PARP1
Gene Ontology Biological Process
- DNA repair [TAS]
- cellular response to insulin stimulus [IDA]
- double-strand break repair [IMP]
- gene expression [TAS]
- macrophage differentiation [TAS]
- negative regulation of transcription from RNA polymerase II promoter [TAS]
- protein ADP-ribosylation [IDA]
- protein poly-ADP-ribosylation [IDA]
- transcription from RNA polymerase II promoter [TAS]
- transcription initiation from RNA polymerase II promoter [TAS]
- transcription, DNA-templated [TAS]
- transforming growth factor beta receptor signaling pathway [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
RB1
Gene Ontology Biological Process
- G1/S transition of mitotic cell cycle [TAS]
- Ras protein signal transduction [IEP]
- androgen receptor signaling pathway [NAS]
- cell cycle arrest [TAS]
- cell cycle checkpoint [TAS]
- chromatin remodeling [TAS]
- maintenance of mitotic sister chromatid cohesion [IMP]
- mitotic cell cycle [TAS]
- mitotic cell cycle checkpoint [TAS]
- myoblast differentiation [IMP]
- negative regulation of G1/S transition of mitotic cell cycle [TAS]
- negative regulation of protein kinase activity [IPI]
- negative regulation of sequence-specific DNA binding transcription factor activity [TAS]
- negative regulation of transcription from RNA polymerase II promoter during mitosis [TAS]
- negative regulation of transcription, DNA-templated [IDA, TAS]
- positive regulation of mitotic metaphase/anaphase transition [IMP]
- positive regulation of transcription, DNA-templated [NAS]
- protein localization to chromosome, centromeric region [IMP]
- regulation of centromere complex assembly [TAS]
- regulation of cohesin localization to chromatin [IMP]
- regulation of lipid kinase activity [IDA]
- regulation of mitotic cell cycle [IMP]
- regulation of transcription involved in G1/S transition of mitotic cell cycle [TAS]
- sister chromatid biorientation [IMP]
Gene Ontology Molecular Function- DNA binding [TAS]
- androgen receptor binding [NAS]
- core promoter binding [IDA]
- identical protein binding [IPI]
- kinase binding [IDA]
- phosphoprotein binding [IPI]
- protein binding [IPI]
- sequence-specific DNA binding transcription factor activity [TAS]
- transcription coactivator activity [NAS]
- transcription factor binding [IPI]
- ubiquitin protein ligase binding [IPI]
- DNA binding [TAS]
- androgen receptor binding [NAS]
- core promoter binding [IDA]
- identical protein binding [IPI]
- kinase binding [IDA]
- phosphoprotein binding [IPI]
- protein binding [IPI]
- sequence-specific DNA binding transcription factor activity [TAS]
- transcription coactivator activity [NAS]
- transcription factor binding [IPI]
- ubiquitin protein ligase binding [IPI]
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 ubiquitin-dependent ATPase p97 removes cytotoxic trapped PARP1 from chromatin.
Poly (ADP-ribose) polymerase (PARP) inhibitors elicit antitumour activity in homologous recombination-defective cancers by trapping PARP1 in a chromatin-bound state. How cells process trapped PARP1 remains unclear. Using wild-type and a trapping-deficient PARP1 mutant combined with rapid immunoprecipitation mass spectrometry of endogenous proteins and Apex2 proximity labelling, we delineated mass spectrometry-based interactomes of trapped and non-trapped PARP1. These analyses identified an ... [more]
Throughput
- High Throughput
Additional Notes
- Affinity Capture-MS was carried out to identify high confidence protein-protein interactors.
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| PARP1 RB1 | 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 | 20.19 | BioGRID | 2998657 |
Curated By
- BioGRID