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Phosphorylation Site Page:
Ser345 - PR (human)

Site Information
AFAPPRSsPCASSTP   SwissProt Entrez-Gene
Predicted information:  Scansite
Orthologous residues: PR (chicken): (S259), PR (mouse): (S345), PR iso2 (human): (S181), PR (rat): (S344)
Blast this site against: NCBI  SwissProt  PDB 
Site Group ID: 450157

In vivo Characterization
Methods used to characterize site in vivo: [32P] bio-synthetic labeling (6, 8), electrophoretic mobility shift (8), immunoprecipitation (1), mass spectrometry (5), mutation of modification site (3, 4), peptide sequencing (8), phospho-antibody (1, 2, 4), phosphopeptide mapping (6, 8), western blotting (1, 2)
Disease tissue studied: breast cancer (1, 2, 4, 6, 8)
Relevant cell line - cell type - tissue: COS (fibroblast) (1, 3), HeLa (cervical) (1, 2), SF9 (5, 6), T47D (breast cell) (1, 2, 4, 6, 8)

Controlled by
Treatments: AG1478 (4), asoprisnil (2), EGF (4), lonaprisan (2), onapristone (2), PP2 (4), progestin_R5020 (1, 2, 4, 5, 8), RU-486 (2), SB203580 (4), U0126 (4)

Downstream Regulation
Effects of modification on PR: molecular association, regulation (4)
Effects of modification on biological processes: transcription, induced (4, 7)
Induce interaction with: SP1 (human) (4)



Hagan CR, Knutson TP, Lange CA (2013) A Common Docking Domain in Progesterone Receptor-B links DUSP6 and CK2 signaling to proliferative transcriptional programs in breast cancer cells. Nucleic Acids Res 41, 8926-42
23921636   Curated Info


Busia L, Faus H, Hoffmann J, Haendler B (2011) The antiprogestin Lonaprisan inhibits breast cancer cell proliferation by inducing p21 expression. Mol Cell Endocrinol 333, 37-46
21138753   Curated Info


Wardell SE, Narayanan R, Weigel NL, Edwards DP (2010) Partial Agonist Activity of the Progesterone Receptor Antagonist RU486 Mediated by an Amino-Terminal Domain Coactivator and Phosphorylation of Serine400. Mol Endocrinol 24, 335-45
20008003   Curated Info


Faivre EJ, Daniel AR, Hillard CJ, Lange CA (2008) Progesterone receptor rapid signaling mediates serine 345 phosphorylation and tethering to specificity protein 1 transcription factors. Mol Endocrinol 22, 823-37
18202149   Curated Info


Knotts TA, et al. (2001) Identification of a phosphorylation site in the hinge region of the human progesterone receptor and additional amino-terminal phosphorylation sites. J Biol Chem 276, 8475-83
11110801   Curated Info


Beck CA, et al. (1996) Stoichiometry and site-specific phosphorylation of human progesterone receptor in native target cells and in the baculovirus expression system. J Biol Chem 271, 19546-55
8702648   Curated Info


Takimoto GS, et al. (1996) Role of phosphorylation on DNA binding and transcriptional functions of human progesterone receptors. J Biol Chem 271, 13308-16
8662865   Curated Info


Zhang Y, et al. (1995) Identification of a group of Ser-Pro motif hormone-inducible phosphorylation sites in the human progesterone receptor. Mol Endocrinol 9, 1029-40
7476977   Curated Info

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