Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P08238

- HS90B_HUMAN

UniProt

P08238 - HS90B_HUMAN

Protein

Heat shock protein HSP 90-beta

Gene

HSP90AB1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 190 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei46 – 461ATPBy similarity
    Binding sitei88 – 881ATP
    Binding sitei107 – 1071ATPBy similarity
    Binding sitei133 – 1331ATP; via amide nitrogenBy similarity
    Binding sitei392 – 3921ATPBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. CTP binding Source: Ensembl
    3. dATP binding Source: Ensembl
    4. double-stranded RNA binding Source: MGI
    5. GTP binding Source: Ensembl
    6. MHC class II protein complex binding Source: UniProt
    7. nitric-oxide synthase regulator activity Source: UniProtKB
    8. poly(A) RNA binding Source: UniProtKB
    9. protein binding Source: UniProtKB
    10. TPR domain binding Source: UniProtKB
    11. UTP binding Source: Ensembl

    GO - Biological processi

    1. axon guidance Source: Reactome
    2. cellular response to interleukin-4 Source: Ensembl
    3. cellular response to organic cyclic compound Source: Ensembl
    4. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
    5. innate immune response Source: Reactome
    6. negative regulation of neuron apoptotic process Source: Ensembl
    7. negative regulation of proteasomal ubiquitin-dependent protein catabolic process Source: MGI
    8. nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway Source: Reactome
    9. placenta development Source: Ensembl
    10. positive regulation of cell size Source: Ensembl
    11. positive regulation of nitric oxide biosynthetic process Source: UniProtKB
    12. positive regulation of protein binding Source: Ensembl
    13. positive regulation of protein import into nucleus, translocation Source: Ensembl
    14. positive regulation of protein serine/threonine kinase activity Source: Ensembl
    15. protein folding Source: InterPro
    16. regulation of interferon-gamma-mediated signaling pathway Source: MGI
    17. regulation of type I interferon-mediated signaling pathway Source: MGI
    18. response to salt stress Source: Ensembl
    19. response to unfolded protein Source: UniProtKB

    Keywords - Molecular functioni

    Chaperone

    Keywords - Biological processi

    Stress response

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_160086. Regulation of actin dynamics for phagocytic cup formation.
    REACT_19236. Sema3A PAK dependent Axon repulsion.
    REACT_200624. Attenuation phase.
    REACT_200744. HSF1 activation.
    REACT_200775. HSF1-dependent transactivation.
    REACT_75808. The NLRP3 inflammasome.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Heat shock protein HSP 90-beta
    Short name:
    HSP 90
    Alternative name(s):
    Heat shock 84 kDa
    Short name:
    HSP 84
    Short name:
    HSP84
    Gene namesi
    Name:HSP90AB1
    Synonyms:HSP90B, HSPC2, HSPCB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:5258. HSP90AB1.

    Subcellular locationi

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

    GO - Cellular componenti

    1. apical plasma membrane Source: Ensembl
    2. basolateral plasma membrane Source: Ensembl
    3. brush border membrane Source: Ensembl
    4. cell surface Source: Ensembl
    5. cytoplasm Source: HPA
    6. cytosol Source: Reactome
    7. extracellular vesicular exosome Source: UniProt
    8. inclusion body Source: Ensembl
    9. melanosome Source: UniProtKB-SubCell
    10. membrane Source: UniProtKB
    11. mitochondrion Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi590 – 5901C → A, N or D: Reduced ATPase activity and client protein activation. 1 Publication

    Organism-specific databases

    PharmGKBiPA29524.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 724723Heat shock protein HSP 90-betaPRO_0000062917Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei219 – 2191N6-succinyllysineBy similarity
    Modified residuei226 – 2261Phosphoserine5 Publications
    Modified residuei255 – 2551Phosphoserine3 Publications
    Modified residuei261 – 2611Phosphoserine1 Publication
    Modified residuei297 – 2971Phosphothreonine2 Publications
    Modified residuei305 – 3051PhosphotyrosineBy similarity
    Modified residuei307 – 3071Phosphoserine2 Publications
    Modified residuei399 – 3991N6-malonyllysine1 Publication
    Glycosylationi434 – 4341O-linked (GlcNAc)By similarity
    Modified residuei435 – 4351N6-acetyllysine1 Publication
    Modified residuei452 – 4521Phosphoserine; alternate1 Publication
    Glycosylationi452 – 4521O-linked (GlcNAc); alternateBy similarity
    Modified residuei481 – 4811N6-acetyllysine1 Publication
    Modified residuei484 – 4841Phosphotyrosine1 Publication
    Modified residuei531 – 5311N6-succinyllysineBy similarity
    Modified residuei532 – 5321Phosphoserine1 Publication
    Modified residuei577 – 5771N6-succinyllysineBy similarity
    Modified residuei590 – 5901S-nitrosocysteine1 Publication
    Modified residuei624 – 6241N6-acetyllysineBy similarity
    Modified residuei718 – 7181Phosphoserine; by PLK2 and PLK32 Publications

