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Protein

Heat shock protein HSP 90-beta

Gene

HSP90AB1

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

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 (PubMed:16478993, PubMed:19696785). Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle (PubMed:27295069, PubMed:26991466). Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels. In the first place, they alter the steady-state levels of certain transcription factors in response to various physiological cues. Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment. Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression (PubMed:25973397). Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation (PubMed:24613385). Promotes cell differentiation by chaperoning BIRC2 and thereby protecting from auto-ubiquitination and degradation by the proteasomal machinery (PubMed:18239673). Main chaperone that is involved in the phosphorylation/activation of the STAT1 by chaperoning both JAK2 and PRKCE under heat shock and in turn, activates its own transcription (PubMed:20353823).3 Publications5 Publications

Enzyme regulationi

In the resting state, through the dimerization of its C-terminal domain, HSP90 forms a homodimer which is defined as the open conformation. Upon ATP-binding, the N-terminal domain undergoes significant conformational changes and comes in contact to form an active closed conformation. After HSP90 finishes its chaperoning tasks of assisting the proper folding, stabilization and activation of client proteins under the active state, ATP molecule is hydrolyzed to ADP which then dissociates from HSP90 and directs the protein back to the resting state.1 Publication

Kineticsi

  1. KM=300 µM for ATP1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei46ATPBy similarity1
    Binding sitei88ATP1
    Binding sitei107ATPBy similarity1
    Sitei126 – 127Cleaved under oxidative stress1 Publication2
    Binding sitei133ATP; via amide nitrogenBy similarity1
    Binding sitei392ATPBy similarity1

    GO - Molecular functioni

    • ATP binding Source: CAFA
    • ATP-dependent protein binding Source: CAFA
    • cadherin binding Source: BHF-UCL
    • CTP binding Source: Ensembl
    • dATP binding Source: Ensembl
    • disordered domain specific binding Source: CAFA
    • DNA polymerase binding Source: BHF-UCL
    • double-stranded RNA binding Source: MGI
    • drug binding Source: Ensembl
    • GTP binding Source: Ensembl
    • heat shock protein binding Source: UniProtKB
    • histone deacetylase binding Source: BHF-UCL
    • histone methyltransferase binding Source: UniProtKB
    • ion channel binding Source: Ensembl
    • kinase binding Source: UniProtKB
    • MHC class II protein complex binding Source: UniProtKB
    • nitric-oxide synthase regulator activity Source: UniProtKB
    • peptide binding Source: UniProtKB
    • protein dimerization activity Source: UniProtKB
    • protein homodimerization activity Source: CAFA
    • protein kinase binding Source: Ensembl
    • protein kinase regulator activity Source: Ensembl
    • RNA binding Source: UniProtKB
    • sulfonylurea receptor binding Source: Ensembl
    • TPR domain binding Source: UniProtKB
    • unfolded protein binding Source: InterPro
    • UTP binding Source: Ensembl

    GO - Biological processi

    Keywordsi

    Molecular functionChaperone
    Biological processStress response
    LigandATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiR-HSA-2029482. Regulation of actin dynamics for phagocytic cup formation.
    R-HSA-3371497. HSP90 chaperone cycle for steroid hormone receptors (SHR).
    R-HSA-3371511. HSF1 activation.
    R-HSA-3371568. Attenuation phase.
    R-HSA-3371571. HSF1-dependent transactivation.
    R-HSA-399954. Sema3A PAK dependent Axon repulsion.
    R-HSA-5336415. Uptake and function of diphtheria toxin.
    R-HSA-6798695. Neutrophil degranulation.
    R-HSA-844456. The NLRP3 inflammasome.
    R-HSA-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.
    R-HSA-8937144. Aryl hydrocarbon receptor signalling.
    SIGNORiP08238.

    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
    Proteomesi
    • UP000005640 Componenti: Chromosome 6

    Organism-specific databases

    EuPathDBiHostDB:ENSG00000096384.19.
    HGNCiHGNC:5258. HSP90AB1.

    Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Nucleus, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi42E → A: Strong ATP-binding. Strong interaction with HSF1, HIF1A, ERBB2, MET, KEAP1 and RHOBTB2. 1 Publication1
    Mutagenesisi88D → A: Impaired ATP-binding. Strong interaction with HIF1A, MET, KEAP1 and RHOBTB2. Loss of interaction with HSF1 and ERBB2. 1 Publication1
    Mutagenesisi226S → A: Increases the binding affinity for AHR; when associated with A-255. Increases AHR transcription activity; when associated with A-255. 1 Publication1
    Mutagenesisi226S → E: No effect on the interaction with AHR; when associated with E-255. 1 Publication1
    Mutagenesisi255S → A: Increases the binding affinity for AHR; when associated with A-226. Increases AHR transcription activity; when associated with A-226. 1 Publication1
    Mutagenesisi255S → E: No effect on the interaction with AHR; when associated with E-226. 1 Publication1
    Mutagenesisi301Y → F: Decreases interaction with NOS3 and SRC. impairs resists LPS-induced tyrosine phosphorylation. Does not block LPS-induced pp60src phosphorylation. 1 Publication1
    Mutagenesisi531K → A: Highly decreases the signal of SMYD2-dependent HSP90AB1 methylation; when associated with A-574. Diminishes dimerized form; when associated with A-574. Reduces interaction with STIP1 or CDC37; when associated with A-574. 1 Publication1
    Mutagenesisi574K → A: Decreases the signal of SMYD2-dependent HSP90AB1 methylation. Highly decreases the signal of SMYD2-dependent HSP90AB1 methylation; when associated with A-531. Diminishes dimerized form; when associated with A-531. Reduces interaction with STIP1 or CDC37; when associated with A-531. 1 Publication1
    Mutagenesisi590C → A, N or D: Reduced ATPase activity and client protein activation. 1 Publication1

    Organism-specific databases

    DisGeNETi3326.
    OpenTargetsiENSG00000096384.
    PharmGKBiPA29524.

    Chemistry databases

    ChEMBLiCHEMBL4303.
    DrugBankiDB05134. CNF1010.
    DB02424. Geldanamycin.
    DB03758. Radicicol.
    DB06070. SNX-5422.
    GuidetoPHARMACOLOGYi2907.

    Polymorphism and mutation databases

    DMDMi17865718.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved1 Publication
    ChainiPRO_00000629172 – 724Heat shock protein HSP 90-betaAdd BLAST723

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei219N6-succinyllysineBy similarity1
    Modified residuei226PhosphoserineCombined sources1
    Modified residuei255PhosphoserineCombined sources1 Publication1
    Modified residuei261Phosphoserine1 Publication1
    Modified residuei297PhosphothreonineCombined sources1
    Modified residuei301Phosphotyrosine; by SRC1 Publication1
    Modified residuei305PhosphotyrosineBy similarity1
    Modified residuei307PhosphoserineCombined sources1
    Modified residuei399N6-malonyllysine1 Publication1
    Glycosylationi434O-linked (GlcNAc) serineBy similarity1
    Modified residuei435N6-acetyllysineCombined sources1
    Modified residuei445PhosphoserineCombined sources1
    Modified residuei452Phosphoserine; alternate1 Publication1
    Glycosylationi452O-linked (GlcNAc) serine; alternateBy similarity1
    Modified residuei479PhosphothreonineCombined sources1
    Modified residuei481N6-acetyllysineCombined sources1
    Modified residuei484Phosphotyrosine1 Publication1
    Modified residuei531N6-methylated lysine; alternate1 Publication1
    Modified residuei531N6-succinyllysine; alternateBy similarity1
    Modified residuei532Phosphoserine1 Publication1
    Modified residuei574N6-methylated lysine1 Publication1
    Modified residuei577N6-succinyllysineBy similarity1
    Modified residuei590S-nitrosocysteine1 Publication1
    Modified residuei624N6-acetyllysineBy similarity1
    Modified residuei669PhosphoserineCombined sources1
    Modified residuei718Phosphoserine; by PLK2 and PLK31 Publication1

