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P04792

- HSPB1_HUMAN

UniProt

P04792 - HSPB1_HUMAN

Protein

Heat shock protein beta-1

Gene

HSPB1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 181 (01 Oct 2014)
      Sequence version 2 (26 Sep 2001)
      Previous versions | rss
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    Functioni

    Involved in stress resistance and actin organization.

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: IntAct
    4. protein kinase binding Source: UniProtKB
    5. protein kinase C binding Source: BHF-UCL
    6. protein kinase C inhibitor activity Source: BHF-UCL
    7. ubiquitin binding Source: BHF-UCL

    GO - Biological processi

    1. cell death Source: UniProtKB-KW
    2. cellular component movement Source: UniProtKB
    3. cellular response to vascular endothelial growth factor stimulus Source: BHF-UCL
    4. gene expression Source: Reactome
    5. intracellular signal transduction Source: BHF-UCL
    6. mRNA metabolic process Source: Reactome
    7. negative regulation of apoptotic process Source: UniProtKB
    8. negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway Source: BHF-UCL
    9. negative regulation of protein kinase activity Source: BHF-UCL
    10. negative regulation of protein serine/threonine kinase activity Source: GOC
    11. positive regulation of angiogenesis Source: BHF-UCL
    12. positive regulation of blood vessel endothelial cell migration Source: BHF-UCL
    13. positive regulation of endothelial cell chemotaxis Source: BHF-UCL
    14. positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway Source: BHF-UCL
    15. positive regulation of interleukin-1 beta production Source: BHF-UCL
    16. positive regulation of tumor necrosis factor biosynthetic process Source: BHF-UCL
    17. regulation of I-kappaB kinase/NF-kappaB signaling Source: BHF-UCL
    18. regulation of translational initiation Source: ProtInc
    19. response to unfolded protein Source: UniProtKB
    20. response to virus Source: UniProtKB
    21. retina homeostasis Source: UniProt
    22. RNA metabolic process Source: Reactome

    Keywords - Molecular functioni

    Chaperone

    Keywords - Biological processi

    Stress response

    Enzyme and pathway databases

    ReactomeiREACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Heat shock protein beta-1
    Short name:
    HspB1
    Alternative name(s):
    28 kDa heat shock protein
    Estrogen-regulated 24 kDa protein
    Heat shock 27 kDa protein
    Short name:
    HSP 27
    Stress-responsive protein 27
    Short name:
    SRP27
    Gene namesi
    Name:HSPB1
    Synonyms:HSP27, HSP28
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:5246. HSPB1.

    Subcellular locationi

    Cytoplasm. Nucleus. Cytoplasmcytoskeletonspindle
    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.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytoskeleton Source: UniProtKB
    3. cytosol Source: Reactome
    4. extracellular space Source: UniProt
    5. extracellular vesicular exosome Source: UniProt
    6. nucleus Source: UniProtKB
    7. plasma membrane Source: Ensembl
    8. proteasome complex Source: BHF-UCL
    9. spindle Source: UniProtKB-SubCell
    10. Z disc Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Charcot-Marie-Tooth disease 2F (CMT2F) [MIM:606595]: A dominant axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. Nerve conduction velocities are normal or slightly reduced. Onset of Charcot-Marie-Tooth disease type 2F is between 15 and 25 years with muscle weakness and atrophy usually beginning in feet and legs (peroneal distribution). Upper limb involvement occurs later.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti135 – 1351S → F in CMT2F and HMN2B. 1 Publication
    VAR_018507
    Natural varianti136 – 1361R → W in CMT2F. 1 Publication
    VAR_018508
    Natural varianti164 – 1641T → A in CMT2F. 1 Publication
    VAR_067085
    Neuronopathy, distal hereditary motor, 2B (HMN2B) [MIM:608634]: A neuromuscular disorder. Distal hereditary motor neuronopathies constitute a heterogeneous group of neuromuscular disorders caused by selective degeneration of motor neurons in the anterior horn of the spinal cord, without sensory deficit in the posterior horn. The overall clinical picture consists of a classical distal muscular atrophy syndrome in the legs without clinical sensory loss. The disease starts with weakness and wasting of distal muscles of the anterior tibial and peroneal compartments of the legs. Later on, weakness and atrophy may expand to the proximal muscles of the lower limbs and/or to the distal upper limbs.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti127 – 1271R → W in HMN2B. 1 Publication
    VAR_018506
    Natural varianti135 – 1351S → F in CMT2F and HMN2B. 1 Publication
    VAR_018507
    Natural varianti151 – 1511T → I in HMN2B. 1 Publication
    VAR_018509
    Natural varianti182 – 1821P → L in HMN2B. 1 Publication
    VAR_018510

