P08238 (HS90B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	HSP90AB1
Synonyms:	HSP90B, HSPC2, HSPCB

Organism

Homo sapiens (Human)

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 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.25 Ref.40
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.16 Ref.25 Ref.34
Subcellular location	Cytoplasm. Melanosome. Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Ref.16 Ref.23
Domain	The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins By similarity.
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.11 Ref.12 Ref.17 Ref.19 Ref.20 Ref.21 Ref.22 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.35 Ref.36 Ref.37 Ref.38 Ref.39 Ref.41 Ref.42 Ref.43 Ubiquitinated in the presence of STUB1-UBE2D1 complex (in vitro). Ref.33 ISGylated. Ref.18 S-nitrosylated; negatively regulates the ATPase activity Probable.
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 S-nitrosylation Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	activation of innate immune response Traceable author statement. Source: Reactome axon guidance Traceable author statement. Source: Reactome innate immune response Traceable author statement. Source: Reactome 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 Non-traceable author statement Ref.2. Source: UniProtKB
Cellular component	cytosol Traceable author statement. Source: Reactome 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 protein serine/threonine kinase activity Traceable author statement. Source: Reactome unfolded protein binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RAF1	P04049	2	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.11

Chain

2 – 724

723

Heat shock protein HSP 90-beta

PRO_0000062917

Regions

Motif

720 – 724

5

TPR repeat-binding

Sites

Binding site

46

1

ATP By similarity

Binding site

88

1

ATP

Binding site

107

1

ATP By similarity

Binding site

133

1

ATP; via amide nitrogen By similarity

Binding site

392

1

ATP By similarity

Amino acid modifications

Modified residue

226

1

Phosphoserine Ref.22 Ref.26 Ref.31 Ref.32 Ref.35 Ref.37 Ref.38 Ref.39

Modified residue

255

1

Phosphoserine Ref.12 Ref.17 Ref.20 Ref.21 Ref.22 Ref.26 Ref.27 Ref.29 Ref.31 Ref.32 Ref.35 Ref.37 Ref.38 Ref.39 Ref.42 Ref.43

Modified residue

261

1

Phosphoserine Ref.17 Ref.26 Ref.36 Ref.37 Ref.38

Modified residue

275

1

N6-acetyllysine Ref.44

Modified residue

284

1

N6-acetyllysine Ref.44

Modified residue

297

1

Phosphothreonine Ref.30

Modified residue

305

1

Phosphotyrosine By similarity

Modified residue

307

1

Phosphoserine Ref.38

Modified residue

354

1

N6-acetyllysine Ref.44

Modified residue

399

1

N6-acetyllysine Ref.44

Modified residue

402

1

N6-acetyllysine Ref.44

Modified residue

435

1

N6-acetyllysine Ref.44

Modified residue

452

1

Phosphoserine Ref.38

Modified residue

481

1

N6-acetyllysine Ref.44

Modified residue

484

1

Phosphotyrosine Ref.19 Ref.28 Ref.41

Modified residue

532

1

Phosphoserine Ref.38

Modified residue

568

1

N6-acetyllysine Ref.44

Modified residue

590

1

S-nitrosocysteine Probable

Modified residue

624

1

N6-acetyllysine Ref.24

Modified residue

718

1

Phosphoserine Ref.38

Natural variations

Natural variant

349

1

K → E. [dbSNP:rs11538975]

