Curated Information
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Curated Information Page
PubMed Id: 16224021 
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.
Cha TL, et al. (2005) Akt-mediated phosphorylation of EZH2 suppresses methylation of lysine 27 in histone H3. Science 310, 306-10 16224021
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S21-p - EZH2 (human)
Orthologous residues
EZH2 (human): S21‑p, EZH2 iso2 (human): S21‑p, EZH2 (mouse): S21‑p, EZH2 (rat): S21‑p
Characterization
 Methods used to characterize site in vivo mutation of modification site, phospho-antibody, western blotting
 Disease tissue studied:  breast cancer
 Relevant cell lines - cell types - tissues:  293T (epithelial), 3T3 (fibroblast), A431 (epithelial), MDA-MB453 (breast cell), T47D (breast cell)
 Cellular systems studied:  cell lines
 Species studied:  human, mouse
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE Akt1 (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE Akt1 (human) pharmacological activator of upstream enzyme, siRNA inhibition of enzyme, transfection of dominant-negative enzyme, transfection of constitutively active enzyme, transfection of wild-type enzyme, modification site within consensus motif, phospho-motif antibody, co-immunoprecipitation, pharmacological inhibitor of upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
LY294002 decrease
Downstream Regulation
 Effect of modification (function):  enzymatic activity, inhibited, molecular association, regulation
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
H3 (human) Disrupts activity, induced transcription, altered co-immunoprecipitation
 Comments:  Phosphorylation suppresses trimethylation of Histone H3's trimethylation on K27. Enzymatic inhibition through a decreased affinity towards H3.


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