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
MED17
Gene Ontology Biological Process
- androgen receptor signaling pathway [IDA]
- gene expression [TAS]
- intracellular steroid hormone receptor signaling pathway [IDA]
- positive regulation of transcription from RNA polymerase II promoter [IDA]
- positive regulation of transcription, DNA-templated [IDA]
- regulation of transcription from RNA polymerase II promoter [IDA]
- transcription initiation from RNA polymerase II promoter [IDA, TAS]
Gene Ontology Molecular Function
- RNA polymerase II transcription cofactor activity [IDA]
- ligand-dependent nuclear receptor transcription coactivator activity [NAS]
- protein binding [IPI]
- receptor activity [IDA]
- thyroid hormone receptor binding [IDA]
- transcription coactivator activity [IDA]
- transcription cofactor activity [IDA]
- vitamin D receptor binding [NAS]
Gene Ontology Cellular Component
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
The bromodomain protein Brd4 is a positive regulatory component of P-TEFb and stimulates RNA polymerase II-dependent transcription.
Brd4 is a mammalian bromodomain protein that binds to acetylated chromatin. Proteomic analysis revealed that Brd4 interacts with cyclinT1 and Cdk9 that constitutes core positive transcription elongation factor b (P-TEFb). Brd4 interacted with P-TEFb in the living nucleus through its bromodomain. About half of P-TEFb was bound to the inhibitory subunit and functionally inactive. Brd4 interacted with P-TEFb that was ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| BRD4 MED17 | 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 | 3323528 | |
| BRD4 MED17 | 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 | - |
Curated By
- BioGRID