Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P07900

- HS90A_HUMAN

UniProt

P07900 - HS90A_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Heat shock protein HSP 90-alpha

Gene

HSP90AA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei51 – 511ATP
Binding sitei93 – 931ATP
Binding sitei112 – 1121ATPBy similarity
Binding sitei138 – 1381ATP; via amide nitrogen
Binding sitei400 – 4001ATPBy similarity

GO - Molecular functioni

  1. ATPase activity Source: UniProtKB
  2. ATP binding Source: UniProtKB
  3. identical protein binding Source: IntAct
  4. MHC class II protein complex binding Source: UniProt
  5. nitric-oxide synthase regulator activity Source: UniProtKB
  6. nucleotide binding Source: UniProtKB
  7. poly(A) RNA binding Source: UniProtKB
  8. protein homodimerization activity Source: UniProtKB
  9. TPR domain binding Source: UniProtKB

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. axon guidance Source: Reactome
  3. chaperone-mediated protein complex assembly Source: BHF-UCL
  4. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
  5. G2/M transition of mitotic cell cycle Source: Reactome
  6. innate immune response Source: Reactome
  7. mitochondrial transport Source: UniProtKB
  8. mitotic cell cycle Source: Reactome
  9. nitric oxide metabolic process Source: Reactome
  10. positive regulation of nitric oxide biosynthetic process Source: UniProtKB
  11. protein import into mitochondrial outer membrane Source: BHF-UCL
  12. protein refolding Source: UniProtKB
  13. regulation of nitric-oxide synthase activity Source: Reactome
  14. response to unfolded protein Source: UniProtKB
  15. signal transduction Source: UniProtKB
  16. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Stress response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_111176. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
REACT_115755. Signaling by ERBB2.
REACT_115852. Signaling by constitutively active EGFR.
REACT_12477. eNOS activation.
REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
REACT_15364. Loss of Nlp from mitotic centrosomes.
REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
REACT_163813. Scavenging by Class F Receptors.
REACT_19236. Sema3A PAK dependent Axon repulsion.
REACT_200624. Attenuation phase.
REACT_200744. HSF1 activation.
REACT_200775. HSF1-dependent transactivation.
REACT_9434. vRNP Assembly.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:HSP90AA1
Synonyms:HSP90A, HSPC1, HSPCA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:5253. HSP90AA1.

Subcellular locationi

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

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: UniProtKB
  3. endocytic vesicle lumen Source: Reactome
  4. extracellular region Source: Reactome
  5. extracellular vesicular exosome Source: UniProtKB
  6. membrane Source: UniProtKB
  7. mitochondrion Source: GOC
  8. nucleus Source: UniProt
  9. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi97 – 971G → D: Abolishes ATPase activity. 1 Publication
Mutagenesisi598 – 5981C → A, N or D: Reduces ATPase activity and client protein activation. 2 Publications
Mutagenesisi598 – 5981C → S: Loss of S-nitrosylation. 2 Publications

Organism-specific databases

PharmGKBiPA29519.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 732731Heat shock protein HSP 90-alphaPRO_0000062911Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei5 – 51Phosphothreonine; by PRKDC1 Publication
Modified residuei7 – 71Phosphothreonine; by PRKDC1 Publication
Modified residuei58 – 581N6-acetyllysineBy similarity
Modified residuei84 – 841N6-acetyllysineBy similarity
Modified residuei231 – 2311Phosphoserine2 Publications
Modified residuei252 – 2521Phosphoserine2 Publications
Modified residuei263 – 2631Phosphoserine7 Publications
Modified residuei313 – 3131PhosphotyrosineBy similarity
Modified residuei399 – 3991Phosphoserine1 Publication
Modified residuei443 – 4431N6-acetyllysine1 Publication
Modified residuei458 – 4581N6-acetyllysine1 Publication
Modified residuei489 – 4891N6-acetyllysine1 Publication
Modified residuei492 – 4921PhosphotyrosineBy similarity
Modified residuei585 – 5851N6-acetyllysine1 Publication
Modified residuei598 – 5981S-nitrosocysteine1 Publication

Post-translational modificationi

ISGylated.1 Publication
S-nitrosylated; negatively regulates the ATPase activity and the activation of eNOS by HSP90AA1.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, S-nitrosylation, Ubl conjugation

Proteomic databases

MaxQBiP07900.
PRIDEiP07900.

