CCT2

This gene encodes a molecular chaperone that is 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. Alternate transcriptional splice variants of the gene described in this record have been observed but have not been thoroughly characterized. [provided by RefSeq]

chaperonin containing TCP1, subunit 2 (beta)

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).

Binding of sperm to zona pellucida Source: Ensembl
Chaperone-mediated protein complex assembly Source: MGI
Chaperone mediated protein folding independent of cofactor Source: BHF-UCL
Neutrophil degranulation Source: Reactome
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 activity 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
scaRNA localization to Cajal body Source: BHF-UCL
Toxin transport Source: Ensembl

Cytoplasm