Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P07900 (HS90A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 190. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Heat shock protein HSP 90-alpha
Alternative name(s):
Heat shock 86 kDa
Short name=HSP 86
Short name=HSP86
Lipopolysaccharide-associated protein 2
Short name=LAP-2
Short name=LPS-associated protein 2
Renal carcinoma antigen NY-REN-38
Gene names
Name:HSP90AA1
Synonyms:HSP90A, HSPC1, HSPCA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length732 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion by monocytes.

Subunit structure

Homodimer. Identified in NR3C1/GCR steroid receptor-chaperone complexes formed at least by NR3C1, HSP90AA1 and a variety of proteins containing TPR repeats such as FKBP4, FKBP5, PPID, PPP5C STIP1. Interacts with AHSA1, FNIP1, HSF1, SMYD3 and TOM34. Interacts with TERT; the interaction, together with PTGES3, is required for correct assembly and stabilization of the TERT holoenzyme complex. Interacts with CHORDC1 and DNAJC7. Interacts with STUB1 and UBE2N; may couple the chaperone and ubiquitination systems. Interacts (via TPR repeat-binding motif) with PPP5C (via TPR repeats); the interaction is direct and activates PPP5C phosphatase activity. Following LPS binding, may form a complex with CXCR4, GDF5 and HSPA8.

Subcellular location

Cytoplasm. Melanosome. Cell membrane. Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV.

Domain

The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins like the co-chaperone STUB1.

Post-translational modification

ISGylated.

S-nitrosylated; negatively regulates the ATPase activity and the activation of eNOS by HSP90AA1.

Sequence similarities

Belongs to the heat shock protein 90 family.

Ontologies

Keywords
   Biological processStress response
   Cellular componentCell membrane
Cytoplasm
Membrane
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Nucleotide-binding
   Molecular functionChaperone
   PTMAcetylation
Phosphoprotein
S-nitrosylation
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay Ref.15. Source: GOC

Fc-gamma receptor signaling pathway involved in phagocytosis

Traceable author statement. Source: Reactome

G2/M transition of mitotic cell cycle

Traceable author statement. Source: Reactome

axon guidance

Traceable author statement. Source: Reactome

cardiac muscle cell apoptotic process

Inferred from electronic annotation. Source: Ensembl

chaperone-mediated protein complex assembly

Inferred from direct assay PubMed 15644312. Source: BHF-UCL

innate immune response

Traceable author statement. Source: Reactome

mitochondrial transport

Traceable author statement PubMed 12526792. Source: UniProtKB

mitotic cell cycle

Traceable author statement. Source: Reactome

neuron migration

Inferred from electronic annotation. Source: Ensembl

nitric oxide metabolic process

Traceable author statement. Source: Reactome

positive regulation of cardiac muscle contraction

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell size

Inferred from electronic annotation. Source: Ensembl

positive regulation of lamellipodium assembly

Inferred from electronic annotation. Source: Ensembl

positive regulation of nitric oxide biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of protein import into nucleus, translocation

Inferred from electronic annotation. Source: Ensembl

protein import into mitochondrial outer membrane

Inferred from direct assay PubMed 15644312. Source: BHF-UCL

protein refolding

Traceable author statement Ref.20. Source: UniProtKB

regulation of nitric-oxide synthase activity

Traceable author statement. Source: Reactome

response to estrogen

Inferred from electronic annotation. Source: Ensembl

response to heat

Inferred from electronic annotation. Source: Ensembl

response to salt stress

Inferred from electronic annotation. Source: Ensembl

response to unfolded protein

Non-traceable author statement Ref.3. Source: UniProtKB

signal transduction

Non-traceable author statement PubMed 11470816. Source: UniProtKB

skeletal muscle contraction

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentapical plasma membrane

Inferred from electronic annotation. Source: Ensembl

basolateral plasma membrane

Inferred from electronic annotation. Source: Ensembl

brush border membrane

Inferred from electronic annotation. Source: Ensembl

cell surface

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Non-traceable author statement PubMed 12526792. Source: UniProtKB

endocytic vesicle lumen

Traceable author statement. Source: Reactome

extracellular matrix

Inferred from electronic annotation. Source: Ensembl

extracellular region

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 11487543PubMed 12519789PubMed 19199708PubMed 20458337. Source: UniProt

