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Protein

Heat shock protein beta-1

Gene

Hspb1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding-competent state. Plays a role in stress resistance and actin organization (PubMed:17661394). Through its molecular chaperone activity may regulate numerous biological processes including the phosphorylation and the axonal transport of neurofilament proteins (By similarity).By similarity1 Publication

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionChaperone
Biological processStress response

Enzyme and pathway databases

ReactomeiR-MMU-4420097. VEGFA-VEGFR2 Pathway.
R-MMU-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-MMU-5687128. MAPK6/MAPK4 signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Heat shock protein beta-1
Short name:
HspB1
Alternative name(s):
Growth-related 25 kDa protein
Heat shock 25 kDa protein
Short name:
HSP 25
Heat shock 27 kDa protein
Short name:
HSP 27
p25
Gene namesi
Name:Hspb1
Synonyms:Hsp25, Hsp27
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:96240. Hspb1.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Disruption phenotypei

Mice are viable and fertile with no apparent morphological abnormalities in tissues under physiological conditions.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001259281 – 209Heat shock protein beta-1Add BLAST209

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei12Omega-N-methylarginineCombined sources1
Modified residuei13PhosphoserineBy similarity1
Modified residuei15Phosphoserine; by MAPKAPK2, MAPKAPK3, PKA and PKC2 Publications1
Modified residuei27PhosphoserineBy similarity1
Modified residuei86Phosphoserine; by MAPKAPK2, MAPKAPK3, MAPKAPK5, PKA and PKCCombined sources2 Publications1
Modified residuei87PhosphoserineBy similarity1
Modified residuei90PhosphoserineBy similarity1
Modified residuei102PhosphoserineBy similarity1
Modified residuei127N6-acetyllysineBy similarity1
Modified residuei178PhosphothreonineBy similarity1
Modified residuei180PhosphoserineBy similarity1
Modified residuei203PhosphoserineBy similarity1

Post-translational modificationi

Phosphorylated upon exposure to protein kinase C activators and heat shock (By similarity). Phosphorylation by MAPKAPK2 and MAPKAPK3 in response to stress dissociates HSPB1 from large small heat-shock protein (sHsps) oligomers and impairs its chaperone activity and ability to protect against oxidative stress effectively. Phosphorylation by MAPKAPK5 in response to PKA stimulation induces F-actin rearrangement (PubMed:1332886, PubMed:1860870, PubMed:21575178, PubMed:8093612).By similarity4 Publications

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

PaxDbiP14602.
PeptideAtlasiP14602.
PRIDEiP14602.

2D gel databases

REPRODUCTION-2DPAGEiIPI00128522.
IPI00468068.
P14602.
SWISS-2DPAGEiP14602.
UCD-2DPAGEiP14602.

PTM databases

iPTMnetiP14602.
PhosphoSitePlusiP14602.

Expressioni

Gene expression databases

BgeeiENSMUSG00000004951.
CleanExiMM_HSPB1.
ExpressionAtlasiP14602. baseline and differential.
GenevisibleiP14602. MM.

Interactioni

Subunit structurei

Homooligomer. Homodimer; becomes monomeric upon activation. Heterooligomer; with HSPB6. Associates with alpha- and beta-tubulin (By similarity). Interacts with TGFB1I1 (PubMed:11546764). Interacts with CRYAB (By similarity). Interacts with HSPB8 (PubMed:11342557). Interacts with HSPBAP1 (PubMed:10751411).By similarity3 Publications

GO - Molecular functioni

Protein-protein interaction databases

BioGridi200449. 16 interactors.
CORUMiP14602.
IntActiP14602. 8 interactors.
MINTiMINT-4098074.
STRINGi10090.ENSMUSP00000005077.

Structurei

3D structure databases

DisProtiDP00142.
ProteinModelPortaliP14602.
SMRiP14602.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini80 – 188sHSPPROSITE-ProRule annotationAdd BLAST109

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni74 – 209Interaction with TGFB1I1By similarityAdd BLAST136

Sequence similaritiesi

Belongs to the small heat shock protein (HSP20) family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3591. Eukaryota.
ENOG410YERS. LUCA.
GeneTreeiENSGT00760000119238.
HOGENOMiHOG000233955.
HOVERGENiHBG054766.
InParanoidiP14602.
KOiK04455.
OMAiFDQSFGM.
OrthoDBiEOG091G0USC.
PhylomeDBiP14602.
TreeFamiTF105049.

