BAIT

UBE2F

NCE2
ubiquitin-conjugating enzyme E2F (putative)
GO Process (2)
GO Function (4)
GO Component (1)
Homo sapiens
PREY

DCUN1D2

C13orf17, RP11-102K13.4
DCN1, defective in cullin neddylation 1, domain containing 2
GO Process (0)
GO Function (0)
GO Component (0)
Homo sapiens

Reconstituted Complex

An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator.

Publication

Structural Conservation of Distinctive N-terminal Acetylation-Dependent Interactions across a Family of Mammalian NEDD8 Ligation Enzymes.

Monda JK, Scott DC, Miller DJ, Lydeard J, King D, Harper JW, Bennett EJ, Schulman BA

Little is known about molecular recognition of acetylated N termini, despite prevalence of this modification among eukaryotic cytosolic proteins. We report that the family of human DCN-like (DCNL) co-E3s, which promote ligation of the ubiquitin-like protein NEDD8 to cullin targets, recognizes acetylated N termini of the E2 enzymes UBC12 and UBE2F. Systematic biochemical and biophysical analyses reveal 40- and 10-fold ... [more]

Structure Jan. 08, 2013; 21(1);42-53 [Pubmed: 23201271]

Throughput

  • Low Throughput

Additional Notes

  • isothermal titration calorimetry
  • only N-terminally acetylated UBE2F

Curated By

  • BioGRID