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    SNL1 Snl1p [ Saccharomyces cerevisiae S288C ]

    Gene ID: 854796, updated on 9-Jun-2024

    Summary

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    Gene symbol
    SNL1
    Gene description
    Snl1p
    Primary source
    FungiDB:YIL016W
    Locus tag
    YIL016W
    See related
    SGD:S000001278; AllianceGenome:SGD:S000001278; VEuPathDB:YIL016W
    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 ribosome binding activity. Involved in nuclear pore organization and protein folding. Located in endoplasmic reticulum membrane and nuclear envelope. [provided by Alliance of Genome Resources, Apr 2022]
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    Genomic context

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    See SNL1 in Genome Data 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-Asp

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001141.2

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. The BAG homology domain of Snl1 cures yeast prion [URE3] through regulation of Hsp70 chaperones. Kumar N, et al. G3 (Bethesda), 2014 Mar 20. PMID 24408033, Free PMC Article
    2. Crystal structure of a complex between the phosphorelay protein YPD1 and the response regulator domain of SLN1 bound to a phosphoryl analog. Zhao X, et al. J Mol Biol, 2008 Jan 25. PMID 18076904, Free PMC Article
    3. Insights into the structural dynamics of the Hsp110-Hsp70 interaction reveal the mechanism for nucleotide exchange activity. Andréasson C, et al. Proc Natl Acad Sci U S A, 2008 Oct 28. PMID 18948593, Free PMC Article
    4. Prediction of novel Bag-1 homologs based on structure/function analysis identifies Snl1p as an Hsp70 co-chaperone in Saccharomyces cerevisiae. Sondermann H, et al. J Biol Chem, 2002 Sep 6. PMID 12105220
    5. The integral membrane protein snl1p is genetically linked to yeast nuclear pore complex function. Ho AK, et al. Mol Biol Cell, 1998 Feb. PMID 9450961, Free PMC Article

    See all (43) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. cytosolic Hsp70 interacts with up to three types of nucleotide exchange factors (NEFs) homologous to human counterparts: Sse1/Sse2 (Heat shock protein 110 (Hsp110)), Fes1 (HspBP1), and Snl1 (Bag-1).
      Title: Hierarchical functional specificity of cytosolic heat shock protein 70 (Hsp70) nucleotide exchange factors in yeast.
    2. Snl1 physically interacts with intact ribosome
      Title: A lysine-rich region within fungal BAG domain-containing proteins mediates a novel association with ribosomes.
    3. Crystal structure of a complex between the phosphorelay protein YPD1 and the response regulator domain of SLN1 bound to a phosphoryl analog is reported.
      Title: Crystal structure of a complex between the phosphorelay protein YPD1 and the response regulator domain of SLN1 bound to a phosphoryl analog.
    Submit: New GeneRIF Correction

    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Homology

    Gene Ontology Provided by SGD

    Function Evidence Code Pubs
    enables protein-folding chaperone binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables ribosome binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in nuclear pore organization IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    involved_in protein folding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in endoplasmic reticulum IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in endoplasmic reticulum membrane IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in endoplasmic reticulum membrane IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in membrane IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in mitochondrion HDA PubMed 
    located_in nuclear envelope IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in nuclear membrane IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in nucleus IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    Snl1p
    NP_012248.1
    • Ribosome-associated protein; proposed to act in protein synthesis, nuclear pore complex biogenesis and maintenance as well as protein folding and prion maintenance; has similarity to the mammalian BAG-1 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_001141.2 Reference assembly

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

    mRNA and Protein(s)

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

      See identical proteins and their annotated locations for NP_012248.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6VVR3, P40548
      UniProtKB/TrEMBL
      A0A7I9EGL1, A6ZVQ1, B3LTM4, C7GSF8, C8ZAN4, G2WGC8, N1P1P9
      Conserved Domains (1) summary
      smart00264
      Location:73 → 159
      BAG; BAG domains, present in regulator of Hsp70 proteins
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P40548.1

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