Curated Information
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Curated Information Page
PubMed Id: 10191262 
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.
Kobayashi T, Cohen P (1999) Activation of serum- and glucocorticoid-regulated protein kinase by agonists that activate phosphatidylinositide 3-kinase is mediated by 3-phosphoinositide-dependent protein kinase-1 (PDK1) and PDK2. Biochem J 339 ( Pt 2), 319-28 10191262
Only sites from this record are displayed on this page. Click on the protein name to open the protein page, and on the RSD number to open the site page. For the complete dataset, click the download button, on the right.
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T256-p - SGK1 (human)
Orthologous residues
SGK1 (human): T256‑p, SGK1 iso3 (human): T270‑p, SGK1 (mouse): T256‑p, SGK1 (rat): T256‑p
Characterization
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE PDK1 (human)
Downstream Regulation
 Effect of modification (function):  enzymatic activity, induced

S422-p - SGK1 (human)
Orthologous residues
SGK1 (human): S422‑p, SGK1 iso3 (human): S436‑p, SGK1 (mouse): S422‑p, SGK1 (rat): S421‑p
Characterization
 Methods used to characterize site in vivo phospho-antibody
 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
IGF-1 increase
wortmannin IGF-1 inhibit treatment-induced increase
H2O2 increase
wortmannin H2O2 inhibit treatment-induced increase
Downstream Regulation
 Effect of modification (function):  enzymatic activity, induced


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