PTGES3

Protein-coding gene in the species Homo sapiens

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)^[1]

Band	12q13.3\|12	Start	56,663,341 bp^[1]
Band	12q13.3\|12	End	56,688,408 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 10 (mouse)^[2]

Band	10\|10 D3	Start	127,894,823 bp^[2]
Band	10\|10 D3	End	127,913,141 bp^[2]

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

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Prostaglandin E synthase 3 (cytosolic) is an enzyme that in humans is encoded by the PTGES3 gene.^[5]

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.^[6]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000110958 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000071072 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Entrez Gene: PTGES3 Prostaglandin E synthase 3 (cytosolic)".
^ Freeman BC, Yamamoto KR (June 2002). "Disassembly of transcriptional regulatory complexes by molecular chaperones". Science. 296 (5576): 2232–2235. Bibcode:2002Sci...296.2232F. doi:10.1126/science.1073051. PMID 12077419. S2CID 8844179.

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.