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    PHO23 Pho23p [ Saccharomyces cerevisiae S288C ]

    Gene ID: 855626, updated on 2-Nov-2024

    Summary

    Official Symbol
    PHO23
    Official Full Name
    Pho23p
    Primary source
    SGD:S000005041
    Locus tag
    YNL097C
    See related
    AllianceGenome:SGD:S000005041; FungiDB:YNL097C; VEuPathDB:YNL097C
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Saccharomyces cerevisiae S288C (strain: S288C)
    Lineage
    Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
    Summary
    Enables methylated histone binding activity. Involved in several processes, including cellular response to heat; positive regulation of invasive growth in response to glucose limitation; and regulation of gene expression. Located in nucleus. Part of Rpd3L complex. Human ortholog(s) of this gene implicated in head and neck squamous cell carcinoma and squamous cell carcinoma. Orthologous to several human genes including ING1 (inhibitor of growth family member 1); ING2 (inhibitor of growth family member 2); and ING3 (inhibitor of growth family member 3). [provided by Alliance of Genome Resources, Nov 2024]
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    Genomic context

    See PHO23 in Genome Data Viewer
    Location:
    chromosome: XIV
    Exon count:
    1
    Sequence:
    Chromosome: XIV; NC_001146.8 (441366..442358, complement)

    Chromosome XIV - NC_001146.8Genomic Context describing neighboring genes Neighboring gene Ras family GTPase RAS2 Neighboring gene Pls1p Neighboring gene tRNA-Leu Neighboring gene ribosomal 40S subunit protein S7B

    Interactions

    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

    Gene Ontology Provided by SGD

    Function Evidence Code Pubs
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
     
    enables methylated histone binding IBA
    Inferred from Biological aspect of Ancestor
    more info
     
    enables methylated histone binding IDA
    Inferred from Direct Assay
    more info
    PubMed 
    enables zinc ion binding RCA
    inferred from Reviewed Computational Analysis
    more info
    PubMed 
    Component Evidence Code Pubs
    part_of Rpd3L complex HDA PubMed 
    part_of Rpd3L complex IBA
    Inferred from Biological aspect of Ancestor
    more info
     
    part_of Rpd3L complex IDA
    Inferred from Direct Assay
    more info
    PubMed 
    part_of Rpd3L-Expanded complex HDA PubMed 
    located_in chromatin IEA
    Inferred from Electronic Annotation
    more info
     
    part_of histone deacetylase complex IDA
    Inferred from Direct Assay
    more info
    PubMed 
    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

    Preferred Names
    Pho23p
    NP_014302.3
    • Component of the Rpd3L histone deacetylase complex; involved in transcriptional regulation of PHO5; affects termination of snoRNAs and cryptic unstable transcripts (CUTs); C-terminus shares significant sequence identity with the human candidate tumor suppressor p33-ING1 and its isoform ING3

    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_001146.8 Reference assembly

      Range
      441366..442358 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001182935.3NP_014302.3  TPA: Pho23p [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_014302.3

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6W183, P50947, Q45TZ9
      UniProtKB/TrEMBL
      A6ZRY4, B3LNV5, C7GR82, C8ZGD3, G2WM08
      Conserved Domains (1) summary
      COG5034
      Location:5330
      TNG2; Chromatin remodeling protein, contains PhD zinc finger [Chromatin structure and dynamics]