CCT5 chaperonin containing TCP1 subunit 5 [Homo sapiens (human)] - Gene

Summary

Official Symbol: CCT5provided by HGNC
Official Full Name: chaperonin containing TCP1 subunit 5provided by HGNC
Primary source: HGNC:HGNC:1618
See related: Ensembl:ENSG00000150753 MIM:610150; AllianceGenome:HGNC:1618
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Homo sapiens
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as: CCTE; HSNSP; HEL-S-69; PNAS-102; CCT-epsilon; TCP-1-epsilon
Summary: 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]
Expression: Ubiquitous expression in testis (RPKM 38.0), appendix (RPKM 31.8) and 25 other tissues See more
Orthologs: mouse all
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Genomic context

Location:: 5p15.2

Exon count:: 13

Annotation release	Status	Assembly	Chr	Location
RS_2024_08	current	GRCh38.p14 (GCF_000001405.40)	5	NC_000005.10 (10249921..10266412)
RS_2024_08	current	T2T-CHM13v2.0 (GCF_009914755.1)	5	NC_060929.1 (10189222..10205724)
RS_2024_09	previous assembly	GRCh37.p13 (GCF_000001405.25)	5	NC_000005.9 (10250033..10266524)

Chromosome 5 - NC_000005.10 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: HPA RNA-seq normal tissues HPA RNA-seq normal tissues
Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
BioProject: PRJEB4337
Publication: PMID 24309898
Analysis date: Wed Apr 4 07:08:55 2018

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Increased CCT5 expression is a potential unfavourable factor promoting the growth of nasopharyngeal carcinoma.
Title: Increased CCT5 expression is a potential unfavourable factor promoting the growth of nasopharyngeal carcinoma.
Structural and Dynamic Disturbances Revealed by Molecular Dynamics Simulations Predict the Impact on Function of CCT5 Chaperonin Mutations Associated with Rare Severe Distal Neuropathies.
Title: Structural and Dynamic Disturbances Revealed by Molecular Dynamics Simulations Predict the Impact on Function of CCT5 Chaperonin Mutations Associated with Rare Severe Distal Neuropathies.
CCT5 induces epithelial-mesenchymal transition to promote gastric cancer lymph node metastasis by activating the Wnt/beta-catenin signalling pathway.
Title: CCT5 induces epithelial-mesenchymal transition to promote gastric cancer lymph node metastasis by activating the Wnt/β-catenin signalling pathway.
CCT5 interacts with cyclin D1 promoting lung adenocarcinoma cell migration and invasion.
Title: CCT5 interacts with cyclin D1 promoting lung adenocarcinoma cell migration and invasion.
A Novel CCT5 Missense Variant Associated with Early Onset Motor Neuropathy.
Title: A Novel CCT5 Missense Variant Associated with Early Onset Motor Neuropathy.
CCT5 complex caps mutant mHTT fibrils at their tips and encapsulates mHTT oligomers, providing a structural description of the inhibition of mHTTQ46-Ex1 by CCT5 complex and a shared mechanism of mHTT inhibition between TRiC chaperonin and the CCT5 complex
Title: Structural Mechanisms of Mutant Huntingtin Aggregation Suppression by the Synthetic Chaperonin-like CCT5 Complex Explained by Cryoelectron Tomography.
H147R CCT5 was not as efficient in chaperoning these substrates as wild type CCT5.
Title: Biochemical characterization of mutants in chaperonin proteins CCT4 and CCT5 associated with hereditary sensory neuropathy.
Both CCT4 and CCT5 homo-oligomers have the property of forming 8-fold double rings absent the other subunits, and these complexes carry out chaperonin reactions without other partner subunits.
Title: Human CCT4 and CCT5 chaperonin subunits expressed in Escherichia coli form biologically active homo-oligomers.
introduction of the truncated human CCT epsilon subunit into yeast cells
Title: A novel function of the human chaperonin CCT epsilon subunit in yeast.
Observational study of gene-disease association. (HuGE Navigator)
Title: Association study of 182 candidate genes in anorexia nervosa.

