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
ALR1
Gene Ontology Biological Process
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 global protein kinase and phosphatase interaction network in yeast.
The interactions of protein kinases and phosphatases with their regulatory subunits and substrates underpin cellular regulation. We identified a kinase and phosphatase interaction (KPI) network of 1844 interactions in budding yeast by mass spectrometric analysis of protein complexes. The KPI network contained many dense local regions of interactions that suggested new functions. Notably, the cell cycle phosphatase Cdc14 associated with ... [more]
Quantitative Score
- 1.0 [Saint Score]
Throughput
- High Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| FUS3 ALR1 | 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 | 198396 |
Curated By
- BioGRID