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P07900

- HS90A_HUMAN

UniProt

P07900 - HS90A_HUMAN

Protein

Heat shock protein HSP 90-alpha

Gene

HSP90AA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 195 (01 Oct 2014)
      Sequence version 5 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion by monocytes.4 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei51 – 511ATP
    Binding sitei93 – 931ATP
    Binding sitei112 – 1121ATPBy similarity
    Binding sitei138 – 1381ATP; via amide nitrogen
    Binding sitei400 – 4001ATPBy similarity

    GO - Molecular functioni

    1. ATPase activity Source: UniProtKB
    2. ATP binding Source: UniProtKB
    3. identical protein binding Source: IntAct
    4. MHC class II protein complex binding Source: UniProt
    5. nitric-oxide synthase regulator activity Source: UniProtKB
    6. nucleotide binding Source: UniProtKB
    7. poly(A) RNA binding Source: UniProtKB
    8. protein binding Source: UniProtKB
    9. protein homodimerization activity Source: UniProtKB
    10. TPR domain binding Source: UniProtKB

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. axon guidance Source: Reactome
    3. chaperone-mediated protein complex assembly Source: BHF-UCL
    4. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
    5. G2/M transition of mitotic cell cycle Source: Reactome
    6. innate immune response Source: Reactome
    7. mitochondrial transport Source: UniProtKB
    8. mitotic cell cycle Source: Reactome
    9. nitric oxide metabolic process Source: Reactome
    10. positive regulation of nitric oxide biosynthetic process Source: UniProtKB
    11. protein import into mitochondrial outer membrane Source: BHF-UCL
    12. protein refolding Source: UniProtKB
    13. regulation of nitric-oxide synthase activity Source: Reactome
    14. response to unfolded protein Source: UniProtKB
    15. signal transduction Source: UniProtKB
    16. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Chaperone

    Keywords - Biological processi

    Stress response

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_111176. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
    REACT_115755. Signaling by ERBB2.
    REACT_115852. Signaling by constitutively active EGFR.
    REACT_12477. eNOS activation.
    REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
    REACT_15364. Loss of Nlp from mitotic centrosomes.
    REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
    REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
    REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
    REACT_163813. Scavenging by Class F Receptors.
    REACT_19236. Sema3A PAK dependent Axon repulsion.
    REACT_200624. Attenuation phase.
    REACT_200744. HSF1 activation.
    REACT_200775. HSF1-dependent transactivation.
    REACT_9434. vRNP Assembly.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Heat shock protein HSP 90-alpha
    Alternative name(s):
    Heat shock 86 kDa
    Short name:
    HSP 86
    Short name:
    HSP86
    Lipopolysaccharide-associated protein 2
    Short name:
    LAP-2
    Short name:
    LPS-associated protein 2
    Renal carcinoma antigen NY-REN-38
    Gene namesi
    Name:HSP90AA1
    Synonyms:HSP90A, HSPC1, HSPCA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:5253. HSP90AA1.

    Subcellular locationi

    Cytoplasm. Melanosome. Cell membrane
    Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: UniProtKB
    3. endocytic vesicle lumen Source: Reactome
    4. extracellular region Source: Reactome
    5. extracellular vesicular exosome Source: UniProt
    6. melanosome Source: UniProtKB-SubCell
    7. membrane Source: UniProtKB
    8. mitochondrion Source: GOC
    9. nucleus Source: UniProt
    10. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi97 – 971G → D: Abolishes ATPase activity. 1 Publication
    Mutagenesisi598 – 5981C → A, N or D: Reduces ATPase activity and client protein activation. 2 Publications
    Mutagenesisi598 – 5981C → S: Loss of S-nitrosylation. 2 Publications

    Organism-specific databases

    PharmGKBiPA29519.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 732731Heat shock protein HSP 90-alphaPRO_0000062911Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei5 – 51Phosphothreonine; by PRKDC2 Publications
    Modified residuei7 – 71Phosphothreonine; by PRKDC2 Publications
    Modified residuei58 – 581N6-acetyllysineBy similarity
    Modified residuei84 – 841N6-acetyllysineBy similarity
    Modified residuei231 – 2311Phosphoserine3 Publications
    Modified residuei252 – 2521Phosphoserine3 Publications
    Modified residuei263 – 2631Phosphoserine8 Publications
    Modified residuei313 – 3131PhosphotyrosineBy similarity
    Modified residuei399 – 3991Phosphoserine1 Publication
    Modified residuei443 – 4431N6-acetyllysine1 Publication
    Modified residuei458 – 4581N6-acetyllysine1 Publication
    Modified residuei489 – 4891N6-acetyllysine1 Publication
    Modified residuei492 – 4921PhosphotyrosineBy similarity
    Modified residuei585 – 5851N6-acetyllysine1 Publication
    Modified residuei598 – 5981S-nitrosocysteine1 Publication

    Post-translational modificationi

    ISGylated.1 Publication
    S-nitrosylated; negatively regulates the ATPase activity and the activation of eNOS by HSP90AA1.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein, S-nitrosylation, Ubl conjugation

    Proteomic databases

    MaxQBiP07900.
    PRIDEiP07900.

    2D gel databases

    OGPiP07900.
    REPRODUCTION-2DPAGEIPI00784295.

    PTM databases

    PhosphoSiteiP07900.

    Miscellaneous databases

    PMAP-CutDBP07900.

    Expressioni

    Gene expression databases

    ArrayExpressiP07900.
    BgeeiP07900.
    CleanExiHS_HSP90AA1.
    GenevestigatoriP07900.

    Organism-specific databases

    HPAiCAB002058.
    HPA047290.

