Curated Information
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Curated Information Page
PubMed Id: 14993287 
Glading A, et al. (2004) Epidermal growth factor activates m-calpain (calpain II), at least in part, by extracellular signal-regulated kinase-mediated phosphorylation. Mol Cell Biol 24, 2499-512 14993287
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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S50-p - Calpain-2 (human)
Orthologous residues
Calpain‑2 (human): S50‑p, Calpain‑2 (mouse): S50‑p, Calpain‑2 (rat): S50‑p
Characterization
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, mutation of modification site
 Relevant cell lines - cell types - tissues:  NR6WT (fibroblast)
 Cellular systems studied:  cell lines
 Species studied:  mouse
 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) pharmacological activator of upstream enzyme, pharmacological inhibitor of upstream enzyme, co-immunoprecipitation
KINASE ERK2 (human) pharmacological activator of upstream enzyme, pharmacological inhibitor of upstream enzyme, co-immunoprecipitation
Downstream Regulation
 Effect of modification (process):  cell adhesion, altered, cell motility, altered


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