DCAF12
Gene Ontology Biological Process
Gene Ontology Cellular Component
CCT5
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Proximity Label-MS
An interaction is inferred when a bait-enzyme fusion protein selectively modifies a vicinal protein with a diffusible reactive product, followed by affinity capture of the modified protein and identification by mass spectrometric methods.
Publication
Pulse-SILAC and interactomics reveal distinct DDB1-CUL4 associated factors (DCAFs), cellular functions, and protein substrates.
Cullin-RING finger ligases (CRLs) represent the largest family of ubiquitin ligases. They are responsible for the ubiquitination of ?20% of cellular proteins degraded through the proteasome, by catalyzing the transfer of E2-loaded ubiquitin to a substrate. Seven Cullins are described in vertebrates. Among them, CUL4 associates with DDB1 to form the CUL4-DDB1 ubiquitin ligase complex, which is involved in protein ... [more]
Throughput
- High Throughput
Additional Notes
- BioID
Related interactions
Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
---|---|---|---|---|---|---|
CCT5 DCAF12 | 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. | High | 0.9999 | BioGRID | 3083931 | |
DCAF12 CCT5 | Biochemical Activity Biochemical Activity 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. | Low | - | BioGRID | 3588416 |
Curated By
- BioGRID