT TURN 103 105
SQ SEQUENCE 160 AA; 18697 MW; 23538BB9D7AFD73F CRC64;
MQPASAKWYD RRDYVFIEFC VEDSKDVNVN FEKSKLTFSC LGGSDNFKHL NEIDLFHCID
PNDSKHKRTD RSILCCLRKG ESGQSWPRLT KERAKLNWLS VDFNNWKDWE DDSDEDMSNF
DRFSEMMNNM GGDEDVDLPE VDGADDDSQD SDDEKMPDLE
//
MIM
607061
*RECORD*
*FIELD* NO
607061
*FIELD* TI
*607061 PROSTAGLANDIN E SYNTHASE 3; PTGES3
;;UNACTIVE PROGESTERONE RECEPTOR, 23-KD; P23;;
read morePROSTAGLANDIN E SYNTHASE, CYTOSOLIC; CPGES
*FIELD* TX
CLONING
P23 was first observed as a component of the unactivated avian
progesterone receptor complex, along with HSP70 (see 140550) and HSP90
(see 140571) (Smith et al., 1990). Using the chicken p23 sequence as
probe, Johnson et al. (1994) cloned P23 from a human testis cDNA
library. The deduced 160-amino acid protein has a calculated molecular
mass of about 19 kD and contains several putative phosphorylation sites.
P23 shares about 96% sequence identity with the chicken homolog. Western
blot analysis revealed a 23-kD band in tissue and cell lysates from
several mammalian species including human.
GENE FUNCTION
Freeman and Yamamoto (2002) determined that the P23 molecular chaperone
localizes to genomic response elements in a hormone-dependent manner and
showed that it could disrupt receptor-mediated transcriptional
activation.
Synthesis of prostaglandin E2 (PGE2) from arachidonic acid involves
multiple enzymes, and 2 isoforms of the terminal enzyme of this
biosynthetic pathway, PGE synthase (PGES), have been identified.
Cytosolic PTGES (cPGES) is identical to the heat-shock protein-90 (see
140571) chaperone p23 (Tanioka et al., 2000) and is functionally coupled
to constitutive prostaglandin-endoperoxide H synthase-1 (176805) (Han et
al., 2002). Microsomal PTGES (mPGES; 605172) is inducible by
proinflammatory cytokines such as IL1B (147720). Meadows et al. (2003)
studied expression and localization of both enzyme isoforms in human
fetal membranes either at term or preterm, with or without labor.
Western blot analysis of the amnion and choriodecidua showed no
differences in amounts of either cPGES or mPGES at term or preterm, with
or without labor, in either tissue with advancing gestation. Meadows et
al. (2003) concluded that expression of PGES is not the rate-limiting
step in PGE2 synthesis in fetal membranes at labor.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the P23
gene to chromosome 12 (TMAP SHGC-35709).
*FIELD* RF
1. Freeman, B. C.; Yamamoto, K. R.: Disassembly of transcriptional
regulatory complexes by molecular chaperones. Science 296: 2232-2235,
2002.
2. Han, R.; Tsui, S.; Smith, T. J.: Up-regulation of prostaglandin
E(2) synthesis by interleukin-1-beta in human orbital fibroblasts
involves coordinate induction of prostaglandin-endoperoxide H synthase-2
and glutathione-dependent prostaglandin E(2) synthase expression. J.
Biol. Chem. 277: 16355-16364, 2002.
3. Johnson, J. L.; Beito, T. G.; Krco, C. J.; Toft, D. O.: Characterization
of a novel 23-kilodalton protein of unactive progesterone receptor
complexes. Molec. Cell. Biol. 14: 1956-1963, 1994.
4. Meadows, J. W.; Eis, A. L. W.; Brockman, D. E.; Myatt, L.: Expression
and localization of prostaglandin E synthase isoforms in human fetal
membranes in term and preterm labor. J. Clin. Endocr. Metab. 88:
433-439, 2003.