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from direct assay PubMed 15644312. Source: GOC

neuron projection

Inferred from electronic annotation. Source: Ensembl

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay. Source: HPA

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Traceable author statement. Source: Reactome

protein complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Traceable author statement PubMed 11470816. Source: UniProtKB

ATPase activity

Inferred from direct assay Ref.15. Source: UniProtKB

CTP binding

Inferred from electronic annotation. Source: Ensembl

GTP binding

Inferred from electronic annotation. Source: Ensembl

MHC class II protein complex binding

Inferred from direct assay PubMed 20458337. Source: UniProt

TPR domain binding

Inferred from direct assay Ref.20. Source: UniProtKB

UTP binding

Inferred from electronic annotation. Source: Ensembl

dATP binding

Inferred from electronic annotation. Source: Ensembl

identical protein binding

Inferred from physical interaction PubMed 16169070PubMed 21360678Ref.17. Source: IntAct

mRNA binding

Inferred from electronic annotation. Source: Ensembl

nitric-oxide synthase regulator activity

Inferred from direct assay Ref.15. Source: UniProtKB

nucleotide binding

Traceable author statement PubMed 11470816. Source: UniProtKB

poly(A) RNA binding

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

protein homodimerization activity

Traceable author statement PubMed 11470816. Source: UniProtKB

Complete GO annotation...

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 732731Heat shock protein HSP 90-alpha
PRO_0000062911

Regions

Region682 – 73251Required for homodimerization
Motif728 – 7325TPR repeat-binding

Sites

Binding site511ATP
Binding site931ATP
Binding site1121ATP By similarity
Binding site1381ATP; via amide nitrogen
Binding site4001ATP By similarity

Amino acid modifications

Modified residue51Phosphothreonine; by PRKDC
Modified residue71Phosphothreonine; by PRKDC
Modified residue581N6-acetyllysine By similarity
Modified residue841N6-acetyllysine By similarity
Modified residue2241N6-acetyllysine
Modified residue2311Phosphoserine
Modified residue2521Phosphoserine
Modified residue2631Phosphoserine
Modified residue3131Phosphotyrosine By similarity
Modified residue3991Phosphoserine
Modified residue4101N6-acetyllysine
Modified residue4431N6-acetyllysine
Modified residue4581N6-acetyllysine
Modified residue4891N6-acetyllysine
Modified residue4921Phosphotyrosine By similarity
Modified residue5761N6-acetyllysine
Modified residue5851N6-acetyllysine
Modified residue5981S-nitrosocysteine

Natural variations

Alternative sequence11M → MPPCSGGDGSTPPGPSLRDR DCPAQSAEYPRDRLDPRPGS PSEASSPPFLRSRAPVNWYQ EKAQVFLWHLMVSGSTTLLC LWKQPFHVSAFPVTASLAFR QSQGAGQHLYKDLQPFILLR LLM in isoform 2.
VSP_026604
Isoform 2:
Natural variant711M → L.
Corresponds to variant rs8005905 [ dbSNP | Ensembl ].

Experimental info

Mutagenesis971G → D: Abolishes ATPase activity.
Mutagenesis5981C → A, N or D: Reduces ATPase activity and client protein activation.
Mutagenesis5981C → S: Loss of S-nitrosylation.
Sequence conflict631S → T in CAA33259. Ref.1
Sequence conflict741K → R in CAI64495. Ref.4
Sequence conflict741K → R in BAG51711. Ref.6
Sequence conflict861D → G in CAI64495. Ref.4
Sequence conflict861D → G in BAG51711. Ref.6

Secondary structure

................................................................................................................ 732
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (HSP90AA1-1) (HSP90-alpha 2) [UniParc].

