Curated Information
Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Curated Information Page
PubMed Id: 9535867 
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.
Deckert M, Elly C, Altman A, Liu YC (1998) Coordinated regulation of the tyrosine phosphorylation of Cbl by Fyn and Syk tyrosine kinases. J Biol Chem 273, 8867-74 9535867
Download Sites

Y323-p - Syk (human)
Orthologous residues
Syk (human): Y323‑p, Syk iso2 (human): Y300‑p, Syk (mouse): Y317‑p, Syk (rat): Y317‑p
Characterization
 Methods used to characterize site in vivo immunoprecipitation, mutation of modification site, western blotting
 Relevant cell lines - cell types - tissues:  COS (fibroblast), Jurkat (T lymphocyte)
 Cellular systems studied:  cell lines
 Species studied:  human, monkey
Downstream Regulation
 Effect of modification (function):  enzymatic activity, induced, molecular association, regulation
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
Cbl (human) Induces molecular association, regulation, phosphorylation co-immunoprecipitation, yeast two-hybrid
Fyn (human) SH2 Induces molecular association, regulation co-immunoprecipitation


Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.