CAF20
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
FUS3
Gene Ontology Biological Process
- cell cycle arrest [IMP]
- invasive growth in response to glucose limitation [IMP]
- negative regulation of MAPK cascade [IPI]
- negative regulation of transposition, RNA-mediated [IMP]
- pheromone-dependent signal transduction involved in conjugation with cellular fusion [IDA]
- positive regulation of protein export from nucleus [IMP]
- protein autophosphorylation [IDA]
- protein phosphorylation [IDA]
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
A Mad2-Mediated Translational Regulatory Mechanism Promoting S-Phase Cyclin Synthesis Controls Origin Firing and Survival to Replication Stress.
Cell survival to replication stress depends on the activation of the Mec1ATR-Rad53 checkpoint response that protects the integrity of stalled forks and controls the origin firing program. Here we found that Mad2, a member of the spindle assembly checkpoint (SAC), contributes to efficient origin firing and to cell survival in response to replication stress. We show that Rad53 and Mad2 promote ... [more]
Throughput
- High Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| FUS3 CAF20 | 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. | High | - | BioGRID | 198407 |
Curated By
- BioGRID