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P14602 (HSPB1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Hspb1
Synonyms:Hsp25, Hsp27
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length209 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in stress resistance and actin organization.

Subunit structure

Associates with alpha- and beta-tubulin, microtubules and CRYAB. Interacts with HSPB8 By similarity. Interacts with HSPBAP1 and TGFB1I1. Ref.9 Ref.10

Subcellular location

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.

Post-translational modification

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.

Disruption phenotype

No visible phoenotype. Mice are viable and fertile with no apparent morphological abnormalities in tissues under physiological conditions. Ref.11

Sequence similarities

Belongs to the small heat shock protein (HSP20) family.

Ontologies

Keywords
   Biological processStress response
   Cellular componentCytoplasm
Cytoskeleton
Nucleus
   Coding sequence diversityAlternative splicing
   Molecular functionChaperone
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processnegative regulation of apoptotic signaling pathway

Inferred from direct assay PubMed 15731106. Source: MGI

negative regulation of intrinsic apoptotic signaling pathway in response to oxidative stress

Inferred from direct assay PubMed 15731106. Source: BHF-UCL

negative regulation of protein kinase activity

Inferred from direct assay PubMed 15731106. Source: BHF-UCL

negative regulation of protein serine/threonine kinase activity

Inferred from direct assay PubMed 15731106. Source: GOC

positive regulation of angiogenesis

Inferred from electronic annotation. Source: Ensembl

positive regulation of blood vessel endothelial cell migration

Inferred from electronic annotation. Source: Ensembl

positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of interleukin-1 beta production

Inferred from direct assay PubMed 12385642. Source: BHF-UCL

positive regulation of tumor necrosis factor biosynthetic process

Inferred from direct assay PubMed 12385642. Source: BHF-UCL

regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from direct assay PubMed 12385642. Source: BHF-UCL

response to unfolded protein

Non-traceable author statement PubMed 10859165. Source: BHF-UCL

response to virus

Inferred from sequence or structural similarity. Source: BHF-UCL

   Cellular_componentZ disc

Inferred from direct assay PubMed 14627610. Source: MGI

cell surface

Inferred from electronic annotation. Source: Ensembl

contractile fiber

Inferred from direct assay PubMed 14627610. Source: MGI

cytoplasm

Inferred from direct assay PubMed 11774370. Source: MGI

intracellular

Inferred from direct assay PubMed 9122205. Source: MGI

nucleus

Inferred from direct assay PubMed 11774370. Source: MGI

plasma membrane

Inferred from direct assay PubMed 14627610. Source: MGI

proteasome complex

Inferred from sequence or structural similarity. Source: BHF-UCL

spindle

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionprotein kinase C binding

Inferred from direct assay PubMed 15731106. Source: BHF-UCL

protein kinase C inhibitor activity

Inferred from direct assay PubMed 15731106. Source: BHF-UCL

ubiquitin binding

Inferred from sequence or structural similarity. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform A (identifier: P14602-1)

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.
Isoform B (identifier: P14602-2)

The sequence of this isoform differs from the canonical sequence as follows:
     61-72: Missing.
Isoform C (identifier: P14602-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 209209Heat shock protein beta-1
PRO_0000125928

Regions

Region74 – 209136Interaction with TGFB1I1 By similarity

Amino acid modifications

Modified residue151Phosphoserine; by MAPKAPK2, MAPKAPK3, PKA and PKC Ref.6 Ref.7
Modified residue271Phosphoserine By similarity
Modified residue861Phosphoserine; by MAPKAPK2, MAPKAPK3, MAPKAPK5, PKA and PKC Ref.6 Ref.7
Modified residue871Phosphoserine By similarity
Modified residue901Phosphoserine By similarity
Modified residue1271N6-acetyllysine By similarity
Modified residue2031Phosphoserine By similarity

Natural variations

Alternative sequence37 – 7034Missing in isoform C.
VSP_002423
Alternative sequence61 – 7212Missing in isoform B.
VSP_002422

