Curated Information
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PubMed Id: 17158447 
Danek EI, et al. (2007) Glycogen synthase kinase-3 phosphorylates CdGAP at a consensus ERK 1 regulatory site. J Biol Chem 282, 3624-31 17158447
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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T776-p - CdGAP (mouse)
Orthologous residues
CdGAP (human): T789‑p, CdGAP (mouse): T776‑p, CdGAP (rat): T779‑p
 Methods used to characterize site in vivo mutation of modification site, phospho-antibody
 Relevant cell lines - cell types - tissues:  3T3 (fibroblast) [SHP-2 (mouse), homozygous knockout], COS (fibroblast)
 Cellular systems studied:  cell lines
 Species studied:  monkey, mouse
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE GSK3A (human)
KINASE GSK3B (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE GSK3A (human) pharmacological inhibitor of upstream enzyme
KINASE GSK3B (human) pharmacological inhibitor of upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
serum starvation increase
lithium decrease
SB415286 decrease
AR-A014418 decrease
Downstream Regulation
 Effect of modification (process):  transcription, altered
 Comments:  increases CdGAP expression

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