2D gel databases

OGPiP07900.
REPRODUCTION-2DPAGEIPI00784295.

PTM databases

PhosphoSiteiP07900.

Miscellaneous databases

PMAP-CutDBP07900.

Expressioni

Gene expression databases

BgeeiP07900.
CleanExiHS_HSP90AA1.
ExpressionAtlasiP07900. baseline and differential.
GenevestigatoriP07900.

Organism-specific databases

HPAiCAB002058.
HPA047290.

Interactioni

Subunit structurei

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 HSPA8.17 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself5EBI-296047,EBI-296047
AHSA1O954334EBI-296047,EBI-448610
CCDC117Q8IWD45EBI-296047,EBI-3387963
CDC37Q1654313EBI-296047,EBI-295634
CDC37L1Q7L3B62EBI-296047,EBI-2841876
CDK9P507502EBI-296047,EBI-1383449
CERS2Q96G232EBI-296047,EBI-1057080
CHORDC1Q9UHD18EBI-296047,EBI-2550959
CHUKO151113EBI-296047,EBI-81249
EGFRP005335EBI-296047,EBI-297353
ERBB2P046264EBI-296047,EBI-641062
FKBP4Q027908EBI-296047,EBI-1047444
FKBP8Q143187EBI-296047,EBI-724839
HSP90AB1Q6PK502EBI-296047,EBI-9356629
IKBKGQ9Y6K93EBI-296047,EBI-81279
JUNP054122EBI-296047,EBI-852823
MAP3K7O43318-25EBI-296047,EBI-358700
PPIDP268824EBI-296047,EBI-6477155From a different organism.
PPP5CP530418EBI-296047,EBI-716663
PTGES3Q151856EBI-296047,EBI-1049387
RPAP3Q9H6T33EBI-296047,EBI-356928
RPS3AP612472EBI-296047,EBI-352378
S100a1P354674EBI-296047,EBI-6477109From a different organism.
STK11Q158312EBI-296047,EBI-306838
STUB1Q9UNE79EBI-296047,EBI-357085

Protein-protein interaction databases

BioGridi109552. 755 interactions.
DIPiDIP-27595N.
IntActiP07900. 193 interactions.
MINTiMINT-132070.
STRINGi9606.ENSP00000335153.

Structurei

Secondary structure

1
732
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi18 – 214
Helixi24 – 3512
Helixi43 – 6321
Helixi67 – 704
Beta strandi78 – 836
Turni84 – 874
Beta strandi88 – 936
Helixi100 – 1045
Helixi106 – 1083
Helixi111 – 12313
Helixi128 – 1347
Helixi137 – 1437
Beta strandi145 – 1539
Beta strandi155 – 1573
Beta strandi159 – 1646
Beta strandi169 – 1746
Beta strandi181 – 19010
Helixi192 – 1987
Helixi200 – 21011
Beta strandi212 – 2165
Beta strandi218 – 2203
Turni221 – 2244
Beta strandi225 – 2273
Helixi228 – 2303
Helixi296 – 2983
Helixi306 – 31712
Beta strandi324 – 3318
Beta strandi333 – 3353
Beta strandi337 – 3437
Beta strandi361 – 3655
Beta strandi368 – 3725
Helixi380 – 3823
Beta strandi386 – 3927
Helixi408 – 42720
Helixi431 – 45121
Helixi453 – 4553
Helixi456 – 4605
Beta strandi464 – 4674
Turni468 – 4725
Helixi477 – 4826
Beta strandi490 – 4956
Helixi499 – 5035
Helixi506 – 5083
Helixi509 – 5146
Beta strandi518 – 5214
Helixi525 – 5295
Turni530 – 5323
Beta strandi539 – 5435
Helixi555 – 56713
Helixi569 – 57810
Helixi580 – 5823
Beta strandi584 – 5885
Beta strandi593 – 6019
Beta strandi603 – 6053
Helixi608 – 6136
Beta strandi632 – 6365
Helixi641 – 65212
Helixi657 – 67317
Helixi681 – 69414
Beta strandi728 – 7303

