CCT5 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: 5p15.2
Cellular Component:  cell body; centrosome; chaperonin-containing T-complex; cytosol; microtubule; nucleolus
Molecular Function:  ATP binding; beta-tubulin binding; G-protein beta-subunit binding; mRNA 3'-UTR binding; mRNA 5'-UTR 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 telomere maintenance via telomerase; protein folding; protein stabilization; response to virus; toxin transport
Disease: Neuropathy, Hereditary Sensory, With Spastic Paraplegia, Autosomal Recessive
Reference #:  P48643 (UniProtKB)
Alt. Names/Synonyms: CCT-epsilon; CCT5; CCTE; chaperonin containing TCP1, subunit 5 (epsilon); KIAA0098; T-complex protein 1 subunit epsilon; T-complex protein 1, epsilon subunit; TCP-1-epsilon; TCPE
Gene Symbols: CCT5
Molecular weight: 59,671 Da
Basal Isoelectric point: 5.45  Predict pI for various phosphorylation states
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CCT5

Protein Structure Not Found.


Cross-references to other databases:  STRING  |  cBioPortal  |  Wikipedia  |  Reactome  |  neXtProt  |  Protein Atlas  |  BioGPS  |  Pfam  |  RCSB PDB  |  Phospho.ELM  |  NetworKIN  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene  |  InnateDB