CCT4

CCT4
Identifiers
Aliases	CCT4, CCT-DELTA, Cctd, SRB, chaperonin containing TCP1 subunit 4
External IDs	OMIM: 605142; MGI: 104689; HomoloGene: 4695; GeneCards: CCT4; OMA:CCT4 - orthologs
Gene location (Human) Chr. Chromosome 2 (human) Band 2p15 Start 61,868,085 bp End 61,888,671 bp
Gene location (Mouse) Chr. Chromosome 11 (mouse) Band 11 A3.2|11 14.25 cM Start 22,940,519 bp End 22,953,780 bp
RNA expression pattern Bgee Human Mouse (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 Species Human Mouse 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 Mb Chr 11: 22.94 – 22.95 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

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

Interactions

CCT4 has been shown to interact with PPP4C.

External links

• Human CCT4 genome location and CCT4 gene details page in the UCSC Genome Browser.

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. 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.