5. Smith, D. F.; Faber, L. E.; Toft, D. O.: Purification of unactivated
progesterone receptor and identification of novel receptor-associated
proteins. J. Biol. Chem. 265: 3996-4003, 1990.
6. 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.
*FIELD* CN
John A. Phillips, III - updated: 8/6/2004
*FIELD* CD
Patricia A. Hartz: 6/24/2002
*FIELD* ED
alopez: 07/13/2005
alopez: 8/6/2004
carol: 6/26/2002
*RECORD*
*FIELD* NO
607061
*FIELD* TI
*607061 PROSTAGLANDIN E SYNTHASE 3; PTGES3
;;UNACTIVE PROGESTERONE RECEPTOR, 23-KD; P23;;
read morePROSTAGLANDIN E SYNTHASE, CYTOSOLIC; CPGES
*FIELD* TX
CLONING
P23 was first observed as a component of the unactivated avian
progesterone receptor complex, along with HSP70 (see 140550) and HSP90
(see 140571) (Smith et al., 1990). Using the chicken p23 sequence as
probe, Johnson et al. (1994) cloned P23 from a human testis cDNA
library. The deduced 160-amino acid protein has a calculated molecular
mass of about 19 kD and contains several putative phosphorylation sites.
P23 shares about 96% sequence identity with the chicken homolog. Western
blot analysis revealed a 23-kD band in tissue and cell lysates from
several mammalian species including human.
GENE FUNCTION
Freeman and Yamamoto (2002) determined that the P23 molecular chaperone
localizes to genomic response elements in a hormone-dependent manner and
showed that it could disrupt receptor-mediated transcriptional
activation.
Synthesis of prostaglandin E2 (PGE2) from arachidonic acid involves
multiple enzymes, and 2 isoforms of the terminal enzyme of this
biosynthetic pathway, PGE synthase (PGES), have been identified.
Cytosolic PTGES (cPGES) is identical to the heat-shock protein-90 (see
140571) chaperone p23 (Tanioka et al., 2000) and is functionally coupled
to constitutive prostaglandin-endoperoxide H synthase-1 (176805) (Han et
al., 2002). Microsomal PTGES (mPGES; 605172) is inducible by
proinflammatory cytokines such as IL1B (147720). Meadows et al. (2003)
studied expression and localization of both enzyme isoforms in human
fetal membranes either at term or preterm, with or without labor.
Western blot analysis of the amnion and choriodecidua showed no
differences in amounts of either cPGES or mPGES at term or preterm, with
or without labor, in either tissue with advancing gestation. Meadows et
al. (2003) concluded that expression of PGES is not the rate-limiting
step in PGE2 synthesis in fetal membranes at labor.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the P23
gene to chromosome 12 (TMAP SHGC-35709).
*FIELD* RF
1. Freeman, B. C.; Yamamoto, K. R.: Disassembly of transcriptional
regulatory complexes by molecular chaperones. Science 296: 2232-2235,
2002.
2. Han, R.; Tsui, S.; Smith, T. J.: Up-regulation of prostaglandin
E(2) synthesis by interleukin-1-beta in human orbital fibroblasts
involves coordinate induction of prostaglandin-endoperoxide H synthase-2
and glutathione-dependent prostaglandin E(2) synthase expression. J.
Biol. Chem. 277: 16355-16364, 2002.
3. Johnson, J. L.; Beito, T. G.; Krco, C. J.; Toft, D. O.: Characterization
of a novel 23-kilodalton protein of unactive progesterone receptor
complexes. Molec. Cell. Biol. 14: 1956-1963, 1994.
4. Meadows, J. W.; Eis, A. L. W.; Brockman, D. E.; Myatt, L.: Expression
and localization of prostaglandin E synthase isoforms in human fetal
membranes in term and preterm labor. J. Clin. Endocr. Metab. 88:
433-439, 2003.
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*FIELD* CN
John A. Phillips, III - updated: 8/6/2004
*FIELD* CD
Patricia A. Hartz: 6/24/2002
*FIELD* ED
alopez: 07/13/2005
alopez: 8/6/2004
carol: 6/26/2002