Skip Header

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

Heat shock protein HSP 90-alpha

Gene

HSP90AA1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 which is essential for its chaperone 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 (PubMed:11274138, PubMed:11276205, PubMed:15577939, PubMed:15937123, PubMed:27353360).5 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei51ATP1
Binding sitei93ATP1
Binding sitei112ATPBy similarity1
Binding sitei138ATP; via amide nitrogen1
Binding sitei400ATPBy similarity1

GO - Molecular functioni

  • ATPase activity Source: UniProtKB
  • ATP binding Source: UniProtKB
  • CTP binding Source: Ensembl
  • dATP binding Source: Ensembl
  • glycoprotein binding Source: Ensembl
  • GTPase binding Source: UniProtKB
  • GTP binding Source: Ensembl
  • histone deacetylase binding Source: BHF-UCL
  • identical protein binding Source: IntAct
  • MHC class II protein complex binding Source: UniProtKB
  • mRNA binding Source: Ensembl
  • nitric-oxide synthase regulator activity Source: UniProtKB
  • nucleotide binding Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • protein tyrosine kinase activity Source: Reactome
  • TPR domain binding Source: UniProtKB
  • UTP binding Source: Ensembl

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Stress response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000080824-MONOMER.
ReactomeiR-HSA-1227986. Signaling by ERBB2.
R-HSA-1236382. Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants.
R-HSA-1474151. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
R-HSA-192905. vRNP Assembly.
R-HSA-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-HSA-203615. eNOS activation.
R-HSA-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-HSA-3000484. Scavenging by Class F Receptors.
R-HSA-3371511. HSF1 activation.
R-HSA-3371568. Attenuation phase.
R-HSA-3371571. HSF1-dependent transactivation.
R-HSA-380259. Loss of Nlp from mitotic centrosomes.
R-HSA-380270. Recruitment of mitotic centrosome proteins and complexes.
R-HSA-3928663. EPHA-mediated growth cone collapse.
R-HSA-399954. Sema3A PAK dependent Axon repulsion.
R-HSA-4420097. VEGFA-VEGFR2 Pathway.
R-HSA-5218920. VEGFR2 mediated vascular permeability.
R-HSA-5336415. Uptake and function of diphtheria toxin.
R-HSA-5601884. PIWI-interacting RNA (piRNA) biogenesis.
R-HSA-5620912. Anchoring of the basal body to the plasma membrane.
R-HSA-5637810. Constitutive Signaling by EGFRvIII.
R-HSA-6798695. Neutrophil degranulation.
R-HSA-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.
R-HSA-8854518. AURKA Activation by TPX2.
R-HSA-8863795. Downregulation of ERBB2 signaling.
SIGNORiP07900.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:5253. HSP90AA1.

Subcellular locationi

GO - Cellular componenti

  • apical plasma membrane Source: Ensembl
  • basolateral plasma membrane Source: Ensembl
  • brush border membrane Source: Ensembl
  • cell surface Source: Ensembl
  • cytoplasm Source: AgBase
  • cytosol Source: UniProtKB
  • endocytic vesicle lumen Source: Reactome
  • extracellular exosome Source: UniProtKB
  • extracellular matrix Source: Ensembl
  • extracellular region Source: Reactome
  • lysosomal lumen Source: ParkinsonsUK-UCL
  • melanosome Source: UniProtKB-SubCell
  • membrane Source: UniProtKB
  • myelin sheath Source: Ensembl
  • neuronal cell body Source: Ensembl
  • neuron projection Source: Ensembl
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • perinuclear region of cytoplasm Source: Ensembl
  • plasma membrane Source: Reactome
  • protein complex Source: Ensembl
  • sperm mitochondrial sheath Source: Ensembl
  • sperm plasma membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi97G → D: Abolishes ATPase activity. 1 Publication1
Mutagenesisi598C → A, N or D: Reduces ATPase activity and client protein activation. 2 Publications1
Mutagenesisi598C → S: Loss of S-nitrosylation. 2 Publications1

Organism-specific databases

DisGeNETi3320.
OpenTargetsiENSG00000080824.
PharmGKBiPA29519.

Chemistry databases

ChEMBLiCHEMBL3880.
DrugBankiDB00716. Nedocromil.
DB00615. Rifabutin.
GuidetoPHARMACOLOGYi2905.

