CCT5 (gene)

CCT5
Identifiers
Aliases	CCT5, CCT-epsilon, CCTE, HEL-S-69, TCP-1-epsilon, PNAS-102, chaperonin containing TCP1 subunit 5
External IDs	OMIM: 610150; MGI: 107185; HomoloGene: 6287; GeneCards: CCT5; OMA:CCT5 - orthologs
Gene location (Human) Chr. Chromosome 5 (human) Band 5p15.2 Start 10,249,929 bp End 10,266,389 bp
Gene location (Mouse) Chr. Chromosome 15 (mouse) Band 15|15 B2 Start 31,590,946 bp End 31,601,950 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in gonad ventricular zone embryo ganglionic eminence monocyte rectum smooth muscle tissue right testis islet of Langerhans left testis Top expressed in primitive streak somite maxillary prominence mandibular prominence superior cervical ganglion abdominal wall Gonadal ridge medial ganglionic eminence vas deferens hand More reference expression data BioGPS More reference expression data
Gene ontology Molecular function nucleotide binding G-protein beta-subunit binding protein binding beta-tubulin binding ATP binding protein folding chaperone activity unfolded protein binding mRNA 3'-UTR binding mRNA 5'-UTR binding Cellular component cell body centrosome myelin sheath microtubule organizing center zona pellucida receptor complex nucleolus 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 response to virus protein stabilization positive regulation of telomere maintenance via telomerase toxin transport protein folding 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 22948 12465 Ensembl ENSG00000150753 ENSMUSG00000022234 UniProt P48643 P80316 RefSeq (mRNA) NM_001306153 NM_001306154 NM_001306155 NM_001306156 NM_012073 NM_007637 NM_001348035 RefSeq (protein) NP_001293082 NP_001293083 NP_001293084 NP_001293085 NP_036205 NP_001334964 NP_031663 Location (UCSC) Chr 5: 10.25 – 10.27 Mb Chr 15: 31.59 – 31.6 Mb PubMed search
Wikidata
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T-complex protein 1 subunit epsilon is a protein that in humans is encoded by the CCT5 gene.

Function

This gene encodes a molecular chaperone that is member of the TRiC complex. 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.

Interactions

CCT5 (gene) has been shown to interact with PPP4C.

External links

• Human CCT5 genome location and CCT5 gene details page in the UCSC Genome Browser.

Further reading

• Roobol A, Holmes FE, Hayes NV, Baines AJ, Carden MJ (Apr 1995). "Cytoplasmic chaperonin complexes enter neurites developing in vitro and differ in subunit composition within single cells". Journal of Cell Science. 108 (4): 1477–88. doi:10.1242/jcs.108.4.1477. PMID 7615668.
• Nagase T, Miyajima N, Tanaka A, Sazuka T, Seki N, Sato S, Tabata S, Ishikawa K, Kawarabayasi Y, Kotani H (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 Research. 2 (1): 37–43. doi:10.1093/dnares/2.1.37. PMID 7788527.
• 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.
• Liou AK, Willison KR (Jul 1997). "Elucidation of the subunit orientation in CCT (chaperonin containing TCP1) from the subunit composition of CCT micro-complexes". The EMBO Journal. 16 (14): 4311–6. doi:10.1093/emboj/16.14.4311. PMC 1170057. PMID 9250675.
• Roperch JP, Lethrone F, Prieur S, Piouffre L, Israeli D, Tuynder M, Nemani M, Pasturaud P, Gendron MC, Dausset J, Oren M, Amson RB, Telerman A (Jul 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)". Proceedings of the National Academy of Sciences of the United States of America. 96 (14): 8070–3. Bibcode:1999PNAS...96.8070R. doi:10.1073/pnas.96.14.8070. PMC 22189. PMID 10393949.
• Yanaka N, Kobayashi K, Wakimoto K, Yamada E, Imahie H, Imai Y, Mori C (May 2000). "Insertional mutation of the murine kisimo locus caused a defect in spermatogenesis". The Journal of Biological Chemistry. 275 (20): 14791–4. doi:10.1074/jbc.C901047199. PMID 10747865.
• Yoo BC, Kim SH, Cairns N, Fountoulakis M, Lubec G (Jan 2001). "Deranged expression of molecular chaperones in brains of patients with Alzheimer's disease". Biochemical and Biophysical Research Communications. 280 (1): 249–58. doi:10.1006/bbrc.2000.4109. PMID 11162507.
• Yoo BC, Vlkolinsky R, Engidawork E, Cairns N, Fountoulakis M, Lubec G (Apr 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. S2CID 22398860.
• Yokota S, Yanagi H, Yura T, Kubota H (Sep 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". European Journal of Biochemistry. 268 (17): 4664–73. doi:10.1046/j.1432-1327.2001.02393.x. PMID 11532003.
• McCormack EA, Llorca O, Carrascosa JL, Valpuesta JM, Willison KR (August 2001). "Point mutations in a hinge linking the small and large domains of beta-actin result in trapped folding intermediates bound to cytosolic chaperonin CCT". Journal of Structural Biology. 135 (2): 198–204. doi:10.1006/jsbi.2001.4385. PMID 11580269.
• 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.
• Guenther MG, Yu J, Kao GD, Yen TJ, Lazar MA (December 2002). "Assembly of the SMRT-histone deacetylase 3 repression complex requires the TCP-1 ring complex". Genes & Development. 16 (24): 3130–5. doi:10.1101/gad.1037502. PMC 187500. PMID 12502735.
• Ludwig A, Dietel M, Lage H (2003). "Identification of differentially expressed genes in classical and atypical multidrug-resistant gastric carcinoma cells". Anticancer Research. 22 (6A): 3213–21. PMID 12530067.
• 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.
• Lehner B, Sanderson CM (Jul 2004). "A protein interaction framework for human mRNA degradation". Genome Research. 14 (7): 1315–23. doi:10.1101/gr.2122004. PMC 442147. PMID 15231747.
• Lukov GL, Hu T, McLaughlin JN, Hamm HE, Willardson BM (Jun 2005). "Phosducin-like protein acts as a molecular chaperone for G protein betagamma dimer assembly". The EMBO Journal. 24 (11): 1965–75. doi:10.1038/sj.emboj.7600673. PMC 1142607. PMID 15889144.
• Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE (Sep 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. hdl:11858/00-001M-0000-0010-8592-0. PMID 16169070. S2CID 8235923.