BAIT
FUS3
DAC2, mitogen-activated serine/threonine-protein kinase FUS3, L000000655, YBL016W
Mitogen-activated serine/threonine protein kinase involved in mating; phosphoactivated by Ste7p; substrates include Ste12p, Far1p, Bni1p, Sst2p; inhibits invasive growth during mating by phosphorylating Tec1p, promoting its; inhibits recruitment of Ste5p, Cdc42p-mediated asymmetry and mating morphogenesis
GO Process (8)
GO Function (2)
GO Component (4)
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
Saccharomyces cerevisiae (S288c)
PREY
FKS1
CND1, CWH53, ETG1, GSC1, PBR1, 1,3-beta-D-glucan synthase, L000000445, L000000732, YLR342W
Catalytic subunit of 1,3-beta-D-glucan synthase; functionally redundant with alternate catalytic subunit Gsc2p; binds to regulatory subunit Rho1p; involved in cell wall synthesis and maintenance; localizes to sites of cell wall remodeling; FKS1 has a paralog, GSC2, that arose from the whole genome duplication
GO Process (3)
GO Function (1)
GO Component (7)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Saccharomyces cerevisiae (S288c)
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]
Science May. 21, 2010; 328(5981);1043-6 [Pubmed: 20489023]
Quantitative Score
- 1.0 [Saint Score]
Throughput
- High Throughput
Curated By
- BioGRID