AURKB
Gene Ontology Biological Process
- abscission [ISS]
- anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process [TAS]
- attachment of spindle microtubules to kinetochore [TAS]
- cellular response to UV [IDA]
- cleavage furrow formation [IDA]
- cytokinesis checkpoint [ISS]
- histone H3-S28 phosphorylation [ISS]
- histone modification [TAS]
- mitotic cell cycle [TAS]
- mitotic spindle midzone assembly [IMP, TAS]
- negative regulation of B cell apoptotic process [IDA]
- negative regulation of cytokinesis [ISS]
- negative regulation of protein binding [IDA]
- negative regulation of transcription from RNA polymerase II promoter [IDA]
- positive regulation of cytokinesis [IMP, TAS]
- protein autophosphorylation [TAS]
- protein localization to kinetochore [IMP]
- protein phosphorylation [IDA]
- regulation of chromosome segregation [TAS]
- spindle stabilization [IMP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
HIST3H3
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Biochemical Activity (Phosphorylation)
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.
Publication
Tumour suppressor CYLD is a negative regulator of the mitotic kinase Aurora-B.
The familial cylindromatosis tumour suppressor CYLD contains three cytoskeleton-associated protein glycine-rich (CAP-Gly) domains and a deubiquitinase domain. The tumour-suppressing function of CYLD has been attributed to its deubiquitinase domain, which removes lysine-63-linked polyubiquitin chains from target proteins, leading to the inhibition of cell survival and proliferation. In this study, we have detected an interaction of CYLD with the mitotic kinase ... [more]
Throughput
- Low Throughput
Additional Notes
- kinase activity inhibited in the presence of cyld
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| AURKB HIST3H3 | 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 | 610745 | |
| AURKB HIST3H3 | 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 | 608934 |
Curated By
- BioGRID