    Interactioni

    Subunit structurei

    Homodimer. Identified in NR3C1/GCR steroid receptor-chaperone complexes formed at least by NR3C1, HSP90AA1 and a variety of proteins containing TPR repeats such as FKBP4, FKBP5, PPID, PPP5C STIP1. Interacts with AHSA1, FNIP1, HSF1, SMYD3 and TOM34. Interacts with TERT; the interaction, together with PTGES3, is required for correct assembly and stabilization of the TERT holoenzyme complex. Interacts with CHORDC1 and DNAJC7. Interacts with STUB1 and UBE2N; may couple the chaperone and ubiquitination systems. Interacts (via TPR repeat-binding motif) with PPP5C (via TPR repeats); the interaction is direct and activates PPP5C phosphatase activity. Following LPS binding, may form a complex with CXCR4, GDF5 and HSPA8.17 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself5EBI-296047,EBI-296047
    AHSA1O954334EBI-296047,EBI-448610
    CCDC117Q8IWD45EBI-296047,EBI-3387963
    CDC37Q1654313EBI-296047,EBI-295634
    CDC37L1Q7L3B62EBI-296047,EBI-2841876
    CDK9P507502EBI-296047,EBI-1383449
    CERS2Q96G232EBI-296047,EBI-1057080
    CHORDC1Q9UHD18EBI-296047,EBI-2550959
    CHUKO151113EBI-296047,EBI-81249
    EGFRP005333EBI-296047,EBI-297353
    ERBB2P046263EBI-296047,EBI-641062
    FKBP4Q027908EBI-296047,EBI-1047444
    FKBP8Q143187EBI-296047,EBI-724839
    HSP90AB1Q6PK502EBI-296047,EBI-9356629
    IKBKGQ9Y6K93EBI-296047,EBI-81279
    JUNP054122EBI-296047,EBI-852823
    MAP3K7O43318-25EBI-296047,EBI-358700
    PPIDP268824EBI-296047,EBI-6477155From a different organism.
    PPP5CP530418EBI-296047,EBI-716663
    PTGES3Q151856EBI-296047,EBI-1049387
    RPAP3Q9H6T33EBI-296047,EBI-356928
    RPS3AP612472EBI-296047,EBI-352378
    S100a1P354674EBI-296047,EBI-6477109From a different organism.
    STK11Q158312EBI-296047,EBI-306838
    STUB1Q9UNE79EBI-296047,EBI-357085

    Protein-protein interaction databases

    BioGridi109552. 740 interactions.
    DIPiDIP-27595N.
    IntActiP07900. 192 interactions.
    MINTiMINT-132070.
    STRINGi9606.ENSP00000335153.

    Structurei

    Secondary structure

    1
    732
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi18 – 214
    Helixi24 – 3512
    Helixi43 – 6321
    Helixi67 – 704
    Beta strandi78 – 836
    Turni84 – 874
    Beta strandi88 – 936
    Helixi100 – 1045
    Helixi106 – 1083
    Helixi111 – 12313
    Helixi128 – 1347
    Helixi137 – 1437
    Beta strandi145 – 1539
    Beta strandi155 – 1573
    Beta strandi159 – 1646
    Beta strandi169 – 1746
    Beta strandi181 – 19010
    Helixi192 – 1987
    Helixi200 – 21011
    Beta strandi212 – 2165
    Beta strandi218 – 2203
    Turni221 – 2244
    Beta strandi225 – 2273
    Helixi228 – 2303
    Helixi296 – 2983
    Helixi306 – 31712
    Beta strandi324 – 3318
    Beta strandi333 – 3353
    Beta strandi337 – 3437
    Beta strandi361 – 3655
    Beta strandi368 – 3725
    Helixi380 – 3823
    Beta strandi386 – 3927
    Helixi408 – 42720
    Helixi431 – 45121
    Helixi453 – 4553
    Helixi456 – 4605
    Beta strandi464 – 4674
    Turni468 – 4725
    Helixi477 – 4826
    Beta strandi490 – 4956
    Helixi499 – 5035
    Helixi506 – 5083
    Helixi509 – 5146
    Beta strandi518 – 5214
    Helixi525 – 5295
    Turni530 – 5323
    Beta strandi539 – 5435
    Helixi555 – 56713
    Helixi569 – 57810
    Helixi580 – 5823
    Beta strandi584 – 5885
    Beta strandi593 – 6019
    Beta strandi603 – 6053
    Helixi608 – 6136
    Beta strandi632 – 6365
    Helixi641 – 65212
    Helixi657 – 67317
    Helixi681 – 69414
    Beta strandi728 – 7303

