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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) (Sid 3177) (Telomerase-binding protein p23)

 TEBP_MOUSE              Reviewed;         160 AA.
Q9R0Q7; Q542V4; Q9D7V0; Q9WV83;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
27-SEP-2017, entry version 161.
RecName: Full=Prostaglandin E synthase 3;
EC=5.3.99.3 {ECO:0000250|UniProtKB:Q15185};
AltName: Full=Cytosolic prostaglandin E2 synthase;
Short=cPGES;
AltName: Full=Hsp90 co-chaperone;
AltName: Full=Progesterone receptor complex p23;
AltName: Full=Sid 3177;
AltName: Full=Telomerase-binding protein p23;
Name=Ptges3; Synonyms=Sid3177, Tebp;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
STRAIN=C57BL/6J; TISSUE=Kidney;
PubMed=14563409; DOI=10.1016/j.bbalip.2003.08.003;
Zhang Y., Schneider A., Rao R., Lu W.J., Fan X., Davis L.,
Breyer R.M., Breyer M.D., Guan Y.;
"Genomic structure and genitourinary expression of mouse cytosolic
prostaglandin E(2) synthase gene.";
Biochim. Biophys. Acta 1634:15-23(2003).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Seki N., Hattori A., Hayashi A., Kozuma S., Muramatsu M., Saito T.;
"Mouse p23 uniactive progesterone receptor complexes.";
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
Cheong C., Lee H.-W.;
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and DBA/2J; TISSUE=Liver, and Stomach;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Mammary gland, and Olfactory epithelium;
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 36-48.
TISSUE=Brain;
Lubec G., Yang J.W., Zigmond M.;
Submitted (JUL-2007) to UniProtKB.
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic brain;
PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
"Phosphoproteomic analysis of the developing mouse brain.";
Mol. Cell. Proteomics 3:1093-1101(2004).
[8]
PHOSPHORYLATION AT SER-113.
PubMed=15378723; DOI=10.1002/rcm.1604;
Jin W.-H., Dai J., Zhou H., Xia Q.-C., Zou H.-F., Zeng R.;
"Phosphoproteome analysis of mouse liver using immobilized metal
affinity purification and linear ion trap mass spectrometry.";
Rapid Commun. Mass Spectrom. 18:2169-2176(2004).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18630941; DOI=10.1021/pr800223m;
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
"Specific phosphopeptide enrichment with immobilized titanium ion
affinity chromatography adsorbent for phosphoproteome analysis.";
J. Proteome Res. 7:3957-3967(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44; SER-100; SER-113;
SER-118; SER-148 AND SER-151, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-33, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
-!- FUNCTION: Cytosolic prostaglandin synthase that catalyzes the
oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to
prostaglandin E2 (PGE2). 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.
Facilitates HIF alpha proteins hydroxylation via interaction with
EGLN1/PHD2, leading to recruit EGLN1/PHD2 to the HSP90 pathway.
{ECO:0000250|UniProtKB:Q15185}.
-!- 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:0000250|UniProtKB:Q15185}.
-!- PATHWAY: Lipid metabolism; prostaglandin biosynthesis.
{ECO:0000250|UniProtKB:Q15185}.
-!- SUBUNIT: Binds to the progesterone receptor. Interacts with TERT;
the interaction, together with HSP90AA1, is required for correct
assembly and stabilization of the telomerase holoenzyme complex.
Interacts (via PXLE motif) with EGLN1/PHD2, recruiting EGLN1/PHD2
to the HSP90 pathway to facilitate HIF alpha proteins
hydroxylation. Interacts with HSP90AA1, FLCN, FNIP1 and FNIP2.
{ECO:0000250|UniProtKB:Q15185}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q3ZBF7}.
-!- TISSUE SPECIFICITY: Expressed in testis, kidney, bladder and
ovary. {ECO:0000269|PubMed:14563409}.
-!- SIMILARITY: Belongs to the p23/wos2 family. {ECO:0000305}.
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EMBL; AY281130; AAP34198.1; -; mRNA.
EMBL; AB024935; BAA84684.1; -; mRNA.
EMBL; AF153479; AAD39543.1; -; mRNA.
EMBL; AK008805; BAB25906.1; -; mRNA.
EMBL; AK075932; BAC36062.1; -; mRNA.
EMBL; AK075987; BAC36099.1; -; mRNA.
EMBL; AK077538; BAC36854.1; -; mRNA.
EMBL; AK168073; BAE40047.1; -; mRNA.
EMBL; AK168210; BAE40169.1; -; mRNA.
EMBL; AK168721; BAE40563.1; -; mRNA.
EMBL; BC003708; AAH03708.1; -; mRNA.
EMBL; BC085264; AAH85264.1; -; mRNA.
CCDS; CCDS36087.1; -.
RefSeq; NP_062740.1; NM_019766.4.
UniGene; Mm.305816; -.
ProteinModelPortal; Q9R0Q7; -.
SMR; Q9R0Q7; -.
BioGrid; 207917; 12.
