CCT2 (gene): Difference between revisions

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{{Infobox_gene}}
{{PBB_Controls
'''T-complex protein 1 subunit beta''' is a [[protein]] that in humans is encoded by the ''CCT2'' [[gene]].<ref name="pmid9819444">{{cite journal | vauthors = Won KA, Schumacher RJ, Farr GW, Horwich AL, Reed SI | title = Maturation of human cyclin E requires the function of eukaryotic chaperonin CCT | journal = Molecular and Cellular Biology | volume = 18 | issue = 12 | pages = 7584–9 | date = Dec 1998 | pmid = 9819444 | pmc = 109339 | doi = }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: CCT2 chaperonin containing TCP1, subunit 2 (beta)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10576| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Chaperonin containing TCP1, subunit 2 (beta)
| HGNCid = 1615
| Symbol = CCT2
| AltSymbols =; CCT-beta; 99D8.1; CCTB; MGC142074; MGC142076; PRO1633; TCP-1-beta
| OMIM = 605139
| ECnumber = 
| Homologene = 4696
| MGIid = 107186
| GeneAtlas_image1 = PBB_GE_CCT2_201946_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_CCT2_201947_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0051082 |text = unfolded protein binding}}
| Component = {{GNF_GO|id=GO:0005829 |text = cytosol}} {{GNF_GO|id=GO:0005832 |text = chaperonin-containing T-complex}}
| Process = {{GNF_GO|id=GO:0000074 |text = regulation of progression through cell cycle}} {{GNF_GO|id=GO:0006457 |text = protein folding}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 10576
    | Hs_Ensembl = ENSG00000166226
    | Hs_RefseqProtein = NP_006422
    | Hs_RefseqmRNA = NM_006431
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 12
    | Hs_GenLoc_start = 68265475
    | Hs_GenLoc_end = 68281624
    | Hs_Uniprot = P78371
    | Mm_EntrezGene = 12461
    | Mm_Ensembl = ENSMUSG00000034024
    | Mm_RefseqmRNA = NM_007636
    | Mm_RefseqProtein = NP_031662
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 10
    | Mm_GenLoc_start = 116455356
    | Mm_GenLoc_end = 116467160
    | Mm_Uniprot = Q542X7
  }}
}}
'''Chaperonin containing TCP1, subunit 2 (beta)''', also known as '''CCT2''', is a human [[gene]].<ref name="entrez">{{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 = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
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.<ref name="entrez" />
{{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.<ref name="entrez">{{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 = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
 
==Further reading==
CCT2 (gene) has been shown to [[Protein-protein interaction|interact]] with [[PPP4C]].<ref name=pmid18715871>{{cite journal | vauthors = Chen GI, Tisayakorn S, Jorgensen C, D'Ambrosio LM, Goudreault M, Gingras AC | title = PP4R4/KIAA1622 forms a novel stable cytosolic complex with phosphoprotein phosphatase 4 | journal = The Journal of Biological Chemistry | volume = 283 | issue = 43 | pages = 29273–84 | date = Oct 2008 | pmid = 18715871 | pmc = 2662017 | doi = 10.1074/jbc.M803443200 }}</ref><ref name=pmid16085932>{{cite journal | vauthors = Gingras AC, Caballero M, Zarske M, Sanchez A, Hazbun TR, Fields S, Sonenberg N, Hafen E, Raught B, Aebersold R | title = A novel, evolutionarily conserved protein phosphatase complex involved in cisplatin sensitivity | journal = Molecular & Cellular Proteomics | volume = 4 | issue = 11 | pages = 1725–40 | date = Nov 2005 | pmid = 16085932 | doi = 10.1074/mcp.M500231-MCP200 }}</ref>
 
