Curated Information

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Curated Information Page

PubMed Id: 8413300

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.

Information from this record has been curated, but not yet edited in PhosphoSitePlus^® and may be incomplete.

Gervais FG, et al. (1993) The SH2 domain is required for stable phosphorylation of p56lck at tyrosine 505, the negative regulatory site. Mol Cell Biol 13, 7112-21 8413300

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.

Y394-p - Lck (mouse)

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Orthologous residues

Lck (human): Y394‑p, Lck (mouse): Y394‑p, Lck (rat): Y394‑p

Y505-p - Lck (mouse)

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Orthologous residues

Lck (human): Y505‑p, Lck (mouse): Y505‑p, Lck (rat): Y505‑p

Characterization

Enzymes shown to modify site in vitro:

Type	Enzyme
PHOSPHATASE	CD45 (mouse)

Comments: inhibited by Lck SH2 domain.

Upstream Regulation

Potential in vivo enzymes for site:

Type	Enzyme	Evidence	Notes
KINASE	CSK (mouse)	transfection of wild-type enzyme, mutation in upstream enzyme recognition motif

Treatments, proteins and their effect on site modification:

Treatments	Referenced Treatments	Manipulated Protein	Referenced Protein	Effect	Notes
vanadate				increase

Downstream Regulation

Effect of modification (function): enzymatic activity, inhibited

Comments: SH2 domain protects from dephosphorylation.

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