Curated Information
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Curated Information Page
PubMed Id: 10722755 
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.
Aguirre V, et al. (2000) The c-Jun NH(2)-terminal kinase promotes insulin resistance during association with insulin receptor substrate-1 and phosphorylation of Ser(307). J Biol Chem 275, 9047-54 10722755
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S307-p - IRS1 (mouse)
Orthologous residues
IRS1 (human): S312‑p, IRS1 (mouse): S307‑p, IRS1 (rat): S307‑p
Characterization
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, mutation of modification site, peptide sequencing
 Relevant cell lines - cell types - tissues:  293 (epithelial), 32D (myeloid) [IRS1 (mouse)], CHO (fibroblast) [EphB1 (human), transfection]
 Cellular systems studied:  cell lines
 Species studied:  hamster, human, mouse
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE JNK1 (rat)
Downstream Regulation
 Effect of modification (function):  phosphorylation
 Comments:  inhibits insulin-stimulated tyrosine phosphorylation of IRS-1


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