CCT4

Protein-coding gene in the species Homo sapiens

CCT4
Identifiers
AliasesCCT4, CCT-DELTA, Cctd, SRB, chaperonin containing TCP1 subunit 4
External IDsOMIM: 605142; MGI: 104689; HomoloGene: 4695; GeneCards: CCT4; OMA:CCT4 - orthologs
Gene location (Human)
Chromosome 2 (human)
Chr.Chromosome 2 (human)[1]
Chromosome 2 (human)
Genomic location for CCT4
Genomic location for CCT4
Band2p15Start61,868,085 bp[1]
End61,888,671 bp[1]
Gene location (Mouse)
Chromosome 11 (mouse)
Chr.Chromosome 11 (mouse)[2]
Chromosome 11 (mouse)
Genomic location for CCT4
Genomic location for CCT4
Band11 A3.2|11 14.25 cMStart22,940,519 bp[2]
End22,953,780 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • gonad

  • ventricular zone

  • parotid gland

  • embryo

  • ganglionic eminence

  • cartilage tissue

  • lactiferous duct

  • epithelium of nasopharynx

  • vulva

  • tibialis anterior muscle
Top expressed in
  • Gonadal ridge

  • abdominal wall

  • primitive streak

  • vas deferens

  • medial ganglionic eminence

  • dermis

  • somite

  • migratory enteric neural crest cell

  • Paneth cell

  • mandibular prominence
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • nucleotide binding
  • protein binding
  • ATP binding
  • protein folding chaperone activity
  • unfolded protein binding
  • RNA binding
Cellular component
  • cell body
  • centrosome
  • cell projection
  • melanosome
  • nucleoplasm
  • microtubule organizing center
  • zona pellucida receptor complex
  • chaperonin-containing T-complex
  • microtubule
  • extracellular exosome
  • cytoskeleton
  • cytoplasm
  • cytosol
Biological process
  • positive regulation of protein localization to Cajal body
  • positive regulation of establishment of protein localization to telomere
  • scaRNA localization to Cajal body
  • protein stabilization
  • positive regulation of telomere maintenance via telomerase
  • toxin transport
  • protein folding
  • positive regulation of telomerase activity
  • positive regulation of telomerase RNA localization to Cajal body
  • binding of sperm to zona pellucida
  • 'de novo' protein folding
  • chaperone-mediated protein folding
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

10575

12464

Ensembl

ENSG00000115484

ENSMUSG00000007739

UniProt

P50991

P80315

RefSeq (mRNA)

NM_006430
NM_001256721

NM_009837

RefSeq (protein)

NP_001243650
NP_006421

NP_033967

Location (UCSC)Chr 2: 61.87 – 61.89 MbChr 11: 22.94 – 22.95 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

T-complex protein 1 subunit delta is a protein that in humans is encoded by the CCT4 gene.[5][6] The CCT4 protein is a component of the TRiC complex.

Interactions

CCT4 has been shown to interact with PPP4C.[7][8]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000115484 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000007739 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Won KA, Schumacher RJ, Farr GW, Horwich AL, Reed SI (Dec 1998). "Maturation of human cyclin E requires the function of eukaryotic chaperonin CCT". Molecular and Cellular Biology. 18 (12): 7584–9. doi:10.1128/mcb.18.12.7584. PMC 109339. PMID 9819444.
  6. ^ "Entrez Gene: CCT4 chaperonin containing TCP1, subunit 4 (delta)".
  7. ^ Chen GI, Tisayakorn S, Jorgensen C, D'Ambrosio LM, Goudreault M, Gingras AC (Oct 2008). "PP4R4/KIAA1622 forms a novel stable cytosolic complex with phosphoprotein phosphatase 4". The Journal of Biological Chemistry. 283 (43): 29273–84. doi:10.1074/jbc.M803443200. PMC 2662017. PMID 18715871.
  8. ^ Gingras AC, Caballero M, Zarske M, Sanchez A, Hazbun TR, Fields S, Sonenberg N, Hafen E, Raught B, Aebersold R (November 2005). "A novel, evolutionarily conserved protein phosphatase complex involved in cisplatin sensitivity". Molecular & Cellular Proteomics. 4 (11): 1725–40. doi:10.1074/mcp.M500231-MCP200. PMID 16085932. S2CID 7531012.

