SHQ1 Hsp90 cochaperone SHQ1 [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: SHQ1
Official Full Name: Hsp90 cochaperone SHQ1
Primary source: SGD:S000001366
Locus tag: YIL104C
See related: AllianceGenome:SGD:S000001366; FungiDB:YIL104C; VEuPathDB:YIL104C
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 unfolded protein binding activity. Involved in box H/ACA snoRNP assembly. Located in cytosol and nucleoplasm. Orthologous to human SHQ1 (SHQ1, H/ACA ribonucleoprotein assembly factor). [provided by Alliance of Genome Resources, Apr 2022]
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Genomic context

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See SHQ1 in Genome Data Viewer

Location:: chromosome: IX

Exon count:: 1

Sequence:: Chromosome: IX; NC_001141.2 (169982..171505, complement)

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?

The authors demonstrate that Shq1p binds the pseudourydilating enzyme Cbf5p through the C-terminal domain, in synergy with the N-terminal domain.
Title: The box H/ACA snoRNP assembly factor Shq1p is a chaperone protein homologous to Hsp90 cochaperones that binds to the Cbf5p enzyme.
the CS domain is essential for Shq1p function in H/ACA snoRNP biogenesis in vivo, possibly in an Hsp90-independent manner.
Title: Structure and functional studies of the CS domain of the essential H/ACA ribonucleoparticle assembly protein SHQ1.

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

Process	Evidence Code	Pubs
involved_in box H/ACA snoRNP assembly	IBA Inferred from Biological aspect of Ancestor more info
involved_in box H/ACA snoRNP assembly	IEA Inferred from Electronic Annotation more info
involved_in box H/ACA snoRNP assembly	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in box H/ACA snoRNP assembly	IPI Inferred from Physical Interaction more info	PubMed

Component	Evidence Code	Pubs
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in cytosol	IDA Inferred from Direct Assay more info	PubMed
is_active_in nucleoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in nucleoplasm	IDA Inferred from Direct Assay more info	PubMed
located_in nucleus	IDA Inferred from Direct Assay more info	PubMed
located_in nucleus	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: Hsp90 cochaperone SHQ1

NP_012162.3

Chaperone protein; required for the assembly of box H/ACA snoRNPs and thus for pre-rRNA processing; functions as an RNA mimic; forms a complex with Naf1p and interacts with H/ACA snoRNP components Nhp2p and Cbf5p; homology with known Hsp90p cochaperones; relocalizes to the cytosol in response to hypoxia

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

169982..171505 complement

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001179452.3 → NP_012162.3 TPA: Hsp90 cochaperone SHQ1 [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_012162.3

Status: REVIEWED

UniProtKB/Swiss-Prot

D6VVI3, P40486

UniProtKB/TrEMBL

B3LTV1, B5VKK6, C7GKN0, C8ZAE2, N1P2H1

Conserved Domains (2) summary

cd06463
Location:9 → 90

p23_like; Proteins containing this p23_like domain include p23 and its Saccharomyces cerevisiae (Sc) homolog Sba1. Both are co-chaperones for the heat shock protein (Hsp) 90. p23 binds Hsp90 and participates in the folding of a number of Hsp90 clients, including ...

pfam04925
Location:268 → 465

SHQ1; SHQ1 protein