Curated Information
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Curated Information Page
PubMed Id: 9335553 
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.
Information from this record has been curated, but not yet edited in PhosphoSitePlus® and may be incomplete.
De Fea K, Roth RA (1997) Protein kinase C modulation of insulin receptor substrate-1 tyrosine phosphorylation requires serine 612. Biochemistry 36, 12939-47 9335553
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S616-p - IRS1 (human)
Orthologous residues
IRS1 (human): S616‑p, IRS1 (mouse): S612‑p, IRS1 (rat): S612‑p
Characterization
 Methods used to characterize site in vivo mutation of modification site, phosphopeptide mapping, western blotting
 Relevant cell lines - cell types - tissues:  293 (epithelial)
 Cellular systems studied:  cell lines
 Species studied:  human
Upstream Regulation
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
phorbol ester increase
PKCA (human) increase
Downstream Regulation
 Effect of modification (function):  activity, inhibited
 Comments:  Phosphorylated S616 results in an inhibition of insulin signaling.


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