Gerard B, et al. (2012) Lysine 394 is a novel Rad6B-induced ubiquitination site on beta-catenin. Biochim Biophys Acta 1823, 1686-96 22705350

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, 2015, 43:D512-20). To learn more about the scope of PhosphoSitePlus®, click here.

Click on the protein name to open the protein page, and on the RSD number to open the site page.

Download

K394-ub - CTNNB1 (human) ▲

Modsite: NLSDAAtkQEGMEGL SwissProt Entrez-Gene Orthologous residues CTNNB1 (human): K394‑ub, CTNNB1 (mouse): K394‑ub, CTNNB1 (rat): K394‑ub, CTNNB1 (rabbit): K394‑ub Characterization Methods used to characterize site in vivo:  mutation of modification site Disease tissue studied:  breast cancer Relevant cell lines - cell types - tissues:  MCF-7 (breast cell), MDA-MB-231 (breast cell) Cellular systems studied:  cell lines Species studied:  human Enzymes shown to modify site in vitro:  Type Enzyme UBIQUITIN LIGASE UBE2B (human) Upstream Regulation Potential in vivo enzymes for site:  Type Enzyme Evidence Notes UBIQUITIN LIGASE UBE2B (human) microscopy-colocalization, transfection of inactive enzyme, siRNA inhibition of enzyme, co-immunoprecipitation, transfection of wild-type enzyme Downstream Regulation Effect of modification (function):  protein stabilization Effect of modification (process):  transcription, induced Associated Diseases Diseases Alterations Comments breast adenocarcinoma increased