U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

Links from Nucleotide

    • Showing Current items.

    cct-5 T-complex protein 1 subunit epsilon [ Caenorhabditis elegans ]

    Gene ID: 175588, updated on 9-Dec-2024

    Summary

    Official Symbol
    cct-5
    Official Full Name
    T-complex protein 1 subunit epsilon
    Primary source
    WormBase:WBGene00000380
    Locus tag
    CELE_C07G2.3
    See related
    AllianceGenome:WB:WBGene00000380
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Caenorhabditis elegans (strain: Bristol N2)
    Lineage
    Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis
    Summary
    Predicted to enable unfolded protein binding activity. Predicted to be involved in protein folding. Part of chaperonin-containing T-complex. Orthologous to human CCT5 (chaperonin containing TCP1 subunit 5). [provided by Alliance of Genome Resources, Dec 2024]
    NEW
    Try the new Gene table
    Try the new Transcript table

    Genomic context

    See cct-5 in Genome Data Viewer
    Location:
    chromosome: III
    Exon count:
    8
    Sequence:
    Chromosome: III; NC_003281.10 (4499188..4508114, complement)

    Chromosome III - NC_003281.10Genomic Context describing neighboring genes Neighboring gene Transcription factor atf-7 Neighboring gene ncRNA Neighboring gene Uncharacterized protein Neighboring gene Protein kinase domain-containing protein Neighboring gene ncRNA

    Pathways from PubChem

    Interactions

    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

    Markers

    Gene Ontology Provided by WormBase

    Function Evidence Code Pubs
    enables ATP binding 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 IEA
    Inferred from Electronic Annotation
    more info
     
    enables unfolded protein binding ISS
    Inferred from Sequence or Structural Similarity
    more info
    PubMed 
    Process Evidence Code Pubs
    involved_in protein folding IBA
    Inferred from Biological aspect of Ancestor
    more info
     
    involved_in protein folding IEA
    Inferred from Electronic Annotation
    more info
     
    involved_in protein folding ISS
    Inferred from Sequence or Structural Similarity
    more info
    PubMed 
    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
     
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
     

    General protein information

    Preferred Names
    T-complex protein 1 subunit epsilon
    NP_741117.1
    • Confirmed by transcript evidence

    NCBI Reference Sequences (RefSeq)

    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_003281.10 Reference assembly

      Range
      4499188..4508114 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_171104.7NP_741117.1  T-complex protein 1 subunit epsilon [Caenorhabditis elegans]

      See identical proteins and their annotated locations for NP_741117.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      P47209
      Conserved Domains (2) summary
      cd03339
      Location:11534
      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 ...
      pfam00118
      Location:45532
      Cpn60_TCP1; TCP-1/cpn60 chaperonin family