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    NAT4 N-terminal L-serine N(alpha)-acetyltransferase NatD [ Saccharomyces cerevisiae S288C ]

    Gene ID: 855091, updated on 9-Dec-2024

    Summary

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    Official Symbol
    NAT4
    Official Full Name
    N-terminal L-serine N(alpha)-acetyltransferase NatD
    Primary source
    SGD:S000004673
    Locus tag
    YMR069W
    See related
    AllianceGenome:SGD:S000004673; FungiDB:YMR069W; VEuPathDB:YMR069W
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Saccharomyces cerevisiae S288C (strain: S288C)
    Lineage
    Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
    Also known as
    NAA40
    Summary
    Predicted to enable histone H2A acetyltransferase activity; histone H4 acetyltransferase activity; and peptide-serine-alpha-N-acetyltransferase activity. Involved in heterochromatin formation. Located in cytoplasm and nucleus. Orthologous to human NAA40 (N-alpha-acetyltransferase 40, NatD catalytic subunit). [provided by Alliance of Genome Resources, Dec 2024]
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    Genomic context

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    See NAT4 in Genome Data Viewer
    Location:
    chromosome: XIII
    Exon count:
    1
    Sequence:
    Chromosome: XIII; NC_001145.3 (407709..408566)

    Chromosome XIII - NC_001145.3Genomic Context describing neighboring genes Neighboring gene Ubx4p Neighboring gene Avo2p Neighboring gene Mot3p Neighboring gene Tvp18p

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001145.3

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Yeast Nat4 regulates DNA damage checkpoint signaling through its N-terminal acetyltransferase activity on histone H4. Constantinou M, et al. PLoS Genet, 2024 Oct. PMID 39356727, Free PMC Article
    2. N-alpha-terminal acetylation of histone H4 regulates arginine methylation and ribosomal DNA silencing. Schiza V, et al. PLoS Genet, 2013. PMID 24068969, Free PMC Article
    3. An Nalpha-acetyltransferase responsible for acetylation of the N-terminal residues of histones H4 and H2A. Song OK, et al. J Biol Chem, 2003 Oct 3. PMID 12915400
    4. Loss of Nat4 and its associated histone H4 N-terminal acetylation mediates calorie restriction-induced longevity. Molina-Serrano D, et al. EMBO Rep, 2016 Dec. PMID 27799288, Free PMC Article
    5. Exploring the Complexity of Protein-Level Dosage Compensation that Fine-Tunes Stoichiometry of Multiprotein Complexes. Ishikawa K, et al. PLoS Genet, 2020 Oct. PMID 33112847, Free PMC Article

    See all (23) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. findings show here that deletion of histone N-alpha-terminal acetyltransferase Nat4 and loss of its associated H4 N-terminal acetylation (N-acH4) extend yeast replicative lifespan.
      Title: Loss of Nat4 and its associated histone H4 N-terminal acetylation mediates calorie restriction-induced longevity.
    2. N-terminal serine acetylation of histone H4 may be a part of an essential charge patch first described for the histone H2A.Z variant in Tetrahymena species.
      Title: Properties of Nat4, an N(alpha)-acetyltransferase of Saccharomyces cerevisiae that modifies N termini of histones H2A and H4.
    Submit: New GeneRIF Correction

    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Homology

    Gene Ontology Provided by SGD

    Function Evidence Code Pubs
    enables acyltransferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables histone H2A acetyltransferase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables histone H2A acetyltransferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables histone H2A acetyltransferase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables histone H4 acetyltransferase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables histone H4 acetyltransferase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables histone H4 acetyltransferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables histone H4 acetyltransferase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables peptide-serine-alpha-N-acetyltransferase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables peptide-serine-alpha-N-acetyltransferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in heterochromatin formation IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in cytoplasm HDA PubMed 
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in nucleus HDA PubMed 
    is_active_in nucleus IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in nucleus IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    N-terminal L-serine N(alpha)-acetyltransferase NatD
    NP_013785.1
    • N alpha-acetyl-transferase; involved in acetylation of the N-terminal residues of histones H4 and H2A

    NCBI Reference Sequences (RefSeq)

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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_001145.3 Reference assembly

      Range
      407709..408566
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001182567.1 → NP_013785.1  TPA: N-terminal L-serine N(alpha)-acetyltransferase NatD [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_013785.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6VZP3, Q04751
      UniProtKB/TrEMBL
      B3LLW2, C7GL55, C8ZES1, N1NY96
      Conserved Domains (1) summary
      pfam00583
      Location:139 → 245
      Acetyltransf_1; Acetyltransferase (GNAT) family
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    Q04751.1

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