Hspa1b heat shock protein 1B [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Hspa1bprovided by MGI
Official Full Name: heat shock protein 1Bprovided by MGI
Primary source: MGI:MGI:99517
See related: Ensembl:ENSMUSG00000090877 AllianceGenome:MGI:99517
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: Hsp70; hsp68; HSP70B1; Hsp70-1; Hsp70.1
Summary: Enables protein folding chaperone. Involved in protein folding. Acts upstream of or within binding activity of sperm to zona pellucida; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; and response to heat. Located in cell body and mitochondrion. Part of zona pellucida receptor complex. Is expressed in several structures, including early conceptus; heart; humerus; and lung. Human ortholog(s) of this gene implicated in several diseases, including brain ischemia; obesity; toxic shock syndrome; type 2 diabetes mellitus; and urinary tract infection. Orthologous to human HSPA1B (heat shock protein family A (Hsp70) member 1B). [provided by Alliance of Genome Resources, Dec 2024]
NEW: Try the new Gene table
Try the new Transcript table

Genomic context

Location:: 17 B1; 17 18.5 cM

Exon count:: 1

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	17	NC_000083.7 (35175405..35178214, complement)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	17	NC_000083.6 (34956429..34959238, complement)

Chromosome 17 - NC_000083.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

Go to the top of the page Help

Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Bibliography

Go to the top of the page Help

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Heat Shock Protein 70 Is Involved in the Efficiency of Preconditioning with Cyclosporine A in Renal Ischemia Reperfusion Injury by Modulating Mitochondrial Functions.
Title: Heat Shock Protein 70 Is Involved in the Efficiency of Preconditioning with Cyclosporine A in Renal Ischemia Reperfusion Injury by Modulating Mitochondrial Functions.
Mechanisms of action of Lycium barbarum polysaccharide in protecting against vitiligo mice through modulation of the STAT3-Hsp70-CXCL9/CXCL10 pathway.
Title: Mechanisms of action of Lycium barbarum polysaccharide in protecting against vitiligo mice through modulation of the STAT3-Hsp70-CXCL9/CXCL10 pathway.
Mechanisms of nucleophosmin (NPM)-mediated regulated cell death elucidated by Hsp70 during renal ischemia.
Title: Mechanisms of nucleophosmin (NPM)-mediated regulated cell death elucidated by Hsp70 during renal ischemia.
Loss of ten-eleven translocation 2 induces cardiac hypertrophy and fibrosis through modulating ERK signaling pathway.
Title: Loss of ten-eleven translocation 2 induces cardiac hypertrophy and fibrosis through modulating ERK signaling pathway.
HSP70 alleviates spinal cord injury by activating the NF-kB pathway.
Title: HSP70 alleviates spinal cord injury by activating the NF-kB pathway.
Overexpression of Heat Shock Protein 70 Improves Cardiac Remodeling and Survival in Protein Phosphatase 2A-Expressing Transgenic Mice with Chronic Heart Failure.
Title: Overexpression of Heat Shock Protein 70 Improves Cardiac Remodeling and Survival in Protein Phosphatase 2A-Expressing Transgenic Mice with Chronic Heart Failure.
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.
Participation of Hsp70 and Hsp90alpha Heat Shock Proteins in Stress Response in the Course of Type 1 Diabetes Mellitus.
Title: Participation of Hsp70 and Hsp90α Heat Shock Proteins in Stress Response in the Course of Type 1 Diabetes Mellitus.
HSP70, a Novel Regulatory Molecule in B Cell-Mediated Suppression of Autoimmune Diseases.
Title: HSP70, a Novel Regulatory Molecule in B Cell-Mediated Suppression of Autoimmune Diseases.
A novel tonicity-responsive microRNA miR-23a-5p modulates renal cell survival under osmotic stress through targeting heat shock protein 70 HSPA1B.
Title: A novel tonicity-responsive microRNA miR-23a-5p modulates renal cell survival under osmotic stress through targeting heat shock protein 70 HSPA1B.

Submit: New GeneRIF Correction See all GeneRIFs (147)

Variation

Go to the top of the page Help

Alleles

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

Endonuclease-mediated (2)
Targeted (5) 1 citation

Interactions

Go to the top of the page Help

Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

Go to the top of the page Help

Markers

PMC314357P1 (e-PCR)
- UniSTS:272944

D17Mit1011 (e-PCR), detects polymorphism
- UniSTS:142145

D17Nds2 (e-PCR), detects polymorphism
- UniSTS:142147

D17Mit83.1 (e-PCR), detects polymorphism
- UniSTS:128108

D17Mit83 (e-PCR), detects polymorphism
- UniSTS:116650

Hspa1b (e-PCR), detects polymorphism
- UniSTS:461998

PMC117401P1 (e-PCR)
- UniSTS:270334

Hspa1b (e-PCR), detects polymorphism
- UniSTS:257022

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables ATP binding	IEA Inferred from Electronic Annotation more info
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 ATP-dependent protein folding chaperone	IEA Inferred from Electronic Annotation 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 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 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 signaling receptor binding	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
involved_in ATP metabolic process	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within binding of sperm to zona pellucida	IDA Inferred from Direct Assay more info	PubMed
involved_in cellular heat acclimation	ISO Inferred from Sequence Orthology more info
involved_in cellular response to heat	ISO Inferred from Sequence Orthology more info
involved_in chaperone cofactor-dependent protein refolding	IBA Inferred from Biological aspect of Ancestor more info
involved_in mRNA catabolic process	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within negative regulation of apoptotic process	IDA Inferred from Direct Assay more info	PubMed
involved_in negative regulation of apoptotic process	ISO Inferred from Sequence Orthology more info
involved_in negative regulation of cell growth	ISO Inferred from Sequence Orthology more info
involved_in negative regulation of cell population proliferation	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within negative regulation of cysteine-type endopeptidase activity	IDA Inferred from Direct Assay more info	PubMed
involved_in negative regulation of extrinsic apoptotic signaling pathway in absence of ligand	ISO Inferred from Sequence Orthology more info
involved_in negative regulation of inclusion body assembly	ISO Inferred from Sequence Orthology more info
involved_in negative regulation of protein ubiquitination	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of NF-kappaB transcription factor activity	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of erythrocyte differentiation	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of gene expression	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of interleukin-8 production	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of microtubule nucleation	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of microtubule nucleation	ISS Inferred from Sequence or Structural Similarity more info
involved_in positive regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of proteasomal ubiquitin-dependent protein catabolic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in positive regulation of tumor necrosis factor-mediated signaling pathway	ISO Inferred from Sequence Orthology 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
involved_in protein refolding	ISO Inferred from Sequence Orthology more info
involved_in protein refolding	ISS Inferred from Sequence or Structural Similarity more info
involved_in protein stabilization	ISO Inferred from Sequence Orthology more info
involved_in regulation of mitotic spindle assembly	ISO Inferred from Sequence Orthology more info
involved_in regulation of mitotic spindle assembly	ISS Inferred from Sequence or Structural Similarity more info
involved_in regulation of protein ubiquitination	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within response to heat	IDA Inferred from Direct Assay more info	PubMed

Component	Evidence Code	Pubs
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 cell body	IDA Inferred from Direct Assay more info	PubMed
located_in centriole	ISO Inferred from Sequence Orthology more info
located_in centrosome	ISO Inferred from Sequence Orthology more info
located_in centrosome	ISS Inferred from Sequence or Structural Similarity more info
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in cytoplasm	ISO Inferred from Sequence Orthology more info
is_active_in cytosol	IBA Inferred from Biological aspect of Ancestor more info
located_in cytosol	ISO Inferred from Sequence Orthology more info
located_in inclusion body	ISO Inferred from Sequence Orthology more info
located_in intracellular anatomical structure	IDA Inferred from Direct Assay more info	PubMed
located_in membrane raft	ISO Inferred from Sequence Orthology more info
located_in mitochondrial matrix	ISO Inferred from Sequence Orthology more info	PubMed
located_in mitochondrion	IDA Inferred from Direct Assay more info	PubMed
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
is_active_in plasma membrane	IBA Inferred from Biological aspect of Ancestor 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
part_of zona pellucida receptor complex	IDA Inferred from Direct Assay more info	PubMed

General protein information

Go to the top of the page Help

Preferred Names: heat shock 70 kDa protein 1B

Names: 68 kDa heat shock protein; heat shock 70 kDa protein 1; heat shock 70kDa protein 1B; heat shock protein 70.1; heat shock protein, 70 kDa 1

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

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_010478.3 → NP_034608.2 heat shock 70 kDa protein 1B

See identical proteins and their annotated locations for NP_034608.2

Status: VALIDATED

Source sequence(s)

AC087117

Consensus CDS

CCDS37592.1

UniProtKB/Swiss-Prot

P17879, Q61689, Q925V6

UniProtKB/TrEMBL

Q3TAI8

Related

ENSMUSP00000133815.2, ENSMUST00000172753.2

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 → 642

PTZ00009; heat shock 70 kDa protein; Provisional