Curated Information
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Curated Information Page
PubMed Id: 9812896 
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.
Cardone MH, et al. (1998) Regulation of cell death protease caspase-9 by phosphorylation. Science 282, 1318-21 9812896
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S196-p - CASP9 (human)
Orthologous residues
CASP9 (human): S196‑p, CASP9 (mouse): W234‑p, CASP9 (rat): W234‑p
Characterization
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, mass spectrometry, mutation of modification site
 Relevant cell lines - cell types - tissues:  267 (epithelial), 293T (epithelial)
 Cellular systems studied:  cell lines
 Species studied:  human, mouse
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE Akt1 (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE Akt1 (human) transfection of inactive enzyme, transfection of constitutively active enzyme Ras(V12) induced phosphorylation of Casp-9.
Downstream Regulation
 Effect of modification (function):  activity, inhibited
 Effect of modification (process):  apoptosis, induced


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