Chaperonin Containing TCP1, Subunit 2 (CCT2)

CCT2  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.Cyclin E (CCNE1), a partner of the cyclin-dependent kinase CDK2, is implicated in the positive control of the G1/S phase transition. CCNE1 degradation is regulated by ubiquitination and proteasomal action, which occur upon autophosphorylation and activation of the CCNE1-CDK2 complex.