Curated Information
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Curated Information Page
PubMed Id: 9030579 
This page summarizes selected information from the article referenced above and curated into PhosphoSitePlus®, a comprehensive online resource for the study of protein post-translational modifications (NAR, 2012,40:D261-70). To learn more about the scope of PhosphoSitePlus®, click here.
Adams M, et al. (1997) Transcriptional activation by peroxisome proliferator-activated receptor gamma is inhibited by phosphorylation at a consensus mitogen-activated protein kinase site. J Biol Chem 272, 5128-32 9030579
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S112-p - PPAR-gamma (human)
Orthologous residues
PPAR‑gamma (human): S112‑p, PPAR‑gamma iso3 (human): S84‑p, PPAR‑gamma (mouse): S112‑p, PPAR‑gamma iso2 (mouse): S82‑p, PPAR‑gamma (rat): S112‑p
Characterization
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, mutation of modification site
 Disease tissue studied:  gestational cancer, gestational trophoblastic choriocarcinoma
 Relevant cell lines - cell types - tissues:  JEG-3 (uterine)
 Cellular systems studied:  cell lines
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE JNK1 (human)
KINASE ERK2 (human)
Upstream Regulation
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
PPP1CA (human) decrease constitutively active
Downstream Regulation
 Effect of modification (process):  cell differentiation, altered, transcription, inhibited


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