    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
    Phosphorylation at Tyr-301 by SRC is induced by lipopolysaccharide (PubMed:23585225). Phosphorylation at Ser-226 and Ser-255 inhibits AHR interaction (PubMed:15581363).2 Publications
    Methylated by SMYD2; facilitates dimerization and chaperone complex formation; promotes cancer cell proliferation.1 Publication
    Cleaved following oxidative stress resulting in HSP90AB1 protein radicals formation; disrupts the chaperoning function and the degradation of its client proteins.1 Publication

    Keywords - PTMi

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

    Proteomic databases

    EPDiP08238.
    MaxQBiP08238.
    PaxDbiP08238.
    PeptideAtlasiP08238.
    PRIDEiP08238.
    TopDownProteomicsiP08238.

    2D gel databases

    OGPiP08238.

    PTM databases

    iPTMnetiP08238.
    PhosphoSitePlusiP08238.
    SwissPalmiP08238.

    Expressioni

    Inductioni

    By heat shock.1 Publication

    Gene expression databases

    BgeeiENSG00000096384.
    CleanExiHS_HSP90AB1.
    ExpressionAtlasiP08238. baseline and differential.
    GenevisibleiP08238. HS.

    Organism-specific databases

    HPAiCAB005230.
    HPA055729.

    Interactioni

    Subunit structurei

    Monomer (PubMed:24880080). Homodimer (PubMed:7588731, PubMed:18400751). Forms a complex with CDK6 and CDC37 (PubMed:9482106, PubMed:25486457). Interacts with UNC45A; binding to UNC45A involves 2 UNC45A monomers per HSP90AB1 dimer (PubMed:16478993). Interacts with CHORDC1 (By similarity). Interacts with DNAJC7 (PubMed:18620420). Interacts with FKBP4 (PubMed:15159550). May interact with NWD1 (PubMed:24681825). Interacts with SGTA (PubMed:16580629). Interacts with HSF1 in an ATP-dependent manner. Interacts with MET; the interaction suppresses MET kinase activity. Interacts with ERBB2 in an ATP-dependent manner; the interaction suppresses ERBB2 kinase activity. Interacts with HIF1A, KEAP1 and RHOBTB2 (PubMed:26517842). Interacts with STUB1 and SMAD3 (PubMed:24613385). Interacts with XPO1 and AHSA1 (PubMed:22022502, PubMed:25486457). Interacts with BIRC2 (PubMed:25486457). Interacts with KCNQ4; promotes cell surface expression of KCNQ4 (PubMed:23431407). Interacts with BIRC2; prevents auto-ubiquitination and degradation of its client protein BIRC2 (PubMed:18239673). Interacts with NOS3 (PubMed:23585225). Interacts with AHR; interaction is inhibited by HSP90AB1 phosphorylation on Ser-226 and Ser-255 (PubMed:15581363). Interacts with STIP1 and CDC37; upon SMYD2-dependent methylation (PubMed:24880080). Interacts with JAK2 and PRKCE; promotes functional activation in a heat shock-dependent manner (PubMed:20353823). Interacts with HSP90AA1; interaction is constitutive (PubMed:20353823). HSP90AB1-CDC37 chaperone complex interacts with inactive MAPK7 (via N-terminal half) in resting cells; the interaction is MAP2K5-independent and prevents from ubiquitination and proteasomal degradation (PubMed:23428871). Interacts with CDC25A; prevents heat shock-mediated CDC25A degradation and contributes to cell cycle progression (PubMed:22843495). Interacts with TP53 (via DNA binding domain); suppresses TP53 aggregation and prevents from irreversible thermal inactivation (PubMed:15358771). Interacts with TGFB1 processed form (LAP); inhibits latent TGFB1 activation (PubMed:20599762). Interacts with TRIM8; prevents nucleus translocation of phosphorylated STAT3 and HSP90AB1 (By similarity).By similarity22 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
