Ubiquitin-conjugating enzyme E2 K (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme K) (Huntingtin-interacting protein 2) (HIP-2) (Ubiquitin carrier protein) (Ubiquitin-conjugating enzyme E2-25 kDa) (Ubiquitin-conjugating enzyme E2(25K)) (Ubiquitin-conjugating enzyme E2-25K) (Ubiquitin-protein ligase)
1_MANIA 6_ VQRIK 11_ REFKE 16_ VLKSE 21_ ETSKN 26_ QIKVD 31_ LVDEN 36_ FTELR 41_ GEIAG 46_ PPDTP 51_ YEGGR 56_ YQLEI 61_ KIPET 66_ YPFNP 71_ PKVRF 76_ ITKIW 81_ HPNIS 86_ SVTGA 91_ ICLDI 96_ LKDQW 101_ AAAMT 106_ LRTVL 111_ LSLQA 116_ LLAAA 121_ EPDDP 126_ QDAVV 131_ ANQYK 136_ QNPEM 141_ FKQTA 146_ RLWAH 151_ VYAGA 156_ PVSSP 161_ EYTKK 166_ IENLC 171_ AMGFD 176_ RNAVI 181_ VALSS 186_ KSWDV 191_ETATE
1: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro, in the presence or in the absence of BRCA1-BARD1 E3 ubiquitin-protein ligase complex, catalyzes the synthesis of 'Lys-48'-linked polyubiquitin chains. Does not transfer ubiquitin directly to but elongates monoubiquitinated substrate protein. Mediates the selective degradation of short-lived and abnormal proteins, such as the endoplasmic reticulum-associated degradation (ERAD) of misfolded lumenal proteins. Ubiquitinates huntingtin. May mediate foam cell formation by the suppression of apoptosis of lipid-bearing macrophages through ubiquitination and subsequence degradation of p53/TP53. Proposed to be involved in ubiquitination and proteolytic processing of NF-kappa-B; in vitro supports ubiquitination of NFKB1. In case of infection by cytomegaloviruses may be involved in the US11-dependent degradation of MHC class I heavy chains following their export from the ER to the cytosol. In case of viral infections may be involved in the HPV E7 protein-dependent degradation of RB1