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.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Protein Aliases: DKFZp564C1216; DKFZp686J24237; E2 ubiquitin-conjugating enzyme K; E2(25K); HIP-2; huntingtin interacting protein 2; Huntingtin-interacting protein 2; Ubiquitin carrier protein; ubiquitin conjugating enzyme E2K; Ubiquitin-conjugating enzyme E2 K; Ubiquitin-conjugating enzyme E2(25K); Ubiquitin-conjugating enzyme E2-25 kDa; ubiquitin-conjugating enzyme E2-25K; ubiquitin-conjugating enzyme E2K (UBC1 homolog, yeast); Ubiquitin-protein ligase
Gene Aliases: AW492011; D5Ertd601e; E2-25K; HIP2; HYPG; LIG; UBC1; UBE2K