Submit: New GeneRIF Correction See all GeneRIFs (12)

Phenotypes

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Review eQTL and phenotype association data in this region using PheGenI

Associated conditions

Description	Tests
Hereditary sensory and autonomic neuropathy with spastic paraplegia MedGen: C1850395 OMIM: 256840 GeneReviews: Not available	Compare labs

EBI GWAS Catalog

Description
Genome-wide association study meta-analysis of chronic widespread pain: evidence for involvement of the 5p15.2 region. EBI GWAS Catalog EBI GWAS CatalogPubMed

Variation

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See variants in ClinVar

See studies and variants in dbVar

See Variation Viewer (GRCh37.p13)

See Variation Viewer (GRCh38)

HIV-1 interactions

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Protein interactions

Protein	Gene	Interaction	Pubs
Vif	vif	HIV-1 Vif interacts with CCT5	PubMed

Go to the HIV-1, Human Interaction Database

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

A002D32 (e-PCR)
- UniSTS:63494

RH48173 (e-PCR)
- UniSTS:64273

RH25325 (e-PCR)
- UniSTS:87179

D5S2412 (e-PCR)
- UniSTS:36250

G19980 (e-PCR)
- UniSTS:3774

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables ATP binding	IEA Inferred from Electronic Annotation more info
enables ATP hydrolysis activity	IEA Inferred from Electronic Annotation more info
enables ATP-dependent protein folding chaperone	IEA Inferred from Electronic Annotation more info
enables G-protein beta-subunit binding	IPI Inferred from Physical Interaction more info	PubMed
enables beta-tubulin binding	IPI Inferred from Physical Interaction more info	PubMed
enables mRNA 3'-UTR binding	IDA Inferred from Direct Assay more info	PubMed
enables mRNA 5'-UTR binding	IDA Inferred from Direct Assay more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein folding chaperone	IDA Inferred from Direct Assay more info	PubMed
enables unfolded protein binding	IBA Inferred from Biological aspect of Ancestor more info

Process	Evidence Code	Pubs
involved_in binding of sperm to zona pellucida	IEA Inferred from Electronic Annotation more info
involved_in chaperone mediated protein folding independent of cofactor	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in chaperone-mediated protein folding	IDA Inferred from Direct Assay more info	PubMed
involved_in positive regulation of protein localization to Cajal body	HMP more info	PubMed
involved_in positive regulation of telomerase RNA localization to Cajal body	HMP more info	PubMed
acts_upstream_of positive regulation of telomere maintenance via telomerase	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein folding	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein folding	IDA Inferred from Direct Assay more info	PubMed
involved_in protein stabilization	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in response to virus	IEP Inferred from Expression Pattern more info	PubMed

Component	Evidence Code	Pubs
located_in cell body	IEA Inferred from Electronic Annotation more info
located_in centrosome	IDA Inferred from Direct Assay more info	PubMed
part_of chaperonin-containing T-complex	IBA Inferred from Biological aspect of Ancestor more info
part_of chaperonin-containing T-complex	IDA Inferred from Direct Assay more info	PubMed
part_of chaperonin-containing T-complex	IPI Inferred from Physical Interaction more info	PubMed
part_of chaperonin-containing T-complex	TAS Traceable Author Statement more info	PubMed
located_in cytosol	TAS Traceable Author Statement more info
located_in extracellular exosome	HDA more info	PubMed
located_in microtubule	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: T-complex protein 1 subunit epsilon

Names: chaperonin containing T-complex polypeptide 1 subunit 5; chaperonin containing TCP1, subunit 5 (epsilon); epididymis secretory protein Li 69

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

Genomic

NG_012160.1 RefSeqGene

Range

5001..21220

Download

GenBank, FASTA, Sequence Viewer (Graphics), LRG_361

mRNA and Protein(s)

NM_001306153.1 → NP_001293082.1 T-complex protein 1 subunit epsilon isoform b

Status: REVIEWED

Description

Transcript Variant: This variant (2) uses an alternate splice site in the 5' terminal exon, resulting in translation initiation at an alternate start codon, compared to variant 1. The encoded isoform (b) has a distinct N-terminus and is shorter than isoform a.