Family and domain databases

Gene3Di2.60.40.790. 1 hit.
InterProiView protein in InterPro
IPR002068. A-crystallin/Hsp20_dom.
IPR001436. Alpha-crystallin/HSP.
IPR031107. HSP20.
IPR008978. HSP20-like_chaperone.
PANTHERiPTHR11527. PTHR11527. 1 hit.
PfamiView protein in Pfam
PF00011. HSP20. 1 hit.
PRINTSiPR00299. ACRYSTALLIN.
SUPFAMiSSF49764. SSF49764. 1 hit.
PROSITEiView protein in PROSITE
PS01031. SHSP. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist.
Isoform A (identifier: P14602-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MTERRVPFSL LRSPSWEPFR DWYPAHSRLF DQAFGVPRLP DEWSQWFSAA
60 70 80 90 100
GWPGYVRPLP AATAEGPAAV TLAAPAFSRA LNRQLSSGVS EIRQTADRWR
110 120 130 140 150
VSLDVNHFAP EELTVKTKEG VVEITGKHEE RQDEHGYISR CFTRKYTLPP
160 170 180 190 200
GVDPTLVSSS LSPEGTLTVE APLPKAVTQS AEITIPVTFE ARAQIGGPEA

GKSEQSGAK
Length:209
Mass (Da):23,014
Last modified:June 1, 1994 - v3
Checksum:i31BD9FAF4E107C50
GO
Isoform B (identifier: P14602-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     61-72: Missing.

Show »
Length:197
Mass (Da):21,961
Checksum:i071D3C112509C01A
GO
Isoform C (identifier: P14602-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     37-70: Missing.

Show »
Length:175
Mass (Da):19,380
Checksum:iAA7E60872B1C485B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti13S → T in AAA18335 (PubMed:8132504).Curated1
Sequence conflicti13S → T in AAA18336 (PubMed:8132504).Curated1
Sequence conflicti13S → T in AAA18337 (PubMed:8132504).Curated1
Sequence conflicti17E → G in AAA18335 (PubMed:8132504).Curated1
Sequence conflicti67 – 68PA → L in AAA18335 (PubMed:8132504).Curated2
Sequence conflicti99Missing in CAA32818 (PubMed:2645135).Curated1
Sequence conflicti99Missing in CAB37341 (PubMed:2645135).Curated1
Sequence conflicti108 – 109FA → VI in CAA32818 (PubMed:2645135).Curated2
Sequence conflicti108 – 109FA → VI in CAB37341 (PubMed:2645135).Curated2
Sequence conflicti141C → Q AA sequence (PubMed:2645135).Curated1
Sequence conflicti181A → T in CAA32818 (PubMed:2645135).Curated1
Sequence conflicti181A → T in CAB37341 (PubMed:2645135).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_00242337 – 70Missing in isoform C. 1 PublicationAdd BLAST34
Alternative sequenceiVSP_00242261 – 72Missing in isoform B. 1 PublicationAdd BLAST12

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14687 mRNA. Translation: CAA32818.1.
X14686 mRNA. Translation: CAB37341.1.
L11609, L11608 Genomic DNA. Translation: AAA37862.1.
L07577 Genomic DNA. Translation: AAA37861.1.
U03560 mRNA. Translation: AAA18335.1.
U03561 mRNA. Translation: AAA18336.1.
U03562 mRNA. Translation: AAA18337.1.
BC018257 mRNA. Translation: AAH18257.1.
CCDSiCCDS39320.1. [P14602-1]
PIRiA53423.
I49763. JN0679.
S02143.
RefSeqiNP_038588.2. NM_013560.2. [P14602-1]
UniGeneiMm.13849.

Genome annotation databases

EnsembliENSMUST00000005077; ENSMUSP00000005077; ENSMUSG00000004951. [P14602-1]
GeneIDi15507.
KEGGimmu:15507.
UCSCiuc008zze.2. mouse. [P14602-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiHSPB1_MOUSE
AccessioniPrimary (citable) accession number: P14602
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: June 1, 1994
Last modified: September 27, 2017
This is version 178 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families