Curated Information
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Curated Information Page
PubMed Id: 21123173 
Shirakawa T, et al. (2011) Deactivation of STAT6 through serine 707 phosphorylation by JNK. J Biol Chem 286, 4003-10 21123173
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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S707-p - STAT6 (human)
Orthologous residues
STAT6 (human): S707‑p, STAT6 (mouse): , STAT6 (rat): P702‑p
Characterization
 Methods used to characterize site in vivo electrophoretic mobility shift, mutation of modification site, western blotting
 Relevant cell lines - cell types - tissues:  293 (epithelial), HeLa (cervical)
 Cellular systems studied:  cell lines
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE JNK1 (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE JNK1 (human) siRNA inhibition of enzyme, pharmacological inhibitor of upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
anisomycin increase
SP600125 anisomycin inhibit treatment-induced increase
siRNA anisomycin inhibit treatment-induced increase siRNA JNK
IL-1b increase
IFN-gamma no change compared to control
Downstream Regulation
 Effect of modification (function):  molecular association, regulation
 Effect of modification (process):  transcription, inhibited
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
DNA Not reported
 Comments:  suppresses transcriptional activity of STAT6


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