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.
Protein modification; protein ubiquitination.
Belongs to the ubiquitin-conjugating enzyme family.
Autoubiquitinated by the APC/C complex during G1, leading to its degradation by the proteasome.
Detection of UBE2S in Immunoprecipitates of 293Twhole cell lysates (1 mg for IP, 20% of IP loaded) using ab177508 at 6 µg/mg lysate for IP (Lane 1). For WB detection, ab177508 was used at 1 µg/ml. Lane 2 represents control IgG IP. Detection: Chemiluminescence with an exposure time of 10 seconds.