Curated Information
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Curated Information Page
PubMed Id: 9890970 
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.
Information from this record has been curated, but not yet edited in PhosphoSitePlus® and may be incomplete.
Hunter S, Burton EA, Wu SC, Anderson SM (1999) Fyn associates with Cbl and phosphorylates tyrosine 731 in Cbl, a binding site for phosphatidylinositol 3-kinase. J Biol Chem 274, 2097-106 9890970
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Y731-p - Cbl (human)
Orthologous residues
Cbl (human): Y731‑p, Cbl (mouse): Y737‑p, Cbl (rat): Y738‑p
Characterization
 Methods used to characterize site in vivo mutation of modification site
 Disease tissue studied:  thymoma
 Relevant cell lines - cell types - tissues:  32Dcl3 (myeloid)
 Cellular systems studied:  cell lines
 Species studied:  mouse, rat
 Comments:  Nb2 cell line
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE Fyn (human)
Downstream Regulation
 Effect of modification (function):  molecular association, regulation
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
PIK3R1 (rat) Induces not reported pull-down assay


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