BAIT
ESA1
TAS1, NuA4 histone acetyltransferase complex catalytic subunit ESA1, KAT5, L000003952, YOR244W
Catalytic subunit of the histone acetyltransferase complex (NuA4); acetylates four conserved internal lysines of histone H4 N-terminal tail and can acetylate histone H2A; master regulator of cellular acetylation balance; required for cell cycle progression and transcriptional silencing at the rDNA locus and regulation of autophagy; human ortholog TIP60/KAT5 is implicated in cancer and other diseases
GO Process (10)
GO Function (3)
GO Component (4)
Gene Ontology Biological Process
- DNA repair [IDA, IMP]
- DNA-templated transcription, elongation [IDA, IMP]
- chromatin organization involved in regulation of transcription [IMP]
- chromatin silencing at rDNA [IGI, IMP]
- histone acetylation [IDA]
- peptidyl-lysine acetylation [IMP]
- positive regulation of macroautophagy [IMP]
- positive regulation of transcription elongation from RNA polymerase II promoter [IGI, IMP]
- regulation of cell cycle [IMP]
- regulation of transcription from RNA polymerase II promoter [IMP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Saccharomyces cerevisiae (S288c)
PREY
CDC31
DSK1, centrin, L000000269, YOR257W
Calcium-binding component of the spindle pole body (SPB) half-bridge; required for SPB duplication in mitosis and meiosis II; homolog of mammalian centrin; binds multiubiquitinated proteins and is involved in proteasomal protein degradation
GO Process (4)
GO Function (2)
GO Component (4)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Saccharomyces cerevisiae (S288c)
Affinity Capture-MS
An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods.
Publication
mChIP-KAT-MS, a method to map protein interactions and acetylation sites for lysine acetyltransferases.
Recent global proteomic and genomic studies have determined that lysine acetylation is a highly abundant posttranslational modification. The next challenge is connecting lysine acetyltransferases (KATs) to their cellular targets. We hypothesize that proteins that physically interact with KATs may not only predict the cellular function of the KATs but may be acetylation targets. We have developed a mass spectrometry-based method ... [more]
Proc. Natl. Acad. Sci. U.S.A. Apr. 23, 2013; 110(17);E1641-50 [Pubmed: 23572591]
Throughput
- High Throughput
Additional Notes
- identified by mChIP-KAT-MS assay, which consists of three steps: isolation of a lysine acetyltransferase (KAT) and its associated protein network from cells, enrichment of acetylated lysine residues within the network by an in vitro KAT reaction; and identification of the interacting proteins and acetylation sites by LC-MS/MS
Curated By
- BioGRID