InterPro domain: IPR014764

The eukaryotic defective in cullin neddylation (DCN) protein family, contributes to neddylation of cullin components of SCF-type E3 ubiquitin ligase complexes. These multi-protein complexes are required for polyubiquitination and subsequent degradation of target proteins by the 26S proteasome [ 1 , 2 , 3 ]. Proteins in the DCN family include:

• Yeast DCN1.
• Vertebrate DCN1-like protein 1-5.
• Plant Defective in cullin neddylation protein AAR3 [ 4 ].

DCN family proteins all contain a Potentiating neddylation (PONY) domain ( IPR005176 ), contains a cullin-binding surface within its C-terminal region and is sufficient to promote neddylation [ 5 , 6 ]. The N-terminal region of the protein often contains a UBA-like domain.

1. The conserved protein DCN-1/Dcn1p is required for cullin neddylation in C. elegans and S. cerevisiae. Nature 435, 1257-61
2. Structural Conservation of Distinctive N-terminal Acetylation-Dependent Interactions across a Family of Mammalian NEDD8 Ligation Enzymes. Structure 21, 42-53
3. Characterization of the mammalian family of DCN-type NEDD8 E3 ligases. J Cell Sci 129, 1441-54
4. Genetic characterization of mutants resistant to the antiauxin p-chlorophenoxyisobutyric acid reveals that AAR3, a gene encoding a DCN1-like protein, regulates responses to the synthetic auxin 2,4-dichlorophenoxyacetic acid in Arabidopsis roots. Plant Physiol 145, 773-85
5. Dcn1 functions as a scaffold-type E3 ligase for cullin neddylation. Mol. Cell 29, 23-35