Ubiquitin Conjugating Enzyme E2C Binding Protein (UBE2CBP)

UBE2CBP bound UBE2C and that the amino acid sequence between 235 and 257 was necessary for this binding. UBE2CBP showed a self-ubiquitinylation activity in a HECT-like sequence-dependent manner. The C-terminal half (amino acids 188-389) showed stronger activity than the full-length UBE2CBP. In addition, the C-terminal half of UBE2CBP was able to bind cyclin B and ubiquitinylate cyclin B in vitro.UBE2CBP gene contains 10 exons and spans approximately 176 kb.The C terminus of UBE2CBP shows weak homology to the HECT domain, which is conserved in one of the ubiquitin ligase (E3) families. Members of this family accept the ubiquitin moiety from E2 and transfer it to the target protein.