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CCT7 chaperonin-containing T-complex subunit CCT7 [ Saccharomyces cerevisiae S288C ]

Gene ID: 853333, updated on 4-Jan-2025

Summary

Official Symbol
CCT7
Official Full Name
chaperonin-containing T-complex subunit CCT7
Primary source
SGD:S000003647
Locus tag
YJL111W
See related
AllianceGenome:SGD:S000003647; FungiDB:YJL111W; VEuPathDB:YJL111W
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
TCP7
Summary
Enables unfolded protein binding activity. Involved in protein folding. Located in cytoplasm. Part of chaperonin-containing T-complex. Orthologous to human CCT7 (chaperonin containing TCP1 subunit 7). [provided by Alliance of Genome Resources, Jan 2025]
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Genomic context

See CCT7 in Genome Data Viewer
Location:
chromosome: X
Exon count:
1
Sequence:
Chromosome: X; NC_001142.9 (207877..209529)

Chromosome X - NC_001142.9Genomic Context describing neighboring genes Neighboring gene tRNA-Asp Neighboring gene Mdv1p Neighboring gene Gzf3p Neighboring gene snoRNA-binding rRNA-processing protein UTP10

Pathways from PubChem

Interactions

Products Interactant Other Gene Complex Source Pubs Description

General gene information

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

Preferred Names
chaperonin-containing T-complex subunit CCT7
NP_012424.1
  • Subunit of the cytosolic chaperonin Cct ring complex; related to Tcp1p, required for the assembly of actin and tubulins in vivo; mutant has increased aneuploidy tolerance

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
    207877..209529
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001181544.1NP_012424.1  TPA: chaperonin-containing T-complex subunit CCT7 [Saccharomyces cerevisiae S288C]

    See identical proteins and their annotated locations for NP_012424.1

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    D6VW73, P42943
    UniProtKB/TrEMBL
    A6ZQL6, B3LQ04, B5VL62, C7GR05, C8ZBA6, G2WGQ8, N1P1K8
    Conserved Domains (1) summary
    cd03340
    Location:9529
    TCP1_eta; TCP-1 (CTT or eukaryotic type II) chaperonin family, eta 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 (GroEL), ...