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cct3 chaperonin-containing T-complex gamma subunit Cct3 [ Schizosaccharomyces pombe (fission yeast) ]

Gene ID: 2540567, updated on 22-Jun-2024

Summary

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Gene symbol
cct3
Gene description
chaperonin-containing T-complex gamma subunit Cct3
Locus tag
SPOM_SPBC1A4.08C
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Schizosaccharomyces pombe (strain: 972h-)
Lineage
Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; Schizosaccharomyces
Old locus tag
SPBC1A4.08c
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Genomic context

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See cct3 in Genome Data Viewer
Location:
chromosome: II
Exon count:
3
Sequence:
Chromosome: II; NC_003423.3 (1990416..1992476, complement)

Chromosome II - NC_003423.3Genomic Context describing neighboring genes Neighboring gene ncRNA Neighboring gene ncRNA Neighboring gene U3 snoRNP-associated protein Sof1 Neighboring gene ncRNA Neighboring gene uncharacterized protein Neighboring gene ncRNA Neighboring gene ncRNA Neighboring gene pseudouridine synthase

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_003423.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. Chromatin Central: towards the comparative proteome by accurate mapping of the yeast proteomic environment. Shevchenko A, et al. Genome Biol, 2008. PMID 19040720, Free PMC Article
  2. SIN-inhibitory phosphatase complex promotes Cdc11p dephosphorylation and propagates SIN asymmetry in fission yeast. Singh NS, et al. Curr Biol, 2011 Dec 6. PMID 22119525, Free PMC Article
  3. Characterization of Mug33 reveals complementary roles for actin cable-dependent transport and exocyst regulators in fission yeast exocytosis. Snaith HA, et al. J Cell Sci, 2011 Jul 1. PMID 21652630, Free PMC Article
  4. Proximity-dependent biotinylation mediated by TurboID to identify protein-protein interaction networks in yeast. Larochelle M, et al. J Cell Sci, 2019 May 31. PMID 31064814
  5. Transcription and chromatin-based surveillance mechanism controls suppression of cryptic antisense transcription. Heo DH, et al. Cell Rep, 2021 Sep 7. PMID 34496258, Free PMC Article

See all (12) 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 PomBase

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
  
Process Evidence Code Pubs
involved_in protein folding IBA
Inferred from Biological aspect of Ancestor
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 
is_active_in cytoskeleton ISO
Inferred from Sequence Orthology
more info
  
is_active_in cytosol HDA PubMed 
is_active_in nucleus HDA PubMed 

General protein information

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Preferred Names
chaperonin-containing T-complex gamma subunit Cct3

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_003423.3 Reference assembly

    Range
    1990416..1992476 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001021713.3 → NP_595810.1  chaperonin-containing T-complex gamma subunit Cct3 [Schizosaccharomyces pombe]

    See identical proteins and their annotated locations for NP_595810.1

    Status: PROVISIONAL

    UniProtKB/Swiss-Prot
    O74341
    Conserved Domains (2) summary
    cd03337
    Location:4 → 522
    TCP1_gamma; TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma 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 ...
    TIGR02344
    Location:4 → 526
    chap_CCT_gamma; T-complex protein 1, gamma subunit
Nucleotide Protein
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