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Protein

Heat shock protein HSP 90-alpha

Gene

Hsp90aa1

Organism
Rattus norvegicus (Rat)
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 (By similarity). Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei51 – 511ATPBy similarity
Binding sitei93 – 931ATPBy similarity
Binding sitei112 – 1121ATPBy similarity
Binding sitei138 – 1381ATP; via amide nitrogenBy similarity
Binding sitei401 – 4011ATPBy similarity

GO - Molecular functioni

  • ATPase activity Source: Ensembl
  • ATP binding Source: RGD
  • CTP binding Source: RGD
  • dATP binding Source: RGD
  • glycoprotein binding Source: ParkinsonsUK-UCL
  • GTP binding Source: RGD
  • ion channel binding Source: RGD
  • mRNA binding Source: RGD
  • nitric-oxide synthase regulator activity Source: UniProtKB
  • protein kinase binding Source: RGD
  • protein phosphatase binding Source: RGD
  • Rho GDP-dissociation inhibitor binding Source: RGD
  • sulfonylurea receptor binding Source: RGD
  • tau protein binding Source: RGD
  • TPR domain binding Source: UniProtKB
  • unfolded protein binding Source: RGD
  • UTP binding Source: RGD

GO - Biological processi

  • cardiac muscle cell apoptotic process Source: RGD
  • chaperone-mediated autophagy Source: ParkinsonsUK-UCL
  • chaperone-mediated protein complex assembly Source: Ensembl
  • chaperone-mediated protein transport involved in chaperone-mediated autophagy Source: ParkinsonsUK-UCL
  • neuron migration Source: RGD
  • positive regulation of cardiac muscle contraction Source: RGD
  • positive regulation of cell size Source: RGD
  • positive regulation of lamellipodium assembly Source: RGD
  • positive regulation of nitric oxide biosynthetic process Source: UniProtKB
  • positive regulation of protein import into nucleus, translocation Source: RGD
  • protein folding Source: RGD
  • protein import into mitochondrial outer membrane Source: Ensembl
  • regulation of protein complex stability Source: ParkinsonsUK-UCL
  • regulation of protein ubiquitination Source: Ensembl
  • response to antibiotic Source: AgBase
  • response to cocaine Source: RGD
  • response to cold Source: AgBase
  • response to drug Source: RGD
  • response to estrogen Source: RGD
  • response to heat Source: AgBase
  • response to salt stress Source: RGD
  • skeletal muscle contraction Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Stress response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-RNO-1227986. Signaling by ERBB2.
R-RNO-1474151. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
R-RNO-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-RNO-203615. eNOS activation.
R-RNO-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-RNO-3371511. HSF1 activation.
R-RNO-3371568. Attenuation phase.
R-RNO-3371571. HSF1-dependent transactivation.
R-RNO-380259. Loss of Nlp from mitotic centrosomes.
R-RNO-380270. Recruitment of mitotic centrosome proteins and complexes.
R-RNO-3928663. EPHA-mediated growth cone collapse.
R-RNO-399954. Sema3A PAK dependent Axon repulsion.
R-RNO-4420097. VEGFA-VEGFR2 Pathway.
R-RNO-5218920. VEGFR2 mediated vascular permeability.
R-RNO-5620912. Anchoring of the basal body to the plasma membrane.

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
Gene namesi
Name:Hsp90aa1
Synonyms:Hsp86, Hspca
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 6

Organism-specific databases

RGDi631409. Hsp90aa1.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 733732Heat shock protein HSP 90-alphaPRO_0000062915Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei5 – 51Phosphothreonine; by PRKDCBy similarity
Modified residuei7 – 71Phosphothreonine; by PRKDCBy similarity
Modified residuei58 – 581N6-acetyllysineBy similarity
Modified residuei84 – 841N6-acetyllysineBy similarity
Modified residuei231 – 2311PhosphoserineCombined sources
Modified residuei252 – 2521PhosphoserineCombined sources
Modified residuei263 – 2631PhosphoserineCombined sources
Modified residuei314 – 3141PhosphotyrosineBy similarity
Modified residuei400 – 4001PhosphoserineBy similarity
Modified residuei444 – 4441N6-acetyllysineBy similarity
Modified residuei454 – 4541PhosphoserineCombined sources
Modified residuei459 – 4591N6-acetyllysineBy similarity
Modified residuei477 – 4771PhosphoserineBy similarity
Modified residuei490 – 4901N6-acetyllysineBy similarity
Modified residuei493 – 4931PhosphotyrosineBy similarity
Modified residuei586 – 5861N6-acetyllysineBy similarity
Modified residuei599 – 5991S-nitrosocysteineBy similarity

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein, S-nitrosylation, Ubl conjugation

Proteomic databases

PaxDbiP82995.
PRIDEiP82995.

