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P08238 (HS90B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 185. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:HSP90AB1
Synonyms:HSP90B, HSPC2, HSPCB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length724 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.22 Ref.29

Subunit structure

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. Ref.17 Ref.22 Ref.25

Subcellular location

Cytoplasm. Melanosome. Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Ref.17 Ref.21

Domain

The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins By similarity. HAMAP-Rule MF_00505

Post-translational modification

Ubiquitinated in the presence of STUB1-UBE2D1 complex (in vitro). Ref.24

ISGylated. Ref.18

S-nitrosylated; negatively regulates the ATPase activity Probable. HAMAP-Rule MF_00505

Sequence similarities

Belongs to the heat shock protein 90 family.

Sequence caution

The sequence AAD14062.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence CAB66478.1 differs from that shown. Reason: Frameshift at position 709.

Ontologies

Keywords
   Biological processStress response
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionChaperone
   PTMAcetylation
Glycoprotein
Phosphoprotein
S-nitrosylation
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processFc-gamma receptor signaling pathway involved in phagocytosis

Traceable author statement. Source: Reactome

axon guidance

Traceable author statement. Source: Reactome

cellular response to interleukin-4

Inferred from electronic annotation. Source: Ensembl

cellular response to organic cyclic compound

Inferred from electronic annotation. Source: Ensembl

innate immune response

Traceable author statement. Source: Reactome

negative regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of proteasomal ubiquitin-dependent protein catabolic process

Inferred from mutant phenotype PubMed 16280321. Source: MGI

nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway

Traceable author statement. Source: Reactome

placenta development

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell size

Inferred from electronic annotation. Source: Ensembl

positive regulation of nitric oxide biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of protein binding

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein import into nucleus, translocation

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein serine/threonine kinase activity

Inferred from electronic annotation. Source: Ensembl

protein folding

Inferred from electronic annotation. Source: InterPro

regulation of interferon-gamma-mediated signaling pathway

Inferred from mutant phenotype PubMed 16280321. Source: MGI

regulation of type I interferon-mediated signaling pathway

Inferred from mutant phenotype PubMed 16280321. Source: MGI

response to salt stress

Inferred from electronic annotation. Source: Ensembl

response to unfolded protein

Non-traceable author statement Ref.2. Source: UniProtKB

   Cellular_componentapical plasma membrane

Inferred from electronic annotation. Source: Ensembl

basolateral plasma membrane

Inferred from electronic annotation. Source: Ensembl

brush border membrane

Inferred from electronic annotation. Source: Ensembl

cell surface

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

inclusion body

Inferred from electronic annotation. Source: Ensembl

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from direct assay PubMed 20833797. Source: UniProt

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

CTP binding

Inferred from electronic annotation. Source: Ensembl

GTP binding

Inferred from electronic annotation. Source: Ensembl

MHC class II protein complex binding

Inferred from direct assay PubMed 20458337. Source: UniProt

TPR domain binding

Inferred from sequence or structural similarity. Source: UniProtKB

UTP binding

Inferred from electronic annotation. Source: Ensembl

dATP binding

Inferred from electronic annotation. Source: Ensembl

double-stranded RNA binding

Inferred from direct assay PubMed 21266579. Source: MGI

nitric-oxide synthase regulator activity

Inferred from sequence or structural similarity. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

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
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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.11
Chain2 – 724723Heat shock protein HSP 90-beta HAMAP-Rule MF_00505
PRO_0000062917

Regions

Motif720 – 7245TPR repeat-binding HAMAP-Rule MF_00505

Sites

Binding site461ATP By similarity
Binding site881ATP
Binding site1071ATP By similarity
Binding site1331ATP; via amide nitrogen By similarity
Binding site3921ATP By similarity