    Post-translational modificationi

    Ubiquitinated in the presence of STUB1-UBE2D1 complex (in vitro).1 Publication
    ISGylated.1 Publication
    S-nitrosylated; negatively regulates the ATPase activity.1 Publication

    Keywords - PTMi

    Acetylation, Glycoprotein, Phosphoprotein, S-nitrosylation, Ubl conjugation

    Proteomic databases

    MaxQBiP08238.
    PaxDbiP08238.
    PeptideAtlasiP08238.
    PRIDEiP08238.

    2D gel databases

    OGPiP08238.

    PTM databases

    PhosphoSiteiP08238.

    Expressioni

    Gene expression databases

    ArrayExpressiP08238.
    BgeeiP08238.
    CleanExiHS_HSP90AB1.
    GenevestigatoriP08238.

    Organism-specific databases

    HPAiCAB005230.
    HPA055729.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with p53/TP53 By similarity. Forms a complex with CDK6 and Hsp90/HSP90AB1. Interacts with UNC45A. Binding to UNC45A involves 2 UNC45A monomers per HSP90AB1 dimer. Interacts with CHORDC1 and DNAJC7 By similarity. Interacts with FKBP4.By similarity5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ACVR1BP368962EBI-352572,EBI-1384128
    AGO1Q9UL183EBI-352572,EBI-527363
    AHSA1O954333EBI-352572,EBI-448610
    AIPO001703EBI-352572,EBI-704197
    AKT2P317512EBI-352572,EBI-296058
    ALKQ9UM732EBI-352572,EBI-357361
    AMHR2Q166712EBI-352572,EBI-6423788
    ARAFP103986EBI-352572,EBI-365961
    AURKBQ96GD42EBI-352572,EBI-624291
    BRAFP150562EBI-352572,EBI-365980
    BTKQ061872EBI-352572,EBI-624835
    CAMK2GQ135552EBI-352572,EBI-1383465
    CDC37Q165436EBI-352572,EBI-295634
    CDK10Q151312EBI-352572,EBI-1646959
    CDK14O949212EBI-352572,EBI-1043945
    CDK15Q96Q402EBI-352572,EBI-1051975
    CDK4P118023EBI-352572,EBI-295644
    CDK6Q005342EBI-352572,EBI-295663
    CDK9P507502EBI-352572,EBI-1383449
    CHEK1O147573EBI-352572,EBI-974488
    CSNK1EP496742EBI-352572,EBI-749343
    CUL3Q136182EBI-352572,EBI-456129
    DDR2Q168322EBI-352572,EBI-1381484
    ECDO959052EBI-352572,EBI-2557598
    EGFRP005335EBI-352572,EBI-297353
    EPHA2P293172EBI-352572,EBI-702104
    ERBB2P046263EBI-352572,EBI-641062
    ERBB3P218603EBI-352572,EBI-720706
    ERBB4Q153032EBI-352572,EBI-80371
    FAM162AQ96A263EBI-352572,EBI-6123466
    FBXL2Q9UKC92EBI-352572,EBI-724253
    FBXO24O754262EBI-352572,EBI-6425658
    FBXW2Q9UKT82EBI-352572,EBI-914727
    FGFR3P226072EBI-352572,EBI-348399
    FGRP097692EBI-352572,EBI-1383732
    FLT4P359162EBI-352572,EBI-1005467
    FYNP062412EBI-352572,EBI-515315
    GSG2Q8TF762EBI-352572,EBI-1237328
    GSK3AP498402EBI-352572,EBI-1044067
    ICKQ9UPZ92EBI-352572,EBI-6381479
    IKBKBO149202EBI-352572,EBI-81266
    IKBKEQ141642EBI-352572,EBI-307369
    KLHL38Q2WGJ63EBI-352572,EBI-6426443
    LCKP062392EBI-352572,EBI-1348
    LIMK2P536712EBI-352572,EBI-1384350
    MAP3K14Q995582EBI-352572,EBI-358011
    MAP3K8P412792EBI-352572,EBI-354900
    MAP3K9P801922EBI-352572,EBI-3951604
    MAPK4P311522EBI-352572,EBI-3906061
    MAPTP10636-84EBI-352572,EBI-366233
    MATKP426792EBI-352572,EBI-751664
    MUSKO151462EBI-352572,EBI-6423196
    NEK9Q8TD192EBI-352572,EBI-1044009
    NR1I2O754692EBI-352572,EBI-3905991
    POGKQ9P2152EBI-352572,EBI-2555775
    PRKAA1Q131312EBI-352572,EBI-1181405
    PRKACBP226942EBI-352572,EBI-2679622
    PRKCEQ021562EBI-352572,EBI-706254
    PRKCZQ055132EBI-352572,EBI-295351
    PRKD1Q151392EBI-352572,EBI-1181072
    PRKXP518172EBI-352572,EBI-4302903
    PSKH1P118012EBI-352572,EBI-3922781
    RAF1P040493EBI-352572,EBI-365996
    RGS6P497582EBI-352572,EBI-6426927
    ROR2Q019742EBI-352572,EBI-6422642
    RPS6KA1Q154182EBI-352572,EBI-963034
    STK11Q158313EBI-352572,EBI-306838
    STK38Q152082EBI-352572,EBI-458376
    STUB1Q9UNE75EBI-352572,EBI-357085
    TBK1Q9UHD22EBI-352572,EBI-356402
    TESK2Q96S532EBI-352572,EBI-1384110
    TSSK6Q9BXA63EBI-352572,EBI-851883
    TYK2P295972EBI-352572,EBI-1383454
    UNC45BQ8IWX72EBI-352572,EBI-9363363

