p23/PTGES3 Products

Description

Steroid receptors are ligand-dependent intracellular proteins that stimulate transcription of specific genes by binding to specific DNA sequences following activation by the appropriate hormone. Prior to activation, steroid receptors associate with a number of different proteins in both a stable and transient fashion. Steroid receptor complex proteins include heat shock proteins (HSP 70 and HSP 90), immunosuppressant binding proteins called immunophilins (the FK 506 binding proteins, FKBP 52 & FKBP 54 and the cyclosporin binding protein, CyP-40) and at least three other proteins termed p23, p60 and p48. p23 along with HSP 70, HSP 90 and p60, combine with progesterone receptor (PR) as members of a transient intermediate complex. Cloned human p23 encodes a protein of 160 amino acids that is highly conserved between species and shows no homology to previously identified proteins. p23 is a highly acidic phosphoprotein with an aspartic acid-rich C-terminal domain and multiple potential phosphorylation sites. In vitro studies have suggested that p23 binds to HSP90 and is necessary for the binding of HSP 90 and CyP-40 to PR. While neither its exact function nor mechanism of action have been identified, p23 appears to be an important factor in PR function.

Bioinformatics

Entrez	10728 Human 56351 Mouse
Uniprot	AAH03005 Human NM_006601 Human NP_006592 Human Q15185 Human
Product By Gene ID	10728
Alternate Names	cPGESp23 Cytosolic prostaglandin E2 synthase Hsp90 co-chaperone P23cytosolic prostaglandin E synthase Progesterone receptor complex p23 prostaglandin E synthase 3 (cytosolic) prostaglandin E synthase 3 TEBPEC 5.3.99.3 Telomerase-binding protein p23 unactive progesterone receptor, 23 kD

Research Areas for p23/PTGES3

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Membrane Trafficking and Chaperones