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

Gene ID: 853527, updated on 9-Dec-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, Dec 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. 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
  5. Trivalent arsenic inhibits the functions of chaperonin complex. Pan X, et al. Genetics, 2010 Oct. PMID 20660648, Free PMC Article

See all (78) 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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