Curated Information
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Curated Information Page
PubMed Id: 19481526 
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.
Hutti JE, et al. (2009) Phosphorylation of the tumor suppressor CYLD by the breast cancer oncogene IKKepsilon promotes cell transformation. Mol Cell 34, 461-72 19481526
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S414-p - CYLD (mouse)
Orthologous residues
CYLD (human): S418‑p, CYLD (mouse): S414‑p, CYLD (rat): S415‑p
Characterization
 Methods used to characterize site in vivo immunoprecipitation, mass spectrometry, mutation of modification site, western blotting
 Relevant cell lines - cell types - tissues:  293 (epithelial)
 Cellular systems studied:  cell lines
 Species studied:  human
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE IKKE (human) co-immunoprecipitation, transfection of inactive enzyme, transfection of wild-type enzyme
Downstream Regulation
 Effect of modification (function):  enzymatic activity, inhibited
 Effect of modification (process):  cell growth, induced
 Comments:  S418 phosphorylation is necessary to induce IKK-epsilon induced transformation and decreases its deubiquitinase activity.


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