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    PICST_9318 histone H2A variant [ Scheffersomyces stipitis CBS 6054 ]

    Gene ID: 4851670, updated on 21-Dec-2023

    Summary

    Gene symbol
    PICST_9318
    Gene description
    histone H2A variant
    Locus tag
    PICST_9318
    Gene type
    protein coding
    RNA name
    histone H2A variant
    RefSeq status
    PROVISIONAL
    Organism
    Scheffersomyces stipitis CBS 6054 (strain: CBS 6054)
    Lineage
    Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Scheffersomyces
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    Genomic context

    See PICST_9318 in Genome Data Viewer
    Location:
    chromosome: 1
    Exon count:
    1
    Sequence:
    Chromosome: 1; NC_009068.1 (2500691..2501077, complement)

    Chromosome 1 - NC_009068.1Genomic Context describing neighboring genes Neighboring gene Inosine/uridine-preferring nucleoside hydrolase Neighboring gene hypothetical protein Neighboring gene Nitrogen permease regulator 2 Neighboring gene hypothetical protein

    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_009068.1 Reference assembly

      Range
      2500691..2501077 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. XM_001387013.2XP_001387050.1  histone H2A variant, partial [Scheffersomyces stipitis CBS 6054]

      See identical proteins and their annotated locations for XP_001387050.1

      Status: PROVISIONAL

      UniProtKB/Swiss-Prot
      A3GHC1
      Conserved Domains (2) summary
      PTZ00017
      Location:5128
      PTZ00017; histone H2A; Provisional
      cd00074
      Location:10121
      H2A; Histone 2A; H2A is a subunit of the nucleosome. The nucleosome is an octamer containing two H2A, H2B, H3, and H4 subunits. The H2A subunit performs essential roles in maintaining structural integrity of the nucleosome, chromatin condensation, and binding ...