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi15 – 151S → D: Mimicks phosphorylation state, leading to dreased ability to act as molecular chaperones; when associated with D-78 and D-82. 1 Publication
    Mutagenesisi78 – 781S → D: Mimicks phosphorylation state, leading to dreased ability to act as molecular chaperones; when associated with D-15 and D-82. 1 Publication
    Mutagenesisi82 – 821S → D: Mimicks phosphorylation state, leading to dreased ability to act as molecular chaperones; when associated with D-15 and D-78. 1 Publication

    Keywords - Diseasei

    Charcot-Marie-Tooth disease, Disease mutation, Neurodegeneration, Neuropathy

    Organism-specific databases

    MIMi606595. phenotype.
    608634. phenotype.
    Orphaneti99940. Autosomal dominant Charcot-Marie-Tooth disease type 2F.
    139525. Distal hereditary motor neuropathy type 2.
    PharmGKBiPA29511.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 205205Heat shock protein beta-1PRO_0000125927Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei15 – 151Phosphoserine; by MAPKAPK2 and MAPKAPK37 Publications
    Modified residuei26 – 261PhosphoserineBy similarity
    Modified residuei65 – 651Phosphoserine2 Publications
    Modified residuei78 – 781Phosphoserine; by MAPKAPK2, MAPKAPK3 and MAPKAPK57 Publications
    Modified residuei82 – 821Phosphoserine; by MAPKAPK2, MAPKAPK3 and MAPKAPK511 Publications
    Modified residuei83 – 831Phosphoserine1 Publication
    Modified residuei86 – 861PhosphoserineBy similarity
    Modified residuei123 – 1231N6-acetyllysine1 Publication
    Modified residuei199 – 1991Phosphoserine3 Publications

    Post-translational modificationi

    Phosphorylated in MCF-7 cells on exposure to protein kinase C activators and heat shock.
    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.

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP04792.
    PaxDbiP04792.
    PeptideAtlasiP04792.
    PRIDEiP04792.

    2D gel databases

    DOSAC-COBS-2DPAGEP04792.
    OGPiP04792.
    REPRODUCTION-2DPAGEIPI00025512.
    P04792.
    SWISS-2DPAGEP04792.
    UCD-2DPAGEP04792.

    PTM databases

    PhosphoSiteiP04792.

    Expressioni

    Tissue specificityi

    Detected in all tissues tested: skeletal muscle, heart, aorta, large intestine, small intestine, stomach, esophagus, bladder, adrenal gland, thyroid, pancreas, testis, adipose tissue, kidney, liver, spleen, cerebral cortex, blood serum and cerebrospinal fluid. Highest levels are found in the heart and in tissues composed of striated and smooth muscle.1 Publication

    Inductioni

    Expressed in response to environmental stresses such as heat shock, or estrogen stimulation in MCF-7 cells. Up-regulated in response to enterovirus 71 (EV71) infection (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiP04792.
    BgeeiP04792.
    CleanExiHS_HSPB1.
    GenevestigatoriP04792.

    Organism-specific databases

    HPAiCAB004439.
    CAB047330.
    CAB047331.
    CAB047332.
    HPA000497.