    Protein-protein interaction databases

    BioGridi109558. 203 interactions.
    DIPiDIP-413N.
    IntActiP08238. 478 interactions.
    MINTiMINT-99712.
    STRINGi9606.ENSP00000325875.

    Structurei

    Secondary structure

    1
    724
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi13 – 164
    Helixi19 – 3012
    Helixi38 – 6023
    Helixi62 – 654
    Beta strandi73 – 786
    Turni79 – 824
    Beta strandi83 – 886
    Helixi95 – 995
    Helixi101 – 11818
    Helixi123 – 1297
    Helixi132 – 1387
    Beta strandi140 – 1489
    Beta strandi155 – 1595
    Beta strandi164 – 1696
    Beta strandi176 – 18510
    Helixi187 – 1937
    Helixi195 – 20511
    Beta strandi213 – 2153
    Helixi288 – 2903
    Helixi293 – 2953
    Helixi298 – 30912
    Beta strandi316 – 3238
    Beta strandi325 – 3273
    Beta strandi329 – 3357
    Beta strandi353 – 3575
    Beta strandi360 – 3645
    Helixi367 – 3693
    Helixi372 – 3743
    Beta strandi378 – 3869
    Helixi395 – 42026
    Helixi423 – 44321
    Helixi445 – 4473
    Helixi448 – 4536
    Beta strandi456 – 4594
    Turni460 – 4645
    Helixi469 – 4746
    Beta strandi482 – 4865
    Helixi491 – 4955
    Helixi498 – 5047
    Turni505 – 5073
    Beta strandi510 – 5123
    Helixi518 – 5258
    Beta strandi531 – 5355

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1QZ2X-ray3.00G/H720-724[»]
    1UYMX-ray2.45A2-221[»]
    2L6JNMR-B720-724[»]
    3NMQX-ray2.20A1-223[»]
    3PRYX-ray2.28A/B/C284-543[»]
    3UQ3X-ray2.60B/C720-724[»]
    ProteinModelPortaliP08238.
    SMRiP08238. Positions 8-691.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP08238.

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi720 – 7245TPR repeat-binding

    Domaini

    The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins.By similarity

    Sequence similaritiesi

    Belongs to the heat shock protein 90 family.Curated

    Phylogenomic databases

    eggNOGiCOG0326.
    HOGENOMiHOG000031988.
    HOVERGENiHBG007374.
    InParanoidiP08238.
    KOiK04079.
    OMAiFNKEDYY.
    OrthoDBiEOG780RM0.
    PhylomeDBiP08238.
    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]

    Sequencei

    Sequence statusi: Complete.

