Curated Information
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Curated Information Page
PubMed Id: 11583630 
Lee MJ, et al. (2001) Akt-mediated phosphorylation of the G protein-coupled receptor EDG-1 is required for endothelial cell chemotaxis. Mol Cell 8, 693-704 11583630
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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T236-p - EDG-1 (human)
Orthologous residues
EDG‑1 (human): T236‑p, EDG‑1 (mouse): T236‑p, EDG‑1 (rat): T237‑p
 Methods used to characterize site in vivo mutation of modification site, western blotting
 Relevant cell lines - cell types - tissues:  CHO (fibroblast) [EphB1 (human), transfection], HUVEC (endothelial), muscle
 Cellular systems studied:  cell lines, primary cells
 Species studied:  hamster, human, mouse
 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) pharmacological activator of upstream enzyme, co-immunoprecipitation, pharmacological inhibitor of upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
sphingosine 1-phosphate Akt1 (human) increase
LY294002 sphingosine 1-phosphate Akt1 (human) inhibit treatment-induced increase
wortmannin sphingosine 1-phosphate Akt1 (human) inhibit treatment-induced increase
IGF-1 increase
Downstream Regulation
 Effect of modification (process):  cell motility, altered, cytoskeletal reorganization
 Comments:  Cortical actin assembly, chemotaxis, and angiogenesis

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