Curated Information
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Curated Information Page
PubMed Id: 11226282 
Baba Y, et al. (2001) BLNK mediates Syk-dependent Btk activation. Proc Natl Acad Sci U S A 98, 2582-6 11226282
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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Y551-p - Btk (human)
Orthologous residues
Btk (human): Y551‑p, Btk (mouse): Y551‑p, Btk (rat): Y552‑p
 Methods used to characterize site in vivo immunoprecipitation, mutation of modification site, phospho-antibody, western blotting
 Disease tissue studied:  lymphoma, B cell lymphoma
 Relevant cell lines - cell types - tissues:  293T (epithelial), DT40 (B lymphocyte) [BLNK (human)]
 Cellular systems studied:  cell lines
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE Syk (human)
 Comments:  Syc phosphorylates Btk and enhances Btk activity in the presence of BLNK.
Upstream Regulation
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
Syk (human), BLNK (human) increase Blnk is required for Syk phosphorylation and activation of Btk.
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
BLNK (human) Induces co-immunoprecipitation
 Comments:  Btk-SH2 domain is reqired for Syk-dependent phosphorylation.

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