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    SIL1 Sil1p [ Saccharomyces cerevisiae S288C ]

    Gene ID: 854126, updated on 2-Nov-2024

    Summary

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    Official Symbol
    SIL1
    Official Full Name
    Sil1p
    Primary source
    SGD:S000005391
    Locus tag
    YOL031C
    See related
    AllianceGenome:SGD:S000005391; FungiDB:YOL031C; VEuPathDB:YOL031C
    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
    SLS1
    Summary
    Enables adenyl-nucleotide exchange factor activity. Involved in SRP-dependent cotranslational protein targeting to membrane, translocation. Located in endoplasmic reticulum. Used to study Marinesco-Sjogren syndrome. Human ortholog(s) of this gene implicated in Marinesco-Sjogren syndrome and primary cerebellar degeneration. Orthologous to human SIL1 (SIL1 nucleotide exchange factor). [provided by Alliance of Genome Resources, Nov 2024]
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    Genomic context

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    See SIL1 in Genome Data Viewer
    Location:
    chromosome: XV
    Exon count:
    1
    Sequence:
    Chromosome: XV; NC_001147.6 (266264..267529, complement)

    Chromosome XV - NC_001147.6Genomic Context describing neighboring genes Neighboring gene glutamate--tRNA ligase MSE1 Neighboring gene Opi10p Neighboring gene 1,3-beta-glucanosyltransferase Neighboring gene uncharacterized protein

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001147.6

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. HspBP1, a homologue of the yeast Fes1 and Sls1 proteins, is an Hsc70 nucleotide exchange factor. Kabani M, et al. FEBS Lett, 2002 Nov 6. PMID 12417338
    2. Structural analysis of the Sil1-Bip complex reveals the mechanism for Sil1 to function as a nucleotide-exchange factor. Yan M, et al. Biochem J, 2011 Sep 15. PMID 21675960
    3. An unexpected role for the yeast nucleotide exchange factor Sil1 as a reductant acting on the molecular chaperone BiP. Siegenthaler KD, et al. Elife, 2017 Mar 3. PMID 28257000, Free PMC Article
    4. Sls1p stimulates Sec63p-mediated activation of Kar2p in a conformation-dependent manner in the yeast endoplasmic reticulum. Kabani M, et al. Mol Cell Biol, 2000 Sep. PMID 10958688, Free PMC Article
    5. Molecular genetics of serine and threonine catabolism in Saccharomyces cerevisiae. Petersen JG, et al. Genetics, 1988 Jul. PMID 2841185, Free PMC Article

    See all (42) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Reductive stress in the endoplasmic reticulum (ER) inhibits the Ost3-dependent N-glycosylation of Sil1, which regulates specific BiP functions appropriate to the needs of the ER under reductive stress.
      Title: Diminished Ost3-dependent N-glycosylation of the BiP nucleotide exchange factor Sil1 is an adaptive response to reductive ER stress.
    2. Here the authors demonstrate that BiP's nucleotide exchange factor - Sil1 - can reverse BiP cysteine oxidation.
      Title: An unexpected role for the yeast nucleotide exchange factor Sil1 as a reductant acting on the molecular chaperone BiP.
    3. Mutation of the Sil1 residues involved in binding the Bip ATPase domain compromise the binding affinity of Sil1 to Bip, and these Sil1 mutants also abolish the ability to stimulate the ATPase activity of Bip.
      Title: Structural analysis of the Sil1-Bip complex reveals the mechanism for Sil1 to function as a nucleotide-exchange factor.
    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 adenyl-nucleotide exchange factor activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables adenyl-nucleotide exchange factor activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables adenyl-nucleotide exchange factor activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in SRP-dependent cotranslational protein targeting to membrane, translocation IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in protein transport IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    located_in endoplasmic reticulum HDA PubMed 
    is_active_in endoplasmic reticulum IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in endoplasmic reticulum IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in endoplasmic reticulum lumen IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    Sil1p
    NP_014611.1
    • Nucleotide exchange factor for the ER lumenal Hsp70 chaperone Kar2p; required for protein translocation into the endoplasmic reticulum (ER); homolog of Yarrowia lipolytica SLS1; GrpE-like 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_001147.6 Reference assembly

      Range
      266264..267529 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001183285.1 → NP_014611.1  TPA: Sil1p [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_014611.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6W234, Q08199, Q6B1H9
      UniProtKB/TrEMBL
      B3LJ26, C7GK01, C8ZHT3, N1NWR5
      Conserved Domains (1) summary
      pfam16782
      Location:123 → 421
      SIL1; Nucleotide exchange factor SIL1
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    Q08199.1

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