BAIT

UBC

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

Gene Ontology Biological Process

Gene Ontology Molecular Function

Homo sapiens
PREY

NOD1

CARD4, CLR7.1, NLRC1
nucleotide-binding oligomerization domain containing 1
GO Process (33)
GO Function (6)
GO Component (3)

Gene Ontology Biological Process

Gene Ontology Cellular Component

Homo sapiens

Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Publication

Ubiquitin regulates CAspase Recruitment Domain mediated signaling by nucleotide binding oligomerization domain proteins NOD1 and NOD2.

Ver Heul AM, Fowler A, Ramaswamy S, Piper RC

NOD1 and NOD2 (Nucleotide-binding oligomerization domain-containing proteins) are intracellular pattern-recognition receptors that activate NF-κB and autophagy. These pathways rely on the CAspase Recruitment Domains (CARD) within the NODs, which serve as a protein interaction platforms that coordinately regulates immune signaling. We show that NOD1 CARD binds ubiquitin, in addition to directly binding its downstream targets RIP2 kinase and ATG16L. NMR ... [more]

J. Biol. Chem. Jan. 08, 2013; 0(0); [Pubmed: 23300079]

Throughput

  • Low Throughput

Additional Notes

  • #LPPI
  • Figure 1
  • Likely protein-protein interaction

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
NOD1 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
1101090

Curated By

  • BioGRID