Source sequence(s)

AI290125, AI470998, AK301760, DC368224, FJ224303

Consensus CDS

CCDS82988.1

UniProtKB/TrEMBL

B4DX08, E9PCA1

Related

ENSP00000423318.1, ENST00000503026.5

Conserved Domains (1) summary

cd03339
Location:15 → 514

TCP1_epsilon; TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins ...
NM_001306154.2 → NP_001293083.1 T-complex protein 1 subunit epsilon isoform c

See identical proteins and their annotated locations for NP_001293083.1

Status: REVIEWED

Description

Transcript Variant: This variant (3) lacks an alternate in-frame exon in the 5' coding region, compared to variant 1, resulting in an isoform (c) that is shorter than isoform a.

Source sequence(s)

AK302368, FJ224303

Consensus CDS

CCDS82989.1

UniProtKB/TrEMBL

B4DYC8, E7ENZ3

Related

ENSP00000426923.1, ENST00000515390.5

Conserved Domains (1) summary

cd03339
Location:10 → 480

TCP1_epsilon; TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins ...
NM_001306155.2 → NP_001293084.1 T-complex protein 1 subunit epsilon isoform d

See identical proteins and their annotated locations for NP_001293084.1

Status: REVIEWED

Description

Transcript Variant: This variant (4) contains an alternate 5' terminal exon, resulting in an alternate 5' UTR and translation initiation at a downstream in-frame start codon, and it also lacks an in-frame exon in the 5' coding region, compared to variant 1. The encoded isoform (d) is shorter at the N-terminus, compared to isoform a.

Source sequence(s)

AC012640, AK302383, DB449481, FJ224303

Consensus CDS

CCDS82990.1

UniProtKB/TrEMBL

B4DYC8

Related

ENSP00000423052.1, ENST00000506600.1

Conserved Domains (1) summary

cd03339
Location:1 → 442

TCP1_epsilon; TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins ...
NM_001306156.2 → NP_001293085.1 T-complex protein 1 subunit epsilon isoform e

See identical proteins and their annotated locations for NP_001293085.1

Status: REVIEWED

Description

Transcript Variant: This variant (5) contains an alternate 5' terminal exon, resulting in an alternate 5' UTR and translation initiation at a downstream in-frame start codon, compared to variant 1. The encoded isoform (e) is shorter at the N-terminus, compared to isoform a.

Source sequence(s)

AC012640, AK293341, DB449481, FJ224303

Consensus CDS

CCDS77996.1

UniProtKB/TrEMBL

B4DDU6, B7ZAR1

Related

ENSP00000427297.1, ENST00000515676.5

Conserved Domains (1) summary

cd03339
Location:1 → 497

TCP1_epsilon; TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins ...
NM_012073.5 → NP_036205.1 T-complex protein 1 subunit epsilon isoform a

See identical proteins and their annotated locations for NP_036205.1

Status: REVIEWED

Description

Transcript Variant: This variant (1) represents the longest transcript and encodes the longest isoform (a).

Source sequence(s)

FJ224303

Consensus CDS

CCDS3877.1

UniProtKB/Swiss-Prot

A8JZY8, A8K2X8, B4DYD8, P48643

UniProtKB/TrEMBL

Q9BU08, V9HW37

Related

ENSP00000280326.4, ENST00000280326.9

Conserved Domains (1) summary

cd03339
Location:10 → 535

TCP1_epsilon; TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins ...