Curated Information

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Curated Information Page

PubMed Id: 8630736

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.

Park H, et al. (1996) Regulation of Btk function by a major autophosphorylation site within the SH3 domain. Immunity 4, 515-25 8630736

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.

Y223-p - Btk (human)

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Orthologous residues

Btk (human): Y223‑p, Btk (mouse): Y223‑p, Btk (rat): Y224‑p

Characterization

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)

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Orthologous residues

Btk (human): Y551‑p, Btk (mouse): Y551‑p, Btk (rat): Y552‑p

Characterization

Methods used to characterize site in vivo: 2D analysis, phosphopeptide mapping

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