BAIT
TCP1
CCT1, chaperonin-containing T-complex alpha subunit TCP1, L000002267, YDR212W
Alpha subunit of chaperonin-containing T-complex; complex mediates protein folding in the cytosol; involved in actin cytoskeleton maintenance; overexpression in neurons suppresses formation of pathogenic conformations of huntingtin protein
GO Process (1)
GO Function (1)
GO Component (2)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Saccharomyces cerevisiae (S288c)
PREY
SCS7
FAH1, fatty acid alpha-hydroxylase, L000004408, YMR272C
Sphingolipid alpha-hydroxylase; functions in the alpha-hydroxylation of sphingolipid-associated very long chain fatty acids, has both cytochrome b5-like and hydroxylase/desaturase domains, not essential for growth
GO Process (1)
GO Function (1)
GO Component (3)
Gene Ontology Biological Process
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
The interaction network of the chaperonin CCT.
The eukaryotic cytosolic chaperonin containing TCP-1 (CCT) has an important function in maintaining cellular homoeostasis by assisting the folding of many proteins, including the cytoskeletal components actin and tubulin. Yet the nature of the proteins and cellular pathways dependent on CCT function has not been established globally. Here, we use proteomic and genomic approaches to define CCT interaction networks involving ... [more]
EMBO J. Jul. 09, 2008; 27(13);1827-39 [Pubmed: 18511909]
Throughput
- High Throughput
Ontology Terms
- phenotype: inviable (APO:0000112)
Additional Notes
- High Throughput: A temperature sensitive cct1-2 mutant was used as the query in an SGA analysis.
Curated By
- BioGRID