BAIT
SEC18
ANU4, AAA family ATPase SEC18, L000001842, YBR080C
AAA ATPase and SNARE disassembly chaperone; required for vesicular transport between ER and Golgi, the 'priming' step in homotypic vacuole fusion, autophagy, and protein secretion; releases Sec17p from SNAP complexes; has similarity to mammalian N-ethylmaleimide-sensitive factor (NSF)
GO Process (7)
GO Function (1)
GO Component (2)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Saccharomyces cerevisiae (S288c)
PREY
SSO1
L000002089, YPL232W
Plasma membrane t-SNARE; involved in fusion of secretory vesicles at the plasma membrane and in vesicle fusion during sporulation; forms a complex with Sec9p that binds v-SNARE Snc2p; syntaxin homolog; functionally redundant with Sso2p; SSO1 has a paralog, SSO2, that arose from the whole genome duplication
GO Process (3)
GO Function (5)
GO Component (4)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Saccharomyces cerevisiae (S288c)
Dosage Lethality
A genetic interaction is inferred when over expression or increased dosage of one gene causes lethality in a strain that is mutated or deleted for another gene.
Publication
Conformational regulation of SNARE assembly and disassembly in vivo.
SNAP receptor (SNARE) proteins function in intracellular trafficking by forming complexes that bridge vesicle and target membranes prior to fusion. Biochemical studies indicate that the entry of certain SNARE proteins into complexes is inhibited by intramolecular interactions that generate a closed conformation. For example, an essential N-terminal regulatory domain of the yeast plasma membrane SNARE Sso1p sequesters the C-terminal SNARE ... [more]
J. Biol. Chem. Mar. 15, 2002; 277(11);9375-81 [Pubmed: 11777922]
Throughput
- Low Throughput
Ontology Terms
- phenotype: inviable (APO:0000112)
Curated By
- BioGRID