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

    P08238-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPEEVHHGEE EVETFAFQAE IAQLMSLIIN TFYSNKEIFL RELISNASDA    50
    LDKIRYESLT DPSKLDSGKE LKIDIIPNPQ ERTLTLVDTG IGMTKADLIN 100
    NLGTIAKSGT KAFMEALQAG ADISMIGQFG VGFYSAYLVA EKVVVITKHN 150
    DDEQYAWESS AGGSFTVRAD HGEPIGRGTK VILHLKEDQT EYLEERRVKE 200
    VVKKHSQFIG YPITLYLEKE REKEISDDEA EEEKGEKEEE DKDDEEKPKI 250
    EDVGSDEEDD SGKDKKKKTK KIKEKYIDQE ELNKTKPIWT RNPDDITQEE 300
    YGEFYKSLTN DWEDHLAVKH FSVEGQLEFR ALLFIPRRAP FDLFENKKKK 350
    NNIKLYVRRV FIMDSCDELI PEYLNFIRGV VDSEDLPLNI SREMLQQSKI 400
    LKVIRKNIVK KCLELFSELA EDKENYKKFY EAFSKNLKLG IHEDSTNRRR 450
    LSELLRYHTS QSGDEMTSLS EYVSRMKETQ KSIYYITGES KEQVANSAFV 500
    ERVRKRGFEV VYMTEPIDEY CVQQLKEFDG KSLVSVTKEG LELPEDEEEK 550
    KKMEESKAKF ENLCKLMKEI LDKKVEKVTI SNRLVSSPCC IVTSTYGWTA 600
    NMERIMKAQA LRDNSTMGYM MAKKHLEINP DHPIVETLRQ KAEADKNDKA 650
    VKDLVVLLFE TALLSSGFSL EDPQTHSNRI YRMIKLGLGI DEDEVAAEEP 700
    NAAVPDEIPP LEGDEDASRM EEVD 724
    Length:724
    Mass (Da):83,264
    Last modified:January 23, 2007 - v4
    Checksum:iA93118C214D03810
    GO

    Sequence cautioni

    The sequence CAB66478.1 differs from that shown. Reason: Frameshift at position 709.
    The sequence AAD14062.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti147 – 1471T → R in AAA36025. (PubMed:3301534)Curated
    Sequence conflicti177 – 1771R → M in AAA36025. (PubMed:3301534)Curated
    Sequence conflicti403 – 4031V → A in CAB66478. (PubMed:11230166)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti349 – 3491K → E.
    Corresponds to variant rs11538975 [ dbSNP | Ensembl ].
    VAR_049624

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M16660 mRNA. Translation: AAA36025.1.
    J04988 Genomic DNA. Translation: AAA36026.1.
    AY359878 mRNA. Translation: AAQ63401.1.
    AL136543 mRNA. Translation: CAB66478.1. Frameshift.
    AK312255 mRNA. Translation: BAG35187.1.
    DQ314872 Genomic DNA. Translation: ABC40731.1.
    AL139392 Genomic DNA. Translation: CAI20095.1.
    CH471081 Genomic DNA. Translation: EAX04257.1.
    BC004928 mRNA. Translation: AAH04928.1.
    BC009206 mRNA. Translation: AAH09206.2.
    BC012807 mRNA. Translation: AAH12807.1.
    BC014485 mRNA. Translation: AAH14485.1.
    BC016753 mRNA. Translation: AAH16753.1.
    BC068474 mRNA. Translation: AAH68474.1.
    AH007358 Genomic DNA. Translation: AAD14062.3. Different initiation.
    AF275719 mRNA. Translation: AAF82792.1.
    CCDSiCCDS4909.1.
    PIRiA29461. HHHU84.
    T46243.
    RefSeqiNP_001258898.1. NM_001271969.1.
    NP_001258899.1. NM_001271970.1.
    NP_001258900.1. NM_001271971.1.
    NP_031381.2. NM_007355.3.
    XP_005249132.1. XM_005249075.1.
    UniGeneiHs.509736.

    Genome annotation databases

    EnsembliENST00000353801; ENSP00000325875; ENSG00000096384.
    ENST00000371554; ENSP00000360609; ENSG00000096384.
    ENST00000371646; ENSP00000360709; ENSG00000096384.
    GeneIDi3326.
    KEGGihsa:3326.
    UCSCiuc003oxa.2. human.

