Reviewed, UniProtKB/Swiss-Prot P07900 (HS90A_HUMAN)

Names and origin

Protein names

Recommended name:
Heat shock protein HSP 90-alpha

Alternative name(s):
Heat shock 86 kDa
Short name=HSP 86
Short name=HSP86
Renal carcinoma antigen NY-REN-38

Gene names

Name:	HSP90AA1
Synonyms:	HSP90A, HSPC1, HSPCA

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	732 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 By similarity.
Subunit structure	Homodimer. Interacts with AHSA1, FNIP1, HSF1, SMYD3 and TOM34. Interacts with TERT; the interaction, together with PTGES3/P23, is required for correct assembly and stabilization of the TERT holoenzyme complex.
Subcellular location	Cytoplasm. Melanosome. Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Ref.25
Sequence similarities	Belongs to the heat shock protein 90 family.

Ontologies

Keywords
Biological process	Stress response
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
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	cellular chaperone-mediated protein complex assembly Inferred from direct assay. Source: UniProtKB mitochondrial outer membrane translocase complex assembly Inferred from direct assay. Source: UniProtKB mitochondrial transport Traceable author statement. Source: UniProtKB positive regulation of nitric oxide biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB protein refolding Ref.17 Traceable author statement. Source: UniProtKB response to unfolded protein Ref.3 Non-traceable author statement. Source: UniProtKB signal transduction Non-traceable author statement. Source: UniProtKB
Cellular component	cytosol Non-traceable author statement. Source: UniProtKB melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Traceable author statement. Source: UniProtKB TPR domain binding Ref.17 Inferred from direct assay. Source: UniProtKB nitric-oxide synthase regulator activity Inferred from sequence or structural similarity. Source: UniProtKB protein homodimerization activity Traceable author statement. Source: UniProtKB unfolded protein binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
LSM1	O15116	1	EBI-296047,EBI-347619
MMP2	P08253	1	EBI-296047,EBI-1033518
NDRG1	Q92597	1	EBI-296047,EBI-716486
RPS3A	P61247	1	EBI-296047,EBI-352378
STUB1	Q9UNE7	2	EBI-296047,EBI-357085

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P07900-1) Also known as: HSP90AA1-1; HSP90-alpha 2; This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P07900-2) Also known as: HSP90AA1-2; The sequence of this isoform differs from the canonical sequence as follows:      1-1: M → MPPCSGGDGS...QPFILLRLLM
Sequence annotation (Features)
	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
	Natural variant	71	1	M → L: dbSNP rs8005905.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.14

Chain

2 – 732

731

Heat shock protein HSP 90-alpha

PRO_0000062911

Amino acid modifications

Modified residue

5

1

Phosphothreonine; by PRKDC Ref.15

Modified residue

7

1

Phosphothreonine; by PRKDC Ref.15

Modified residue

224

1

N6-acetyllysine Ref.36

Modified residue

231

1

Phosphoserine Ref.23 Ref.24 Ref.27 Ref.28 Ref.32

Modified residue

252

1

Phosphoserine Ref.24 Ref.28

Modified residue

263

1

Phosphoserine Ref.23 Ref.24 Ref.27 Ref.28 Ref.32 Ref.26 Ref.29 Ref.30 Ref.31 Ref.34

Modified residue

313

1

Phosphotyrosine By similarity

Modified residue

399

1

Phosphoserine Ref.35

Modified residue

410

1

N6-acetyllysine Ref.36

Modified residue

443

1

N6-acetyllysine Ref.36

Modified residue

458

1

N6-acetyllysine Ref.36

Modified residue

489

1

N6-acetyllysine Ref.36

Modified residue

492

1

Phosphotyrosine By similarity

Modified residue

576

1

N6-acetyllysine Ref.36

Modified residue

585

1

N6-acetyllysine Ref.36

Natural variations

Alternative sequence

1

1

M → MPPCSGGDGSTPPGPSLRDR DCPAQSAEYPRDRLDPRPGS PSEASSPPFLRSRAPVNWYQ EKAQVFLWHLMVSGSTTLLC LWKQPFHVSAFPVTASLAFR QSQGAGQHLYKDLQPFILLR LLM in isoform 2.

