PTGES3

Prostaglandin E synthase 3 (cytosolic), also known as PTGES3, is a human gene (and associated protein). [cite web | title = Entrez Gene: PTGES3 Prostaglandin E synthase 3 (cytosolic)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10728| accessdate = ]

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.cite journal | author = Freeman BC, Yamamoto KR | title = Disassembly of transcriptional regulatory complexes by molecular chaperones | journal = Science (journal) | volume = 296 | issue = 5576 | pages = 2232–5 | year = 2002 | month = June | pmid = 12077419 | doi = 10.1126/science.1073051 | url = | issn = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Johnson JL, Beito TG, Krco CJ, Toft DO |title=Characterization of a novel 23-kilodalton protein of unactive progesterone receptor complexes. |journal=Mol. Cell. Biol. |volume=14 |issue= 3 |pages= 1956–63 |year= 1994 |pmid= 8114727 |doi=
*cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791–806 |year= 1997 |pmid= 8889548 |doi=
*cite journal | author=Dittmar KD, Pratt WB |title=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. |journal=J. Biol. Chem. |volume=272 |issue= 20 |pages= 13047–54 |year= 1997 |pmid= 9148915 |doi=
*cite journal | author=Dittmar KD, Demady DR, Stancato LF, "et al." |title=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. |journal=J. Biol. Chem. |volume=272 |issue= 34 |pages= 21213–20 |year= 1997 |pmid= 9261129 |doi=
*cite journal | author=Zou J, Guo Y, Guettouche T, "et al." |title=Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1. |journal=Cell |volume=94 |issue= 4 |pages= 471–80 |year= 1998 |pmid= 9727490 |doi=
*cite journal | author=Yoo JY, Hamburger AW |title=Interaction of the p23/p198 protein with ErbB-3. |journal=Gene |volume=229 |issue= 1-2 |pages= 215–21 |year= 1999 |pmid= 10095121 |doi=
*cite journal | author=Knoblauch R, Garabedian MJ |title=Role for Hsp90-associated cochaperone p23 in estrogen receptor signal transduction. |journal=Mol. Cell. Biol. |volume=19 |issue= 5 |pages= 3748–59 |year= 1999 |pmid= 10207098 |doi=
*cite journal | author=Muñoz MJ, Bejarano ER, Daga RR, Jimenez J |title=The identification of Wos2, a p23 homologue that interacts with Wee1 and Cdc2 in the mitotic control of fission yeasts. |journal=Genetics |volume=153 |issue= 4 |pages= 1561–72 |year= 2000 |pmid= 10581266 |doi=
*cite journal | author=Freeman BC, Felts SJ, Toft DO, Yamamoto KR |title=The p23 molecular chaperones act at a late step in intracellular receptor action to differentially affect ligand efficacies. |journal=Genes Dev. |volume=14 |issue= 4 |pages= 422–34 |year= 2000 |pmid= 10691735 |doi=
*cite journal | author=Weaver AJ, Sullivan WP, Felts SJ, "et al." |title=Crystal structure and activity of human p23, a heat shock protein 90 co-chaperone. |journal=J. Biol. Chem. |volume=275 |issue= 30 |pages= 23045–52 |year= 2000 |pmid= 10811660 |doi= 10.1074/jbc.M003410200
*cite journal | author=Tanioka T, Nakatani Y, Semmyo N, "et al." |title=Molecular identification of cytosolic prostaglandin E2 synthase that is functionally coupled with cyclooxygenase-1 in immediate prostaglandin E2 biosynthesis. |journal=J. Biol. Chem. |volume=275 |issue= 42 |pages= 32775–82 |year= 2000 |pmid= 10922363 |doi= 10.1074/jbc.M003504200
*cite journal | author=Kazlauskas A, Poellinger L, Pongratz I |title=The immunophilin-like protein XAP2 regulates ubiquitination and subcellular localization of the dioxin receptor. |journal=J. Biol. Chem. |volume=275 |issue= 52 |pages= 41317–24 |year= 2001 |pmid= 11013261 |doi= 10.1074/jbc.M007765200
*cite journal | author=Futatsumori M, Kasai K, Takatsu H, "et al." |title=Identification and characterization of novel isoforms of COP I subunits. |journal=J. Biochem. |volume=128 |issue= 5 |pages= 793–801 |year= 2001 |pmid= 11056392 |doi=
*cite journal | author=Kazlauskas A, Sundström S, Poellinger L, Pongratz I |title=The hsp90 chaperone complex regulates intracellular localization of the dioxin receptor. |journal=Mol. Cell. Biol. |volume=21 |issue= 7 |pages= 2594–607 |year= 2001 |pmid= 11259606 |doi= 10.1128/MCB.21.7.2594-2607.2001
*cite journal | author=Forsythe HL, Jarvis JL, Turner JW, "et al." |title=Stable association of hsp90 and p23, but Not hsp70, with active human telomerase. |journal=J. Biol. Chem. |volume=276 |issue= 19 |pages= 15571–4 |year= 2001 |pmid= 11274138 |doi= 10.1074/jbc.C100055200
*cite journal | author=Donzé O, Abbas-Terki T, Picard D |title=The Hsp90 chaperone complex is both a facilitator and a repressor of the dsRNA-dependent kinase PKR. |journal=EMBO J. |volume=20 |issue= 14 |pages= 3771–80 |year= 2001 |pmid= 11447118 |doi= 10.1093/emboj/20.14.3771
*cite journal | author=Elder RT, Yu M, Chen M, "et al." |title=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. |journal=Virology |volume=287 |issue= 2 |pages= 359–70 |year= 2001 |pmid= 11531413 |doi= 10.1006/viro.2001.1007
*cite journal | author=Hernández MP, Chadli A, Toft DO |title=HSP40 binding is the first step in the HSP90 chaperoning pathway for the progesterone receptor. |journal=J. Biol. Chem. |volume=277 |issue= 14 |pages= 11873–81 |year= 2002 |pmid= 11809754 |doi= 10.1074/jbc.M111445200
*cite journal | author=McLaughlin SH, Smith HW, Jackson SE |title=Stimulation of the weak ATPase activity of human hsp90 by a client protein. |journal=J. Mol. Biol. |volume=315 |issue= 4 |pages= 787–98 |year= 2002 |pmid= 11812147 |doi= 10.1006/jmbi.2001.5245
*cite journal | author=Cox MB, Miller CA |title=The p23 co-chaperone facilitates dioxin receptor signaling in a yeast model system. |journal=Toxicol. Lett. |volume=129 |issue= 1-2 |pages= 13–21 |year= 2002 |pmid= 11879970 |doi=

PBB_Controls
update_page = yes
require_manual_inspection = no
update_protein_box = yes
update_summary = no
update_citations = yes