Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Catalyzes 'Lys-11'-linked polyubiquitination. Acts as an essential factor of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated ubiquitin ligase that controls progression through mitosis. Acts by specifically elongating 'Lys-11'-linked polyubiquitin chains initiated by the E2 enzyme UBE2C/UBCH10 on APC/C substrates, enhancing the degradation of APC/C substrates by the proteasome and promoting mitotic exit. Also acts by elongating ubiquitin chains initiated by the E2 enzyme UBE2D1/UBCH5 in vitro; it is however unclear whether UBE2D1/UBCH5 acts as a E2 enzyme for the APC/C in vivo. Also involved in ubiquitination and subsequent degradation of VHL, resulting in an accumulation of HIF1A. In vitro able to promote polyubiquitination using all 7 ubiquitin Lys residues, except 'Lys-48'-linked polyubiquitination. Component of the APC/C complex. Interacts with CDC20, FZR1/CDH1 and VHL. Belongs to the ubiquitin-conjugating enzyme family. Note: This description may include information from UniProtKB.
Protein type: Ligase; Ubiquitin ligase; Ubiquitin conjugating system; EC 126.96.36.199
Molecular Function: ATP binding; ubiquitin protein ligase binding; ubiquitin-protein ligase activity
Biological Process: anaphase-promoting complex activation; anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; cell division; exit from mitosis; protein modification process
LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.