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BYQX-ray1.50A9-236[»]
    1OSFX-ray1.75A9-223[»]
    1UY6X-ray1.90A2-236[»]
    1UY7X-ray1.90A2-236[»]
    1UY8X-ray1.98A2-236[»]
    1UY9X-ray2.00A2-236[»]
    1UYCX-ray2.00A2-236[»]
    1UYDX-ray2.20A2-236[»]
    1UYEX-ray2.00A2-236[»]
    1UYFX-ray2.00A2-236[»]
    1UYGX-ray2.00A2-236[»]
    1UYHX-ray2.20A2-236[»]
    1UYIX-ray2.20A2-236[»]
    1UYKX-ray2.20A2-236[»]
    1UYLX-ray1.40A2-236[»]
    1YC1X-ray1.70A9-236[»]
    1YC3X-ray2.12A9-236[»]
    1YC4X-ray1.81A9-236[»]
    1YERX-ray1.65A9-236[»]
    1YESX-ray2.20A9-236[»]
    1YETX-ray1.90A9-236[»]
    2BSMX-ray2.05A2-236[»]
    2BT0X-ray1.90A/B2-236[»]
    2BUGNMR-B-[»]
    2BYHX-ray1.90A11-236[»]
    2BYIX-ray1.60A11-236[»]
    2BZ5X-ray1.90A/B2-236[»]
    2C2LX-ray3.30E/F/G/H724-732[»]
    2CCSX-ray1.79A1-236[»]
    2CCTX-ray2.30A1-236[»]
    2CCUX-ray2.70A1-236[»]
    2CDDX-ray1.90A/B1-236[»]
    2FWYX-ray2.10A1-236[»]
    2FWZX-ray2.10A1-236[»]
    2H55X-ray2.00A1-236[»]
    2JJCX-ray1.95A9-223[»]
    2K5BNMR-A14-223[»]
    2QF6X-ray3.10A/B/C/D17-223[»]
    2QFOX-ray1.68A/B17-223[»]
    2QG0X-ray1.85A/B17-223[»]
    2QG2X-ray1.80A17-223[»]
    2UWDX-ray1.90A2-236[»]
    2VCIX-ray2.00A1-236[»]
    2VCJX-ray2.50A1-236[»]
    2WI1X-ray2.30A1-236[»]
    2WI2X-ray2.09A/B1-236[»]
    2WI3X-ray1.90A1-236[»]
    2WI4X-ray2.40A1-236[»]
    2WI5X-ray2.10A1-236[»]
    2WI6X-ray2.18A1-236[»]
    2WI7X-ray2.50A1-236[»]
    2XABX-ray1.90A/B9-236[»]
    2XDKX-ray1.97A9-236[»]
    2XDLX-ray1.98A9-236[»]
    2XDSX-ray1.97A9-236[»]
    2XDUX-ray1.74A14-224[»]
    2XDXX-ray2.42A9-236[»]
    2XHRX-ray2.20A9-236[»]
    2XHTX-ray2.27A9-236[»]
    2XHXX-ray2.80A9-236[»]
    2XJGX-ray2.25A9-236[»]
    2XJJX-ray1.90A/B9-236[»]
    2XJXX-ray1.66A9-236[»]
    2XK2X-ray1.95A9-236[»]
    2YE2X-ray1.90A9-236[»]
    2YE3X-ray1.95A9-236[»]
    2YE4X-ray2.30A9-236[»]
    2YE5X-ray1.73A9-236[»]
    2YE6X-ray2.56A9-236[»]
    2YE7X-ray2.20A9-236[»]
    2YE8X-ray2.30A9-236[»]
    2YE9X-ray2.20A9-236[»]
    2YEAX-ray1.73A9-236[»]
    2YEBX-ray2.40A9-236[»]
    2YECX-ray2.10A9-236[»]
    2YEDX-ray2.10A9-236[»]
    2YEEX-ray2.30A9-236[»]
    2YEFX-ray1.55A9-236[»]
    2YEGX-ray2.50A/B9-236[»]
    2YEHX-ray2.10A9-236[»]
    2YEIX-ray2.20A9-236[»]
    2YEJX-ray2.20A9-236[»]
    2YI0X-ray1.60A1-229[»]
    2YI5X-ray2.50A1-229[»]
    2YI6X-ray1.80A1-229[»]
    2YI7X-ray1.40A1-229[»]
    2YJWX-ray1.61A18-223[»]
    2YJXX-ray1.83A18-223[»]
    2YK2X-ray1.74A18-223[»]
    2YK9X-ray1.32A18-223[»]
    2YKBX-ray1.93A18-223[»]
    2YKCX-ray1.67A18-223[»]
    2YKEX-ray1.43A18-223[»]
    2YKIX-ray1.67A18-223[»]
    2YKJX-ray1.46A18-223[»]
    3B24X-ray1.70A/B9-236[»]
    3B25X-ray1.75A9-236[»]
    3B26X-ray2.10A/B9-236[»]
    3B27X-ray1.50A9-236[»]
    3B28X-ray1.35A/B9-236[»]
    3BM9X-ray1.60A14-236[»]
    3BMYX-ray1.60A14-236[»]
    3D0BX-ray1.74A1-232[»]
    3EKOX-ray1.55A/B9-225[»]
    3EKRX-ray2.00A/B9-225[»]
    3FT5X-ray1.90A9-236[»]
    3FT8X-ray2.00A9-236[»]
    3HEKX-ray1.95A/B9-225[»]
    3HHUX-ray1.59A/B1-224[»]
    3HYYX-ray1.90A9-236[»]
    3HYZX-ray2.30A/B9-236[»]
    3HZ1X-ray2.30A9-236[»]
    3HZ5X-ray1.90A9-236[»]
    3INWX-ray1.95A10-236[»]
    3INXX-ray1.75A10-236[»]
    3K97X-ray1.95A9-236[»]
    3K98X-ray2.40A/B9-225[»]
    3K99X-ray2.10A/B/C/D9-225[»]
    3MNRX-ray1.90P1-232[»]
    3O0IX-ray1.47A1-236[»]
    3OW6X-ray1.80A17-223[»]
    3OWBX-ray2.05A17-223[»]
    3OWDX-ray1.63A17-223[»]
    3Q6MX-ray3.00A/B/C293-732[»]
    3Q6NX-ray3.05A/B/C/D/E/F293-732[»]
    3QDDX-ray1.79A1-236[»]
    3QTFX-ray1.57A14-236[»]
    3R4MX-ray1.70A9-236[»]
    3R4NX-ray2.00A/B9-225[»]
    3R4OX-ray2.65A/B9-225[»]
    3R4PX-ray1.70A/B9-225[»]
    3R91X-ray1.58A14-236[»]
    3R92X-ray1.58A14-236[»]
    3RKZX-ray1.57A14-236[»]
    3RLPX-ray1.70A/B9-225[»]
    3RLQX-ray1.90A/B9-225[»]
    3RLRX-ray1.70A/B9-225[»]
    3T0HX-ray1.20A9-236[»]
    3T0ZX-ray2.19A9-236[»]
    3T10X-ray1.24A9-236[»]
    3T1KX-ray1.50A/B9-236[»]
    3T2SX-ray1.50A/B9-236[»]
    3TUHX-ray1.80A/B16-224[»]
    3VHAX-ray1.39A9-236[»]
    3VHCX-ray1.41A9-236[»]
    3VHDX-ray1.52A/B9-236[»]
    3WHAX-ray1.30A/B9-236[»]
    4AIFX-ray2.01D/E726-732[»]
    4AWOX-ray1.70A/B9-236[»]
    4AWPX-ray1.82A/B9-236[»]
    4AWQX-ray1.60A/B9-236[»]
    4B7PX-ray1.70A9-236[»]
    4BQJX-ray2.00A9-236[»]
    4CGUX-ray2.11C726-732[»]
    4CGVX-ray2.54E/F726-732[»]
    4CGWX-ray3.00C/D726-732[»]
    4EEHX-ray1.60A9-236[»]
    4EFTX-ray2.12A9-236[»]
    4EFUX-ray2.00A9-236[»]
    4EGHX-ray1.60A9-236[»]
    4EGIX-ray1.79A9-236[»]
    4EGKX-ray1.69A9-236[»]
    4FCPX-ray2.00A/B1-236[»]
    4FCQX-ray2.15A1-236[»]
    4FCRX-ray1.70A1-236[»]
    4HY6X-ray1.65A9-236[»]
    4JQLX-ray1.72A9-236[»]
    4L8ZX-ray1.70A9-236[»]
    4L90X-ray2.00A9-236[»]
    4L91X-ray1.75A9-236[»]
    4L93X-ray1.84A/B9-236[»]
    4L94X-ray1.65A9-236[»]
    4NH7X-ray2.00A/B9-236[»]
    4NH8X-ray1.65A9-236[»]
    4O05X-ray1.79A9-236[»]
    4O07X-ray1.86A9-236[»]
    4O09X-ray1.96A9-236[»]
    4O0BX-ray1.93A9-236[»]
    ProteinModelPortaliP07900.
    SMRiP07900. Positions 15-699.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07900.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni682 – 73251Required for homodimerizationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi728 – 7325TPR repeat-binding

    Domaini

    The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins like the co-chaperone STUB1.

