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P15991 (HSPB1_CRILO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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):
Heat shock 27 kDa protein
Short name=HSP 27
Gene names
Name:HSPB1
Synonyms:HSP27
OrganismCricetulus longicaudatus (Long-tailed dwarf hamster) (Chinese hamster)
Taxonomic identifier10030 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeCricetulus

Protein attributes

Sequence length213 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 and HSPBAP1 By similarity.

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 By similarity.

Sequence similarities

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

Ontologies

Keywords
   Biological processStress response
   Cellular componentCytoplasm
Cytoskeleton
Nucleus
   Molecular functionChaperone
   PTMAcetylation
Phosphoprotein
Gene Ontology (GO)
   Biological_processresponse to stress

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

spindle

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 11003656. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DAXXQ9UER73EBI-1559114,EBI-77321From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 213213Heat shock protein beta-1
PRO_0000125926

Regions

Region78 – 213136Interaction with TGFB1I1 By similarity

Amino acid modifications

Modified residue151Phosphoserine; by MAPKAPK2 and MAPKAPK3 By similarity
Modified residue271Phosphoserine By similarity
Modified residue901Phosphoserine; by MAPKAPK2, MAPKAPK3 and MAPKAPK5 By similarity
Modified residue911Phosphoserine By similarity
Modified residue941Phosphoserine By similarity
Modified residue1311N6-acetyllysine By similarity
Modified residue2071Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
P15991 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 29E633DBBFA3F89F

FASTA21323,419
        10         20         30         40         50         60 
MTERRVPFSL LRSPSWEPFR DWYPAHSRLF DQAFGVPRLP DEWSQWFSAA GWPGYVRPLP 

        70         80         90        100        110        120 
AATAEGPAAV ALAAPLAAPA FHRALNRQLS SGVSEIRQTA DRWRVSLDVN HFAPEELTVK 

       130        140        150        160        170        180 
TKEGVVEITG KHEERQDEHG YISRCFTRKY TLPPGVDPTL VSSSLSPEGT LTVEAPLPKT 

       190        200        210 
ATQSAEITIP VTFEARAQIG GQEAGKSEQS GAK 

« Hide

References

[1]"Sequence of the Chinese hamster small heat shock protein HSP27."
Lavoie J., Chretien P., Landry J.
Nucleic Acids Res. 18:1637-1637(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Lung fibroblast.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X51747 mRNA. Translation: CAA36036.1.
PIRS15907.

3D structure databases

ProteinModelPortalP15991.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP15991. 3 interactions.
MINTMINT-146233.

Proteomic databases

PRIDEP15991.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG054766.

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...

Entry information

Entry nameHSPB1_CRILO
AccessionPrimary (citable) accession number: P15991
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: June 11, 2014
This is version 82 of the entry and version 1 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