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.
Only sites from this record are displayed on this page. Click on the protein name to open the protein page, and on the RSD number to open the site page. For the complete dataset, click the download button, on the right.
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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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