Curated Information
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Curated Information Page
PubMed Id: 17434145 
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.
Fei E, et al. (2007) Phosphorylation of ataxin-3 by glycogen synthase kinase 3beta at serine 256 regulates the aggregation of ataxin-3. Biochem Biophys Res Commun 357, 487-92 17434145
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S256-p - ataxin-3 (human)
Orthologous residues
ataxin‑3 (human): S256‑p, ataxin‑3 iso2 (human): S256‑p, ataxin‑3 (mouse): S256‑p, ataxin‑3 (rat): S256‑p
Characterization
 Methods used to characterize site in vivo mutation of modification site
 Relevant cell lines - cell types - tissues:  293 (epithelial)
 Cellular systems studied:  cell lines
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE GSK3B (human)
Downstream Regulation
 Effect of modification (function):  molecular association, regulation
 Comments:  phosphorylation of this site prevents protein aggregation; excessive aggregation of mutant S256A is inhibited by Hsp70;


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