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O14558

- HSPB6_HUMAN

UniProt

O14558 - HSPB6_HUMAN

Protein

Heat shock protein beta-6

Gene

HSPB6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. Functioni

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. protein homodimerization activity Source: UniProtKB
    3. structural constituent of eye lens Source: InterPro

    GO - Biological processi

    1. regulation of muscle contraction Source: Ensembl
    2. response to stress Source: UniProtKB-KW

    Keywords - Biological processi

    Stress response

    Enzyme and pathway databases

    SignaLinkiO14558.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Heat shock protein beta-6
    Short name:
    HspB6
    Alternative name(s):
    Heat shock 20 kDa-like protein p20
    Gene namesi
    Name:HSPB6
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:26511. HSPB6.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication
    Note: Translocates to nuclear foci during heat shock.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134983584.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 160160Heat shock protein beta-6PRO_0000125939Add
    BLAST

    Post-translational modificationi

    The N-terminus is blocked.

    Proteomic databases

    PaxDbiO14558.
    PRIDEiO14558.

    2D gel databases

    REPRODUCTION-2DPAGEO14558.
    UCD-2DPAGEO14558.

    PTM databases

    PhosphoSiteiO14558.

    Expressioni

    Gene expression databases

    ArrayExpressiO14558.
    BgeeiO14558.
    CleanExiHS_HSPB6.
    GenevestigatoriO14558.

    Organism-specific databases

    HPAiCAB001974.
    HPA044153.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HSPB8Q9UJY12EBI-739095,EBI-739074

    Protein-protein interaction databases

    BioGridi125988. 3 interactions.
    IntActiO14558. 3 interactions.
    MINTiMINT-7002024.
    STRINGi9606.ENSP00000004982.

    Structurei

    Secondary structure

    1
    160
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi74 – 796
    Helixi85 – 873
    Beta strandi88 – 936
    Beta strandi96 – 10712
    Beta strandi109 – 12214
    Helixi129 – 1313
    Beta strandi133 – 1364
    Beta strandi140 – 1467

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4JUSX-ray2.50A/B/C/D/E/F/G/H57-160[»]
    4JUTX-ray2.20A/B/C/D/E/F/G/H57-160[»]
    ProteinModelPortaliO14558.
    SMRiO14558. Positions 5-154.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiNOG236548.
    HOGENOMiHOG000233954.
    HOVERGENiHBG054766.
    InParanoidiO14558.
    KOiK09545.
    OMAiFIAREFH.
    OrthoDBiEOG7WHHBK.
    PhylomeDBiO14558.

    Family and domain databases

    Gene3Di2.60.40.790. 1 hit.
    InterProiIPR002068. a-crystallin/Hsp20_dom.
    IPR001436. Alpha-crystallin/HSP.
    IPR003090. Alpha-crystallin_N.
    IPR008978. HSP20-like_chaperone.
    [Graphical view]
    PfamiPF00525. Crystallin. 1 hit.
    PF00011. 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.

    O14558-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEIPVPVQPS WLRRASAPLP GLSAPGRLFD QRFGEGLLEA ELAALCPTTL    50
    APYYLRAPSV ALPVAQVPTD PGHFSVLLDV KHFSPEEIAV KVVGEHVEVH 100
    ARHEERPDEH GFVAREFHRR YRLPPGVDPA AVTSALSPEG VLSIQAAPAS 150
    AQAPPPAAAK 160
    Length:160
    Mass (Da):17,136
    Last modified:August 2, 2002 - v2
    Checksum:i3BFB1FFB5877F2E7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti20 – 201P → L in AAH68046. (PubMed:15489334)Curated
    Sequence conflicti64 – 663Missing in AAB81196. (PubMed:15057824)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK056951 mRNA. Translation: BAB71323.1.
    AC002398 Genomic DNA. Translation: AAB81196.1.
    BC068046 mRNA. Translation: AAH68046.1.
    CCDSiCCDS12475.1.
    PIRiB53814.
    T00703.
    RefSeqiNP_653218.1. NM_144617.2.
    UniGeneiHs.534538.
    Hs.744178.

