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Protein

Heat shock protein beta-1

Gene

HSPB1

Organism
Cricetulus longicaudatus (Long-tailed dwarf hamster) (Chinese hamster)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Involved in stress resistance and actin organization.

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Stress response

Names & Taxonomyi

Protein namesi
Recommended name:
Heat shock protein beta-1
Short name:
HspB1
Alternative name(s):
Heat shock 27 kDa protein
Short name:
HSP 27
Gene namesi
Name:HSPB1
Synonyms:HSP27
OrganismiCricetulus longicaudatus (Long-tailed dwarf hamster) (Chinese hamster)
Taxonomic identifieri10030 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeCricetulus

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

  1. cytoplasm Source: UniProtKB
  2. nucleus Source: UniProtKB
  3. spindle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 213213Heat shock protein beta-1PRO_0000125926Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei15 – 151Phosphoserine; by MAPKAPK2 and MAPKAPK3By similarity
Modified residuei27 – 271PhosphoserineBy similarity
Modified residuei90 – 901Phosphoserine; by MAPKAPK2, MAPKAPK3 and MAPKAPK5By similarity
Modified residuei91 – 911PhosphoserineBy similarity
Modified residuei94 – 941PhosphoserineBy similarity
Modified residuei106 – 1061PhosphoserineBy similarity
Modified residuei131 – 1311N6-acetyllysineBy similarity
Modified residuei207 – 2071PhosphoserineBy 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 (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiP15991.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
DAXXQ9UER73EBI-1559114,EBI-77321From a different organism.

Protein-protein interaction databases

IntActiP15991. 3 interactions.
MINTiMINT-146233.

Structurei

3D structure databases

ProteinModelPortaliP15991.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni78 – 213136Interaction with TGFB1I1By similarityAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

HOVERGENiHBG054766.

Family and domain databases

Gene3Di2.60.40.790. 2 hits.
InterProiIPR002068. a-crystallin/Hsp20_dom.
IPR001436. Alpha-crystallin/HSP.
IPR008978. HSP20-like_chaperone.
[Graphical view]
PfamiPF00011. HSP20. 1 hit.
[Graphical view]
PIRSFiPIRSF036514. Sm_HSP_B1. 1 hit.
PRINTSiPR00299. ACRYSTALLIN.
SUPFAMiSSF49764. SSF49764. 1 hit.
PROSITEiPS01031. HSP20. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P15991-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTERRVPFSL LRSPSWEPFR DWYPAHSRLF DQAFGVPRLP DEWSQWFSAA
60 70 80 90 100
GWPGYVRPLP AATAEGPAAV ALAAPLAAPA FHRALNRQLS SGVSEIRQTA
110 120 130 140 150
DRWRVSLDVN HFAPEELTVK TKEGVVEITG KHEERQDEHG YISRCFTRKY
160 170 180 190 200
TLPPGVDPTL VSSSLSPEGT LTVEAPLPKT ATQSAEITIP VTFEARAQIG
210
GQEAGKSEQS GAK
Length:213
Mass (Da):23,419
Last modified:April 1, 1990 - v1
Checksum:i29E633DBBFA3F89F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51747 mRNA. Translation: CAA36036.1.
PIRiS15907.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51747 mRNA. Translation: CAA36036.1.
PIRiS15907.

3D structure databases

ProteinModelPortaliP15991.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP15991. 3 interactions.
MINTiMINT-146233.

Proteomic databases

PRIDEiP15991.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG054766.

Family and domain databases

Gene3Di2.60.40.790. 2 hits.
InterProiIPR002068. a-crystallin/Hsp20_dom.
IPR001436. Alpha-crystallin/HSP.
IPR008978. HSP20-like_chaperone.
[Graphical view]
PfamiPF00011. HSP20. 1 hit.
[Graphical view]
PIRSFiPIRSF036514. Sm_HSP_B1. 1 hit.
PRINTSiPR00299. ACRYSTALLIN.
SUPFAMiSSF49764. SSF49764. 1 hit.
PROSITEiPS01031. HSP20. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiHSPB1_CRILO
AccessioniPrimary (citable) accession number: P15991
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: March 4, 2015
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. 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.