PREY

UBC

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

Gene Ontology Biological Process

Gene Ontology Molecular Function

Homo sapiens

Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Publication

Structural and biochemical studies of RIG-I antiviral signaling.

Feng M, Ding Z, Xu L, Kong L, Wang W, Jiao S, Shi Z, Greene MI, Cong Y, Zhou Z

Retinoic acid-inducible gene I (RIG-I) is an important pattern recognition receptor that detects viral RNA and triggers the production of type-I interferons through the downstream adaptor MAVS (also called IPS-1, CARDIF, or VISA). A series of structural studies have elaborated some of the mechanisms of dsRNA recognition and activation of RIG-I. Recent studies have proposed that K63-linked ubiquitination of, or ... [more]

Protein Cell Dec. 20, 2012; 0(0); [Pubmed: 23264040]

Throughput

  • Low Throughput

Additional Notes

  • #LPPI
  • Likely protein-protein interaction

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
DDX58 UBC
Affinity Capture-Western
Affinity Capture-Western

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 identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins.

Low-BioGRID
3626607
DDX58 UBC
Reconstituted Complex
Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Low-BioGRID
3626608
DDX58 UBC
Reconstituted Complex
Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Low-BioGRID
1067342

Curated By

  • BioGRID