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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.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei46ATPBy similarity1
Binding sitei88ATP1
Binding sitei107ATPBy similarity1
Binding sitei133ATP; via amide nitrogenBy similarity1
Binding sitei392ATPBy similarity1

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • CTP binding Source: Ensembl
  • dATP binding Source: Ensembl
  • double-stranded RNA binding Source: MGI
  • drug binding Source: Ensembl
  • glycoprotein binding Source: Ensembl
  • GTP binding Source: Ensembl
  • histone deacetylase binding Source: BHF-UCL
  • kinase binding Source: ParkinsonsUK-UCL
  • MHC class II protein complex binding Source: UniProtKB
  • nitric-oxide synthase regulator activity Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • protein kinase regulator activity Source: Ensembl
  • TPR domain binding Source: UniProtKB
  • UTP binding Source: Ensembl

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Stress response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000096384-MONOMER.
ReactomeiR-HSA-2029482. Regulation of actin dynamics for phagocytic cup formation.
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.
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

HGNCiHGNC:5258. HSP90AB1.

Subcellular locationi

  • Cytoplasm
  • Melanosome

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

GO - Cellular componenti

  • apical plasma membrane Source: Ensembl
  • basolateral plasma membrane Source: Ensembl
  • brush border membrane Source: Ensembl
  • cell-cell adherens junction Source: BHF-UCL
  • cell surface Source: Ensembl
  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • inclusion body Source: Ensembl
  • lysosomal membrane Source: Ensembl
  • melanosome Source: UniProtKB-SubCell
  • membrane Source: UniProtKB
  • mitochondrion Source: UniProtKB
  • nucleoplasm Source: Reactome
  • ooplasm Source: Ensembl
  • sperm head plasma membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi590C → A, N or D: Reduced ATPase activity and client protein activation. 1 Publication1

Organism-specific databases

DisGeNETi3326.
OpenTargetsiENSG00000096384.
PharmGKBiPA29524.

Chemistry databases

ChEMBLiCHEMBL4303.
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 residuei305PhosphotyrosineBy similarity1
Modified residuei307PhosphoserineCombined sources1
Modified residuei399N6-malonyllysine1 Publication1
Glycosylationi434O-linked (GlcNAc)By similarity1
Modified residuei435N6-acetyllysineCombined sources1
Modified residuei445PhosphoserineCombined sources1
Modified residuei452Phosphoserine; alternate1 Publication1
Glycosylationi452O-linked (GlcNAc); alternateBy similarity1
Modified residuei479PhosphothreonineCombined sources1
Modified residuei481N6-acetyllysineCombined sources1
Modified residuei484Phosphotyrosine1 Publication1
Modified residuei531N6-succinyllysineBy similarity1
Modified residuei532Phosphoserine1 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

Keywords - PTMi

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

Proteomic databases

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

2D gel databases

OGPiP08238.

PTM databases

iPTMnetiP08238.
PhosphoSitePlusiP08238.
SwissPalmiP08238.

Expressioni

Gene expression databases

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

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. May interact with NWD1 (PubMed:24681825).By similarity6 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
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
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
FLNAP213332EBI-352572,EBI-350432
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
IKBKGQ9Y6K93EBI-352572,EBI-81279
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
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
ROR2Q019742EBI-352572,EBI-6422642
RPS6KA1Q154182EBI-352572,EBI-963034
STK11Q158313EBI-352572,EBI-306838
STK38Q152082EBI-352572,EBI-458376
STUB1Q9UNE75EBI-352572,EBI-357085
SUGT1Q9Y2Z0-22EBI-352572,EBI-10768076
TBK1Q9UHD22EBI-352572,EBI-356402
TESK2Q96S532EBI-352572,EBI-1384110
TSSK6Q9BXA63EBI-352572,EBI-851883
TYK2P295972EBI-352572,EBI-1383454
UNC45BQ8IWX72EBI-352572,EBI-9363363

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • histone deacetylase binding Source: BHF-UCL
  • kinase binding Source: ParkinsonsUK-UCL
  • MHC class II protein complex binding Source: UniProtKB
  • TPR domain binding Source: UniProtKB

Protein-protein interaction databases

BioGridi109558. 311 interactors.
DIPiDIP-413N.
IntActiP08238. 511 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[»]
ProteinModelPortaliP08238.
SMRiP08238.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08238.

Family & Domainsi

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.
OMAiAFANDIC.
OrthoDBiEOG091G0270.
PhylomeDBiP08238.
TreeFamiTF300686.

Family and domain databases

Gene3Di3.30.565.10. 2 hits.
HAMAPiMF_00505. HSP90. 1 hit.
InterProiIPR003594. HATPase_C.
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

        10         20         30         40         50
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 rs11538975dbSNPEnsembl.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. 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.
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

Cross-referencesi

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. 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.
UniGeneiHs.509736.

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[»]
ProteinModelPortaliP08238.
SMRiP08238.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109558. 311 interactors.
DIPiDIP-413N.
IntActiP08238. 511 interactors.
MINTiMINT-99712.
STRINGi9606.ENSP00000325875.

Chemistry databases

BindingDBiP08238.
ChEMBLiCHEMBL4303.
GuidetoPHARMACOLOGYi2907.

PTM databases

iPTMnetiP08238.
PhosphoSitePlusiP08238.
SwissPalmiP08238.

Polymorphism and mutation databases

DMDMi17865718.

2D gel databases

OGPiP08238.

Proteomic databases

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

Protocols and materials databases

DNASUi3326.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi3326.
DisGeNETi3326.
GeneCardsiHSP90AB1.
H-InvDBHIX0031498.
HIX0057380.
HGNCiHGNC:5258. HSP90AB1.
HPAiCAB005230.
HPA055729.
MIMi140572. gene.
neXtProtiNX_P08238.
OpenTargetsiENSG00000096384.
PharmGKBiPA29524.
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCyciZFISH:ENSG00000096384-MONOMER.
ReactomeiR-HSA-2029482. Regulation of actin dynamics for phagocytic cup formation.
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.
SIGNORiP08238.

Miscellaneous databases

ChiTaRSiHSP90AB1. human.
EvolutionaryTraceiP08238.
GeneWikiiHSP90AB1.
GenomeRNAii3326.
PROiP08238.
SOURCEiSearch...

Gene expression databases

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

Family and domain databases

Gene3Di3.30.565.10. 2 hits.
HAMAPiMF_00505. HSP90. 1 hit.
InterProiIPR003594. HATPase_C.
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]
ProtoNetiSearch...

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: November 30, 2016
This is version 215 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.