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: 11 A3.2|11 14.25 cM
Cellular Component:  cell body; cell projection; centrosome; chaperonin-containing T-complex; cilium; cytoplasm; cytoskeleton; cytosol; microtubule; nucleoplasm; zona pellucida receptor complex
Molecular Function:  ATP binding; nucleotide binding; protein binding; unfolded protein binding
Biological Process:  binding of sperm to zona pellucida; 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; toxin transport
Reference #:  P80315 (UniProtKB)
Alt. Names/Synonyms: 2610204B21Rik; A45; C78323; CCT-delta; Cct4; Cctd; chaperonin containing Tcp1, subunit 4 (delta); chaperonin subunit 4 (delta); OTTMUSP00000005437; RP24-143D17.2; T complex protein 1, delta; T-complex protein 1 subunit delta; TCP-1 delta; TCP-1-delta; TCPD
Gene Symbols: Cct4
Molecular weight: 58,066 Da
Basal Isoelectric point: 8.24  Predict pI for various phosphorylation states
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CCT4

Protein Structure Not Found.


Cross-references to other databases:  STRING  |  Reactome  |  BioGPS  |  Pfam  |  Phospho.ELM  |  NetworKIN  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene