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    HSP10 Hsp10p [ Saccharomyces cerevisiae S288C ]

    Gene ID: 854185, updated on 28-Oct-2024

    Summary

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    Official Symbol
    HSP10
    Official Full Name
    Hsp10p
    Primary source
    SGD:S000005546
    Locus tag
    YOR020C
    See related
    AllianceGenome:SGD:S000005546; FungiDB:YOR020C; VEuPathDB:YOR020C
    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
    CPN10
    Summary
    Enables protein-folding chaperone binding activity and unfolded protein binding activity. Involved in chaperone-mediated protein complex assembly; protein import into mitochondrial intermembrane space; and protein refolding. Located in mitochondrial matrix. Orthologous to human HSPE1 (heat shock protein family E (Hsp10) member 1). [provided by Alliance of Genome Resources, Oct 2024]
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    Genomic context

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    See HSP10 in Genome Data Viewer
    Location:
    chromosome: XV
    Exon count:
    1
    Sequence:
    Chromosome: XV; NC_001147.6 (370524..370844, complement)

    Chromosome XV - NC_001147.6Genomic Context describing neighboring genes Neighboring gene Rod1p Neighboring gene uncharacterized protein Neighboring gene Mco10p Neighboring gene protein-arginine N-methyltransferase SFM1

    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. Role of the chaperonin cofactor Hsp10 in protein folding and sorting in yeast mitochondria. Höhfeld J, et al. J Cell Biol, 1994 Jul. PMID 7913473, Free PMC Article
    2. Cloning and disruption of the gene encoding yeast mitochondrial chaperonin 10, the homolog of E. coli groES. Rospert S, et al. FEBS Lett, 1993 Dec 13. PMID 7903252
    3. SCS1, a multicopy suppressor of hsp60-ts mutant alleles, does not encode a mitochondrially targeted protein. Shu Y, et al. Mol Cell Biol, 1995 Oct. PMID 7565713, Free PMC Article
    4. Significance of chaperonin 10-mediated inhibition of ATP hydrolysis by chaperonin 60. Dubaquié Y, et al. Proc Natl Acad Sci U S A, 1997 Aug 19. PMID 9256426, Free PMC Article
    5. Identification and functional analysis of chaperonin 10, the groES homolog from yeast mitochondria. Rospert S, et al. Proc Natl Acad Sci U S A, 1993 Dec 1. PMID 7902576, Free PMC Article

    See all (56) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. coupling to Hsp10 recruits mtHsp70 to mediate the biogenesis of the heptameric Hsp60 rings
      Title: Mitochondrial heat shock protein (Hsp) 70 and Hsp10 cooperate in the formation of Hsp60 complexes.
    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 IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables metal ion binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables protein folding chaperone IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables protein-folding chaperone binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables protein-folding chaperone binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables unfolded protein binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables unfolded protein binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in chaperone cofactor-dependent protein refolding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in chaperone-mediated protein complex assembly IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in protein folding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in protein folding IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in protein import into mitochondrial intermembrane space IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in protein refolding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in protein refolding IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    is_active_in mitochondrial matrix IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in mitochondrial matrix IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in mitochondrial matrix IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in mitochondrion HDA PubMed 
    is_active_in mitochondrion IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in mitochondrion IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    Hsp10p
    NP_014663.1
    • Mitochondrial matrix co-chaperonin; inhibits the ATPase activity of Hsp60p, a mitochondrial chaperonin; involved in protein folding and sorting in the mitochondria; 10 kD heat shock protein with similarity to E. coli groES

    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
      370524..370844 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001183439.1 → NP_014663.1  TPA: Hsp10p [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_014663.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6W286, E9P935, P38910
      UniProtKB/TrEMBL
      A6ZNM4, B3LJ74, C7GLF0, C8ZHY2, G2WMQ1, N1NVQ8
      Conserved Domains (1) summary
      cd00320
      Location:10 → 103
      cpn10; Chaperonin 10 Kd subunit (cpn10 or GroES); Cpn10 cooperates with chaperonin 60 (cpn60 or GroEL), an ATPase, to assist the folding and assembly of proteins and is found in eubacterial cytosol, as well as in the matrix of mitochondria and chloroplasts. It ...
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P38910.1

    Gene LinkOut

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