PREY

UBC

HMG20
ubiquitin C
GO Process (75)
GO Function (3)
GO Component (6)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Homo sapiens

Co-crystal Structure

Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.

Publication

Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis.

Plechanovova A, Jaffray EG, Tatham MH, Naismith JH, Hay RT

Ubiquitin modification is mediated by a large family of specificity determining ubiquitin E3 ligases. To facilitate ubiquitin transfer, RING E3 ligases bind both substrate and a ubiquitin E2 conjugating enzyme linked to ubiquitin via a thioester bond, but the mechanism of transfer has remained elusive. Here we report the crystal structure of the dimeric RING domain of rat RNF4 in ... [more]

Unknown Jul. 29, 2012; 0(0); [Pubmed: 22842904]

Throughput

  • Low Throughput

Additional Notes

  • #LPPI
  • Crystal structure of rat E3 ubiquitin-protein ligase RNF4 with human UBE2D1 and UBC ubiquitin.
  • Likely protein-protein interaction

Curated By

  • BioGRID