    Sequence similaritiesi

    Belongs to the heat shock protein 90 family.Curated

    Phylogenomic databases

    HOVERGENiHBG007374.
    InParanoidiP07900.
    KOiK04079.
    OMAiMSHLTEF.
    OrthoDBiEOG780RM0.
    PhylomeDBiP07900.
    TreeFamiTF300686.

    Family and domain databases

    Gene3Di3.30.565.10. 2 hits.
    HAMAPiMF_00505. HSP90.
    InterProiIPR003594. HATPase_ATP-bd.
    IPR019805. Heat_shock_protein_90_CS.
    IPR001404. Hsp90_fam.
    IPR020575. Hsp90_N.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    [Graphical view]
    PANTHERiPTHR11528. PTHR11528. 1 hit.
    PfamiPF02518. HATPase_c. 1 hit.
    PF00183. HSP90. 1 hit.
    [Graphical view]
    PIRSFiPIRSF002583. Hsp90. 1 hit.
    PRINTSiPR00775. HEATSHOCK90.
    SMARTiSM00387. HATPase_c. 1 hit.
    [Graphical view]
    SUPFAMiSSF54211. SSF54211. 1 hit.
    SSF55874. SSF55874. 1 hit.
    PROSITEiPS00298. HSP90. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P07900-1) [UniParc]FASTAAdd to Basket

    Also known as: HSP90AA1-1, HSP90-alpha 2

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MPEETQTQDQ PMEEEEVETF AFQAEIAQLM SLIINTFYSN KEIFLRELIS    50
    NSSDALDKIR YESLTDPSKL DSGKELHINL IPNKQDRTLT IVDTGIGMTK 100
    ADLINNLGTI AKSGTKAFME ALQAGADISM IGQFGVGFYS AYLVAEKVTV 150
    ITKHNDDEQY AWESSAGGSF TVRTDTGEPM GRGTKVILHL KEDQTEYLEE 200
    RRIKEIVKKH SQFIGYPITL FVEKERDKEV SDDEAEEKED KEEEKEKEEK 250
    ESEDKPEIED VGSDEEEEKK DGDKKKKKKI KEKYIDQEEL NKTKPIWTRN 300
    PDDITNEEYG EFYKSLTNDW EDHLAVKHFS VEGQLEFRAL LFVPRRAPFD 350
    LFENRKKKNN IKLYVRRVFI MDNCEELIPE YLNFIRGVVD SEDLPLNISR 400
    EMLQQSKILK VIRKNLVKKC LELFTELAED KENYKKFYEQ FSKNIKLGIH 450
    EDSQNRKKLS ELLRYYTSAS GDEMVSLKDY CTRMKENQKH IYYITGETKD 500
    QVANSAFVER LRKHGLEVIY MIEPIDEYCV QQLKEFEGKT LVSVTKEGLE 550
    LPEDEEEKKK QEEKKTKFEN LCKIMKDILE KKVEKVVVSN RLVTSPCCIV 600
    TSTYGWTANM ERIMKAQALR DNSTMGYMAA KKHLEINPDH SIIETLRQKA 650
    EADKNDKSVK DLVILLYETA LLSSGFSLED PQTHANRIYR MIKLGLGIDE 700
    DDPTADDTSA AVTEEMPPLE GDDDTSRMEE VD 732
    Length:732
    Mass (Da):84,660
    Last modified:January 23, 2007 - v5
    Checksum:i969F65FCC0BC86FD
    GO
    Isoform 2 (identifier: P07900-2) [UniParc]FASTAAdd to Basket

    Also known as: HSP90AA1-2

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MPPCSGGDGS...QPFILLRLLM

    Show »
    Length:854
    Mass (Da):98,161
    Checksum:i404BD8CAD5E68DB0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti63 – 631S → T in CAA33259. (PubMed:2780322)Curated
    Sequence conflicti74 – 741K → R in CAI64495. (PubMed:16269234)Curated
    Sequence conflicti74 – 741K → R in BAG51711. (PubMed:14702039)Curated
    Sequence conflicti86 – 861D → G in CAI64495. (PubMed:16269234)Curated
    Sequence conflicti86 – 861D → G in BAG51711. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Isoform 2 (identifier: P07900-2)
    Natural varianti71 – 711M → L.
    Corresponds to variant rs8005905 [ dbSNP | Ensembl ].

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MPPCSGGDGSTPPGPSLRDR DCPAQSAEYPRDRLDPRPGS PSEASSPPFLRSRAPVNWYQ EKAQVFLWHLMVSGSTTLLC LWKQPFHVSAFPVTASLAFR QSQGAGQHLYKDLQPFILLR LLM in isoform 2. 2 PublicationsVSP_026604

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X15183 mRNA. Translation: CAA33259.1.
    M27024 Genomic DNA. Translation: AAA63194.1.
    AJ890082 mRNA. Translation: CAI64495.1.
    AJ890083 mRNA. Translation: CAI64496.1.
    DQ314871 Genomic DNA. Translation: ABC40730.1.
    AK056446 mRNA. Translation: BAG51711.1.
    AK291115 mRNA. Translation: BAF83804.1.
    AK291607 mRNA. Translation: BAF84296.1.
    AL133223 Genomic DNA. No translation available.
    CH471061 Genomic DNA. Translation: EAW81765.1.
    X07270 mRNA. Translation: CAA30255.1.
    M30626 Genomic DNA. Translation: AAA36023.1.
    BC000987 mRNA. Translation: AAH00987.1.
    BC121062 mRNA. Translation: AAI21063.1.
    D87666 mRNA. Translation: BAA13430.1.
    D87666 mRNA. Translation: BAA13431.1.
    CCDSiCCDS32160.1. [P07900-2]
    CCDS9967.1. [P07900-1]
    PIRiA32319. HHHU86.
    RefSeqiNP_001017963.2. NM_001017963.2. [P07900-2]
    NP_005339.3. NM_005348.3. [P07900-1]
    UniGeneiHs.525600.