    Interactioni

    Subunit structurei

    Interacts with TGFB1I1 By similarity. Associates with alpha- and beta-tubulin, microtubules and CRYAB. Interacts with HSPB8 and HSPBAP1.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-352682,EBI-352682
    BAG3O958172EBI-352682,EBI-747185
    CRYABP025112EBI-352682,EBI-739060
    DAXXQ9UER74EBI-352682,EBI-77321
    EFTUD2Q150292EBI-352682,EBI-357897
    EGFRP005333EBI-352682,EBI-297353
    G6PDP114132EBI-352682,EBI-4289891
    HSPB8Q9UJY13EBI-352682,EBI-739074
    MAPKAPK2P491373EBI-352682,EBI-993299
    MAPKAPK3Q166443EBI-352682,EBI-1384657
    MAPKAPK5Q8IW412EBI-352682,EBI-1201460
    MMEP084734EBI-352682,EBI-353759
    TP53P046373EBI-352682,EBI-366083
    YWHAZP631042EBI-352682,EBI-347088

    Protein-protein interaction databases

    BioGridi109547. 102 interactions.
    DIPiDIP-412N.
    IntActiP04792. 66 interactions.
    MINTiMINT-1368692.

    Structurei

    Secondary structure

    1
    205
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi86 – 883
    Beta strandi94 – 1007
    Turni102 – 1043
    Beta strandi107 – 1148
    Beta strandi117 – 1248
    Beta strandi136 – 1438
    Helixi150 – 1523
    Beta strandi154 – 1574
    Beta strandi161 – 1688

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3Q9PX-ray2.00A90-171[»]
    3Q9QX-ray2.20A/B90-171[»]
    4MJHX-ray2.60A/C84-176[»]
    B/D179-186[»]
    ProteinModelPortaliP04792.
    SMRiP04792. Positions 18-188.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni70 – 205136Interaction with TGFB1I1By similarityAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiNOG307785.
    HOVERGENiHBG054766.
    InParanoidiP04792.
    KOiK04455.
    OMAiDQSFGMP.
    OrthoDBiEOG7WHHBK.
    PhylomeDBiP04792.
    TreeFamiTF105049.

    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.

    P04792-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTERRVPFSL LRGPSWDPFR DWYPHSRLFD QAFGLPRLPE EWSQWLGGSS    50
    WPGYVRPLPP AAIESPAVAA PAYSRALSRQ LSSGVSEIRH TADRWRVSLD 100
    VNHFAPDELT VKTKDGVVEI TGKHEERQDE HGYISRCFTR KYTLPPGVDP 150
    TQVSSSLSPE GTLTVEAPMP KLATQSNEIT IPVTFESRAQ LGGPEAAKSD 200
    ETAAK 205
    Length:205
    Mass (Da):22,783
    Last modified:September 26, 2001 - v2
    Checksum:i1B4DC44A6F6606D5
    GO

    Sequence cautioni

    The sequence AAA62175.1 differs from that shown. Reason: Frameshift at position 194.
    The sequence AAB20722.1 differs from that shown. Reason: Frameshift at position 194.
    The sequence CAA34498.1 differs from that shown. Reason: Frameshift at position 194.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti10 – 101L → I AA sequence (PubMed:2295696)Curated
    Sequence conflicti109 – 1091L → R in AAH12292. (PubMed:15489334)Curated
    Sequence conflicti121 – 1211T → S in AAH12292. (PubMed:15489334)Curated
    Sequence conflicti127 – 1271R → L in AAH12292. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti127 – 1271R → W in HMN2B. 1 Publication
    VAR_018506
    Natural varianti135 – 1351S → F in CMT2F and HMN2B. 1 Publication
    VAR_018507
    Natural varianti136 – 1361R → W in CMT2F. 1 Publication
    VAR_018508
    Natural varianti151 – 1511T → I in HMN2B. 1 Publication
    VAR_018509
    Natural varianti164 – 1641T → A in CMT2F. 1 Publication
    VAR_067085
    Natural varianti182 – 1821P → L in HMN2B. 1 Publication
    VAR_018510

