Curated Information

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Curated Information Page

PubMed Id: 18328268

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.

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

Y213-p - Abi-1 (human)

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Orthologous residues

Abi‑1 (human): Y213‑p, Abi‑1 iso2 (human): Y208‑p, Abi‑1 iso3 (human): Y213‑p, Abi‑1 (mouse): Y213‑p, Abi‑1 iso4 (mouse): Y208‑p, Abi‑1 (rat): Y208‑p

Characterization

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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