SHE2 She2p [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: SHE2
Official Full Name: She2p
Primary source: SGD:S000001613
Locus tag: YKL130C
See related: AllianceGenome:SGD:S000001613; FungiDB:YKL130C; VEuPathDB:YKL130C
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 lipid binding activity and sequence-specific mRNA binding activity. Involved in intracellular mRNA localization and mating type switching. Located in cellular bud tip and cytoplasm. [provided by Alliance of Genome Resources, Nov 2024]
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Genomic context

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See SHE2 in Genome Data Viewer

Location:: chromosome: XI

Exon count:: 1

Sequence:: Chromosome: XI; NC_001143.9 (195288..196028, complement)

Chromosome XI - NC_001143.9 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001143.9

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Phosphorylation controls the oligomeric state of She2 and mRNA localization in yeast.
Title: Phosphorylation controls the oligomeric state of She2 and mRNA localization in yeast.
Combining RNA- and membrane-binding features makes She2p an ideal coordinator of ER tubule and mRNA cotransport.
Title: Association of the yeast RNA-binding protein She2p with the tubular endoplasmic reticulum depends on membrane curvature.
The binding site for She3p was mapped to a single alpha helix that protrudes at right angles from She2p.
Title: Two single-headed myosin V motors bound to a tetrameric adapter protein form a processive complex.
She2p is recruited cotranscriptionally to the nascent bud-localized ASH1, IST2, and EAR1 mRNA
Title: Cotranscriptional recruitment of She2p by RNA pol II elongation factor Spt4-Spt5/DSIF promotes mRNA localization to the yeast bud.
finding on She2p tetramerization resolves previously raised questions on complex formation and mRNP function.
Title: Formation of She2p tetramers is required for mRNA binding, mRNP assembly, and localization.
She2p interacts with both Loc1p and Puf6p and excluding She2p from the nucleus decreases this interaction.
Title: Nuclear shuttling of She2p couples ASH1 mRNA localization to its translational repression by recruiting Loc1p and Puf6p.
Results indicate that the nucleolar transit of RNA-binding proteins such as She2 is necessary for the correct assembly of translationally silenced localizing messenger ribonucleoproteins.
Title: Nuclear transit of the RNA-binding protein She2 is required for translational control of localized ASH1 mRNA.
continuous transport of mRNA by Myo4p-She3p in yeast is accomplished either by multiple high duty cycle monomers or by molecules that may be dimerized by She2p, the homodimeric downstream binding partner of She3p
Title: She3p binds to the rod of yeast myosin V and prevents it from dimerizing, forming a single-headed motor complex.
anchoring of ASH1 mRNA requires molecular remodeling of the Myo4p-She3p-She2p heterotrimeric complex, a process that is apparently altered when mRNA is artificially tethered to She2p.
Title: ASH1 mRNA anchoring requires reorganization of the Myo4p-She3p-She2p transport complex.
She2p is a member of a previously unknown class of nucleic acid binding proteins, composed of a single globular domain with a five alpha helix bundle that forms a symmetric homodimer.
Title: She2p is a novel RNA binding protein with a basic helical hairpin motif.

Submit: New GeneRIF Correction See all GeneRIFs (11)

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 RNA binding	IEA Inferred from Electronic Annotation more info
enables lipid binding	IDA Inferred from Direct Assay more info	PubMed
enables mRNA binding	IDA Inferred from Direct Assay more info	PubMed
enables sequence-specific mRNA binding	IDA Inferred from Direct Assay more info	PubMed

Process	Evidence Code	Pubs
involved_in intracellular mRNA localization	IDA Inferred from Direct Assay more info	PubMed
involved_in intracellular mRNA localization	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in mRNA transport	IEA Inferred from Electronic Annotation more info
involved_in mating type switching	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in cellular bud tip	IDA Inferred from Direct Assay more info	PubMed
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
located_in cytosol	HDA more info	PubMed
located_in nucleus	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: She2p

NP_012792.1

RNA-binding protein that binds specific mRNAs and interacts with She3p; part of the mRNA localization machinery that restricts accumulation of certain proteins to the bud; binds to ER-derived membranes and targets mRNAs to cortical ER