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    SSA1 Hsp70 family ATPase SSA1 [ Saccharomyces cerevisiae S288C ]

    Gene ID: 851259, updated on 9-Dec-2024

    Summary

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    Official Symbol
    SSA1
    Official Full Name
    Hsp70 family ATPase SSA1
    Primary source
    SGD:S000000004
    Locus tag
    YAL005C
    See related
    AllianceGenome:SGD:S000000004; FungiDB:YAL005C; VEuPathDB:YAL005C
    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
    YG100
    Summary
    Enables ATP hydrolysis activity; tRNA binding activity; and unfolded protein binding activity. Involved in several processes, including establishment of protein localization to organelle; gene expression; and protein-containing complex disassembly. Located in fungal-type cell wall; fungal-type vacuole membrane; and nucleus. Human ortholog(s) of this gene implicated in Parkinson's disease and renal hypertension. Orthologous to human HSPA8 (heat shock protein family A (Hsp70) member 8). [provided by Alliance of Genome Resources, Dec 2024]
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    Genomic context

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    See SSA1 in Genome Data Viewer
    Location:
    chromosome: I
    Exon count:
    1
    Sequence:
    Chromosome: I; NC_001133.9 (139503..141431, complement)

    Chromosome I - NC_001133.9Genomic Context describing neighboring genes Neighboring gene Erp2p Neighboring gene tRNA-Pro Neighboring gene translation elongation factor 1 subunit beta Neighboring gene ncRNA Neighboring gene CORVET complex membrane-binding subunit VPS8

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001133.9

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Using steered molecular dynamics to study the interaction between ADP and the nucleotide-binding domain of yeast Hsp70 protein Ssa1. Xue YL, et al. J Comput Aided Mol Des, 2018 Nov. PMID 30392073
    2. Using steered molecular dynamics to predict and assess Hsp70 substrate-binding domain mutants that alter prion propagation. Xu L, et al. PLoS Comput Biol, 2013. PMID 23382668, Free PMC Article
    3. Targeting of aminopeptidase I to the yeast vacuole is mediated by Ssa1p, a cytosolic member of the 70-kDa stress protein family. Silles E, et al. J Biol Chem, 2000 Nov 3. PMID 10903313
    4. Primate chaperones Hsc70 (constitutive) and Hsp70 (induced) differ functionally in supporting growth and prion propagation in Saccharomyces cerevisiae. Tutar Y, et al. Genetics, 2006 Feb. PMID 16299395, Free PMC Article
    5. The β6/β7 region of the Hsp70 substrate-binding domain mediates heat-shock response and prion propagation. Xu L, et al. Cell Mol Life Sci, 2018 Apr. PMID 29124308, Free PMC Article