VSP_026604

Experimental info

Sequence conflict

63

1

S → T in CAA33259. Ref.1

Sequence conflict

74

1

K → R in CAI64495. Ref.4

Sequence conflict

74

1

K → R in BAG51711. Ref.6

Sequence conflict

86

1

D → G in CAI64495. Ref.4

Sequence conflict

86

1

D → G in BAG51711. Ref.6

Secondary structure

1

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732

Helix Strand Turn

Details...

Beta strand

18 – 21

4

Helix

24 – 35

12

Helix

43 – 65

23

Helix

67 – 70

4

Beta strand

78 – 83

6

Turn

84 – 87

4

Beta strand

88 – 93

6

Helix

100 – 104

5

Helix

106 – 108

3

Helix

111 – 123

13

Helix

128 – 134

7

Helix

137 – 143

7

Beta strand

145 – 153

9

Beta strand

160 – 164

5

Beta strand

169 – 174

6

Beta strand

181 – 190

10

Helix

192 – 198

7

Helix

200 – 210

11

Beta strand

218 – 220

3

Beta strand

728 – 730

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (HSP90AA1-1) (HSP90-alpha 2) [UniParc]. Last modified January 23, 2007. Version 5. Checksum: 969F65FCC0BC86FD	FASTA	732	84,660
	10 20 30 40 50 60 MPEETQTQDQ PMEEEEVETF AFQAEIAQLM SLIINTFYSN KEIFLRELIS NSSDALDKIR 70 80 90 100 110 120 YESLTDPSKL DSGKELHINL IPNKQDRTLT IVDTGIGMTK ADLINNLGTI AKSGTKAFME 130 140 150 160 170 180 ALQAGADISM IGQFGVGFYS AYLVAEKVTV ITKHNDDEQY AWESSAGGSF TVRTDTGEPM 190 200 210 220 230 240 GRGTKVILHL KEDQTEYLEE RRIKEIVKKH SQFIGYPITL FVEKERDKEV SDDEAEEKED 250 260 270 280 290 300 KEEEKEKEEK ESEDKPEIED VGSDEEEEKK DGDKKKKKKI KEKYIDQEEL NKTKPIWTRN 310 320 330 340 350 360 PDDITNEEYG EFYKSLTNDW EDHLAVKHFS VEGQLEFRAL LFVPRRAPFD LFENRKKKNN 370 380 390 400 410 420 IKLYVRRVFI MDNCEELIPE YLNFIRGVVD SEDLPLNISR EMLQQSKILK VIRKNLVKKC 430 440 450 460 470 480 LELFTELAED KENYKKFYEQ FSKNIKLGIH EDSQNRKKLS ELLRYYTSAS GDEMVSLKDY 490 500 510 520 530 540 CTRMKENQKH IYYITGETKD QVANSAFVER LRKHGLEVIY MIEPIDEYCV QQLKEFEGKT 550 560 570 580 590 600 LVSVTKEGLE LPEDEEEKKK QEEKKTKFEN LCKIMKDILE KKVEKVVVSN RLVTSPCCIV 610 620 630 640 650 660 TSTYGWTANM ERIMKAQALR DNSTMGYMAA KKHLEINPDH SIIETLRQKA EADKNDKSVK 670 680 690 700 710 720 DLVILLYETA LLSSGFSLED PQTHANRIYR MIKLGLGIDE DDPTADDTSA AVTEEMPPLE 730 GDDDTSRMEE VD
	Isoform 2 (HSP90AA1-2). Checksum: 404BD8CAD5E68DB0	FASTA	854	98,161
	10 20 30 40 50 60 MPPCSGGDGS TPPGPSLRDR DCPAQSAEYP RDRLDPRPGS PSEASSPPFL RSRAPVNWYQ 70 80 90 100 110 120 EKAQVFLWHL MVSGSTTLLC LWKQPFHVSA FPVTASLAFR QSQGAGQHLY KDLQPFILLR 130 140 150 160 170 180 LLMPEETQTQ DQPMEEEEVE TFAFQAEIAQ LMSLIINTFY SNKEIFLREL ISNSSDALDK 190 200 210 220 230 240 IRYESLTDPS KLDSGKELHI NLIPNKQDRT LTIVDTGIGM TKADLINNLG TIAKSGTKAF 250 260 270 280 290 300 MEALQAGADI SMIGQFGVGF YSAYLVAEKV TVITKHNDDE QYAWESSAGG SFTVRTDTGE 310 320 330 340 350 360 PMGRGTKVIL HLKEDQTEYL EERRIKEIVK KHSQFIGYPI TLFVEKERDK EVSDDEAEEK 370 380 390 400 410 420 EDKEEEKEKE EKESEDKPEI EDVGSDEEEE KKDGDKKKKK KIKEKYIDQE ELNKTKPIWT 430 440 450 460 470 480 RNPDDITNEE YGEFYKSLTN DWEDHLAVKH FSVEGQLEFR ALLFVPRRAP FDLFENRKKK 490 500 510 520 530 540 NNIKLYVRRV FIMDNCEELI PEYLNFIRGV VDSEDLPLNI SREMLQQSKI LKVIRKNLVK 550 560 570 580 590 600 KCLELFTELA EDKENYKKFY EQFSKNIKLG IHEDSQNRKK LSELLRYYTS ASGDEMVSLK 610 620 630 640 650 660 DYCTRMKENQ KHIYYITGET KDQVANSAFV ERLRKHGLEV IYMIEPIDEY CVQQLKEFEG 670 680 690 700 710 720 KTLVSVTKEG LELPEDEEEK KKQEEKKTKF ENLCKIMKDI LEKKVEKVVV SNRLVTSPCC 730 740 750 760 770 780 IVTSTYGWTA NMERIMKAQA LRDNSTMGYM AAKKHLEINP DHSIIETLRQ KAEADKNDKS 790 800 810 820 830 840 VKDLVILLYE TALLSSGFSL EDPQTHANRI YRMIKLGLGI DEDDPTADDT SAAVTEEMPP 850 LEGDDDTSRM EEVD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of a full-length cDNA for 90 kDa heat-shock protein from human peripheral blood lymphocytes." Soeda E., Yokoyama K., Yamazaki M., Akaogi K., Miwa T., Imai T. Nucleic Acids Res. 17:7108-7108(1989) [PubMed: 2780322] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Peripheral blood lymphocyte.
