U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

TCP1 chaperonin-containing T-complex alpha subunit TCP1 [ Saccharomyces cerevisiae S288C ]

Gene ID: 851798, updated on 23-Apr-2026
Official Symbol
TCP1
Official Full Name
chaperonin-containing T-complex alpha subunit TCP1
Primary source
SGD:S000002620
Locus tag
YDR212W
See related
AllianceGenome:SGD:S000002620; FungiDB:YDR212W; VEuPathDB:YDR212W
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
CCT1
Summary
Enables unfolded protein binding activity. Involved in protein folding. Located in plasma membrane. Part of chaperonin-containing T-complex. Orthologous to human TCP1 (t-complex 1). [provided by Alliance of Genome Resources, Jul 2025]
Orthologs
Try the new Gene page
Try the new Transcripts and proteins table
See TCP1 in Genome Data Viewer
Location:
chromosome: IV
Exon count:
1
Sequence:
Chromosome: IV; NC_001136.10 (887232..888911)

Chromosome IV - NC_001136.10Genomic Context describing neighboring genes Neighboring gene tRNA-Ile Neighboring gene translation initiation factor eIF2B catalytic subunit epsilon Neighboring gene Upc2p Neighboring gene Aha1p

Genomic Sequence:
NC_001136.10
Products Interactant Other Gene Complex Source Pubs Description

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 protein binding IPI
Inferred from Physical Interaction
more info
PubMed 
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 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
 
located_in plasma membrane HDA PubMed 
Preferred Names
chaperonin-containing T-complex alpha subunit TCP1
NP_010498.1
  • Alpha subunit of chaperonin-containing T-complex; complex mediates protein folding in the cytosol; involved in actin cytoskeleton maintenance; overexpression in neurons suppresses formation of pathogenic conformations of huntingtin protein

NEW Try the new Transcript table

Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_001136.10 Reference assembly

    Range
    887232..888911
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001180520.1NP_010498.1  chaperonin-containing T-complex alpha subunit TCP1

    See identical proteins and their annotated locations for NP_010498.1

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    D6VSJ6, P12612
    UniProtKB/TrEMBL
    A6ZYG8, B3LG74, C7GMI5, C8Z5C5, G2WAV8, N1P6L0
    Conserved Domains (1) summary
    cd03335
    Location:17549
    TCP1_alpha; TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha 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 ...