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LHS1 Hsp70 family chaperone LHS1 [ Saccharomyces cerevisiae S288C ]

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

Summary

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Gene symbol
LHS1
Gene description
Hsp70 family chaperone LHS1
Primary source
FungiDB:YKL073W
Locus tag
YKL073W
See related
SGD:S000001556; AllianceGenome:SGD:S000001556; 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 posttranslational 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, Apr 2022]
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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. 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
  2. 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
  3. Nucleotide binding by Lhs1p is essential for its nucleotide exchange activity and for function in vivo. de Keyzer J, et al. J Biol Chem, 2009 Nov 13. PMID 19759005, Free PMC Article
  4. 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
  5. 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

See all (72) 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 protein folding chaperone 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 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 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
    A0A8H4BZ18, 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

Gene LinkOut

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