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
CENPU
Gene Ontology Biological Process
Gene Ontology Cellular Component
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.
Publication
Structural and functional analyses of minimal phosphopeptides targeting the polo-box domain of polo-like kinase 1.
Polo-like kinase-1 (Plk1) has a pivotal role in cell proliferation and is considered a potential target for anticancer therapy. The noncatalytic polo-box domain (PBD) of Plk1 forms a phosphoepitope binding module for protein-protein interaction. Here, we report the identification of minimal phosphopeptides that specifically interact with the PBD of human PLK1, but not those of the closely related PLK2 and ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| PLK1 CENPU | 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 | 136 | BioGRID | 3482771 | |
| CENPU PLK1 | 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 | 0.9808 | BioGRID | 2244777 | |
| CENPU PLK1 | 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 | 0.9603 | BioGRID | 3087856 | |
| PLK1 CENPU | 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 | - | |
| CENPU 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 | - | |
| PLK1 CENPU | Protein-peptide Protein-peptide An interaction is detected between a protein and a peptide derived from an interaction partner. This includes phage display experiments. | Low | - | BioGRID | - | |
| CENPU PLK1 | 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 | - | |
| CENPU PLK1 | 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