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

Summary

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; protein folding chaperone; 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 ER overload response; cellular response to interleukin-4; and negative regulation of transforming growth factor beta receptor signaling pathway. 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 long bone. 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, Nov 2024]
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

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_000068.8 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

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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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Piezo1 activation on microglial cells exacerbates demyelination in sepsis by influencing the CCL25/GRP78 pathway.
Title: Piezo1 activation on microglial cells exacerbates demyelination in sepsis by influencing the CCL25/GRP78 pathway.
Grp78 destabilization of infectious prions is strain-specific and modified by multiple factors including accessory chaperones and pH.
Title: Grp78 destabilization of infectious prions is strain-specific and modified by multiple factors including accessory chaperones and pH.
GRP78 Contributes to the Beneficial Effects of SGLT2 Inhibitor on Proximal Tubular Cells in DKD.
Title: GRP78 Contributes to the Beneficial Effects of SGLT2 Inhibitor on Proximal Tubular Cells in DKD.
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.
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.
Grp78 is required for intestinal Kras-dependent glycolysis proliferation and adenomagenesis.
Title: Grp78 is required for intestinal Kras-dependent glycolysis proliferation and adenomagenesis.
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.
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.
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.
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.

Submit: New GeneRIF Correction See all GeneRIFs (183)

Variation

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Alleles

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

Chemically induced (ENU) (1) 1 citation
Endonuclease-mediated (4) 1 citation
Targeted (7) 1 citation

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

D2Wsu141e (e-PCR), detects polymorphism
- UniSTS:142373

D2Wsu17e (e-PCR), detects polymorphism
- UniSTS:142375

UniSTS:259180 (e-PCR)
- UniSTS:259180

Hspa5 (e-PCR), detects polymorphism
- UniSTS:259180

RH125368 (e-PCR)
- UniSTS:162190

Hspa5 (e-PCR), detects polymorphism
- UniSTS:525967

Hspa5 (e-PCR), detects polymorphism
- UniSTS:143268

RH94472 (e-PCR)
- UniSTS:119720

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 hydrolysis activity	ISS Inferred from Sequence or Structural Similarity more info
enables ATP-dependent H2AZ histone chaperone activity	IEA Inferred from Electronic Annotation more info
enables ATP-dependent H3-H4 histone complex chaperone activity	IEA Inferred from Electronic Annotation more info
enables ATP-dependent protein folding chaperone	IEA Inferred from Electronic Annotation more info
enables DNA clamp loader activity	IEA Inferred from Electronic Annotation more info
enables chromatin extrusion motor activity	IEA Inferred from Electronic Annotation more info
enables cohesin loader activity	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 misfolded protein binding	IDA Inferred from Direct Assay more info	PubMed
enables misfolded protein binding	ISO Inferred from Sequence Orthology more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein domain specific binding	IEA Inferred from Electronic Annotation more info
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 protein serine/threonine kinase inhibitor activity	IEA Inferred from Electronic Annotation more info
enables ribosome binding	IDA Inferred from Direct Assay more info	PubMed
enables ubiquitin protein ligase binding	IEA Inferred from Electronic Annotation 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 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	IEA Inferred from Electronic Annotation more info
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 chromatin looping	IEA Inferred from Electronic Annotation more info
involved_in chromatin remodeling	IEA Inferred from Electronic Annotation 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 maintenance of protein localization in endoplasmic reticulum	ISS Inferred from Sequence or Structural Similarity more info
involved_in negative regulation of IRE1-mediated unfolded protein response	ISS Inferred from Sequence or Structural Similarity more info
involved_in negative regulation of PERK-mediated unfolded protein response	IEA Inferred from Electronic Annotation more info
involved_in negative regulation of apoptotic process	IEA Inferred from Electronic Annotation more info
involved_in negative regulation of apoptotic process	ISO Inferred from Sequence Orthology more info
involved_in negative regulation of protein-containing complex assembly	ISS Inferred from Sequence or Structural Similarity 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 cell migration	ISS Inferred from Sequence or Structural Similarity 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 post-translational protein targeting to membrane, translocation	ISS Inferred from Sequence or Structural Similarity more info
involved_in protein folding	IEA Inferred from Electronic Annotation 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	IEA Inferred from Electronic Annotation more info
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 cytosol	ISS Inferred from Sequence or Structural Similarity 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
located_in melanosome	IEA Inferred from Electronic Annotation 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	IEA Inferred from Electronic Annotation more info
located_in midbody	ISO Inferred from Sequence Orthology more info
located_in mitochondrion	ISO Inferred from Sequence Orthology more info
located_in mitochondrion	ISS Inferred from Sequence or Structural Similarity more info
located_in myelin sheath	HDA more info	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

EC 3.6.4.10

NP_071705.3

EC 3.6.4.10

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_001163434.1 → NP_001156906.1 endoplasmic reticulum chaperone BiP precursor

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

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