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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

Involved in stress resistance and actin organization.

GO - Molecular functioni

  • identical protein binding Source: MGI
  • poly(A) RNA binding Source: MGI
  • protein kinase binding Source: MGI
  • protein kinase C binding Source: BHF-UCL
  • protein kinase C inhibitor activity Source: BHF-UCL
  • ubiquitin binding Source: BHF-UCL

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Stress response

Enzyme and pathway databases

ReactomeiREACT_278878. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_315885. VEGFA-VEGFR2 Pathway.

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:96240. Hspb1.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity
  • Cytoplasmcytoskeletonspindle By similarity

  • Note: Cytoplasmic in interphase cells. Colocalizes with mitotic spindles in mitotic cells. Translocates to the nucleus during heat shock and resides in sub-nuclear structures known as SC35 speckles or nuclear splicing speckles (By similarity).By similarity

GO - Cellular componenti

  • contractile fiber Source: MGI
  • cytoplasm Source: MGI
  • extracellular exosome Source: MGI
  • extracellular space Source: MGI
  • focal adhesion Source: MGI
  • intracellular Source: MGI
  • nucleus Source: MGI
  • plasma membrane Source: MGI
  • proteasome complex Source: BHF-UCL
  • spindle Source: UniProtKB-SubCell
  • Z disc Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Disruption phenotypei

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 209209Heat shock protein beta-1PRO_0000125928Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei15 – 151Phosphoserine; by MAPKAPK2, MAPKAPK3, PKA and PKC2 Publications
Modified residuei27 – 271PhosphoserineBy similarity
Modified residuei86 – 861Phosphoserine; by MAPKAPK2, MAPKAPK3, MAPKAPK5, PKA and PKC2 Publications
Modified residuei87 – 871PhosphoserineBy similarity
Modified residuei90 – 901PhosphoserineBy similarity
Modified residuei102 – 1021PhosphoserineBy similarity
Modified residuei127 – 1271N6-acetyllysineBy similarity
Modified residuei203 – 2031PhosphoserineBy similarity

Post-translational modificationi

Phosphorylation by MAPKAPK2 and MAPKAPK3 in response to stress leads to dissociate HSP27/HSPB1 from large small heat-shock protein (sHsps) oligomers and impair its chaperone activity and ability to protect against oxidative stress effectively. Phosphorylation by MAPKAPK5 in response to PKA stimulation induces F-actin rearrangement.4 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP14602.
PaxDbiP14602.
PRIDEiP14602.

2D gel databases

REPRODUCTION-2DPAGEIPI00128522.
IPI00468068.
P14602.
SWISS-2DPAGEP14602.
UCD-2DPAGEP14602.

PTM databases

PhosphoSiteiP14602.

Expressioni

Gene expression databases

BgeeiP14602.
CleanExiMM_HSPB1.
ExpressionAtlasiP14602. baseline.
GenevisibleiP14602. MM.

Interactioni

Subunit structurei

Associates with alpha- and beta-tubulin, microtubules and CRYAB. Interacts with HSPB8 (By similarity). Interacts with HSPBAP1 and TGFB1I1.By similarity2 Publications

Protein-protein interaction databases

BioGridi200449. 13 interactions.
IntActiP14602. 7 interactions.
MINTiMINT-4098074.
STRINGi10090.ENSMUSP00000005077.

Structurei

3D structure databases

DisProtiDP00142.
ProteinModelPortaliP14602.
SMRiP14602. Positions 20-195.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni74 – 209136Interaction with TGFB1I1By similarityAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiNOG307785.
GeneTreeiENSGT00760000119238.
HOGENOMiHOG000233955.
HOVERGENiHBG054766.
InParanoidiP14602.
KOiK04455.
OMAiDQSFGMP.
OrthoDBiEOG7WHHBK.
PhylomeDBiP14602.
TreeFamiTF105049.

Family and domain databases

Gene3Di2.60.40.790. 2 hits.
InterProiIPR002068. A-crystallin/Hsp20_dom.
IPR001436. Alpha-crystallin/HSP.
IPR031107. HSP20.
IPR008978. HSP20-like_chaperone.
[Graphical view]
PANTHERiPTHR11527. PTHR11527. 1 hit.
PfamiPF00011. HSP20. 1 hit.
[Graphical view]
PRINTSiPR00299. ACRYSTALLIN.
SUPFAMiSSF49764. SSF49764. 1 hit.
PROSITEiPS01031. HSP20. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 131S → T in AAA18335 (PubMed:8132504).Curated
Sequence conflicti13 – 131S → T in AAA18336 (PubMed:8132504).Curated
Sequence conflicti13 – 131S → T in AAA18337 (PubMed:8132504).Curated
Sequence conflicti17 – 171E → G in AAA18335 (PubMed:8132504).Curated
Sequence conflicti67 – 682PA → L in AAA18335 (PubMed:8132504).Curated
Sequence conflicti99 – 991Missing in CAA32818 (PubMed:2645135).Curated
Sequence conflicti99 – 991Missing in CAB37341 (PubMed:2645135).Curated
Sequence conflicti108 – 1092FA → VI in CAA32818 (PubMed:2645135).Curated
Sequence conflicti108 – 1092FA → VI in CAB37341 (PubMed:2645135).Curated
Sequence conflicti141 – 1411C → Q AA sequence (PubMed:2645135).Curated
Sequence conflicti181 – 1811A → T in CAA32818 (PubMed:2645135).Curated
Sequence conflicti181 – 1811A → T in CAB37341 (PubMed:2645135).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei37 – 7034Missing in isoform C. 1 PublicationVSP_002423Add
BLAST
Alternative sequencei61 – 7212Missing in isoform B. 1 PublicationVSP_002422Add
BLAST

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

Cross-referencesi

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.

