BRD4
Gene Ontology Biological Process
- cellular response to DNA damage stimulus [IMP]
- chromatin remodeling [IDA]
- negative regulation of DNA damage checkpoint [IMP]
- positive regulation of G2/M transition of mitotic cell cycle [IMP]
- positive regulation of I-kappaB kinase/NF-kappaB signaling [IDA]
- positive regulation of transcription elongation from RNA polymerase II promoter [IDA, IMP]
- positive regulation of transcription from RNA polymerase II promoter [IDA]
- regulation of inflammatory response [IDA]
- regulation of phosphorylation of RNA polymerase II C-terminal domain [IDA]
- regulation of transcription involved in G1/S transition of mitotic cell cycle [IMP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
BRD4
Gene Ontology Biological Process
- cellular response to DNA damage stimulus [IMP]
- chromatin remodeling [IDA]
- negative regulation of DNA damage checkpoint [IMP]
- positive regulation of G2/M transition of mitotic cell cycle [IMP]
- positive regulation of I-kappaB kinase/NF-kappaB signaling [IDA]
- positive regulation of transcription elongation from RNA polymerase II promoter [IDA, IMP]
- positive regulation of transcription from RNA polymerase II promoter [IDA]
- regulation of inflammatory response [IDA]
- regulation of phosphorylation of RNA polymerase II C-terminal domain [IDA]
- regulation of transcription involved in G1/S transition of mitotic cell cycle [IMP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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.
Publication
TRIP12 promotes small-molecule-induced degradation through K29/K48-branched ubiquitin chains.
Targeted protein degradation is an emerging therapeutic paradigm. Small-molecule degraders such as proteolysis-targeting chimeras (PROTACs) induce the degradation of neo-substrates by hijacking E3 ubiquitin ligases. Although ubiquitylation of endogenous substrates has been extensively studied, the mechanism underlying forced degradation of neo-substrates is less well understood. We found that the ubiquitin ligase TRIP12 promotes PROTAC-induced and CRL2VHL-mediated degradation of BRD4 but ... [more]
Throughput
- Low Throughput
Related interactions
Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
---|---|---|---|---|---|---|
BRD4 BRD4 | 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. | Low | - | BioGRID | - | |
BRD4 BRD4 | 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 | - | BioGRID | - | |
BRD4 BRD4 | Negative Genetic Negative Genetic Mutations/deletions in separate genes, each of which alone causes a minimal phenotype, but when combined in the same cell results in a more severe fitness defect or lethality under a given condition. This term is reserved for high or low throughput studies with scores. | High | - | BioGRID | 2463330 | |
BRD4 BRD4 | Proximity Label-MS 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. | High | - | BioGRID | 3458247 |
Curated By
- BioGRID