EC Number   |
Posttranslational Modification |
Reference |
|---|
   2.3.2.27 | more |
enzyme is N-terminally mono-ubiquitinated by the ubiquitin conjugating enzyme Ubc16 |
694303 |
| 2.3.2.27 | phosphoprotein |
isoform RBCK1 undergoes efficient phosphorylation by protein kinase Cbeta. The phosphorylated RBCK1 shows no self-ubiquitination activity in vitro. Overexpression of protein kinase Cbeta leads to significant increases in the amounts of intracellular RBCK1, presumably suppressing the proteasomal degradation of RBCK1 through self-ubiquitination |
693039 |
| 2.3.2.27 | phosphoprotein |
the E3 ubiquitin ligase activity of isoform c-Cbl is negatively regulated by other domains present in the amino-terminal half of the protein, i.e. the TKB and linker helix domains, and this negative regulation is removed when the protein is phosphorylated on tyrosine residues. Tyrosine phosphorylation alters the conformation of c-Cbl. Mutation of certain conserved tyrosine residues to glutamate can constitutively activate the E3 activity of c-Cbl |
727846 |
| 2.3.2.27 | ubiquitination |
isoform RNF180 itself is heavily ubiquitinated and degraded by the proteasome |
692490 |
| 2.3.2.27 | ubiquitination |
isoform TRIM5 is monoubiquitinated both by itself and by E3 ubiquitin ligase Ro52, and ubiquitination does not lead to proteasomal degradation. Monoubiquitination may be a signal for TRIM5 to translocate from cytoplasmic bodies to the cytoplasm |
692286 |
| 2.3.2.27 | ubiquitination |
RNF43 is ubiquitinated in intact cells |
692211 |
