CCT6A 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. 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 mouse Ortholog: 5|5 G1.3
Cellular Component:  acrosomal vesicle; cell body; chaperonin-containing T-complex; cytoplasm; cytosol; microtubule; zona pellucida receptor complex
Molecular Function:  ATP binding; ATP hydrolysis activity; ATP-dependent protein folding chaperone; nucleotide binding; protein binding; protein folding chaperone; unfolded protein binding; WD40-repeat domain 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 telomere maintenance via telomerase; protein folding; protein stabilization
Reference #:  P80317 (UniProtKB)
Alt. Names/Synonyms: CCT-zeta; CCT-zeta-1; Cct6; Cct6a; Cctz; Cctz-1; Cctz1; chaperonin containing TCP-1; chaperonin containing Tcp1, subunit 6a (zeta); chaperonin subunit 6a (zeta); T-complex protein 1 subunit zeta; TCP-1-zeta; TCPZ
Gene Symbols: Cct6a
Molecular weight: 58,004 Da
Basal Isoelectric point: 6.63  Predict pI for various phosphorylation states
Select Structure to View Below

CCT6A

Protein Structure Not Found.


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