BAIT

UBB

ubiquitin B
GO Process (81)
GO Function (1)
GO Component (9)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Homo sapiens
PREY

RAD18

RNF73
RAD18 E3 ubiquitin protein ligase
GO Process (1)
GO Function (5)
GO Component (2)

Gene Ontology Biological Process

Gene Ontology Cellular Component

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

Mechanisms of Ubiquitin-Nucleosome Recognition and Regulation of 53BP1 Chromatin Recruitment by RNF168/169 and RAD18.

Hu Q, Botuyan MV, Cui G, Zhao D, Mer G

The protein 53BP1 plays a central regulatory role in DNA double-strand break repair. 53BP1 relocates to chromatin by recognizing RNF168-mediated mono-ubiquitylation of histone H2A Lys15 in the nucleosome core particle dimethylated at histone H4 Lys20 (NCP-ubme). 53BP1 relocation is terminated by ubiquitin ligases RNF169 and RAD18 via unknown mechanisms. Using nuclear magnetic resonance (NMR) spectroscopy and biochemistry, we show that ... [more]

Mol. Cell May. 18, 2017; 66(4);473-487.e9 [Pubmed: 28506460]

Throughput

  • Low Throughput

Additional Notes

  • NMR structure

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
RAD18 UBB
Affinity Capture-MS
Affinity Capture-MS

An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods.

High21.9403BioGRID
2945845

Curated By

  • BioGRID