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P15991

- HSPB1_CRILO

UniProt

P15991 - HSPB1_CRILO

Protein

Heat shock protein beta-1

Gene

HSPB1

Organism
Cricetulus longicaudatus (Long-tailed dwarf hamster) (Chinese hamster)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 83 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      Previous versions | rss
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    Functioni

    Involved in stress resistance and actin organization.

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. response to stress Source: UniProtKB-KW

    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

    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 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

    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...
    MobiDBi 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: October 1, 2014
    This is version 83 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