The protein encoded by this gene is 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. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Nov 2010].
Machida, Masutani, Kobayashi, Mikami, Nishino, Miyazawa, Imataka: "Reconstitution of the human chaperonin CCT by co-expression of the eight distinct subunits in mammalian cells." in: Protein expression and purification, Vol. 82, Issue 1, pp. 61-9, (2012) (PubMed).
Seo, Baye, Schulz, Beck, Zhang, Slusarski, Sheffield: "BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family chaperonins and mediate BBSome assembly." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 107, Issue 4, pp. 1488-93, (2010) (PubMed).
Abe, Yoon, Kubota, Mendoza, Gygi, Blenis: "p90 ribosomal S6 kinase and p70 ribosomal S6 kinase link phosphorylation of the eukaryotic chaperonin containing TCP-1 to growth factor, insulin, and nutrient signaling." in: The Journal of biological chemistry, Vol. 284, Issue 22, pp. 14939-48, (2009) (PubMed).
Goudreault, DAmbrosio, Kean, Mullin, Larsen, Sanchez, Chaudhry, Chen, Sicheri, Nesvizhskii, Aebersold, Raught, Gingras: "A PP2A phosphatase high density interaction network identifies a novel striatin-interacting phosphatase and kinase complex linked to the cerebral cavernous malformation 3 (CCM3) protein." in: Molecular & cellular proteomics : MCP, Vol. 8, Issue 1, pp. 157-71, (2009) (PubMed).