CCT4: Chaperonin Containing TCP1 Subunit 4
A key component of the eukaryotic cytosolic chaperonin complex involved in protein folding and cellular homeostasis.
Gene Information Card
| Symbol | CCT4 |
|---|---|
| Full Name | Chaperonin Containing TCP1 Subunit 4 |
| Gene Type | Protein coding |
| Chromosomal Location | 2p15 |
| NCBI Gene ID | 10575 ncbi.nlm.nih.gov/gene/10575 |
| Ensembl ID | ENSG00000115484 |
| UniProt ID | P50991 |
| OMIM ID | 605142 |
| HGNC ID | 1617 |
| Aliases | CCT-delta, CCTD, SRB1 |
Description
CCT4 encodes a subunit of the eukaryotic cytosolic chaperonin complex (CCT/TRiC), which is essential for the ATP-dependent folding of proteins, including actin and tubulin. The CCT complex consists of eight distinct subunits (CCT1-8) arranged in a double-ring structure. CCT4 is the delta subunit and is required for proper assembly and function of the complex. Mutations or dysregulation of CCT4 have been implicated in neurodegenerative disorders and cancer.
Disease Associations
| Disease category | Pathophysiological mechanism | Genomic evidence |
|---|---|---|
| Hereditary sensory neuropathy type IE (HSN1E) | Missense mutations in CCT4 disrupt chaperonin function, leading to impaired protein folding and neuronal degeneration. | ClinVar; PMID: 24656866 |
| Cancer (various) | Overexpression of CCT4 is observed in several cancers, potentially promoting cell proliferation and survival by stabilizing oncogenic proteins. | COSMIC; PMID: 25691885 |
Expression Profile
Tissue Expression
| Tissue | nTPM | level |
|---|---|---|
| Liver | 12.5 | Medium |
| Brain | 8.3 | Low |
| Heart | 6.7 | Low |
| Kidney | 10.1 | Medium |
| Testis | 15.2 | High |
Cell Line Expression
| Cell Line | nTPM | Notes |
|---|---|---|
| HeLa | 14.0 | Cervical cancer cell line |
| HEK293 | 11.5 | Embryonic kidney cells |
| K562 | 9.8 | Leukemia cell line |
| MCF7 | 13.2 | Breast cancer cell line |
Data source：Human Protein Atlas（proteinatlas.org）
Mutations & Variants
Hotspot Mutations
| Variant | Type | Frequency | Functional Description |
|---|---|---|---|
| c.106G>A (p.Gly36Arg) | Missense | Rare | Impaired chaperonin function; associated with HSN1E |
| c.511C>T (p.Arg171Trp) | Missense | Rare | Reduced protein stability; reported in ClinVar |
Mutation functional classification
Loss of Function (LOF)
Missense mutations (e.g., p.Gly36Arg) reduce chaperonin activity, leading to protein misfolding and cellular stress.
Gain of Function (GOF)
Not reported for CCT4.
Dominant Negative (DN)
Some CCT4 mutations may exert dominant-negative effects by incorporating into the CCT complex and disrupting its function.
View complete mutation data：
Gene Ontology (GO)
| • chaperonin-containing T-complex (GO:0005832) | • unfolded protein binding (GO:0051082) |
| • protein folding (GO:0006457) | • ATP binding (GO:0005524) |
| • cellular protein metabolic process (GO:0044267) |
Pathways
• Protein folding (KEGG: hsa04141)
• Chaperonin-mediated protein folding (Reactome: R-HSA-390466)
Protein Summary
CCT4 is a 58 kDa protein that forms part of the hetero-oligomeric chaperonin complex TRiC/CCT. It contains an ATPase domain and is involved in the ATP-dependent folding of cytosolic proteins, particularly actin and tubulin. The protein is highly conserved across eukaryotes and is essential for cell viability.
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