Curated Information
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Curated Information Page
PubMed Id: 8630736 
Park H, et al. (1996) Regulation of Btk function by a major autophosphorylation site within the SH3 domain. Immunity 4, 515-25 8630736
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.
Click on the protein name to open the protein page, and on the RSD number to open the site page.
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Y223-p - Btk (human)
Orthologous residues
Btk (human): Y223‑p, Btk (mouse): Y223‑p, Btk (rat): Y224‑p
 Methods used to characterize site in vivo 2D analysis, [32P] bio-synthetic labeling, mutation of modification site, peptide sequencing, phosphoamino acid analysis, phosphopeptide mapping
 Relevant cell lines - cell types - tissues:  3T3 (fibroblast)
 Cellular systems studied:  cell lines
 Species studied:  mouse
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE Btk (mouse)
Downstream Regulation
 Effect of modification (process):  cell growth, altered
 Comments:  BTK*/Y223F mutant showed increased transformation, as compared to BTK*.

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 2D analysis, phosphopeptide mapping

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