BAIT
RTC3
HGI1, YHR087W
Protein of unknown function involved in RNA metabolism; has structural similarity to SBDS, the human protein mutated in Shwachman-Diamond Syndrome (the yeast SBDS ortholog = SDO1); null mutation suppresses cdc13-1 temperature sensitivity; protein abundance increases in response to DNA replication stress
GO Process (1)
GO Function (0)
GO Component (2)
Saccharomyces cerevisiae (S288c)
PREY
AIR1
S000028413, YIL079C
Zinc knuckle protein; involved in nuclear RNA processing and degradation as a component of the TRAMP complex; stimulates the poly(A) polymerase activity of Pap2p in vitro; AIR1 has a paralog, AIR2, that arose from the whole genome duplication; although Air1p and Air2p are homologous TRAMP subunits, they have nonredundant roles in regulation of substrate specificity of the exosome
GO Process (7)
GO Function (1)
GO Component (2)
Gene Ontology Biological Process
- ncRNA polyadenylation [IDA]
- nuclear mRNA surveillance of mRNA 3'-end processing [IGI]
- nuclear polyadenylation-dependent CUT catabolic process [IGI]
- nuclear polyadenylation-dependent rRNA catabolic process [IGI]
- nuclear polyadenylation-dependent snRNA catabolic process [IGI]
- nuclear polyadenylation-dependent snoRNA catabolic process [IGI]
- nuclear polyadenylation-dependent tRNA catabolic process [IDA]
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 Shwachman-Bodian-Diamond syndrome protein family is involved in RNA metabolism.
A combination of structural, biochemical, and genetic studies in model organisms was used to infer a cellular role for the human protein (SBDS) responsible for Shwachman-Bodian-Diamond syndrome. The crystal structure of the SBDS homologue in Archaeoglobus fulgidus, AF0491, revealed a three domain protein. The N-terminal domain, which harbors the majority of disease-linked mutations, has a novel three-dimensional fold. The central ... [more]
J. Biol. Chem. May. 13, 2005; 280(19);19213-20 [Pubmed: 15701634]
Throughput
- Low Throughput
Ontology Terms
- phenotype: inviable (APO:0000112)
Curated By
- BioGRID