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P08238

- HS90B_HUMAN

UniProt

P08238 - HS90B_HUMAN

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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

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. TPR domain binding Source: UniProtKB
  10. 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
Complete GO annotation...

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: UniProtKB
  8. inclusion body Source: Ensembl
  9. membrane Source: UniProtKB
  10. mitochondrion Source: UniProt
Complete GO annotation...

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 – 2261Phosphoserine4 Publications
Modified residuei255 – 2551Phosphoserine2 Publications
Modified residuei261 – 2611Phosphoserine1 Publication
Modified residuei297 – 2971Phosphothreonine1 Publication
Modified residuei305 – 3051PhosphotyrosineBy similarity
Modified residuei307 – 3071Phosphoserine1 Publication
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 PLK31 Publication

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

BgeeiP08238.
CleanExiHS_HSP90AB1.
ExpressionAtlasiP08238. baseline and differential.
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
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
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
IKBKGQ9Y6K92EBI-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
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. 241 interactions.
DIPiDIP-413N.
IntActiP08238. 479 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.
GeneTreeiENSGT00760000119253.
HOGENOMiHOG000031988.
HOVERGENiHBG007374.
InParanoidiP08238.
KOiK04079.
OMAiFNKEDYY.
OrthoDBiEOG780RM0.
PhylomeDBiP08238.
TreeFamiTF300686.

Family and domain databases

Gene3Di3.30.565.10. 2 hits.
HAMAPiMF_00505. HSP90.
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 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.
ENST00000620073; ENSP00000481908; 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. 241 interactions.
DIPi DIP-413N.
IntActi P08238. 479 interactions.
MINTi MINT-99712.
STRINGi 9606.ENSP00000325875.

Chemistry

BindingDBi P08238.
ChEMBLi CHEMBL4303.

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 .
ENST00000620073 ; ENSP00000481908 ; 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.
GeneTreei ENSGT00760000119253.
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

Bgeei P08238.
CleanExi HS_HSP90AB1.
ExpressionAtlasi P08238. baseline and differential.
Genevestigatori P08238.

Family and domain databases

Gene3Di 3.30.565.10. 2 hits.
HAMAPi MF_00505. HSP90.
InterProi IPR003594. HATPase_C.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 191 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

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