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    SNL1 Snl1p [ Saccharomyces cerevisiae S288C ]

    Gene ID: 854796, updated on 9-Jul-2017
    Gene symbol
    SNL1
    Gene description
    Snl1p
    Primary source
    SGD:S000001278
    Locus tag
    YIL016W
    Gene type
    protein coding
    RNA name
    Snl1p
    RefSeq status
    REVIEWED
    Organism
    Saccharomyces cerevisiae S288C (strain: S288c)
    Lineage
    Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
    See SNL1 in Map Viewer
    Location:
    chromosome: IX
    Exon count:
    1
    Sequence:
    Chromosome: IX; NC_001141.2 (321454..321933)

    Chromosome IX - NC_001141.2Genomic Context describing neighboring genes Neighboring gene ribosomal 60S subunit protein L2B Neighboring gene glucose-induced degradation complex subunit VID28 Neighboring gene aspartyl protease BAR1 Neighboring gene tRNA

    GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?

    • Protein processing in endoplasmic reticulum, organism-specific biosystem (from KEGG)
      Protein processing in endoplasmic reticulum, organism-specific biosystemThe endoplasmic reticulum (ER) is a subcellular organelle where proteins are folded with the help of lumenal chaperones. Newly synthesized peptides enter the ER via the sec61 pore and are glycosylate...
    • Protein processing in endoplasmic reticulum, conserved biosystem (from KEGG)
      Protein processing in endoplasmic reticulum, conserved biosystemThe endoplasmic reticulum (ER) is a subcellular organelle where proteins are folded with the help of lumenal chaperones. Newly synthesized peptides enter the ER via the sec61 pore and are glycosylate...
    Products Interactant Other Gene Complex Source Pubs Description

    Gene Ontology Provided by GO

    Function Evidence Code Pubs
    chaperone binding IEA
    Inferred from Electronic Annotation
    more info
     
    ribosome binding IDA
    Inferred from Direct Assay
    more info
    PubMed 
    Process Evidence Code Pubs
    nuclear pore organization IGI
    Inferred from Genetic Interaction
    more info
    PubMed 
    protein folding IPI
    Inferred from Physical Interaction
    more info
    PubMed 
    Component Evidence Code Pubs
    colocalizes_with cytosolic ribosome IDA
    Inferred from Direct Assay
    more info
    PubMed 
    endoplasmic reticulum IEA
    Inferred from Electronic Annotation
    more info
     
    endoplasmic reticulum membrane IDA
    Inferred from Direct Assay
    more info
    PubMed 
    endoplasmic reticulum membrane IEA
    Inferred from Electronic Annotation
    more info
     
    integral component of membrane IEA
    Inferred from Electronic Annotation
    more info
     
    membrane IEA
    Inferred from Electronic Annotation
    more info
     
    membrane ISS
    Inferred from Sequence or Structural Similarity
    more info
    PubMed 
    mitochondrion IDA
    Inferred from Direct Assay
    more info
    PubMed 
    nuclear envelope IDA
    Inferred from Direct Assay
    more info
    PubMed 
    nuclear membrane IEA
    Inferred from Electronic Annotation
    more info
     
    nucleus IEA
    Inferred from Electronic Annotation
    more info
     
    Names
    Snl1p
    NP_012248.1
    • Ribosome-associated protein; proposed to act in protein synthesis and nuclear pore complex biogenesis and maintenance as well as protein folding; has similarity to the mammalian BAG-1 protein

    Genome Annotation

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference assembly

    Genomic

    1. NC_001141.2 Reference assembly

      Range
      321454..321933
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001179366.1NP_012248.1  TPA: Snl1p [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_012248.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      P40548
      Conserved Domains (1) summary
      smart00264
      Location:73159
      BAG; BAG domains, present in regulator of Hsp70 proteins
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