BAIT
BRD4
CAP, HUNK1, HUNKI, MCAP
bromodomain containing 4
GO Process (10)
GO Function (4)
GO Component (5)
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
Homo sapiens
PREY
TRIM4
RNF87
tripartite motif containing 4
GO Process (1)
GO Function (0)
GO Component (2)
Gene Ontology Biological Process
Gene Ontology Cellular Component
Homo sapiens
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]
Mol Cell Dec. 01, 2020; 81(7);1411-1424.e7 [Pubmed: 33567268]
Throughput
- Low Throughput
Curated By
- BioGRID