Cct2 chaperonin containing TCP1 subunit 2 [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Cct2provided by MGI
Official Full Name: chaperonin containing TCP1 subunit 2provided by MGI
Primary source: MGI:MGI:107186
See related: Ensembl:ENSMUSG00000034024 AllianceGenome:MGI:107186
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Also known as: Cctb
Summary: Predicted to enable protein folding chaperone; ubiquitin protein ligase binding activity; and unfolded protein binding activity. Acts upstream of or within binding activity of sperm to zona pellucida. Located in cell body. Part of chaperonin-containing T-complex and zona pellucida receptor complex. Is expressed in central nervous system; nasal process; and somite. Orthologous to human CCT2 (chaperonin containing TCP1 subunit 2). [provided by Alliance of Genome Resources, Dec 2024]
Expression: Ubiquitous expression in CNS E11.5 (RPKM 94.1), placenta adult (RPKM 81.3) and 28 other tissues See more
Orthologs: human all
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Genomic context

Location:: 10 D2; 10 65.07 cM

Exon count:: 17

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	10	NC_000076.7 (116886902..116899757, complement)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	10	NC_000076.6 (117050997..117063852, complement)

Chromosome 10 - NC_000076.7 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: Mouse ENCODE transcriptome data
Description: RNA profiling data sets generated by the Mouse ENCODE project.
BioProject: PRJNA66167
Publication: PMID 25409824
Analysis date: n/a

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Compound heterozygous mutations in a mouse model of Leber congenital amaurosis reveal the role of CCT2 in photoreceptor maintenance.
Title: Compound heterozygous mutations in a mouse model of Leber congenital amaurosis reveal the role of CCT2 in photoreceptor maintenance.
CCT2 is an aggrephagy receptor for clearance of solid protein aggregates.
Title: CCT2 is an aggrephagy receptor for clearance of solid protein aggregates.
role of chaperonin-containing t-complex polypeptide 1 beta (CCT2) in the regulation of mesangial cell contraction, proliferation, and migration with filamentous/globular-(F/G-) actin ratio under high glucose induction
Title: Involvement of F-actin in chaperonin-containing t-complex 1 beta regulating mouse mesangial cell functions in a glucose-induction cell model.

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Variation

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Alleles

Alleles of this type are documented at Mouse Genome Informatics (MGI)

Endonuclease-mediated (2) 1 citation

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

RH143421 (e-PCR)
- UniSTS:232668

Gene Ontology Provided by MGI

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	ISO Inferred from Sequence Orthology more info
enables ubiquitin protein ligase binding	IEA Inferred from Electronic Annotation more info
enables ubiquitin protein ligase binding	ISO Inferred from Sequence Orthology more info
enables unfolded protein binding	IBA Inferred from Biological aspect of Ancestor more info
enables unfolded protein binding	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
acts_upstream_of_or_within binding of sperm to zona pellucida	IDA Inferred from Direct Assay more info	PubMed
involved_in chaperone mediated protein folding independent of cofactor	IEA Inferred from Electronic Annotation more info
involved_in chaperone mediated protein folding independent of cofactor	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within chaperone-mediated protein complex assembly	ISO Inferred from Sequence Orthology more info
involved_in chaperone-mediated protein folding	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of establishment of protein localization to telomere	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of telomerase RNA localization to Cajal body	IEA Inferred from Electronic Annotation more info
involved_in positive regulation of telomerase RNA localization to Cajal body	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of telomere maintenance via telomerase	IEA Inferred from Electronic Annotation more info
involved_in positive regulation of telomere maintenance via telomerase	ISO Inferred from Sequence Orthology more info
involved_in protein folding	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein folding	ISO Inferred from Sequence Orthology more info
involved_in protein stabilization	IEA Inferred from Electronic Annotation more info
involved_in protein stabilization	ISO Inferred from Sequence Orthology more info
involved_in scaRNA localization to Cajal body	IEA Inferred from Electronic Annotation more info
involved_in scaRNA localization to Cajal body	ISO Inferred from Sequence Orthology more info

Component	Evidence Code	Pubs
located_in cell body	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	ISO Inferred from Sequence Orthology more info
located_in cytosol	ISO Inferred from Sequence Orthology more info
located_in microtubule	IEA Inferred from Electronic Annotation more info
located_in microtubule	ISO Inferred from Sequence Orthology more info
located_in myelin sheath	HDA more info	PubMed
part_of zona pellucida receptor complex	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: T-complex protein 1 subunit beta

Names: CCT-beta; TCP-1-beta; chaperonin containing Tcp1, subunit 2 (beta); chaperonin subunit 2 (beta)

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_001358767.1 → NP_001345696.1 T-complex protein 1 subunit beta

Status: VALIDATED

Source sequence(s)

AK145406, BU755483, BY075050, CJ076140

UniProtKB/Swiss-Prot

P80314, Q9R1U0

UniProtKB/TrEMBL

Q542X7, Q9JJD8

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) ...
NM_007636.3 → NP_031662.2 T-complex protein 1 subunit beta

See identical proteins and their annotated locations for NP_031662.2

Status: VALIDATED

Source sequence(s)

AK145406, AL589661, BU755483

Consensus CDS

CCDS36067.1

UniProtKB/Swiss-Prot

P80314, Q9R1U0

UniProtKB/TrEMBL

Q542X7, Q9JJD8

Related

ENSMUSP00000036288.8, ENSMUST00000047672.9

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) ...