CCT6A

CCT6A
Identifiers
Aliases	CCT6A, CCT-zeta, CCT-zeta-1, CCT6, Cctz, HTR3, MoDP-2, TCP-1-zeta, TCP20, TCPZ, TTCP20, chaperonin containing TCP1 subunit 6A
External IDs	OMIM: 104613 MGI: 107943 HomoloGene: 1336 GeneCards: CCT6A
Gene location (Human)
Chr.	Chromosome 7 (human)[1]
End	56,063,989 bp[1]
RNA expression pattern
	; ;
	More reference expression data
Gene ontology
Molecular function	• protein binding involved in protein folding; • nucleotide binding; • WD40-repeat domain binding; • GO:0001948 protein binding; • ATP binding; • unfolded protein binding; • RNA binding;
Cellular component	• chaperonin-containing T-complex; • microtubules; • extracellular exosome; • extracellular matrix; • cytoplasm; • cytosol;
Biological process	• positive regulation of establishment of protein localization to telomere; • protein stabilization; • positive regulation of telomere maintenance via telomerase; • protein folding; • positive regulation of protein localization to Cajal body; • positive regulation of telomerase RNA localization to Cajal body; • 'de novo' protein folding; • chaperone-mediated protein folding;
	Sources:Amigo / QuickGO
Orthologs
	908
	12466
	ENSG00000146731
	ENSMUSG00000029447
	P40227
	P80317
	NM_001762; NM_001009186
	NM_009838
	NP_001009186; NP_001753
	NP_033968
	Wikidata
View/Edit Human	View/Edit Mouse

T-complex protein 1 subunit zeta is a protein that in humans is encoded by the CCT6A gene.[4][5][6]

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, encoding different isoforms, have been characterized.[6]

Interactions

CCT6A has been shown to interact with PPP4C.[7][8]

References

GRCh38: Ensembl release 89: ENSG00000146731 - 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.
Segel GB, Boal TR, Cardillo TS, Murant FG, Lichtman MA, Sherman F (August 1992). "Isolation of a gene encoding a chaperonin-like protein by complementation of yeast amino acid transport mutants with human cDNA". Proc Natl Acad Sci U S A. 89 (13): 6060–4. doi:10.1073/pnas.89.13.6060. PMC 49437. PMID 1352881.
Li WZ, Lin P, Frydman J, Boal TR, Cardillo TS, Richard LM, Toth D, Lichtman MA, Hartl FU, Sherman F (August 1994). "Tcp20, a subunit of the eukaryotic TRiC chaperonin from humans and yeast". J Biol Chem. 269 (28): 18616–22. PMID 8034610.
"Entrez Gene: CCT6A chaperonin containing TCP1, subunit 6A (zeta 1)".
Chen GI, Tisayakorn S, Jorgensen C, D'Ambrosio LM, Goudreault M, Gingras AC (October 2008). "PP4R4/KIAA1622 Forms a Novel Stable Cytosolic Complex with Phosphoprotein Phosphatase 4". J. Biol. Chem. 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 (November 2005). "A novel, evolutionarily conserved protein phosphatase complex involved in cisplatin sensitivity". Mol. Cell. Proteomics. 4 (11): 1725–40. doi:10.1074/mcp.M500231-MCP200. PMID 16085932.

External links

Human CCT6A genome location and CCT6A gene details page in the UCSC Genome Browser.

Dawson SJ, White LA (1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin". J. Infect. 24 (3): 317–20. doi:10.1016/S0163-4453(05)80037-4. PMID 1602151.
Kubota H, Hynes G, Carne A, Ashworth A, Willison K (1994). "Identification of six Tcp-1-related genes encoding divergent subunits of the TCP-1-containing chaperonin". Curr. Biol. 4 (2): 89–99. doi:10.1016/S0960-9822(94)00024-2. PMID 7953530. S2CID 31300131.
Schwartz GJ, Kittelberger AM, Segel GB (2000). "Cloning of rabbit Cct6 and the distribution of the Cct complex in mammalian tissues". Exp. Nephrol. 8 (3): 152–60. doi:10.1159/000020663. PMID 10810232. S2CID 28781053.
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. doi:10.1046/j.1432-1327.2001.02393.x. PMID 11532003.
Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801. S2CID 23783563.
Imai Y, Soda M, Murakami T, Shoji M, Abe K, Takahashi R (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.
Bouwmeester T, Bauch A, Ruffner H, Angrand PO, Bergamini G, Croughton K, Cruciat C, Eberhard D, Gagneur J, Ghidelli S, Hopf C, Huhse B, Mangano R, Michon AM, Schirle M, Schlegl J, Schwab M, Stein MA, Bauer A, Casari G, Drewes G, Gavin AC, Jackson DB, Joberty G, Neubauer G, Rick J, Kuster B, Superti-Furga G (2004). "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway". Nat. Cell Biol. 6 (2): 97–105. doi:10.1038/ncb1086. PMID 14743216. S2CID 11683986.
Higo M, Uzawa K, Kouzu Y, Bukawa H, Nimura Y, Seki N, Tanzawa H (2005). "Identification of candidate radioresistant genes in human squamous cell carcinoma cells through gene expression analysis using DNA microarrays". Oncol. Rep. 14 (5): 1293–8. doi:10.3892/or.14.5.1293. PMID 16211299.
Guo D, Han J, Adam BL, Colburn NH, Wang MH, Dong Z, Eizirik DL, She JX, Wang CY (2005). "Proteomic analysis of SUMO4 substrates in HEK293 cells under serum starvation-induced stress". Biochem. Biophys. Res. Commun. 337 (4): 1308–18. doi:10.1016/j.bbrc.2005.09.191. PMID 16236267.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000146731 - Ensembl, May 2017

[2] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[3] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid1352881-4] Segel GB, Boal TR, Cardillo TS, Murant FG, Lichtman MA, Sherman F (August 1992). "Isolation of a gene encoding a chaperonin-like protein by complementation of yeast amino acid transport mutants with human cDNA". Proc Natl Acad Sci U S A. 89 (13): 6060–4. doi:10.1073/pnas.89.13.6060. PMC 49437. PMID 1352881.

[pmid8034610-5] Li WZ, Lin P, Frydman J, Boal TR, Cardillo TS, Richard LM, Toth D, Lichtman MA, Hartl FU, Sherman F (August 1994). "Tcp20, a subunit of the eukaryotic TRiC chaperonin from humans and yeast". J Biol Chem. 269 (28): 18616–22. PMID 8034610.

[entrez-6] "Entrez Gene: CCT6A chaperonin containing TCP1, subunit 6A (zeta 1)".

[pmid18715871-7] Chen GI, Tisayakorn S, Jorgensen C, D'Ambrosio LM, Goudreault M, Gingras AC (October 2008). "PP4R4/KIAA1622 Forms a Novel Stable Cytosolic Complex with Phosphoprotein Phosphatase 4". J. Biol. Chem. 283 (43): 29273–84. doi:10.1074/jbc.M803443200. PMC 2662017. PMID 18715871.

[pmid16085932-8] 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". Mol. Cell. Proteomics. 4 (11): 1725–40. doi:10.1074/mcp.M500231-MCP200. PMID 16085932.

CCT6A

Function

Interactions

References

External links

Further reading