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    CCT5 chaperonin-containing T-complex subunit CCT5 [ Saccharomyces cerevisiae S288C ]

    Gene ID: 853527, updated on 2-Nov-2024

    Summary

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    Official Symbol
    CCT5
    Official Full Name
    chaperonin-containing T-complex subunit CCT5
    Primary source
    SGD:S000003825
    Locus tag
    YJR064W
    See related
    AllianceGenome:SGD:S000003825; FungiDB:YJR064W; VEuPathDB:YJR064W
    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
    TCP5
    Summary
    Enables unfolded protein binding activity. Involved in protein folding. Part of chaperonin-containing T-complex. Used to study Bardet-Biedl syndrome 10. Orthologous to human CCT5 (chaperonin containing TCP1 subunit 5). [provided by Alliance of Genome Resources, Nov 2024]
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    Genomic context

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    See CCT5 in Genome Data Viewer
    Location:
    chromosome: X
    Exon count:
    1
    Sequence:
    Chromosome: X; NC_001142.9 (555914..557602)

    Chromosome X - NC_001142.9Genomic Context describing neighboring genes Neighboring gene amidase Neighboring gene DNA-directed RNA polymerase I core subunit RPA12 Neighboring gene actin-related protein 3 Neighboring gene phosphatidylinositol kinase-related protein kinase TOR1

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001142.9

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. A novel function of the human chaperonin CCT epsilon subunit in yeast. Nikawa J, et al. Biosci Biotechnol Biochem, 2012. PMID 22232265
    2. Development of a yeast internal-subunit eGFP labeling strategy and its application in subunit identification in eukaryotic group II chaperonin TRiC/CCT. Zang Y, et al. Sci Rep, 2018 Feb 5. PMID 29403048, Free PMC Article
    3. Analysis of mutationally altered forms of the Cct6 subunit of the chaperonin from Saccharomyces cerevisiae. Lin P, et al. Genetics, 1997 Dec. PMID 9409825, Free PMC Article
    4. Trivalent arsenic inhibits the functions of chaperonin complex. Pan X, et al. Genetics, 2010 Oct. PMID 20660648, Free PMC Article
    5. Staggered ATP binding mechanism of eukaryotic chaperonin TRiC (CCT) revealed through high-resolution cryo-EM. Zang Y, et al. Nat Struct Mol Biol, 2016 Dec. PMID 27775711

    See all (77) citations in PubMed

    GeneRIFs: Gene References Into Functions

    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 ATP binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    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 unfolded protein binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables unfolded protein binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables unfolded protein binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in chaperone mediated protein folding independent of cofactor IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in protein folding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in protein folding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in protein folding IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    part_of chaperonin-containing T-complex IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    part_of chaperonin-containing T-complex IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    part_of chaperonin-containing T-complex IEA
    Inferred from Electronic Annotation
    more info
    		  
    part_of chaperonin-containing T-complex IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    chaperonin-containing T-complex subunit CCT5
    NP_012598.1
    • Subunit of the cytosolic chaperonin Cct ring complex; related to Tcp1p, required for the assembly of actin and tubulins in vivo

    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_001142.9 Reference assembly

      Range
      555914..557602
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001181722.1 → NP_012598.1  TPA: chaperonin-containing T-complex subunit CCT5 [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_012598.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6VWN5, P40413
      UniProtKB/TrEMBL
      A6ZQ23, B3LQF2, B5VLL7, C7GMD9, C8ZBL2, G2WH69, N1P3H3
      Conserved Domains (1) summary
      cd03339
      Location:23 → 555
      TCP1_epsilon; TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins ...
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P40413.3

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