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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. 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

  • ATPase activity Source: UniProtKB
  • ATP binding Source: UniProtKB
  • CTP binding Source: Ensembl
  • dATP 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

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-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.
R-HSA-8854518. AURKA Activation by TPX2.
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
  • ruffle membrane Source: Ensembl
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.

Chemistry

ChEMBLiCHEMBL2095165.
DrugBankiDB00716. Nedocromil.
DB00615. Rifabutin.

Polymorphism and mutation databases

BioMutaiHSP90AA1.
DMDMi92090606.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 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 – 2311PhosphoserineCombined sources
Modified residuei252 – 2521PhosphoserineCombined sources
Modified residuei263 – 2631PhosphoserineCombined sources
Modified residuei313 – 3131PhosphotyrosineBy similarity
Modified residuei399 – 3991Phosphoserine1 Publication
Modified residuei443 – 4431N6-acetyllysineCombined sources
Modified residuei453 – 4531PhosphoserineBy similarity
Modified residuei458 – 4581N6-acetyllysineCombined sources
Modified residuei476 – 4761PhosphoserineCombined sources
Modified residuei489 – 4891N6-acetyllysineCombined sources
Modified residuei492 – 4921PhosphotyrosineBy similarity
Modified residuei585 – 5851N6-acetyllysineCombined sources
Modified residuei598 – 5981S-nitrosocysteine1 Publication
Modified residuei641 – 6411PhosphoserineCombined sources

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.
PhosphoSiteiP07900.
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 AHSA1, FNIP1, HSF1, SMYD3 and TOM34 (PubMed:11583998, PubMed:12604615, PubMed:15235609, PubMed:17028174, 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). 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). Following LPS binding, may form a complex with CXCR4, GDF5 and HSPA8 (PubMed:11276205). Interacts with KSR1 (PubMed:10409742). May interact with NWD1 (PubMed:24681825).19 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. 799 interactions.
DIPiDIP-27595N.
IntActiP07900. 222 interactions.
MINTiMINT-132070.
STRINGi9606.ENSP00000335153.

Chemistry

BindingDBiP07900.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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-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[»]
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

eggNOGiKOG0019. Eukaryota.
KOG0020. Eukaryota.
COG0326. LUCA.
GeneTreeiENSGT00840000129758.
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)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
Sequence conflicti162 – 1621W → D AA sequence (PubMed:10409742).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:
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
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[»]
ProteinModelPortaliP07900.
SMRiP07900. Positions 15-699.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109552. 799 interactions.
DIPiDIP-27595N.
IntActiP07900. 222 interactions.
MINTiMINT-132070.
STRINGi9606.ENSP00000335153.

Chemistry

BindingDBiP07900.
ChEMBLiCHEMBL2095165.
DrugBankiDB00716. Nedocromil.
DB00615. Rifabutin.

PTM databases

iPTMnetiP07900.
PhosphoSiteiP07900.
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.
GeneCardsiHSP90AA1.
HGNCiHGNC:5253. HSP90AA1.
HPAiCAB002058.
HPA047290.
MIMi140571. gene.
neXtProtiNX_P07900.
PharmGKBiPA29519.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0019. Eukaryota.
KOG0020. Eukaryota.
COG0326. LUCA.
GeneTreeiENSGT00840000129758.
HOVERGENiHBG007374.
InParanoidiP07900.
KOiK04079.
OMAiCERPAIS.
OrthoDBiEOG091G0270.
PhylomeDBiP07900.
TreeFamiTF300686.

Enzyme and pathway databases

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-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.
R-HSA-8854518. AURKA Activation by TPX2.
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: September 7, 2016
This is version 217 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.