== References ==
{{reflist}}
 
==External links==
* {{UCSC gene info|CCT2}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Kubota H, Hynes G, Carne A, Ashworth A, Willison K | title = Identification of six Tcp-1-related genes encoding divergent subunits of the TCP-1-containing chaperonin | journal = Current Biology | volume = 4 | issue = 2 | pages = 89–99 | date = Feb 1994 | pmid = 7953530 | doi = 10.1016/S0960-9822(94)00024-2 }}
| citations =
* {{cite journal | vauthors = Llorca O, Smyth MG, Carrascosa JL, Willison KR, Radermacher M, Steinbacher S, Valpuesta JM | title = 3D reconstruction of the ATP-bound form of CCT reveals the asymmetric folding conformation of a type II chaperonin | journal = Nature Structural Biology | volume = 6 | issue = 7 | pages = 639–42 | date = Jul 1999 | pmid = 10404219 | doi = 10.1038/10689 }}
*{{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 | vauthors = Hynes GM, Willison KR | title = Individual subunits of the eukaryotic cytosolic chaperonin mediate interactions with binding sites located on subdomains of beta-actin | journal = The Journal of Biological Chemistry | volume = 275 | issue = 25 | pages = 18985–94 | date = Jun 2000 | pmid = 10748209 | doi = 10.1074/jbc.M910297199 }}
*{{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 | vauthors = 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 = European Journal of Biochemistry / FEBS | volume = 268 | issue = 17 | pages = 4664–73 | date = Sep 2001 | pmid = 11532003 | doi = 10.1046/j.1432-1327.2001.02393.x }}
*{{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 | vauthors = McCormack EA, Llorca O, Carrascosa JL, Valpuesta JM, Willison KR | 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 = Journal of Structural Biology | volume = 135 | issue = 2 | pages = 198–204 | date = Aug 2001 | pmid = 11580269 | doi = 10.1006/jsbi.2001.4385 }}
*{{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 | vauthors = Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J | title = Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides | journal = Nature Biotechnology | volume = 21 | issue = 5 | pages = 566–9 | date = May 2003 | pmid = 12665801 | doi = 10.1038/nbt810 }}
*{{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 | vauthors = Imai Y, Soda M, Murakami T, Shoji M, Abe K, Takahashi R | title = A product of the human gene adjacent to parkin is a component of Lewy bodies and suppresses Pael receptor-induced cell death | journal = The Journal of Biological Chemistry | volume = 278 | issue = 51 | pages = 51901–10 | date = Dec 2003 | pmid = 14532270 | doi = 10.1074/jbc.M309655200 }}
*{{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 | vauthors = 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 | title = Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization | journal = Current Biology | volume = 14 | issue = 16 | pages = 1436–50 | date = Aug 2004 | pmid = 15324660 | doi = 10.1016/j.cub.2004.07.051 }}
*{{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 | vauthors = Andersen JS, Lam YW, Leung AK, Ong SE, Lyon CE, Lamond AI, Mann M | title = Nucleolar proteome dynamics | journal = Nature | volume = 433 | issue = 7021 | pages = 77–83 | date = Jan 2005 | pmid = 15635413 | doi = 10.1038/nature03207 }}
*{{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 | vauthors = Guo D, Han J, Adam BL, Colburn NH, Wang MH, Dong Z, Eizirik DL, She JX, Wang CY | title = Proteomic analysis of SUMO4 substrates in HEK293 cells under serum starvation-induced stress | journal = Biochemical and Biophysical Research Communications | volume = 337 | issue = 4 | pages = 1308–18 | date = Dec 2005 | pmid = 16236267 | doi = 10.1016/j.bbrc.2005.09.191 }}
*{{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 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
{{gene-12-stub}}
{{WikiDoc Sources}}

Latest revision as of 09:19, 30 August 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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n/a

Ensembl

n/a

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UniProt

n/a

n/a

RefSeq (mRNA)

n/a

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RefSeq (protein)

n/a

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

T-complex protein 1 subunit beta is a protein that in humans is encoded by the CCT2 gene.[1][2]

Function

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.[2]

Interactions

CCT2 (gene) has been shown to interact with PPP4C.[3][4]

References

  1. ↑ 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. PMC 109339. PMID 9819444.
  2. ↑ 2.0 2.1 "Entrez Gene: CCT2 chaperonin containing TCP1, subunit 2 (beta)".
  3. ↑ 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.
  4. ↑ 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

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.
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