    Polymorphism databases

    DMDMi17865718.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M16660 mRNA. Translation: AAA36025.1 .
    J04988 Genomic DNA. Translation: AAA36026.1 .
    AY359878 mRNA. Translation: AAQ63401.1 .
    AL136543 mRNA. Translation: CAB66478.1 . Frameshift.
    AK312255 mRNA. Translation: BAG35187.1 .
    DQ314872 Genomic DNA. Translation: ABC40731.1 .
    AL139392 Genomic DNA. Translation: CAI20095.1 .
    CH471081 Genomic DNA. Translation: EAX04257.1 .
    BC004928 mRNA. Translation: AAH04928.1 .
    BC009206 mRNA. Translation: AAH09206.2 .
    BC012807 mRNA. Translation: AAH12807.1 .
    BC014485 mRNA. Translation: AAH14485.1 .
    BC016753 mRNA. Translation: AAH16753.1 .
    BC068474 mRNA. Translation: AAH68474.1 .
    AH007358 Genomic DNA. Translation: AAD14062.3 . Different initiation.
    AF275719 mRNA. Translation: AAF82792.1 .
    CCDSi CCDS4909.1.
    PIRi A29461. HHHU84.
    T46243.
    RefSeqi NP_001258898.1. NM_001271969.1.
    NP_001258899.1. NM_001271970.1.
    NP_001258900.1. NM_001271971.1.
    NP_031381.2. NM_007355.3.
    XP_005249132.1. XM_005249075.1.
    UniGenei Hs.509736.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1QZ2 X-ray 3.00 G/H 720-724 [» ]
    1UYM X-ray 2.45 A 2-221 [» ]
    2L6J NMR - B 720-724 [» ]
    3NMQ X-ray 2.20 A 1-223 [» ]
    3PRY X-ray 2.28 A/B/C 284-543 [» ]
    3UQ3 X-ray 2.60 B/C 720-724 [» ]
    ProteinModelPortali P08238.
    SMRi P08238. Positions 8-691.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109558. 203 interactions.
    DIPi DIP-413N.
    IntActi P08238. 478 interactions.
    MINTi MINT-99712.
    STRINGi 9606.ENSP00000325875.

    Chemistry

    BindingDBi P08238.
    ChEMBLi CHEMBL2095165.

    PTM databases

    PhosphoSitei P08238.

    Polymorphism databases

    DMDMi 17865718.

    2D gel databases

    OGPi P08238.

    Proteomic databases

    MaxQBi P08238.
    PaxDbi P08238.
    PeptideAtlasi P08238.
    PRIDEi P08238.

    Protocols and materials databases

    DNASUi 3326.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000353801 ; ENSP00000325875 ; ENSG00000096384 .
    ENST00000371554 ; ENSP00000360609 ; ENSG00000096384 .
    ENST00000371646 ; ENSP00000360709 ; ENSG00000096384 .
    GeneIDi 3326.
    KEGGi hsa:3326.
    UCSCi uc003oxa.2. human.

    Organism-specific databases

    CTDi 3326.
    GeneCardsi GC06P044214.
    H-InvDB HIX0031498.
    HIX0057380.
    HGNCi HGNC:5258. HSP90AB1.
    HPAi CAB005230.
    HPA055729.
    MIMi 140572. gene.
    neXtProti NX_P08238.
    PharmGKBi PA29524.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0326.
    HOGENOMi HOG000031988.
    HOVERGENi HBG007374.
    InParanoidi P08238.
    KOi K04079.
    OMAi FNKEDYY.
    OrthoDBi EOG780RM0.
    PhylomeDBi P08238.
    TreeFami TF300686.

    Enzyme and pathway databases

    Reactomei REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
    REACT_19236. Sema3A PAK dependent Axon repulsion.
    REACT_200624. Attenuation phase.
    REACT_200744. HSF1 activation.
    REACT_200775. HSF1-dependent transactivation.
    REACT_75808. The NLRP3 inflammasome.

    Miscellaneous databases

    ChiTaRSi HSP90AB1. human.
    EvolutionaryTracei P08238.
    GeneWikii HSP90AB1.
    GenomeRNAii 3326.
    NextBioi 13182.
    PROi P08238.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P08238.
    Bgeei P08238.
    CleanExi HS_HSP90AB1.
    Genevestigatori P08238.

