CCT4 Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. 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. The TRiC complex plays a role in the folding of actin and tubulin. Belongs to the TCP-1 chaperonin family. 2 alternatively spliced human isoforms have been reported. Note: This description may include information from UniProtKB.

Protein type: Chaperone

Chromosomal Location of human Ortholog: 2p15

Cellular Component: cell body; cell projection; centrosome; chaperonin-containing T-complex; cytosol; melanosome; microtubule; nucleoplasm; zona pellucida receptor complex

Molecular Function: ATP binding; ATP hydrolysis activity; ATP-dependent protein folding chaperone; protein binding; protein folding chaperone; unfolded protein binding

Biological Process: binding of sperm to zona pellucida; chaperone-mediated protein folding; positive regulation of establishment of protein localization to telomere; positive regulation of telomerase activity; positive regulation of telomerase RNA localization to Cajal body; positive regulation of telomere maintenance via telomerase; protein folding; protein stabilization; scaRNA localization to Cajal body

Reference #: P50991 (UniProtKB)

Alt. Names/Synonyms: CCT-delta; CCT4; CCTD; chaperonin containing t-complex polypeptide 1, delta subunit; chaperonin containing TCP1 subunit 4; chaperonin containing TCP1, subunit 4 (delta); MGC126164; MGC126165; SRB; Stimulator of TAR RNA-binding; T-complex protein 1 subunit delta; TCP-1-delta; TCPD

Gene Symbols: CCT4

Molecular weight: 57,924 Da

Basal Isoelectric point: 7.96 Predict pI for various phosphorylation states

Select Structure to View Below
CCT4

Get PyMOL Script Get Chimera Script