    Genome annotation databases

    EnsembliENST00000216281; ENSP00000216281; ENSG00000080824. [P07900-1]
    ENST00000334701; ENSP00000335153; ENSG00000080824. [P07900-2]
    GeneIDi3320.
    KEGGihsa:3320.
    UCSCiuc001yku.4. human. [P07900-1]
    uc001ykv.4. human. [P07900-2]

    Polymorphism databases

    DMDMi92090606.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X15183 mRNA. Translation: CAA33259.1 .
    M27024 Genomic DNA. Translation: AAA63194.1 .
    AJ890082 mRNA. Translation: CAI64495.1 .
    AJ890083 mRNA. Translation: CAI64496.1 .
    DQ314871 Genomic DNA. Translation: ABC40730.1 .
    AK056446 mRNA. Translation: BAG51711.1 .
    AK291115 mRNA. Translation: BAF83804.1 .
    AK291607 mRNA. Translation: BAF84296.1 .
    AL133223 Genomic DNA. No translation available.
    CH471061 Genomic DNA. Translation: EAW81765.1 .
    X07270 mRNA. Translation: CAA30255.1 .
    M30626 Genomic DNA. Translation: AAA36023.1 .
    BC000987 mRNA. Translation: AAH00987.1 .
    BC121062 mRNA. Translation: AAI21063.1 .
    D87666 mRNA. Translation: BAA13430.1 .
    D87666 mRNA. Translation: BAA13431.1 .
    CCDSi CCDS32160.1. [P07900-2 ]
    CCDS9967.1. [P07900-1 ]
    PIRi A32319. HHHU86.
    RefSeqi NP_001017963.2. NM_001017963.2. [P07900-2 ]
    NP_005339.3. NM_005348.3. [P07900-1 ]
    UniGenei Hs.525600.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BYQ X-ray 1.50 A 9-236 [» ]
    1OSF X-ray 1.75 A 9-223 [» ]
    1UY6 X-ray 1.90 A 2-236 [» ]
    1UY7 X-ray 1.90 A 2-236 [» ]
    1UY8 X-ray 1.98 A 2-236 [» ]
    1UY9 X-ray 2.00 A 2-236 [» ]
    1UYC X-ray 2.00 A 2-236 [» ]
    1UYD X-ray 2.20 A 2-236 [» ]
    1UYE X-ray 2.00 A 2-236 [» ]
    1UYF X-ray 2.00 A 2-236 [» ]
    1UYG X-ray 2.00 A 2-236 [» ]
    1UYH X-ray 2.20 A 2-236 [» ]
    1UYI X-ray 2.20 A 2-236 [» ]
    1UYK X-ray 2.20 A 2-236 [» ]
    1UYL X-ray 1.40 A 2-236 [» ]
    1YC1 X-ray 1.70 A 9-236 [» ]
    1YC3 X-ray 2.12 A 9-236 [» ]
    1YC4 X-ray 1.81 A 9-236 [» ]
    1YER X-ray 1.65 A 9-236 [» ]
    1YES X-ray 2.20 A 9-236 [» ]
    1YET X-ray 1.90 A 9-236 [» ]
    2BSM X-ray 2.05 A 2-236 [» ]
    2BT0 X-ray 1.90 A/B 2-236 [» ]
    2BUG NMR - B - [» ]
    2BYH X-ray 1.90 A 11-236 [» ]
    2BYI X-ray 1.60 A 11-236 [» ]
    2BZ5 X-ray 1.90 A/B 2-236 [» ]
    2C2L X-ray 3.30 E/F/G/H 724-732 [» ]
    2CCS X-ray 1.79 A 1-236 [» ]
    2CCT X-ray 2.30 A 1-236 [» ]
    2CCU X-ray 2.70 A 1-236 [» ]
    2CDD X-ray 1.90 A/B 1-236 [» ]
    2FWY X-ray 2.10 A 1-236 [» ]
    2FWZ X-ray 2.10 A 1-236 [» ]
    2H55 X-ray 2.00 A 1-236 [» ]
    2JJC X-ray 1.95 A 9-223 [» ]
    2K5B NMR - A 14-223 [» ]
    2QF6 X-ray 3.10 A/B/C/D 17-223 [» ]
    2QFO X-ray 1.68 A/B 17-223 [» ]
    2QG0 X-ray 1.85 A/B 17-223 [» ]
    2QG2 X-ray 1.80 A 17-223 [» ]
    2UWD X-ray 1.90 A 2-236 [» ]
    2VCI X-ray 2.00 A 1-236 [» ]
    2VCJ X-ray 2.50 A 1-236 [» ]
    2WI1 X-ray 2.30 A 1-236 [» ]
    2WI2 X-ray 2.09 A/B 1-236 [» ]
    2WI3 X-ray 1.90 A 1-236 [» ]
    2WI4 X-ray 2.40 A 1-236 [» ]
    2WI5 X-ray 2.10 A 1-236 [» ]
    2WI6 X-ray 2.18 A 1-236 [» ]
    2WI7 X-ray 2.50 A 1-236 [» ]
    2XAB X-ray 1.90 A/B 9-236 [» ]
    2XDK X-ray 1.97 A 9-236 [» ]
    2XDL X-ray 1.98 A 9-236 [» ]
    2XDS X-ray 1.97 A 9-236 [» ]
    2XDU X-ray 1.74 A 14-224 [» ]
    2XDX X-ray 2.42 A 9-236 [» ]
    2XHR X-ray 2.20 A 9-236 [» ]
    2XHT X-ray 2.27 A 9-236 [» ]
    2XHX X-ray 2.80 A 9-236 [» ]
    2XJG X-ray 2.25 A 9-236 [» ]
    2XJJ X-ray 1.90 A/B 9-236 [» ]
    2XJX X-ray 1.66 A 9-236 [» ]
    2XK2 X-ray 1.95 A 9-236 [» ]
    2YE2 X-ray 1.90 A 9-236 [» ]
    2YE3 X-ray 1.95 A 9-236 [» ]
    2YE4 X-ray 2.30 A 9-236 [» ]
    2YE5 X-ray 1.73 A 9-236 [» ]
    2YE6 X-ray 2.56 A 9-236 [» ]
    2YE7 X-ray 2.20 A 9-236 [» ]
    2YE8 X-ray 2.30 A 9-236 [» ]
    2YE9 X-ray 2.20 A 9-236 [» ]
    2YEA X-ray 1.73 A 9-236 [» ]
