BAIT
HSP82
HSP90, Hsp90 family chaperone HSP82, L000000822, YPL240C
Hsp90 chaperone; redundant in function with Hsc82p; required for pheromone signaling, negative regulation of Hsf1p; docks with Tom70p for mitochondrial preprotein delivery; promotes telomerase DNA binding, nucleotide addition; protein abundance increases in response to DNA replication stress; contains two acid-rich unstructured regions that promote solubility of chaperone-substrate complexes; HSP82 has a paralog, HSC82, that arose from the whole genome duplication
GO Process (7)
GO Function (2)
GO Component (1)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Saccharomyces cerevisiae (S288c)
PREY
NUP53
FG-nucleoporin NUP53, YMR153W
FG-nucleoporin component of central core of nuclear pore complex (NPC); also part of the NPC nuclear basket; contributes directly to nucleocytoplasmic transport; involved in regulation of transcription and mitosis; induces membrane tubulation, which may contribute to nuclear pore assembly; NUP53 has a paralog, ASM4, that arose from the whole genome duplication
GO Process (8)
GO Function (3)
GO Component (4)
Gene Ontology Biological Process
- NLS-bearing protein import into nucleus [IGI, IMP]
- nuclear pore organization [IGI]
- positive regulation of transcription, DNA-templated [IDA, IGI]
- protein import into nucleus [IGI]
- protein localization to kinetochore [IMP]
- regulation of mitosis [IMP, IPI]
- regulation of protein desumoylation [IMP, IPI]
- response to spindle checkpoint signaling [IMP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Saccharomyces cerevisiae (S288c)
Synthetic Lethality
A genetic interaction is inferred when mutations or deletions in separate genes, each of which alone causes a minimal phenotype, result in lethality when combined in the same cell under a given condition.
Publication
Navigating the chaperone network: an integrative map of physical and genetic interactions mediated by the hsp90 chaperone.
Physical, genetic, and chemical-genetic interactions centered on the conserved chaperone Hsp90 were mapped at high resolution in yeast using systematic proteomic and genomic methods. Physical interactions were identified using genome-wide two hybrid screens combined with large-scale affinity purification of Hsp90-containing protein complexes. Genetic interactions were uncovered using synthetic genetic array technology and by a microarray-based chemical-genetic screen of a set ... [more]
Cell Mar. 11, 2005; 120(5);715-27 [Pubmed: 15766533]
Throughput
- High Throughput
Ontology Terms
- phenotype: inviable (APO:0000112)
Curated By
- BioGRID