Further reading

  • Kubota H, Hynes G, Carne A, Ashworth A, Willison K (Feb 1994). "Identification of six Tcp-1-related genes encoding divergent subunits of the TCP-1-containing chaperonin". Current Biology. 4 (2): 89–99. Bibcode:1994CBio....4...89K. doi:10.1016/S0960-9822(94)00024-2. PMID 7953530. S2CID 31300131.
  • Wu-Baer F, Lane WS, Gaynor RB (Feb 1996). "Identification of a group of cellular cofactors that stimulate the binding of RNA polymerase II and TRP-185 to human immunodeficiency virus 1 TAR RNA". The Journal of Biological Chemistry. 271 (8): 4201–8. doi:10.1074/jbc.271.8.4201. PMID 8626763.
  • Nabetani A, Hatada I, Morisaki H, Mukai T (June 1996). "Chromosomal assignment and imprinting tests for the mouse delta subunit of the cytosolic chaperonin containing TCP-1 (Cct4) gene to proximal chromosome 11". Genomics. 34 (2): 246–9. doi:10.1006/geno.1996.0276. PMID 8661059.
  • Melki R, Batelier G, Soulié S, Williams RC (May 1997). "Cytoplasmic chaperonin containing TCP-1: structural and functional characterization". Biochemistry. 36 (19): 5817–26. doi:10.1021/bi962830o. PMID 9153422.
  • Llorca O, McCormack EA, Hynes G, Grantham J, Cordell J, Carrascosa JL, Willison KR, Fernandez JJ, Valpuesta JM (December 1999). "Eukaryotic type II chaperonin CCT interacts with actin through specific subunits". Nature. 402 (6762): 693–6. Bibcode:1999Natur.402..693L. doi:10.1038/45294. PMID 10604479. S2CID 4421057.
  • Llorca O, Martín-Benito J, Gómez-Puertas P, Ritco-Vonsovici M, Willison KR, Carrascosa JL, Valpuesta JM (August 2001). "Analysis of the interaction between the eukaryotic chaperonin CCT and its substrates actin and tubulin". Journal of Structural Biology. 135 (2): 205–18. doi:10.1006/jsbi.2001.4359. PMID 11580270.
  • Parissi V, Calmels C, De Soultrait VR, Caumont A, Fournier M, Chaignepain S, Litvak S (Dec 2001). "Functional interactions of human immunodeficiency virus type 1 integrase with human and yeast HSP60". Journal of Virology. 75 (23): 11344–53. doi:10.1128/JVI.75.23.11344-11353.2001. PMC 114720. PMID 11689615.
  • Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J (May 2003). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nature Biotechnology. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801. S2CID 23783563.
  • Imai Y, Soda M, Murakami T, Shoji M, Abe K, Takahashi R (December 2003). "A product of the human gene adjacent to parkin is a component of Lewy bodies and suppresses Pael receptor-induced cell death". The Journal of Biological Chemistry. 278 (51): 51901–10. doi:10.1074/jbc.M309655200. PMID 14532270.
  • Kimura K, Wakamatsu A, Suzuki Y, Ota T, Nishikawa T, Yamashita R, Yamamoto J, Sekine M, Tsuritani K, Wakaguri H, Ishii S, Sugiyama T, Saito K, Isono Y, Irie R, Kushida N, Yoneyama T, Otsuka R, Kanda K, Yokoi T, Kondo H, Wagatsuma M, Murakawa K, Ishida S, Ishibashi T, Takahashi-Fujii A, Tanase T, Nagai K, Kikuchi H, Nakai K, Isogai T, Sugano S (Jan 2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Research. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
  • Chi A, Valencia JC, Hu ZZ, Watabe H, Yamaguchi H, Mangini NJ, Huang H, Canfield VA, Cheng KC, Yang F, Abe R, Yamagishi S, Shabanowitz J, Hearing VJ, Wu C, Appella E, Hunt DF (November 2006). "Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes". Journal of Proteome Research. 5 (11): 3135–44. doi:10.1021/pr060363j. PMID 17081065.


  • v
  • t
  • e