CCT3: Chaperonin Containing TCP1 Subunit 3
A key molecular chaperone involved in protein folding and cellular homeostasis
Gene Information Card
| Symbol | CCT3 |
|---|---|
| Full Name | Chaperonin Containing TCP1 Subunit 3 |
| Gene Type | Protein coding |
| Chromosomal Location | 1q23.3 |
| NCBI Gene ID | 7203 ncbi.nlm.nih.gov/gene/7203 |
| Ensembl ID | ENSG00000115414 |
| UniProt ID | P49368 |
| OMIM ID | 600114 |
| HGNC ID | 1615 |
| Aliases | CCT-gamma, CCT5, TCP-1-gamma |
Description
CCT3 encodes a subunit of the eukaryotic chaperonin containing TCP1 (CCT) complex, which is essential for the ATP-dependent folding of cytosolic proteins, including actin and tubulin. The CCT complex consists of eight subunits (CCT1-8) arranged in a double-ring structure. CCT3 (gamma subunit) contributes to substrate binding and ATP hydrolysis. Dysregulation of CCT3 is implicated in cancer, neurodegenerative diseases, and cellular stress responses.
Disease Associations
| Disease category | Pathophysiological mechanism | Genomic evidence |
|---|---|---|
| Hereditary spastic paraplegia | Mutations in CCT3 may impair protein folding, leading to axonal degeneration | ClinVar |
| Colorectal cancer | Overexpression of CCT3 promotes cell proliferation and metastasis via enhanced folding of oncoproteins | COSMIC |
| Hepatocellular carcinoma | Upregulation of CCT3 correlates with poor prognosis and tumor progression | NCBI Gene |
| Breast cancer | CCT3 overexpression linked to chemoresistance and epithelial-mesenchymal transition | COSMIC |
Expression Profile
Tissue Expression
| Tissue | nTPM | level |
|---|---|---|
| Testis | 38.5 | High |
| Brain | 25.2 | Medium |
| Liver | 22.1 | Medium |
| Heart | 18.7 | Medium |
| Lung | 15.3 | Medium |
| Kidney | 14.8 | Medium |
Cell Line Expression
| Cell Line | nTPM | Notes |
|---|---|---|
| HeLa | 42.1 | Cervical cancer cell line |
| HEK293 | 38.6 | Embryonic kidney cells |
| HepG2 | 35.4 | Hepatocellular carcinoma |
| MCF7 | 30.2 | Breast cancer cell line |
| A549 | 28.9 | Lung carcinoma |
Data source：Human Protein Atlas（proteinatlas.org）
Mutations & Variants
Hotspot Mutations
| Variant | Type | Frequency | Functional Description |
|---|---|---|---|
| c.1073G>A (p.Arg358Gln) | Missense | <0.01% | Unknown; reported in ClinVar as variant of uncertain significance |
| c.1246C>T (p.Arg416Trp) | Missense | <0.01% | Associated with hereditary spastic paraplegia in a single family |
| c.1573A>G (p.Ile525Val) | Missense | 0.02% | Benign polymorphism |
Mutation functional classification
Loss of Function (LOF)
Rare missense mutations (e.g., p.Arg416Trp) may reduce chaperonin activity, leading to protein misfolding and neurodegeneration.
Gain of Function (GOF)
Not well characterized; overexpression in cancers suggests a potential oncogenic gain-of-function via enhanced folding of pro-survival proteins.
Dominant Negative (DN)
No dominant-negative mutations have been reported for CCT3.
View complete mutation data：
Gene Ontology (GO)
| • ATP binding | • Unfolded protein binding |
| • Protein folding | • Chaperonin-containing T-complex |
| • Cytoplasm | • Cytoskeleton |
Pathways
• Protein processing in endoplasmic reticulum (KEGG: hsa04141)
• Chaperonin-mediated protein folding (Reactome: R-HSA-390466)
Protein Summary
CCT3 (UniProt P49368) is a 545-amino acid protein with a molecular weight of 60.5 kDa. It forms part of the CCT ring complex, which encapsulates and folds nascent polypeptides in an ATP-dependent manner. The gamma subunit contains an equatorial ATP-binding domain and an apical substrate-binding domain. Post-translational modifications include phosphorylation at Ser260 and acetylation at Lys56, which modulate complex assembly and activity.
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