Curated Information
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Curated Information Page
PubMed Id: 11013245 
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.
Landrieu I, et al. (2001) p13(SUC1) and the WW domain of PIN1 bind to the same phosphothreonine-proline epitope. J Biol Chem 276, 1434-8 11013245
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T48-p - Cdc25C (frog)
Orthologous residues
Cdc25C (human): T48‑p, Cdc25C iso3 (human): T48‑p, Cdc25C (mouse): S48‑p, Cdc25C (frog): T48‑p
Downstream Regulation
 Effect of modification (function):  molecular association, regulation
 Effect of modification (process):  cell cycle regulation
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
CKS1 (human) WW Induces enzymatic activity, induced, molecular association, regulation cell cycle regulation NMR spectroscopy, in vitro
Pin1 (human) WW Induces molecular association, regulation in vitro, NMR spectroscopy
 Comments:  Pin1 and CKS1 compete for binding to phosphorylated T48 Cdc25C.


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