Reviewed, UniProtKB/Swiss-Prot P08238 (HS90B_HUMAN)

Names and origin

Protein names

Recommended name:
    Heat shock protein HSP 90-beta
      Short name=HSP 90
Alternative name(s):
    HSP 84

Gene names

Name:	HSP90AB1
Synonyms:	HSP90B, HSPC2, HSPCB

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	724 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Molecular chaperone. Has ATPase activity. Ref.21
Subunit structure	Homodimer. Interacts with TP53/p53 By similarity. Interacts with UNC45A. Binding to UNC45A involves 2 UNC45A monomers per HSP90AB1 dimer.
Subcellular location	Cytoplasm. Melanosome. Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Ref.19
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.9 Ref.10 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31
Sequence similarities	Belongs to the heat shock protein 90 family.
Sequence caution	The sequence CAB66478.1 differs from that shown. Reason: Frameshift at position 709.

Ontologies

Keywords
Biological process	Stress response
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Chaperone
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	negative regulation of proteasomal ubiquitin-dependent protein catabolic process Inferred from mutant phenotype. Source: MGI positive regulation of nitric oxide biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB protein folding Inferred from electronic annotation. Source: InterPro regulation of interferon-gamma-mediated signaling pathway Inferred from mutant phenotype. Source: MGI regulation of type I interferon-mediated signaling pathway Inferred from mutant phenotype. Source: MGI response to unfolded protein Ref.2 Non-traceable author statement. Source: UniProtKB
Cellular component	melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW TPR domain binding Inferred from sequence or structural similarity. Source: UniProtKB nitric-oxide synthase regulator activity Inferred from sequence or structural similarity. Source: UniProtKB unfolded protein binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CHEK1	O14757	1	EBI-352572,EBI-974488
RAF1	P04049	1	EBI-352572,EBI-365996

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.9

Chain

2 – 724

723

Heat shock protein HSP 90-beta

PRO_0000062917

Amino acid modifications

Modified residue

226

1

Phosphoserine Ref.18 Ref.22 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31

Modified residue

255

1

Phosphoserine Ref.10 Ref.14 Ref.16 Ref.17 Ref.18 Ref.22 Ref.23 Ref.25 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31

Modified residue

261

1

Phosphoserine Ref.14 Ref.22 Ref.29 Ref.30

Modified residue

297

1

Phosphothreonine Ref.26

Modified residue

305

1

Phosphotyrosine By similarity

Modified residue

307

1

Phosphoserine Ref.30

Modified residue

452

1

Phosphoserine Ref.30

Modified residue

484

1

Phosphotyrosine Ref.15 Ref.24

Modified residue

532

1

Phosphoserine Ref.30

Modified residue

624

1

N6-acetyllysine Ref.20

Modified residue

718

1

Phosphoserine Ref.30

Natural variations

Natural variant

349

1

K → E: dbSNP rs11538975.

VAR_049624

Experimental info

Sequence conflict

147

1

T → R in AAA36025. Ref.1

Sequence conflict

177

1

R → M in AAA36025. Ref.1

Sequence conflict

403

1

V → A in CAB66478. Ref.5

Secondary structure

1

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724

Helix Strand Turn

Details...

Beta strand

13 – 16

4

Helix

19 – 30

12

Helix

38 – 57

20

Turn

58 – 60

3

Helix

62 – 65

4

Beta strand

73 – 78

6

Turn

79 – 82

4

Beta strand

83 – 88

6

Helix

95 – 99

5

Helix

101 – 117

17

Turn

118 – 120

3

Helix

123 – 129

7

Helix

132 – 138

7

Beta strand

140 – 148

9

Beta strand

155 – 159

5

Beta strand

164 – 169

6

Beta strand

176 – 185

10

Helix

187 – 193

7

Helix

195 – 205

11

Beta strand

213 – 215

3

Sequences

	Sequence		Length	Mass (Da)
	P08238-1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: A93118C214D03810	FASTA	724	83,264
	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

