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Hspa5 heat shock protein 5 [ Mus musculus (house mouse) ]

Gene ID: 14828, updated on 11-Apr-2024

Summary

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Official Symbol
Hspa5provided by MGI
Official Full Name
heat shock protein 5provided by MGI
Primary source
MGI:MGI:95835
See related
Ensembl:ENSMUSG00000026864 AllianceGenome:MGI:95835
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
Bip; Sez7; mBiP; Grp78; SEZ-7; Hsce70; baffled; D2Wsu17e; D2Wsu141e
Summary
Enables misfolded protein binding activity and ribosome binding activity. Involved in several processes, including IRE1-mediated unfolded protein response; cerebellum development; and positive regulation of protein ubiquitination. Acts upstream of or within several processes, including cellular response to interleukin-4; negative regulation of transforming growth factor beta receptor signaling pathway; and toxin transport. Located in several cellular components, including cell surface; endoplasmic reticulum; and endoplasmic reticulum-Golgi intermediate compartment. Part of endoplasmic reticulum chaperone complex. Is expressed in several structures, including alimentary system; brain; eye; genitourinary system; and musculoskeletal system. Human ortholog(s) of this gene implicated in dopamine beta-hydroxylase deficiency. Orthologous to human HSPA5 (heat shock protein family A (Hsp70) member 5). [provided by Alliance of Genome Resources, Apr 2022]
Expression
Ubiquitous expression in placenta adult (RPKM 321.6), genital fat pad adult (RPKM 154.1) and 28 other tissues See more
Orthologs
human all
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Genomic context

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See Hspa5 in Genome Data Viewer
Location:
2 B; 2 22.94 cM
Exon count:
9
Annotation release Status Assembly Chr Location
RS_2024_02 current GRCm39 (GCF_000001635.27) 2 NC_000068.8 (34662102..34666541)
108.20200622 previous assembly GRCm38.p6 (GCF_000001635.26) 2 NC_000068.7 (34772090..34776529)

Chromosome 2 - NC_000068.8Genomic Context describing neighboring genes Neighboring gene predicted gene, 34372 Neighboring gene DnaJ (Hsp40) homolog, subfamily B, member 6 pseudogene Neighboring gene GTPase activating protein and VPS9 domains 1 Neighboring gene STARR-seq mESC enhancer starr_04265 Neighboring gene Rab9 effector protein with kelch motifs Neighboring gene predicted gene, 53241 Neighboring gene STARR-seq mESC enhancer starr_04266 Neighboring gene STARR-seq mESC enhancer starr_04267 Neighboring gene F-box and WD-40 domain protein 2

Genomic regions, transcripts, and products

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Go to nucleotide: Graphics FASTA GenBank

Expression

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  • Project title: Mouse ENCODE transcriptome data
  • Description: RNA profiling data sets generated by the Mouse ENCODE project.
  • BioProject: PRJNA66167
  • Publication: PMID 25409824
  • Analysis date: n/a

Bibliography

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Related articles in PubMed

  1. Extracellular HSPA5 is autocrinally involved in the regulation of neuronal process elongation. Fukawa M, et al. Biochem Biophys Res Commun, 2023 Jul 5. PMID 37137223
  2. Conditional deletion of Hspa5 leads to spermatogenesis failure and male infertility in mice. Wen Z, et al. Life Sci, 2023 Feb 1. PMID 36574945
  3. Citrullinated glucose-regulated protein 78 is a candidate target for melanoma immunotherapy. Brentville VA, et al. Front Immunol, 2022. PMID 36544781, Free PMC Article
  4. A new liver regeneration molecular mechanism involving hepatic stellate cells, Kupffer cells, and glucose-regulated protein 78 as a new hepatotrophic factor. Hagiwara K, et al. J Hepatobiliary Pancreat Sci, 2023 Feb. PMID 35586893
  5. Covalent inhibition of endoplasmic reticulum chaperone GRP78 disconnects the transduction of ER stress signals to inflammation and lipid accumulation in diet-induced obese mice. Luo D, et al. Elife, 2022 Feb 9. PMID 35138251, Free PMC Article