Last modified January 23, 2007. Version 5.
Checksum: 969F65FCC0BC86FD

FASTA73284,660
        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 

« Hide

Isoform 2 (HSP90AA1-2) [UniParc].

Checksum: 404BD8CAD5E68DB0
Show »

FASTA85498,161

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), NOMENCLATURE.
[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. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (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. expand/collapse author list , 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] [Europe PMC] [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. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] [Europe PMC] [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] [Europe PMC] [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, IDENTIFICATION BY 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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-21, PHOSPHORYLATION.
[15]"S-nitrosylation of Hsp90 promotes the inhibition of its ATPase and endothelial nitric oxide synthase regulatory activities."
Martinez-Ruiz A., Villanueva L., Gonzalez de Orduna C., Lopez-Ferrer D., Higueras M.A., Tarin C., Rodriguez-Crespo I., Vazquez J., Lamas S.
Proc. Natl. Acad. Sci. U.S.A. 102:8525-8530(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 592-612, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-598, S-NITROSYLATION AT CYS-598.
[16]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-5 AND THR-7.
[17]"The carboxy-terminal region of mammalian HSP90 is required for its dimerization and function in vivo."
Minami Y., Kimura Y., Kawasaki H., Suzuki K., Yahara I.
Mol. Cell. Biol. 14:1459-1464(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: HOMODIMERIZATION.
[18]"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] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[19]"Protein phosphatase 5 is a major component of glucocorticoid receptor.hsp90 complexes with properties of an FK506-binding immunophilin."
Silverstein A.M., Galigniana M.D., Chen M.S., Owens-Grillo J.K., Chinkers M., Pratt W.B.
J. Biol. Chem. 272:16224-16230(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH NR3C1 AND FKBP4; PPID; PPP5C OR STIP1.
[20]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TOM34.
[21]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN.
Tissue: Renal cell carcinoma.
[22]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TERT, FUNCTION AS A CO-CHAPERONE IN TELOMERASE HOLOENZYME ASSEMBLY.
[23]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HSF1.
[24]"A CD14-independent LPS receptor cluster."
Triantafilou K., Triantafilou M., Dedrick R.L.
Nat. Immunol. 2:338-345(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION AS LPS RECEPTOR, INTERACTION WITH CXCR4; GDF5 AND HSPA8, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[25]"Cofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone system."
Brychzy A., Rein T., Winklhofer K.F., Hartl F.U., Young J.C., Obermann W.M.
EMBO J. 22:3613-3623(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DNAJC7.
[26]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AHSA1.
[27]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SMYD3.
[28]"Human protein phosphatase 5 dissociates from heat-shock proteins and is proteolytically activated in response to arachidonic acid and the microtubule-depolymerizing drug nocodazole."
Zeke T., Morrice N., Vazquez-Martin C., Cohen P.T.
Biochem. J. 385:45-56(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PPP5C, IDENTIFICATION BY MASS SPECTROMETRY.
[29]"Molecular basis for TPR domain-mediated regulation of protein phosphatase 5."
Yang J., Roe S.M., Cliff M.J., Williams M.A., Ladbury J.E., Cohen P.T., Barford D.
