BAIT

WDR48

P80, SPG60, UAF1
WD repeat domain 48
GO Process (1)
GO Function (1)
GO Component (2)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Homo sapiens
PREY

UBC

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

Gene Ontology Biological Process

Gene Ontology Molecular Function

Homo sapiens

Biochemical Activity (Deubiquitination)

An interaction is inferred from the biochemical effect of one protein upon another, for example, GTP-GDP exchange activity or phosphorylation of a substrate by a kinase. The bait protein executes the activity on the substrate hit protein. A Modification value is recorded for interactions of this type with the possible values Phosphorylation, Ubiquitination, Sumoylation, Dephosphorylation, Methylation, Prenylation, Acetylation, Deubiquitination, Proteolytic Processing, Glucosylation, Nedd(Rub1)ylation, Deacetylation, No Modification, Demethylation.

Publication

USP1 Is Required for Replication Fork Protection in BRCA1-Deficient Tumors.

Lim KS, Li H, Roberts EA, Gaudiano EF, Clairmont C, Sambel LA, Ponnienselvan K, Liu JC, Yang C, Kozono D, Parmar K, Yusufzai T, Zheng N, D'Andrea AD

BRCA1-deficient tumor cells have defects in homologous-recombination repair and replication fork stability, resulting in PARP inhibitor sensitivity. Here, we demonstrate that a deubiquitinase, USP1, is upregulated in tumors with mutations in BRCA1. Knockdown or inhibition of USP1 resulted in replication fork destabilization and decreased viability of BRCA1-deficient cells, revealing a synthetic lethal relationship. USP1 binds to and is stimulated by ... [more]

Mol. Cell Dec. 20, 2017; 72(6);925-941.e4 [Pubmed: 30576655]

Throughput

  • Low Throughput

Additional Notes

  • in vitro deubiquitination with USP1 and UAF1 as deubiquitinase and an artificial ubiquitin-reporter-enzyme fusion (Ub-Chop2) as substrate

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
WDR48 UBC
Co-crystal Structure
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.

Low-BioGRID
1505508

Curated By

  • BioGRID