Podjedinica proteina 1 T-kompleksa beta

Podjedinica proteina 1 T-kompleksa beta
Identifikatori
Aliasi	CCT2
Vanjski ID-jevi	OMIM: 605139 MGI: 107186 HomoloGene: 4696 GeneCards: CCT2
Lokacija gena (čovjek)
Hrom.	Hromosom 12 (čovjek)
Kraj	69,601,570 bp
Lokacija gena (miš)
Hrom.	Hromosom 10 (miš)
Kraj	116,899,719 bp
Obrazac RNK ekspresije
	; ;
	Više referentnih podataka o ekspresiji
Ontologija gena
Molekularna funkcija	• nucleotide binding; • protein folding chaperone activity; • GO:0001948, GO:0016582 vezivanje za proteine; • ATP binding; • ubiquitin protein ligase binding; • unfolded protein binding;
Ćelijska komponenta	• cell body; • myelin sheath; • zona pellucida receptor complex; • TRiC; • Mikrotubula; • Egzosom; • GO:0005578 Vanćelijski matriks; • extracellular region; • citoplazma; • citosol; • azurophil granule lumen;
Biološki proces	• 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; • Savijanje proteina; • positive regulation of telomerase activity; • positive regulation of telomerase RNA localization to Cajal body; • binding of sperm to zona pellucida; • neutrophil degranulation;
	Izvori:Amigo / QuickGO
Ortolozi
	10576
	12461
	ENSG00000166226
	ENSMUSG00000034024
	P78371
	P80314
	NM_006431; NM_001198842
	NM_007636; NM_001358767
	NP_001185771; NP_006422
	NP_031662; NP_001345696
	Wikipodaci
Pogledaj/uredi – čovjek	Pogledaj/uredi – miš

Podjedinica proteina 1 T-kompleksa beta je protein koji je kod ljudi kodiran iz gena CCT2.^[5]^[6]

Funkcija

Ovaj gen kodira molekulski šaperon koji je član kompleksa TRiC. Ovaj kompleks sastoji se od dva identična naslagana prstena, od kojih svaki sadrži po osam različitih proteina. Nerazvijeni polipeptidi ulaze u središnju šupljinu kompleksa i savijaju se na način koji je ovisan o ATP-u. Kompleks savija različite proteine, uključujući aktin i tubulin. Primijećene su alternativne transkripcijske spojne varijante gena, opisane u ovom transkriptu, ali nisu detaljno okarakterizirane.

Interakcije

Pokazano je da CCT2 (gen) ima interakcije s PPP4C.^[7]^[8]

Reference

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000166226 - Ensembl, maj 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000034024 - Ensembl, maj 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.
^ 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.
^ "Entrez Gene: CCT2 chaperonin containing TCP1, subunit 2 (beta)".
^ 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.

Dopunska literatura

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 (maj 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.

Vanjski linkovi

Lokacija ljudskog genoma CCT2 i stranica sa detaljima o genu CCT2 u UCSC Genome Browseru.
P78371

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000166226 - Ensembl, maj 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000034024 - Ensembl, maj 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.

[pmid9819444-5] 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.

[entrez-6] "Entrez Gene: CCT2 chaperonin containing TCP1, subunit 2 (beta)".

[pmid18715871-7] 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.

[pmid16085932-8] 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.

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