Curated Information
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Curated Information Page
PubMed Id: 12792650 
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.
Allan LA, et al. (2003) Inhibition of caspase-9 through phosphorylation at Thr 125 by ERK MAPK. Nat Cell Biol 5, 647-54 12792650
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T125-p - CASP9 (human)
Orthologous residues
CASP9 (human): T125‑p, CASP9 (mouse): T163‑p, CASP9 (rat): T163‑p
Characterization
 Methods used to characterize site in vivo mutation of modification site, phospho-antibody, western blotting
 Relevant cell lines - cell types - tissues:  293 (epithelial), HeLa (cervical)
 Cellular systems studied:  cell lines
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE ERK2 (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE ERK1 (human) pharmacological inhibitor of upstream enzyme, transfection of constitutively active enzyme, co-immunoprecipitation
KINASE ERK2 (human) pharmacological inhibitor of upstream enzyme, transfection of constitutively active enzyme, co-immunoprecipitation
 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
PD184352 phorbol ester inhibit treatment-induced increase
EGF increase
U0126 EGF inhibit treatment-induced increase
PD184352 EGF inhibit treatment-induced increase


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