Curated Information
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Curated Information Page
PubMed Id: 10792047 
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.
Dong LQ, et al. (2000) Phosphorylation of protein kinase N by phosphoinositide-dependent protein kinase-1 mediates insulin signals to the actin cytoskeleton. Proc Natl Acad Sci U S A 97, 5089-94 10792047
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T774-p - PKN1 (human)
Orthologous residues
PKN1 (human): T774‑p, PKN1 (mouse): T778‑p, PKN1 (rat): T778‑p
Characterization
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, immunoprecipitation, mutation of modification site, phosphoamino acid analysis, phosphopeptide mapping
 Relevant cell lines - cell types - tissues:  CHO (fibroblast) [EphB1 (human), transfection]
 Cellular systems studied:  cell lines
 Species studied:  hamster
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE PDK1 (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE PDK1 (human) transfection of inactive enzyme, transfection of wild-type enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
insulin increase
wortmannin insulin no effect upon treatment-induced increase
LY294002 insulin no effect upon treatment-induced increase
Downstream Regulation
 Effect of modification (function):  enzymatic activity, induced, molecular association, regulation
 Effect of modification (process):  cytoskeletal reorganization
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
PDK1 (human) Induces co-immunoprecipitation, electrophoretic visualization


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