Polymorphism and mutation databases

BioMutaiHSP90AA1.
DMDMi92090606.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000629112 – 732Heat shock protein HSP 90-alphaAdd BLAST731

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei5Phosphothreonine; by PRKDC1 Publication1
Modified residuei7Phosphothreonine; by PRKDC1 Publication1
Modified residuei58N6-acetyllysineBy similarity1
Modified residuei84N6-acetyllysineBy similarity1
Modified residuei231PhosphoserineCombined sources1
Modified residuei252PhosphoserineCombined sources1
Modified residuei263PhosphoserineCombined sources1
Modified residuei313PhosphotyrosineBy similarity1
Modified residuei399Phosphoserine1 Publication1
Modified residuei443N6-acetyllysineCombined sources1
Modified residuei453PhosphoserineBy similarity1
Modified residuei458N6-acetyllysineCombined sources1
Modified residuei476PhosphoserineCombined sources1
Modified residuei489N6-acetyllysineCombined sources1
Modified residuei492PhosphotyrosineBy similarity1
Modified residuei585N6-acetyllysineCombined sources1
Modified residuei598S-nitrosocysteine1 Publication1
Modified residuei641PhosphoserineCombined sources1

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

EPDiP07900.
MaxQBiP07900.
PaxDbiP07900.
PeptideAtlasiP07900.
PRIDEiP07900.
TopDownProteomicsiP07900-1. [P07900-1]

2D gel databases

OGPiP07900.
REPRODUCTION-2DPAGEIPI00784295.

PTM databases

iPTMnetiP07900.
PhosphoSitePlusiP07900.
SwissPalmiP07900.

Miscellaneous databases

PMAP-CutDBP07900.

Expressioni

Gene expression databases

BgeeiENSG00000080824.
CleanExiHS_HSP90AA1.
ExpressionAtlasiP07900. baseline and differential.
GenevisibleiP07900. HS.

Organism-specific databases

HPAiCAB002058.
HPA047290.

Interactioni

Subunit structurei

Homodimer (PubMed:7588731, PubMed:8289821). 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 or STIP1 (PubMed:15383005, PubMed:9195923). Interacts with HSF1, SMYD3 and TOM34 (PubMed:11583998, PubMed:15235609, PubMed:9660753). Interacts with TERT; the interaction, together with PTGES3, is required for correct assembly and stabilization of the TERT holoenzyme complex (PubMed:11274138, PubMed:9817749). Interacts with CHORDC1 and DNAJC7 (PubMed:12853476, PubMed:19875381). Interacts with STUB1 and UBE2N; may couple the chaperone and ubiquitination systems (PubMed:16307917, PubMed:27353360). Interacts (via TPR repeat-binding motif) with PPP5C (via TPR repeats); the interaction is direct and activates PPP5C phosphatase activity (PubMed:15383005, PubMed:15577939, PubMed:16531226, PubMed:27353360). Following LPS binding, may form a complex with CXCR4, GDF5 and HSPA8 (PubMed:11276205). Interacts with KSR1 (PubMed:10409742). Interacts with co-chaperone CDC37 (via C-terminus); the interaction inhibits HSP90AA1 ATPase activity (PubMed:23569206, PubMed:27353360). May interact with NWD1 (PubMed:24681825). Interacts with FNIP1 and FNIP2; the interaction inhibits HSP90AA1 ATPase activity (PubMed:17028174, PubMed:27353360). Interacts with AHSA1; the interaction activates HSP90AA1 ATPase activity (PubMed:12604615, PubMed:27353360). Interacts with FLCN in the presence of FNIP1. Interacts with HSP70, STIP1 and PTGES3 (PubMed:27353360).21 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself5EBI-296047,EBI-296047
AHSA1O954334EBI-296047,EBI-448610
CCDC117Q8IWD45EBI-296047,EBI-3387963
CDC37Q1654314EBI-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
JUNP054124EBI-296047,EBI-852823
MAP3K7O43318-25EBI-296047,EBI-358700
NR3C1P041507EBI-296047,EBI-493507
PPIDP268824EBI-296047,EBI-6477155From a different organism.
PPP5CP530419EBI-296047,EBI-716663
PTGES3Q151856EBI-296047,EBI-1049387
RPAP3Q9H6T33EBI-296047,EBI-356928
RPS3AP612473EBI-296047,EBI-352378
S100a1P354674EBI-296047,EBI-6477109From a different organism.
STK11Q158312EBI-296047,EBI-306838
STUB1Q9UNE79EBI-296047,EBI-357085

