FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination (PubMed:22496338). Cooperates with the E2 UBCH5C and the SCF(FBXW11) E3 ligase complex for the polyubiquitination of NFKBIA leading to its su...
FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination (PubMed:22496338). Cooperates with the E2 UBCH5C and the SCF(FBXW11) E3 ligase complex for the polyubiquitination of NFKBIA leading to its subsequent proteasomal degradation. Performs ubiquitin chain elongation building ubiquitin chains from the UBE2D3-primed NFKBIA-linked ubiquitin. UBE2D3 acts as an initiator E2, priming the phosphorylated NFKBIA target at positions 'Lys-21' and/or 'Lys-22' with a monoubiquitin. Cooperates with the SCF(SKP2) E3 ligase complex to regulate cell proliferation through ubiquitination and degradation of MYBL2 and KIP1. Involved in ubiquitin conjugation and degradation of CREM isoform ICERIIgamma and ATF15 resulting in abrogation of ICERIIgamma- and ATF5-mediated repression of cAMP-induced transcription during both meiotic and mitotic cell cycles. Involved in the regulation of the cell cycle G2/M phase through its targeting of the WEE1 kinase for ubiquitination and degradation. Also involved in the degradation of beta-catenin. Is target of human herpes virus 1 protein ICP0, leading to ICP0-dependent dynamic interaction with proteasomes (PubMed:10329681, PubMed:10373550, PubMed:10871850, PubMed:11675391, PubMed:12037680, PubMed:15652359, PubMed:17461777, PubMed:17698585, PubMed:19112177, PubMed:19126550, PubMed:19945379, PubMed:20061386, PubMed:20347421). {ECO:0000269|PubMed:10329681, ECO:0000269|PubMed:10373550, ECO:0000269|PubMed:10871850, ECO:0000269|PubMed:11675391, ECO:0000269|PubMed:12037680, ECO:0000269|PubMed:15652359, ECO:0000269|PubMed:17461777, ECO:0000269|PubMed:17698585, ECO:0000269|PubMed:19112177, ECO:0000269|PubMed:19126550, ECO:0000269|PubMed:19945379, ECO:0000269|PubMed:20061386, ECO:0000269|PubMed:20347421, ECO:0000269|PubMed:22496338}.
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GO - Biological processes (BP):
cellular protein modification process [GO:0006464]; cellular response to interferon-beta [GO:0035458]; DNA replication initiation [GO:0006270]; G1/S transition of mitotic cell cycle [GO:0000082]; negative regulation of cAMP-mediated signaling [GO:0043951]; positive regulation of inclusion body assem...
cellular protein modification process [GO:0006464]; cellular response to interferon-beta [GO:0035458]; DNA replication initiation [GO:0006270]; G1/S transition of mitotic cell cycle [GO:0000082]; negative regulation of cAMP-mediated signaling [GO:0043951]; positive regulation of inclusion body assembly [GO:0090261]; positive regulation of neuron apoptotic process [GO:0043525]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein K48-linked ubiquitination [GO:0070936]; protein polyubiquitination [GO:0000209]; protein ubiquitination [GO:0016567]; response to growth factor [GO:0070848]; ubiquitin-dependent protein catabolic process [GO:0006511]
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GO - Molecular function (MF):
ATP binding [GO:0005524]; ubiquitin conjugating enzyme activity [GO:0061631]; ubiquitin-protein transferase activity [GO:0004842]...
ATP binding [GO:0005524]; ubiquitin conjugating enzyme activity [GO:0061631]; ubiquitin-protein transferase activity [GO:0004842]
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GO - Cellular component (CC):
cytosol [GO:0005829]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]...
cytosol [GO:0005829]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
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