SSA2 Hsp70 family chaperone SSA2 [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: SSA2
Official Full Name: Hsp70 family chaperone SSA2
Primary source: SGD:S000003947
Locus tag: YLL024C
See related: AllianceGenome:SGD:S000003947; FungiDB:YLL024C; VEuPathDB:YLL024C
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: YG102
Summary: Enables ATP binding activity; tRNA binding activity; and unfolded protein binding activity. Involved in several processes, including SRP-dependent cotranslational protein targeting to membrane, translocation; protein folding; and tRNA import into nucleus. Located in several cellular components, including fungal-type cell wall; fungal-type vacuole membrane; and mitochondrion. Is active in extracellular vesicle. Human ortholog(s) of this gene implicated in Parkinson's disease and renal hypertension. Orthologous to human HSPA8 (heat shock protein family A (Hsp70) member 8). [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

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See SSA2 in Genome Data Viewer

Location:: chromosome: XII

Exon count:: 1

Sequence:: Chromosome: XII; NC_001144.5 (95566..97485, complement)

Chromosome XII - NC_001144.5 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001144.5

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Effects of HSP70 chaperones Ssa1 and Ssa2 on Ste5 scaffold and the mating mitogen-activated protein kinase (MAPK) pathway in Saccharomyces cerevisiae.
Title: Effects of HSP70 chaperones Ssa1 and Ssa2 on Ste5 scaffold and the mating mitogen-activated protein kinase (MAPK) pathway in Saccharomyces cerevisiae.
Spatial sequestration of misfolded proteins as an active chaperone-mediated process during heat stress.
Title: Spatial sequestration of misfolded proteins as an active chaperone-mediated process during heat stress.
The Yeast Hsp70 Cochaperone Ydj1 Regulates Functional Distinction of Ssa Hsp70s in the Hsp90 Chaperoning Pathway.
Title: The Yeast Hsp70 Cochaperone Ydj1 Regulates Functional Distinction of Ssa Hsp70s in the Hsp90 Chaperoning Pathway.
The extent of Ssa1/Ssa2 Hsp70 chaperone involvement in nuclear protein quality control degradation varies with the substrate.
Title: The extent of Ssa1/Ssa2 Hsp70 chaperone involvement in nuclear protein quality control degradation varies with the substrate.
Hsp110 (Sse1 and Sse2) associates with the 19S regulatory particle of the 26S proteasome and interacts with Hsp70 (Ssa1, Ssa2) to facilitate the delivery of Hsp70 substrates for proteasomal degradation.
Title: Hsp70-Hsp110 chaperones deliver ubiquitin-dependent and -independent substrates to the 26S proteasome for proteolysis in yeast.
Yeast ACO1 mitochondrial import is modulated by interactions of its C and N terminal domains and SSA1/SSA2.
Title: Yeast aconitase mitochondrial import is modulated by interactions of its C and N terminal domains and Ssa1/2 (Hsp70).
The authors mapped a discrete Hsp70 binding site on Hsf1 to a C-terminal segment known as conserved element 2 (CE2). In vitro, CE2 binds to Hsp70 with low affinity (9 microM), in agreement with model requirements. In cells, removal of CE2 resulted in increased basal Hsf1 activity and delayed deactivation during heat shock, while tandem repeats of CE2 sped up Hsf1 deactivation.
Title: Hsf1 and Hsp70 constitute a two-component feedback loop that regulates the yeast heat shock response.
Molecular chaperones of the Hsp70 family, SSA1 and SSA2, assist in the assembly of 20S proteasomes.
Title: Molecular chaperones of the Hsp70 family assist in the assembly of 20S proteasomes.
Ssa1 and Ssa2 are both necessary for the degradation of short-lived proteins. Ssa1 stably associates with its substrates and promotes their ubiquitylation.
Title: The requirements of yeast Hsp70 of SSA family for the ubiquitin-dependent degradation of short-lived and abnormal proteins.
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.

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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 ATP binding	IDA Inferred from Direct Assay more info	PubMed
enables ATP binding	IEA Inferred from Electronic Annotation more info
enables ATP hydrolysis activity	IBA Inferred from Biological aspect of Ancestor more info
enables ATP hydrolysis activity	ISS Inferred from Sequence or Structural Similarity more info	PubMed
enables ATP-dependent protein folding chaperone	IEA Inferred from Electronic Annotation more info
enables heat shock protein binding	IBA Inferred from Biological aspect of Ancestor more info
enables protein folding chaperone	IBA Inferred from Biological aspect of Ancestor more info
enables tRNA binding	IDA Inferred from Direct Assay more info	PubMed
enables unfolded protein binding	IGI Inferred from Genetic Interaction more info	PubMed
enables unfolded protein binding	ISS Inferred from Sequence or Structural Similarity more info	PubMed

Process	Evidence Code	Pubs
involved_in SRP-dependent cotranslational protein targeting to membrane, translocation	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 proteasome-mediated ubiquitin-dependent protein catabolic process	IGI Inferred from Genetic Interaction more info	PubMed
involved_in protein folding	IDA Inferred from Direct Assay more info	PubMed
involved_in protein folding	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein refolding	IBA Inferred from Biological aspect of Ancestor more info
involved_in tRNA import into nucleus	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
is_active_in cytosol	IBA Inferred from Biological aspect of Ancestor more info
located_in cytosol	IDA Inferred from Direct Assay more info	PubMed
located_in extracellular region	IEA Inferred from Electronic Annotation more info
is_active_in extracellular vesicle	IDA Inferred from Direct Assay more info	PubMed
located_in fungal-type cell wall	IDA Inferred from Direct Assay more info	PubMed
located_in fungal-type vacuole membrane	IDA Inferred from Direct Assay more info	PubMed
located_in mitochondrion	HDA more info	PubMed
located_in mitochondrion	IDA Inferred from Direct Assay more info	PubMed
is_active_in nucleus	IBA Inferred from Biological aspect of Ancestor more info
located_in plasma membrane	HDA more info	PubMed
is_active_in plasma membrane	IBA Inferred from Biological aspect of Ancestor more info

General protein information

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Preferred Names: Hsp70 family chaperone SSA2

NP_013076.1

HSP70 family ATP-binding protein; role in protein folding and vacuolar protein import; required for Ub-dependent degradation of short-lived proteins; associated with the chaperonin-containing T-complex; unique specificity in propagation of [URE3] prions and vacuolar degradation of gluconeogenic enzymes; contributes to tRNA nuclear import during starvation; targeted to vacuoles via the AP-3 pathway; localizes to exosomes during heat stress with a role in thermotolerance; 98% identity with Ssa1p

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_001144.5 Reference assembly

Range

95566..97485 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001181844.1 → NP_013076.1 TPA: Hsp70 family chaperone SSA2 [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_013076.1

Status: REVIEWED

UniProtKB/Swiss-Prot

D6VXY0, P10592

UniProtKB/TrEMBL

C8ZCU8

Conserved Domains (1) summary

PTZ00009
Location:4 → 639

PTZ00009; heat shock 70 kDa protein; Provisional