    Genome annotation databases

    EnsembliENST00000004982; ENSP00000004982; ENSG00000004776.
    ENST00000592984; ENSP00000468057; ENSG00000004776.
    GeneIDi126393.
    KEGGihsa:126393.
    UCSCiuc002obn.2. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK056951 mRNA. Translation: BAB71323.1 .
    AC002398 Genomic DNA. Translation: AAB81196.1 .
    BC068046 mRNA. Translation: AAH68046.1 .
    CCDSi CCDS12475.1.
    PIRi B53814.
    T00703.
    RefSeqi NP_653218.1. NM_144617.2.
    UniGenei Hs.534538.
    Hs.744178.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4JUS X-ray 2.50 A/B/C/D/E/F/G/H 57-160 [» ]
    4JUT X-ray 2.20 A/B/C/D/E/F/G/H 57-160 [» ]
    ProteinModelPortali O14558.
    SMRi O14558. Positions 5-154.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 125988. 3 interactions.
    IntActi O14558. 3 interactions.
    MINTi MINT-7002024.
    STRINGi 9606.ENSP00000004982.

    PTM databases

    PhosphoSitei O14558.

    2D gel databases

    REPRODUCTION-2DPAGE O14558.
    UCD-2DPAGE O14558.

    Proteomic databases

    PaxDbi O14558.
    PRIDEi O14558.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000004982 ; ENSP00000004982 ; ENSG00000004776 .
    ENST00000592984 ; ENSP00000468057 ; ENSG00000004776 .
    GeneIDi 126393.
    KEGGi hsa:126393.
    UCSCi uc002obn.2. human.

    Organism-specific databases

    CTDi 126393.
    GeneCardsi GC19M036245.
    HGNCi HGNC:26511. HSPB6.
    HPAi CAB001974.
    HPA044153.
    MIMi 610695. gene.
    neXtProti NX_O14558.
    PharmGKBi PA134983584.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG236548.
    HOGENOMi HOG000233954.
    HOVERGENi HBG054766.
    InParanoidi O14558.
    KOi K09545.
    OMAi FIAREFH.
    OrthoDBi EOG7WHHBK.
    PhylomeDBi O14558.

    Enzyme and pathway databases

    SignaLinki O14558.

    Miscellaneous databases

    GeneWikii HSPB6.
    GenomeRNAii 126393.
    NextBioi 81816.
    PROi O14558.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O14558.
    Bgeei O14558.
    CleanExi HS_HSPB6.
    Genevestigatori O14558.

    Family and domain databases

    Gene3Di 2.60.40.790. 1 hit.
    InterProi IPR002068. a-crystallin/Hsp20_dom.
    IPR001436. Alpha-crystallin/HSP.
    IPR003090. Alpha-crystallin_N.
    IPR008978. HSP20-like_chaperone.
    [Graphical view ]
    Pfami PF00525. Crystallin. 1 hit.
    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. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Skeletal muscle.
    2. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Skin.
    4. "Purification and characterization of a 20-kDa protein that is highly homologous to alpha B crystallin."
      Kato K., Goto S., Inaguma Y., Hasegawa K., Morishita R., Asano T.
      J. Biol. Chem. 269:15302-15309(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-160, CHARACTERIZATION.
      Tissue: Muscle.
    5. "HSPB7 is a SC35 speckle resident small heat shock protein."
      Vos M.J., Kanon B., Kampinga H.H.
      Biochim. Biophys. Acta 1793:1343-1353(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiHSPB6_HUMAN
    AccessioniPrimary (citable) accession number: O14558
    Secondary accession number(s): O14551, Q6NVI3, Q96MG9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: August 2, 2002
    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 programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3