CCT7
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Official Full Name
chaperonin containing TCP1, subunit 7 (eta) -
Overview
This gene encodes a molecular chaperone that is a 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. Alternative splicing results in multiple transcript variants. Related pseudogenes have been identified on chromosomes 5 and 6. -
Synonyms
CCT7;chaperonin containing TCP1, subunit 7 (eta);T-complex protein 1 subunit eta;Ccth;Nip7 1;CCT ETA;CCT-eta;Chaperonin containing t complex polypeptide 1 eta subunit;Chaperonin containing TCP1 subunit 7 (eta);Chaperonin containing TCP1 subunit 7;HIV 1 Nef interacting protein;HIV-1 Nef-interacting protein;T complex protein 1 eta subunit;TCP-1-eta;TCPH_HUMAN;OTTHUMP00000202321;OTTHUMP00000202322;OTTHUMP00000213063;HIV-1 Nef interacting protein;chaperonin containing t-complex polypeptide 1, eta subunit;CCTETA;NIP7-1;TCP1ETA
Recombinant Proteins
- Human
- Mouse
- Chicken
- Rhesus macaque
- Zebrafish
- E.coli
- Wheat Germ
- Mammalian Cell
- HEK293
- In Vitro Cell Free System
- HEK293T
- His
- GST
- Non
- His&Fc&Avi
- Myc&DDK
Involved Pathway
CCT7 involved in several pathways and played different roles in them. We selected most pathways CCT7 participated on our site, such as Association of TriC/CCT with target proteins during biosynthesis,Chaperonin-mediated protein folding,Cooperation of Prefoldin and TriC/CCT in actin and tubulin folding, which may be useful for your reference. Also, other proteins which involved in the same pathway with CCT7 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
| Pathway Name | Pathway Related Protein |
|---|---|
| Protein folding | FBXL5,KIFC3,FBXW5,PFDN5,SERPINA7,FBXW9,TBCA,TBCB,FKBP9,TBCC |
| Prefoldin mediated transfer of substrate to CCT/TriC | PFDN6,PFDN2,PFDN4,PFDN5,PFDN1,VBP1,CCT6A |
| Chaperonin-mediated protein folding | CCT8,FKBP9,TUBA1B,CCT5,FBXW4,PFDN2,PFDN6,FBXW2,CCT6A,CCT2 |
| Metabolism of proteins | IGFBP5A,PFDN5,SPON1B,GCNT3,PDIA6,ST8SIA3,DHPS,ALG2,NAPB,ADAMTS8 |
| Formation of tubulin folding intermediates by CCT/TriC | CCT6A,CCT3,TCP1,CCT5,CCT4,TUBB4B,TUBA3D,CCT2,TUBA1B,CCT8 |
| Association of TriC/CCT with target proteins during biosynthesis | FBXL5,FBXW2,KIFC3,CCT8,FBXW4,FBXW9,CCT5,FKBP9,NOP56,CCT2 |
| Cooperation of Prefoldin and TriC/CCT in actin and tubulin folding | PFDN4,TUBA3D,PFDN2,CCT5,PFDN1,VBP1,TUBA1B,CCT6A,PFDN6,TUBB4A |
| Folding of actin by CCT/TriC | CCT5,CCT4,CCT3,CCT6A,CCT2,CCT8,TCP1 |
Protein Function
CCT7 has several biochemical functions, for example, ATP binding,identical protein binding,protein binding. Some of the functions are cooperated with other proteins, some of the functions could acted by CCT7 itself. We selected most functions CCT7 had, and list some proteins which have the same functions with CCT7. You can find most of the proteins on our site.
| Function | Related Protein |
|---|---|
| ATP binding | PAK4,CAMK4,PRKCBB,RAD54L,NLRP4,TWF1,G3BP1,ALDH18A1,ITPKC,NAT10 |
| protein binding | ARR3,KCNQ1,C12orf68,POLM,BIRC7,UBE2A,CASP8,FSHB,ALDH7A1,TFR2 |
| unfolded protein binding | RUVBL2,APCS,AFG3L2,ST13,RP2,DNAJA2L,HSPA2,HTRA2,TOMM20,HSP104 |
| identical protein binding | FRS3,LTBR,ASMT,ZHX2,NISCH,BLOC1S6,HGF,PCM1,ESR1,TNK2 |
Interacting Protein
CCT7 has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with CCT7 here. Most of them are supplied by our site. Hope this information will be useful for your research of CCT7.
PPP4C;PPP2CB;PPP2CA;STRN3;ILK;SSSCA1;STRN
Resources
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References
- Erdmann, J; Stark, K; et al. Dysfunctional nitric oxide signalling increases risk of myocardial infarction. NATURE 504:432-+(2013).
- Hirata, H; Ishinabe, S; et al. Molecular Characterization and Phylogenetic Analysis of Babesia sp NV-1 Detected from Wild American Mink (Neovison vison) in Hokkaido, Japan. JOURNAL OF PARASITOLOGY 99:350-352(2013).
