PTGES3

PTGES3
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1EJF
Identifiers
Aliases	PTGES3, P23, TEBP, cPGES, prostaglandin E synthase 3
External IDs	OMIM: 607061; MGI: 1929282; HomoloGene: 128197; GeneCards: PTGES3; OMA:PTGES3 - orthologs
Gene location (Human) Chr. Chromosome 12 (human) Band 12q13.3|12 Start 56,663,341 bp End 56,688,408 bp
Gene location (Mouse) Chr. Chromosome 10 (mouse) Band 10|10 D3 Start 127,894,823 bp End 127,913,141 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in secondary oocyte bronchial epithelial cell gonad mucosa of sigmoid colon caput epididymis ventricular zone embryo ganglionic eminence corpus epididymis trabecular bone Top expressed in abdominal wall medullary collecting duct renal corpuscle Gonadal ridge endocardial cushion cumulus cell primitive streak vas deferens migratory enteric neural crest cell epiblast More reference expression data BioGPS n/a
Gene ontology Molecular function unfolded protein binding telomerase activity isomerase activity protein binding prostaglandin-E synthase activity Hsp90 protein binding DNA polymerase binding chaperone binding Cellular component nucleoplasm telomere telomerase holoenzyme complex extracellular exosome nucleus cytoplasm cytosol protein-containing complex chaperone complex Biological process prostaglandin metabolic process lipid metabolism cyclooxygenase pathway fatty acid metabolic process fatty acid biosynthetic process regulation of cellular response to heat prostaglandin biosynthetic process telomere maintenance signal transduction xenobiotic metabolic process telomere maintenance via telomerase positive regulation of phosphorylation positive regulation of telomerase activity telomerase holoenzyme complex assembly protein stabilization chaperone-mediated protein complex assembly protein folding chaperone cofactor-dependent protein refolding Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 10728 56351 Ensembl ENSG00000110958 ENSMUSG00000071072 UniProt Q15185 Q9R0Q7 RefSeq (mRNA) NM_001282601 NM_001282602 NM_001282603 NM_001282604 NM_001282605 NM_006601 NM_019766 RefSeq (protein) NP_001269530 NP_001269531 NP_001269532 NP_001269533 NP_001269534 NP_006592 NP_062740 Location (UCSC) Chr 12: 56.66 – 56.69 Mb Chr 10: 127.89 – 127.91 Mb PubMed search
Wikidata
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Prostaglandin E synthase 3 (cytosolic) is an enzyme that in humans is encoded by the PTGES3 gene.

The protein encoded by this gene is also known as p23 which functions as a chaperone which is required for proper functioning of the glucocorticoid and other steroid receptors.