    2YEB X-ray 2.40 A 9-236 [» ]
    2YEC X-ray 2.10 A 9-236 [» ]
    2YED X-ray 2.10 A 9-236 [» ]
    2YEE X-ray 2.30 A 9-236 [» ]
    2YEF X-ray 1.55 A 9-236 [» ]
    2YEG X-ray 2.50 A/B 9-236 [» ]
    2YEH X-ray 2.10 A 9-236 [» ]
    2YEI X-ray 2.20 A 9-236 [» ]
    2YEJ X-ray 2.20 A 9-236 [» ]
    2YI0 X-ray 1.60 A 1-229 [» ]
    2YI5 X-ray 2.50 A 1-229 [» ]
    2YI6 X-ray 1.80 A 1-229 [» ]
    2YI7 X-ray 1.40 A 1-229 [» ]
    2YJW X-ray 1.61 A 18-223 [» ]
    2YJX X-ray 1.83 A 18-223 [» ]
    2YK2 X-ray 1.74 A 18-223 [» ]
    2YK9 X-ray 1.32 A 18-223 [» ]
    2YKB X-ray 1.93 A 18-223 [» ]
    2YKC X-ray 1.67 A 18-223 [» ]
    2YKE X-ray 1.43 A 18-223 [» ]
    2YKI X-ray 1.67 A 18-223 [» ]
    2YKJ X-ray 1.46 A 18-223 [» ]
    3B24 X-ray 1.70 A/B 9-236 [» ]
    3B25 X-ray 1.75 A 9-236 [» ]
    3B26 X-ray 2.10 A/B 9-236 [» ]
    3B27 X-ray 1.50 A 9-236 [» ]
    3B28 X-ray 1.35 A/B 9-236 [» ]
    3BM9 X-ray 1.60 A 14-236 [» ]
    3BMY X-ray 1.60 A 14-236 [» ]
    3D0B X-ray 1.74 A 1-232 [» ]
    3EKO X-ray 1.55 A/B 9-225 [» ]
    3EKR X-ray 2.00 A/B 9-225 [» ]
    3FT5 X-ray 1.90 A 9-236 [» ]
    3FT8 X-ray 2.00 A 9-236 [» ]
    3HEK X-ray 1.95 A/B 9-225 [» ]
    3HHU X-ray 1.59 A/B 1-224 [» ]
    3HYY X-ray 1.90 A 9-236 [» ]
    3HYZ X-ray 2.30 A/B 9-236 [» ]
    3HZ1 X-ray 2.30 A 9-236 [» ]
    3HZ5 X-ray 1.90 A 9-236 [» ]
    3INW X-ray 1.95 A 10-236 [» ]
    3INX X-ray 1.75 A 10-236 [» ]
    3K97 X-ray 1.95 A 9-236 [» ]
    3K98 X-ray 2.40 A/B 9-225 [» ]
    3K99 X-ray 2.10 A/B/C/D 9-225 [» ]
    3MNR X-ray 1.90 P 1-232 [» ]
    3O0I X-ray 1.47 A 1-236 [» ]
    3OW6 X-ray 1.80 A 17-223 [» ]
    3OWB X-ray 2.05 A 17-223 [» ]
    3OWD X-ray 1.63 A 17-223 [» ]
    3Q6M X-ray 3.00 A/B/C 293-732 [» ]
    3Q6N X-ray 3.05 A/B/C/D/E/F 293-732 [» ]
    3QDD X-ray 1.79 A 1-236 [» ]
    3QTF X-ray 1.57 A 14-236 [» ]
    3R4M X-ray 1.70 A 9-236 [» ]
    3R4N X-ray 2.00 A/B 9-225 [» ]
    3R4O X-ray 2.65 A/B 9-225 [» ]
    3R4P X-ray 1.70 A/B 9-225 [» ]
    3R91 X-ray 1.58 A 14-236 [» ]
    3R92 X-ray 1.58 A 14-236 [» ]
    3RKZ X-ray 1.57 A 14-236 [» ]
    3RLP X-ray 1.70 A/B 9-225 [» ]
    3RLQ X-ray 1.90 A/B 9-225 [» ]
    3RLR X-ray 1.70 A/B 9-225 [» ]
    3T0H X-ray 1.20 A 9-236 [» ]
    3T0Z X-ray 2.19 A 9-236 [» ]
    3T10 X-ray 1.24 A 9-236 [» ]
    3T1K X-ray 1.50 A/B 9-236 [» ]
    3T2S X-ray 1.50 A/B 9-236 [» ]
    3TUH X-ray 1.80 A/B 16-224 [» ]
    3VHA X-ray 1.39 A 9-236 [» ]
    3VHC X-ray 1.41 A 9-236 [» ]
    3VHD X-ray 1.52 A/B 9-236 [» ]
    3WHA X-ray 1.30 A/B 9-236 [» ]
    4AIF X-ray 2.01 D/E 726-732 [» ]
    4AWO X-ray 1.70 A/B 9-236 [» ]
    4AWP X-ray 1.82 A/B 9-236 [» ]
    4AWQ X-ray 1.60 A/B 9-236 [» ]
    4B7P X-ray 1.70 A 9-236 [» ]
    4BQJ X-ray 2.00 A 9-236 [» ]
    4CGU X-ray 2.11 C 726-732 [» ]
    4CGV X-ray 2.54 E/F 726-732 [» ]
    4CGW X-ray 3.00 C/D 726-732 [» ]
    4EEH X-ray 1.60 A 9-236 [» ]
    4EFT X-ray 2.12 A 9-236 [» ]
    4EFU X-ray 2.00 A 9-236 [» ]
    4EGH X-ray 1.60 A 9-236 [» ]
    4EGI X-ray 1.79 A 9-236 [» ]
    4EGK X-ray 1.69 A 9-236 [» ]
    4FCP X-ray 2.00 A/B 1-236 [» ]
    4FCQ X-ray 2.15 A 1-236 [» ]
    4FCR X-ray 1.70 A 1-236 [» ]
    4HY6 X-ray 1.65 A 9-236 [» ]
    4JQL X-ray 1.72 A 9-236 [» ]
    4L8Z X-ray 1.70 A 9-236 [» ]
    4L90 X-ray 2.00 A 9-236 [» ]
    4L91 X-ray 1.75 A 9-236 [» ]
    4L93 X-ray 1.84 A/B 9-236 [» ]
    4L94 X-ray 1.65 A 9-236 [» ]
    4NH7 X-ray 2.00 A/B 9-236 [» ]
    4NH8 X-ray 1.65 A 9-236 [» ]
    4O05 X-ray 1.79 A 9-236 [» ]
    4O07 X-ray 1.86 A 9-236 [» ]
    4O09 X-ray 1.96 A 9-236 [» ]
    4O0B X-ray 1.93 A 9-236 [» ]
    ProteinModelPortali P07900.
    SMRi P07900. Positions 15-699.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109552. 740 interactions.
    DIPi DIP-27595N.
    IntActi P07900. 192 interactions.
    MINTi MINT-132070.
    STRINGi 9606.ENSP00000335153.

