PLK1
Gene Ontology Biological Process
- G2 DNA damage checkpoint [IDA]
- G2/M transition of mitotic cell cycle [IDA, TAS]
- activation of mitotic anaphase-promoting complex activity [IDA]
- anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process [TAS]
- cell proliferation [TAS]
- centrosome organization [IMP]
- cytokinesis [IDA, IMP]
- establishment of protein localization [IMP]
- metaphase/anaphase transition of mitotic cell cycle [TAS]
- microtubule bundle formation [IDA]
- mitotic cell cycle [TAS]
- mitotic cytokinesis [IDA]
- mitotic nuclear division [IDA, IMP]
- mitotic nuclear envelope disassembly [TAS]
- mitotic sister chromatid segregation [IMP]
- mitotic spindle assembly checkpoint [IMP]
- negative regulation of apoptotic process [IMP]
- negative regulation of cyclin-dependent protein serine/threonine kinase activity [IMP]
- negative regulation of transcription from RNA polymerase II promoter [IMP]
- peptidyl-serine phosphorylation [IDA]
- positive regulation of peptidyl-threonine phosphorylation [IMP]
- positive regulation of proteasomal ubiquitin-dependent protein catabolic process [IMP]
- positive regulation of proteolysis [IDA]
- positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [TAS]
- positive regulation of ubiquitin-protein transferase activity [IMP]
- protein destabilization [IDA]
- protein localization to chromatin [IDA]
- protein phosphorylation [IDA]
- protein ubiquitination [IDA]
- regulation of cell cycle [TAS]
- regulation of mitotic cell cycle [IMP]
- regulation of mitotic metaphase/anaphase transition [IMP]
- regulation of protein binding [IMP]
- regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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
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
JIP4 is a PLK1 binding protein that regulates p38MAPK activity in G2 phase.
Cell cycle progression from G2 phase into mitosis is regulated by a complex network of mechanisms, all of which finally control the timing of Cyclin B/CDK1 activation. PLK1 regulates a network of events that contribute to regulating G2/M phase progression. Here we have used a proteomics approach to identify proteins that specifically bind to the Polobox domain of PLK1. This ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| PLK1 TP53BP1 | 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 | 612 | BioGRID | 3482764 | |
| PLK1 TP53BP1 | 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 | - | |
| PLK1 TP53BP1 | 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 | - | |
| TP53BP1 PLK1 | Affinity Capture-Western Affinity Capture-Western 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 identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins. | Low | - | BioGRID | 1508625 | |
| PLK1 TP53BP1 | Affinity Capture-Western Affinity Capture-Western 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 identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins. | Low | - | BioGRID | - | |
| TP53BP1 PLK1 | Affinity Capture-Western Affinity Capture-Western 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 identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins. | Low | - | BioGRID | 870542 | |
| PLK1 TP53BP1 | Biochemical Activity Biochemical Activity An interaction is inferred from the biochemical effect of one protein upon another, for example, GTP-GDP exchange activity or phosphorylation of a substrate by a kinase. The bait protein executes the activity on the substrate hit protein. A Modification value is recorded for interactions of this type with the possible values Phosphorylation, Ubiquitination, Sumoylation, Dephosphorylation, Methylation, Prenylation, Acetylation, Deubiquitination, Proteolytic Processing, Glucosylation, Nedd(Rub1)ylation, Deacetylation, No Modification, Demethylation. | Low | - | BioGRID | 1508624 | |
| PLK1 TP53BP1 | Biochemical Activity Biochemical Activity An interaction is inferred from the biochemical effect of one protein upon another, for example, GTP-GDP exchange activity or phosphorylation of a substrate by a kinase. The bait protein executes the activity on the substrate hit protein. A Modification value is recorded for interactions of this type with the possible values Phosphorylation, Ubiquitination, Sumoylation, Dephosphorylation, Methylation, Prenylation, Acetylation, Deubiquitination, Proteolytic Processing, Glucosylation, Nedd(Rub1)ylation, Deacetylation, No Modification, Demethylation. | Low | - | BioGRID | 870541 | |
| PLK1 TP53BP1 | 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