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    SAS2 histone acetyltransferase [ Saccharomyces cerevisiae S288C ]

    Gene ID: 855157, updated on 18-Sep-2024

    Summary

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    Official Symbol
    SAS2
    Official Full Name
    histone acetyltransferase
    Primary source
    SGD:S000004734
    Locus tag
    YMR127C
    See related
    AllianceGenome:SGD:S000004734; FungiDB:YMR127C; VEuPathDB:YMR127C
    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
    KAT8
    Summary
    Enables histone acetyltransferase activity. Involved in chromatin organization and histone H3 acetylation. Located in chromatin. Part of SAS acetyltransferase complex. Orthologous to human KAT5 (lysine acetyltransferase 5). [provided by Alliance of Genome Resources, Apr 2022]
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    Genomic context

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    See SAS2 in Genome Data Viewer
    Location:
    chromosome: XIII
    Exon count:
    1
    Sequence:
    Chromosome: XIII; NC_001145.3 (522329..523345, complement)

    Chromosome XIII - NC_001145.3Genomic Context describing neighboring genes Neighboring gene Sto1p Neighboring gene Dlt1p Neighboring gene ATP-dependent RNA helicase ECM16 Neighboring gene Pom152p

    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. Donor Preference Meets Heterochromatin: Moonlighting Activities of a Recombinational Enhancer in Saccharomyces cerevisiae. Dodson AE, et al. Genetics, 2016 Nov. PMID 27655944, Free PMC Article
    2. RNA polymerase III and RNA polymerase II promoter complexes are heterochromatin barriers in Saccharomyces cerevisiae. Donze D, et al. EMBO J, 2001 Feb 1. PMID 11157758, Free PMC Article
    3. Synthesis of a novel series of thiazole-based histone acetyltransferase inhibitors. Secci D, et al. Bioorg Med Chem, 2014 Mar 1. PMID 24513187
    4. Acetylated H4K16 by MYST1 protects UROtsa cells from arsenic toxicity and is decreased following chronic arsenic exposure. Jo WJ, et al. Toxicol Appl Pharmacol, 2009 Dec 15. PMID 19732783, Free PMC Article
    5. Induction by adozelesin and hydroxyurea of origin recognition complex-dependent DNA damage and DNA replication checkpoints in Saccharomyces cerevisiae. Weinberger M, et al. J Biol Chem, 1999 Dec 10. PMID 10585487

    See all (78) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Nut1/Hos1 and Sas2/Rpd3 control the H3 acetylation of two different sets of osmotic stress-induced genes.
      Title: Nut1/Hos1 and Sas2/Rpd3 control the H3 acetylation of two different sets of osmotic stress-induced genes.
    2. Here, we find that Sas2-dependent acetylated histone H4 K16Ac in bulk histones requires passage of the cells through the S-phase of the cell cycle, and the rate of increase in H4 K16Ac depends on both CAF-I and Asf1.
      Title: A link between Sas2-mediated H4 K16 acetylation, chromatin assembly in S-phase by CAF-I and Asf1, and nucleosome assembly by Spt6 during transcription.
    3. Sas2 acetylates histone H4 lysine 16 (H4K16), and telomere shortening in tlc1 mutants was accompanied by a selective and Sas2-dependent increase in subtelomeric H4K16 acetylation.
      Title: Inactivation of the Sas2 histone acetyltransferase delays senescence driven by telomere dysfunction.
    4. The functional relationships between Sas2p and the origin recognition complex in DNA replication and transcriptional silencing was examined in different genetic backgrounds.
      Title: Positive roles of SAS2 in DNA replication and transcriptional silencing in yeast.
    5. SAS2 is essential for the organization of the chromatin structure at HMLalpha locus.
      Title: Chromatin assembly factor Asf1p-dependent occupancy of the SAS histone acetyltransferase complex at the silent mating-type locus HMLalpha.
    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 acetyltransferase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables acyltransferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables chromatin binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables histone H4K16 acetyltransferase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables histone acetyltransferase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables histone acetyltransferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables peptide-lysine-N-acetyltransferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables transcription coregulator activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables zinc ion binding RCA
    inferred from Reviewed Computational Analysis
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in chromatin organization IEA
    Inferred from Electronic Annotation
    more info
    		  
    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 silent mating-type cassette heterochromatin formation IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in subtelomeric heterochromatin formation IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Component Evidence Code Pubs
    part_of NuA4 histone acetyltransferase complex IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    part_of SAS acetyltransferase complex IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    part_of SAS acetyltransferase complex IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    located_in chromatin IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in chromatin IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in chromosome, telomeric region IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  
    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
    histone acetyltransferase
    NP_013846.1
    • Histone acetyltransferase (HAT) catalytic subunit of the SAS complex; acetylates free histones and nucleosomes and regulates transcriptional silencing; member of the MYSTacetyltransferase family; other members are Sas4p and Sas5p

    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
      522329..523345 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001182628.1 → NP_013846.1  TPA: histone acetyltransferase [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_013846.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6VZV0, P40963
      UniProtKB/TrEMBL
      B3LM18, C7GU91, C8ZEY2, G2WKH8, N1NXD5
      Conserved Domains (1) summary
      COG5027
      Location:31 → 338
      SAS2; Histone acetyltransferase (MYST family) [Chromatin structure and dynamics]
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P40963.1

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