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BYQX-ray1.50A9-236[»]
1OSFX-ray1.75A9-223[»]
1UY6X-ray1.90A2-236[»]
1UY7X-ray1.90A2-236[»]
1UY8X-ray1.98A2-236[»]
1UY9X-ray2.00A2-236[»]
1UYCX-ray2.00A2-236[»]
1UYDX-ray2.20A2-236[»]
1UYEX-ray2.00A2-236[»]
1UYFX-ray2.00A2-236[»]
1UYGX-ray2.00A2-236[»]
1UYHX-ray2.20A2-236[»]
1UYIX-ray2.20A2-236[»]
1UYKX-ray2.20A2-236[»]
1UYLX-ray1.40A2-236[»]
1YC1X-ray1.70A9-236[»]
1YC3X-ray2.12A9-236[»]
1YC4X-ray1.81A9-236[»]
1YERX-ray1.65A9-236[»]
1YESX-ray2.20A9-236[»]
1YETX-ray1.90A9-236[»]
2BSMX-ray2.05A2-236[»]
2BT0X-ray1.90A/B2-236[»]
2BUGNMR-B-[»]
2BYHX-ray1.90A11-236[»]
2BYIX-ray1.60A11-236[»]
2BZ5X-ray1.90A/B2-236[»]
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-ray1.90A2-236[»]
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[»]
4CGUX-ray2.11C726-732[»]
4CGVX-ray2.54E/F726-732[»]
4CGWX-ray3.00C/D726-732[»]
4CWFX-ray2.00A9-236[»]
4CWNX-ray1.80A9-236[»]
4CWOX-ray2.31A9-236[»]
4CWPX-ray1.95A9-236[»]
4CWQX-ray2.00A9-236[»]
4CWRX-ray2.00A9-236[»]
4CWSX-ray2.30A9-236[»]
4CWTX-ray1.90A9-236[»]
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[»]
4L8ZX-ray1.70A9-236[»]
4L90X-ray2.00A9-236[»]
4L91X-ray1.75A9-236[»]
4L93X-ray1.84A/B9-236[»]
4L94X-ray1.65A9-236[»]
4LWEX-ray1.50A17-224[»]
4LWFX-ray1.75A17-224[»]
4LWGX-ray1.60A17-224[»]
4LWHX-ray1.70A16-224[»]
4LWIX-ray1.70A17-224[»]
4NH7X-ray2.00A/B9-236[»]
4NH8X-ray1.65A9-236[»]
4O05X-ray1.79A9-236[»]
4O07X-ray1.86A9-236[»]
4O09X-ray1.96A9-236[»]
4O0BX-ray1.93A9-236[»]
ProteinModelPortaliP07900.
SMRiP07900. Positions 15-699.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07900.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni682 – 73251Required for homodimerizationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi728 – 7325TPR repeat-binding

Domaini

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

Sequence similaritiesi

Belongs to the heat shock protein 90 family.Curated

Phylogenomic databases

GeneTreeiENSGT00760000119253.
HOVERGENiHBG007374.
InParanoidiP07900.
KOiK04079.
OMAiMSHLTEF.
OrthoDBiEOG780RM0.
PhylomeDBiP07900.
TreeFamiTF300686.