    See all (515) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Effects of HSP70 chaperones Ssa1 and Ssa2 on Ste5 scaffold and the mating mitogen-activated protein kinase (MAPK) pathway in Saccharomyces cerevisiae.
      Title: Effects of HSP70 chaperones Ssa1 and Ssa2 on Ste5 scaffold and the mating mitogen-activated protein kinase (MAPK) pathway in Saccharomyces cerevisiae.
    2. Ydj1 interaction at nucleotide-binding-domain of yeast Ssa1 impacts Hsp90 collaboration and client maturation.
      Title: Ydj1 interaction at nucleotide-binding-domain of yeast Ssa1 impacts Hsp90 collaboration and client maturation.
    3. Oxidation of two cysteines within yeast Hsp70 impairs proteostasis while directly triggering an Hsf1-dependent cytoprotective response.
      Title: Oxidation of two cysteines within yeast Hsp70 impairs proteostasis while directly triggering an Hsf1-dependent cytoprotective response.
    4. The APE2 Exonuclease Is a Client of the Hsp70-Hsp90 Axis in Yeast and Mammalian Cells.
      Title: The APE2 Exonuclease Is a Client of the Hsp70-Hsp90 Axis in Yeast and Mammalian Cells.
    5. Differential role of cytosolic Hsp70s in longevity assurance and protein quality control.
      Title: Differential role of cytosolic Hsp70s in longevity assurance and protein quality control.
    6. Interdomain communication suppressing high intrinsic ATPase activity of Sse1 is essential for its co-disaggregase activity with Ssa1.
      Title: Interdomain communication suppressing high intrinsic ATPase activity of Sse1 is essential for its co-disaggregase activity with Ssa1.
    7. The extent of Ssa1/Ssa2 Hsp70 chaperone involvement in nuclear protein quality control degradation varies with the substrate.
      Title: The extent of Ssa1/Ssa2 Hsp70 chaperone involvement in nuclear protein quality control degradation varies with the substrate.
    8. Activity of the yeast cytoplasmic Hsp70 nucleotide-exchange factor Fes1 is regulated by reversible methionine oxidation.
      Title: Activity of the yeast cytoplasmic Hsp70 nucleotide-exchange factor Fes1 is regulated by reversible methionine oxidation.
    9. Growth-Regulated Hsp70 Phosphorylation Regulates Stress Responses and Prion Maintenance.
      Title: Growth-Regulated Hsp70 Phosphorylation Regulates Stress Responses and Prion Maintenance.
    10. Yeast Hsp90 and Hsp70 directly interact through regions homologous to those of E. coli Hsp90Ec and DnaK. Hsp82 and Ssa1 residues directly interact.
      Title: Intermolecular Interactions between Hsp90 and Hsp70.
    Submit: New GeneRIF Correction See all GeneRIFs (56)

    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 ATP hydrolysis activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables ATP hydrolysis activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables ATP-dependent protein folding chaperone IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables heat shock protein binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables protein folding chaperone IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables tRNA binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables unfolded protein binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in SRP-dependent cotranslational protein targeting to membrane, translocation IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in cellular response to heat IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in chaperone cofactor-dependent protein refolding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in clathrin coat disassembly IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in cytoplasmic translation IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in mitochondria-associated ubiquitin-dependent protein catabolic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in proteasome-mediated ubiquitin-dependent protein catabolic process IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    involved_in proteasome-mediated ubiquitin-dependent protein catabolic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in protein folding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in protein import into nucleus IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in protein import into nucleus IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    involved_in protein polyubiquitination IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in protein refolding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in protein refolding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in protein targeting to mitochondrion IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in stress granule disassembly IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in cytoplasm HDA PubMed 
    is_active_in cytoplasm IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in cytoplasm IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in cytosol HDA PubMed 
    is_active_in cytosol IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in extracellular region IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in fungal-type cell wall IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in fungal-type vacuole membrane IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in nucleus HDA PubMed 
    is_active_in nucleus IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in nucleus IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in plasma membrane HDA PubMed 
    is_active_in plasma membrane IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  

    General protein information

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    Preferred Names
    Hsp70 family ATPase SSA1
    NP_009396.2
    • ATPase involved in protein folding and NLS-directed nuclear transport; HSP70 family member; required for ubiquitin-dependent degradation of short-lived proteins; forms a chaperone complex with Ydj1p; localizes to the nucleus, cytoplasm and cell wall; unique functional specificity in the propagation of yeast [URE3] prions and vacuolar-mediated degradation of gluconeogenic enzymes; general targeting factor of Hsp104p to prion fibrils; 98% identity with paralog Ssa2p

    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_001133.9 Reference assembly

      Range
      139503..141431 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001178151.1 → NP_009396.2  TPA: Hsp70 family ATPase SSA1 [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_009396.2

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6VPL2, P10591
      UniProtKB/TrEMBL
      A7A0G3, B3LUU3, G2W8M6, G9BX85
      Conserved Domains (1) summary
      PTZ00009
      Location:4 → 642
      PTZ00009; heat shock 70 kDa protein; Provisional
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P10591.4

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