CCT2 chaperonin-containing T-complex subunit CCT2 [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: CCT2
Official Full Name: chaperonin-containing T-complex subunit CCT2
Primary source: SGD:S000001404
Locus tag: YIL142W
See related: AllianceGenome:SGD:S000001404; FungiDB:YIL142W; VEuPathDB:YIL142W
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Also known as: BIN3; TCP2
Summary: Enables unfolded protein binding activity. Involved in protein folding. Located in cytoplasm. Part of chaperonin-containing T-complex. Used to study Leber congenital amaurosis. Orthologous to human CCT2 (chaperonin containing TCP1 subunit 2). [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

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See CCT2 in Genome Data Viewer

Location:: chromosome: IX

Exon count:: 1

Sequence:: Chromosome: IX; NC_001141.2 (83302..84885)

Chromosome IX - NC_001141.2 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001141.2

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

ATP binding induces a dramatic conformational change on the CCT2 side, thereby suggesting that CCT2 plays an essential role in the eukaryotic chaperonin TRiC (or CCT) allosteric cooperativity.
Title: Staggered ATP binding mechanism of eukaryotic chaperonin TRiC (CCT) revealed through high-resolution cryo-EM.

Submit: New GeneRIF Correction

Pathways from PubChem

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Homology

Orthologs from OrthoDB

Gene Ontology Provided by SGD

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 unfolded protein binding	IBA Inferred from Biological aspect of Ancestor more info
enables unfolded protein binding	IDA Inferred from Direct Assay more info	PubMed
enables unfolded protein binding	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in chaperone mediated protein folding independent of cofactor	IEA Inferred from Electronic Annotation more info
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	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
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	IEA Inferred from Electronic Annotation more info
part_of chaperonin-containing T-complex	IPI Inferred from Physical Interaction more info	PubMed
located_in cytoplasm	HDA more info	PubMed
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
located_in cytosol	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: chaperonin-containing T-complex subunit CCT2

NP_012124.1

Subunit beta of the cytosolic chaperonin Cct ring complex; related to Tcp1p, required for the assembly of actin and tubulins in vivo

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

NC_001141.2 Reference assembly

Range

83302..84885

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001179490.1 → NP_012124.1 TPA: chaperonin-containing T-complex subunit CCT2 [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_012124.1

Status: REVIEWED

UniProtKB/Swiss-Prot

D6VVE5, P39076

UniProtKB/TrEMBL

A6ZVD4, B3LTY9, B5VKG7, C7GUQ9, G2WG10, N1P996

Conserved Domains (1) summary

cd03336
Location:5 → 520

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) ...