See all (432) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Nuclear GRP78 Promotes Metabolic Reprogramming and Therapeutic Resistance in Pancreatic Ductal Adenocarcinoma.
    Title: Nuclear GRP78 Promotes Metabolic Reprogramming and Therapeutic Resistance in Pancreatic Ductal Adenocarcinoma.
  2. Pirh2 modulates amyloid-beta aggregation through the regulation of glucose-regulated protein 78 and chaperone-mediated signaling.
    Title: Pirh2 modulates amyloid-β aggregation through the regulation of glucose-regulated protein 78 and chaperone-mediated signaling.
  3. Grp78 is required for intestinal Kras-dependent glycolysis proliferation and adenomagenesis.
    Title: Grp78 is required for intestinal Kras-dependent glycolysis proliferation and adenomagenesis.
  4. The ER chaperone, BIP protects Microglia from ER stress-mediated Apoptosis in Hyperglycemia.
    Title: The ER chaperone, BIP protects Microglia from ER stress-mediated Apoptosis in Hyperglycemia.
  5. The GRP78-PERK axis contributes to memory and synaptic impairments in Huntington's disease R6/1 mice.
    Title: The GRP78-PERK axis contributes to memory and synaptic impairments in Huntington's disease R6/1 mice.
  6. Disturbance of neuron-microglia crosstalk mediated by GRP78 in Neuropsychiatric systemic lupus erythematosus mice.
    Title: Disturbance of neuron-microglia crosstalk mediated by GRP78 in Neuropsychiatric systemic lupus erythematosus mice.
  7. Endoplasmic reticulum chaperone GRP78 participates in fluoride-induced autophagy in LS8 cells by regulating the IRE1-TRAF2-JNK pathway.
    Title: Endoplasmic reticulum chaperone GRP78 participates in fluoride-induced autophagy in LS8 cells by regulating the IRE1-TRAF2-JNK pathway.
  8. Extracellular HSPA5 is autocrinally involved in the regulation of neuronal process elongation.
    Title: Extracellular HSPA5 is autocrinally involved in the regulation of neuronal process elongation.
  9. The inhibition of ORMDL3 prevents Alzheimer's disease through ferroptosis by PERK/ATF4/HSPA5 pathway.
    Title: The inhibition of ORMDL3 prevents Alzheimer's disease through ferroptosis by PERK/ATF4/HSPA5 pathway.
  10. A new liver regeneration molecular mechanism involving hepatic stellate cells, Kupffer cells, and glucose-regulated protein 78 as a new hepatotrophic factor.
    Title: A new liver regeneration molecular mechanism involving hepatic stellate cells, Kupffer cells, and glucose-regulated protein 78 as a new hepatotrophic factor.
Submit: New GeneRIF Correction See all GeneRIFs (180)

Variation

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Alleles

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

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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Markers

Homology

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 folding chaperone IEA
Inferred from Electronic Annotation
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 hydrolase activity IEA
Inferred from Electronic Annotation
more info
  
enables misfolded protein binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables misfolded protein binding ISO
Inferred from Sequence Orthology
more info
 PubMed 
enables nucleotide binding IEA
Inferred from Electronic Annotation
more info
  
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables protein domain specific binding ISO
Inferred from Sequence Orthology
more info
  
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 ribosome binding IDA
Inferred from Direct Assay
more info
 PubMed 
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 ER overload response IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in ERAD pathway IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in IRE1-mediated unfolded protein response IEP
Inferred from Expression Pattern
more info
 PubMed 
involved_in cellular response to glucose starvation ISO
Inferred from Sequence Orthology
more info
  
acts_upstream_of_or_within cellular response to interleukin-4 IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in cerebellar Purkinje cell layer development IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in cerebellum structural organization 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 endoplasmic reticulum unfolded protein response IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in endoplasmic reticulum unfolded protein response IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in maintenance of protein localization in endoplasmic reticulum ISO
Inferred from Sequence Orthology
more info
  
involved_in negative regulation of apoptotic process ISO
Inferred from Sequence Orthology
more info
  
acts_upstream_of_or_within negative regulation of transforming growth factor beta receptor signaling pathway IGI
Inferred from Genetic Interaction
more info
 PubMed 
involved_in positive regulation of cell migration ISO
Inferred from Sequence Orthology
more info
  
involved_in positive regulation of embryonic development TAS
Traceable Author Statement
more info
 PubMed 
involved_in positive regulation of neuron projection development ISO
Inferred from Sequence Orthology
more info
  
involved_in positive regulation of protein ubiquitination IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in post-translational protein targeting to membrane, translocation ISO
Inferred from Sequence Orthology
more info
  
involved_in protein refolding IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in proteolysis involved in protein catabolic process IDA
Inferred from Direct Assay
more info
 PubMed 
acts_upstream_of_or_within response to endoplasmic reticulum stress ISO
Inferred from Sequence Orthology
more info
 PubMed 
Component Evidence Code Pubs
part_of COP9 signalosome ISO
Inferred from Sequence Orthology
more info
  
located_in cell surface IDA
Inferred from Direct Assay
more info
 PubMed 
is_active_in cytoplasm IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in cytoplasm ISO
Inferred from Sequence Orthology
more info
  