    AMPD3Q014322EBI-352572,EBI-1223554
    ARAFP103986EBI-352572,EBI-365961
    AURKBQ96GD42EBI-352572,EBI-624291
    BRAFP150562EBI-352572,EBI-365980
    BTKQ061872EBI-352572,EBI-624835
    CAMK2GQ135552EBI-352572,EBI-1383465
    CDC37Q165437EBI-352572,EBI-295634
    CDC37L1Q7L3B65EBI-352572,EBI-2841876
    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
    CHORDC1Q9UHD13EBI-352572,EBI-2550959
    CHUKO151112EBI-352572,EBI-81249
    CSNK1EP496742EBI-352572,EBI-749343
    CUL3Q136182EBI-352572,EBI-456129
    DDR2Q168322EBI-352572,EBI-1381484
    EGFRP005338EBI-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
    FLNAP213333EBI-352572,EBI-350432
    FLT4P359162EBI-352572,EBI-1005467
    FYNP062412EBI-352572,EBI-515315
    GNAI2P048992EBI-352572,EBI-353997
    GSG2Q8TF762EBI-352572,EBI-1237328
    GSK3AP498402EBI-352572,EBI-1044067
    ICKQ9UPZ92EBI-352572,EBI-6381479
    IKBKBO149203EBI-352572,EBI-81266
    IKBKEQ141643EBI-352572,EBI-307369
    IKBKGQ9Y6K94EBI-352572,EBI-81279
    KLHL38Q2WGJ63EBI-352572,EBI-6426443
    LCKP062392EBI-352572,EBI-1348
    LIMK2P536712EBI-352572,EBI-1384350
    MAP3K1Q132332EBI-352572,EBI-49776
    MAP3K14Q995583EBI-352572,EBI-358011
    MAP3K3Q997592EBI-352572,EBI-307281
    MAP3K7O43318-22EBI-352572,EBI-358700
    MAP3K8P412793EBI-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
    NFKB1P198383EBI-352572,EBI-300010
    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
    RIPK1Q135462EBI-352572,EBI-358507
    ROR2Q019742EBI-352572,EBI-6422642
    RPL11P629132EBI-352572,EBI-354380
    RPS6KA1Q154182EBI-352572,EBI-963034
    STK11Q158313EBI-352572,EBI-306838
    STK38Q152082EBI-352572,EBI-458376
    STUB1Q9UNE75EBI-352572,EBI-357085
    SUGT1Q9Y2Z0-22EBI-352572,EBI-10768076
    TBK1Q9UHD23EBI-352572,EBI-356402
    TESK2Q96S532EBI-352572,EBI-1384110
    TRAF2Q129332EBI-352572,EBI-355744
    TSSK6Q9BXA63EBI-352572,EBI-851883
    TYK2P295972EBI-352572,EBI-1383454
    UNC45BQ8IWX72EBI-352572,EBI-9363363

    GO - Molecular functioni

    • ATP-dependent protein binding Source: CAFA
    • cadherin binding Source: BHF-UCL
    • disordered domain specific binding Source: CAFA
    • DNA polymerase binding Source: BHF-UCL
    • heat shock protein binding Source: UniProtKB
    • histone deacetylase binding Source: BHF-UCL
    • histone methyltransferase binding Source: UniProtKB
    • ion channel binding Source: Ensembl
    • kinase binding Source: UniProtKB
    • MHC class II protein complex binding Source: UniProtKB
    • protein dimerization activity Source: UniProtKB
    • protein homodimerization activity Source: CAFA
    • protein kinase binding Source: Ensembl
    • sulfonylurea receptor binding Source: Ensembl
    • TPR domain binding Source: UniProtKB
    • unfolded protein binding Source: InterPro

    Protein-protein interaction databases

    BioGridi109558. 330 interactors.
    CORUMiP08238.
    DIPiDIP-413N.
    IntActiP08238. 569 interactors.
    MINTiMINT-99712.
    STRINGi9606.ENSP00000325875.

