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    CCT8 chaperonin-containing T-complex subunit CCT8 [ Saccharomyces cerevisiae S288C ]

    Gene ID: 853447, updated on 18-Sep-2024

    Summary

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    Official Symbol
    CCT8
    Official Full Name
    chaperonin-containing T-complex subunit CCT8
    Primary source
    SGD:S000003545
    Locus tag
    YJL008C
    See related
    AllianceGenome:SGD:S000003545; FungiDB:YJL008C; VEuPathDB:YJL008C
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Saccharomyces cerevisiae S288C (strain: S288C)
    Lineage
    Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
    Summary
    Enables unfolded protein binding activity. Involved in protein folding. Located in cytoplasm. Part of chaperonin-containing T-complex. Orthologous to human CCT8 (chaperonin containing TCP1 subunit 8). [provided by Alliance of Genome Resources, Apr 2022]
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    Genomic context

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    See CCT8 in Genome Data Viewer
    Location:
    chromosome: X
    Exon count:
    1
    Sequence:
    Chromosome: X; NC_001142.9 (419957..421663, complement)

    Chromosome X - NC_001142.9Genomic Context describing neighboring genes Neighboring gene tRNA-Trp Neighboring gene RNA-binding RNA processing protein NOP9 Neighboring gene uncharacterized protein Neighboring gene tRNA-Met Neighboring gene Ctk2p

    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. Disruption of six open reading frames on chromosome X of Saccharomyces cerevisiae reveals a cluster of four essential genes. Esser K, et al. Yeast, 1999 Jul. PMID 10407272
    2. Transcriptional regulation of protein complexes within and across species. Tan K, et al. Proc Natl Acad Sci U S A, 2007 Jan 23. PMID 17227853, 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. An ensemble of cryo-EM structures of TRiC reveal its conformational landscape and subunit specificity. Jin M, et al. Proc Natl Acad Sci U S A, 2019 Sep 24. PMID 31492816, 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 (88) 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 HDA 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 CCT8
    NP_012526.1
    • 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
      419957..421663 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001181442.2 → NP_012526.1  TPA: chaperonin-containing T-complex subunit CCT8 [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_012526.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6VWG8, P47079
      UniProtKB/TrEMBL
      A6ZPW0, C7GV41, C8ZBK3, N1P3A5
      Conserved Domains (1) summary
      TIGR02346
      Location:9 → 559
      chap_CCT_theta; T-complex protein 1, theta subunit
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P47079.1

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