Amino acid modifications

Modified residue2191N6-succinyllysine By similarity
Modified residue2261Phosphoserine Ref.26 Ref.28 Ref.31 Ref.34
Modified residue2551Phosphoserine Ref.12 Ref.20
Modified residue2611Phosphoserine HAMAP-Rule MF_00505
Modified residue2751N6-acetyllysine HAMAP-Rule MF_00505
Modified residue2841N6-acetyllysine HAMAP-Rule MF_00505
Modified residue2971Phosphothreonine Ref.23
Modified residue3051Phosphotyrosine By similarity
Modified residue3071Phosphoserine Ref.27
Modified residue3541N6-acetyllysine HAMAP-Rule MF_00505
Modified residue3991N6-acetyllysine; alternate HAMAP-Rule MF_00505
Modified residue3991N6-malonyllysine; alternate Ref.33
Modified residue4021N6-acetyllysine HAMAP-Rule MF_00505
Modified residue4351N6-acetyllysine Ref.30
Modified residue4521Phosphoserine; alternate HAMAP-Rule MF_00505
Modified residue4811N6-acetyllysine Ref.30
Modified residue4841Phosphotyrosine HAMAP-Rule MF_00505
Modified residue5311N6-succinyllysine By similarity
Modified residue5321Phosphoserine HAMAP-Rule MF_00505
Modified residue5681N6-acetyllysine HAMAP-Rule MF_00505
Modified residue5771N6-succinyllysine By similarity
Modified residue5901S-nitrosocysteine Probable
Modified residue6241N6-acetyllysine HAMAP-Rule MF_00505
Modified residue7181Phosphoserine HAMAP-Rule MF_00505
Glycosylation4341O-linked (GlcNAc) By similarity
Glycosylation4521O-linked (GlcNAc); alternate By similarity

Natural variations

Natural variant3491K → E.
Corresponds to variant rs11538975 [ dbSNP | Ensembl ].
VAR_049624

Experimental info

Mutagenesis5901C → A, N or D: Reduced ATPase activity and client protein activation. Ref.29
Sequence conflict1471T → R in AAA36025. Ref.1
Sequence conflict1771R → M in AAA36025. Ref.1
Sequence conflict4031V → A in CAB66478. Ref.5

Secondary structure

.................................................................................. 724
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P08238 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: A93118C214D03810

FASTA72483,264
        10         20         30         40         50         60 
MPEEVHHGEE EVETFAFQAE IAQLMSLIIN TFYSNKEIFL RELISNASDA LDKIRYESLT 

        70         80         90        100        110        120 
DPSKLDSGKE LKIDIIPNPQ ERTLTLVDTG IGMTKADLIN NLGTIAKSGT KAFMEALQAG 

       130        140        150        160        170        180 
ADISMIGQFG VGFYSAYLVA EKVVVITKHN DDEQYAWESS AGGSFTVRAD HGEPIGRGTK 

       190        200        210        220        230        240 
VILHLKEDQT EYLEERRVKE VVKKHSQFIG YPITLYLEKE REKEISDDEA EEEKGEKEEE 

       250        260        270        280        290        300 
DKDDEEKPKI EDVGSDEEDD SGKDKKKKTK KIKEKYIDQE ELNKTKPIWT RNPDDITQEE 

       310        320        330        340        350        360 
YGEFYKSLTN DWEDHLAVKH FSVEGQLEFR ALLFIPRRAP FDLFENKKKK NNIKLYVRRV 

       370        380        390        400        410        420 
FIMDSCDELI PEYLNFIRGV VDSEDLPLNI SREMLQQSKI LKVIRKNIVK KCLELFSELA 

       430        440        450        460        470        480 
EDKENYKKFY EAFSKNLKLG IHEDSTNRRR LSELLRYHTS QSGDEMTSLS EYVSRMKETQ 

       490        500        510        520        530        540 
KSIYYITGES KEQVANSAFV ERVRKRGFEV VYMTEPIDEY CVQQLKEFDG KSLVSVTKEG 

       550        560        570        580        590        600 
LELPEDEEEK KKMEESKAKF ENLCKLMKEI LDKKVEKVTI SNRLVSSPCC IVTSTYGWTA 

       610        620        630        640        650        660 
NMERIMKAQA LRDNSTMGYM MAKKHLEINP DHPIVETLRQ KAEADKNDKA VKDLVVLLFE 

       670        680        690        700        710        720 
TALLSSGFSL EDPQTHSNRI YRMIKLGLGI DEDEVAAEEP NAAVPDEIPP LEGDEDASRM 


