CCT2 (gene)

CCT2 (gene)

Chaperonin containing TCP1, subunit 2 (beta), also known as CCT2, is a human gene.cite web | title = Entrez Gene: CCT2 chaperonin containing TCP1, subunit 2 (beta)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10576| accessdate = ]

PBB_Summary
section_title =
summary_text = This gene encodes a molecular chaperone that is member of the chaperonin containing TCP1 complex (CCT), also known as the TCP1 ring complex (TRiC). 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.cite web | title = Entrez Gene: CCT2 chaperonin containing TCP1, subunit 2 (beta)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10576| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Kubota H, Hynes G, Carne A, "et al." |title=Identification of six Tcp-1-related genes encoding divergent subunits of the TCP-1-containing chaperonin. |journal=Curr. Biol. |volume=4 |issue= 2 |pages= 89–99 |year= 1994 |pmid= 7953530 |doi=
*cite journal | author=Won KA, Schumacher RJ, Farr GW, "et al." |title=Maturation of human cyclin E requires the function of eukaryotic chaperonin CCT. |journal=Mol. Cell. Biol. |volume=18 |issue= 12 |pages= 7584–9 |year= 1998 |pmid= 9819444 |doi=
*cite journal | author=Llorca O, Smyth MG, Carrascosa JL, "et al." |title=3D reconstruction of the ATP-bound form of CCT reveals the asymmetric folding conformation of a type II chaperonin. |journal=Nat. Struct. Biol. |volume=6 |issue= 7 |pages= 639–42 |year= 1999 |pmid= 10404219 |doi= 10.1038/10689
*cite journal | author=Hynes GM, Willison KR |title=Individual subunits of the eukaryotic cytosolic chaperonin mediate interactions with binding sites located on subdomains of beta-actin. |journal=J. Biol. Chem. |volume=275 |issue= 25 |pages= 18985–94 |year= 2000 |pmid= 10748209 |doi= 10.1074/jbc.M910297199
*cite journal | author=Yokota S, Yanagi H, Yura T, Kubota H |title=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. |journal=Eur. J. Biochem. |volume=268 |issue= 17 |pages= 4664–73 |year= 2001 |pmid= 11532003 |doi=
*cite journal | author=McCormack EA, Llorca O, Carrascosa JL, "et al." |title=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=J. Struct. Biol. |volume=135 |issue= 2 |pages= 198–204 |year= 2002 |pmid= 11580269 |doi= 10.1006/jsbi.2001.4385
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Gevaert K, Goethals M, Martens L, "et al." |title=Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. |journal=Nat. Biotechnol. |volume=21 |issue= 5 |pages= 566–9 |year= 2004 |pmid= 12665801 |doi= 10.1038/nbt810
*cite journal | author=Imai Y, Soda M, Murakami T, "et al." |title=A product of the human gene adjacent to parkin is a component of Lewy bodies and suppresses Pael receptor-induced cell death. |journal=J. Biol. Chem. |volume=278 |issue= 51 |pages= 51901–10 |year= 2004 |pmid= 14532270 |doi= 10.1074/jbc.M309655200
*cite journal | author=Jin J, Smith FD, Stark C, "et al." |title=Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization. |journal=Curr. Biol. |volume=14 |issue= 16 |pages= 1436–50 |year= 2004 |pmid= 15324660 |doi= 10.1016/j.cub.2004.07.051
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Andersen JS, Lam YW, Leung AK, "et al." |title=Nucleolar proteome dynamics. |journal=Nature |volume=433 |issue= 7021 |pages= 77–83 |year= 2005 |pmid= 15635413 |doi= 10.1038/nature03207
*cite journal | author=Guo D, Han J, Adam BL, "et al." |title=Proteomic analysis of SUMO4 substrates in HEK293 cells under serum starvation-induced stress. |journal=Biochem. Biophys. Res. Commun. |volume=337 |issue= 4 |pages= 1308–18 |year= 2005 |pmid= 16236267 |doi= 10.1016/j.bbrc.2005.09.191

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