TP53BP1
Gene Ontology Biological Process
- DNA repair [TAS]
- cellular response to DNA damage stimulus [IDA]
- double-strand break repair [TAS]
- double-strand break repair via homologous recombination [TAS]
- positive regulation of sequence-specific DNA binding transcription factor activity [IC]
- positive regulation of transcription from RNA polymerase II promoter [IMP]
- positive regulation of transcription, DNA-templated [NAS]
- transcription from RNA polymerase II promoter [IMP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
HIST2H4A
Gene Ontology Biological Process
- CENP-A containing nucleosome assembly [TAS]
- DNA replication-dependent nucleosome assembly [IDA]
- DNA replication-independent nucleosome assembly [IDA]
- chromatin organization [TAS]
- histone H4-K20 demethylation [TAS]
- mitotic cell cycle [TAS]
- negative regulation of megakaryocyte differentiation [IDA]
- nucleosome assembly [TAS]
- telomere maintenance [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Protein-peptide
An interaction is detected between a protein and a peptide derived from an interaction partner. This includes phage display experiments.
Publication
Acetylation limits 53BP1 association with damaged chromatin to promote homologous recombination.
The pathogenic sequelae of BRCA1 mutation in human and mouse cells are mitigated by concomitant deletion of 53BP1, which binds histone H4 dimethylated at Lys20 (H4K20me2) to promote nonhomologous end joining, suggesting that a balance between BRCA1 and 53BP1 regulates DNA double strand-break (DSB) repair mechanism choice. Here we document that acetylation is a key determinant of this balance. TIP60 ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| TP53BP1 HIST2H4A | Co-crystal Structure Co-crystal Structure Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex. | Low | - | BioGRID | 948148 |
Curated By
- BioGRID