[2]	"Molecular cloning of cDNA encoding a human heat-shock protein whose expression is induced by adenovirus type 12 E1A in HeLa cells." Yamazaki M., Tashiro H., Yokoyama K., Soeda E. Agric. Biol. Chem. 54:3163-3170(1990) [PubMed: 1368637] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	"Sequence and regulation of a gene encoding a human 89-kilodalton heat shock protein." Hickey E., Brandon S.E., Smale G., Lloyd D., Weber L.A. Mol. Cell. Biol. 9:2615-2626(1989) [PubMed: 2527334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Placenta.
[4]	"The HSP90 family of genes in the human genome: insights into their divergence and evolution." Chen B., Piel W.H., Gui L., Bruford E., Monteiro A. Genomics 86:627-637(2005) [PubMed: 16269234] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
[5]	NHLBI resequencing and genotyping service (RS&G) Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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] (ISOFORMS 1 AND 2). Tissue: Placenta and Teratocarcinoma.
[7]	"The DNA sequence and analysis of human chromosome 14." Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J. Nature 421:601-607(2003) [PubMed: 12508121] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	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].
[9]	"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] OF 1-312.
[10]	"Cloning and analysis of a human 86-kDa heat-shock-protein-encoding gene." Walter T., Drabent B., Krebs H., Tomalak M., Heiss S., Benecke B.J.J. Gene 83:105-115(1989) [PubMed: 2591742] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-312.
[11]	Lubec G., Vishwanath V., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 101-112; 210-224; 300-314; 328-338; 346-355; 387-400; 465-478 AND 633-647, MASS SPECTROMETRY. Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[12]	"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] OF 185-732. Tissue: Placenta.
[13]	"The analysis of the genes reactive to monoclonal antibody, CE5." Tanaka M., Tanaka T., Mitsui Y., Yamamoto M., Wood J.N. Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 539-732. Tissue: Heart.
[14]	"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.
[15]	"The human double-stranded DNA-activated protein kinase phosphorylates the 90-kDa heat-shock protein, hsp90 alpha at two NH2-terminal threonine residues." Lees-Miller S.P., Anderson C.W. J. Biol. Chem. 264:17275-17280(1989) [PubMed: 2507541] [Abstract] Cited for: PHOSPHORYLATION AT THR-5 AND THR-7.
[16]	"Mechanism of dimer formation of the 90-kDa heat-shock protein." Nemoto T., Ohara-Nemoto Y., Ota M., Takagi T., Yokoyama K. Eur. J. Biochem. 233:1-8(1995) [PubMed: 7588731] [Abstract] Cited for: SUBUNIT.
[17]	"Specific binding of tetratricopeptide repeat proteins to the C-terminal 12-kDa domain of hsp90." Young J.C., Obermann W.M., Hartl F.U. J. Biol. Chem. 273:18007-18010(1998) [PubMed: 9660753] [Abstract] Cited for: INTERACTION WITH TOM34.
[18]	"Antigens recognized by autologous antibody in patients with renal-cell carcinoma." Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H., Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T., Old L.J. Int. J. Cancer 83:456-464(1999) [PubMed: 10508479] [Abstract] Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN. Tissue: Renal cell carcinoma.
[19]	"Stable association of hsp90 and p23, but Not hsp70, with active human telomerase." Forsythe H.L., Jarvis J.L., Turner J.W., Elmore L.W., Holt S.E. J. Biol. Chem. 276:15571-15574(2001) [PubMed: 11274138] [Abstract] Cited for: INTERACTION WITH TERT, FUNCTION AS A CO-CHAPERONE IN TELOMERASE HOLOENZYME ASSEMBLY.
[20]	"Evidence for a mechanism of repression of heat shock factor 1 transcriptional activity by a multichaperone complex." Guo Y., Guettouche T., Fenna M., Boellmann F., Pratt W.B., Toft D.O., Smith D.F., Voellmy R. J. Biol. Chem. 276:45791-45799(2001) [PubMed: 11583998] [Abstract] Cited for: INTERACTION WITH HSF1.
