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
CTK1
cyclin-dependent serine/threonine protein kinase CTK1, L000000432, YKL139W
Catalytic (alpha) subunit of C-terminal domain kinase I (CTDK-I); phosphorylates both RNA pol II subunit Rpo21p to affect transcription and pre-mRNA 3' end processing, and ribosomal protein Rps2p to increase translational fidelity; required for H3K36 trimethylation but not dimethylation by Set2p; similar to the Drosophila dCDK12 and human CDK12 and probably CDK13
GO Process (7)
GO Function (2)
GO Component (5)
Gene Ontology Biological Process
- mRNA 3'-end processing [IGI, IMP]
- peptidyl-serine phosphorylation [IDA]
- phosphorylation of RNA polymerase II C-terminal domain [IMP]
- positive regulation of DNA-templated transcription, elongation [IDA]
- positive regulation of transcription from RNA polymerase I promoter [IMP]
- positive regulation of translational fidelity [IMP]
- protein phosphorylation [IDA, IMP, ISS]
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