Lys388
Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage PhosphoSitePlus® v6.7.7
Powered by Cell Signaling Technology
Home > Sumoylation Site Page: > Lys388  -  PR (human)

Site Information
QPPALKIkEEEEGAE   SwissProt Entrez-Gene
Blast this site against: NCBI  SwissProt  PDB 
Site Group ID: 486289

In vivo Characterization
Methods used to characterize site in vivo:
electrophoretic mobility shift ( 5 , 9 ) , immunoassay ( 2 ) , immunoprecipitation ( 6 , 7 ) , modification-specific antibody ( 5 ) , mutation of modification site ( 2 , 3 , 4 , 5 , 6 , 7 , 9 , 10 , 11 ) , western blotting ( 3 , 4 , 5 , 6 , 7 , 9 , 10 )
Disease tissue studied:
breast cancer ( 2 , 4 , 5 , 6 , 7 , 9 )
Relevant cell line - cell type - tissue:
breast ( 2 ) , COS (fibroblast) ( 6 ) , COS7 (fibroblast) ( 9 ) , CV1 (fibroblast) ( 10 ) , HEK293T (epithelial) ( 7 , 9 ) , HeLa (cervical) ( 3 , 4 , 5 , 6 , 7 , 9 , 11 ) , T47D (breast cell) ( 2 , 4 , 5 , 6 , 7 , 9 )

Upstream Regulation
Regulatory protein:
CUEDC2 (human) ( 7 ) , PIAS4 (human) ( 9 )
Treatments:
cAMP_analog ( 8 ) , mifepristone ( 6 ) , MPA ( 8 ) , progesterone ( 9 ) , progestin_R5020 ( 4 , 6 ) , siRNA ( 9 )

Downstream Regulation
Effects of modification on PR:
activity, inhibited ( 11 ) , intracellular localization ( 9 ) , protein conformation ( 9 ) , protein stabilization ( 9 ) , sumoylation ( 9 )
Effects of modification on biological processes:
cell differentiation, inhibited ( 8 ) , cell growth, altered ( 4 ) , transcription, induced ( 10 ) , transcription, inhibited ( 3 , 4 , 5 , 6 , 8 , 9 , 11 )

References 

1

Chen CC, et al. (2017) The transcriptional repressor GATAD2B mediates progesterone receptor suppression of myometrial contractile gene expression. J Biol Chem
28576827   Curated Info

2

Knutson TP, et al. (2017) Posttranslationally modified progesterone receptors direct ligand-specific expression of breast cancer stem cell-associated gene programs. J Hematol Oncol 10, 89
28412963   Curated Info

3

Abdel-Hafiz HA, Horwitz KB (2012) Control of progesterone receptor transcriptional synergy by SUMOylation and deSUMOylation. BMC Mol Biol 13, 10
22439847   Curated Info

4

Daniel AR, Lange CA (2009) Protein kinases mediate ligand-independent derepression of sumoylated progesterone receptors in breast cancer cells. Proc Natl Acad Sci U S A 106, 14287-92
19706513   Curated Info

5

Abdel-Hafiz H, Dudevoir ML, Horwitz KB (2009) Mechanisms Underlying the Control of Progesterone Receptor Transcriptional Activity by SUMOylation. J Biol Chem 284, 9099-108
19211567   Curated Info

6

Daniel AR, Faivre EJ, Lange CA (2007) Phosphorylation-dependent antagonism of sumoylation derepresses progesterone receptor action in breast cancer cells. Mol Endocrinol 21, 2890-906
17717077   Curated Info

7

Zhang PJ, et al. (2007) CUE domain containing 2 regulates degradation of progesterone receptor by ubiquitin-proteasome. EMBO J 26, 1831-42
17347654   Curated Info

8

Jones MC, et al. (2006) Regulation of the SUMO pathway sensitizes differentiating human endometrial stromal cells to progesterone. Proc Natl Acad Sci U S A 103, 16272-7
17053081   Curated Info

9

Man JH, et al. (2006) PIAS3 induction of PRB sumoylation represses PRB transactivation by destabilizing its retention in the nucleus. Nucleic Acids Res 34, 5552-66
17020914   Curated Info

10

Chauchereau A, et al. (2003) Sumoylation of the progesterone receptor and of the steroid receptor coactivator SRC-1. J Biol Chem 278, 12335-43
12529333   Curated Info

11

Abdel-Hafiz H, Takimoto GS, Tung L, Horwitz KB (2002) The inhibitory function in human progesterone receptor N termini binds SUMO-1 protein to regulate autoinhibition and transrepression. J Biol Chem 277, 33950-6
12114521   Curated Info

Developed with grants from  NIH Logo and literature mining with Linguamatics  I2E Logo Creative Commons License PhosphoSite, created by Cell Signaling Technology is licensed under a Creative Commons Attribution-NonCommercial-ShareAlike 3.0 Unported License.

©2003-2024 Cell Signaling Technology, Inc.