EMBO J. 24:1-10(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PPP5C.
[30]"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-231 AND SER-263, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[31]"Phosphoproteomic analysis of the human pituitary."
Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.
Pituitary 9:109-120(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Pituitary.
[32]"Conformational diversity in the TPR domain-mediated interaction of protein phosphatase 5 with Hsp90."
Cliff M.J., Harris R., Barford D., Ladbury J.E., Williams M.A.
Structure 14:415-426(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PPP5C.
[33]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: T-cell.
[34]"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-252 AND SER-263, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[35]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[36]"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-263, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[37]"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-231 AND SER-263, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[38]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[39]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[40]"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-443; LYS-458; LYS-489 AND LYS-585, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[41]"A proteomic investigation of ligand-dependent HSP90 complexes reveals CHORDC1 as a novel ADP-dependent HSP90-interacting protein."
Gano J.J., Simon J.A.
Mol. Cell. Proteomics 9:255-270(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CHORDC1.
[42]"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.
[43]"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], IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Melanoma.
[44]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FNIP1, IDENTIFICATION BY MASS SPECTROMETRY.
[45]"The ATPase-dependent chaperoning activity of Hsp90a regulates thick filament formation and integration during skeletal muscle myofibrillogenesis."
Hawkins T.A., Haramis A.P., Etard C., Prodromou C., Vaughan C.K., Ashworth R., Ray S., Behra M., Holder N., Talbot W.S., Pearl L.H., Strahle U., Wilson S.W.
Development 135:1147-1156(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF GLY-97.
[46]"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: MUTAGENESIS OF CYS-598.
[47]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[48]"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].
[49]"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-252, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[50]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 11-223 IN COMPLEX WITH GELDANAMYCIN.
[51]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 11-223 IN COMPLEX WITH ADP, CATALYTIC ACTIVITY, INTERACTION WITH PTGES3.
[52]"Chaperoned ubiquitylation -- crystal structures of the CHIP U box E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex."
Zhang M., Windheim M., Roe S.M., Peggie M., Cohen P., Prodromou C., Pearl L.H.
Mol. Cell 20:525-538(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 724-732 IN COMPLEX WITH STUB1, INTERACTION WITH STUB1 AND UBE2N.
+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.
PIRHHHU86. A32319.
RefSeqNP_001017963.2. NM_001017963.2.
NP_005339.3. NM_005348.3.
UniGeneHs.525600.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BYQX-ray1.50A9-236[»]
1OSFX-ray1.75A9-223[»]
1UY6X-ray1.90A1-236[»]
1UY7X-ray1.90A1-236[»]
1UY8X-ray1.98A1-236[»]
1UY9X-ray2.00A1-236[»]
1UYCX-ray2.00A1-236[»]
1UYDX-ray2.00A1-236[»]
1UYEX-ray2.00A1-236[»]
1UYFX-ray2.00A1-236[»]
1UYGX-ray2.00A1-236[»]
1UYHX-ray2.20A1-236[»]
1UYIX-ray2.00A1-236[»]
1UYKX-ray2.00A1-236[»]
1UYLX-ray1.40A1-236[»]
1YC1X-ray1.70A9-235[»]
1YC3X-ray2.12A9-235[»]
1YC4X-ray1.81A9-235[»]
1YERX-ray1.65A9-236[»]
1YESX-ray2.20A9-236[»]
1YETX-ray1.90A9-236[»]
2BSMX-ray2.05A2-235[»]
2BT0X-ray1.90A/B2-235[»]
2BUGNMR-B-[»]
2BYHX-ray1.90A11-235[»]
2BYIX-ray1.60A11-235[»]
2BZ5X-ray1.90A/B2-235[»]
2C2LX-ray3.30E/F/G/H724-732[»]
2CCSX-ray1.79A1-236[»]
2CCTX-ray2.30A1-236[»]
2CCUX-ray2.70A1-236[»]
2CDDX-ray1.90A/B1-236[»]
2FWYX-ray2.10A1-236[»]
2FWZX-ray2.10A1-236[»]
2H55X-ray2.00A1-236[»]
2JJCX-ray1.95A9-223[»]
2K5BNMR-A14-223[»]
2QF6X-ray3.10A/B/C/D17-223[»]
2QFOX-ray1.68A/B17-223[»]
2QG0X-ray1.85A/B17-223[»]
2QG2X-ray1.80A17-223[»]
2UWDX-ray1.90A2-235[»]
2VCIX-ray2.00A1-236[»]
2VCJX-ray2.50A1-236[»]
2WI1X-ray2.30A1-236[»]
2WI2X-ray2.09A/B1-236[»]
2WI3X-ray1.90A1-236[»]
2WI4X-ray2.40A1-236[»]
2WI5X-ray2.10A1-236[»]
2WI6X-ray2.18A1-236[»]
2WI7X-ray2.50A1-236[»]
2XABX-ray1.90A/B9-236[»]
2XDKX-ray1.97A9-236[»]
2XDLX-ray1.98A9-236[»]
2XDSX-ray1.97A9-236[»]
2XDUX-ray1.74A14-224[»]
2XDXX-ray2.42A9-236[»]
2XHRX-ray2.20A9-236[»]
2XHTX-ray2.27A9-236[»]
2XHXX-ray2.80A9-236[»]
2XJGX-ray2.25A9-236[»]
2XJJX-ray1.90A/B9-236[»]
2XJXX-ray1.66A9-236[»]
2XK2X-ray1.95A9-236[»]
2YE2X-ray1.90A9-236[»]
2YE3X-ray1.95A9-236[»]
2YE4X-ray2.30A9-236[»]
2YE5X-ray1.73A9-236[»]
2YE6X-ray2.56A9-236[»]
2YE7X-ray2.20A9-236[»]
2YE8X-ray2.30A9-236[»]
2YE9X-ray2.20A9-236[»]
2YEAX-ray1.73A9-236[»]
2YEBX-ray2.40A9-236[»]
2YECX-ray2.10A9-236[»]
2YEDX-ray2.10A9-236[»]
2YEEX-ray2.30A9-236[»]
2YEFX-ray1.55A9-236[»]
2YEGX-ray2.50A/B9-236[»]
2YEHX-ray2.10A9-236[»]
2YEIX-ray2.20A9-236[»]
2YEJX-ray2.20A9-236[»]
2YI0X-ray1.60A1-229[»]
2YI5X-ray2.50A1-229[»]
2YI6X-ray1.80A1-229[»]
2YI7X-ray1.40A1-229[»]
2YJWX-ray1.61A18-223[»]
2YJXX-ray1.83A18-223[»]
2YK2X-ray1.74A18-223[»]
2YK9X-ray1.32A18-223[»]
2YKBX-ray1.93A18-223[»]
2YKCX-ray1.67A18-223[»]
2YKEX-ray1.43A18-223[»]
2YKIX-ray1.67A18-223[»]
2YKJX-ray1.46A18-223[»]
3B24X-ray1.70A/B9-236[»]
3B25X-ray1.75A9-236[»]
3B26X-ray2.10A/B9-236[»]
3B27X-ray1.50A9-236[»]
3B28X-ray1.35A/B9-236[»]
3BM9X-ray1.60A14-236[»]
3BMYX-ray1.60A14-236[»]
3D0BX-ray1.74A1-232[»]
3EKOX-ray1.55A/B9-225[»]
3EKRX-ray2.00A/B9-225[»]
3FT5X-ray1.90A9-236[»]
3FT8X-ray2.00A9-236[»]
3HEKX-ray1.95A/B9-225[»]
3HHUX-ray1.59A/B1-224[»]
3HYYX-ray1.90A9-236[»]
3HYZX-ray2.30A/B9-236[»]
3HZ1X-ray2.30A9-236[»]
3HZ5X-ray1.90A9-236[»]
3INWX-ray1.95A10-236[»]
3INXX-ray1.75A10-236[»]
3K97X-ray1.95A9-236[»]
3K98X-ray2.40A/B9-225[»]
3K99X-ray2.10A/B/C/D9-225[»]
3MNRX-ray1.90P1-232[»]
3O0IX-ray1.47A1-236[»]
3OW6X-ray1.80A17-223[»]
3OWBX-ray2.05A17-223[»]
3OWDX-ray1.63A17-223[»]
3Q6MX-ray3.00A/B/C293-732[»]
3Q6NX-ray3.05A/B/C/D/E/F293-732[»]
3QDDX-ray1.79A1-236[»]
3QTFX-ray1.57A14-236[»]
3R4MX-ray1.70A9-236[»]
3R4NX-ray2.00A/B9-225[»]
3R4OX-ray2.65A/B9-225[»]
3R4PX-ray1.70A/B9-225[»]
3R91X-ray1.58A14-236[»]
3R92X-ray1.58A14-236[»]
3RKZX-ray1.57A14-236[»]
3RLPX-ray1.70A/B9-225[»]
3RLQX-ray1.90A/B9-225[»]
3RLRX-ray1.70A/B9-225[»]
3T0HX-ray1.20A9-236[»]
3T0ZX-ray2.19A9-236[»]
3T10X-ray1.24A9-236[»]
3T1KX-ray1.50A/B9-236[»]
3T2SX-ray1.50A/B9-236[»]
3TUHX-ray1.80A/B16-224[»]
3VHAX-ray1.39A9-236[»]
3VHCX-ray1.41A9-236[»]
3VHDX-ray1.52A/B9-236[»]
3WHAX-ray1.30A/B9-236[»]
4AIFX-ray2.01D/E726-732[»]
4AWOX-ray1.70A/B9-236[»]
4AWPX-ray1.82A/B9-236[»]
4AWQX-ray1.60A/B9-236[»]
4B7PX-ray1.70A9-236[»]
4BQJX-ray2.00A9-236[»]
4EEHX-ray1.60A9-236[»]
4EFTX-ray2.12A9-236[»]
4EFUX-ray2.00A9-236[»]
4EGHX-ray1.60A9-236[»]
4EGIX-ray1.79A9-236[»]
4EGKX-ray1.69A9-236[»]
4FCPX-ray2.00A/B1-236[»]
4FCQX-ray2.15A1-236[»]
4FCRX-ray1.70A1-236[»]
4HY6X-ray1.65A9-236[»]
4JQLX-ray1.72A9-236[»]
4NH7X-ray2.00A/B9-236[»]
4NH8X-ray1.65A9-236[»]
ProteinModelPortalP07900.
SMRP07900. Positions 16-699.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109552. 751 interactions.
DIPDIP-27595N.
IntActP07900. 149 interactions.
MINTMINT-132070.
STRING9606.ENSP00000335153.

