CCT8 (Chaperonin Containing TCP1 Subunit 8) is a Protein Coding gene. Among its related pathways are Organelle biogenesis and maintenance and Innate Immune System. Gene Ontology (GO) annotations related to this gene include unfolded protein binding and ATPase activity, coupled. An important paralog of this gene is CCT8L2.
Full Name
Chaperonin Containing TCP1 Subunit 8
Function
Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis (PubMed:25467444). The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance (PubMed:25467444). As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia (PubMed:20080638). The TRiC complex plays a role in the folding of actin and tubulin (Probable).
Biological Process
Binding of sperm to zona pellucida Source: Ensembl Neutrophil degranulation Source: Reactome Pore complex assembly Source: Ensembl Positive regulation of establishment of protein localization to telomere Source: BHF-UCL Positive regulation of protein localization to Cajal body Source: BHF-UCL Positive regulation of telomerase RNA localization to Cajal body Source: BHF-UCL Positive regulation of telomere maintenance via telomerase Source: BHF-UCL Protein folding Source: FlyBase Protein stabilization Source: BHF-UCL Toxin transport Source: Ensembl