Experimental info

Sequence conflict131S → T in AAA18335. Ref.4
Sequence conflict131S → T in AAA18336. Ref.4
Sequence conflict131S → T in AAA18337. Ref.4
Sequence conflict171E → G in AAA18335. Ref.4
Sequence conflict67 – 682PA → L in AAA18335. Ref.4
Sequence conflict991Missing in CAA32818. Ref.3
Sequence conflict991Missing in CAB37341. Ref.3
Sequence conflict108 – 1092FA → VI in CAA32818. Ref.3
Sequence conflict108 – 1092FA → VI in CAB37341. Ref.3
Sequence conflict1411C → Q AA sequence Ref.3
Sequence conflict1811A → T in CAA32818. Ref.3
Sequence conflict1811A → T in CAB37341. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform A [UniParc].

Last modified June 1, 1994. Version 3.
Checksum: 31BD9FAF4E107C50

FASTA20923,014
        10         20         30         40         50         60 
MTERRVPFSL LRSPSWEPFR DWYPAHSRLF DQAFGVPRLP DEWSQWFSAA GWPGYVRPLP 

        70         80         90        100        110        120 
AATAEGPAAV TLAAPAFSRA LNRQLSSGVS EIRQTADRWR VSLDVNHFAP EELTVKTKEG 

       130        140        150        160        170        180 
VVEITGKHEE RQDEHGYISR CFTRKYTLPP GVDPTLVSSS LSPEGTLTVE APLPKAVTQS 

       190        200 
AEITIPVTFE ARAQIGGPEA GKSEQSGAK 

« Hide

Isoform B [UniParc].

Checksum: 071D3C112509C01A
Show »

FASTA19721,961
Isoform C [UniParc].

Checksum: AA7E60872B1C485B
Show »

FASTA17519,380

References

« Hide 'large scale' references
[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]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA53423.
JN0679. I49763.
S02143.
RefSeqNP_038588.2. NM_013560.2.
UniGeneMm.13849.

3D structure databases

DisProtDP00142.
ProteinModelPortalP14602.
SMRP14602. Positions 20-195.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200449. 13 interactions.
IntActP14602. 7 interactions.
MINTMINT-4098074.
STRING10090.ENSMUSP00000005077.

PTM databases

PhosphoSiteP14602.

2D gel databases

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

Proteomic databases

PaxDbP14602.
PRIDEP14602.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000005077; ENSMUSP00000005077; ENSMUSG00000004951. [P14602-1]
GeneID15507.
KEGGmmu:15507.
UCSCuc008zze.2. mouse. [P14602-1]

Organism-specific databases

CTD3315.
MGIMGI:96240. Hspb1.

Phylogenomic databases

eggNOGNOG307785.
HOGENOMHOG000233955.
HOVERGENHBG054766.
InParanoidP14602.
KOK04455.
OMARTPSWDP.
OrthoDBEOG7WHHBK.
PhylomeDBP14602.
TreeFamTF105049.

Gene expression databases

BgeeP14602.
CleanExMM_HSPB1.
GenevestigatorP14602.

Family and domain databases

Gene3D2.60.40.790. 2 hits.
InterProIPR002068. a-crystallin/Hsp20_dom.
IPR001436. Alpha-crystallin/HSP.
IPR008978. HSP20-like_chaperone.
[Graphical view]
PfamPF00011. HSP20. 1 hit.
[Graphical view]
PIRSFPIRSF036514. Sm_HSP_B1. 1 hit.
PRINTSPR00299. ACRYSTALLIN.
SUPFAMSSF49764. SSF49764. 1 hit.
PROSITEPS01031. HSP20. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio288412.
PROP14602.
SOURCESearch...

Entry information

Entry nameHSPB1_MOUSE
AccessionPrimary (citable) accession number: P14602
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: June 1, 1994
Last modified: April 16, 2014
This is version 147 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot