CCT2 chaperonin containing TCP1 subunit 2 [Homo sapiens (human)] - Gene

Summary

Official Symbol: CCT2provided by HGNC
Official Full Name: chaperonin containing TCP1 subunit 2provided by HGNC
Primary source: HGNC:HGNC:1615
See related: Ensembl:ENSG00000166226 MIM:605139; AllianceGenome:HGNC:1615
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: CCTB; 99D8.1; PRO1633; CCT-beta; HEL-S-100n; TCP-1-beta
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. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Nov 2010]
Expression: Broad expression in testis (RPKM 107.5), bone marrow (RPKM 41.1) and 24 other tissues See more
Orthologs: mouse all
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Genomic context

Location:: 12q15

Exon count:: 17

Annotation release	Status	Assembly	Chr	Location
RS_2023_10	current	GRCh38.p14 (GCF_000001405.40)	12	NC_000012.12 (69585459..69601570)
RS_2023_10	current	T2T-CHM13v2.0 (GCF_009914755.1)	12	NC_060936.1 (69564374..69580485)
105.20220307	previous assembly	GRCh37.p13 (GCF_000001405.25)	12	NC_000012.11 (69979239..69995350)

Chromosome 12 - NC_000012.12 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: 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?

CCT2 prevented beta-catenin proteasomal degradation to sustain cancer stem cell traits and promote tumor progression in epithelial ovarian cancer.
Title: CCT2 prevented β-catenin proteasomal degradation to sustain cancer stem cell traits and promote tumor progression in epithelial ovarian cancer.
Investigating Chaperonin-Containing TCP-1 subunit 2 as an essential component of the chaperonin complex for tumorigenesis.
Title: Investigating Chaperonin-Containing TCP-1 subunit 2 as an essential component of the chaperonin complex for tumorigenesis.
we suggest that CCT2 correlates with Gli-1 expression and is an important determinant of survival in the colorectal cancer (CRC) patients. The results reveal that CCT2 can regulate the folding of Gli-1 in relation to hypoxia in CRC
Title: Activating CCT2 triggers Gli-1 activation during hypoxic condition in colorectal cancer.
We applied whole-genome sequencing (WGS) on 9 trios where the probands are sporadically affected with the most severe form of the disorder and harbor no coding sequence variants affecting the function of known Hirschsprung disease (HSCR) genes. We found de novo protein-altering variants in three intolerant to change genes-CCT2, VASH1, and CYP26A1-for which a plausible link with the enteric nervous system (ENS) exists
Title: Uncovering the genetic lesions underlying the most severe form of Hirschsprung disease by whole-genome sequencing.
the novel LCA mutations in CCTbeta and the impact of chaperon disability by these mutations in cellular biology.
Title: CCT2 Mutations Evoke Leber Congenital Amaurosis due to Chaperone Complex Instability.
A role for the TRiC subunits TCP1 and CCT2, and potentially the entire TRiC complex, in breast cancer.
Title: Two members of the TRiC chaperonin complex, CCT2 and TCP1 are essential for survival of breast cancer cells and are linked to driving oncogenes.
Increased expression of CCT2 is associated with tumor progression and the clinical behavior of gallbladder carcinoma.
Title: Clinicopathological features and CCT2 and PDIA2 expression in gallbladder squamous/adenosquamous carcinoma and gallbladder adenocarcinoma.
PDCD5 bound the apical domain of the CCTbeta subunit, projecting above the folding cavity without entering it. Like PDCD5, beta-tubulin also interacts with the CCTbeta apical domain, but a second site is found at the sensor loop deep within the folding cavity.
Title: Programmed cell death protein 5 interacts with the cytosolic chaperonin containing tailless complex polypeptide 1 (CCT) to regulate β-tubulin folding.
Destruction of the beta-tubulin:CCT-beta complex provokes Hsp90-dependent protein ubiquitination and degradation.
Title: Targeting β-tubulin:CCT-β complexes incurs Hsp90- and VCP-related protein degradation and induces ER stress-associated apoptosis by triggering capacitative Ca2+ entry, mitochondrial perturbation and caspase overactivation.
PB2 associates with CCT2 as a monomer and the CCT binding site is located in a central region of the PB2 protein.
Title: Association of the influenza virus RNA polymerase subunit PB2 with the host chaperonin CCT.

Submit: New GeneRIF Correction See all GeneRIFs (12)

Phenotypes

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Find tests for this gene in the NIH Genetic Testing Registry (GTR)

Review eQTL and phenotype association data in this region using PheGenI

EBI GWAS Catalog

Description
Many sequence variants affecting diversity of adult human height. 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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Replication interactions

Interaction	Pubs
Knockdown of chaperonin containing TCP1, subunit 2 (CCT2) by siRNA inhibits HIV-1 replication in HeLa P4/R5 cells	PubMed

Protein interactions

Protein	Gene	Interaction	Pubs
Envelope surface glycoprotein gp120	env	Tandem affinity purification and mass spectrometry analysis identify chaperonin containing TCP1 subunit 2 (CCT2), HIV-1 Gag, Gag/Pol, gp120, and Nef incorporated into staufen1 RNP complexes isolated from HIV-1-expressing cells	PubMed
Gag-Pol	gag-pol	Tandem affinity purification and mass spectrometry analysis identify chaperonin containing TCP1 subunit 2 (CCT2), HIV-1 Gag, Gag/Pol, gp120, and Nef incorporated into staufen1 RNP complexes isolated from HIV-1-expressing cells	PubMed
Nef	nef	Tandem affinity purification and mass spectrometry analysis identify chaperonin containing TCP1 subunit 2 (CCT2), HIV-1 Gag, Gag/Pol, gp120, and Nef incorporated into staufen1 RNP complexes isolated from HIV-1-expressing cells	PubMed
Pr55(Gag)	gag	Tandem affinity purification and mass spectrometry analysis identify chaperonin containing TCP1 subunit 2 (CCT2), HIV-1 Gag, Gag/Pol, gp120, and Nef incorporated into staufen1 RNP complexes isolated from HIV-1-expressing cells	PubMed
Tat	tat	Expression of HIV-1 Tat upregulates the abundance of chaperonin containing TCP1, subunit 2 (CCT2) in the nucleoli of Jurkat T-cells	PubMed
Vif	vif	HIV-1 Vif interacts with CCT2	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

WI-19751 (e-PCR)
- UniSTS:82731

RH69725 (e-PCR)
- UniSTS:51770

SHGC-60534 (e-PCR)
- UniSTS:82784

D12S384E (e-PCR)
- UniSTS:148578

RH48183 (e-PCR)
- UniSTS:28851

RH44186 (e-PCR)
- UniSTS:39648

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 protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein folding chaperone	IDA Inferred from Direct Assay more info	PubMed
enables ubiquitin protein ligase binding	IPI Inferred from Physical Interaction more info	PubMed
enables unfolded protein binding	IBA Inferred from Biological aspect of Ancestor more info
enables unfolded protein binding	NAS Non-traceable Author Statement more info	PubMed

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
acts_upstream_of_or_within chaperone-mediated protein complex assembly	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 establishment of protein localization to telomere	IMP Inferred from Mutant Phenotype 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
involved_in positive regulation of telomerase RNA localization to Cajal body	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in positive regulation of telomerase activity	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in 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 folding	NAS Non-traceable Author Statement more info	PubMed
involved_in protein stabilization	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in scaRNA localization to Cajal body	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in azurophil granule lumen	TAS Traceable Author Statement more info
located_in cell body	IEA Inferred from Electronic Annotation more info
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
located_in cytosol	IDA Inferred from Direct Assay more info
located_in cytosol	NAS Non-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 extracellular region	TAS Traceable Author Statement more info
located_in microtubule	IDA Inferred from Direct Assay more info	PubMed
part_of zona pellucida receptor complex	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: T-complex protein 1 subunit beta

Names: T-complex protein 1, beta subunit; chaperonin containing TCP1, subunit 2 (beta); chaperonin containing t-complex polypeptide 1, beta subunit; chaperonin containing t-complex polypeptide 1, subunit 2; epididymis secretory sperm binding protein Li 100n

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.

mRNA and Protein(s)

NM_001198842.2 → NP_001185771.1 T-complex protein 1 subunit beta isoform 2

See identical proteins and their annotated locations for NP_001185771.1

Status: REVIEWED

Description

Transcript Variant: This variant (2) differs in the 5' UTR and coding sequence compared to variant 1. The resulting isoform (2) is shorter at the N-terminus compared to isoform 1.

Source sequence(s)

AA401491, AK316408

Consensus CDS

CCDS55843.1

UniProtKB/TrEMBL

B7Z4R3

Related

ENSP00000445471.2, ENST00000543146.2

Conserved Domains (1) summary

cd03336
Location:1 → 480

TCP1_beta; TCP-1 (CTT or eukaryotic type II) chaperonin family, beta 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 (GroEL) ...
NM_006431.3 → NP_006422.1 T-complex protein 1 subunit beta isoform 1

See identical proteins and their annotated locations for NP_006422.1

Status: REVIEWED

Description

Transcript Variant: This variant (1) encodes the longer isoform (1).

Source sequence(s)

AA401491, AF026166, CB138063

Consensus CDS

CCDS8991.1

UniProtKB/Swiss-Prot

A8K402, B5BTY7, B7Z243, B7Z7K4, B7ZAT2, P78371, Q14D36, Q6IAT3

UniProtKB/TrEMBL

B7Z4R3, V9HW96

Related

ENSP00000299300.6, ENST00000299300.11

Conserved Domains (1) summary

cd03336
Location:11 → 527

TCP1_beta; TCP-1 (CTT or eukaryotic type II) chaperonin family, beta 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 (GroEL) ...