Family and domain databases

Gene3Di3.30.565.10. 2 hits.
HAMAPiMF_00505. HSP90.
InterProiIPR003594. HATPase_C.
IPR019805. Heat_shock_protein_90_CS.
IPR001404. Hsp90_fam.
IPR020575. Hsp90_N.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]
PANTHERiPTHR11528. PTHR11528. 1 hit.
PfamiPF02518. HATPase_c. 1 hit.
PF00183. HSP90. 1 hit.
[Graphical view]
PIRSFiPIRSF002583. Hsp90. 1 hit.
PRINTSiPR00775. HEATSHOCK90.
SMARTiSM00387. HATPase_c. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 1 hit.
PROSITEiPS00298. HSP90. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P07900-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MPEETQTQDQ PMEEEEVETF AFQAEIAQLM SLIINTFYSN KEIFLRELIS
60 70 80 90 100
NSSDALDKIR YESLTDPSKL DSGKELHINL IPNKQDRTLT IVDTGIGMTK
110 120 130 140 150
ADLINNLGTI AKSGTKAFME ALQAGADISM IGQFGVGFYS AYLVAEKVTV
160 170 180 190 200
ITKHNDDEQY AWESSAGGSF TVRTDTGEPM GRGTKVILHL KEDQTEYLEE
210 220 230 240 250
RRIKEIVKKH SQFIGYPITL FVEKERDKEV SDDEAEEKED KEEEKEKEEK
260 270 280 290 300
ESEDKPEIED VGSDEEEEKK DGDKKKKKKI KEKYIDQEEL NKTKPIWTRN
310 320 330 340 350
PDDITNEEYG EFYKSLTNDW EDHLAVKHFS VEGQLEFRAL LFVPRRAPFD
360 370 380 390 400
LFENRKKKNN IKLYVRRVFI MDNCEELIPE YLNFIRGVVD SEDLPLNISR
410 420 430 440 450
EMLQQSKILK VIRKNLVKKC LELFTELAED KENYKKFYEQ FSKNIKLGIH
460 470 480 490 500
EDSQNRKKLS ELLRYYTSAS GDEMVSLKDY CTRMKENQKH IYYITGETKD
510 520 530 540 550
QVANSAFVER LRKHGLEVIY MIEPIDEYCV QQLKEFEGKT LVSVTKEGLE
560 570 580 590 600
LPEDEEEKKK QEEKKTKFEN LCKIMKDILE KKVEKVVVSN RLVTSPCCIV
610 620 630 640 650
TSTYGWTANM ERIMKAQALR DNSTMGYMAA KKHLEINPDH SIIETLRQKA
660 670 680 690 700
EADKNDKSVK DLVILLYETA LLSSGFSLED PQTHANRIYR MIKLGLGIDE
710 720 730
DDPTADDTSA AVTEEMPPLE GDDDTSRMEE VD
Length:732
Mass (Da):84,660
Last modified:January 23, 2007 - v5
Checksum:i969F65FCC0BC86FD
GO
Isoform 2 (identifier: P07900-2) [UniParc]FASTAAdd to Basket

Also known as: HSP90AA1-2

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MPPCSGGDGS...QPFILLRLLM

Show »
Length:854
Mass (Da):98,161
Checksum:i404BD8CAD5E68DB0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti63 – 631S → T in CAA33259. (PubMed:2780322)Curated
Sequence conflicti74 – 741K → R in CAI64495. (PubMed:16269234)Curated
Sequence conflicti74 – 741K → R in BAG51711. (PubMed:14702039)Curated
Sequence conflicti86 – 861D → G in CAI64495. (PubMed:16269234)Curated
Sequence conflicti86 – 861D → G in BAG51711. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Isoform 2 (identifier: P07900-2)
Natural varianti71 – 711M → L.
Corresponds to variant rs8005905 [ dbSNP | Ensembl ].

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MPPCSGGDGSTPPGPSLRDR DCPAQSAEYPRDRLDPRPGS PSEASSPPFLRSRAPVNWYQ EKAQVFLWHLMVSGSTTLLC LWKQPFHVSAFPVTASLAFR QSQGAGQHLYKDLQPFILLR LLM in isoform 2. 2 PublicationsVSP_026604

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS32160.1. [P07900-2]
CCDS9967.1. [P07900-1]
PIRiA32319. HHHU86.
RefSeqiNP_001017963.2. NM_001017963.2. [P07900-2]
NP_005339.3. NM_005348.3. [P07900-1]
UniGeneiHs.525600.

Genome annotation databases

EnsembliENST00000216281; ENSP00000216281; ENSG00000080824. [P07900-1]
ENST00000334701; ENSP00000335153; ENSG00000080824. [P07900-2]
GeneIDi3320.
KEGGihsa:3320.
UCSCiuc001yku.4. human. [P07900-1]
uc001ykv.4. human. [P07900-2]