    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 cDNA for a member of the human 90-kDa heat-shock protein family."
      Rebbe N.F., Ware J., Bertina R.M., Modrich P., Stafford D.W.
      Gene 53:235-245(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Nucleotide sequence and regulation of a human 90-kDa heat shock protein gene."
      Rebbe N.F., Hickman W.S., Ley T.J., Stafford D.W., Hickman S.
      J. Biol. Chem. 264:15006-15011(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "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].
    4. "Cloning a new isoform of heat shock 90kDa in testis."
      Lu L., Huang X.Y., Yin L.L., Xu M., Li J.M., Zhou Z.M., Sha J.H.
      Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Testis.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Amygdala.
    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].
    7. NHLBI resequencing and genotyping service (RS&G)
      Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    8. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. "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: Colon, Lymph, Muscle, Skin and Testis.
    11. "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.
    12. Bienvenut W.V., Waridel P., Quadroni M.
      Submitted (MAR-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 42-107; 149-168; 181-197; 204-221; 250-265; 274-284; 292-348; 360-392; 412-427; 439-448; 450-475; 482-502; 506-526; 539-551; 584-604; 613-639 AND 653-679, PHOSPHORYLATION AT SER-255, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryonic kidney.
    13. "A cosmid clone at the D6S182 locus on human chromosome 6p12 contains the 90-kDa heat shock protein beta gene (HSP90 beta)."
      Takahashi I., Tanuma R., Hirata M., Hashimoto K.
      Mamm. Genome 5:121-122(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 50-118.
    14. Takahashi I., Tanuma R., Hirata M., Hashimoto K.
      Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    15. "A two-dimensional gel database of human colon carcinoma proteins."
      Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J.
      Electrophoresis 18:605-613(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 54-64 AND 187-199.
      Tissue: Colon carcinoma.
    16. "Novel sequence for human Hsp90 beta giving a substitution of R55T (R147 in original sequence) and M85R (M177 in original sequence)."
      Mason A., O'Connor D., Greenhalf W.
      Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 93-724.
      Tissue: Pancreas.
    17. "Active cdk6 complexes are predominantly nuclear and represent only a minority of the cdk6 in T cells."
      Mahony D., Parry D.A., Lees E.
      Oncogene 16:603-611(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CDK6 AND CDC37.
    18. Cited for: ISGYLATION.
    19. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "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-255, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Melanoma.
    22. "GCUNC-45 is a novel regulator for the progesterone receptor/hsp90 chaperoning pathway."
      Chadli A., Graham J.D., Abel M.G., Jackson T.A., Gordon D.F., Wood W.M., Felts S.J., Horwitz K.B., Toft D.
      Mol. Cell. Biol. 26:1722-1730(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH UNC45A.
    23. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-297, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    24. "Two different classes of E2 ubiquitin-conjugating enzymes are required for the mono-ubiquitination of proteins and elongation by polyubiquitin chains with a specific topology."
      Windheim M., Peggie M., Cohen P.
      Biochem. J. 409:723-729(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION.
    25. Cited for: INTERACTION WITH DNAJC7.
    26. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    27. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    28. "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-226, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    29. "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: FUNCTION, S-NITROSYLATION AT CYS-590, MUTAGENESIS OF CYS-590.
    30. "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-435 AND LYS-481, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    31. "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-226, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    32. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    33. Cited for: MALONYLATION AT LYS-399.
    34. "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-226, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    35. Cited for: PHOSPHORYLATION AT SER-718 BY PLK2 AND PLK3.
    36. Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 1-221 IN COMPLEX WITH PURINE ANALOG.
    37. "3D structure of human FK506-binding protein 52: implications for the assembly of the glucocorticoid receptor/Hsp90/immunophilin heterocomplex."
      Wu B., Li P., Liu Y., Lou Z., Ding Y., Shu C., Ye S., Bartlam M., Shen B., Rao Z.
      Proc. Natl. Acad. Sci. U.S.A. 101:8348-8353(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 720-724 IN COMPLEX WITH FKBP4.
    38. "Crystal structure of the middle domain of human hsp90-beta."
      Structural genomics consortium (SGC)
      Submitted (DEC-2010) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 284-543.

    Entry informationi

    Entry nameiHS90B_HUMAN
    AccessioniPrimary (citable) accession number: P08238
    Secondary accession number(s): B2R5P0
    , Q5T9W7, Q9NQW0, Q9NTK6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 190 of the entry and version 4 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 6
      Human chromosome 6: 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