Human Gene CCT7 (uc002siz.3) Description and Page Index
Description: Homo sapiens chaperonin containing TCP1, subunit 7 (eta) (CCT7), transcript variant 1, mRNA. RefSeq Summary (NM_006429): 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. [provided by RefSeq, Oct 2009]. Transcript (Including UTRs) Position: hg19 chr2:73,461,364-73,480,150 Size: 18,787 Total Exon Count: 12 Strand: + Coding Region Position: hg19 chr2:73,461,507-73,479,989 Size: 18,483 Coding Exon Count: 12
ID:TCPH_HUMAN DESCRIPTION: RecName: Full=T-complex protein 1 subunit eta; Short=TCP-1-eta; AltName: Full=CCT-eta; AltName: Full=HIV-1 Nef-interacting protein; FUNCTION: Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin (By similarity). SUBUNIT: Heterooligomeric complex of about 850 to 900 kDa that forms two stacked rings, 12 to 16 nm in diameter. Interacts with PACRG. SUBCELLULAR LOCATION: Cytoplasm (By similarity). SIMILARITY: Belongs to the TCP-1 chaperonin family.
Genetic Association Studies of Complex Diseases and Disorders
Genetic Association Database (archive): CCT7 CDC HuGE Published Literature: CCT7 Positive Disease Associations: Breath Tests Related Studies:
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on Q99832
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
Biological Process: GO:0006457 protein folding GO:0006458 'de novo' protein folding GO:0007339 binding of sperm to zona pellucida GO:0032212 positive regulation of telomere maintenance via telomerase GO:0050821 protein stabilization GO:0061077 chaperone-mediated protein folding GO:1901998 toxin transport GO:1904851 positive regulation of establishment of protein localization to telomere GO:1904871 positive regulation of protein localization to Cajal body GO:1904874 positive regulation of telomerase RNA localization to Cajal body
R-HSA-389954 Hydrolysis of ATP and release of tubulin folding intermediate from CCT/TriC R-HSA-389961 ADP is exchanged for ATP in the (ADP:CCT/TriC):tubulin complex R-HSA-389970 Actin/tubulin:prefoldin complex associates with CCT/TriC R-HSA-390470 Association of CCT/TriC with other substrates during biosynthesis (unknown chaperone) R-HSA-391266 Association of CCT/TriC with sphingosine kinase 1 R-HSA-6814119 TRiC/CCT binds unfolded G-protein beta subunit R-HSA-390453 Hydrolysis of ATP and release of folded actin from CCT/TriC R-HSA-8850527 PDCL releases folded G-beta from TRiC/CCT R-HSA-8850539 Release of GNB5:RGS dimers from CCT/TRiC R-HSA-390459 Exchange of ADP for ATP in CCT/TriC:actin complex R-HSA-6814124 ATP binds G-protein beta associated TRiC/CCT R-HSA-8850529 RGS proteins bind GNB5 and CCT/TRiC R-HSA-8850534 PDCL promotes G-protein beta 5 folding R-HSA-6814121 PDCL binds G-protein beta and TRiC/CCT R-HSA-6814120 ATP hydrolysis promotes folding of G-protein beta by TRiC/CCT R-HSA-389960 Formation of tubulin folding intermediates by CCT/TriC R-HSA-389957 Prefoldin mediated transfer of substrate to CCT/TriC R-HSA-390471 Association of TriC/CCT with target proteins during biosynthesis R-HSA-6814122 Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding R-HSA-390450 Folding of actin by CCT/TriC R-HSA-389958 Cooperation of Prefoldin and TriC/CCT in actin and tubulin folding R-HSA-390466 Chaperonin-mediated protein folding R-HSA-391251 Protein folding R-HSA-392499 Metabolism of proteins