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    ASR1 ubiquitin-protein ligase ASR1 [ Saccharomyces cerevisiae S288C ]

    Gene ID: 856208, updated on 2-Nov-2024

    Summary

    Official Symbol
    ASR1
    Official Full Name
    ubiquitin-protein ligase ASR1
    Primary source
    SGD:S000006297
    Locus tag
    YPR093C
    See related
    AllianceGenome:SGD:S000006297; FungiDB:YPR093C; VEuPathDB:YPR093C
    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 ubiquitin-protein transferase activity. Involved in protein ubiquitination; response to ethanol; and septin ring assembly. Located in cytoplasm and nucleus. [provided by Alliance of Genome Resources, Nov 2024]
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    Genomic context

    See ASR1 in Genome Data Viewer
    Location:
    chromosome: XVI
    Exon count:
    1
    Sequence:
    Chromosome: XVI; NC_001148.4 (719558..720424, complement)

    Chromosome XVI - NC_001148.4Genomic Context describing neighboring genes Neighboring gene ncRNA Neighboring gene ncRNA Neighboring gene U2 snRNP complex subunit RDS3 Neighboring gene Arf family guanine nucleotide exchange factor SYT1

    Bibliography

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?

    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 ubiquitin protein ligase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
     
    enables ubiquitin-protein transferase activity IDA
    Inferred from Direct Assay
    more info
    PubMed 
    enables zinc ion binding RCA
    inferred from Reviewed Computational Analysis
    more info
    PubMed 
    Process Evidence Code Pubs
    involved_in protein ubiquitination IDA
    Inferred from Direct Assay
    more info
    PubMed 
    involved_in protein ubiquitination IMP
    Inferred from Mutant Phenotype
    more info
    PubMed 
    involved_in response to ethanol IMP
    Inferred from Mutant Phenotype
    more info
    PubMed 
    involved_in septin ring assembly IMP
    Inferred from Mutant Phenotype
    more info
    PubMed 
    Component Evidence Code Pubs
    located_in cytoplasm IDA
    Inferred from Direct Assay
    more info
    PubMed 
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
     
    located_in nucleus IDA
    Inferred from Direct Assay
    more info
    PubMed 
    located_in nucleus IEA
    Inferred from Electronic Annotation
    more info
     

    General protein information

    Preferred Names
    ubiquitin-protein ligase ASR1
    NP_015418.2
    • Ubiquitin ligase that modifies and regulates RNA Pol II; involved in a putative alcohol-responsive signaling pathway; accumulates in the nucleus under alcohol stress; has a role in organization of septins and the actin cytoskeleton; contains a Ring/PHD finger domain similar to the mammalian rA9 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_001148.4 Reference assembly

      Range
      719558..720424 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001184190.1NP_015418.2  TPA: ubiquitin-protein ligase ASR1 [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_015418.2

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6W492, Q06834
      UniProtKB/TrEMBL
      B3LK59, C8ZJB6
      Conserved Domains (2) summary
      smart00249
      Location:121167
      PHD; PHD zinc finger
      cd16448
      Location:448
      RING-H2; H2 subclass of RING (RING-H2) finger and its variants