DCUN1D4 Human

DCUN1D4 is involved in the positive regulation of protein neddylation. It contributes to the neddylation of all cullins by transferring NEDD8 from N-terminally acetylated NEDD8-conjugating E2 enzymes to different cullin C-terminal domain-RBX complexes. This process is necessary for the activation of cullin-RING E3 ubiquitin ligases (CRLs), which are crucial for protein degradation .

The protein encoded by DCUN1D4 binds to cullin-RBX1 complexes within the cytoplasm, promoting their nuclear translocation. This enhances the recruitment of E2-NEDD8 (UBE2M-NEDD8) thioester to the complex, optimizing the introduction of proteins within the complex so that NEDD8 can be efficiently transferred to the cullin substrates from the E2 .

DCUN1D4 has been associated with various diseases, including hemangioma of the lung and cecum carcinoma . It also acts as an oncogene, facilitating carcinogenic progression and malignant transformation . The gene is part of pathways related to the metabolism of proteins and Class I MHC-mediated antigen processing and presentation .

Recombinant forms of DCUN1D4 are used in research to study its function and role in neddylation. These recombinant proteins are available in various quantities and are shipped with ice packs to maintain their stability .

An important paralog of DCUN1D4 is DCUN1D5, which shares similar functions and mechanisms . The gene encoding DCUN1D2, another related gene, is found on human chromosome 13 and is linked with significant tumor suppressor genes such as BRCA2 and RB1 .