Curated Information
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Curated Information Page
PubMed Id: 11323415 
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.
Deng X, et al. (2001) Novel role for JNK as a stress-activated Bcl2 kinase. J Biol Chem 276, 23681-8 11323415
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S70-p - Bcl-2 (mouse)
Orthologous residues
Bcl‑2 (human): S70‑p, Bcl‑2 (mouse): S70‑p, Bcl‑2 (rat): S70‑p
Characterization
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, mutation of modification site
 Disease tissue studied:  leukemia
 Relevant cell lines - cell types - tissues:  FDCP-1 (myeloid), NSF/N1.H7 (myeloid)
 Cellular systems studied:  cell lines
 Species studied:  mouse
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE JNK1 (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE JNK1 (human) pharmacological activator of upstream enzyme, transfection of dominant-negative enzyme, microscopy-colocalization
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
anisomycin increase
okadaic acid increase
okadaic acid okadaic acid inhibit treatment-induced increase
IL-3 increase
Downstream Regulation
 Effect of modification (process):  apoptosis, inhibited


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