Polymorphism databases

DMDMi92090606.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS32160.1. [P07900-2 ]
CCDS9967.1. [P07900-1 ]
PIRi A32319. HHHU86.
RefSeqi NP_001017963.2. NM_001017963.2. [P07900-2 ]
NP_005339.3. NM_005348.3. [P07900-1 ]
UniGenei Hs.525600.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 2-236 [» ]
1UY7 X-ray 1.90 A 2-236 [» ]
1UY8 X-ray 1.98 A 2-236 [» ]
1UY9 X-ray 2.00 A 2-236 [» ]
1UYC X-ray 2.00 A 2-236 [» ]
1UYD X-ray 2.20 A 2-236 [» ]
1UYE X-ray 2.00 A 2-236 [» ]
1UYF X-ray 2.00 A 2-236 [» ]
1UYG X-ray 2.00 A 2-236 [» ]
1UYH X-ray 2.20 A 2-236 [» ]
1UYI X-ray 2.20 A 2-236 [» ]
1UYK X-ray 2.20 A 2-236 [» ]
1UYL X-ray 1.40 A 2-236 [» ]
1YC1 X-ray 1.70 A 9-236 [» ]
1YC3 X-ray 2.12 A 9-236 [» ]
1YC4 X-ray 1.81 A 9-236 [» ]
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 2-236 [» ]
2BT0 X-ray 1.90 A/B 2-236 [» ]
2BUG NMR - B - [» ]
2BYH X-ray 1.90 A 11-236 [» ]
2BYI X-ray 1.60 A 11-236 [» ]
2BZ5 X-ray 1.90 A/B 2-236 [» ]
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 2-236 [» ]
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 [» ]
2XAB X-ray 1.90 A/B 9-236 [» ]
2XDK X-ray 1.97 A 9-236 [» ]
2XDL X-ray 1.98 A 9-236 [» ]
2XDS X-ray 1.97 A 9-236 [» ]
2XDU X-ray 1.74 A 14-224 [» ]
2XDX X-ray 2.42 A 9-236 [» ]
2XHR X-ray 2.20 A 9-236 [» ]
2XHT X-ray 2.27 A 9-236 [» ]
2XHX X-ray 2.80 A 9-236 [» ]
2XJG X-ray 2.25 A 9-236 [» ]
2XJJ X-ray 1.90 A/B 9-236 [» ]
2XJX X-ray 1.66 A 9-236 [» ]
2XK2 X-ray 1.95 A 9-236 [» ]
2YE2 X-ray 1.90 A 9-236 [» ]
2YE3 X-ray 1.95 A 9-236 [» ]
2YE4 X-ray 2.30 A 9-236 [» ]
2YE5 X-ray 1.73 A 9-236 [» ]
2YE6 X-ray 2.56 A 9-236 [» ]
2YE7 X-ray 2.20 A 9-236 [» ]
2YE8 X-ray 2.30 A 9-236 [» ]
2YE9 X-ray 2.20 A 9-236 [» ]
2YEA X-ray 1.73 A 9-236 [» ]
2YEB X-ray 2.40 A 9-236 [» ]
2YEC X-ray 2.10 A 9-236 [» ]
2YED X-ray 2.10 A 9-236 [» ]
2YEE X-ray 2.30 A 9-236 [» ]
2YEF X-ray 1.55 A 9-236 [» ]
2YEG X-ray 2.50 A/B 9-236 [» ]
2YEH X-ray 2.10 A 9-236 [» ]
2YEI X-ray 2.20 A 9-236 [» ]
2YEJ X-ray 2.20 A 9-236 [» ]
2YI0 X-ray 1.60 A 1-229 [» ]
2YI5 X-ray 2.50 A 1-229 [» ]
2YI6 X-ray 1.80 A 1-229 [» ]
2YI7 X-ray 1.40 A 1-229 [» ]
2YJW X-ray 1.61 A 18-223 [» ]
2YJX X-ray 1.83 A 18-223 [» ]
2YK2 X-ray 1.74 A 18-223 [» ]
2YK9 X-ray 1.32 A 18-223 [» ]
2YKB X-ray 1.93 A 18-223 [» ]
2YKC X-ray 1.67 A 18-223 [» ]
2YKE X-ray 1.43 A 18-223 [» ]
2YKI X-ray 1.67 A 18-223 [» ]
2YKJ X-ray 1.46 A 18-223 [» ]
3B24 X-ray 1.70 A/B 9-236 [» ]
3B25 X-ray 1.75 A 9-236 [» ]
3B26 X-ray 2.10 A/B 9-236 [» ]
3B27 X-ray 1.50 A 9-236 [» ]
3B28 X-ray 1.35 A/B 9-236 [» ]
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 [» ]
3HYY X-ray 1.90 A 9-236 [» ]
3HYZ X-ray 2.30 A/B 9-236 [» ]
