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) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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.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.
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.
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 process	Stress response
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Chaperone
PTM	Acetylation Glycoprotein Phosphoprotein S-nitrosylation Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	axon guidance Traceable author statement. Source: Reactome cellular response to organic cyclic compound Inferred from electronic annotation. Source: Compara innate immune response Traceable author statement. Source: Reactome negative regulation of neuron apoptotic process Inferred from electronic annotation. Source: Compara 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: Compara positive regulation of cell size Inferred from electronic annotation. Source: Compara 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: Compara positive regulation of protein import into nucleus, translocation Inferred from electronic annotation. Source: Compara positive regulation of protein serine/threonine kinase activity Inferred from electronic annotation. Source: Compara 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: Compara response to unfolded protein Non-traceable author statement Ref.2. Source: UniProtKB
Cellular_component	apical plasma membrane Inferred from electronic annotation. Source: Compara basolateral plasma membrane Inferred from electronic annotation. Source: Compara brush border membrane Inferred from electronic annotation. Source: Compara cell surface Inferred from electronic annotation. Source: Compara cytosol Traceable author statement. Source: Reactome inclusion body Inferred from electronic annotation. Source: Compara melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW CTP binding Inferred from electronic annotation. Source: Compara GTP binding Inferred from electronic annotation. Source: Compara TPR domain binding Inferred from sequence or structural similarity. Source: UniProtKB UTP binding Inferred from electronic annotation. Source: Compara dATP binding Inferred from electronic annotation. Source: Compara nitric-oxide synthase regulator activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ACVR1B	P36896	2	EBI-352572,EBI-1384128
AKT2	P31751	2	EBI-352572,EBI-296058
ALK	Q9UM73	2	EBI-352572,EBI-357361
AMHR2	Q16671	2	EBI-352572,EBI-6423788
ARAF	P10398	3	EBI-352572,EBI-365961
AURKB	Q96GD4	2	EBI-352572,EBI-624291
BRAF	P15056	2	EBI-352572,EBI-365980
BTK	Q06187	2	EBI-352572,EBI-624835
CAMK2G	Q13555	2	EBI-352572,EBI-1383465
CDC37	Q16543	3	EBI-352572,EBI-295634
CDK10	Q15131	2	EBI-352572,EBI-1646959
CDK14	O94921	2	EBI-352572,EBI-1043945
CDK15	Q96Q40	2	EBI-352572,EBI-1051975
CDK4	P11802	3	EBI-352572,EBI-295644
CDK6	Q00534	2	EBI-352572,EBI-295663
CDK9	P50750	2	EBI-352572,EBI-1383449
CHEK1	O14757	3	EBI-352572,EBI-974488
CSNK1E	P49674	2	EBI-352572,EBI-749343
CUL3	Q13618	2	EBI-352572,EBI-456129
DDR2	Q16832	2	EBI-352572,EBI-1381484
EGFR	P00533	3	EBI-352572,EBI-297353
EPHA2	P29317	2	EBI-352572,EBI-702104
ERBB2	P04626	2	EBI-352572,EBI-641062
ERBB4	Q15303	2	EBI-352572,EBI-80371
FGFR3	P22607	2	EBI-352572,EBI-348399
FGR	P09769	2	EBI-352572,EBI-1383732
FLT4	P35916	2	EBI-352572,EBI-1005467
FYN	P06241	2	EBI-352572,EBI-515315
GSG2	Q8TF76	2	EBI-352572,EBI-1237328
GSK3A	P49840	2	EBI-352572,EBI-1044067
ICK	Q9UPZ9	2	EBI-352572,EBI-6381479
KLHL38	Q2WGJ6	2	EBI-352572,EBI-6426443
LCK	P06239	2	EBI-352572,EBI-1348
LIMK2	P53671	2	EBI-352572,EBI-1384350
MAP3K8	P41279	2	EBI-352572,EBI-354900
MAP3K9	P80192	2	EBI-352572,EBI-3951604
MAPK4	P31152	2	EBI-352572,EBI-3906061
MATK	P42679	2	EBI-352572,EBI-751664
MUSK	O15146	2	EBI-352572,EBI-6423196
NEK9	Q8TD19	2	EBI-352572,EBI-1044009
NR1I2	O75469	2	EBI-352572,EBI-3905991
POGK	Q9P215	2	EBI-352572,EBI-2555775
PRKAA1	Q13131	2	EBI-352572,EBI-1181405
PRKACB	P22694	2	EBI-352572,EBI-2679622
PRKCE	Q02156	2	EBI-352572,EBI-706254
PRKCZ	Q05513	2	EBI-352572,EBI-295351
PRKD1	Q15139	2	EBI-352572,EBI-1181072
PRKX	P51817	2	EBI-352572,EBI-4302903
PSKH1	P11801	2	EBI-352572,EBI-3922781
RAF1	P04049	3	EBI-352572,EBI-365996
RGS6	P49758	2	EBI-352572,EBI-6426927
ROR2	Q01974	2	EBI-352572,EBI-6422642
RPS6KA1	Q15418	2	EBI-352572,EBI-963034
STK11	Q15831	3	EBI-352572,EBI-306838
STK38	Q15208	2	EBI-352572,EBI-458376
TESK2	Q96S53	2	EBI-352572,EBI-1384110
TSSK6	Q9BXA6	3	EBI-352572,EBI-851883
TYK2	P29597	2	EBI-352572,EBI-1383454