EEVD 

« Hide

References

« Hide 'large scale' references
[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]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Proteomic identification of proteins conjugated to ISG15 in mouse and human cells."
Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J., Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.
Biochem. Biophys. Res. Commun. 336:496-506(2005) [PubMed] [Europe PMC] [Abstract]
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]"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes."
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.
J. Proteome Res. 5:3135-3144(2006) [PubMed] [Europe PMC] [Abstract]
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]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
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]"Role of the cochaperone Tpr2 in Hsp90 chaperoning."
Moffatt N.S., Bruinsma E., Uhl C., Obermann W.M., Toft D.
Biochemistry 47:8203-8213(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DNAJC7.
[26]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[27]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[33]"The first identification of lysine malonylation substrates and its regulatory enzyme."
Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y., He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C., Dai J., Verdin E., Ye Y., Zhao Y.
Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011) [PubMed] [Europe PMC] [Abstract]
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]"Structure-activity relationships in purine-based inhibitor binding to HSP90 isoforms."
Wright L., Barril X., Dymock B., Sheridan L., Surgenor A., Beswick M., Drysdale M., Collier A., Massey A., Davies N., Fink A., Fromont C., Aherne W., Boxall K., Sharp S., Workman P., Hubbard R.E.
Chem. Biol. 11:775-785(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 1-221 IN COMPLEX WITH PURINE ANALOG.
[36]"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.
[37]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRHHHU84. A29461.
T46243.
RefSeqNP_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.
UniGeneHs.509736.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1QZ2X-ray3.00G/H720-724[»]
1UYMX-ray2.45A2-221[»]
3NMQX-ray2.20A1-223[»]
3PRYX-ray2.28A/B/C284-543[»]
ProteinModelPortalP08238.
SMRP08238. Positions 8-691.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109558. 217 interactions.
DIPDIP-413N.
IntActP08238. 454 interactions.
MINTMINT-99712.
STRING9606.ENSP00000325875.

Chemistry

BindingDBP08238.
ChEMBLCHEMBL4303.

PTM databases

PhosphoSiteP08238.

Polymorphism databases

DMDM17865718.

2D gel databases

OGPP08238.

Proteomic databases

PaxDbP08238.
PeptideAtlasP08238.
PRIDEP08238.

Protocols and materials databases

DNASU3326.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000353801; ENSP00000325875; ENSG00000096384.
ENST00000371554; ENSP00000360609; ENSG00000096384.
ENST00000371646; ENSP00000360709; ENSG00000096384.
GeneID3326.
KEGGhsa:3326.
UCSCuc003oxa.2. human.

Organism-specific databases

CTD3326.
GeneCardsGC06P044214.
H-InvDBHIX0031498.
HIX0057380.
HGNCHGNC:5258. HSP90AB1.
HPACAB005230.
HPA055729.
MIM140572. gene.
neXtProtNX_P08238.
PharmGKBPA29524.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0326.
HOGENOMHOG000031988.
HOVERGENHBG007374.
InParanoidP08238.
KOK04079.
OMAFAPKRAP.
OrthoDBEOG780RM0.
PhylomeDBP08238.
TreeFamTF300686.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressP08238.
BgeeP08238.
CleanExHS_HSP90AB1.
GenevestigatorP08238.

Family and domain databases

Gene3D3.30.565.10. 2 hits.
HAMAPMF_00505. HSP90.
InterProIPR003594. HATPase_ATP-bd.
IPR019805. Heat_shock_protein_90_CS.
IPR001404. Hsp90_fam.
IPR020575. Hsp90_N.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]
PANTHERPTHR11528. PTHR11528. 1 hit.
PfamPF02518. HATPase_c. 1 hit.
PF00183. HSP90. 1 hit.
[Graphical view]
PIRSFPIRSF002583. Hsp90. 1 hit.
PRINTSPR00775. HEATSHOCK90.
SMARTSM00387. HATPase_c. 1 hit.
[Graphical view]
SUPFAMSSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 1 hit.
PROSITEPS00298. HSP90. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHSP90AB1. human.
EvolutionaryTraceP08238.
GeneWikiHSP90AB1.
GenomeRNAi3326.
NextBio13182.
PROP08238.
SOURCESearch...

Entry information

Entry nameHS90B_HUMAN
AccessionPrimary (citable) accession number: P08238
Secondary accession number(s): B2R5P0 expand/collapse secondary AC list , Q5T9W7, Q9NQW0, Q9NTK6
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 185 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM