CCT7 chaperonin containing TCP1 subunit 7 [Homo sapiens (human)] - Gene

Summary

Official Symbol: CCT7provided by HGNC
Official Full Name: chaperonin containing TCP1 subunit 7provided by HGNC
Primary source: HGNC:HGNC:1622
See related: Ensembl:ENSG00000135624 MIM:605140; AllianceGenome:HGNC:1622
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: CCTH; CCTETA; NIP7-1; TCP1ETA
Summary: 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]
Expression: Ubiquitous expression in testis (RPKM 102.9), adrenal (RPKM 73.8) and 25 other tissues See more
Orthologs: mouse all
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Genomic context

Location:: 2p13.2

Exon count:: 13

Annotation release	Status	Assembly	Chr	Location
RS_2023_10	current	GRCh38.p14 (GCF_000001405.40)	2	NC_000002.12 (73234308..73253005)
RS_2023_10	current	T2T-CHM13v2.0 (GCF_009914755.1)	2	NC_060926.1 (73246421..73265996)
105.20220307	previous assembly	GRCh37.p13 (GCF_000001405.25)	2	NC_000002.11 (73461436..73480133)

Chromosome 2 - NC_000002.12 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

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Overexpression of chaperonin containing TCP1 subunit 7 has diagnostic and prognostic value for hepatocellular carcinoma.
Title: Overexpression of chaperonin containing TCP1 subunit 7 has diagnostic and prognostic value for hepatocellular carcinoma.
the increased expression of CCT-eta appears to be a marker for latent and active Dupuytren's contracture and to be essential for the increased contractility exhibited by these fibroblasts
Title: Increased CCT-eta expression is a marker of latent and active disease and a modulator of fibroblast contractility in Dupuytren's contracture.
Observational study of gene-disease association. (HuGE Navigator)
Title: Genetic variants in nuclear-encoded mitochondrial genes influence AIDS progression.
Functional characterization of the CCT complex and its subunits in mouse.
Title: Cytosolic chaperonin-containing t-complex polypeptide 1 changes the content of a particular subunit species concomitant with substrate binding and folding activities during the cell cycle.
A protein in mouse, that is highly similar to the one described in this record, was found to interact with a protein involved in the Nitric oxide (NO) signal transduction pathway, soluble guanylyl cyclase (sGC).
Title: CCTeta, a novel soluble guanylyl cyclase-interacting protein.

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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

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
HIV-1 infection (VSV-G pseudotyped) of CEMT4 T cells downregulates plasma membrane expression of CCT7	PubMed

Protein interactions

Protein	Gene	Interaction	Pubs
Vif	vif	HIV-1 Vif interacts with CCT7	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

CCT7 (e-PCR)
- UniSTS:510345

RH41801 (e-PCR)
- UniSTS:87954

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 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	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 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

Component	Evidence Code	Pubs
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
part_of chaperonin-containing T-complex	TAS Traceable Author Statement more info	PubMed
located_in cytoplasm	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 eta

Names: CCT-eta; HIV-1 Nef interacting protein; TCP-1-eta; chaperonin containing t-complex polypeptide 1, eta subunit

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_047121.1 RefSeqGene

Range

5884..24581

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001009570.3 → NP_001009570.1 T-complex protein 1 subunit eta isoform b

See identical proteins and their annotated locations for NP_001009570.1

Status: REVIEWED

Description

Transcript Variant: This variant (2) lacks an alternate in-frame segment of the 5' coding region, compared to variant 1, resulting in a shorter isoform (b), compared to isoform a.

Source sequence(s)

AK098825, AK293597, CX781741, DC395264

Consensus CDS

CCDS42696.1

UniProtKB/Swiss-Prot

Q99832

Related

ENSP00000381456.2, ENST00000398422.2

Conserved Domains (1) summary

cl02777
Location:1 → 321

chaperonin_like; chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I ...
NM_001166284.2 → NP_001159756.1 T-complex protein 1 subunit eta isoform c

See identical proteins and their annotated locations for NP_001159756.1

Status: REVIEWED

Description

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

Source sequence(s)

AK098825, AK298153, CX781741, DC395264

Consensus CDS

CCDS54366.1

UniProtKB/TrEMBL

B7Z7I4

Related

ENSP00000442058.1, ENST00000540468.5

Conserved Domains (1) summary

cd03340
Location:3 → 438

TCP1_eta; TCP-1 (CTT or eukaryotic type II) chaperonin family, eta 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_001166285.2 → NP_001159757.1 T-complex protein 1 subunit eta isoform d

See identical proteins and their annotated locations for NP_001159757.1

Status: REVIEWED

Description

Transcript Variant: This variant (4) includes an alternate exon in its 5' UTR and uses a downstream translational start codon, compared to variant 1. The encoded isoform (d) is shorter at the N-terminus, compared to isoform a.

Source sequence(s)

AK098825, AK297846, CX781741

Consensus CDS

CCDS54367.1

UniProtKB/TrEMBL

Q53HV2, Q6IBT3

Related

ENSP00000437824.1, ENST00000539919.5

Conserved Domains (1) summary

cd03340
Location:1 → 481

TCP1_eta; TCP-1 (CTT or eukaryotic type II) chaperonin family, eta 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_006429.4 → NP_006420.1 T-complex protein 1 subunit eta isoform a

See identical proteins and their annotated locations for NP_006420.1

Status: REVIEWED

Description

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

Source sequence(s)

AK098825, BC019296, CX781741, DC395264

Consensus CDS

CCDS46336.1

UniProtKB/Swiss-Prot

A8K7E6, A8MWI8, B7WNW9, B7Z4T9, B7Z4Z7, O14871, Q6FI26, Q99832

UniProtKB/TrEMBL

Q53HV2

Related

ENSP00000258091.5, ENST00000258091.10

Conserved Domains (1) summary

cd03340
Location:5 → 525

TCP1_eta; TCP-1 (CTT or eukaryotic type II) chaperonin family, eta 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), ...

RNA

NR_029402.2 RNA Sequence

Status: REVIEWED

Description

Transcript Variant: This variant (5) lacks an alternate internal exon, compared to variant 1. This variant is represented as non-coding because the use of the supported translational start codon, as used in variant 1, renders the transcript a candidate for nonsense-mediated mRNA decay (NMD).

Source sequence(s)

AK098825, AK293175, CX781741, DC395264
NR_029403.2 RNA Sequence

Status: REVIEWED

Description

Transcript Variant: This variant (6) lacks an alternate internal exon and uses an alternate internal splice site, compared to variant 1. This variant is represented as non-coding because the use of the supported translational start codon, as used in variant 1, renders the transcript a candidate for nonsense-mediated mRNA decay (NMD).

Source sequence(s)

AK098825, AK302078, CX781741, DC395264