[21]	"Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone." Lotz G.P., Lin H., Harst A., Obermann W.M.J. J. Biol. Chem. 278:17228-17235(2003) [PubMed: 12604615] [Abstract] Cited for: INTERACTION WITH AHSA1.
[22]	"SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells." Hamamoto R., Furukawa Y., Morita M., Iimura Y., Silva F.P., Li M., Yagyu R., Nakamura Y. Nat. Cell Biol. 6:731-740(2004) [PubMed: 15235609] [Abstract] Cited for: INTERACTION WITH SMYD3.
[23]	"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-231 AND SER-263, MASS SPECTROMETRY. Tissue: Brain cortex.
[24]	"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-231; SER-252 AND SER-263, MASS SPECTROMETRY. Tissue: Epithelium.
[25]	"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.
[26]	"Phosphoproteomic analysis of the human pituitary." Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F. Pituitary 9:109-120(2006) [PubMed: 16807684] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, MASS SPECTROMETRY. Tissue: Pituitary.
[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-231 AND SER-263, 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-231; SER-252 AND SER-263, MASS SPECTROMETRY. Tissue: Platelet.
[29]	"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-263, MASS SPECTROMETRY. Tissue: T-cell.
[30]	"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-263, MASS SPECTROMETRY.
[31]	"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-263, MASS SPECTROMETRY.
[32]	"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-231 AND SER-263, MASS SPECTROMETRY. Tissue: Liver.
[33]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[34]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, MASS SPECTROMETRY.
[35]	"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-399, MASS SPECTROMETRY. Tissue: T-cell.
[36]	"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-224; LYS-410; LYS-443; LYS-458; LYS-489; LYS-576 AND LYS-585, MASS SPECTROMETRY.
[37]	"Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent." Stebbins C.E., Russo A.A., Schneider C., Rosen N., Hartl F.U., Pavletich N.P. Cell 89:239-250(1997) [PubMed: 9108479] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 11-223.
[38]	"In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis." Obermann W.M., Sondermann H., Russo A.A., Pavletich N.P., Hartl F.U. J. Cell Biol. 143:901-910(1998) [PubMed: 9817749] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 11-223.
[39]	"Folliculin encoded by the BHD gene interacts with a binding protein, FNIP1, and AMPK, and is involved in AMPK and mTOR signaling." Baba M., Hong S.-B., Sharma N., Warren M.B., Nickerson M.L., Iwamatsu A., Esposito D., Gillette W.K., Hopkins R.F. III, Hartley J.L., Furihata M., Oishi S., Zhen W., Burke T.R. Jr., Linehan W.M., Schmidt L.S., Zbar B. Proc. Natl. Acad. Sci. U.S.A. 103:15552-15557(2006) [PubMed: 17028174] [Abstract] Cited for: INTERACTION WITH FNIP1, IDENTIFICATION BY MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X15183 mRNA. Translation: CAA33259.1.
M27024 Genomic DNA. Translation: AAA63194.1.
AJ890082 mRNA. Translation: CAI64495.1.
AJ890083 mRNA. Translation: CAI64496.1.
DQ314871 Genomic DNA. Translation: ABC40730.1.
AK056446 mRNA. Translation: BAG51711.1.
AK291115 mRNA. Translation: BAF83804.1.
AK291607 mRNA. Translation: BAF84296.1.
AL133223 Genomic DNA. No translation available.
CH471061 Genomic DNA. Translation: EAW81765.1.
X07270 mRNA. Translation: CAA30255.1.
M30626 Genomic DNA. Translation: AAA36023.1.
BC000987 mRNA. Translation: AAH00987.1.
BC121062 mRNA. Translation: AAI21063.1.
D87666 mRNA. Translation: BAA13430.1.
D87666 mRNA. Translation: BAA13431.1.

