Curated Information
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Curated Information Page
PubMed Id: 12037680 
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.
Semplici F, Meggio F, Pinna LA, Oliviero S (2002) CK2-dependent phosphorylation of the E2 ubiquitin conjugating enzyme UBC3B induces its interaction with beta-TrCP and enhances beta-catenin degradation. Oncogene 21, 3978-87 12037680
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S233-p - UBC3B (human)
Orthologous residues
UBC3B (human): S233‑p, UBC3B (mouse): S233‑p, UBC3B (rat): S233‑p
Characterization
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, mutation of modification site, western blotting
 Relevant cell lines - cell types - tissues:  293 (epithelial), HeLa (cervical)
 Cellular systems studied:  cell lines
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE CK2A1 (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE CK2A1 (human) pharmacological inhibitor of upstream enzyme, transfection of wild-type enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
TBB decrease
Downstream Regulation
 Effect of modification (function):  molecular association, regulation
 Effect of modification (process):  transcription, altered
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
BRD8 iso1 (human) Induces molecular association, regulation in vitro, pull-down assay
 Comments:  CK2-dependent phosphorylation of UCB3C leads to beta-catenin degredation and inhibition of beta-catenin transcription.


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