Curated Information
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Curated Information Page
PubMed Id: 11042191 
Krasel C, et al. (2001) Phosphorylation of GRK2 by protein kinase C abolishes its inhibition by calmodulin. J Biol Chem 276, 1911-5 11042191
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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S29-p - GRK2 (human)
Orthologous residues
GRK2 (human): S29‑p, GRK2 (mouse): S29‑p, GRK2 (rat): S29‑p, GRK2 (cow): S29‑p
Characterization
 Methods used to characterize site in vivo mutation of modification site
 Relevant cell lines - cell types - tissues:  293 (epithelial)
 Cellular systems studied:  cell lines
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE PKCA (rat)
KINASE PKCD (rat)
KINASE PKCG (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE PKCA (human) pharmacological activator of upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
phorbol ester increase
Downstream Regulation
 Effect of modification (function):  activity, induced


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