Hspa1a heat shock protein 1A [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Hspa1aprovided by MGI
Official Full Name: heat shock protein 1Aprovided by MGI
Primary source: MGI:MGI:96244
See related: Ensembl:ENSMUSG00000091971 AllianceGenome:MGI:96244
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Also known as: Hsp72; hsp68; Hsp70-3; Hsp70.3; hsp70A1
Summary: Enables protein folding chaperone. Involved in lysosomal transport and protein folding. Acts upstream of or within DNA repair; response to heat; and telomere maintenance. Located in cytoplasm. Is expressed in several structures, including adrenal gland; early conceptus; genitourinary system; and vibrissa. Human ortholog(s) of this gene implicated in several diseases, including Kawasaki disease; autoimmune disease of musculoskeletal system (multiple); cystic fibrosis; schizophrenia (multiple); and toxic shock syndrome. Orthologous to several human genes including HSPA1B (heat shock protein family A (Hsp70) member 1B). [provided by Alliance of Genome Resources, Apr 2022]
Orthologs: human all
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Genomic context

Location:: 17 B1; 17 18.51 cM

Exon count:: 1

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	17	NC_000083.7 (35188335..35191132, complement)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	17	NC_000083.6 (34969359..34972156, complement)

Chromosome 17 - NC_000083.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Heat stress induced arginylation of HuR promotes alternative polyadenylation of Hsp70.3 by regulating HuR stability and RNA binding.
Title: Heat stress induced arginylation of HuR promotes alternative polyadenylation of Hsp70.3 by regulating HuR stability and RNA binding.
HSP70 role in the liver ischemia/reperfusion injury.INOS increases the HSF1 binding to the HSP70 gene promoter in the hepatocytes after ischemia/reperfusion injury.INOS increases HSP70 expression in the hepatocytes after ischemia/reperfusion injury.[HSP70]
Title: Hepatocellular iNOS protects liver from ischemia/reperfusion injury through HSF1-dependent activation of HSP70.
Study reveals that Sirt1 may maintain the quiescent state in resting B cells by suppressing the increase of Hspa1a and Hspa1b.
Title: Increase of Hspa1a and Hspa1b genes in the resting B cells of Sirt1 knockout mice.
HSP72 KO caused a deterioration in glucose metabolism, hepatic gluconeogenic activity, and beta-cell function. Moreover, liver-specific recovery of HSP72 restored glucose homeostasis. Therefore, hepatic HSP72 may play a critical role in the pathogenesis of type 2 diabetes.
Title: Impact of hepatic HSP72 on insulin signaling.
In contrast to wild-type mice, HSPA1A transgenic mice exhibited generalized seizures very early during the kindling paradigm.
Title: Genetic Modulation of HSPA1A Accelerates Kindling Progression and Exerts Pro-convulsant Effects.
CM-695, a small molecule that induces the expression of the HSPA1A/B genes, increases the vessel wall levels of Hsp70 and prevents thrombosis at least as efficiently as rivaroxaban without increasing bleeding risk.
Title: Inducing heat shock protein 70 expression provides a robust antithrombotic effect with minimal bleeding risk.
HSPA1A and HSPA8 have roles in parturition through stimulating immune inflammatory and estrogen response
Title: Functional analysis of HSPA1A and HSPA8 in parturition.
HSPA1A/B induction is a novel approach to delay thrombus formation with minimal bleeding risk in knockout mice.
Title: Hsp70 protects from stroke in atrial fibrillation patients by preventing thrombosis without increased bleeding risk.
HspA1A-phosphoinositide binding is complex yet specific, is mediated by both electrostatic and hydrophobic interactions, is not related to the lipid-head charge, and depends on the physicochemical properties of the lipid.
Title: Characterization of the binding between a 70-kDa heat shock protein, HspA1A, and phosphoinositides.
The protective mechanism of HAS2 involves an increased expression of the heat-shock protein Hsp72, a chaperone with antiapoptotic activity
Title: Hyaluronan synthase-2 upregulation protects smpd3-deficient fibroblasts against cell death induced by nutrient deprivation, but not against apoptosis evoked by oxidized LDL.

Submit: New GeneRIF Correction See all GeneRIFs (55)

Variation

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Alleles

Alleles of this type are documented at Mouse Genome Informatics (MGI)

Targeted (2) 1 citation
Endonuclease-mediated (1)