    Chemistry databases

    BindingDBiP08238.

    Structurei

    Secondary structure

    1724
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi13 – 16Combined sources4
    Helixi19 – 30Combined sources12
    Helixi38 – 60Combined sources23
    Helixi62 – 65Combined sources4
    Beta strandi73 – 78Combined sources6
    Turni79 – 82Combined sources4
    Beta strandi83 – 88Combined sources6
    Helixi95 – 99Combined sources5
    Helixi101 – 118Combined sources18
    Helixi123 – 129Combined sources7
    Helixi132 – 138Combined sources7
    Beta strandi140 – 148Combined sources9
    Beta strandi155 – 159Combined sources5
    Beta strandi164 – 169Combined sources6
    Beta strandi176 – 185Combined sources10
    Helixi187 – 193Combined sources7
    Helixi195 – 205Combined sources11
    Beta strandi213 – 215Combined sources3
    Helixi288 – 290Combined sources3
    Helixi293 – 295Combined sources3
    Helixi298 – 309Combined sources12
    Beta strandi316 – 323Combined sources8
    Beta strandi325 – 327Combined sources3
    Beta strandi329 – 335Combined sources7
    Beta strandi353 – 357Combined sources5
    Beta strandi360 – 364Combined sources5
    Helixi367 – 369Combined sources3
    Helixi372 – 374Combined sources3
    Beta strandi378 – 386Combined sources9
    Helixi395 – 420Combined sources26
    Helixi423 – 443Combined sources21
    Helixi445 – 447Combined sources3
    Helixi448 – 453Combined sources6
    Beta strandi456 – 459Combined sources4
    Turni460 – 464Combined sources5
    Helixi469 – 474Combined sources6
    Beta strandi482 – 486Combined sources5
    Helixi491 – 495Combined sources5
    Helixi498 – 504Combined sources7
    Turni505 – 507Combined sources3
    Beta strandi510 – 512Combined sources3
    Helixi518 – 525Combined sources8
    Beta strandi531 – 535Combined sources5

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1QZ2X-ray3.00G/H720-724[»]
    1UYMX-ray2.45A2-221[»]
    2L6JNMR-B720-724[»]
    3FWVX-ray2.20C/D719-723[»]
    3NMQX-ray2.20A1-223[»]
    3PRYX-ray2.28A/B/C284-543[»]
    3UQ3X-ray2.60B/C720-724[»]
    5FWKelectron microscopy3.90A/B1-724[»]
    5FWLelectron microscopy9.00A/B1-724[»]
    5FWMelectron microscopy8.00A/B1-724[»]
    5FWPelectron microscopy7.20A/B1-724[»]
    ProteinModelPortaliP08238.
    SMRiP08238.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP08238.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni2 – 527Interaction with TP531 PublicationAdd BLAST526
    Regioni2 – 214Interaction with BIRC21 PublicationAdd BLAST213
    Regioni215 – 552Interaction with AHSA11 PublicationAdd BLAST338

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Motifi720 – 724TPR repeat-binding5

    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

    eggNOGiKOG0019. Eukaryota.
    KOG0020. Eukaryota.
    COG0326. LUCA.
    GeneTreeiENSGT00840000129758.
    HOGENOMiHOG000031988.
    HOVERGENiHBG007374.
    InParanoidiP08238.
    KOiK04079.
    OMAiLRYHSSQ.
    OrthoDBiEOG091G0270.
    PhylomeDBiP08238.
    TreeFamiTF300686.