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L39370 Genomic DNA. Translation: AAA62175.1. Frameshift.
    X54079 mRNA. Translation: CAA38016.1.
    Z23090 mRNA. Translation: CAA80636.1.
    AB020027 mRNA. Translation: BAB17232.1.
    U90906 mRNA. Translation: AAB51056.1.
    CR407614 mRNA. Translation: CAG28542.1.
    CR536489 mRNA. Translation: CAG38728.1.
    BT019888 mRNA. Translation: AAV38691.1.
    AK311894 mRNA. Translation: BAG34835.1.
    DQ379985 Genomic DNA. Translation: ABC88475.1.
    AC006388 Genomic DNA. No translation available.
    CH471220 Genomic DNA. Translation: EAW71803.1.
    BC000510 mRNA. Translation: AAH00510.1.
    BC012292 mRNA. Translation: AAH12292.1.
    BC012768 mRNA. Translation: AAH12768.1.
    BC014920 mRNA. Translation: AAH14920.1.
    BC073768 mRNA. Translation: AAH73768.1.
    X16477 mRNA. Translation: CAA34498.1. Frameshift.
    S74571 mRNA. Translation: AAB20722.1. Frameshift.
    CCDSiCCDS5583.1.
    PIRiS12102. HHHU27.
    RefSeqiNP_001531.1. NM_001540.3.
    UniGeneiHs.520973.

    Genome annotation databases

    EnsembliENST00000248553; ENSP00000248553; ENSG00000106211.
    GeneIDi3315.
    KEGGihsa:3315.
    UCSCiuc003uew.3. human.

    Polymorphism databases

    DMDMi19855073.

    Cross-referencesi

    Web resourcesi

    Inherited peripheral neuropathies mutation db
    NIEHS SNPs
    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L39370 Genomic DNA. Translation: AAA62175.1 . Frameshift.
    X54079 mRNA. Translation: CAA38016.1 .
    Z23090 mRNA. Translation: CAA80636.1 .
    AB020027 mRNA. Translation: BAB17232.1 .
    U90906 mRNA. Translation: AAB51056.1 .
    CR407614 mRNA. Translation: CAG28542.1 .
    CR536489 mRNA. Translation: CAG38728.1 .
    BT019888 mRNA. Translation: AAV38691.1 .
    AK311894 mRNA. Translation: BAG34835.1 .
    DQ379985 Genomic DNA. Translation: ABC88475.1 .
    AC006388 Genomic DNA. No translation available.
    CH471220 Genomic DNA. Translation: EAW71803.1 .
    BC000510 mRNA. Translation: AAH00510.1 .
    BC012292 mRNA. Translation: AAH12292.1 .
    BC012768 mRNA. Translation: AAH12768.1 .
    BC014920 mRNA. Translation: AAH14920.1 .
    BC073768 mRNA. Translation: AAH73768.1 .
    X16477 mRNA. Translation: CAA34498.1 . Frameshift.
    S74571 mRNA. Translation: AAB20722.1 . Frameshift.
    CCDSi CCDS5583.1.
    PIRi S12102. HHHU27.
    RefSeqi NP_001531.1. NM_001540.3.
    UniGenei Hs.520973.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3Q9P X-ray 2.00 A 90-171 [» ]
    3Q9Q X-ray 2.20 A/B 90-171 [» ]
    4MJH X-ray 2.60 A/C 84-176 [» ]
    B/D 179-186 [» ]
    ProteinModelPortali P04792.
    SMRi P04792. Positions 18-188.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109547. 102 interactions.
    DIPi DIP-412N.
    IntActi P04792. 66 interactions.
    MINTi MINT-1368692.

    Chemistry

    BindingDBi P04792.
    ChEMBLi CHEMBL5976.

    PTM databases

    PhosphoSitei P04792.

    Polymorphism databases

    DMDMi 19855073.

    2D gel databases

    DOSAC-COBS-2DPAGE P04792.
    OGPi P04792.
    REPRODUCTION-2DPAGE IPI00025512.
    P04792.
    SWISS-2DPAGE P04792.
    UCD-2DPAGE P04792.

    Proteomic databases

    MaxQBi P04792.
    PaxDbi P04792.
    PeptideAtlasi P04792.
    PRIDEi P04792.

    Protocols and materials databases

    DNASUi 3315.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000248553 ; ENSP00000248553 ; ENSG00000106211 .
    GeneIDi 3315.
    KEGGi hsa:3315.
    UCSCi uc003uew.3. human.