Chemistry

BindingDBP07900.
ChEMBLCHEMBL2095165.
DrugBankDB00615. Rifabutin.

PTM databases

PhosphoSiteP07900.

Polymorphism databases

DMDM92090606.

2D gel databases

OGPP07900.
REPRODUCTION-2DPAGEIPI00784295.

Proteomic databases

PRIDEP07900.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000216281; ENSP00000216281; ENSG00000080824. [P07900-1]
ENST00000334701; ENSP00000335153; ENSG00000080824. [P07900-2]
GeneID3320.
KEGGhsa:3320.
UCSCuc001yku.4. human. [P07900-1]
uc001ykv.4. human. [P07900-2]

Organism-specific databases

CTD3320.
GeneCardsGC14M102547.
HGNCHGNC:5253. HSP90AA1.
HPACAB002058.
HPA047290.
MIM140571. gene.
neXtProtNX_P07900.
PharmGKBPA29519.
GenAtlasSearch...

Phylogenomic databases

HOVERGENHBG007374.
InParanoidP07900.
KOK04079.
OMALTDSPAC.
OrthoDBEOG780RM0.
PhylomeDBP07900.
TreeFamTF300686.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_115566. Cell Cycle.
REACT_116125. Disease.
REACT_160300. Binding and Uptake of Ligands by Scavenger Receptors.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressP07900.
BgeeP07900.
CleanExHS_HSP90AA1.
GenevestigatorP07900.

Family and domain databases

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

Other

ChiTaRSHSP90AA1. human.
EvolutionaryTraceP07900.
GenomeRNAi3320.
NextBio13162.
PMAP-CutDBP07900.
PROP07900.
SOURCESearch...

Entry information

Entry nameHS90A_HUMAN
AccessionPrimary (citable) accession number: P07900
Secondary accession number(s): A8K500 expand/collapse secondary AC list , B3KPJ9, Q2PP14, Q5CAQ6, Q5CAQ7, Q9BVQ5
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 190 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM