DCN1 cDNA ORF clone, Saccharomyces cerevisiae S288C

The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.
Johnston M, Hillier L, Riles L, Albermann K, Andr? B, Ansorge W, Benes V, Br?ckner M, Delius H, Dubois E, D?sterh?ft A, Entian KD, Floeth M, Goffeau A, Hebling U, Heumann K, Heuss-Neitzel D, Hilbert H, Hilger F, Kleine K, K?tter P, Louis EJ, Messenguy F, Mewes HW, Hoheisel JD
Nature387(6632 Suppl)87-90(1997 May)

Life with 6000 genes.
Goffeau A, Barrell BG, Bussey H, Davis RW, Dujon B, Feldmann H, Galibert F, Hoheisel JD, Jacq C, Johnston M, Louis EJ, Mewes HW, Murakami Y, Philippsen P, Tettelin H, Oliver SG
Science (New York, N.Y.)274(5287)546, 563-7(1996 Oct)

The 1.9 A X-ray crystal structure of Dcn1 has an N-terminal ubiquitin-binding domain & a unique C-terminal domain. It does not require Cys for catalysis. It interacts with the Nedd8 E2 Ubc12 on a surface that overlaps the E1-binding site.
Title: Dcn1 functions as a scaffold-type E3 ligase for cullin neddylation.

DCN-1 is a scaffold protein in a multisubunit neddylation E3 ligase complex
Title: Structural basis for the function of DCN-1 in protein Neddylation.

Both in vivo and in vitro experiments indicate that Dcn1p does not inhibit deneddylation of Cdc53p by the COP9 signalosome, but greatly increases the kinetics of the neddylation reaction
Title: The conserved protein DCN-1/Dcn1p is required for cullin neddylation in C. elegans and S. cerevisiae.