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    SBA1 Hsp90 cochaperone SBA1 [ Saccharomyces cerevisiae S288C ]

    Gene ID: 853743, updated on 13-Apr-2024

    Summary

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    Gene symbol
    SBA1
    Gene description
    Hsp90 cochaperone SBA1
    Primary source
    SGD:S000001600
    Locus tag
    YKL117W
    See related
    AllianceGenome:SGD:S000001600
    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
    CST18
    Summary
    Enables chaperone binding activity. Involved in negative regulation of DNA binding activity; protein folding; and regulation of DNA biosynthetic process. Located in cytoplasm and nucleus. Orthologous to several human genes including PTGES3 (prostaglandin E synthase 3). [provided by Alliance of Genome Resources, Apr 2022]
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    Genomic context

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    Location:
    chromosome: XI
    Exon count:
    1
    Sequence:
    Chromosome: XI; NC_001143.9 (220324..220974)

    Chromosome XI - NC_001143.9Genomic Context describing neighboring genes Neighboring gene Vph2p Neighboring gene tRNA-Ala Neighboring gene serine/threonine protein kinase PRR1 Neighboring gene DNA-(apurinic or apyrimidinic site) lyase APN1

    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. Characterization of orchardgrass p23, a flowering plant Hsp90 cohort protein. Cha JY, et al. Cell Stress Chaperones, 2009 May. PMID 18800239, Free PMC Article
    2. Monitoring the Conformation of the Sba1/Hsp90 Complex in the Presence of Nucleotides with Mn(II)-Based Double Electron-Electron Resonance. Giannoulis A, et al. J Phys Chem Lett, 2021 Dec 30. PMID 34928609, Free PMC Article
    3. Importance of cycle timing for the function of the molecular chaperone Hsp90. Zierer BK, et al. Nat Struct Mol Biol, 2016 Nov. PMID 27723736, Free PMC Article
    4. Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex. Ali MM, et al. Nature, 2006 Apr 20. PMID 16625188, Free PMC Article
    5. Cooperation of heat shock protein 90 and p23 in aryl hydrocarbon receptor signaling. Cox MB, et al. Cell Stress Chaperones, 2004 Mar. PMID 15270073, Free PMC Article

    See all (79) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Monitoring the Conformation of the Sba1/Hsp90 Complex in the Presence of Nucleotides with Mn(II)-Based Double Electron-Electron Resonance.
      Title: Monitoring the Conformation of the Sba1/Hsp90 Complex in the Presence of Nucleotides with Mn(II)-Based Double Electron-Electron Resonance.
    2. Data support a model in which p23 molecular chaperone and GCN5 regulate diverse multistep pathways by controlling the longevity of protein-DNA complexes.
      Title: The p23 molecular chaperone and GCN5 acetylase jointly modulate protein-DNA dynamics and open chromatin status.
    3. Structure-function analysis suggests that Sba1p undergoes structural rearrangements upon binding Hsp90, and the large size of the p23/Sba1p-Hsp90 interaction surface facilitates maintenance of high affinity despite sequence divergence during evolution.
      Title: p23/Sba1p protects against Hsp90 inhibitors independently of its intrinsic chaperone activity.
    4. crystal structure of full-length yeast Hsp90 in complex with an ATP analogue and the co-chaperone p23/Sba1
      Title: Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex.
    5. SBA1 is required for teleomere length maintenance. It can moderate telomerase DNA binding and extension activities in vitro.
      Title: The p23 molecular chaperone promotes functional telomerase complexes through DNA dissociation.
    Submit: New GeneRIF Correction

    Pathways from PubChem

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    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 Hsp90 protein binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables Hsp90 protein binding 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 IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables protein-folding chaperone binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in chaperone-mediated protein complex assembly IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in negative regulation of DNA binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in positive regulation of telomere maintenance via telomerase IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in positive regulation of telomere maintenance via telomerase IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in protein folding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in protein folding IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in protein folding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in cytoplasm IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    is_active_in cytosol IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    is_active_in nucleus IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in nucleus IDA
    Inferred from Direct Assay
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    Hsp90 cochaperone SBA1
    NP_012805.1
    • Co-chaperone that binds and regulates Hsp90 family chaperones; plays a role in determining prion variants; important for pp60v-src activity in yeast; homologous to the mammalian p23 proteins, and like p23 can regulate telomerase activity; protein abundance increases in response to DNA replication stress

    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
      220324..220974
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001179683.1 → NP_012805.1  TPA: Hsp90 cochaperone SBA1 [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_012805.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6VXH2, P28707
      UniProtKB/TrEMBL
      A0A6A5PS88, G2WHR8, N1NZR4
      Conserved Domains (1) summary
      cd06465
      Location:8 → 129
      p23_hB-ind1_like; p23_like domain found in human (h) butyrate-induced transcript 1 (B-ind1) and similar proteins. hB-ind1 participates in signaling by the small GTPase Rac1. It binds to Rac1 and enhances different Rac1 effects including activation of nuclear factor (NF) ...
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P28707.3

    Gene LinkOut

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