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
NPL3
MTR13, MTS1, NAB1, NOP3, mRNA-binding protein NPL3, L000001270, YDR432W
RNA-binding protein; promotes elongation, regulates termination, and carries poly(A) mRNA from nucleus to cytoplasm; represses translation initiation by binding eIF4G; required for pre-mRNA splicing; interacts with E3 ubiquitin ligase Bre1p, linking histone ubiquitination to mRNA processing; may have role in telomere maintenance; dissociation from mRNAs promoted by Mtr10p; phosphorylated by Sky1p in cytoplasm; protein abundance increases in response to DNA replication stress
GO Process (6)
GO Function (4)
GO Component (2)
Gene Ontology Biological Process
- mRNA export from nucleus [IGI]
- mRNA splicing, via spliceosome [IGI, IMP]
- negative regulation of termination of RNA polymerase II transcription, poly(A)-coupled [IDA, IMP]
- negative regulation of translation [IDA]
- positive regulation of transcription elongation from RNA polymerase II promoter [IDA, IMP]
- translational termination [IGI, IMP]
Gene Ontology Molecular Function
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