References

	« Hide 'large scale' referencesShow '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: 3301534] [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: 2768249] [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: 2469626] [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. , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A. Genome Res. 11:422-435(2001) [PubMed: 11230166] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Amygdala.
[6]	NHLBI resequencing and genotyping service (RS&G) Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]	"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: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Colon, Lymph, Muscle, Skin and Testis.
[9]	"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: 2492519] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-21, PHOSPHORYLATION.
[10]	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, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[11]	"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: 8180474] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 51-118.
[12]	"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: 9150948] [Abstract] Cited for: PROTEIN SEQUENCE OF 54-64 AND 187-199. Tissue: Colon carcinoma.
[13]	"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.
[14]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255 AND SER-261, MASS SPECTROMETRY. Tissue: Epithelium.
[15]	"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: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-484, MASS SPECTROMETRY.
[16]	"Phosphoproteomic analysis of synaptosomes from human cerebral cortex." DeGiorgis J.A., Jaffe H., Moreira J.E., Carlotti C.G. Jr., Leite J.P., Pant H.C., Dosemeci A. J. Proteome Res. 4:306-315(2005) [PubMed: 15822905] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, MASS SPECTROMETRY. Tissue: Brain cortex.
[17]	"Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry." Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J., Bodenmiller B., Watts J.D., Hood L., Aebersold R. Nat. Methods 2:591-598(2005) [PubMed: 16094384] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, MASS SPECTROMETRY. Tissue: T-cell.
[18]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226 AND SER-255, MASS SPECTROMETRY. Tissue: Epithelium.
[19]	"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: 17081065] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[20]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-624, MASS SPECTROMETRY. Tissue: Epithelium.
[21]	"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: 16478993] [Abstract] Cited for: FUNCTION, INTERACTION WITH UNC45A.
[22]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226; SER-255 AND SER-261, MASS SPECTROMETRY. Tissue: Epithelium.
[23]	"Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, MASS SPECTROMETRY. Tissue: Epithelium.
[24]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-484, MASS SPECTROMETRY.
[25]	"Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line." Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S. Electrophoresis 28:2027-2034(2007) [PubMed: 17487921] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, MASS SPECTROMETRY.
[26]	"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: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-297, MASS SPECTROMETRY.
[27]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226 AND SER-255, MASS SPECTROMETRY.
[28]	"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: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226 AND SER-255, MASS SPECTROMETRY. Tissue: Platelet.
[29]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226; SER-255 AND SER-261, MASS SPECTROMETRY.
[30]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226; SER-255; SER-261; SER-307; SER-452; SER-532 AND SER-718, MASS SPECTROMETRY.
[31]	"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: 18318008] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226 AND SER-255, MASS SPECTROMETRY. Tissue: Liver.
[32]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[33]	"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: 15217611] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 1-221 IN COMPLEX WITH PURINE ANALOG.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M16660 mRNA. Translation: AAA36025.1.
J04988 Genomic DNA. Translation: AAA36026.1.
AY359878 mRNA. Translation: AAQ63401.1.
AL136543 mRNA. Translation: CAB66478.1. Frameshift.
DQ314872 Genomic DNA. Translation: ABC40731.1.
AL139392 Genomic DNA. Translation: CAI20095.1.
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.
S70561 Genomic DNA. Translation: AAD14062.1.
AF275719 mRNA. Translation: AAF82792.1.

IPI

IPI00414676.

PIR

HHHU84. A29461.
T46243.

RefSeq

NP_031381.2.

UniGene

Hs.509736
Hs.689683

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1QZ2	X-ray	3.00	G/H	720-724	[»]
1UYM	X-ray	2.45	A	2-221	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:413N.

IntAct

P08238. 74 interactions.

PTM databases

PhosphoSite

P08238.

2-D gel databases

HSC-2DPAGE

P08238.

OGP

P08238.

Proteomic databases

PeptideAtlas

P08238.

PRIDE

P08238.

Genome annotation databases

Ensembl

ENSG00000096384. Homo sapiens. [Contig view]

GeneID

3326.

KEGG

hsa:3326.

NMPDR

fig|9606.3.peg.27233.

UCSC

uc003oxa.1. human.

Organism-specific databases

GeneCards

GC06P044324.

H-InvDB

HIX0005922.
HIX0059399.

HGNC

HGNC:5258. HSP90AB1.

HPA

CAB005230.

MIM

140572. gene.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P08238.

OMA

P08238. EVLYMTE.

Gene expression databases

Bgee

P08238.

CleanEx

HS_HSP90AB1.

GermOnline

ENSG00000096384. Homo sapiens.

Family and domain databases

InterPro

IPR003594. ATP_bd_ATPase.
IPR019805. Heat_shock_protein_90_CS.
IPR001404. Hsp90.
[Graphical view]

Gene3D

G3DSA:3.30.565.10. ATP_bd_ATPase. 1 hit.

PANTHER

PTHR11528. Hsp90. 1 hit.

Pfam

PF02518. HATPase_c. 1 hit.
PF00183. HSP90. 1 hit.
[Graphical view]

PIRSF

PIRSF002583. Hsp90. 1 hit.

PRINTS

PR00775. HEATSHOCK90.

SMART

SM00387. HATPase_c. 1 hit.
[Graphical view]

PROSITE

PS00298. HSP90. 1 hit.
[Graphical view]

ProtoNet

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Other Resources

NextBio

13182.

SOURCE

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Entry information

Entry name

HS90B_HUMAN

Accession

Primary (citable) accession number: P08238
Secondary accession number(s): Q5T9W7, Q9NQW0, Q9NTK6

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	January 23, 2007
Last modified:	July 7, 2009
This is version 130 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)