SBA1 Hsp90 cochaperone SBA1 [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: SBA1
Official Full Name: Hsp90 cochaperone SBA1
Primary source: SGD:S000001600
Locus tag: YKL117W
See related: AllianceGenome:SGD:S000001600; FungiDB:YKL117W; VEuPathDB:YKL117W
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: CST18
Summary: Enables protein-folding chaperone binding activity. Involved in positive regulation of telomere maintenance via telomerase and protein folding. Located in cytoplasm and nucleus. Orthologous to several human genes including PTGES3 (prostaglandin E synthase 3). [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

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See SBA1 in Genome Data Viewer

Location:: chromosome: XI

Exon count:: 1

Sequence:: Chromosome: XI; NC_001143.9 (220324..220974)

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?

Monitoring the Conformation of the Sba1/Hsp90 Complex in the Presence of Nucleotides with Mn(II)-Based Double Electron-Electron Resonance.
Title: Monitoring the Conformation of the Sba1/Hsp90 Complex in the Presence of Nucleotides with Mn(II)-Based Double Electron-Electron Resonance.
Data support a model in which p23 molecular chaperone and GCN5 regulate diverse multistep pathways by controlling the longevity of protein-DNA complexes.
Title: The p23 molecular chaperone and GCN5 acetylase jointly modulate protein-DNA dynamics and open chromatin status.
Structure-function analysis suggests that Sba1p undergoes structural rearrangements upon binding Hsp90, and the large size of the p23/Sba1p-Hsp90 interaction surface facilitates maintenance of high affinity despite sequence divergence during evolution.
Title: p23/Sba1p protects against Hsp90 inhibitors independently of its intrinsic chaperone activity.
crystal structure of full-length yeast Hsp90 in complex with an ATP analogue and the co-chaperone p23/Sba1
Title: Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex.
SBA1 is required for teleomere length maintenance. It can moderate telomerase DNA binding and extension activities in vitro.
Title: The p23 molecular chaperone promotes functional telomerase complexes through DNA dissociation.

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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 Hsp90 protein binding	IBA Inferred from Biological aspect of Ancestor more info
enables Hsp90 protein binding	IEA Inferred from Electronic Annotation more info
enables protein-folding chaperone binding	IBA Inferred from Biological aspect of Ancestor more info
enables protein-folding chaperone binding	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 chaperone-mediated protein complex assembly	IBA Inferred from Biological aspect of Ancestor more info
involved_in negative regulation of DNA binding	IDA Inferred from Direct Assay more info	PubMed
involved_in positive regulation of telomere maintenance via telomerase	IDA Inferred from Direct Assay more info	PubMed
involved_in positive regulation of telomere maintenance via telomerase	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein folding	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein folding	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein folding	IPI Inferred from Physical Interaction more info	PubMed

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

General protein information

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Preferred Names: Hsp90 cochaperone SBA1

NP_012805.1

Co-chaperone that binds and regulates Hsp90 family chaperones; plays a role in determining prion variants; important for pp60v-src activity in yeast; homologous to the mammalian p23 proteins, and like p23 can regulate telomerase activity; protein abundance increases in response to DNA replication stress

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_001143.9 Reference assembly

Range

220324..220974

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001179683.1 → NP_012805.1 TPA: Hsp90 cochaperone SBA1 [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_012805.1

Status: REVIEWED

UniProtKB/Swiss-Prot

D6VXH2, P28707

UniProtKB/TrEMBL

G2WHR8, N1NZR4

Conserved Domains (1) summary

cd06465
Location:8 → 129

p23_hB-ind1_like; p23_like domain found in human (h) butyrate-induced transcript 1 (B-ind1) and similar proteins. hB-ind1 participates in signaling by the small GTPase Rac1. It binds to Rac1 and enhances different Rac1 effects including activation of nuclear factor (NF) ...