SIS1 type II HSP40 co-chaperone SIS1 [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: SIS1
Official Full Name: type II HSP40 co-chaperone SIS1
Primary source: SGD:S000004952
Locus tag: YNL007C
See related: AllianceGenome:SGD:S000004952; FungiDB:YNL007C; VEuPathDB:YNL007C
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 misfolded protein binding activity. Involved in several processes, including detection of misfolded protein; gene expression; and proteasome-mediated ubiquitin-dependent protein catabolic process. Located in nucleus. Part of cytosolic small ribosomal subunit. Is active in cytosol and nucleolus. Used to study autosomal dominant limb-girdle muscular dystrophy type 1 and congenital myopathy 21. Human ortholog(s) of this gene implicated in congenital myopathy 21 and primary ciliary dyskinesia 34. Orthologous to several human genes including DNAJB1 (DnaJ heat shock protein family (Hsp40) member B1). [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

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See SIS1 in Genome Data Viewer

Location:: chromosome: XIV

Exon count:: 1

Sequence:: Chromosome: XIV; NC_001146.8 (618507..619565, complement)

Chromosome XIV - NC_001146.8 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001146.8

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Transcriptional regulation of Sis1 promotes fitness but not feedback in the heat shock response.
Title: Transcriptional regulation of Sis1 promotes fitness but not feedback in the heat shock response.
Essentiality of Sis1, a J-domain protein Hsp70 cochaperone, can be overcome by Tti1, a specialized PIKK chaperone.
Title: Essentiality of Sis1, a J-domain protein Hsp70 cochaperone, can be overcome by Tti1, a specialized PIKK chaperone.
Yeast J-protein Sis1 prevents prion toxicity by moderating depletion of prion protein.
Title: Yeast J-protein Sis1 prevents prion toxicity by moderating depletion of prion protein.
Elevated constitutive expression of Hsp40 chaperone Sis1 reduces TDP-43 aggregation-induced oxidative stress in Ire1 pathway dependent-manner in yeast TDP-43 proteinopathy model of amyotrophic lateral sclerosis.
Title: Elevated constitutive expression of Hsp40 chaperone Sis1 reduces TDP-43 aggregation-induced oxidative stress in Ire1 pathway dependent-manner in yeast TDP-43 proteinopathy model of amyotrophic lateral sclerosis.
Class-specific interactions between Sis1 J-domain protein and Hsp70 chaperone potentiate disaggregation of misfolded proteins.
Title: Class-specific interactions between Sis1 J-domain protein and Hsp70 chaperone potentiate disaggregation of misfolded proteins.
Sis1 potentiates the stress response to protein aggregation and elevated temperature.
Title: Sis1 potentiates the stress response to protein aggregation and elevated temperature.
this study shows that cytosolic Hsp70 chaperones and their Hsp40 cochaperones Ydj1 and Sis1 interact with newly synthesized beta-barrel proteins.
Title: Cytosolic Hsp70 and Hsp40 chaperones enable the biogenesis of mitochondrial β-barrel proteins.
Differences in sensitivity of prion fragmentation to Sis1 and in relative inputs of fragmentation and malpartition in prion propagation result in opposite effects of Sis1 relocalization on [PSI (+)] and [URE3].
Title: Differential effects of chaperones on yeast prions: CURrent view.
Sis1 plays a role in prion replication.
Title: Hsp40s specify functions of Hsp104 and Hsp90 protein chaperone machines.
SSA2p and co-chaperones, SIS1p and YDJ1p, constitute a novel system for tRNA import into the nucleus.
Title: Cytosolic Hsp70 and co-chaperones constitute a novel system for tRNA import into the nucleus.

Submit: New GeneRIF Correction See all GeneRIFs (26)

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

Process	Evidence Code	Pubs
involved_in cellular response to heat	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in cellular response to starvation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in chaperone cofactor-dependent protein refolding	IBA Inferred from Biological aspect of Ancestor more info
involved_in detection of misfolded protein	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in misfolded protein transport	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in mitochondria-associated ubiquitin-dependent protein catabolic process	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in nuclear protein quality control by the ubiquitin-proteasome system	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein folding	IDA Inferred from Direct Assay more info	PubMed
involved_in protein folding	IEA Inferred from Electronic Annotation more info
involved_in protein folding	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in tRNA import into nucleus	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in translational initiation	IBA Inferred from Biological aspect of Ancestor more info
involved_in translational initiation	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
is_active_in cytosol	IBA Inferred from Biological aspect of Ancestor more info
is_active_in cytosol	IDA Inferred from Direct Assay more info	PubMed
part_of cytosolic small ribosomal subunit	IDA Inferred from Direct Assay more info	PubMed
is_active_in nucleolus	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: type II HSP40 co-chaperone SIS1

NP_014391.1

Type II HSP40 co-chaperone that interacts with the HSP70 protein Ssa1p; shuttles between cytosol and nucleus; mediates delivery of misfolded proteins into the nucleus for degradation; involved in proteasomal degradation of misfolded cytosolic proteins; protein abundance increases in response to DNA replication stress; polyQ aggregates sequester Sis1p and interfere with clearance of misfolded proteins; similar to bacterial DnaJ proteins and mammalian DnaJB1

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_001146.8 Reference assembly

Range

618507..619565 complement

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001182846.1 → NP_014391.1 TPA: type II HSP40 co-chaperone SIS1 [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_014391.1

Status: REVIEWED

UniProtKB/Swiss-Prot

D6W1H0, P25294

UniProtKB/TrEMBL

B3LPP5, N1NY39

Conserved Domains (1) summary

COG0484
Location:2 → 350

DnaJ; DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational modification, protein turnover, chaperones]