Curated Information
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Curated Information Page
PubMed Id: 23202365 
Heo KS, et al. (2013) Phosphorylation of protein inhibitor of activated STAT1 (PIAS1) by MAPK-activated protein kinase-2 inhibits endothelial inflammation via increasing both PIAS1 transrepression and SUMO E3 ligase activity. Arterioscler Thromb Vasc Biol 33, 321-9 23202365
This page summarizes selected information from the record 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.
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S522-p - PIAS1 (human)
Orthologous residues
PIAS1 (human): S522‑p, PIAS1 (mouse): S522‑p, PIAS1 (rat): S522‑p
Characterization
 Methods used to characterize site in vivo mutation of modification site, phospho-antibody, western blotting
 Relevant cell lines - cell types - tissues:  bEnd3, HUVEC (endothelial)
 Cellular systems studied:  cell lines
 Species studied:  human, mouse
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE MAPKAPK2 (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE MAPKAPK2 (human) pharmacological activator of upstream enzyme, siRNA inhibition of enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
TNF increase
siRNA TNF inhibit treatment-induced increase MK2 siRNA
Downstream Regulation
 Effect of modification (function):  enzymatic activity, induced, sumoylation
 Effect of modification (process):  transcription, inhibited
 Comments:  PIAS1 S522A expression inhibits TNF-induced sumoylation of p53; inhibits inflammatory genes expression;


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