    Organism-specific databases

    CTDi 3315.
    GeneCardsi GC07P075931.
    GeneReviewsi HSPB1.
    HGNCi HGNC:5246. HSPB1.
    HPAi CAB004439.
    CAB047330.
    CAB047331.
    CAB047332.
    HPA000497.
    MIMi 602195. gene.
    606595. phenotype.
    608634. phenotype.
    neXtProti NX_P04792.
    Orphaneti 99940. Autosomal dominant Charcot-Marie-Tooth disease type 2F.
    139525. Distal hereditary motor neuropathy type 2.
    PharmGKBi PA29511.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG307785.
    HOVERGENi HBG054766.
    InParanoidi P04792.
    KOi K04455.
    OMAi DQSFGMP.
    OrthoDBi EOG7WHHBK.
    PhylomeDBi P04792.
    TreeFami TF105049.

    Enzyme and pathway databases

    Reactomei REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.

    Miscellaneous databases

    ChiTaRSi HSPB1. human.
    GeneWikii Hsp27.
    GenomeRNAii 3315.
    NextBioi 13148.
    PROi P04792.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P04792.
    Bgeei P04792.
    CleanExi HS_HSPB1.
    Genevestigatori P04792.

    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 and organization of genes encoding the human 27 kDa heat shock protein."
      Hickey E., Brandon S.E., Potter R., Stein G., Stein J., Weber L.A.
      Nucleic Acids Res. 14:4127-4145(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "cDNA sequence of a human heat shock protein HSP27."
      Carper S.W., Rocheleau T.A., Storm F.K.
      Nucleic Acids Res. 18:6457-6457(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Lung.
    3. "Small heat shock protein 27 (HSP27) associates with tubulin/microtubules in HeLa cells."
      Hino M., Kurogi K., Okubo M.-A., Murata-Hori M., Hosoya H.
      Biochem. Biophys. Res. Commun. 271:164-169(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, SUBUNIT.
      Tissue: Cervix carcinoma.
    4. "Identification of a new cDNA sequence from human breast carcinoma cells encoding the 28kDa heat shock protein."
      Briolay J., Chareyron P., Mehlen P., Arrigo A.
      Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Mammary carcinoma.
    5. "Large-scale concatenation cDNA sequencing."
      Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W., Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.
      Genome Res. 7:353-358(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    6. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    7. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    8. "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.
    9. NIEHS SNPs program
      Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    10. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    11. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    12. "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: Lung, Ovary, Pancreas, Skin and Uterus.
    13. "Identification of two related markers for common acute lymphoblastic leukemia as heat shock proteins."
      Strahler J.R., Kuick R., Eckerskorn C., Lottspeich F., Richardson B.C., Fox D.A., Stoolman L.M., Hanson C.A., Nichols D., Tueche H.J., Hanash S.M.
      J. Clin. Invest. 85:200-207(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 5-12; 97-112; 141-154 AND 172-188.
    14. Bienvenut W.V., Waridel P., Quadroni M.
      Submitted (MAR-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 6-37; 57-75; 80-89; 97-127 AND 141-188, PHOSPHORYLATION AT SER-82, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryonic kidney.
    15. "The 28-kDa protein whose phosphorylation is induced by protein kinase C activators in MCF-7 cells belongs to the family of low molecular mass heat shock proteins and is the estrogen-regulated 24-kDa protein."
      Faucher C., Capdevielle J., Canal I., Ferrara P., Mazarguil H., McGuire W.L., Darbon J.-M.
      J. Biol. Chem. 268:15168-15173(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 13-20; 38-46; 97-110; 141-154 AND 172-186, PHOSPHORYLATION.
      Tissue: Mammary carcinoma.
    16. "Copurification of small heat shock protein with alpha B crystallin from human skeletal muscle."
      Kato K., Shinohara H., Goto S., Inaguma Y., Morishita R., Asano T.
      J. Biol. Chem. 267:7718-7725(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 21-59; 93-98; 129-134 AND 178-193, ASSOCIATION WITH CRYAB, TISSUE SPECIFICITY.
      Tissue: Pectoralis muscle.
    17. "Human HSP27 is phosphorylated at serines 78 and 82 by heat shock and mitogen-activated kinases that recognize the same amino acid motif as S6 kinase II."
      Landry J., Lambert H., Zhou M., Lavoie J.N., Hickey E., Weber L.A., Anderson C.W.
      J. Biol. Chem. 267:794-803(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 76-89, PHOSPHORYLATION AT SER-78 AND SER-82.
    18. "Induction of the estrogen-regulated '24K' protein by heat shock."
      Fuqua S.A.W., Blum-Salingaros M., McGuire W.L.
      Cancer Res. 49:4126-4129(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 109-205.
