Curated Information
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Curated Information Page
PubMed Id: 12468540 
Zhang Z, Shen K, Lu W, Cole PA (2003) The role of C-terminal tyrosine phosphorylation in the regulation of SHP-1 explored via expressed protein ligation. J Biol Chem 278, 4668-74 12468540
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.
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.
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Y536-p - SHP-1 (human)
Orthologous residues
SHP‑1 (human): Y536‑p, SHP‑1 iso4 (human): Y536‑p, SHP‑1 (mouse): Y536‑p, SHP‑1 (rat): Y538‑p
Downstream Regulation
 Effect of modification (function):  enzymatic activity, induced, molecular association, regulation
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
Grb2 (human) Induces in vitro, pull-down assay
 Comments:  allows intramolecular interaction with an SH2 domain relieving inhibition (in vitro)

Y564-p - SHP-1 (human)
Orthologous residues
SHP‑1 (human): Y564‑p, SHP‑1 iso4 (human): , SHP‑1 (mouse): Y564‑p, SHP‑1 (rat): Y566‑p
Downstream Regulation
 Effect of modification (function):  molecular association, regulation
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
Grb2 (human) Induces in vitro, pull-down assay


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