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P15991

- HSPB1_CRILO

UniProt

P15991 - HSPB1_CRILO

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Protein
Heat shock protein beta-1
Gene
HSPB1, HSP27
Organism
Cricetulus longicaudatus (Long-tailed dwarf hamster) (Chinese hamster)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Involved in stress resistance and actin organization.

GO - Molecular functioni

  1. protein binding Source: IntAct
Complete GO annotation...

GO - Biological processi

  1. response to stress Source: UniProtKB-KW
Complete GO annotation...

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.

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-1
PRO_0000125926Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei15 – 151Phosphoserine; by MAPKAPK2 and MAPKAPK3 By similarity
Modified residuei27 – 271Phosphoserine By similarity
Modified residuei90 – 901Phosphoserine; by MAPKAPK2, MAPKAPK3 and MAPKAPK5 By similarity
Modified residuei91 – 911Phosphoserine By similarity
Modified residuei94 – 941Phosphoserine By similarity
Modified residuei131 – 1311N6-acetyllysine By similarity
Modified residuei207 – 2071Phosphoserine By 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.

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.

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.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni78 – 213136Interaction with TGFB1I1 By similarity
Add
BLAST

Sequence similaritiesi

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

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MTERRVPFSL LRSPSWEPFR DWYPAHSRLF DQAFGVPRLP DEWSQWFSAA    50
GWPGYVRPLP AATAEGPAAV ALAAPLAAPA FHRALNRQLS SGVSEIRQTA 100
DRWRVSLDVN HFAPEELTVK TKEGVVEITG KHEERQDEHG YISRCFTRKY 150
TLPPGVDPTL VSSSLSPEGT LTVEAPLPKT ATQSAEITIP VTFEARAQIG 200
GQEAGKSEQS GAK 213
Length:213
Mass (Da):23,419
Last modified:April 1, 1990 - v1
Checksum:i29E633DBBFA3F89F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X51747 mRNA. Translation: CAA36036.1.
PIRiS15907.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X51747 mRNA. Translation: CAA36036.1 .
PIRi S15907.

3D structure databases

ProteinModelPortali P15991.
ModBasei Search...

Protein-protein interaction databases

IntActi P15991. 3 interactions.
MINTi MINT-146233.

Proteomic databases

PRIDEi P15991.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG054766.

Family and domain databases

Gene3Di 2.60.40.790. 2 hits.
InterProi IPR002068. a-crystallin/Hsp20_dom.
IPR001436. Alpha-crystallin/HSP.
IPR008978. HSP20-like_chaperone.
[Graphical view ]
Pfami PF00011. HSP20. 1 hit.
[Graphical view ]
PIRSFi PIRSF036514. Sm_HSP_B1. 1 hit.
PRINTSi PR00299. ACRYSTALLIN.
SUPFAMi SSF49764. SSF49764. 1 hit.
PROSITEi PS01031. HSP20. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: June 11, 2014
This is version 82 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

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