Curated Information
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Curated Information Page
PubMed Id: 10871840 
Langlais P, Dong LQ, Hu D, Liu F (2000) Identification of Grb10 as a direct substrate for members of the Src tyrosine kinase family. Oncogene 19, 2895-903 10871840
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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Y67-p - Grb10 (human)
Orthologous residues
Grb10 (human): Y67‑p, Grb10 (mouse): N13‑p, Grb10 (rat): N13‑p
Characterization
 Methods used to characterize site in vivo mutation of modification site, phospho-antibody, western blotting
 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 Fyn (human)
KINASE Src (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE Fyn (human) transfection of constitutively active enzyme, genetic transfer of dominant-negative enzyme
KINASE Src (human) transfection of constitutively active enzyme, genetic transfer of dominant-negative enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
insulin increase
vanadate insulin augment treatment-induced increase
herbimycin A vanadate inhibit treatment-induced increase
vanadate no change compared to control
Downstream Regulation
 Effect of modification (function):  molecular association, regulation
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
InsR (human) Disrupts co-immunoprecipitation


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