Expressioni

Gene expression databases

GenevisibleiP82995. RN.

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 or 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. Interacts with KSR1. May interact with NWD1.By similarity

GO - Molecular functioni

  • glycoprotein binding Source: ParkinsonsUK-UCL
  • ion channel binding Source: RGD
  • protein kinase binding Source: RGD
  • protein phosphatase binding Source: RGD
  • Rho GDP-dissociation inhibitor binding Source: RGD
  • sulfonylurea receptor binding Source: RGD
  • tau protein binding Source: RGD
  • TPR domain binding Source: UniProtKB
  • unfolded protein binding Source: RGD

Protein-protein interaction databases

BioGridi256205. 20 interactions.
IntActiP82995. 2 interactions.
MINTiMINT-1775917.
STRINGi10116.ENSRNOP00000009556.

Structurei

3D structure databases

ProteinModelPortaliP82995.
SMRiP82995. Positions 9-223, 294-697.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni683 – 73351Required for homodimerizationBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi729 – 7335TPR repeat-binding

Domaini

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

Sequence similaritiesi

Belongs to the heat shock protein 90 family.Curated

Phylogenomic databases

eggNOGiKOG0019. Eukaryota.
KOG0020. Eukaryota.
COG0326. LUCA.
GeneTreeiENSGT00840000129758.
ENSGT00840000130044.
HOGENOMiHOG000031988.
HOVERGENiHBG007374.
InParanoidiP82995.
KOiK04079.
OMAiAWTWASD.
OrthoDBiEOG780RM0.
PhylomeDBiP82995.
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]

Sequencei

Sequence statusi: Complete.

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

P82995-1 [UniParc]FASTAAdd to basket

« 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 SDDEAEEKEE KEEEKEKEEK
260 270 280 290 300
ESDDKPEIED VGSDEEEEEK KDGDKKKKKK IKEKYIDQEE LNKTKPIWTR
310 320 330 340 350
NPDDITNEEY GEFYKSLTND WEEHLAVKHF SVEGQLEFRA LLFVPRRAPF
360 370 380 390 400
DLFENRKKKN NIKLYVRRVF IMDNCEELIP EYLNFIRGVV DSEDLPLNIS
410 420 430 440 450
REMLQQSKIL KVIRKNLVKK CLELFTELAE DKENYKKFYE QFSKNIKLGI
460 470 480 490 500
HEDSQNRKKL SELLRYYTSA SGDEMVSLKD YCTRMKENQK HIYFITGETK
510 520 530 540 550
DQVANSAFVE RLRKHGLEVI YMIEPIDEYC VQQLKEFEGK TLVSVTKEGL
560 570 580 590 600
ELPEDEEEKK KQEEKKTKFE NLCKIMKDIL EKKVEKVVVS NRLVTSPCCI
610 620 630 640 650
VTSTYGWTAN MERIMKAQAL RDNSTMGYMA AKKHLEINPD HSIIETLRQK
660 670 680 690 700
AEADKNDKSV KDLVILLYET ALLSSGFSLE DPQTHANRIY RMIKLGLGID
710 720 730
EDDPTVDDTS AAVTEEMPPL EGDDDTSRME EVD
Length:733
Mass (Da):84,815
Last modified:January 23, 2007 - v3
Checksum:iDF2C8383A6581D07
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ297736 Genomic DNA. Translation: CAC39453.1.
AJ428213 mRNA. Translation: CAD21648.1.
BC072489 mRNA. Translation: AAH72489.1.
BC085120 mRNA. Translation: AAH85120.1.
RefSeqiNP_786937.1. NM_175761.2.
XP_008763191.1. XM_008764969.1.
UniGeneiRn.119867.
Rn.231905.
Rn.232226.
Rn.3277.

