CCT2 (gene)

T-complex protein 1 subunit beta is a protein that in humans is encoded by the CCT2 gene.[5][6]

CCT2
Identifiers
Aliases	CCT2, 99D8.1, CCT-beta, CCTB, HEL-S-100n, PRO1633, TCP-1-beta, chaperonin containing TCP1 subunit 2
External IDs	OMIM: 605139 MGI: 107186 HomoloGene: 4696 GeneCards: CCT2
Gene location (Human) Chr. Chromosome 12 (human)[1] Band 12q15 Start 69,585,426 bp[1] End 69,601,570 bp[1]
Gene location (Mouse) Chr. Chromosome 10 (mouse)[2] Band 10|10 D2 Start 117,051,001 bp[2] End 117,063,814 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • nucleotide binding • protein binding involved in protein folding • GO:0001948 protein binding • ATP binding • ubiquitin protein ligase binding • unfolded protein binding Cellular component • cell body • myelin • zona pellucida receptor complex • chaperonin-containing T-complex • microtubule • extracellular exosome • extracellular matrix • extracellular region • cytoplasm • cytosol • azurophil granule lumen Biological process • chaperone mediated protein folding independent of cofactor • chaperone-mediated protein complex assembly • 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 • neutrophil degranulation Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	10576	12461
Ensembl	ENSG00000166226	ENSMUSG00000034024
UniProt	P78371	P80314
RefSeq (mRNA)	NM_006431 NM_001198842	NM_007636 NM_001358767
RefSeq (protein)	NP_001185771 NP_006422	NP_031662 NP_001345696
Location (UCSC)	Chr 12: 69.59 – 69.6 Mb	Chr 10: 117.05 – 117.06 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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 the gene described in this record have been observed but have not been thoroughly characterized.[6]

Interactions

CCT2 (gene) has been shown to interact with PPP4C.[7][8]

References

1. GRCh38: Ensembl release 89: ENSG00000166226 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000034024 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Won KA, Schumacher RJ, Farr GW, Horwich AL, Reed SI (Dec 1998). "Maturation of human cyclin E requires the function of eukaryotic chaperonin CCT". Molecular and Cellular Biology. 18 (12): 7584–9. doi:10.1128/mcb.18.12.7584. PMC 109339. PMID 9819444.
6. "Entrez Gene: CCT2 chaperonin containing TCP1, subunit 2 (beta)".
7. 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.
8. 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.

External links

• Human CCT2 genome location and CCT2 gene details page in the UCSC Genome Browser.
• Overview of all the structural information available in the PDB for UniProt: P78371 (T-complex protein 1 subunit beta) at the PDBe-KB.

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.
• Llorca O, Smyth MG, Carrascosa JL, Willison KR, Radermacher M, Steinbacher S, Valpuesta JM (Jul 1999). "3D reconstruction of the ATP-bound form of CCT reveals the asymmetric folding conformation of a type II chaperonin". Nature Structural Biology. 6 (7): 639–42. doi:10.1038/10689. PMID 10404219.
• Hynes GM, Willison KR (Jun 2000). "Individual subunits of the eukaryotic cytosolic chaperonin mediate interactions with binding sites located on subdomains of beta-actin". The Journal of Biological Chemistry. 275 (25): 18985–94. doi:10.1074/jbc.M910297199. PMID 10748209.
• 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 / FEBS. 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 (Aug 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.
• 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.
• Imai Y, Soda M, Murakami T, Shoji M, Abe K, Takahashi R (Dec 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.
• Jin J, Smith FD, Stark C, Wells CD, Fawcett JP, Kulkarni S, Metalnikov P, O'Donnell P, Taylor P, Taylor L, Zougman A, Woodgett JR, Langeberg LK, Scott JD, Pawson T (Aug 2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization". Current Biology. 14 (16): 1436–50. doi:10.1016/j.cub.2004.07.051. PMID 15324660.
• Andersen JS, Lam YW, Leung AK, Ong SE, Lyon CE, Lamond AI, Mann M (Jan 2005). "Nucleolar proteome dynamics". Nature. 433 (7021): 77–83. doi:10.1038/nature03207. PMID 15635413.
• Guo D, Han J, Adam BL, Colburn NH, Wang MH, Dong Z, Eizirik DL, She JX, Wang CY (Dec 2005). "Proteomic analysis of SUMO4 substrates in HEK293 cells under serum starvation-induced stress". Biochemical and Biophysical Research Communications. 337 (4): 1308–18. doi:10.1016/j.bbrc.2005.09.191. PMID 16236267.