Progesterone Receptor Antibody (YA5657)

Nucleus; Cytoplasm; Nucleus; Cytoplasm; Mitochondrion outer membrane

Tissue_specificity:In reproductive tissues, the expression of type A and type B isoforms varies with development and hormone levels. During the proliferative phase of the menstrual cycle, the expression levels of type A and type B isoforms are comparable in the uterine glandular epithelium. During the mid-secretory phase, type B isoform is persistently expressed in the glands, while type A is no longer expressed. In the stroma, type A is the predominant form throughout the cycle. The heterogeneity of isoform expression between the basal and functional layers of the endometrium suggests differences in the response to hormonal stimulation in different regions.

P06401 has 5 isomers: P06401-1: 98981 Da (predicted); P06401-2: 82295 Da (predicted); P06401-3: 38798 Da (predicted); P06401-4: 36318 Da (predicted); P06401-5: 87747 Da (predicted).
Phosphorylated on multiple serine sites. Several of these sites are hormone-dependent. Phosphorylation on Ser-294 occurs preferentially on isoform B, is highly hormone-dependent and modulates ubiquitination and sumoylation on Lys-388. Phosphorylation on Ser-102 and Ser-345 also requires induction by hormone. Basal phosphorylation on Ser-81, Ser-162, Ser-190 and Ser-400 is increased in response to progesterone and can be phosphorylated in vitro by the CDK2-A1 complex. Increased levels of phosphorylation on Ser-400 also in the presence of EGF, heregulin, IGF, PMA and FBS. Phosphorylation at this site by CDK2 is ligand-independent, and increases nuclear translocation and transcriptional activity. Phosphorylation at Ser-162 and Ser-294, but not at Ser-190, is impaired during the G(2)/M phase of the cell cycle. Phosphorylation on Ser-345 by ERK1/2 MAPK is required for interaction with SP1;Sumoylation is hormone-dependent and represses transcriptional activity. Sumoylation on all three sites is enhanced by PIAS3. Desumoylated by SENP1. Sumoylation on Lys-388, the main site of sumoylation, is repressed by ubiquitination on the same site, and modulated by phosphorylation at Ser-294;Ubiquitination is hormone-dependent and represses sumoylation on the same site (PubMed:10628747, PubMed:10655479, PubMed:15798179, PubMed:17173941, PubMed:17717077, PubMed:18202149, PubMed:8702648). Promoted by MAPK-mediated phosphorylation on Ser-294 (PubMed:10628747, PubMed:10655479, PubMed:15798179, PubMed:17173941, PubMed:17717077, PubMed:18202149, PubMed:8702648). Ubiquitinated by UBR5, leading to its degradation: UBR5 specifically recognizes and binds ligand-bound PGR when it is not associated with coactivators (NCOAs) (PubMed:37478846). In presence of NCOAs, the UBR5-degron is not accessible, preventing its ubiquitination and degradation (PubMed:37478846);Palmitoylated by ZDHHC7 and ZDHHC21. Palmitoylation is required for plasma membrane targeting and for rapid intracellular signaling via ERK and AKT kinases and cAMP generation

Interacts with SMARD1 and UNC45A. Interacts with CUEDC2; the interaction promotes ubiquitination, decreases sumoylation, and represses transcriptional activity. Interacts with PIAS3; the interaction promotes sumoylation of PR in a hormone-dependent manner, inhibits DNA-binding, and alters nuclear export. Interacts with SP1; the interaction requires ligand-induced phosphorylation on Ser-345 by ERK1/2 MAPK. Interacts with PRMT2. Isoform A interacts with NCOR2. Isoform B (but not isoform A) interacts with NCOA2 and NCOA1. Isoform B (but not isoform A) interacts with KLF9. Interacts with GTF2B (PubMed:1517211)

P06401

Progesterone receptor; PR; Nuclear receptor subfamily 3 group C member 3;