Curated Information
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Curated Information Page
PubMed Id: 9381178 
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.
del Peso L, et al. (1997) Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt. Science 278, 687-9 9381178
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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S112-p - BAD (mouse) ▲
Orthologous residues
BAD (human): S75‑p, BAD (mouse): S112‑p, BAD (rat): S113‑p
Characterization
 Methods used to characterize site in vivo:  [32P] bio-synthetic labeling, mutation of modification site
 Cellular systems studied:  cell lines
 Comments:  Both endogenous mouse and transfected forms of Akt were shown to regulate this phosphorylation.
 Enzymes shown to modify site in vitro: 
Type Enzyme
KINASE Akt1 (mouse)
 Comments:  WT, kinase-dead and myristoylated Akt (constitutively active) constructs were used in these experiments.
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE Akt1 (mouse) pharmacological activator of upstream enzyme, genetic transfer of dominant-negative enzyme, genetic transfer of constitutively active upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
IL-3 increase
wortmannin IL-3 inhibit treatment-induced increase
LY294002 IL-3 inhibit treatment-induced increase

S136-p - BAD (mouse) ▲
Orthologous residues
BAD (human): S99‑p, BAD (mouse): S136‑p, BAD (rat): S137‑p
Characterization
 Methods used to characterize site in vivo:  [32P] bio-synthetic labeling, mutation of modification site
 Cellular systems studied:  cell lines
 Comments:  Both endogenous mouse and transfected forms of Akt were shown to regulate this phosphorylation.
 Enzymes shown to modify site in vitro: 
Type Enzyme
KINASE Akt1 (mouse)
 Comments:  WT, kinase-dead and myristoylated Akt (constitutively active) constructs were used in these experiments.
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE Akt1 (mouse) pharmacological activator of upstream enzyme, genetic transfer of dominant-negative enzyme, genetic transfer of constitutively active upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
IL-3 increase
wortmannin IL-3 inhibit treatment-induced increase
LY294002 IL-3 inhibit treatment-induced increase


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