BAIT
YNG2
EAF4, NBN1, histone acetyltransferase YNG2, L000004452, YHR090C
Subunit of NuA4, an essential histone acetyltransferase complex; positions Piccolo NuA4 for efficient acetylation of histone H4 or histone H2A; relocalizes to the cytosol in response to hypoxia; similar to human tumor suppressor ING1 and its isoforms ING4 and ING5
GO Process (3)
GO Function (2)
GO Component (4)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Saccharomyces cerevisiae (S288c)
PREY
HDA1
histone deacetylase HDA1, L000004088, YNL021W
Putative catalytic subunit of a class II histone deacetylase complex; role in azole resistance via Hsp90p, and in the heat shock response; Hda1p interacts with the Hda2p-Hda3p subcomplex to form an active tetramer; deletion increases histone H2B, H3 and H4 acetylation; other members of the HDA1 histone deacetylase complex are Hda2p and Hda3p
GO Process (9)
GO Function (2)
GO Component (1)
Gene Ontology Biological Process
- chromatin organization involved in regulation of transcription [IMP]
- gene silencing by RNA [IMP]
- gene silencing involved in chronological cell aging [IGI, IMP]
- histone deacetylation [IDA, IMP]
- negative regulation of chromatin silencing involved in replicative cell aging [IGI, IMP]
- negative regulation of transcription by transcription factor localization [IGI]
- negative regulation of transcription from RNA polymerase II promoter [IMP]
- positive regulation of transcription from RNA polymerase II promoter [IMP]
- regulation of chromatin silencing at telomere [IMP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
- HDA1 complex [IDA, IPI]
Saccharomyces cerevisiae (S288c)
Negative Genetic
Mutations/deletions in separate genes, each of which alone causes a minimal phenotype, but when combined in the same cell results in a more severe fitness defect or lethality under a given condition. This term is reserved for high or low throughput studies with scores.
Publication
Combined Action of Histone Reader Modules Regulates NuA4 Local Acetyltransferase Function but Not Its Recruitment on the Genome.
Recognition of histone marks by reader modules is thought to be at the heart of epigenetic mechanisms. These protein domains are considered to function by targeting regulators to chromosomal loci carrying specific histone modifications. This is important for proper gene regulation as well as propagation of epigenetic information. The NuA4 acetyltransferase complex contains two of these reader modules, an H3K4me3-specific ... [more]
Mol. Cell. Biol. Nov. 15, 2016; 36(22);2768-2781 [Pubmed: 27550811]
Throughput
- High Throughput
Ontology Terms
- phenotype: colony size (APO:0000063)
Additional Notes
- E-MAP, significance >2 or <-2.5
- yng2 - W247A
Related interactions
Curated By
- BioGRID