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    LHS1 Hsp70 family chaperone LHS1 [ Saccharomyces cerevisiae S288C ]

    Gene ID: 853789, updated on 9-Dec-2024

    Summary

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    Official Symbol
    LHS1
    Official Full Name
    Hsp70 family chaperone LHS1
    Primary source
    SGD:S000001556
    Locus tag
    YKL073W
    See related
    AllianceGenome:SGD:S000001556; FungiDB:YKL073W; VEuPathDB:YKL073W
    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
    CER1; SSI1
    Summary
    Enables ATP binding activity; adenyl-nucleotide exchange factor activity; and unfolded protein binding activity. Involved in post-translational protein targeting to membrane, translocation and response to unfolded protein. Located in endoplasmic reticulum lumen. Human ortholog(s) of this gene implicated in immunodeficiency 59. Orthologous to human HYOU1 (hypoxia up-regulated 1). [provided by Alliance of Genome Resources, Dec 2024]
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    Genomic context

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    See LHS1 in Genome Data Viewer
    Location:
    chromosome: XI
    Exon count:
    1
    Sequence:
    Chromosome: XI; NC_001143.9 (296430..299075)

    Chromosome XI - NC_001143.9Genomic Context describing neighboring genes Neighboring gene Aan1p Neighboring gene Mud2p Neighboring gene Stb6p Neighboring gene tRNA-Trp

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001143.9

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Transient ER retention as stress response: conformational repair of heat-damaged proteins to secretion-competent structures. Saris N, et al. J Cell Sci, 1998 Jun. PMID 9580565
    2. Cer1p functions as a molecular chaperone in the endoplasmic reticulum of Saccharomyces cerevisiae. Hamilton TG, et al. Mol Cell Biol, 1999 Aug. PMID 10409721, Free PMC Article
    3. A novel Hsp70 of the yeast ER lumen is required for the efficient translocation of a number of protein precursors. Craven RA, et al. EMBO J, 1996 Jun 3. PMID 8654361, Free PMC Article
    4. SSI1 encodes a novel Hsp70 of the Saccharomyces cerevisiae endoplasmic reticulum. Baxter BK, et al. Mol Cell Biol, 1996 Nov. PMID 8887673, Free PMC Article
    5. The Hsp70 homologue Lhs1p is involved in a novel function of the yeast endoplasmic reticulum, refolding and stabilization of heat-denatured protein aggregates. Saris N, et al. J Cell Biol, 1997 May 19. PMID 9151684, Free PMC Article

    See all (79) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. The data indicate that the Lhs1 chaperone selectively recognizes an immature form of alphaENaC, one which has failed to correctly assemble with the other channel subunits via its transmembrane domain.
      Title: Interactions between intersubunit transmembrane domains regulate the chaperone-dependent degradation of an oligomeric membrane protein.
    2. Interactions between Kar2p and its nucleotide exchange factors Sil1p and Lhs1p are mechanistically distinct
      Title: Interactions between Kar2p and its nucleotide exchange factors Sil1p and Lhs1p are mechanistically distinct.
    3. compare Grp170 Lhs1 with Hsp110 Sse1 and find that residues important for Sse1 nucleotide exchange factor (NEF) activity are conserved in Lhs1 and that mutations in these residues in Lhs1 compromise NEF activity
      Title: The endoplasmic reticulum Grp170 acts as a nucleotide exchange factor of Hsp70 via a mechanism similar to that of the cytosolic Hsp110.
    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 ATP binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables ATP binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables ATP binding IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables ATP hydrolysis activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables ATP-dependent H2AZ histone chaperone activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables ATP-dependent H3-H4 histone complex chaperone activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables ATP-dependent protein folding chaperone IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables DNA clamp loader activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    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 chromatin extrusion motor activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables cohesin loader activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables hydrolase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables unfolded protein binding IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in chromatin looping IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in chromatin remodeling IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in post-translational protein targeting to membrane, translocation IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in protein folding IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in response to unfolded protein IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in endoplasmic reticulum HDA PubMed 
    located_in endoplasmic reticulum IEA
    Inferred from Electronic Annotation
    more info
    		  
    part_of endoplasmic reticulum chaperone complex IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in endoplasmic reticulum lumen IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in endoplasmic reticulum lumen IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    Hsp70 family chaperone LHS1
    NP_012850.1
    • Molecular chaperone of the endoplasmic reticulum lumen; involved in polypeptide translocation and folding; nucleotide exchange factor for the ER lumenal Hsp70 chaperone Kar2p; regulated by the unfolded protein response pathway

    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_001143.9 Reference assembly

      Range
      296430..299075
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001179639.1 → NP_012850.1  TPA: Hsp70 family chaperone LHS1 [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_012850.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6VXL3, P36016
      UniProtKB/TrEMBL
      A6ZZP2, C8ZC99
      Conserved Domains (2) summary
      cd10230
      Location:23 → 430
      HYOU1-like_NBD; Nucleotide-binding domain of human HYOU1 and similar proteins
      COG1196
      Location:581 → 737
      Smc; Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P36016.1

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