3D structure databases

DisProtiDP00142.
ProteinModelPortaliP14602.
SMRiP14602. Positions 20-195.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200449. 13 interactions.
IntActiP14602. 7 interactions.
MINTiMINT-4098074.
STRINGi10090.ENSMUSP00000005077.

PTM databases

PhosphoSiteiP14602.

2D gel databases

REPRODUCTION-2DPAGEIPI00128522.
IPI00468068.
P14602.
SWISS-2DPAGEP14602.
UCD-2DPAGEP14602.

Proteomic databases

MaxQBiP14602.
PaxDbiP14602.
PRIDEiP14602.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi3315.
MGIiMGI:96240. Hspb1.

Phylogenomic databases

eggNOGiNOG307785.
GeneTreeiENSGT00760000119238.
HOGENOMiHOG000233955.
HOVERGENiHBG054766.
InParanoidiP14602.
KOiK04455.
OMAiDQSFGMP.
OrthoDBiEOG7WHHBK.
PhylomeDBiP14602.
TreeFamiTF105049.

Enzyme and pathway databases

ReactomeiREACT_278878. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_315885. VEGFA-VEGFR2 Pathway.

Miscellaneous databases

NextBioi288412.
PROiP14602.
SOURCEiSearch...

Gene expression databases

BgeeiP14602.
CleanExiMM_HSPB1.
ExpressionAtlasiP14602. baseline.
GenevisibleiP14602. MM.

Family and domain databases

Gene3Di2.60.40.790. 2 hits.
InterProiIPR002068. A-crystallin/Hsp20_dom.
IPR001436. Alpha-crystallin/HSP.
IPR031107. HSP20.
IPR008978. HSP20-like_chaperone.
[Graphical view]
PANTHERiPTHR11527. PTHR11527. 1 hit.
PfamiPF00011. HSP20. 1 hit.
[Graphical view]
PRINTSiPR00299. ACRYSTALLIN.
SUPFAMiSSF49764. SSF49764. 1 hit.
PROSITEiPS01031. HSP20. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structure and organisation of a murine gene encoding small heat-shock protein Hsp25."
    Gaestel M., Gotthardt R., Mueller T.
    Gene 128:279-283(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A).
  2. "Cloning of the mouse hsp25 gene and an extremely conserved hsp25 pseudogene."
    Froehli E., Aoyama X., Klemenz R.
    Gene 128:273-277(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A).
  3. "Molecular cloning, sequencing and expression in Escherichia coli of the 25-kDa growth-related protein of Ehrlich ascites tumor and its homology to mammalian stress proteins."
    Gaestel M., Gross B., Benndorf R., Strauss M., Schunk W.-H., Kraft R., Otto A., Boehm H., Stahl J., Drabsch H., Bielka H.
    Eur. J. Biochem. 179:209-213(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A), PARTIAL PROTEIN SEQUENCE.
  4. "Differential estrogenic regulation of small M(r) heat shock protein expression in osteoblasts."
    Cooper L.F., Uoshima K.
    J. Biol. Chem. 269:7869-7873(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND C).
    Tissue: Bone.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
    Strain: FVB/N.
    Tissue: Mammary gland.
  6. "Identification of the phosphorylation sites of the murine small heat shock protein hsp25."
    Gaestel M., Schroeder W., Benndorf R., Lippmann C., Buchner K., Hucho F., Erdmann V.A., Bielka H.
    J. Biol. Chem. 266:14721-14724(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-15 AND SER-86.
  7. "Identification of MAPKAP kinase 2 as a major enzyme responsible for the phosphorylation of the small mammalian heat shock proteins."
    Stokoe D., Engel K., Campbell D.G., Cohen P., Gaestel M.
    FEBS Lett. 313:307-313(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-15 AND SER-86 BY MAPKAPK2.
  8. "Small heat shock proteins are molecular chaperones."
    Jakob U., Gaestel M., Engel K., Buchner J.
    J. Biol. Chem. 268:1517-1520(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY MAPKAPK2.
  9. "Identification and characterization of a novel protein from Sertoli cells, PASS1, that associates with mammalian small stress protein hsp27."
    Liu C., Gilmont R.R., Benndorf R., Welsh M.J.
    J. Biol. Chem. 275:18724-18731(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HSPBAP1.
  10. "Identification and characterization of hic-5/ARA55 as an hsp27 binding protein."
    Jia Y., Ransom R.F., Shibanuma M., Liu C., Welsh M.J., Smoyer W.E.
    J. Biol. Chem. 276:39911-39918(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TGFB1I1.
  11. "Insights into function and regulation of small heat shock protein 25 (HSPB1) in a mouse model with targeted gene disruption."
    Huang L., Min J.N., Masters S., Mivechi N.F., Moskophidis D.
    Genesis 45:487-501(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  13. "Distinct roles of MK2 and MK5 in cAMP/PKA- and stress/p38MAPK-induced heat shock protein 27 phosphorylation."
    Shiryaev A., Dumitriu G., Moens U.
    J. Mol. Signal. 6:4-4(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY MAPKAPK5.

Entry informationi

Entry nameiHSPB1_MOUSE
AccessioniPrimary (citable) accession number: P14602
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: June 1, 1994
Last modified: July 22, 2015
This is version 161 of the entry and version 3 of the sequence. [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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.