IPI

IPI00382470.
IPI00784295.

PIR

HHHU86. A32319.

RefSeq

NP_001017963.2.
NP_005339.3.

UniGene

Hs.525600
Hs.700831

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BYQ	X-ray	1.50	A	9-236	[»]
1OSF	X-ray	1.75	A	9-223	[»]
1UY6	X-ray	1.90	A	1-236	[»]
1UY7	X-ray	1.90	A	1-236	[»]
1UY8	X-ray	1.98	A	1-236	[»]
1UY9	X-ray	2.00	A	1-236	[»]
1UYC	X-ray	2.00	A	1-236	[»]
1UYD	X-ray	2.00	A	1-236	[»]
1UYE	X-ray	2.00	A	1-236	[»]
1UYF	X-ray	2.00	A	1-236	[»]
1UYG	X-ray	2.00	A	1-236	[»]
1UYH	X-ray	2.20	A	1-236	[»]
1UYI	X-ray	2.00	A	1-236	[»]
1UYK	X-ray	2.00	A	1-236	[»]
1UYL	X-ray	1.40	A	1-236	[»]
1YC1	X-ray	1.70	A	9-235	[»]
1YC3	X-ray	2.12	A	9-235	[»]
1YC4	X-ray	1.81	A	9-235	[»]
1YER	X-ray	1.65	A	9-236	[»]
1YES	X-ray	2.20	A	9-236	[»]
1YET	X-ray	1.90	A	9-236	[»]
2BSM	X-ray	2.05	A	2-235	[»]
2BT0	X-ray	1.90	A/B	2-235	[»]
2BUG	NMR	-	B	-	[»]
2BYH	X-ray	1.90	A	11-235	[»]
2BYI	X-ray	1.60	A	11-235	[»]
2BZ5	X-ray	1.90	A/B	2-235	[»]
2C2L	X-ray	3.30	E/F/G/H	724-732	[»]
2CCS	X-ray	1.79	A	1-236	[»]
2CCT	X-ray	2.30	A	1-236	[»]
2CCU	X-ray	2.70	A	1-236	[»]
2CDD	X-ray	1.90	A/B	1-236	[»]
2FWY	X-ray	2.10	A	1-236	[»]
2FWZ	X-ray	2.10	A	1-236	[»]
2H55	X-ray	2.00	A	1-236	[»]
2JJC	X-ray	1.95	A	9-223	[»]
2K5B	NMR	-	A	14-223	[»]
2QF6	X-ray	3.10	A/B/C/D	17-223	[»]
2QFO	X-ray	1.68	A/B	17-223	[»]
2QG0	X-ray	1.85	A/B	17-223	[»]
2QG2	X-ray	1.80	A	17-223	[»]
2UWD	X-ray	1.90	A	2-235	[»]
2VCI	X-ray	2.00	A	1-236	[»]
2VCJ	X-ray	2.50	A	1-236	[»]
2WI1	X-ray	2.30	A	1-236	[»]
2WI2	X-ray	2.09	A/B	1-236	[»]
2WI3	X-ray	1.90	A	1-236	[»]
2WI4	X-ray	2.40	A	1-236	[»]
2WI5	X-ray	2.10	A	1-236	[»]
2WI6	X-ray	2.18	A	1-236	[»]
2WI7	X-ray	2.50	A	1-236	[»]
3BM9	X-ray	1.60	A	14-236	[»]
3BMY	X-ray	1.60	A	14-236	[»]
3D0B	X-ray	1.74	A	1-232	[»]
3EKO	X-ray	1.55	A/B	9-225	[»]
3EKR	X-ray	2.00	A/B	9-225	[»]
3FT5	X-ray	1.90	A	9-236	[»]
3FT8	X-ray	2.00	A	9-236	[»]
3HEK	X-ray	1.95	A/B	9-225	[»]
3HHU	X-ray	1.59	A/B	1-224	[»]

