Curated Information
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Curated Information Page
PubMed Id: 10191262 
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
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, 2012,40:D261-70). To learn more about the scope of PhosphoSitePlus®, click here.
Click on the protein name to open the protein page, and on the RSD number to open the site page.
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T256-p - SGK1 (human)
Orthologous residues
SGK1 (human): T256‑p, SGK1 iso2 (human): T351‑p, SGK1 iso3 (human): T270‑p, SGK1 (mouse): T256‑p, SGK1 (rat): T256‑p
 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 iso2 (human): S517‑p, SGK1 iso3 (human): S436‑p, SGK1 (mouse): S422‑p, SGK1 (rat): S421‑p
 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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