CCT5 (gene)

CCT5

Identifiers

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

Gene location (Human)

Chr.	Chromosome 5 (human)^[1]

Band	5p15.2	Start	10,249,929 bp^[1]
Band	5p15.2	End	10,266,389 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 15 (mouse)^[2]

Band	15\|15 B2	Start	31,590,946 bp^[2]
Band	15\|15 B2	End	31,601,950 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

embryo

ganglionic eminence

monocyte

rectum

smooth muscle tissue

islet of Langerhans

stromal cell of endometrium

appendix

right adrenal gland

left adrenal gland

Top expressed in

primitive streak

somite

maxillary prominence

superior cervical ganglion

abdominal wall

medial ganglionic eminence

vas deferens

hand

dermis

endocardial cushion

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

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

T-complex protein 1 subunit epsilon is a protein that in humans is encoded by the CCT5 gene.^[5]

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.^[5]

Interactions

CCT5 (gene) has been shown to interact with PPP4C.^[6]^[7]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000150753 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000022234 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ ^a ^b "Entrez Gene: CCT5 chaperonin containing TCP1, subunit 5 (epsilon)".
^ 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.
^ Gingras AC, Caballero M, Zarske M, Sanchez A, Hazbun TR, Fields S, Sonenberg N, Hafen E, Raught B, Aebersold R (Nov 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.

External links

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

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.

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This page was last edited on 25 March 2024, at 14:31

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Function

Interactions

References

External links

Further reading