IntAct; Q9R0Q7; 3.
MINT; MINT-3289867; -.
STRING; 10090.ENSMUSP00000050292; -.
iPTMnet; Q9R0Q7; -.
PhosphoSitePlus; Q9R0Q7; -.
EPD; Q9R0Q7; -.
MaxQB; Q9R0Q7; -.
PaxDb; Q9R0Q7; -.
PRIDE; Q9R0Q7; -.
Ensembl; ENSMUST00000052798; ENSMUSP00000050292; ENSMUSG00000071072.
GeneID; 56351; -.
KEGG; mmu:56351; -.
UCSC; uc007hld.1; mouse.
CTD; 10728; -.
MGI; MGI:1929282; Ptges3.
eggNOG; KOG3158; Eukaryota.
eggNOG; ENOG41121RT; LUCA.
GeneTree; ENSGT00510000046493; -.
HOGENOM; HOG000177563; -.
HOVERGEN; HBG002143; -.
InParanoid; Q9R0Q7; -.
KO; K15730; -.
OMA; KAAGPYW; -.
OrthoDB; EOG091G0XLQ; -.
PhylomeDB; Q9R0Q7; -.
TreeFam; TF315077; -.
Reactome; R-MMU-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
Reactome; R-MMU-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR).
Reactome; R-MMU-3371511; HSF1 activation.
Reactome; R-MMU-3371568; Attenuation phase.
Reactome; R-MMU-8937144; Aryl hydrocarbon receptor signalling.
UniPathway; UPA00662; -.
ChiTaRS; Ptges3; mouse.
PRO; PR:Q9R0Q7; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000071072; -.
CleanEx; MM_PTGES3; -.
ExpressionAtlas; Q9R0Q7; baseline and differential.
Genevisible; Q9R0Q7; MM.
GO; GO:0005884; C:actin filament; IEA:Ensembl.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0043005; C:neuron projection; IEA:Ensembl.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0043234; C:protein complex; ISO:MGI.
GO; GO:0005697; C:telomerase holoenzyme complex; ISO:MGI.
GO; GO:0070182; F:DNA polymerase binding; IPI:BHF-UCL.
GO; GO:0051879; F:Hsp90 protein binding; ISO:MGI.
GO; GO:0002039; F:p53 binding; IEA:Ensembl.
GO; GO:0050220; F:prostaglandin-E synthase activity; ISS:UniProtKB.
GO; GO:0003720; F:telomerase activity; ISO:MGI.
GO; GO:0051082; F:unfolded protein binding; ISS:UniProtKB.
GO; GO:0008283; P:cell proliferation; IMP:MGI.
GO; GO:0070389; P:chaperone cofactor-dependent protein refolding; ISO:MGI.
GO; GO:0051131; P:chaperone-mediated protein complex assembly; ISO:MGI.
GO; GO:0042921; P:glucocorticoid receptor signaling pathway; IMP:MGI.
GO; GO:0005978; P:glycogen biosynthetic process; IMP:MGI.
GO; GO:0060430; P:lung saccule development; IMP:MGI.
GO; GO:0060548; P:negative regulation of cell death; IEA:Ensembl.
GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
GO; GO:0042327; P:positive regulation of phosphorylation; ISO:MGI.
GO; GO:0051973; P:positive regulation of telomerase activity; IDA:BHF-UCL.
GO; GO:0001516; P:prostaglandin biosynthetic process; IMP:MGI.
GO; GO:0050821; P:protein stabilization; ISO:MGI.
GO; GO:0019233; P:sensory perception of pain; IEA:Ensembl.
GO; GO:0043588; P:skin development; IMP:MGI.
GO; GO:1905323; P:telomerase holoenzyme complex assembly; IDA:BHF-UCL.
GO; GO:0007004; P:telomere maintenance via telomerase; IDA:BHF-UCL.
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;
Acetylation; 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_0000218953.
DOMAIN 1 90 CS. {ECO:0000255|PROSITE-
ProRule:PRU00547}.
MOTIF 157 160 PXLE motif.
{ECO:0000250|UniProtKB:Q15185}.
COMPBIAS 108 160 Asp/Glu-rich.
MOD_RES 33 33 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 44 44 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 85 85 Phosphoserine.
{ECO:0000250|UniProtKB:Q15185}.
MOD_RES 100 100 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 113 113 Phosphoserine.
{ECO:0000244|PubMed:15345747,
ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:18630941,
ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:15378723}.
MOD_RES 118 118 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 148 148 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 151 151 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CROSSLNK 35 35 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q15185}.
CROSSLNK 65 65 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q15185}.
CONFLICT 87 88 PR -> LG (in Ref. 3; AAD39543).
{ECO:0000305}.
CONFLICT 108 108 D -> N (in Ref. 1; AAP34198 and 4;
BAB25906). {ECO:0000305}.
SEQUENCE 160 AA; 18721 MW; 7702CB59D7AFD739 CRC64;
MQPASAKWYD RRDYVFIEFC VEDSKDVNVN FEKSKLTFSC LGGSDNFKHL NEIDLFHCID
PNDSKHKRTD RSILCCLRKG ESGQSWPRLT KERAKLNWLS VDFNNWKDWE DDSDEDMSNF
DRFSEMMDHM GGDEDVDLPE VDGADDDSQD SDDEKMPDLE


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U0122h CLIA COX1,COX-1,Cyclooxygenase-1,Homo sapiens,Human,PGH synthase 1,PGHS-1,PHS 1,Prostaglandin G_H synthase 1,Prostaglandin H2 synthase 1,Prostaglandin-endoperoxide synthase 1,PTGS1 96T


 

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