CCT5

Chr 5

chaperonin containing TCP1 subunit 5

Also known as: CCT-epsilon, CCTE, HEL-S-69, HSNSP, PNAS-102, TCP-1-epsilon

NCBI Gene: 22948 ENSG00000150753 UniProt: P48643

The CCT5 protein is a component of the chaperonin-containing T-complex (TRiC) that assists in folding actin, tubulin, and other proteins in an ATP-dependent manner. Mutations cause hereditary sensory neuropathy with spastic paraplegia, inherited in an autosomal recessive pattern. This gene is highly constrained against loss-of-function variants, indicating it is essential for normal cellular function.

ResearchSummary from RefSeq, OMIM, UniProt

The protein encoded by this gene is a molecular chaperone that is a member of the chaperonin containing TCP1 complex (CCT), also known as the TCP1 ring complex (TRiC). This complex consists of two identical stacked rings, each containing eight different proteins. Unfolded polypeptides enter the central cavity of the complex and are folded in an ATP-dependent manner. The complex folds various proteins, including actin and tubulin. Mutations in this gene cause hereditary sensory and autonomic neuropathy with spastic paraplegia (HSNSP). Alternative splicing results in multiple transcript variants. Related pseudogenes have been identified on chromosomes 5 and 13. [provided by RefSeq, Apr 2015]

ResearchGenerating clinical summary…

Primary Disease Associations & Inheritance

UniProtNeuropathy, hereditary sensory, with spastic paraplegia, autosomal recessive

Clinical highlights

Interpreting a novel variant

Loss of function is the curated mechanism (Gene2Phenotype) and the gene is intolerant of it in the population — truncating, frameshift and canonical splice variants carry more prior weight here than missense.Curated gene-level mechanism — a prior for triage, not a per-variant call.

Active trials

Pubs (1 yr)

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P/LP submissions

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P/LP missense

0.19

LOEUF· LoF intol.

LOF

Mechanism· G2P

Some data sources returned errors (1)

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