VAR_049624

Experimental info

Mutagenesis

590

1

C → A, N or D: Reduced ATPase activity and client protein activation. Ref.40

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 [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]	"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: 14702039] [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: 14574404] [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. , 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: 15489334] [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: 2492519] [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, 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: 8180474] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 51-118.
[14]	"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.
[15]	"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.
[16]	"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: 9482106] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CDK6 AND CDC37.
[17]	"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: Cervix carcinoma.
[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: 16139798] [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: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-484, MASS SPECTROMETRY.
[20]	"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.
[21]	"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: Leukemic T-cell.
[22]	"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: Cervix carcinoma.
[23]	"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. Tissue: Melanoma.
[24]	"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: Cervix carcinoma.
[25]	"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.
[26]	"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: Cervix carcinoma.
[27]	"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: Cervix adenocarcinoma.
[28]	"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. Tissue: Lung carcinoma.
[29]	"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. Tissue: Prostate cancer.
[30]	"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. Tissue: Embryonic kidney.
[31]	"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. Tissue: Embryonic kidney.
[32]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226 AND SER-255, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[33]	"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: 18042044] [Abstract] Cited for: UBIQUITINATION.
[34]	"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: 18620420] [Abstract] Cited for: INTERACTION WITH DNAJC7.
[35]	"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.
[36]	"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment." Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J. J. Proteome Res. 7:5167-5176(2008) [PubMed: 19367720] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, MASS SPECTROMETRY. Tissue: T-cell.
[37]	"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. Tissue: Cervix carcinoma.
[38]	"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. Tissue: Cervix carcinoma.
[39]	"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.
[40]	"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: 19696785] [Abstract] Cited for: FUNCTION, S-NITROSYLATION AT CYS-590, MUTAGENESIS OF CYS-590.
[41]	"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells." Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J. J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-484, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[42]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, MASS SPECTROMETRY.
[43]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[44]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-275; LYS-284; LYS-354; LYS-399; LYS-402; LYS-435; LYS-481 AND LYS-568, MASS SPECTROMETRY.
[45]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[46]	"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.
[47]	"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: 15159550] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 720-724 IN COMPLEX WITH FKBP4.
[48]	"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.
S70561 Genomic DNA. Translation: AAD14062.1.
AF275719 mRNA. Translation: AAF82792.1.

IPI

IPI00414676.

PIR

HHHU84. A29461.
T46243.

RefSeq

NP_031381.2. NM_007355.2.

UniGene

Hs.509736.
Hs.696394.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1QZ2	X-ray	3.00	G/H	720-724	[»]
1UYM	X-ray	2.45	A	2-221	[»]
3NMQ	X-ray	2.20	A	1-223	[»]
3PRY	X-ray	2.28	A/B/C	284-543	[»]

ProteinModelPortal

P08238.

SMR

P08238. Positions 8-691.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-413N.

IntAct

P08238. 78 interactions.

MINT

MINT-99712.

STRING

P08238.

PTM databases

PhosphoSite

P08238.

Polymorphism databases

DMDM

17865718.

2D gel databases

OGP

P08238.

Proteomic databases

PeptideAtlas

P08238.

PRIDE

P08238.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000353801; ENSP00000325875; ENSG00000096384.
ENST00000371554; ENSP00000360609; ENSG00000096384.
ENST00000371646; ENSP00000360709; ENSG00000096384.

GeneID

3326.

KEGG

hsa:3326.

NMPDR

fig|9606.3.peg.27233.

UCSC

uc003oxa.1. human.

Organism-specific databases

CTD

3326.

GeneCards

GC06P044214.

H-InvDB

HIX0005922.

HGNC

HGNC:5258. HSP90AB1.

HPA

CAB005230.

MIM

140572. gene.

neXtProt

NX_P08238.

PharmGKB

PA29524.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

HBG631012.

HOVERGEN

HBG007374.

InParanoid

P08238.

OMA

GFSKNIK.

OrthoDB

EOG42V8FM.

PhylomeDB

P08238.

Enzyme and pathway databases

Reactome

REACT_111045. Developmental Biology.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P08238.

Bgee

P08238.

CleanEx

HS_HSP90AB1.

Genevestigator

P08238.

GermOnline

ENSG00000096384. Homo sapiens.

Family and domain databases

InterPro

IPR003594. ATPase-like_ATP-bd.
IPR019805. Heat_shock_protein_90_CS.
IPR001404. Hsp90.
IPR020575. Hsp90_N.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]

Gene3D

G3DSA:3.30.565.10. ATP_bd_ATPase. 2 hits.

KO

K04079.

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]

SUPFAM

SSF55874. ATP_bd_ATPase. 1 hit.
SSF54211. Ribosomal_S5_D2-typ_fold. 1 hit.

PROSITE

PS00298. HSP90. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

13182.

SOURCE

Search...

Entry information

Entry name

HS90B_HUMAN

Accession

Primary (citable) accession number: P08238
Secondary accession number(s): B2R5P0 , Q5T9W7, Q9NQW0, Q9NTK6

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 161 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.