CCT5 (gene)
Chaperonin containing TCP1, subunit 5 (epsilon) | |||||||||||
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Identifiers | |||||||||||
Symbols | CCT5 ; CCT-epsilon; CCTE; KIAA0098; TCP-1-epsilon | ||||||||||
External IDs | Template:OMIM5 Template:MGI HomoloGene: 6287 | ||||||||||
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RNA expression pattern | |||||||||||
More reference expression data | |||||||||||
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Template:GNF Ortholog box | |||||||||||
Species | Human | Mouse | |||||||||
Entrez | n/a | n/a | |||||||||
Ensembl | n/a | n/a | |||||||||
UniProt | n/a | n/a | |||||||||
RefSeq (mRNA) | n/a | n/a | |||||||||
RefSeq (protein) | n/a | n/a | |||||||||
Location (UCSC) | n/a | n/a | |||||||||
PubMed search | n/a | n/a |
Chaperonin containing TCP1, subunit 5 (epsilon), also known as CCT5, is a human gene.[1]
This gene encodes a molecular chaperone that is member of the chaperonin containing TCP1 complex (CCT), also known as the TCP1 ring complex (TRiC). This complex consists of two identical stacked rings, each containing eight different proteins. Unfolded polypeptides enter the central cavity of the complex and are folded in an ATP-dependent manner. The complex folds various proteins, including actin and tubulin. Alternate transcriptional splice variants of this gene have been observed but have not been thoroughly characterized.[1]
References
Further reading
- Roobol A, Holmes FE, Hayes NV; et al. (1995). "Cytoplasmic chaperonin complexes enter neurites developing in vitro and differ in subunit composition within single cells". J. Cell. Sci. 108 ( Pt 4): 1477–88. PMID 7615668.
- Nagase T, Miyajima N, Tanaka A; et al. (1995). "Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1". DNA Res. 2 (1): 37–43. PMID 7788527.
- Kubota H, Hynes G, Carne A; et al. (1994). "Identification of six Tcp-1-related genes encoding divergent subunits of the TCP-1-containing chaperonin". Curr. Biol. 4 (2): 89–99. PMID 7953530.
- Liou AK, Willison KR (1997). "Elucidation of the subunit orientation in CCT (chaperonin containing TCP1) from the subunit composition of CCT micro-complexes". EMBO J. 16 (14): 4311–6. PMID 9250675.
- Roperch JP, Lethrone F, Prieur S; et al. (1999). "SIAH-1 promotes apoptosis and tumor suppression through a network involving the regulation of protein folding, unfolding, and trafficking: identification of common effectors with p53 and p21(Waf1)". Proc. Natl. Acad. Sci. U.S.A. 96 (14): 8070–3. PMID 10393949.
- Yanaka N, Kobayashi K, Wakimoto K; et al. (2000). "Insertional mutation of the murine kisimo locus caused a defect in spermatogenesis". J. Biol. Chem. 275 (20): 14791–4. doi:10.1074/jbc.C901047199. PMID 10747865.
- Yoo BC, Kim SH, Cairns N; et al. (2001). "Deranged expression of molecular chaperones in brains of patients with Alzheimer's disease". Biochem. Biophys. Res. Commun. 280 (1): 249–58. doi:10.1006/bbrc.2000.4109. PMID 11162507.
- Yoo BC, Vlkolinsky R, Engidawork E; et al. (2001). "Differential expression of molecular chaperones in brain of patients with Down syndrome". Electrophoresis. 22 (6): 1233–41. doi:10.1002/1522-2683()22:6<1233::AID-ELPS1233>3.0.CO;2-M. PMID 11358150.
- Yokota S, Yanagi H, Yura T, Kubota H (2001). "Cytosolic chaperonin-containing t-complex polypeptide 1 changes the content of a particular subunit species concomitant with substrate binding and folding activities during the cell cycle". Eur. J. Biochem. 268 (17): 4664–73. PMID 11532003.
- McCormack EA, Llorca O, Carrascosa JL; et al. (2002). "Point mutations in a hinge linking the small and large domains of beta-actin result in trapped folding intermediates bound to cytosolic chaperonin CCT". J. Struct. Biol. 135 (2): 198–204. doi:10.1006/jsbi.2001.4385. PMID 11580269.
- Llorca O, Martín-Benito J, Gómez-Puertas P; et al. (2002). "Analysis of the interaction between the eukaryotic chaperonin CCT and its substrates actin and tubulin". J. Struct. Biol. 135 (2): 205–18. doi:10.1006/jsbi.2001.4359. PMID 11580270.
- Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
- Guenther MG, Yu J, Kao GD; et al. (2003). "Assembly of the SMRT-histone deacetylase 3 repression complex requires the TCP-1 ring complex". Genes Dev. 16 (24): 3130–5. doi:10.1101/gad.1037502. PMID 12502735.
- Ludwig A, Dietel M, Lage H (2003). "Identification of differentially expressed genes in classical and atypical multidrug-resistant gastric carcinoma cells". Anticancer Res. 22 (6A): 3213–21. PMID 12530067.
- Imai Y, Soda M, Murakami T; et al. (2004). "A product of the human gene adjacent to parkin is a component of Lewy bodies and suppresses Pael receptor-induced cell death". J. Biol. Chem. 278 (51): 51901–10. doi:10.1074/jbc.M309655200. PMID 14532270.
- Ota T, Suzuki Y, Nishikawa T; et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
- Lehner B, Sanderson CM (2004). "A protein interaction framework for human mRNA degradation". Genome Res. 14 (7): 1315–23. doi:10.1101/gr.2122004. PMID 15231747.
- Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
- Lukov GL, Hu T, McLaughlin JN; et al. (2005). "Phosducin-like protein acts as a molecular chaperone for G protein betagamma dimer assembly". EMBO J. 24 (11): 1965–75. doi:10.1038/sj.emboj.7600673. PMID 15889144.
- Stelzl U, Worm U, Lalowski M; et al. (2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. PMID 16169070.
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