Curated Information
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Curated Information Page
PubMed Id: 14555991 
Luciano F, et al. (2003) Phosphorylation of Bim-EL by Erk1/2 on serine 69 promotes its degradation via the proteasome pathway and regulates its proapoptotic function. Oncogene 22, 6785-93 14555991
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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S69-p - BIM (human)
Orthologous residues
BIM (human): S69‑p, BIM iso2 (human): , BIM iso3 (human): , BIM (mouse): S65‑p, BIM (rat): S65‑p
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, electrophoretic mobility shift, mutation of modification site
 Disease tissue studied:  leukemia, chronic myelogenous leukemia, lymphoma, Burkitt's lymphoma
 Relevant cell lines - cell types - tissues:  293 (epithelial), K562 (erythroid), RAMOS (B lymphocyte)
 Cellular systems studied:  cell lines
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE ERK1 (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE ERK1 (human) phospho-antibody, pharmacological inhibitor of upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
phorbol ester increase
U0126 phorbol ester inhibit treatment-induced increase
GF109203X phorbol ester inhibit treatment-induced increase
SB203580 phorbol ester no effect upon treatment-induced increase
LY294002 phorbol ester no effect upon treatment-induced increase
tamoxifen increase
Downstream Regulation
 Effect of modification (function):  protein degradation
 Effect of modification (process):  apoptosis, inhibited

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