Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin. Heterooligomeric complex of about 850 to 900 kDa that forms two stacked rings, 12 to 16 nm in diameter. Interacts with PACRG. Component of the BBS/CCT complex composed at least of MKKS, BBS10, BBS12, TCP1, CCT2, CCT3, CCT4, CCT5 AND CCT8. Belongs to the TCP-1 chaperonin family. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Molecular Function: protein binding; ubiquitin protein ligase binding; unfolded protein binding
Biological Process: chaperone cofactor-independent protein folding; chaperone-mediated protein complex assembly; neutrophil degranulation; positive regulation of telomerase activity; positive regulation of telomere maintenance via telomerase; protein folding; protein stabilization