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EAF7 Eaf7p [ Saccharomyces cerevisiae S288C ]

Gene ID: 855586, updated on 30-Jul-2025
Official Symbol
EAF7
Official Full Name
Eaf7p
Primary source
SGD:S000005080
Locus tag
YNL136W
See related
AllianceGenome:SGD:S000005080; FungiDB:YNL136W; VEuPathDB:YNL136W
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Saccharomyces cerevisiae S288C (strain: S288C)
Lineage
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Summary
Involved in DNA repair and regulation of transcription by RNA polymerase II. Located in nucleus. Part of NuA4 histone acetyltransferase complex. Orthologous to human MRGBP (MRG domain binding protein). [provided by Alliance of Genome Resources, Jul 2025]
Orthologs
all
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See EAF7 in Genome Data Viewer
Location:
chromosome: XIV
Exon count:
1
Sequence:
Chromosome: XIV; NC_001146.8 (370368..371645)

Chromosome XIV - NC_001146.8Genomic Context describing neighboring genes Neighboring gene adenylate cyclase-binding protein Neighboring gene mitochondrial 37S ribosomal protein uS4m NAM9 Neighboring gene peptidylprolyl isomerase FPR1 Neighboring gene uncharacterized protein

Genomic Sequence:
NC_001146.8

Go to nucleotide: Graphics FASTA GenBank

Related articles in PubMed

  1. Biochemical Characterization of the TINTIN Module of the NuA4 Complex Reveals Allosteric Regulation of Nucleosome Interaction. Dalwadi U, et al. Mol Cell Biol, 2022 Nov 17. PMID 36190236, Free PMC Article
  2. NuA4 Lysine Acetyltransferase Complex Contributes to Phospholipid Homeostasis in Saccharomyces cerevisiae. Dacquay L, et al. G3 (Bethesda), 2017 Jun 7. PMID 28455416, Free PMC Article
  3. The essential function of Swc4p - a protein shared by two chromatin-modifying complexes of the yeast Saccharomyces cerevisiae - resides within its N-terminal part. Miciałkiewicz A, et al. Acta Biochim Pol, 2008. PMID 18726008
  4. Deletion of host histone acetyltransferases and deacetylases strongly affects Agrobacterium-mediated transformation of Saccharomyces cerevisiae. Soltani J, et al. FEMS Microbiol Lett, 2009 Sep. PMID 19659745
  5. Loss of nonsense mediated decay suppresses mutations in Saccharomyces cerevisiae TRA1. Kvas S, et al. BMC Genet, 2012 Mar 22. PMID 22439631, Free PMC Article

See all (85) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. In vitro binding assays showed that Eaf3/5/7 specifically stimulates NuA4 binding to di- and trimethylated histone H3 Lys-36 and that this binding is important for NuA4 occupancy in transcribed ORFs.
    Title: The Eaf3/5/7 Subcomplex Stimulates NuA4 Interaction with Methylated Histone H3 Lys-36 and RNA Polymerase II.
  2. Eaf5 and Eaf7 form a subcomplex. Eaf7 interacts with NuA4 through Eaf5.
    Title: Functional dissection of the NuA4 histone acetyltransferase reveals its role as a genetic hub and that Eaf1 is essential for complex integrity.
Submit: New GeneRIF Correction
Products Interactant Other Gene Complex Source Pubs Description

Homology

Gene Ontology Provided by SGD

Function Evidence Code Pubs
enables molecular_function ND
No biological Data available
more info
  
Process Evidence Code Pubs
involved_in DNA damage response IEA
Inferred from Electronic Annotation
more info
  
involved_in DNA repair IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in DNA repair IEA
Inferred from Electronic Annotation
more info
  
involved_in DNA replication-dependent chromatin assembly IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in DNA-templated transcription NAS
Non-traceable Author Statement
more info
 PubMed 
involved_in chromatin organization IEA
Inferred from Electronic Annotation
more info
  
involved_in nucleosome disassembly IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in positive regulation of transcription elongation by RNA polymerase II IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in regulation of DNA-templated transcription IEA
Inferred from Electronic Annotation
more info
  
involved_in regulation of transcription by RNA polymerase II IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in regulation of transcription by RNA polymerase II IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in regulation of transcription by RNA polymerase II IPI
Inferred from Physical Interaction
more info
 PubMed 
Component Evidence Code Pubs
part_of H4/H2A histone acetyltransferase complex IEA
Inferred from Electronic Annotation
more info
  
part_of NuA4 histone acetyltransferase complex IBA
Inferred from Biological aspect of Ancestor
more info
  
part_of NuA4 histone acetyltransferase complex IDA
Inferred from Direct Assay
more info
 PubMed 
part_of NuA4 histone acetyltransferase complex IPI
Inferred from Physical Interaction
more info
 PubMed 
part_of nucleosome disassembly/reassembly complex IPI
Inferred from Physical Interaction
more info
 PubMed 
located_in nucleus HDA PubMed 
located_in nucleus IDA
Inferred from Direct Assay
more info
 PubMed 
located_in nucleus IEA
Inferred from Electronic Annotation
more info
  
located_in nucleus NAS
Non-traceable Author Statement
more info
 PubMed 
Preferred Names
Eaf7p
NP_014263.1
  • Subunit of the NuA4 histone acetyltransferase complex; NuA4 acetylates the N-terminal tails of histones H4 and H2A

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_001146.8 Reference assembly

    Range
    370368..371645
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001182974.1 → NP_014263.1  TPA: Eaf7p

    See identical proteins and their annotated locations for NP_014263.1

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    D6W146, P53911
    UniProtKB/TrEMBL
    C7GKB1, G2WLX0, N1NXU8
    Conserved Domains (1) summary
    pfam07904
    Location:9 → 132
    Eaf7; Chromatin modification-related protein EAF7
Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
P53911.1

Gene LinkOut

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