    Family and domain databases

    Gene3Di3.30.565.10. 1 hit.
    HAMAPiMF_00505. HSP90. 1 hit.
    InterProiView protein in InterPro
    IPR003594. HATPase_C.
    IPR019805. Heat_shock_protein_90_CS.
    IPR001404. Hsp90_fam.
    IPR020575. Hsp90_N.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    PANTHERiPTHR11528. PTHR11528. 1 hit.
    PfamiView protein in Pfam
    PF02518. HATPase_c. 1 hit.
    PF00183. HSP90. 1 hit.
    PIRSFiPIRSF002583. Hsp90. 1 hit.
    PRINTSiPR00775. HEATSHOCK90.
    SMARTiView protein in SMART
    SM00387. HATPase_c. 1 hit.
    SUPFAMiSSF54211. SSF54211. 1 hit.
    SSF55874. SSF55874. 1 hit.
    PROSITEiView protein in PROSITE
    PS00298. HSP90. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P08238-1 [UniParc]FASTAAdd to basket

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    MPEEVHHGEE EVETFAFQAE IAQLMSLIIN TFYSNKEIFL RELISNASDA
    60 70 80 90 100
    LDKIRYESLT DPSKLDSGKE LKIDIIPNPQ ERTLTLVDTG IGMTKADLIN
    110 120 130 140 150
    NLGTIAKSGT KAFMEALQAG ADISMIGQFG VGFYSAYLVA EKVVVITKHN
    160 170 180 190 200
    DDEQYAWESS AGGSFTVRAD HGEPIGRGTK VILHLKEDQT EYLEERRVKE
    210 220 230 240 250
    VVKKHSQFIG YPITLYLEKE REKEISDDEA EEEKGEKEEE DKDDEEKPKI
    260 270 280 290 300
    EDVGSDEEDD SGKDKKKKTK KIKEKYIDQE ELNKTKPIWT RNPDDITQEE
    310 320 330 340 350
    YGEFYKSLTN DWEDHLAVKH FSVEGQLEFR ALLFIPRRAP FDLFENKKKK
    360 370 380 390 400
    NNIKLYVRRV FIMDSCDELI PEYLNFIRGV VDSEDLPLNI SREMLQQSKI
    410 420 430 440 450
    LKVIRKNIVK KCLELFSELA EDKENYKKFY EAFSKNLKLG IHEDSTNRRR
    460 470 480 490 500
    LSELLRYHTS QSGDEMTSLS EYVSRMKETQ KSIYYITGES KEQVANSAFV
    510 520 530 540 550
    ERVRKRGFEV VYMTEPIDEY CVQQLKEFDG KSLVSVTKEG LELPEDEEEK
    560 570 580 590 600
    KKMEESKAKF ENLCKLMKEI LDKKVEKVTI SNRLVSSPCC IVTSTYGWTA
    610 620 630 640 650
    NMERIMKAQA LRDNSTMGYM MAKKHLEINP DHPIVETLRQ KAEADKNDKA
    660 670 680 690 700
    VKDLVVLLFE TALLSSGFSL EDPQTHSNRI YRMIKLGLGI DEDEVAAEEP
    710 720
    NAAVPDEIPP LEGDEDASRM EEVD
    Length:724
    Mass (Da):83,264
    Last modified:January 23, 2007 - v4
    Checksum:iA93118C214D03810
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti147T → R in AAA36025 (PubMed:3301534).Curated1
    Sequence conflicti177R → M in AAA36025 (PubMed:3301534).Curated1
    Sequence conflicti403V → A in CAB66478 (PubMed:11230166).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_049624349K → E. Corresponds to variant dbSNP:rs11538975Ensembl.1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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. No translation available.
    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.
    UniGeneiHs.509736.

    Genome annotation databases

    EnsembliENST00000353801; ENSP00000325875; ENSG00000096384.
    ENST00000371554; ENSP00000360609; ENSG00000096384.
    ENST00000371646; ENSP00000360709; ENSG00000096384.
    ENST00000620073; ENSP00000481908; ENSG00000096384.
    GeneIDi3326.
    KEGGihsa:3326.
    UCSCiuc003oxa.3. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Similar proteinsi

    Entry informationi

    Entry nameiHS90B_HUMAN
    AccessioniPrimary (citable) accession number: P08238
    Secondary accession number(s): B2R5P0
    , Q5T9W7, Q9NQW0, Q9NTK6
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: January 23, 2007
    Last modified: September 27, 2017
    This is version 224 of the entry and version 4 of the sequence. See 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