Curated Information
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Curated Information Page
PubMed Id: 8413300 
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
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.
Information from this record has been curated, but not yet edited in PhosphoSitePlus® and may be incomplete.
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Y394-p - Lck (mouse)
Orthologous residues
Lck (human): Y394‑p, Lck iso3 (human): Y424‑p, Lck (mouse): Y394‑p, Lck (rat): Y394‑p

Y505-p - Lck (mouse)
Orthologous residues
Lck (human): Y505‑p, Lck iso3 (human): Y535‑p, Lck (mouse): Y505‑p, Lck (rat): Y505‑p
 Enzymes shown to modify site in vitro
Type Enzyme
 Comments:  inhibited by Lck SH2 domain.
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE CSK (mouse) mutation in upstream enzyme recognition motif, transfection of wild-type enzyme
 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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