Curated Information
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Home > Curated Information Page > PubMed Id: 14623899
Giraud J, Leshan R, Lee YH, White MF (2004) Nutrient-dependent and insulin-stimulated phosphorylation of insulin receptor substrate-1 on serine 302 correlates with increased insulin signaling. J Biol Chem 279, 3447-54 14623899
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, 2015, 43:D512-20). To learn more about the scope of PhosphoSitePlus®, click here.
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S302-p - IRS1 (mouse)
Modsite: TRRSRtEsITAtsPA SwissProt Entrez-Gene
Orthologous residues
IRS1 (human): S307‑p, IRS1 (mouse): S302‑p, IRS1 (rat): S302‑p
Methods used to characterize site in vivo mutation of modification site, phospho-antibody, western blotting
Relevant cell lines - cell types - tissues:  'muscle, skeletal', 32D (myeloid) [IRS1 (mouse)], 3T3 (fibroblast) [SHP-2 (mouse), homozygous knockout], CHO (fibroblast) [EphB1 (human), transfection]
Cellular systems studied:  cell lines, tissue
Species studied:  hamster, mouse
Upstream Regulation
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
insulin increase
LY294002 insulin inhibit treatment-induced increase
PD98059 insulin no effect upon treatment-induced increase
rapamycin insulin inhibit treatment-induced increase
IGF-1 increase
TNF no change compared to control
EGF no change compared to control
PDGF increase modest increase
glucose increase
amino_acids increase
okadaic_acid increase
Downstream Regulation
Effect of modification (function):  phosphorylation
Effect of modification (process):  cell growth, altered
Comments:  leads to increased tyrosine phosphorylation of IRS-1 and increased phosphorylation of p70S6K, S6, and 4E-BP1.