DCUN1D1

Intracellular

Cell type enriched (Late spermatids)

Low immune cell specificity

Low cell line specificity

Part of an E3 complex for neddylation composed of cullins, RBX1, UBE2M and CAND1 (PubMed:18826954). Interacts (via the DCUN1 domain) with the unneddylated cullins: interacts with CUL1, CUL2, CUL3, CUL4A, CUL4B and CUL5; these interactions promote the cullin neddylation and the identity of the cullin dictates the affinity of the interaction (PubMed:26906416, PubMed:18826954, PubMed:23201271, PubMed:19617556, PubMed:23401859, PubMed:30587576). Binds neddylated CUL1. Interacts (via the C-terminus 50 AA) directly with RBX1 (PubMed:18826954, PubMed:26906416). Interacts (via DCUN1 domain) with the N-terminally acetylated form of UBE2M and UBE2F (PubMed:28581483, PubMed:23201271, PubMed:19617556). Interacts preferentially with UBE2M-NEDD8 thioester (via N-terminus 1-26 AA) than with free UBE2M (PubMed:18826954, PubMed:25349211). UBE2M N-terminal acetylation increases the affinity of this interaction by about 2 orders of magnitude (PubMed:21940857). Interacts with CAND1; this interaction is indirect and is bridged by cullins such as CUL1 and CUL3 (PubMed:18826954, PubMed:26906416). May also interact with regulators or subunits of cullin-RING ligases such as RNF7, ELOB and DDB1; these interactions are bridged by cullins (PubMed:26906416). Component of VCB complex that contains at least DCUN1D1, CUL2 and VHL; this complex triggers CUL2 neddylation and consequently cullin ring ligase (CRL) substrates polyubiquitylation (PubMed:23401859). Interacts with VHL; this interaction triggers engagement of HIF1A in the VCB complex and is independent of CUL2 (PubMed:23401859). Interacts with CUL2 independently of VHL (PubMed:23401859). Interacts with SOCS1 and SOCS2 (PubMed:23401859). Interacts with HIF1A; this interaction increases the interaction between VHL and DCUN1D1 (PubMed:23401859). Interacts (via UBA-like domain) with ARIH2; promotes DCUN1D1 ubiquitination (PubMed:30587576).