TCP-1 beta is a molecular chaperone that is member of the chaperonin containing TCP1 complex (CCT), also known as the TCP1 ring complex (TRiC). The CCT 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 TCP-1 beta gene have been observed but not thoroughly characterized. A disease associated with TCP-1 beta protein dysfunction include epididymo-orchitis.
99D8.1 CCT-beta CCTB PRO1633 TCP-1-beta T-complex protein 1 subunit beta T-complex protein 1 beta subunit chaperonin containing t-complex polypeptide 1 beta subunit chaperonin containing t-complex polypeptide 1 subunit 2; CCT-beta; chaperonin containing t-complex polypeptide 1, beta subunit; chaperonin containing t-complex polypeptide 1, subunit 2; chaperonin containing TCP1, subunit 2 (beta); chaperonin subunit 2 (beta); epididymis secretory sperm binding protein Li 100n; T-complex protein 1 subunit beta; T-complex protein 1, beta subunit; TCP-1-beta
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