GO - Molecular functioni

  • GTPase binding Source: UniProtKB
  • histone deacetylase binding Source: BHF-UCL
  • identical protein binding Source: IntAct
  • MHC class II protein complex binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • TPR domain binding Source: UniProtKB

Protein-protein interaction databases

BioGridi109552. 800 interactors.
DIPiDIP-27595N.
IntActiP07900. 225 interactors.
MINTiMINT-132070.
STRINGi9606.ENSP00000335153.

Chemistry databases

BindingDBiP07900.

Structurei

Secondary structure

1732
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi18 – 21Combined sources4
Helixi24 – 35Combined sources12
Helixi43 – 63Combined sources21
Helixi67 – 70Combined sources4
Beta strandi78 – 83Combined sources6
Turni84 – 87Combined sources4
Beta strandi88 – 93Combined sources6
Helixi100 – 104Combined sources5
Helixi106 – 108Combined sources3
Helixi111 – 123Combined sources13
Helixi128 – 134Combined sources7
Helixi137 – 143Combined sources7
Beta strandi145 – 153Combined sources9
Beta strandi155 – 157Combined sources3
Beta strandi159 – 164Combined sources6
Beta strandi169 – 174Combined sources6
Beta strandi181 – 190Combined sources10
Helixi192 – 198Combined sources7
Helixi200 – 210Combined sources11
Beta strandi212 – 216Combined sources5
Beta strandi218 – 220Combined sources3
Turni221 – 224Combined sources4
Beta strandi225 – 227Combined sources3
Helixi228 – 230Combined sources3
Helixi296 – 298Combined sources3
Helixi306 – 317Combined sources12
Beta strandi324 – 331Combined sources8
Beta strandi333 – 335Combined sources3
Beta strandi337 – 343Combined sources7
Beta strandi361 – 365Combined sources5
Beta strandi368 – 372Combined sources5
Helixi380 – 382Combined sources3
Beta strandi386 – 392Combined sources7
Helixi408 – 427Combined sources20
Helixi431 – 451Combined sources21
Helixi453 – 455Combined sources3
Helixi456 – 460Combined sources5
Beta strandi464 – 467Combined sources4
Turni468 – 472Combined sources5
Helixi477 – 482Combined sources6
Beta strandi490 – 495Combined sources6
Helixi499 – 503Combined sources5
Helixi506 – 508Combined sources3
Helixi509 – 514Combined sources6
Beta strandi518 – 521Combined sources4
Helixi525 – 529Combined sources5
Turni530 – 532Combined sources3
Beta strandi539 – 543Combined sources5
Helixi555 – 567Combined sources13
Helixi569 – 578Combined sources10
Helixi580 – 582Combined sources3
Beta strandi584 – 588Combined sources5
Beta strandi593 – 601Combined sources9
Beta strandi603 – 605Combined sources3
Helixi608 – 613Combined sources6
Beta strandi632 – 636Combined sources5
Helixi641 – 652Combined sources12
Helixi657 – 673Combined sources17
Helixi681 – 694Combined sources14
Beta strandi728 – 730Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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-B728-732[»]
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[»]
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[»]
3WQ9X-ray1.80A1-236[»]
4AIFX-ray2.01D/E726-732[»]
4AWOX-ray1.70A/B9-236[»]
4AWPX-ray1.82A/B9-236[»]
4AWQX-ray1.60A/B9-236[»]
4B7PX-ray1.70A9-236[»]
4BQGX-ray1.90A9-236[»]
4BQJX-ray2.00A9-236[»]
4CGQX-ray2.00Q726-732[»]
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[»]
4O04X-ray1.82A9-236[»]
4O05X-ray1.79A9-236[»]
4O07X-ray1.86A9-236[»]
4O09X-ray1.96A9-236[»]
4O0BX-ray1.93A9-236[»]
4R3MX-ray1.80A16-224[»]
4U93X-ray1.55A1-236[»]
4W7TX-ray1.80A1-236[»]
4XIPX-ray1.70A9-236[»]
4XIQX-ray1.84A9-236[»]
4XIRX-ray1.70A9-236[»]
4XITX-ray1.86A9-236[»]
4YKQX-ray1.91A2-236[»]
4YKRX-ray1.61A2-236[»]
4YKTX-ray1.85A2-236[»]
4YKUX-ray1.70A2-236[»]
4YKWX-ray1.85A/B2-236[»]
4YKXX-ray1.80A2-236[»]
4YKYX-ray1.78A2-236[»]
4YKZX-ray1.85A2-236[»]
5CF0X-ray1.80A9-236[»]
ProteinModelPortaliP07900.
SMRiP07900.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07900.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni284 – 732Interaction with FLCN and FNIP11 PublicationAdd BLAST449
Regioni284 – 620Interaction with FNIP21 PublicationAdd BLAST337
Regioni682 – 732Required for homodimerization1 PublicationAdd BLAST51

