Progesterone receptor (PR) is a member of the nuclear/steroid hormone receptor (SHR) family of ligand-dependent transcription factors that is expressed primarily in female reproductive tissues and in the central nervous system.  In response to binding its cognate steroid hormone, progesterone, PR regulates expression of gene networks to control development, differentiation, and proliferation of target tissues as well as pathological processes in endocrine-based cacer. In common with other SHRs, PR is a modular protein composed of a well-folded Cterminal ligand-binding domain (LBD), a central globular DNA binding (DBD) domain, and an amino-terminal domain (NTD) that is comprised largely of intrinsically disordered protein (IDP). There are two PR protein isoforms that arise from the same gene by utilization of two promoters; PR-A with a truncated NTD and full length PR-B. PR undergoes extensive post-translational modifications that includes phosphorylation, acetylation, ubiquitination, SUMOylation, and methylation. Specific kinases that phosphorylate PR have been identified including CDK1/2, MAPK, PKA, DNA-PK and casein kinase II (CK2).

References

1.Grimm SL,et al. J Mol Biol. 2016;428(19):3831–3849.