    Chemistry

    BindingDBi P07900.
    ChEMBLi CHEMBL3880.
    DrugBanki DB00615. Rifabutin.

    PTM databases

    PhosphoSitei P07900.

    Polymorphism databases

    DMDMi 92090606.

    2D gel databases

    OGPi P07900.
    REPRODUCTION-2DPAGE IPI00784295.

    Proteomic databases

    MaxQBi P07900.
    PRIDEi P07900.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000216281 ; ENSP00000216281 ; ENSG00000080824 . [P07900-1 ]
    ENST00000334701 ; ENSP00000335153 ; ENSG00000080824 . [P07900-2 ]
    GeneIDi 3320.
    KEGGi hsa:3320.
    UCSCi uc001yku.4. human. [P07900-1 ]
    uc001ykv.4. human. [P07900-2 ]

    Organism-specific databases

    CTDi 3320.
    GeneCardsi GC14M102547.
    HGNCi HGNC:5253. HSP90AA1.
    HPAi CAB002058.
    HPA047290.
    MIMi 140571. gene.
    neXtProti NX_P07900.
    PharmGKBi PA29519.
    GenAtlasi Search...

    Phylogenomic databases

    HOVERGENi HBG007374.
    InParanoidi P07900.
    KOi K04079.
    OMAi MSHLTEF.
    OrthoDBi EOG780RM0.
    PhylomeDBi P07900.
    TreeFami TF300686.

    Enzyme and pathway databases

    Reactomei REACT_111176. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
    REACT_115755. Signaling by ERBB2.
    REACT_115852. Signaling by constitutively active EGFR.
    REACT_12477. eNOS activation.
    REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
    REACT_15364. Loss of Nlp from mitotic centrosomes.
    REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
    REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
    REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
    REACT_163813. Scavenging by Class F Receptors.
    REACT_19236. Sema3A PAK dependent Axon repulsion.
    REACT_200624. Attenuation phase.
    REACT_200744. HSF1 activation.
    REACT_200775. HSF1-dependent transactivation.
    REACT_9434. vRNP Assembly.

    Miscellaneous databases

    ChiTaRSi HSP90AA1. human.
    EvolutionaryTracei P07900.
    GenomeRNAii 3320.
    NextBioi 13162.
    PMAP-CutDB P07900.
    PROi P07900.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P07900.
    Bgeei P07900.
    CleanExi HS_HSP90AA1.
    Genevestigatori P07900.