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.26 Ref.28 Ref.31 Ref.34

Modified residue

255

1

Phosphoserine Ref.12 Ref.20

Modified residue

261

1

Phosphoserine

Modified residue

275

1

N6-acetyllysine

Modified residue

284

1

N6-acetyllysine

Modified residue

297

1

Phosphothreonine Ref.23

Modified residue

305

1

Phosphotyrosine By similarity

Modified residue

307

1

Phosphoserine Ref.27

Modified residue

354

1

N6-acetyllysine

Modified residue

399

1

N6-acetyllysine; alternate

Modified residue

399

1

N6-malonyllysine; alternate Ref.33

Modified residue

402

1

N6-acetyllysine

Modified residue

435

1

N6-acetyllysine Ref.30

Modified residue

452

1

Phosphoserine; alternate

Modified residue

481

1

N6-acetyllysine Ref.30

Modified residue

484

1

Phosphotyrosine

Modified residue

532

1

Phosphoserine

Modified residue

568

1

N6-acetyllysine

Modified residue

590

1

S-nitrosocysteine Probable

Modified residue

624

1

N6-acetyllysine

Modified residue

718

1

Phosphoserine

Glycosylation

434

1

O-linked (GlcNAc...) By similarity

Glycosylation

452

1

O-linked (GlcNAc...); alternate By similarity

Natural variations

Natural variant

349

1

K → E.
Corresponds to variant rs11538975 [ dbSNP | Ensembl ].

VAR_049624

Experimental info

Mutagenesis

590

1

C → A, N or D: Reduced ATPase activity and client protein activation. Ref.29

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

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724

Helix Strand Turn

Details...

Beta strand

13 – 16

4

Helix

19 – 30

12

Helix

38 – 60

23

Helix

62 – 65

4

Beta strand

73 – 78

6

Turn

79 – 82

4

Beta strand

83 – 88

6

Helix

95 – 99

5

Helix

101 – 118

18

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

Helix

288 – 290

3

Helix

293 – 295

3

Helix

298 – 309

12

Beta strand

316 – 323

8

Beta strand

325 – 327

3

Beta strand

329 – 335

7

Beta strand

353 – 357

5

Beta strand

360 – 364

5

Helix

367 – 369

3

Helix

372 – 374

3

Beta strand

378 – 386

9

Helix

395 – 420

26

Helix

423 – 443

21

Helix

445 – 447

3

Helix

448 – 453

6

Beta strand

456 – 459

4

Turn

460 – 464

5

Helix

469 – 474

6

Beta strand

482 – 486

5

Helix

491 – 495

5

Helix

498 – 504

7

Turn

505 – 507

3

Beta strand

510 – 512

3

Helix

518 – 525

8

Beta strand

531 – 535

5

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] [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. , 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. , 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]	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] [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, 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, MASS SPECTROMETRY. 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], MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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.

IPI

IPI00414676.

PIR

HHHU84. A29461.
T46243.

RefSeq

NP_001258898.1. NM_001271969.1.
NP_001258899.1. NM_001271970.1.
NP_001258900.1. NM_001271971.1.
NP_031381.2. NM_007355.3.

UniGene

Hs.509736.

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.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-413N.

IntAct

P08238. 463 interactions.

MINT

MINT-99712.

STRING

9606.ENSP00000325875.

PTM databases

PhosphoSite

P08238.

Polymorphism databases

DMDM

17865718.

2D gel databases

OGP

P08238.

Proteomic databases

PaxDb

P08238.

PeptideAtlas

P08238.

PRIDE

P08238.

Protocols and materials databases

DNASU

3326.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

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

GeneID

3326.

KEGG

hsa:3326.

UCSC

uc003oxa.1. human.

Organism-specific databases

CTD

3326.

GeneCards

GC06P044214.

H-InvDB

HIX0031498.
HIX0057380.

HGNC

HGNC:5258. HSP90AB1.

HPA

CAB005230.

MIM

140572. gene.

neXtProt

NX_P08238.

PharmGKB

PA29524.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0326.

HOGENOM

HOG000031988.

HOVERGEN

HBG007374.

InParanoid

P08238.

KO

K04079.

OMA

MEYLEPR.

OrthoDB

EOG42V8FM.

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

Gene3D

3.30.565.10. 2 hits.

InterPro

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

PANTHER

PTHR11528. PTHR11528. 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

BindingDB

P08238.

ChEMBL

CHEMBL4303.

ChiTaRS

HSP90AB1. human.

EvolutionaryTrace

P08238.

GenomeRNAi

3326.

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:	May 1, 2013
This is version 175 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.