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P02518

- HSP27_DROME

UniProt

P02518 - HSP27_DROME

Protein

Heat shock protein 27

Gene

Hsp27

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 2 (01 Nov 1990)
      Previous versions | rss
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    Functioni

    GO - Molecular functioni

    1. protein binding Source: FlyBase

    GO - Biological processi

    1. behavioral response to starvation Source: FlyBase
    2. defense response to bacterium Source: FlyBase
    3. defense response to fungus Source: FlyBase
    4. determination of adult lifespan Source: FlyBase
    5. imaginal disc-derived wing morphogenesis Source: FlyBase

    Keywords - Biological processi

    Stress response

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Heat shock protein 27
    Gene namesi
    Name:Hsp27
    ORF Names:CG4466
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3L

    Organism-specific databases

    FlyBaseiFBgn0001226. Hsp27.

    Subcellular locationi

    GO - Cellular componenti

    1. microtubule associated complex Source: FlyBase

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 213213Heat shock protein 27PRO_0000125966Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei58 – 581Phosphoserine1 Publication
    Modified residuei75 – 751Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP02518.
    PRIDEiP02518.

    Expressioni

    Gene expression databases

    BgeeiP02518.

    Interactioni

    Protein-protein interaction databases

    BioGridi64473. 31 interactions.
    DIPiDIP-18749N.
    IntActiP02518. 4 interactions.
    MINTiMINT-749799.
    STRINGi7227.FBpp0076182.

    Structurei

    3D structure databases

    ProteinModelPortaliP02518.
    SMRiP02518. Positions 90-160.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiNOG256133.
    GeneTreeiENSGT00740000115405.
    InParanoidiP02518.
    OMAiRKYTLPK.
    OrthoDBiEOG7WHHBK.
    PhylomeDBiP02518.

    Family and domain databases

    Gene3Di2.60.40.790. 1 hit.
    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.

    P02518-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSIIPLLHLA RELDHDYRTD WGHLLEDDFG FGVHAHDLFH PRRLLLPNTL    50
    GLGRRRYSPY ERSHGHHNQM SRRASGGPNA LLPAVGKDGF QVCMDVSQFK 100
    PNELTVKVVD NTVVVEGKHE EREDGHGMIQ RHFVRKYTLP KGFDPNEVVS 150
    TVSSDGVLTL KAPPPPSKEQ AKSERIVQIQ QTGPAHLSVK APAPEAGDGK 200
    AENGSGEKME TSK 213
    Length:213
    Mass (Da):23,617
    Last modified:November 1, 1990 - v2
    Checksum:iE08B39801A181F39
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti40 – 401H → N(PubMed:6285380)Curated
    Sequence conflicti66 – 661H → P(PubMed:6285380)Curated
    Sequence conflicti94 – 941M → I(PubMed:6285380)Curated
    Sequence conflicti143 – 1475FDPNE → LTPTK(PubMed:6285380)Curated
    Sequence conflicti161 – 1611K → R(PubMed:6285380)Curated
    Sequence conflicti167 – 1704SKEQ → GRER(PubMed:6285380)Curated
    Sequence conflicti178 – 1781Q → R(PubMed:6285380)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01101 Genomic DNA. Translation: AAA28638.1.
    X03891 Genomic DNA. Translation: CAA27527.1.
    AE014296 Genomic DNA. Translation: AAF50285.1.
    AY118471 mRNA. Translation: AAM49840.1.
    PIRiA02921. HHFF27.
    D20647.
    RefSeqiNP_524000.1. NM_079276.4.
    UniGeneiDm.2803.

    Genome annotation databases

    EnsemblMetazoaiFBtr0076454; FBpp0076182; FBgn0001226.
    GeneIDi39078.
    KEGGidme:Dmel_CG4466.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01101 Genomic DNA. Translation: AAA28638.1 .
    X03891 Genomic DNA. Translation: CAA27527.1 .
    AE014296 Genomic DNA. Translation: AAF50285.1 .
    AY118471 mRNA. Translation: AAM49840.1 .
    PIRi A02921. HHFF27.
    D20647.
    RefSeqi NP_524000.1. NM_079276.4.
    UniGenei Dm.2803.

    3D structure databases

    ProteinModelPortali P02518.
    SMRi P02518. Positions 90-160.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 64473. 31 interactions.
    DIPi DIP-18749N.
    IntActi P02518. 4 interactions.
    MINTi MINT-749799.
    STRINGi 7227.FBpp0076182.

    Proteomic databases

    PaxDbi P02518.
    PRIDEi P02518.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0076454 ; FBpp0076182 ; FBgn0001226 .
    GeneIDi 39078.
    KEGGi dme:Dmel_CG4466.

    Organism-specific databases

    CTDi 39078.
    FlyBasei FBgn0001226. Hsp27.

    Phylogenomic databases

    eggNOGi NOG256133.
    GeneTreei ENSGT00740000115405.
    InParanoidi P02518.
    OMAi RKYTLPK.
    OrthoDBi EOG7WHHBK.
    PhylomeDBi P02518.

    Miscellaneous databases

    ChiTaRSi HSPB1. drosophila.
    GenomeRNAii 39078.
    NextBioi 811805.

    Gene expression databases

    Bgeei P02518.

    Family and domain databases

    Gene3Di 2.60.40.790. 1 hit.
    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. "Nucleotide sequence analysis of the Drosophila small heat shock gene cluster at locus 67B."
      Southgate R., Ayme A., Voellmy R.
      J. Mol. Biol. 165:35-57(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Four small Drosophila heat shock proteins are related to each other and to mammalian alpha-crystallin."
      Ingolia T.D., Craig E.A.
      Proc. Natl. Acad. Sci. U.S.A. 79:2360-2364(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    4. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Ovary.
    6. "An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells."
      Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A.
      Mol. Biosyst. 3:275-286(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75, IDENTIFICATION BY MASS SPECTROMETRY.
    7. "Phosphoproteome analysis of Drosophila melanogaster embryos."
      Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
      J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryo.

    Entry informationi

    Entry nameiHSP27_DROME
    AccessioniPrimary (citable) accession number: P02518
    Secondary accession number(s): Q9VSX6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: November 1, 1990
    Last modified: October 1, 2014
    This is version 122 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3