Anti-UBE3C antibody,Abcam,AB101512

Target data E3 ubiquitin-protein ligase that specifically catalyzes 'Lys-29'- and 'Lys-48'-linked polyubiquitin chains (PubMed : 11278995, PubMed : 12692129, PubMed : 16341092, PubMed : 16601690, PubMed : 24158444, PubMed : 24811749, PubMed : 25752573, PubMed : 25752577, PubMed : 32039437, PubMed : 33637724, PubMed : 34239127). Accepts ubiquitin from the E2 ubiquitin-conjugating enzyme UBE2D1 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates (PubMed : 32039437, PubMed : 9575161). Associates with the proteasome and promotes elongation of ubiquitin chains on substrates bound to the 26S proteasome (PubMed : 24158444, PubMed : 28396413, PubMed : 31375563). Also catalyzes 'Lys-29'- and 'Lys-48'-linked ubiquitination of 26S proteasome subunit ADRM1/RPN13 in response to proteotoxic stress, impairing the ability of the proteasome to bind and degrade ubiquitin-conjugated proteins (PubMed : 24811749, PubMed : 31375563). Acts as a negative regulator of autophagy by mediating 'Lys-29'- and 'Lys-48'-linked ubiquitination of PIK3C3/VPS34, promoting its degradation (PubMed : 33637724). Can assemble unanchored poly-ubiquitin chains in either 'Lys-29'- or 'Lys-48'-linked polyubiquitin chains; with some preference for 'Lys-48' linkages (PubMed : 11278995, PubMed : 16601690, PubMed : 25752577). Acts as a negative regulator of type I interferon by mediating 'Lys-48'-linked ubiquitination of IRF3 and IRF7, leading to their degradation by the proteasome (PubMed : 21167755). Catalyzes ubiquitination and degradation of CAND2 (PubMed : 12692129). See full target information UBE3C