3HZ1 X-ray 2.30 A 9-236 [» ]
3HZ5 X-ray 1.90 A 9-236 [» ]
3INW X-ray 1.95 A 10-236 [» ]
3INX X-ray 1.75 A 10-236 [» ]
3K97 X-ray 1.95 A 9-236 [» ]
3K98 X-ray 2.40 A/B 9-225 [» ]
3K99 X-ray 2.10 A/B/C/D 9-225 [» ]
3MNR X-ray 1.90 P 1-232 [» ]
3O0I X-ray 1.47 A 1-236 [» ]
3OW6 X-ray 1.80 A 17-223 [» ]
3OWB X-ray 2.05 A 17-223 [» ]
3OWD X-ray 1.63 A 17-223 [» ]
3Q6M X-ray 3.00 A/B/C 293-732 [» ]
3Q6N X-ray 3.05 A/B/C/D/E/F 293-732 [» ]
3QDD X-ray 1.79 A 1-236 [» ]
3QTF X-ray 1.57 A 14-236 [» ]
3R4M X-ray 1.70 A 9-236 [» ]
3R4N X-ray 2.00 A/B 9-225 [» ]
3R4O X-ray 2.65 A/B 9-225 [» ]
3R4P X-ray 1.70 A/B 9-225 [» ]
3R91 X-ray 1.58 A 14-236 [» ]
3R92 X-ray 1.58 A 14-236 [» ]
3RKZ X-ray 1.57 A 14-236 [» ]
3RLP X-ray 1.70 A/B 9-225 [» ]
3RLQ X-ray 1.90 A/B 9-225 [» ]
3RLR X-ray 1.70 A/B 9-225 [» ]
3T0H X-ray 1.20 A 9-236 [» ]
3T0Z X-ray 2.19 A 9-236 [» ]
3T10 X-ray 1.24 A 9-236 [» ]
3T1K X-ray 1.50 A/B 9-236 [» ]
3T2S X-ray 1.50 A/B 9-236 [» ]
3TUH X-ray 1.80 A/B 16-224 [» ]
3VHA X-ray 1.39 A 9-236 [» ]
3VHC X-ray 1.41 A 9-236 [» ]
3VHD X-ray 1.52 A/B 9-236 [» ]
3WHA X-ray 1.30 A/B 9-236 [» ]
4AIF X-ray 2.01 D/E 726-732 [» ]
4AWO X-ray 1.70 A/B 9-236 [» ]
4AWP X-ray 1.82 A/B 9-236 [» ]
4AWQ X-ray 1.60 A/B 9-236 [» ]
4B7P X-ray 1.70 A 9-236 [» ]
4BQJ X-ray 2.00 A 9-236 [» ]
4CGU X-ray 2.11 C 726-732 [» ]
4CGV X-ray 2.54 E/F 726-732 [» ]
4CGW X-ray 3.00 C/D 726-732 [» ]
4CWF X-ray 2.00 A 9-236 [» ]
4CWN X-ray 1.80 A 9-236 [» ]
4CWO X-ray 2.31 A 9-236 [» ]
4CWP X-ray 1.95 A 9-236 [» ]
4CWQ X-ray 2.00 A 9-236 [» ]
4CWR X-ray 2.00 A 9-236 [» ]
4CWS X-ray 2.30 A 9-236 [» ]
4CWT X-ray 1.90 A 9-236 [» ]
4EEH X-ray 1.60 A 9-236 [» ]
4EFT X-ray 2.12 A 9-236 [» ]
4EFU X-ray 2.00 A 9-236 [» ]
4EGH X-ray 1.60 A 9-236 [» ]
4EGI X-ray 1.79 A 9-236 [» ]
4EGK X-ray 1.69 A 9-236 [» ]
4FCP X-ray 2.00 A/B 1-236 [» ]
4FCQ X-ray 2.15 A 1-236 [» ]
4FCR X-ray 1.70 A 1-236 [» ]
4HY6 X-ray 1.65 A 9-236 [» ]
4JQL X-ray 1.72 A 9-236 [» ]
4L8Z X-ray 1.70 A 9-236 [» ]
4L90 X-ray 2.00 A 9-236 [» ]
4L91 X-ray 1.75 A 9-236 [» ]
4L93 X-ray 1.84 A/B 9-236 [» ]
4L94 X-ray 1.65 A 9-236 [» ]
4LWE X-ray 1.50 A 17-224 [» ]
4LWF X-ray 1.75 A 17-224 [» ]
4LWG X-ray 1.60 A 17-224 [» ]
4LWH X-ray 1.70 A 16-224 [» ]
4LWI X-ray 1.70 A 17-224 [» ]
4NH7 X-ray 2.00 A/B 9-236 [» ]
4NH8 X-ray 1.65 A 9-236 [» ]
4O05 X-ray 1.79 A 9-236 [» ]
4O07 X-ray 1.86 A 9-236 [» ]
4O09 X-ray 1.96 A 9-236 [» ]
4O0B X-ray 1.93 A 9-236 [» ]
ProteinModelPortali P07900.
SMRi P07900. Positions 15-699.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109552. 755 interactions.
DIPi DIP-27595N.
IntActi P07900. 193 interactions.
MINTi MINT-132070.
STRINGi 9606.ENSP00000335153.

