Curated Information
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PubMed Id: 18328268 
Xiong X, et al. (2008) Allosteric inhibition of the nonMyristoylated c-Abl tyrosine kinase by phosphopeptides derived from Abi1/Hssh3bp1. Biochim Biophys Acta 1783, 737-47 18328268
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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Y213-p - Abi-1 (human)
Orthologous residues
Abi‑1 (human): Y213‑p, Abi‑1 iso2 (human): Y208‑p, Abi‑1 iso3 (human): Y213‑p, Abi‑1 iso11 (human): Y149‑p, Abi‑1 iso12 (human): Y230‑p, Abi‑1 (mouse): Y213‑p, Abi‑1 iso4 (mouse): Y208‑p, Abi‑1 (rat): Y208‑p
 Methods used to characterize site in vivo mutation of modification site
 Disease tissue studied:  prostate cancer
 Relevant cell lines - cell types - tissues:  LNCaP (prostate cell)
 Cellular systems studied:  cell lines
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE Abl (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE Abl (human) co-immunoprecipitation phosphorylation of this site inhibits Abl
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
vanadate increase
STI571 vanadate inhibit treatment-induced increase

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