Genome annotation databases

EnsembliENSRNOT00000009556; ENSRNOP00000009556; ENSRNOG00000007219.
ENSRNOT00000086310; ENSRNOP00000075715; ENSRNOG00000059714.
GeneIDi103692716.
299331.
KEGGirno:103692716.
rno:299331.
UCSCiRGD:631409. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ297736 Genomic DNA. Translation: CAC39453.1.
AJ428213 mRNA. Translation: CAD21648.1.
BC072489 mRNA. Translation: AAH72489.1.
BC085120 mRNA. Translation: AAH85120.1.
RefSeqiNP_786937.1. NM_175761.2.
XP_008763191.1. XM_008764969.1.
UniGeneiRn.119867.
Rn.231905.
Rn.232226.
Rn.3277.

3D structure databases

ProteinModelPortaliP82995.
SMRiP82995. Positions 9-223, 294-697.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi256205. 20 interactions.
IntActiP82995. 2 interactions.
MINTiMINT-1775917.
STRINGi10116.ENSRNOP00000009556.

Proteomic databases

PaxDbiP82995.
PRIDEiP82995.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000009556; ENSRNOP00000009556; ENSRNOG00000007219.
ENSRNOT00000086310; ENSRNOP00000075715; ENSRNOG00000059714.
GeneIDi103692716.
299331.
KEGGirno:103692716.
rno:299331.
UCSCiRGD:631409. rat.

Organism-specific databases

CTDi3320.
RGDi631409. Hsp90aa1.

Phylogenomic databases

eggNOGiKOG0019. Eukaryota.
KOG0020. Eukaryota.
COG0326. LUCA.
GeneTreeiENSGT00840000129758.
ENSGT00840000130044.
HOGENOMiHOG000031988.
HOVERGENiHBG007374.
InParanoidiP82995.
KOiK04079.
OMAiAWTWASD.
OrthoDBiEOG780RM0.
PhylomeDBiP82995.
TreeFamiTF300686.

Enzyme and pathway databases

ReactomeiR-RNO-1227986. Signaling by ERBB2.
R-RNO-1474151. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
R-RNO-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-RNO-203615. eNOS activation.
R-RNO-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-RNO-3371511. HSF1 activation.
R-RNO-3371568. Attenuation phase.
R-RNO-3371571. HSF1-dependent transactivation.
R-RNO-380259. Loss of Nlp from mitotic centrosomes.
R-RNO-380270. Recruitment of mitotic centrosome proteins and complexes.
R-RNO-3928663. EPHA-mediated growth cone collapse.
R-RNO-399954. Sema3A PAK dependent Axon repulsion.
R-RNO-4420097. VEGFA-VEGFR2 Pathway.
R-RNO-5218920. VEGFR2 mediated vascular permeability.
R-RNO-5620912. Anchoring of the basal body to the plasma membrane.

Miscellaneous databases

NextBioi645227.
PROiP82995.

Gene expression databases

GenevisibleiP82995. RN.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of rat 86-kDa heat shock protein gene and promoter."
    Li C.W., Chang M.T., Lai Y., Chang W.M., Lai Y.K.
    Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Brain.
  2. "Cloning of full length cDNA of rat 86-kDa heat shock protein gene."
    Lai Y.R., Chang M.D., Chang W.M., Su C.Y., Lai Y.K.
    Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  3. "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].
    Tissue: Heart and Testis.
  4. "Isolation and quantification of the heat shock protein 90 alpha and beta isoforms from rat liver."
    Langer T., Fasold H.
    Protoplasma 218:54-56(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-13.
    Strain: Sprague-Dawley.
    Tissue: Liver.
  5. Lubec G., Afjehi-Sadat L.
    Submitted (NOV-2006) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 154-173; 329-339 AND 347-356, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Spinal cord.
  6. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231; SER-252; SER-263 AND SER-454, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiHS90A_RAT
AccessioniPrimary (citable) accession number: P82995
Secondary accession number(s): Q91XW0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 118 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 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.