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    SCL1 proteasome core particle subunit alpha 1 [ Saccharomyces cerevisiae S288C ]

    Gene ID: 852873, updated on 13-Apr-2024

    Summary

    Gene symbol
    SCL1
    Gene description
    proteasome core particle subunit alpha 1
    Primary source
    SGD:S000002979
    Locus tag
    YGL011C
    See related
    AllianceGenome:SGD:S000002979
    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
    PRC2
    Summary
    Involved in proteasomal ubiquitin-independent protein catabolic process and proteasome-mediated ubiquitin-dependent protein catabolic process. Located in mitochondrion. Part of proteasome core complex, alpha-subunit complex. Human ortholog(s) of this gene implicated in myocardial infarction. Orthologous to human PSMA6 (proteasome 20S subunit alpha 6). [provided by Alliance of Genome Resources, Apr 2022]
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    Genomic context

    Location:
    chromosome: VII
    Exon count:
    1
    Sequence:
    Chromosome: VII; NC_001139.9 (474489..475247, complement)

    Chromosome VII - NC_001139.9Genomic Context describing neighboring genes Neighboring gene drug-responsive transcription factor PDR1 Neighboring gene delta(24(24(1)))-sterol reductase Neighboring gene Mpo1p Neighboring gene 3-isopropylmalate dehydratase LEU1

    Pathways from PubChem

    Interactions

    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

    Gene Ontology Provided by SGD

    Function Evidence Code Pubs
    enables molecular_function ND
    No biological Data available
    more info
     
    Component Evidence Code Pubs
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
     
    located_in mitochondrion 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
     
    part_of proteasome complex IEA
    Inferred from Electronic Annotation
    more info
     
    part_of proteasome core complex IEA
    Inferred from Electronic Annotation
    more info
     
    part_of proteasome core complex, alpha-subunit complex IBA
    Inferred from Biological aspect of Ancestor
    more info
     
    part_of proteasome core complex, alpha-subunit complex IDA
    Inferred from Direct Assay
    more info
    PubMed 
    part_of proteasome core complex, alpha-subunit complex IEA
    Inferred from Electronic Annotation
    more info
     

    General protein information

    Preferred Names
    proteasome core particle subunit alpha 1
    NP_011504.3
    • Alpha 1 subunit of the 20S proteasome; involved in the degradation of ubiquitinated substrates; 20S proteasome is the core complex of the 26S proteasome; essential for growth; detected in the mitochondria

    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_001139.9 Reference assembly

      Range
      474489..475247 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001180876.3 → NP_011504.3  TPA: proteasome core particle subunit alpha 1 [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_011504.3

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6VUC6, P15708, P21243
      UniProtKB/TrEMBL
      A0A6A5PYC9, A6ZUY2, B3LIM6, B5VIV2, C7GK62, C8Z8N2, G2WE82, N1P3C8
      Conserved Domains (1) summary
      cd03754
      Location:12 → 228
      proteasome_alpha_type_6; The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming ...