Harmonizome 3.0

chaperonin containing TCP1, subunit 4 (delta) pseudogene 2

heat shock 60kDa protein 1 (chaperonin)

This gene encodes a member of the chaperonin family. The encoded mitochondrial protein may function as a signaling molecule in the innate immune system. This protein is essential for the folding and assembly of newly imported proteins in the mitochondria. This gene is adjacent to a related family member and the region between the 2 genes functions as a bidirectional promoter. Several pseudogenes have been associated with this gene. Two transcript variants encoding the same protein have been identified for this gene. Mutations associated with this gene cause autosomal recessive spastic paraplegia 13. [provided by RefSeq, Jun 2010]

heat shock 60kDa protein 1 (chaperonin) pseudogene

chaperonin containing TCP1, subunit 8 (theta) pseudogene 1

heat shock 60kDa protein 1 (chaperonin) pseudogene 17

heat shock 60kDa protein 1 (chaperonin) pseudogene 16

heat shock 60kDa protein 1 (chaperonin) pseudogene 15

heat shock 60kDa protein 1 (chaperonin) pseudogene 14

heat shock 60kDa protein 1 (chaperonin) pseudogene 13

heat shock 60kDa protein 1 (chaperonin) pseudogene 12

heat shock 60kDa protein 1 (chaperonin) pseudogene 11

heat shock 60kDa protein 1 (chaperonin) pseudogene 10

heat shock 60kDa protein 1 (chaperonin) pseudogene 19

heat shock 60kDa protein 1 (chaperonin) pseudogene 18

ClpB homolog, mitochondrial AAA ATPase chaperonin

This gene belongs to the ATP-ases associated with diverse cellular activities (AAA+) superfamily. Members of this superfamily form ring-shaped homo-hexamers and have highly conserved ATPase domains that are involved in various processes including DNA replication, protein degradation and reactivation of misfolded proteins. All members of this family hydrolyze ATP through their AAA+ domains and use the energy generated through ATP hydrolysis to exert mechanical force on their substrates. In addition to an AAA+ domain, the protein encoded by this gene contains a C-terminal D2 domain, which is characteristic of the AAA+ subfamily of Caseinolytic peptidases to which this protein belongs. It cooperates with Hsp70 in the disaggregation of protein aggregates. Allelic variants of this gene are associated with 3-methylglutaconic aciduria, which causes cataracts and neutropenia. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Apr 2015]

chaperonin containing TCP1, subunit 5 (epsilon) pseudogene 1

chaperonin containing TCP1, subunit 4 (delta) pseudogene 1

chaperonin containing TCP1, subunit 3 (gamma) pseudogene 1

chaperonin containing TCP1, subunit 8 (theta)-like 1, pseudogene

Predicted to enable unfolded protein binding activity. Predicted to be involved in protein folding. Predicted to be located in cytoplasm. Predicted to be part of chaperonin-containing T-complex. [provided by Alliance of Genome Resources, Mar 2025]

chaperonin containing TCP1, subunit 6A (zeta 1)

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. Alternate transcriptional splice variants of this gene, encoding different isoforms, have been characterized. In addition, several pseudogenes of this gene have been located. [provided by RefSeq, Jun 2010]

chaperonin containing TCP1, subunit 6B (zeta 2)

This gene encodes 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. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Feb 2015]

heat shock 60kDa protein 1 (chaperonin) pseudogene 3

heat shock 60kDa protein 1 (chaperonin) pseudogene 2

heat shock 60kDa protein 1 (chaperonin) pseudogene 1

heat shock 60kDa protein 1 (chaperonin) pseudogene 7

heat shock 60kDa protein 1 (chaperonin) pseudogene 6

heat shock 60kDa protein 1 (chaperonin) pseudogene 5

heat shock 60kDa protein 1 (chaperonin) pseudogene 4

heat shock 60kDa protein 1 (chaperonin) pseudogene 9

heat shock 60kDa protein 1 (chaperonin) pseudogene 8

chaperonin containing TCP1, subunit 8 (theta)

This gene encodes the theta subunit of the CCT chaperonin, which is abundant in the eukaryotic cytosol and may be involved in the transport and assembly of newly synthesized proteins. Alternative splicing results in multiple transcript variants of this gene. A pseudogene related to this gene is located on chromosome 1. [provided by RefSeq, Sep 2013]

chaperonin containing TCP1, subunit 2 (beta)

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. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Nov 2010]

chaperonin containing TCP1, subunit 3 (gamma)

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. Alternate transcriptional splice variants have been characterized for this gene. In addition, a pseudogene of this gene has been found on chromosome 8. [provided by RefSeq, Aug 2010]

chaperonin containing TCP1, subunit 7 (eta)

This gene encodes 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. Alternative splicing results in multiple transcript variants. Related pseudogenes have been identified on chromosomes 5 and 6. [provided by RefSeq, Oct 2009]

chaperonin containing TCP1, subunit 4 (delta)

The chaperonin containing TCP1 (MIM 186980) complex (CCT), also called the TCP1 ring complex, consists of 2 back-to-back rings, each containing 8 unique but homologous subunits, such as CCT4. CCT assists the folding of newly translated polypeptide substrates through multiple rounds of ATP-driven release and rebinding of partially folded intermediate forms. Substrates of CCT include the cytoskeletal proteins actin (see MIM 102560) and tubulin (see MIM 191130), as well as alpha-transducin (MIM 139330) (Won et al., 1998 [PubMed 9819444]).[supplied by OMIM, Mar 2008]

chaperonin containing TCP1, subunit 5 (epsilon)

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]

chaperonin containing TCP1, subunit 7 (eta) pseudogene 2

chaperonin containing TCP1, subunit 7 (eta) pseudogene 1

chaperonin containing TCP1, subunit 5 (epsilon) pseudogene 2

chaperonin containing TCP1, subunit 6 (zeta) pseudogene 4

chaperonin containing TCP1, subunit 6 (zeta) pseudogene 5

chaperonin containing TCP1, subunit 6 (zeta) pseudogene 2

chaperonin containing TCP1, subunit 6 (zeta) pseudogene 3

chaperonin containing TCP1, subunit 6 (zeta) pseudogene 1

chaperonin containing TCP1, subunit 8 (theta)-like 2

Predicted to enable unfolded protein binding activity. Predicted to be involved in protein folding. Predicted to be located in cytoplasm. Predicted to be part of chaperonin-containing T-complex. [provided by Alliance of Genome Resources, Mar 2025]

heat shock 60kDa protein 1 (chaperonin) pseudogene 22

heat shock 60kDa protein 1 (chaperonin) pseudogene 20

heat shock 60kDa protein 1 (chaperonin) pseudogene 21

chaperonin containing TCP1, subunit 5 (epsilon) pseudogene 2

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Chaperonin Cpn10 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Chaperonin Cpn10, conserved site protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From GeneRIF Biological Term Annotations

genes co-occuring with the biological term cpn10 in literature-supported statements describing functions of genes from the GeneRIF Biological Term Annotations dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the chaperonin-containing t-complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the chaperonin-containing t-complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From CORUM Protein Complexes

proteins in the CCT complex (chaperonin containing TCP1 complex) protein complex from the CORUM Protein Complexes dataset.

From CORUM Protein Complexes

proteins in the CCT complex (chaperonin containing TCP1 complex), testis specific protein complex from the CORUM Protein Complexes dataset.

From GeneRIF Biological Term Annotations

genes co-occuring with the biological term chaperonin in literature-supported statements describing functions of genes from the GeneRIF Biological Term Annotations dataset.

From GO Biological Process Annotations 2015

genes participating in the post-chaperonin tubulin folding pathway biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the chaperonin-containing t-complex cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Chaperonin TCP-1, conserved site protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Chaperonin Cpn60 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Chaperonin Cpn60, conserved site protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the McKusick-Kaufman/Bardet-Biedl syndromes putative chaperonin protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Heat shock chaperonin-binding protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the GroES (chaperonin 10)-like protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Chaperonin Cpn60/TCP-1 family protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the TCP-1-like chaperonin intermediate domain protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From Reactome Pathways 2014

proteins participating in the Chaperonin-mediated protein folding pathway from the Reactome Pathways dataset.

From Reactome Pathways 2014

proteins participating in the Post-chaperonin tubulin folding pathway pathway from the Reactome Pathways dataset.

From Reactome Pathways 2024

proteins participating in the Chaperonin-mediated protein folding pathway from the Reactome Pathways 2024 dataset.

From Reactome Pathways 2024

proteins participating in the Post-chaperonin tubulin folding pathway pathway from the Reactome Pathways 2024 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the chaperonin-containing T-complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the Chaperonin ATPase complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the chaperonin-containing T-complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.