Curated Information
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Curated Information Page
PubMed Id: 16880201 
Ramm G, Larance M, Guilhaus M, James DE (2006) A role for 14-3-3 in insulin-stimulated GLUT4 translocation through its interaction with the RabGAP AS160. J Biol Chem 281, 29174-80 16880201
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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T642-p - AS160 (human)
Orthologous residues
AS160 (human): T642‑p, AS160 iso2 (human): T642‑p, AS160 iso3 (human): T642‑p, AS160 (mouse): T649‑p, AS160 iso2 (mouse): T649‑p, AS160 (rat): T651‑p
 Methods used to characterize site in vivo mutation of modification site
 Cellular systems studied:  cell lines
 Species studied:  hamster
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE Akt1 (human) transfection of constitutively active enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
insulin INSR (human) 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
14-3-3 theta (human) Induces co-immunoprecipitation
14-3-3 epsilon (human) Induces co-immunoprecipitation
 Comments:  phosphorylation of this site has an effect on insulin-stimulated GLUT4 trafficking to the cell surface

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