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)
Saccharomyces cerevisiae (S288c)
PREY

CIN2

L000000337, YPL241C
GTPase-activating protein (GAP) for Cin4p; tubulin folding factor C involved in beta-tubulin (Tub2p) folding; mutants display increased chromosome loss and benomyl sensitivity; deletion complemented by human GAP, retinitis pigmentosa 2
GO Process (3)
GO Function (1)
GO Component (0)

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

Regulation of chromosome stability by the histone H2A variant Htz1, the Swr1 chromatin remodeling complex, and the histone acetyltransferase NuA4.

Krogan NJ, Baetz K, Keogh MC, Datta N, Sawa C, Kwok TC, Thompson NJ, Davey MG, Pootoolal J, Hughes TR, Emili A, Buratowski S, Hieter P, Greenblatt JF

NuA4, the only essential histone acetyltransferase complex in Saccharomyces cerevisiae, acetylates the N-terminal tails of histones H4 and H2A. Affinity purification of NuA4 revealed the presence of three previously undescribed subunits, Vid21/Eaf1/Ydr359c, Swc4/Eaf2/Ygr002c, and Eaf7/Ynl136w. Experimental analyses revealed at least two functionally distinct sets of polypeptides in NuA4: (i) Vid21 and Yng2, and (ii) Eaf5 and Eaf7. Vid21 and Yng2 ... [more]

Proc. Natl. Acad. Sci. U.S.A. Sep. 14, 2004; 101(37);13513-8 [Pubmed: 15353583]

Throughput

  • High Throughput

Ontology Terms

  • phenotype: inviable (APO:0000112)

Curated By

  • BioGRID