FZR1
Gene Ontology Biological Process
- G2 DNA damage checkpoint [IDA]
- activation of anaphase-promoting complex activity [IDA]
- anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process [IDA, TAS]
- mitotic cell cycle [TAS]
- negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [TAS]
- positive regulation of protein catabolic process [IGI]
- positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [TAS]
- protein K11-linked ubiquitination [TAS]
- regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
NEK2
Gene Ontology Biological Process
- G2/M transition of mitotic cell cycle [TAS]
- centrosome separation [IDA]
- chromosome segregation [IDA]
- mitotic cell cycle [TAS]
- mitotic nuclear division [TAS]
- negative regulation of centriole-centriole cohesion [IMP]
- protein autophosphorylation [IDA, IMP]
- protein phosphorylation [IDA, IMP]
- regulation of attachment of spindle microtubules to kinetochore [IMP]
- regulation of mitosis [TAS]
- regulation of mitotic centrosome separation [TAS]
- spindle assembly [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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.
Publication
Transcriptional intermediary factor 1γ binds to the anaphase-promoting complex/cyclosome and promotes mitosis.
The anaphase-promoting complex/cyclosome (APC/C) is an ubiquitin ligase that functions during mitosis. Here we identify the transcriptional regulator, transcriptional intermediary factor 1γ, TIF1γ, as an APC/C-interacting protein that regulates APC/C function. TIF1γ is not a substrate for APC/C-dependent ubiquitylation but instead, associates specifically with the APC/C holoenzyme and Cdc20 to affect APC/C activity and progression through mitosis. RNA interference studies ... [more]
Throughput
- Low Throughput
Related interactions
Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
---|---|---|---|---|---|---|
NEK2 FZR1 | 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 | 0.8663 | BioGRID | 3550248 | |
NEK2 FZR1 | 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 | 1509018 | |
FZR1 NEK2 | 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 | 1509996 |
Curated By
- BioGRID