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi723 – 732TPR repeat-binding1 Publication10

Domaini

The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins like the co-chaperone STUB1.1 Publication

Sequence similaritiesi

Belongs to the heat shock protein 90 family.Curated

Phylogenomic databases

eggNOGiKOG0019. Eukaryota.
KOG0020. Eukaryota.
COG0326. LUCA.
GeneTreeiENSGT00850000132363.
HOVERGENiHBG007374.
InParanoidiP07900.
KOiK04079.
OMAiCERPAIS.
OrthoDBiEOG091G0270.
PhylomeDBiP07900.
TreeFamiTF300686.

Family and domain databases

Gene3Di3.30.565.10. 2 hits.
HAMAPiMF_00505. HSP90. 1 hit.
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. AlignAdd to basket

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)DescriptionActionsGraphical viewLength
Sequence conflicti63S → T in CAA33259 (PubMed:2780322).Curated1
Sequence conflicti74K → R in CAI64495 (PubMed:16269234).Curated1
Sequence conflicti74K → R in BAG51711 (PubMed:14702039).Curated1
Sequence conflicti86D → G in CAI64495 (PubMed:16269234).Curated1
Sequence conflicti86D → G in BAG51711 (PubMed:14702039).Curated1
Sequence conflicti162W → D AA sequence (PubMed:10409742).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Isoform 2 (identifier: P07900-2)
Natural varianti71M → L.Corresponds to variant rs8005905dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0266041M → MPPCSGGDGSTPPGPSLRDR DCPAQSAEYPRDRLDPRPGS PSEASSPPFLRSRAPVNWYQ EKAQVFLWHLMVSGSTTLLC LWKQPFHVSAFPVTASLAFR QSQGAGQHLYKDLQPFILLR LLM in isoform 2. 2 Publications1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.5. human. [P07900-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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-B728-732[»]
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[»]
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[»]
3WQ9X-ray1.80A1-236[»]
4AIFX-ray2.01D/E726-732[»]
4AWOX-ray1.70A/B9-236[»]
4AWPX-ray1.82A/B9-236[»]
4AWQX-ray1.60A/B9-236[»]
4B7PX-ray1.70A9-236[»]
4BQGX-ray1.90A9-236[»]
4BQJX-ray2.00A9-236[»]
4CGQX-ray2.00Q726-732[»]
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[»]
4O04X-ray1.82A9-236[»]
4O05X-ray1.79A9-236[»]
4O07X-ray1.86A9-236[»]
4O09X-ray1.96A9-236[»]
4O0BX-ray1.93A9-236[»]
4R3MX-ray1.80A16-224[»]
4U93X-ray1.55A1-236[»]
4W7TX-ray1.80A1-236[»]
4XIPX-ray1.70A9-236[»]
4XIQX-ray1.84A9-236[»]
4XIRX-ray1.70A9-236[»]
4XITX-ray1.86A9-236[»]
4YKQX-ray1.91A2-236[»]
4YKRX-ray1.61A2-236[»]
4YKTX-ray1.85A2-236[»]
4YKUX-ray1.70A2-236[»]
4YKWX-ray1.85A/B2-236[»]
4YKXX-ray1.80A2-236[»]
4YKYX-ray1.78A2-236[»]
4YKZX-ray1.85A2-236[»]
5CF0X-ray1.80A9-236[»]
ProteinModelPortaliP07900.
SMRiP07900.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109552. 800 interactors.
DIPiDIP-27595N.
IntActiP07900. 225 interactors.
MINTiMINT-132070.
STRINGi9606.ENSP00000335153.

