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P08238

- HS90B_HUMAN

UniProt

P08238 - HS90B_HUMAN

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Protein
Heat shock protein HSP 90-beta
Gene
HSP90AB1, HSP90B, HSPC2, HSPCB
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 – 461ATP By similarity
Binding sitei88 – 881ATP
Binding sitei107 – 1071ATP By similarity
Binding sitei133 – 1331ATP; via amide nitrogen By similarity
Binding sitei392 – 3921ATP By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
  2. axon guidance Source: Reactome
  3. cellular response to interleukin-4 Source: Ensembl
  4. cellular response to organic cyclic compound Source: Ensembl
  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
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.2 Publications

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. 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-betaUniRule annotation
PRO_0000062917Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei219 – 2191N6-succinyllysine By similarity
Modified residuei226 – 2261Phosphoserine4 Publications
Modified residuei255 – 2551Phosphoserine2 Publications
Modified residuei261 – 2611PhosphoserineUniRule annotation
Modified residuei297 – 2971Phosphothreonine1 Publication
Modified residuei305 – 3051Phosphotyrosine By similarity
Modified residuei307 – 3071Phosphoserine1 Publication
Modified residuei399 – 3991N6-malonyllysine1 Publication
Glycosylationi434 – 4341O-linked (GlcNAc) By similarity
Modified residuei435 – 4351N6-acetyllysine1 Publication
Modified residuei452 – 4521Phosphoserine; alternateUniRule annotation
Glycosylationi452 – 4521O-linked (GlcNAc); alternate By similarity
Modified residuei481 – 4811N6-acetyllysine1 Publication
Modified residuei484 – 4841PhosphotyrosineUniRule annotation
Modified residuei531 – 5311N6-succinyllysine By similarity
Modified residuei532 – 5321PhosphoserineUniRule annotation
Modified residuei577 – 5771N6-succinyllysine By similarity
Modified residuei590 – 5901S-nitrosocysteine Inferred
Modified residuei624 – 6241N6-acetyllysine By 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 Inferred.UniRule annotation

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 FKBP4.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ACVR1BP368962EBI-352572,EBI-1384128
AKT2P317512EBI-352572,EBI-296058
ALKQ9UM732EBI-352572,EBI-357361
AMHR2Q166712EBI-352572,EBI-6423788
ARAFP103983EBI-352572,EBI-365961
AURKBQ96GD42EBI-352572,EBI-624291
BRAFP150562EBI-352572,EBI-365980
BTKQ061872EBI-352572,EBI-624835
CAMK2GQ135552EBI-352572,EBI-1383465
CDC37Q165434EBI-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
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
IKBKEQ141642EBI-352572,EBI-307369
KLHL38Q2WGJ62EBI-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
STUB1Q9UNE74EBI-352572,EBI-357085
TBK1Q9UHD22EBI-352572,EBI-356402
TESK2Q96S532EBI-352572,EBI-1384110
TSSK6Q9BXA63EBI-352572,EBI-851883
TYK2P295972EBI-352572,EBI-1383454

Protein-protein interaction databases

BioGridi109558. 203 interactions.
DIPiDIP-413N.
IntActiP08238. 455 interactions.
MINTiMINT-99712.
STRINGi9606.ENSP00000325875.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiP08238.

Family & Domainsi

Motif

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

Domaini

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

Sequence similaritiesi

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.

Natural variant

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti147 – 1471T → R in AAA36025. 1 Publication
Sequence conflicti177 – 1771R → M in AAA36025. 1 Publication
Sequence conflicti403 – 4031V → A in CAB66478. 1 Publication

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...

Protein-protein interaction databases

BioGridi 109558. 203 interactions.
DIPi DIP-413N.
IntActi P08238. 455 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

« 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: September 3, 2014
This is version 189 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

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