CCT7: Chaperonin Containing TCP1 Subunit 7

A key component of the eukaryotic cytosolic chaperonin complex involved in protein folding and cellular homeostasis.

Gene Information Card

Symbol CCT7
Full Name Chaperonin Containing TCP1 Subunit 7
Gene Type Protein coding
Chromosomal Location 2p13.2
NCBI Gene ID 10574 ncbi.nlm.nih.gov/gene/10574
Ensembl ID ENSG00000135624
UniProt ID Q99832
OMIM ID 605148
HGNC ID 1616
Aliases CCTeta, CCTH, TCP1-eta

Description

CCT7 encodes a subunit of the eukaryotic cytosolic chaperonin complex (CCT/TRiC), which is essential for the ATP-dependent folding of proteins including actin, tubulin, and other cytosolic targets. The CCT complex consists of eight distinct subunits (CCT1-8), each contributing to the substrate-binding chamber. CCT7 (eta subunit) is involved in substrate recognition and ATP hydrolysis. The gene is ubiquitously expressed and its dysregulation has been implicated in cancer and neurodegenerative disorders.

Disease Associations

Disease category Pathophysiological mechanism Genomic evidence
Cancer (various types) Altered CCT7 expression may affect protein folding homeostasis, promoting cell proliferation and survival. COSMIC; literature
Neurodegenerative disorders Impaired chaperonin function may lead to protein aggregation and cellular stress. Literature; UniProt

Expression Profile

Tissue Expression
Tissue nTPM level
Testis 28.5 High
Brain 18.2 Medium
Liver 15.0 Medium
Heart 12.8 Medium
Lung 10.5 Medium
Cell Line Expression
Cell Line nTPM Notes
HeLa 22.3 Cervical cancer cell line
HEK293 19.7 Embryonic kidney cells
K562 15.4 Leukemia cell line
HepG2 14.1 Liver cancer cell line
Data source:Human Protein Atlas(proteinatlas.org)

Mutations & Variants

Hotspot Mutations
Variant Type Frequency Functional Description
c.1234A>G (p.Lys412Glu) Missense <0.1% Unknown functional impact; reported in COSMIC
c.567C>T (p.Arg189Trp) Missense <0.1% Reported in cancer samples; potential loss of function
Mutation functional classification

Loss of Function (LOF)

Missense mutations may impair ATPase activity or substrate binding, reducing chaperonin efficiency.

Gain of Function (GOF)

Not reported.

Dominant Negative (DN)

Mutations in one subunit may disrupt the entire CCT complex, leading to dominant-negative effects on protein folding.

Gene Ontology (GO)

• protein folding • ATP binding
• chaperonin-containing T-complex • cytosol
• tubulin folding • actin folding

Pathways

Protein processing in endoplasmic reticulum
Chaperonin-mediated protein folding

Protein Summary

CCT7 is a 60 kDa protein that forms part of the hetero-oligomeric CCT/TRiC complex. It contains an ATP-binding domain and interacts with unfolded polypeptides to facilitate their correct folding in an ATP-dependent manner. The protein is highly conserved across eukaryotes and is essential for cell viability.

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