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
TCEB1
Gene Ontology Biological Process
- cellular response to hypoxia [TAS]
- gene expression [TAS]
- positive regulation of viral transcription [TAS]
- regulation of transcription from RNA polymerase II promoter [TAS]
- regulation of transcription from RNA polymerase II promoter in response to hypoxia [TAS]
- transcription elongation from RNA polymerase II promoter [TAS]
- transcription from RNA polymerase II promoter [TAS]
- viral process [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
- cytosol [TAS]
- nucleoplasm [TAS]
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.
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 TCEB1 | 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 TCEB1 | Reconstituted Complex Reconstituted Complex An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator. | Low | - | BioGRID | - |
Curated By
- BioGRID