    Family and domain databases

    Gene3Di 3.30.565.10. 2 hits.
    HAMAPi MF_00505. HSP90.
    InterProi IPR003594. HATPase_ATP-bd.
    IPR019805. Heat_shock_protein_90_CS.
    IPR001404. Hsp90_fam.
    IPR020575. Hsp90_N.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    [Graphical view ]
    PANTHERi PTHR11528. PTHR11528. 1 hit.
    Pfami PF02518. HATPase_c. 1 hit.
    PF00183. HSP90. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF002583. Hsp90. 1 hit.
    PRINTSi PR00775. HEATSHOCK90.
    SMARTi SM00387. HATPase_c. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54211. SSF54211. 1 hit.
    SSF55874. SSF55874. 1 hit.
    PROSITEi PS00298. HSP90. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of a full-length cDNA for 90 kDa heat-shock protein from human peripheral blood lymphocytes."
      Soeda E., Yokoyama K., Yamazaki M., Akaogi K., Miwa T., Imai T.
      Nucleic Acids Res. 17:7108-7108(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Peripheral blood lymphocyte.
    2. "Molecular cloning of cDNA encoding a human heat-shock protein whose expression is induced by adenovirus type 12 E1A in HeLa cells."
      Yamazaki M., Tashiro H., Yokoyama K., Soeda E.
      Agric. Biol. Chem. 54:3163-3170(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Sequence and regulation of a gene encoding a human 89-kilodalton heat shock protein."
      Hickey E., Brandon S.E., Smale G., Lloyd D., Weber L.A.
      Mol. Cell. Biol. 9:2615-2626(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Placenta.
    4. "The HSP90 family of genes in the human genome: insights into their divergence and evolution."
      Chen B., Piel W.H., Gui L., Bruford E., Monteiro A.
      Genomics 86:627-637(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), NOMENCLATURE.
    5. NHLBI resequencing and genotyping service (RS&G)
      Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    6. "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] (ISOFORMS 1 AND 2).
      Tissue: Placenta and Teratocarcinoma.
    7. "The DNA sequence and analysis of human chromosome 14."
      Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
      , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
      Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "Heat-shock proteins, Hsp84 and Hsp86, of mice and men: two related genes encode formerly identified tumour-specific transplantation antigens."
      Hoffmann T., Hovemann B.
      Gene 74:491-501(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-312.
    10. "Cloning and analysis of a human 86-kDa heat-shock-protein-encoding gene."
      Walter T., Drabent B., Krebs H., Tomalak M., Heiss S., Benecke B.J.J.
      Gene 83:105-115(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-312.
    11. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 101-112; 210-224; 300-314; 328-338; 346-355; 387-400; 465-478 AND 633-647, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    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] OF 185-732.
      Tissue: Placenta.
    13. "The analysis of the genes reactive to monoclonal antibody, CE5."
      Tanaka M., Tanaka T., Mitsui Y., Yamamoto M., Wood J.N.
      Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 539-732.
      Tissue: Heart.
    14. "Two human 90-kDa heat shock proteins are phosphorylated in vivo at conserved serines that are phosphorylated in vitro by casein kinase II."
      Lees-Miller S.P., Anderson C.W.
      J. Biol. Chem. 264:2431-2437(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-21, PHOSPHORYLATION.
    15. "S-nitrosylation of Hsp90 promotes the inhibition of its ATPase and endothelial nitric oxide synthase regulatory activities."
      Martinez-Ruiz A., Villanueva L., Gonzalez de Orduna C., Lopez-Ferrer D., Higueras M.A., Tarin C., Rodriguez-Crespo I., Vazquez J., Lamas S.
      Proc. Natl. Acad. Sci. U.S.A. 102:8525-8530(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 592-612, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-598, S-NITROSYLATION AT CYS-598.
    16. "The human double-stranded DNA-activated protein kinase phosphorylates the 90-kDa heat-shock protein, hsp90 alpha at two NH2-terminal threonine residues."
      Lees-Miller S.P., Anderson C.W.
      J. Biol. Chem. 264:17275-17280(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-5 AND THR-7.
    17. "The carboxy-terminal region of mammalian HSP90 is required for its dimerization and function in vivo."
      Minami Y., Kimura Y., Kawasaki H., Suzuki K., Yahara I.
      Mol. Cell. Biol. 14:1459-1464(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: HOMODIMERIZATION.
    18. "Mechanism of dimer formation of the 90-kDa heat-shock protein."
      Nemoto T., Ohara-Nemoto Y., Ota M., Takagi T., Yokoyama K.
      Eur. J. Biochem. 233:1-8(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    19. "Protein phosphatase 5 is a major component of glucocorticoid receptor.hsp90 complexes with properties of an FK506-binding immunophilin."
      Silverstein A.M., Galigniana M.D., Chen M.S., Owens-Grillo J.K., Chinkers M., Pratt W.B.
      J. Biol. Chem. 272:16224-16230(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH NR3C1 AND FKBP4; PPID; PPP5C OR STIP1.
    20. "Specific binding of tetratricopeptide repeat proteins to the C-terminal 12-kDa domain of hsp90."
      Young J.C., Obermann W.M., Hartl F.U.
      J. Biol. Chem. 273:18007-18010(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TOM34.
    21. Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN.
      Tissue: Renal cell carcinoma.
    22. "Stable association of hsp90 and p23, but Not hsp70, with active human telomerase."
      Forsythe H.L., Jarvis J.L., Turner J.W., Elmore L.W., Holt S.E.
      J. Biol. Chem. 276:15571-15574(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TERT, FUNCTION AS A CO-CHAPERONE IN TELOMERASE HOLOENZYME ASSEMBLY.
    23. "Evidence for a mechanism of repression of heat shock factor 1 transcriptional activity by a multichaperone complex."
      Guo Y., Guettouche T., Fenna M., Boellmann F., Pratt W.B., Toft D.O., Smith D.F., Voellmy R.
      J. Biol. Chem. 276:45791-45799(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HSF1.
    24. Cited for: FUNCTION, IDENTIFICATION AS LPS RECEPTOR, INTERACTION WITH CXCR4; GDF5 AND HSPA8, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    25. "Cofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone system."
      Brychzy A., Rein T., Winklhofer K.F., Hartl F.U., Young J.C., Obermann W.M.
      EMBO J. 22:3613-3623(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DNAJC7.
    26. "Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone."
      Lotz G.P., Lin H., Harst A., Obermann W.M.J.
      J. Biol. Chem. 278:17228-17235(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AHSA1.
    27. "SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells."
      Hamamoto R., Furukawa Y., Morita M., Iimura Y., Silva F.P., Li M., Yagyu R., Nakamura Y.
      Nat. Cell Biol. 6:731-740(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SMYD3.
    28. "Human protein phosphatase 5 dissociates from heat-shock proteins and is proteolytically activated in response to arachidonic acid and the microtubule-depolymerizing drug nocodazole."
      Zeke T., Morrice N., Vazquez-Martin C., Cohen P.T.
      Biochem. J. 385:45-56(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PPP5C, IDENTIFICATION BY MASS SPECTROMETRY.
    29. "Molecular basis for TPR domain-mediated regulation of protein phosphatase 5."
      Yang J., Roe S.M., Cliff M.J., Williams M.A., Ladbury J.E., Cohen P.T., Barford D.
      EMBO J. 24:1-10(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PPP5C.
    30. "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-231 AND SER-263, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    31. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Pituitary.
    32. "Conformational diversity in the TPR domain-mediated interaction of protein phosphatase 5 with Hsp90."
      Cliff M.J., Harris R., Barford D., Ladbury J.E., Williams M.A.
      Structure 14:415-426(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PPP5C.
    33. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
      Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
      J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: T-cell.
    34. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252 AND SER-263, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    35. "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-263, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    36. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    37. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
      Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
      Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231 AND SER-263, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    38. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    39. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    40. "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-443; LYS-458; LYS-489 AND LYS-585, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    41. "A proteomic investigation of ligand-dependent HSP90 complexes reveals CHORDC1 as a novel ADP-dependent HSP90-interacting protein."
      Gano J.J., Simon J.A.
      Mol. Cell. Proteomics 9:255-270(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CHORDC1.
    42. Cited for: ISGYLATION.
    43. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Melanoma.
    44. Cited for: INTERACTION WITH FNIP1, IDENTIFICATION BY MASS SPECTROMETRY.
    45. "The ATPase-dependent chaperoning activity of Hsp90a regulates thick filament formation and integration during skeletal muscle myofibrillogenesis."
      Hawkins T.A., Haramis A.P., Etard C., Prodromou C., Vaughan C.K., Ashworth R., Ray S., Behra M., Holder N., Talbot W.S., Pearl L.H., Strahle U., Wilson S.W.
      Development 135:1147-1156(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF GLY-97.
    46. "Hsp90 is regulated by a switch point in the C-terminal domain."
      Retzlaff M., Stahl M., Eberl H.C., Lagleder S., Beck J., Kessler H., Buchner J.
      EMBO Rep. 10:1147-1153(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CYS-598.
    47. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    48. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    49. "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-252, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    50. "Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent."
      Stebbins C.E., Russo A.A., Schneider C., Rosen N., Hartl F.U., Pavletich N.P.
      Cell 89:239-250(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 11-223 IN COMPLEX WITH GELDANAMYCIN.
    51. "In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis."
      Obermann W.M., Sondermann H., Russo A.A., Pavletich N.P., Hartl F.U.
      J. Cell Biol. 143:901-910(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 11-223 IN COMPLEX WITH ADP, CATALYTIC ACTIVITY, INTERACTION WITH PTGES3.
    52. "Chaperoned ubiquitylation -- crystal structures of the CHIP U box E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex."
      Zhang M., Windheim M., Roe S.M., Peggie M., Cohen P., Prodromou C., Pearl L.H.
      Mol. Cell 20:525-538(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 724-732 IN COMPLEX WITH STUB1, INTERACTION WITH STUB1 AND UBE2N.

    Entry informationi

    Entry nameiHS90A_HUMAN
    AccessioniPrimary (citable) accession number: P07900
    Secondary accession number(s): A8K500
    , B3KPJ9, Q2PP14, Q5CAQ6, Q5CAQ7, Q9BVQ5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 195 of the entry and version 5 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 14
      Human chromosome 14: 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