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
Saccharomyces cerevisiae (S288c)
PREY

SSE1

LPG3, MSI3, adenyl-nucleotide exchange factor SSE1, L000002078, YPL106C
ATPase component of heat shock protein Hsp90 chaperone complex; plays a role in determining prion variants; binds unfolded proteins; member of the heat shock protein 70 (HSP70) family; localized to the cytoplasm; deletion results in spindle elongation in S phase; SSE1 has a paralog, SSE2, that arose from the whole genome duplication
GO Process (2)
GO Function (3)
GO Component (2)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)

Biochemical Activity (Acetylation)

An interaction is inferred from the biochemical effect of one protein upon another, for example, GTP-GDP exchange activity or phosphorylation of a substrate by a kinase. The bait protein executes the activity on the substrate hit protein. A Modification value is recorded for interactions of this type with the possible values Phosphorylation, Ubiquitination, Sumoylation, Dephosphorylation, Methylation, Prenylation, Acetylation, Deubiquitination, Proteolytic Processing, Glucosylation, Nedd(Rub1)ylation, Deacetylation, No Modification, Demethylation.

Publication

Protein acetylation microarray reveals that NuA4 controls key metabolic target regulating gluconeogenesis.

Lin YY, Lu JY, Zhang J, Walter W, Dang W, Wan J, Tao SC, Qian J, Zhao Y, Boeke JD, Berger SL, Zhu H

Histone acetyltransferases (HATs) and histone deacetylases (HDACs) conduct many critical functions through nonhistone substrates in metazoans, but only chromatin-associated nonhistone substrates are known in Saccharomyces cerevisiae. Using yeast proteome microarrays, we identified and validated many nonchromatin substrates of the essential nucleosome acetyltransferase of H4 (NuA4) complex. Among these, acetylation sites (Lys19 and 514) of phosphoenolpyruvate carboxykinase (Pck1p) were determined by ... [more]

Cell Mar. 20, 2009; 136(6);1073-84 [Pubmed: 19303850]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
ESA1 SSE1
Synthetic Lethality
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.

Low/High-BioGRID
284944

Curated By

  • BioGRID