BTN2 Btn2p [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: BTN2
Official Full Name: Btn2p
Primary source: SGD:S000003374
Locus tag: YGR142W
See related: AllianceGenome:SGD:S000003374; FungiDB:YGR142W; VEuPathDB:YGR142W
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Summary: Enables SNARE binding activity; chaperone binding activity; and protein sequestering activity. Involved in several processes, including protein localization to nucleus; regulation of pH; and retrograde transport, endosome to Golgi. Located in several cellular components, including late endosome; nuclear periphery; and perinuclear region of cytoplasm. [provided by Alliance of Genome Resources, Apr 2022]
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Genomic context

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See BTN2 in Genome Data Viewer

Location:: chromosome: VII

Exon count:: 1

Sequence:: Chromosome: VII; NC_001139.9 (772454..773686)

Chromosome VII - NC_001139.9 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001139.9

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Dynamics of DNA damage-induced nuclear inclusions are regulated by SUMOylation of Btn2.
Title: Dynamics of DNA damage-induced nuclear inclusions are regulated by SUMOylation of Btn2.
Proteasome Control of [URE3] Prion Propagation by Degradation of Anti-Prion Proteins Cur1 and Btn2 in Saccharomyces cerevisiae.
Title: Proteasome Control of [URE3] Prion Propagation by Degradation of Anti-Prion Proteins Cur1 and Btn2 in Saccharomyces cerevisiae.
Innate immunity to yeast prions: Btn2p and Cur1p curing of the [URE3] prion is prevented by 60S ribosomal protein deficiency or ubiquitin/proteasome system overactivity.
Title: Innate immunity to yeast prions: Btn2p and Cur1p curing of the [URE3] prion is prevented by 60S ribosomal protein deficiency or ubiquitin/proteasome system overactivity.
Severe ethanol stress causes the accumulation of denatured proteins in living Saccharomyces cerevisiae cells and Btn2 is involved in the efficient clearance of denatured proteins during the recovery process
Title: Btn2 is involved in the clearance of denatured proteins caused by severe ethanol stress in Saccharomyces cerevisiae.
Hsp42 and Btn2 sequestrases constitute a stress rescue system that is essential for viability upon misfolded protein overload, by mitigating the burden on the Hsp70 chaperone machinery.
Title: Cellular sequestrases maintain basal Hsp70 capacity ensuring balanced proteostasis.
Juxtanuclear deposits of misfolded protein reside in an intranuclear quality control compartment whose formation is dependent on Btn2.
Title: Compartment-specific aggregases direct distinct nuclear and cytoplasmic aggregate deposition.
Normal levels of the antiprion proteins Btn2 and Cur1 cure most newly formed [URE3] prion variants.
Title: Normal levels of the antiprion proteins Btn2 and Cur1 cure most newly formed [URE3] prion variants.
Protein redistribution by Btn2 is accompanied by a gradual depletion of Sis1 from the cytosol, which is mediated by the sorting factor Cur1.
Title: Molecular chaperones and stress-inducible protein-sorting factors coordinate the spatiotemporal distribution of protein aggregates.
Btn2-mediated endosomal protein trafficking and prion curing in yeast is regulated by Btn3
Title: Btn3 is a negative regulator of Btn2-mediated endosomal protein trafficking and prion curing in yeast.
Btn2p is part of a system that collects aggregates preventing their efficient distribution to progeny cells
Title: Curing of the [URE3] prion by Btn2p, a Batten disease-related protein.

Submit: New GeneRIF Correction See all GeneRIFs (12)

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 SNARE binding	IDA Inferred from Direct Assay more info	PubMed
enables SNARE binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein sequestering activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables protein-folding chaperone binding	IPI Inferred from Physical Interaction more info	PubMed

Process	Evidence Code	Pubs
involved_in amino acid transport	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in intracellular protein transport	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in intracellular protein transport	IPI Inferred from Physical Interaction more info	PubMed
involved_in protein folding	IGI Inferred from Genetic Interaction more info	PubMed
involved_in protein folding	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein folding	IPI Inferred from Physical Interaction more info	PubMed
involved_in protein localization to nucleus	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein localization to nucleus	IPI Inferred from Physical Interaction more info	PubMed
involved_in regulation of pH	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in retrograde transport, endosome to Golgi	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
located_in cytosol	IDA Inferred from Direct Assay more info	PubMed
located_in endosome	IEA Inferred from Electronic Annotation more info
located_in late endosome	IDA Inferred from Direct Assay more info	PubMed
located_in late endosome	IEA Inferred from Electronic Annotation more info
located_in nuclear periphery	IDA Inferred from Direct Assay more info	PubMed
located_in nucleus	IDA Inferred from Direct Assay more info	PubMed
located_in perinuclear region of cytoplasm	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: Btn2p

NP_011658.3

Compartment-specific sequestrase chaperone; small hsp that sequesters proteins at intranuclear quality control sites (INQs); sumoylated form promotes protein clearance from INQs during recovery from genotoxic stress; v-SNARE binding protein that mediates late endosome-Golgi protein sorting; modulates arginine uptake and pH homeostasis between the vacuole and plasma membrane H(+)-ATPase; role in prion curing; expression after severe ethanol stress is involved in clearance of denatured proteins