Curated Information
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Curated Information Page
PubMed Id: 16139227 
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.
Enomoto A, et al. (2005) Akt/PKB regulates actin organization and cell motility via Girdin/APE. Dev Cell 9, 389-402 16139227
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S1417-p - girdin (human)
Orthologous residues
girdin (human): S1417‑p, girdin iso5 (human): S592‑p, girdin (mouse): S1417‑p, girdin (rat): S1397‑p
Characterization
 Methods used to characterize site in vivo mutation of modification site, phospho-antibody
 Relevant cell lines - cell types - tissues:  Vero (epithelial) [girdin (human)]
 Cellular systems studied:  cell lines
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE Akt1 (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE Akt1 (human) transfection of dominant-negative enzyme, co-immunoprecipitation, siRNA inhibition of enzyme, transfection of constitutively active enzyme, transfection of wild-type enzyme, pharmacological inhibitor of upstream enzyme, inhibition of upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
EGF increase
LY294002 EGF inhibit treatment-induced increase
wortmannin EGF inhibit treatment-induced increase
PD98059 EGF no effect upon treatment-induced increase
Downstream Regulation
 Effect of modification (function):  intracellular localization, molecular association, regulation
 Effect of modification (process):  cell motility, altered, cytoskeletal reorganization
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
ACTB (human) Induces cell motility, altered, cytoskeletal reorganization yeast two-hybrid, microscopy-colocalization


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