Progesterone Receptor (PGR)

NR3C3; PR; Nuclear Receptor Subfamily 3,Group C,Member 3

SPN	V557
HGNC	8910
MGI	97567
PubMed	15272277
RGD	3317
UniProt	P06401
Wiki	PGR

The PR) also known as NR3C3 (nuclear receptor subfamily 3, group C, member 3), is an intracellular steroid receptor that specifically binds progesterone.

PR is encoded by a single gene PGR residing on chromosome 11q22, it has two main forms, A and B, that differ in their molecular weight.Like all steroid receptors, the progesterone receptor has an amino and a carboxyl terminal, and between them the regulatory domain, a DNA binding domain, the hinge section, and the hormone binding domain. A special transcription activation function (TAF), called TAF-3, is present in the progesterone receptor-B, in a B-upstream segment (BUS) at the amino acid terminal. This segment is not present in the receptor-A.

Reference

"Two distinct estrogen-regulated promoters generate transcripts encoding the two functionally different human progesterone receptor forms A and B."
EMBO J. 9:1603-1614(1990) [PubMed] [Europe PMC] [Abstract]

"Complete amino acid sequence of the human progesterone receptor deduced from cloned cDNA."
Biochem. Biophys. Res. Commun. 143:740-748(1987) [PubMed] [Europe PMC] [Abstract]

"The human progesterone receptor shows evidence of adaptive evolution associated with its ability to act as a transcription factor."
Mol. Phylogenet. Evol. 47:637-649(2008) [PubMed] [Europe PMC] [Abstract]

"Cloning and expression of a novel, truncated, progesterone receptor."
Mol. Cell. Endocrinol. 200:155-163(2003) [PubMed] [Europe PMC] [Abstract]

"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]

"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]

"Identification of a phosphorylation site in the hinge region of the human progesterone receptor and additional amino-terminal phosphorylation sites."
J. Biol. Chem. 276:8475-8483(2001) [PubMed] [Europe PMC] [Abstract]

"A truncated progesterone receptor (PR-M) localizes to the mitochondrion and controls cellular respiration."
Mol. Endocrinol. 27:741-753(2013) [PubMed] [Europe PMC] [Abstract]

"Identification of a group of Ser-Pro motif hormone-inducible phosphorylation sites in the human progesterone receptor."
Mol. Endocrinol. 9:1029-1040(1995) [PubMed] [Europe PMC] [Abstract]

"Stoichiometry and site-specific phosphorylation of human progesterone receptor in native target cells and in the baculovirus expression system."
J. Biol. Chem. 271:19546-19555(1996) [PubMed] [Europe PMC] [Abstract]

"Phosphorylation of human progesterone receptor by cyclin-dependent kinase 2 on three sites that are authentic basal phosphorylation sites in vivo."
Mol. Endocrinol. 11:823-832(1997) [PubMed] [Europe PMC] [Abstract]

"Differential hormone-dependent phosphorylation of progesterone receptor A and B forms revealed by a phosphoserine site-specific monoclonal antibody."
Mol. Endocrinol. 14:52-65(2000) [PubMed] [Europe PMC] [Abstract]

"Phosphorylation of human progesterone receptors at serine-294 by mitogen-activated protein kinase signals their degradation by the 26S proteasome."
Proc. Natl. Acad. Sci. U.S.A. 97:1032-1037(2000) [PubMed] [Europe PMC] [Abstract]

"Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor alpha."
J. Biol. Chem. 277:28624-28630(2002) [PubMed] [Europe PMC] [Abstract]

"BAF60a mediates critical interactions between nuclear receptors and the BRG1 chromatin-remodeling complex for transactivation."
Mol. Cell. Biol. 23:6210-6220(2003) [PubMed] [Europe PMC] [Abstract]

"Phosphorylation of progesterone receptor serine 400 mediates ligand-independent transcriptional activity in response to activation of cyclin-dependent protein kinase 2."
Mol. Cell. Biol. 24:10542-10557(2004) [PubMed] [Europe PMC] [Abstract]

"Human progesterone receptor displays cell cycle-dependent changes in transcriptional activity."
Mol. Cell. Biol. 25:2885-2898(2005) [PubMed] [Europe PMC] [Abstract]

"GCUNC-45 is a novel regulator for the progesterone receptor/hsp90 chaperoning pathway."
Mol. Cell. Biol. 26:1722-1730(2006) [PubMed] [Europe PMC] [Abstract]

"PIAS3 induction of PRB sumoylation represses PRB transactivation by destabilizing its retention in the nucleus."
Nucleic Acids Res. 34:5552-5566(2006) [PubMed] [Europe PMC] [Abstract]

"CUE domain containing 2 regulates degradation of progesterone receptor by ubiquitin-proteasome."
EMBO J. 26:1831-1842(2007) [PubMed] [Europe PMC] [Abstract]

"Phosphorylation-dependent antagonism of sumoylation derepresses progesterone receptor action in breast cancer cells."
Mol. Endocrinol. 21:2890-2906(2007) [PubMed] [Europe PMC] [Abstract]

"Linkage of progestin and epidermal growth factor signaling: phosphorylation of progesterone receptors mediates transcriptional hypersensitivity and increased ligand-independent breast cancer cell growth."
Steroids 72:188-201(2007) [PubMed] [Europe PMC] [Abstract]

"Progesterone receptor rapid signaling mediates serine 345 phosphorylation and tethering to specificity protein 1 transcription factors."
Mol. Endocrinol. 22:823-837(2008) [PubMed] [Europe PMC] [Abstract]

"DHHC-7 and -21 are palmitoylacyltransferases for sex steroid receptors."
Mol. Biol. Cell 23:188-199(2012) [PubMed] [Europe PMC] [Abstract]

"Atomic structure of progesterone complexed with its receptor."
Nature 393:392-396(1998) [PubMed] [Europe PMC] [Abstract]

"Molecular and pharmacological properties of a potent and selective novel nonsteroidal progesterone receptor agonist tanaproget."
J. Biol. Chem. 280:28468-28475(2005) [PubMed] [Europe PMC] [Abstract]