Hspb2 heat shock protein 2 [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Hspb2provided by MGI
Official Full Name: heat shock protein 2provided by MGI
Primary source: MGI:MGI:1916503
See related: Ensembl:ENSMUSG00000038086 AllianceGenome:MGI:1916503
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: MKBP; 27kDa; HSP27; 2810021G24Rik
Summary: Predicted to be a structural constituent of eye lens. Acts upstream of or within somatic muscle development. Predicted to be located in cytoplasm and nucleus. Is expressed in several structures, including adrenal gland; cardiovascular system; gut; limb segment; and skeletal musculature. Orthologous to human HSPB2 (heat shock protein family B (small) member 2). [provided by Alliance of Genome Resources, Apr 2022]
Expression: Biased expression in heart adult (RPKM 66.3), lung adult (RPKM 22.9) and 11 other tissues See more
Orthologs: human all
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Genomic context

Location:: 9 A5.3; 9 27.75 cM

Exon count:: 2

Annotation release	Status	Assembly	Chr	Location
109	current	GRCm39 (GCF_000001635.27)	9	NC_000075.7 (50662372..50663654, complement)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	9	NC_000075.6 (50751072..50752354, complement)

Chromosome 9 - NC_000075.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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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?

HSP27 exerts its protective role by suppressing reactive oxygen species and atherosclerosis progression by inhibiting mitochondria apoptosis pathway in coronary heart disease.
Title: Protective effect of HSP27 in atherosclerosis and coronary heart disease by inhibiting reactive oxygen species.
HSP27 is a partner of JAK2-STAT5 and a potential therapeutic target in myelofibrosis.
Title: HSP27 is a partner of JAK2-STAT5 and a potential therapeutic target in myelofibrosis.
We found significantly slower retrograde transport of mitochondria in Ser135Phe, Pro39Leu and Arg140Gly mutant Hsp27 expressing motor neurons than in wild type Hsp27 neurons, although anterograde movement velocities remained normal.
Title: Mitochondrial deficits and abnormal mitochondrial retrograde axonal transport play a role in the pathogenesis of mutant Hsp27-induced Charcot Marie Tooth Disease.
HSP27 expression is upregulated in lung fibroblasts during pulmonary fibrosis, and subsequently, HSP27 modulates lung fibroblast differentiation through the Smad3 and ERK pathways.
Title: HSP27 regulates TGF-β mediated lung fibroblast differentiation through the Smad3 and ERK pathways.
phosphorylated Hsp27 stimulates autophagy and lipid droplet clearance and interacts with STAT3.
Title: Phosphorylated heat shock protein 27 promotes lipid clearance in hepatic cells through interacting with STAT3 and activating autophagy.
Heat shock proteins 27 and 70 were involved in the protective effect.
Title: Heat shock proteins 27 and 70 contribute to the protection of Schisandrin B against d-galactosamine-induced liver injury in mice.
The phosphorylation of S82 of the heat shock protein 27 kDa (HSP27), was especially abundant and consistently upregulated in tissues with delays in freezing as short as 2 minutes.
Title: Phosphoproteomic profiling of tumor tissues identifies HSP27 Ser82 phosphorylation as a robust marker of early ischemia.
HspB2 has roles in maintaining ATP levels and as well as chaperone-dependent functions for metabolic homeostasis
Title: Characterization of the Cardiac Overexpression of HSPB2 Reveals Mitochondrial and Myogenic Roles Supported by a Cardiac HspB2 Interactome.
Hsp27 binding to the 3'UTR of Bim mRNA prevents neuronal death during oxidative stress-induced injury.
Title: Hsp27 binding to the 3'UTR of bim mRNA prevents neuronal death during oxidative stress-induced injury: a novel cytoprotective mechanism.
These findings indicate that in mice HSP27 and HSP70 play a key role in the induction of cell-mediated immunity to carcinogenic polyaromatic hydrocarbons
Title: In Vivo Suppression of Heat Shock Protein (HSP)27 and HSP70 Accelerates DMBA-Induced Skin Carcinogenesis by Inducing Antigenic Unresponsiveness to the Initiating Carcinogenic Chemical.

Submit: New GeneRIF Correction See all GeneRIFs (61)

Variation

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Alleles

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

Targeted (3) 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

PMC123035P1 (e-PCR)
- UniSTS:270427

RH143847 (e-PCR)
- UniSTS:233093

D9Mit96 (e-PCR), detects polymorphism
- UniSTS:131983

Homology

Homologs of the Hspb2 gene: The Hspb2 gene is conserved in human, Rhesus monkey, dog, cow, rat, chicken, zebrafish, and frog.
Orthologs from Annotation Pipeline: 388 organisms have orthologs with human gene Hspb2
Orthologs

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables structural constituent of eye lens	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in response to heat	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within somatic muscle development	IGI Inferred from Genetic Interaction more info	PubMed

Component	Evidence Code	Pubs
located_in cytoplasm	ISO Inferred from Sequence Orthology more info
located_in nucleus	ISO Inferred from Sequence Orthology more info

General protein information

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Preferred Names: heat shock protein beta-2

Names: heat shock 27kD protein 2

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_001164708.1 → NP_001158180.1 heat shock protein beta-2 isoform 2

See identical proteins and their annotated locations for NP_001158180.1

Status: VALIDATED

Description

Transcript Variant: This variant (2) uses a different splice site, compared to variant 1. The resulting protein (isoform 2) is missing an internal segment when it is compared to isoform 1.

Source sequence(s)

AK012780, BU704695

Consensus CDS

CCDS90564.1

UniProtKB/Swiss-Prot

Q99PR8

Related

ENSMUSP00000148970.2, ENSMUST00000217159.2

Conserved Domains (1) summary

cl00175
Location:32 → 54

alpha-crystallin-Hsps_p23-like; alpha-crystallin domain (ACD) found in alpha-crystallin-type small heat shock proteins, and a similar domain found in p23 (a cochaperone for Hsp90) and in other p23-like proteins.
NM_024441.3 → NP_077761.3 heat shock protein beta-2 isoform 1

See identical proteins and their annotated locations for NP_077761.3

Status: VALIDATED

Description

Transcript Variant: This variant (1) represents the longer transcript and it encodes the longer protein (isoform 1).

Source sequence(s)

AK012780, BC064051, BU704695

Consensus CDS

CCDS23171.1

UniProtKB/Swiss-Prot

Q99PR8, Q9CZC2

UniProtKB/TrEMBL

A0A6P5QAB3, Q6P3C8

Related

ENSMUSP00000042374.4, ENSMUST00000042790.5

Conserved Domains (1) summary

cl00175
Location:67 → 148

alpha-crystallin-Hsps_p23-like; alpha-crystallin domain (ACD) found in alpha-crystallin-type small heat shock proteins, and a similar domain found in p23 (a cochaperone for Hsp90) and in other p23-like proteins.