FUNCTION: E3 ubiquitin-protein ligase that specifically catalyzes 'Lys-29'- and 'Lys-48'-linked polyubiquitin chains (PubMed:11278995, PubMed:12692129, PubMed:16341092, PubMed:16601690, PubMed:24811749, PubMed:24158444, PubMed:25752573, PubMed:25752577, PubMed:34239127, PubMed:33637724, PubMed:32039...
FUNCTION: E3 ubiquitin-protein ligase that specifically catalyzes 'Lys-29'- and 'Lys-48'-linked polyubiquitin chains (PubMed:11278995, PubMed:12692129, PubMed:16341092, PubMed:16601690, PubMed:24811749, PubMed:24158444, PubMed:25752573, PubMed:25752577, PubMed:34239127, PubMed:33637724, PubMed:32039437). 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:9575161, PubMed:32039437). 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). {ECO:0000269|PubMed:11278995, ECO:0000269|PubMed:12692129, ECO:0000269|PubMed:16341092, ECO:0000269|PubMed:16601690, ECO:0000269|PubMed:21167755, ECO:0000269|PubMed:24158444, ECO:0000269|PubMed:24811749, ECO:0000269|PubMed:25752573, ECO:0000269|PubMed:25752577, ECO:0000269|PubMed:28396413, ECO:0000269|PubMed:31375563, ECO:0000269|PubMed:32039437, ECO:0000269|PubMed:33637724, ECO:0000269|PubMed:34239127, ECO:0000269|PubMed:9575161}.
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GO - Biological processes (BP):
protein K29-linked ubiquitination [GO:0035519]; protein K48-linked ubiquitination [GO:0070936]; protein polyubiquitination [GO:0000209]; ubiquitin-dependent protein catabolic process [GO:0006511]...
protein K29-linked ubiquitination [GO:0035519]; protein K48-linked ubiquitination [GO:0070936]; protein polyubiquitination [GO:0000209]; ubiquitin-dependent protein catabolic process [GO:0006511]
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GO - Molecular function (MF):
ubiquitin protein ligase activity [GO:0061630]...
ubiquitin protein ligase activity [GO:0061630]
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GO - Cellular component (CC):
nucleus [GO:0005634]; proteasome complex [GO:0000502]...
nucleus [GO:0005634]; proteasome complex [GO:0000502]
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