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CCT5

Function

Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis (PubMed:25467444). The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance (PubMed:25467444). 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 (PubMed:20080638). The TRiC complex plays a role in the folding of actin and tubulin (Probable).

Involvement in disease

Neuropathy, hereditary sensory, with spastic paraplegia, autosomal recessive

HSNSP

A disease characterized by spastic paraplegia and progressive distal sensory neuropathy leading to mutilating ulcerations of the upper and lower limbs.

None

The disease is caused by variants affecting the gene represented in this entry.

Post-translational modifications

Ubiquitinated by the DCX(DCAF12) complex specifically recognizes the diglutamate (Glu-Glu) at the C-terminus, leading to its degradation.

Sequence Similarities

Belongs to the TCP-1 chaperonin family.

Cellular localization

Alternative names

CCTE, KIAA0098, CCT5, T-complex protein 1 subunit epsilon, TCP-1-epsilon, CCT-epsilon, Chaperonin containing T-complex polypeptide 1 subunit 5

swissprot:P48643 entrezGene:22948 omim:610150