SMR

P07900. Positions 293-696.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-27595N.

IntAct

P07900. 47 interactions.

STRING

P07900.

PTM databases

PhosphoSite

P07900.

2-D gel databases

OGP

P07900.

REPRODUCTION-2DPAGE

IPI00784295.

Proteomic databases

PRIDE

P07900.

Genome annotation databases

Ensembl

ENST00000216281; ENSP00000216281; ENSG00000080824; Homo sapiens. [Genome view]
ENST00000334701; ENSP00000335153; ENSG00000080824; Homo sapiens. [Genome view]

GeneID

3320.

KEGG

hsa:3320.

UCSC

uc001yku.2. human.

Organism-specific databases

CTD

3320.

GeneCards

GC14M101619.

H-InvDB

HIX0011983.
HIX0057379.

HGNC

HGNC:5253. HSP90AA1.

HPA

CAB002058.

MIM

140571. gene.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

HBG007374.

InParanoid

P07900.

OMA

AIYYITA.

PhylomeDB

P07900.

Enzyme and pathway databases

Pathway_Interaction_DB

pi3kcipathway. Class I PI3K signaling events.
pi3kciaktpathway. Class I PI3K signaling events mediated by Akt.
hif1apathway. Hypoxic and oxygen homeostasis regulation of HIF-1-alpha.
il2_pi3kpathway. IL2 signaling events mediated by PI3K.
avb3_integrin_pathway. Integrins in angiogenesis.
ar_tf_pathway. Regulation of Androgen receptor activity.
telomerasepathway. Regulation of Telomerase.
hdac_classii_pathway. Signaling events mediated by HDAC Class II.
vegfr1_2_pathway. Signaling events mediated by VEGFR1 and VEGFR2.
vegfr1_pathway. VEGFR1 specific signals.

Reactome

REACT_12508. Metabolism of nitric oxide.
REACT_152. Cell Cycle, Mitotic.
REACT_18266. Axon guidance.

Gene expression databases

ArrayExpress

P07900.

Bgee

P07900.

CleanEx

HS_HSP90AA1.

Genevestigator

P07900.

GermOnline

ENSG00000080824. Homo sapiens.

Family and domain databases

InterPro

IPR003594. ATPase-like_ATP-bd.
IPR001404. Chaperone_htpG.
IPR019805. Heat_shock_protein_90_CS.
IPR020576. Hsp90_C.
IPR020575. Hsp90_N.
IPR020568. Ribosomal_S5_D2-typ_fold.
[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]

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 Resources

DrugBank

DB00615. Rifabutin.

NextBio

13162.

PMAP-CutDB

P07900.

SOURCE

Search...

Entry information

Entry name

HS90A_HUMAN

Accession

Primary (citable) accession number: P07900
Secondary accession number(s): A8K500 , B3KPJ9, Q2PP14, Q5CAQ6, Q5CAQ7, Q9BVQ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	January 23, 2007
Last modified:	March 2, 2010
This is version 145 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.