Ubiquitin-conjugating enzyme E2 S (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme S) (E2-EPF) (Ubiquitin carrier protein S) (Ubiquitin-conjugating enzyme E2-24 kDa) (Ubiquitin-conjugating enzyme E2-EPF5) (Ubiquitin-protein ligase S)
1_MNSNV 6_ ENLPP 11_ HIIRL 16_ VYKEV 21_ TTLTA 26_ DPPDG 31_ IKVFP 36_ NEEDL 41_ TDLQV 46_ TIEGP 51_ EGTPY 56_ AGGLF 61_ RMKLL 66_ LGKDF 71_ PASPP 76_ KGYFL 81_ TKIFH 86_ PNVGA 91_ NGEIC 96_ VNVLK 101_ RDWTA 106_ ELGIR 111_ HVLLT 116_ IKCLL 121_ IHPNP 126_ ESALN 131_ EEAGR 136_ LLLEN 141_ YEEYA 146_ ARARL 151_ LTEIH 156_ GGAGG 161_ PSGRA 166_ EAGRA 171_ LASGT 176_ EASST 181_ DPGAP 186_ GGPGG 191_ AEGPM 196_ AKKHA 201_ GERDK 206_ KLAAK 211_ KKTDK 216_KRALR
1: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins (PubMed:19820702, PubMed:19822757, PubMed:22496338, PubMed:27259151). 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 (PubMed:19820702, PubMed:19822757, PubMed:27259151, PubMed:27910872). 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 (PubMed:19820702, PubMed:19822757, PubMed:27259151). Also acts by elongating ubiquitin chains initiated by the E2 enzyme UBE2D1/UBCH5 in vitro; it is however unclear whether UBE2D1/UBCH5 acts as an E2 enzyme for the APC/C in vivo. Also involved in ubiquitination and subsequent degradation of VHL, resulting in an accumulation of HIF1A (PubMed:16819549). In vitro able to promote polyubiquitination using all 7 ubiquitin Lys residues, except 'Lys-48'-linked polyubiquitination (PubMed:20061386, PubMed:20622874)