Further reading

• Johnson JL, Beito TG, Krco CJ, et al. (1994). "Characterization of a novel 23-kilodalton protein of inactive progesterone receptor complexes". Mol. Cell. Biol. 14 (3): 1956–63. doi:10.1128/MCB.14.3.1956. PMC 358554. PMID 8114727.
• Wu T, Wu H, Wang J, et al. (2011). "Expression and cellular localization of cyclooxygenases and prostaglandin E synthases in the hemorrhagic brain". J Neuroinflammation. 8: 22. doi:10.1186/1742-2094-8-22. PMC 3062590. PMID 21385433.
• Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
• Dittmar KD, Pratt WB (1997). "Folding of the glucocorticoid receptor by the reconstituted Hsp90-based chaperone machinery. The initial hsp90.p60.hsp70-dependent step is sufficient for creating the steroid binding conformation". J. Biol. Chem. 272 (20): 13047–13054. doi:10.1074/jbc.272.20.13047. PMID 9148915.
• Dittmar KD, Demady DR, Stancato LF, et al. (1997). "Folding of the glucocorticoid receptor by the heat shock protein (hsp) 90-based chaperone machinery. The role of p23 is to stabilize receptor.hsp90 heterocomplexes formed by hsp90.p60.hsp70". J. Biol. Chem. 272 (34): 21213–21220. doi:10.1074/jbc.272.34.21213. PMID 9261129.
• Zou J, Guo Y, Guettouche T, et al. (1998). "Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1". Cell. 94 (4): 471–480. doi:10.1016/S0092-8674(00)81588-3. PMID 9727490. S2CID 9234420.
• Yoo JY, Hamburger AW (1999). "Interaction of the p23/p198 protein with ErbB-3". Gene. 229 (1–2): 215–221. doi:10.1016/S0378-1119(98)00604-0. PMID 10095121.
• Knoblauch R, Garabedian MJ (1999). "Role for Hsp90-associated cochaperone p23 in estrogen receptor signal transduction". Mol. Cell. Biol. 19 (5): 3748–59. doi:10.1128/MCB.19.5.3748. PMC 84199. PMID 10207098.
• Muñoz MJ, Bejarano ER, Daga RR, et al. (2000). "The identification of Wos2, a p23 homologue that interacts with Wee1 and Cdc2 in the mitotic control of fission yeasts". Genetics. 153 (4): 1561–72. doi:10.1093/genetics/153.4.1561. PMC 1460861. PMID 10581266.
• Freeman BC, Felts SJ, Toft DO, et al. (2000). "The p23 molecular chaperones act at a late step in intracellular receptor action to differentially affect ligand efficacies". Genes Dev. 14 (4): 422–34. doi:10.1101/gad.14.4.422. PMC 316379. PMID 10691735.
• Weaver AJ, Sullivan WP, Felts SJ, et al. (2000). "Crystal structure and activity of human p23, a heat shock protein 90 co-chaperone". J. Biol. Chem. 275 (30): 23045–23052. doi:10.1074/jbc.M003410200. PMID 10811660.
• Tanioka T, Nakatani Y, Semmyo N, et al. (2000). "Molecular identification of cytosolic prostaglandin E2 synthase that is functionally coupled with cyclooxygenase-1 in immediate prostaglandin E2 biosynthesis". J. Biol. Chem. 275 (42): 32775–32782. doi:10.1074/jbc.M003504200. PMID 10922363.
• Kazlauskas A, Poellinger L, Pongratz I (2001). "The immunophilin-like protein XAP2 regulates ubiquitination and subcellular localization of the dioxin receptor". J. Biol. Chem. 275 (52): 41317–41324. doi:10.1074/jbc.M007765200. PMID 11013261.
• Futatsumori M, Kasai K, Takatsu H, et al. (2001). "Identification and characterization of novel isoforms of COP I subunits". J. Biochem. 128 (5): 793–801. doi:10.1093/oxfordjournals.jbchem.a022817. PMID 11056392.
• Kazlauskas A, Sundström S, Poellinger L, et al. (2001). "The hsp90 chaperone complex regulates intracellular localization of the dioxin receptor". Mol. Cell. Biol. 21 (7): 2594–2607. doi:10.1128/MCB.21.7.2594-2607.2001. PMC 86890. PMID 11259606.
• Forsythe HL, Jarvis JL, Turner JW, et al. (2001). "Stable association of hsp90 and p23, but Not hsp70, with active human telomerase". J. Biol. Chem. 276 (19): 15571–15574. doi:10.1074/jbc.C100055200. PMID 11274138.
• Donzé O, Abbas-Terki T, Picard D (2001). "The Hsp90 chaperone complex is both a facilitator and a repressor of the dsRNA-dependent kinase PKR". EMBO J. 20 (14): 3771–3780. doi:10.1093/emboj/20.14.3771. PMC 125551. PMID 11447118.
• Elder RT, Yu M, Chen M, et al. (2001). "HIV-1 Vpr induces cell cycle G2 arrest in fission yeast (Schizosaccharomyces pombe) through a pathway involving regulatory and catalytic subunits of PP2A and acting on both Wee1 and Cdc25". Virology. 287 (2): 359–370. doi:10.1006/viro.2001.1007. PMID 11531413.
• Hernández MP, Chadli A, Toft DO (2002). "HSP40 binding is the first step in the HSP90 chaperoning pathway for the progesterone receptor". J. Biol. Chem. 277 (14): 11873–11881. doi:10.1074/jbc.M111445200. PMID 11809754.
• McLaughlin SH, Smith HW, Jackson SE (2002). "Stimulation of the weak ATPase activity of human hsp90 by a client protein". J. Mol. Biol. 315 (4): 787–798. doi:10.1006/jmbi.2001.5245. PMID 11812147.
• Cox MB, Miller CA (2002). "The p23 co-chaperone facilitates dioxin receptor signaling in a yeast model system". Toxicol. Lett. 129 (1–2): 13–21. doi:10.1016/S0378-4274(01)00465-9. PMID 11879970.