      Tissue: Mammary carcinoma.
    19. "The 29-kDa proteins phosphorylated in thrombin-activated human platelets are forms of the estrogen receptor-related 27-kDa heat shock protein."
      Mendelsohn M.E., Zhu Y., O'Neill S.
      Proc. Natl. Acad. Sci. U.S.A. 88:11212-11216(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 122-205.
    20. "Identification of MAPKAP kinase 2 as a major enzyme responsible for the phosphorylation of the small mammalian heat shock proteins."
      Stokoe D., Engel K., Campbell D.G., Cohen P., Gaestel M.
      FEBS Lett. 313:307-313(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-15; SER-78 AND SER-82 BY MAPKAPK2.
    21. "Small heat shock proteins are molecular chaperones."
      Jakob U., Gaestel M., Engel K., Buchner J.
      J. Biol. Chem. 268:1517-1520(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY MAPKAPK2.
    22. "A comparison of the substrate specificity of MAPKAP kinase-2 and MAPKAP kinase-3 and their activation by cytokines and cellular stress."
      Clifton A.D., Young P.R., Cohen P.
      FEBS Lett. 392:209-214(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-15; SER-78 AND SER-82.
    23. "Regulation of Hsp27 oligomerization, chaperone function, and protective activity against oxidative stress/tumor necrosis factor alpha by phosphorylation."
      Rogalla T., Ehrnsperger M., Preville X., Kotlyarov A., Lutsch G., Ducasse C., Paul C., Wieske M., Arrigo A.P., Buchner J., Gaestel M.
      J. Biol. Chem. 274:18947-18956(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-15; SER-78 AND SER-82, MUTAGENESIS OF SER-15; SER-78 AND SER-82.
    24. "Identification and characterization of a novel protein from Sertoli cells, PASS1, that associates with mammalian small stress protein hsp27."
      Liu C., Gilmont R.R., Benndorf R., Welsh M.J.
      J. Biol. Chem. 275:18724-18731(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HSPBAP1.
    25. "Heat shock protein 27 is associated with freedom from graft vasculopathy after human cardiac transplantation."
      De Souza A.I., Wait R., Mitchell A.G., Banner N.R., Dunn M.J., Rose M.L.
      Circ. Res. 97:192-198(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-78 AND SER-82, IDENTIFICATION BY MASS SPECTROMETRY.
    26. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-65, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    27. "Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal differential cellular gene expression in response to enterovirus 71 infection."
      Leong W.F., Chow V.T.
      Cell. Microbiol. 8:565-580(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION, IDENTIFICATION BY MASS SPECTROMETRY.
    28. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82 AND SER-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    29. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
      Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
      J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    30. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    31. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-199, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    32. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82 AND SER-199, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    33. "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.
    34. "PKA-induced F-actin rearrangement requires phosphorylation of Hsp27 by the MAPKAP kinase MK5."
      Kostenko S., Johannessen M., Moens U.
      Cell. Signal. 21:712-718(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-78 AND SER-82.
    35. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    36. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-123, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    37. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-65; SER-78; SER-82 AND SER-199, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    38. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    39. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    40. Cited for: VARIANTS CMT2F PHE-135 AND TRP-136, VARIANTS HMN2B TRP-127; PHE-135; ILE-151 AND LEU-182.
    41. "The mutational spectrum in a cohort of Charcot-Marie-Tooth disease type 2 among the Han Chinese in Taiwan."
      Lin K.P., Soong B.W., Yang C.C., Huang L.W., Chang M.H., Lee I.H., Antonellis A., Lee Y.C.
      PLoS ONE 6:E29393-E29393(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CMT2F ALA-164.

    Entry informationi

    Entry nameiHSPB1_HUMAN
    AccessioniPrimary (citable) accession number: P04792
    Secondary accession number(s): B2R4N8
    , Q6FI47, Q96C20, Q96EI7, Q9UC31, Q9UC34, Q9UC35, Q9UC36
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: September 26, 2001
    Last modified: October 1, 2014
    This is version 181 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 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3