Curated Information
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Curated Information Page
PubMed Id: 10230394 
Harada H, et al. (1999) Phosphorylation and inactivation of BAD by mitochondria-anchored protein kinase A. Mol Cell 3, 413-22 10230394
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.
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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, immunoprecipitation, mutation of modification site, western blotting
 Relevant cell lines - cell types - tissues:  FL5.12 (lymphoid)
 Cellular systems studied:  cell lines
 Species studied:  mouse
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE PKACA (mouse)
 Comments:  PKA inhibitor blocks endogenous kinase that phosphorylates S112.
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE PKACA (mouse) co-immunoprecipitation, pharmacological inhibitor of upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
IL-3 increase
IL-3, H-89 IL-3 inhibit treatment-induced increase
LY294002, IL-3 IL-3 inhibit treatment-induced increase
IL-3, PD98059 IL-3 inhibit treatment-induced increase
IL-3, 8-Rp-cAMP IL-3 inhibit treatment-induced increase
LY294002, IL-3, PD98059 IL-3 augment treatment-induced decrease
Downstream Regulation
 Effect of modification (function):  intracellular localization
 Effect of modification (process):  apoptosis, altered
 Comments:  Bad is phosphoryated by PKA associated with mitochondrial membrane fraction.


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