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

PMC314357P1 (e-PCR)
- UniSTS:272944

NoName (e-PCR)
- UniSTS:548457

Hspa1a (e-PCR), detects polymorphism
- UniSTS:461997

M12572 (e-PCR)
- UniSTS:124915

PMC117401P1 (e-PCR)
- UniSTS:270334

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables ATP binding	ISO Inferred from Sequence Orthology more info
enables ATP hydrolysis activity	IBA Inferred from Biological aspect of Ancestor more info
enables ATP hydrolysis activity	ISO Inferred from Sequence Orthology more info
enables ATP-dependent protein disaggregase activity	ISO Inferred from Sequence Orthology more info
enables C3HC4-type RING finger domain binding	ISO Inferred from Sequence Orthology more info
enables G protein-coupled receptor binding	ISO Inferred from Sequence Orthology more info
enables NF-kappaB binding	ISO Inferred from Sequence Orthology more info
enables death receptor agonist activity	ISO Inferred from Sequence Orthology more info
enables denatured protein binding	ISO Inferred from Sequence Orthology more info
enables disordered domain specific binding	ISO Inferred from Sequence Orthology more info
enables double-stranded RNA binding	ISO Inferred from Sequence Orthology more info	PubMed
enables enzyme binding	ISO Inferred from Sequence Orthology more info
enables heat shock protein binding	IBA Inferred from Biological aspect of Ancestor more info
enables heat shock protein binding	ISO Inferred from Sequence Orthology more info
enables histone deacetylase binding	ISO Inferred from Sequence Orthology more info
enables misfolded protein binding	ISO Inferred from Sequence Orthology more info
enables protease binding	ISO Inferred from Sequence Orthology more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein folding chaperone	IBA Inferred from Biological aspect of Ancestor more info
enables protein folding chaperone	IDA Inferred from Direct Assay more info	PubMed
enables protein folding chaperone	ISO Inferred from Sequence Orthology more info
enables receptor ligand activity	ISO Inferred from Sequence Orthology more info
enables signaling receptor binding	ISO Inferred from Sequence Orthology more info
enables transcription corepressor activity	ISO Inferred from Sequence Orthology more info
enables transcription regulator inhibitor activity	ISO Inferred from Sequence Orthology more info
enables ubiquitin protein ligase binding	ISO Inferred from Sequence Orthology more info
enables unfolded protein binding	ISO Inferred from Sequence Orthology more info

Process	Evidence Code	Pubs
acts_upstream_of_or_within DNA repair	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 lysosomal transport	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in positive regulation of proteasomal ubiquitin-dependent protein catabolic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein folding	IDA Inferred from Direct Assay more info	PubMed
involved_in protein refolding	IBA Inferred from Biological aspect of Ancestor more info
acts_upstream_of_or_within response to heat	IDA Inferred from Direct Assay more info	PubMed
acts_upstream_of_or_within response to heat	IMP Inferred from Mutant Phenotype more info	PubMed
acts_upstream_of_or_within telomere maintenance	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
part_of COP9 signalosome	ISO Inferred from Sequence Orthology more info
located_in aggresome	ISO Inferred from Sequence Orthology more info
located_in apical plasma membrane	ISO Inferred from Sequence Orthology more info
located_in basolateral plasma membrane	ISO Inferred from Sequence Orthology more info
located_in centriole	ISO Inferred from Sequence Orthology more info
located_in centrosome	ISO Inferred from Sequence Orthology more info
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	ISO Inferred from Sequence Orthology more info
located_in cytosol	ISO Inferred from Sequence Orthology more info
is_active_in extracellular space	ISO Inferred from Sequence Orthology more info
located_in inclusion body	ISO Inferred from Sequence Orthology more info
located_in membrane raft	ISO Inferred from Sequence Orthology more info
located_in mitochondrion	ISS Inferred from Sequence or Structural Similarity more info	PubMed
located_in nuclear speck	ISO Inferred from Sequence Orthology more info
is_active_in nucleus	IBA Inferred from Biological aspect of Ancestor more info
located_in nucleus	ISO Inferred from Sequence Orthology more info
located_in perinuclear region of cytoplasm	ISO Inferred from Sequence Orthology more info
part_of protein-containing complex	ISO Inferred from Sequence Orthology more info
part_of ribonucleoprotein complex	ISO Inferred from Sequence Orthology more info

General protein information

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Preferred Names: heat shock 70 kDa protein 1A

Names: 68 kDa heat shock protein; heat shock 70 kDa protein 3; heat shock 70kDa protein 1A; heat shock protein, 70 kDa 3; inducible heat shock protein 70

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_010479.2 → NP_034609.2 heat shock 70 kDa protein 1A

See identical proteins and their annotated locations for NP_034609.2

Status: VALIDATED

Source sequence(s)

AC087117

Consensus CDS

CCDS50080.1

UniProtKB/Swiss-Prot

Q61696, Q61697, Q7TQD8, Q9QWJ5

UniProtKB/TrEMBL

Q3TAI8, Q3TU85

Related

ENSMUSP00000084586.3, ENSMUST00000087328.4

Conserved Domains (2) summary

cd10233
Location:6 → 381

HSPA1-2_6-8-like_NBD; Nucleotide-binding domain of HSPA1-A, -B, -L, HSPA-2, -6, -7, -8, and similar proteins

PTZ00009
Location:1 → 641

PTZ00009; heat shock 70 kDa protein; Provisional