Chemistry databases

BindingDBiP07900.
ChEMBLiCHEMBL3880.
DrugBankiDB00716. Nedocromil.
DB00615. Rifabutin.
GuidetoPHARMACOLOGYi2905.

PTM databases

iPTMnetiP07900.
PhosphoSitePlusiP07900.
SwissPalmiP07900.

Polymorphism and mutation databases

BioMutaiHSP90AA1.
DMDMi92090606.

2D gel databases

OGPiP07900.
REPRODUCTION-2DPAGEIPI00784295.

Proteomic databases

EPDiP07900.
MaxQBiP07900.
PaxDbiP07900.
PeptideAtlasiP07900.
PRIDEiP07900.
TopDownProteomicsiP07900-1. [P07900-1]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000216281; ENSP00000216281; ENSG00000080824. [P07900-1]
ENST00000334701; ENSP00000335153; ENSG00000080824. [P07900-2]
GeneIDi3320.
KEGGihsa:3320.
UCSCiuc001yku.5. human. [P07900-1]

Organism-specific databases

CTDi3320.
DisGeNETi3320.
GeneCardsiHSP90AA1.
HGNCiHGNC:5253. HSP90AA1.
HPAiCAB002058.
HPA047290.
MIMi140571. gene.
neXtProtiNX_P07900.
OpenTargetsiENSG00000080824.
PharmGKBiPA29519.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0019. Eukaryota.
KOG0020. Eukaryota.
COG0326. LUCA.
GeneTreeiENSGT00850000132363.
HOVERGENiHBG007374.
InParanoidiP07900.
KOiK04079.
OMAiCERPAIS.
OrthoDBiEOG091G0270.
PhylomeDBiP07900.
TreeFamiTF300686.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000080824-MONOMER.
ReactomeiR-HSA-1227986. Signaling by ERBB2.
R-HSA-1236382. Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants.
R-HSA-1474151. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
R-HSA-192905. vRNP Assembly.
R-HSA-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-HSA-203615. eNOS activation.
R-HSA-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-HSA-3000484. Scavenging by Class F Receptors.
R-HSA-3371511. HSF1 activation.
R-HSA-3371568. Attenuation phase.
R-HSA-3371571. HSF1-dependent transactivation.
R-HSA-380259. Loss of Nlp from mitotic centrosomes.
R-HSA-380270. Recruitment of mitotic centrosome proteins and complexes.
R-HSA-3928663. EPHA-mediated growth cone collapse.
R-HSA-399954. Sema3A PAK dependent Axon repulsion.
R-HSA-4420097. VEGFA-VEGFR2 Pathway.
R-HSA-5218920. VEGFR2 mediated vascular permeability.
R-HSA-5336415. Uptake and function of diphtheria toxin.
R-HSA-5601884. PIWI-interacting RNA (piRNA) biogenesis.
R-HSA-5620912. Anchoring of the basal body to the plasma membrane.
R-HSA-5637810. Constitutive Signaling by EGFRvIII.
R-HSA-6798695. Neutrophil degranulation.
R-HSA-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.
R-HSA-8854518. AURKA Activation by TPX2.
R-HSA-8863795. Downregulation of ERBB2 signaling.
SIGNORiP07900.

Miscellaneous databases

ChiTaRSiHSP90AA1. human.
EvolutionaryTraceiP07900.
GenomeRNAii3320.
PMAP-CutDBP07900.
PROiP07900.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000080824.
CleanExiHS_HSP90AA1.
ExpressionAtlasiP07900. baseline and differential.
GenevisibleiP07900. HS.

Family and domain databases

Gene3Di3.30.565.10. 2 hits.
HAMAPiMF_00505. HSP90. 1 hit.
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]
ProtoNetiSearch...

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: November 30, 2016
This is version 220 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.