Chemistry

BindingDBi P07900.
ChEMBLi CHEMBL2095165.
DrugBanki DB00716. Nedocromil.
DB00615. Rifabutin.

PTM databases

PhosphoSitei P07900.

Polymorphism databases

DMDMi 92090606.

2D gel databases

OGPi P07900.
REPRODUCTION-2DPAGE IPI00784295.

Proteomic databases

MaxQBi P07900.
PRIDEi P07900.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000216281 ; ENSP00000216281 ; ENSG00000080824 . [P07900-1 ]
ENST00000334701 ; ENSP00000335153 ; ENSG00000080824 . [P07900-2 ]
GeneIDi 3320.
KEGGi hsa:3320.
UCSCi uc001yku.4. human. [P07900-1 ]
uc001ykv.4. human. [P07900-2 ]

Organism-specific databases

CTDi 3320.
GeneCardsi GC14M102547.
HGNCi HGNC:5253. HSP90AA1.
HPAi CAB002058.
HPA047290.
MIMi 140571. gene.
neXtProti NX_P07900.
PharmGKBi PA29519.
GenAtlasi Search...

Phylogenomic databases

GeneTreei ENSGT00760000119253.
HOVERGENi HBG007374.
InParanoidi P07900.
KOi K04079.
OMAi MSHLTEF.
OrthoDBi EOG780RM0.
PhylomeDBi P07900.
TreeFami TF300686.

Enzyme and pathway databases

Reactomei REACT_111176. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
REACT_115755. Signaling by ERBB2.
REACT_115852. Signaling by constitutively active EGFR.
REACT_12477. eNOS activation.
REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
REACT_15364. Loss of Nlp from mitotic centrosomes.
REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
REACT_163813. Scavenging by Class F Receptors.
REACT_19236. Sema3A PAK dependent Axon repulsion.
REACT_200624. Attenuation phase.
REACT_200744. HSF1 activation.
REACT_200775. HSF1-dependent transactivation.
REACT_9434. vRNP Assembly.

Miscellaneous databases

ChiTaRSi HSP90AA1. human.
EvolutionaryTracei P07900.
GenomeRNAii 3320.
NextBioi 13162.
PMAP-CutDB P07900.
PROi P07900.
SOURCEi Search...

Gene expression databases

Bgeei P07900.
CleanExi HS_HSP90AA1.
ExpressionAtlasi P07900. baseline and differential.
Genevestigatori P07900.

Family and domain databases

Gene3Di 3.30.565.10. 2 hits.
HAMAPi MF_00505. HSP90.
InterProi IPR003594. HATPase_C.
IPR019805. Heat_shock_protein_90_CS.
IPR001404. Hsp90_fam.
IPR020575. Hsp90_N.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view ]
PANTHERi PTHR11528. PTHR11528. 1 hit.
Pfami PF02518. HATPase_c. 1 hit.
PF00183. HSP90. 1 hit.
[Graphical view ]
PIRSFi PIRSF002583. Hsp90. 1 hit.
PRINTSi PR00775. HEATSHOCK90.
SMARTi SM00387. HATPase_c. 1 hit.
[Graphical view ]
SUPFAMi SSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 1 hit.
PROSITEi PS00298. HSP90. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. 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. 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. 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. 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. 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. Cited for: ISGYLATION.
  43. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Melanoma.
  44. 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. 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.

Entry informationi

Entry nameiHS90A_HUMAN
AccessioniPrimary (citable) accession number: P07900
Secondary accession number(s): A8K500
, B3KPJ9, Q2PP14, Q5CAQ6, Q5CAQ7, Q9BVQ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 196 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3