located_in cytosol ISO
Inferred from Sequence Orthology
more info
  
located_in dendritic shaft ISO
Inferred from Sequence Orthology
more info
  
located_in endoplasmic reticulum IDA
Inferred from Direct Assay
more info
 PubMed 
located_in endoplasmic reticulum ISO
Inferred from Sequence Orthology
more info
 PubMed 
part_of endoplasmic reticulum chaperone complex IBA
Inferred from Biological aspect of Ancestor
more info
  
part_of endoplasmic reticulum chaperone complex IDA
Inferred from Direct Assay
more info
 PubMed 
part_of endoplasmic reticulum chaperone complex ISO
Inferred from Sequence Orthology
more info
  
is_active_in endoplasmic reticulum lumen IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in endoplasmic reticulum lumen IDA
Inferred from Direct Assay
more info
 PubMed 
located_in endoplasmic reticulum lumen ISO
Inferred from Sequence Orthology
more info
  
located_in endoplasmic reticulum lumen TAS
Traceable Author Statement
more info
  
located_in endoplasmic reticulum membrane IDA
Inferred from Direct Assay
more info
 PubMed 
located_in endoplasmic reticulum membrane ISO
Inferred from Sequence Orthology
more info
  
located_in endoplasmic reticulum-Golgi intermediate compartment IDA
Inferred from Direct Assay
more info
 PubMed 
located_in endoplasmic reticulum-Golgi intermediate compartment ISO
Inferred from Sequence Orthology
more info
  
located_in extracellular region TAS
Traceable Author Statement
more info
  
located_in intracellular membrane-bounded organelle ISO
Inferred from Sequence Orthology
more info
  
is_active_in membrane IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in membrane ISO
Inferred from Sequence Orthology
more info
 PubMed 
located_in midbody ISO
Inferred from Sequence Orthology
more info
  
located_in mitochondrion ISO
Inferred from Sequence Orthology
more info
  
located_in myelin sheath HDA PubMed 
located_in neuronal cell body 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 plasma membrane IDA
Inferred from Direct Assay
more info
 PubMed 
part_of protein-containing complex ISO
Inferred from Sequence Orthology
more info
  
located_in smooth endoplasmic reticulum ISO
Inferred from Sequence Orthology
more info
  

General protein information

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Preferred Names
endoplasmic reticulum chaperone BiP
Names
78 kDa glucose-regulated protein
GRP-78
HSP70 family protein 5
XAP-1 antigen
binding-immunoglobulin protein
glucose regulated protein, 78 kDa
heat shock 70 kDa protein 5
heat shock 70kD protein 5 (glucose-regulated protein, 78kD)
heat shock protein 70 family protein 5
heat shock protein family A member 5
immunoglobulin heavy chain-binding protein
NP_001156906.1
NP_071705.3

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)

  1. NM_001163434.1 → NP_001156906.1  endoplasmic reticulum chaperone BiP precursor

    See identical proteins and their annotated locations for NP_001156906.1

    Status: VALIDATED

    Description
    Transcript Variant: This variant (1) represents the longer transcript. Variants 1 and 2 encode the same protein.
    Source sequence(s)
    AK148539, AL929106
    Consensus CDS
    CCDS15950.1
    UniProtKB/Swiss-Prot
    O35642, P20029, Q3UFF2, Q61630
    UniProtKB/TrEMBL
    Q3TI47, Q3TKF8, Q3U9G2
    Related
    ENSMUSP00000028222.7, ENSMUST00000028222.13
    Conserved Domains (1) summary
    pfam00012
    Location:31 → 636
    HSP70; Hsp70 protein

  2. NM_022310.3 → NP_071705.3  endoplasmic reticulum chaperone BiP precursor

    See identical proteins and their annotated locations for NP_071705.3

    Status: VALIDATED

    Description
    Transcript Variant: This variant (2) differs in the 5' UTR compared to variant 1. Variants 1 and 2 encode the same protein.
    Source sequence(s)
    AK152521, AL929106
    Consensus CDS
    CCDS15950.1
    UniProtKB/Swiss-Prot
    O35642, P20029, Q3UFF2, Q61630
    UniProtKB/TrEMBL
    Q3TI47, Q3TKF8, Q3U9G2
    Related
    ENSMUSP00000097747.3, ENSMUST00000100171.3
    Conserved Domains (1) summary
    pfam00012
    Location:31 → 636
    HSP70; Hsp70 protein

RefSeqs of Annotated Genomes: GCF_000001635.27-RS_2024_02

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCm39 C57BL/6J

Genomic

  1. NC_000068.8 Reference GRCm39 C57BL/6J

    Range
    34662102..34666541
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)
Nucleotide Protein Strain
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
P20029.3 GenPept UniProtKB/Swiss-Prot:P20029

Gene LinkOut

The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.

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