Curated Information
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Curated Information Page
PubMed Id: 12551925 
Corbit KC, et al. (2003) Activation of Raf-1 signaling by protein kinase C through a mechanism involving Raf kinase inhibitory protein. J Biol Chem 278, 13061-8 12551925
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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S153-p - RKIP (rat)
Orthologous residues
RKIP (human): S153‑p, RKIP (mouse): T153‑p, RKIP (rat): S153‑p
 Methods used to characterize site in vivo mutation of modification site, phospho-antibody
 Relevant cell lines - cell types - tissues:  H19-7 (neuron) [IGF1R (human)]
 Cellular systems studied:  cell lines
 Species studied:  rat
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE PKCB iso2 (rat)
 Comments:  Classic and atypical but not novel PKC isoforms phosphorylate RKIP at serine 153.
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE PKCA (rat) pharmacological inhibitor of upstream enzyme, pharmacological activator of upstream enzyme Although the exact PKC isotype(s) responsible for in vivo phosphorylation were not proven in this paper, in vitro evidence indicates that classic and atypical but not novel PKC isoforms phosphorylate RKIP at serine 153.
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
phorbol ester increase
EGF increase
Downstream Regulation
 Effect of modification (function):  molecular association, regulation
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
RAF1 (rat) Disrupts enzymatic activity, inhibited co-immunoprecipitation
 Comments:  RKIP inhibits MAP kinase activation in response to growth factors or PKC activators, and PKC can regulate Raf-1 signaling through phosphorylation of RKIP. Classical and atypical PKCs phosphorylate RKIP on Ser-153, which results in the displacement of RKIP from Raf-1, freeing Raf-1 to activate downstream targets..

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