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Protein

Heat shock protein 90-1

Gene

HSP90-1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Functions as a holding molecular chaperone (holdase) which stabilizes unfolding protein intermediates and rapidly releases them in an active form once stress has abated. Functions as a folding molecular chaperone (foldase) that assists the non-covalent folding of proteins in an ATP-dependent manner (PubMed:23827697). Molecular chaperone involved in R gene-mediated disease resistance. Required for full RPS2-mediated resistance through interaction with RAR1. Possesses probably ATPase activity (PubMed:14504384).2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei34 – 341ATPBy similarity
Binding sitei38 – 381ATPBy similarity
Binding sitei80 – 801ATPBy similarity
Binding sitei85 – 851ATPBy similarity
Binding sitei93 – 931ATPBy similarity
Binding sitei99 – 991ATPBy similarity
Binding sitei172 – 1721ATPBy similarity
Binding sitei372 – 3721ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi100 – 1012ATPBy similarity
Nucleotide bindingi120 – 1256ATPBy similarity

GO - Molecular functioni

GO - Biological processi

  • defense response to bacterium, incompatible interaction Source: UniProtKB
  • protein folding Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Immunity, Innate immunity, Plant defense, Stress response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-ATH-3371511. HSF1 activation.
R-ATH-3371568. Attenuation phase.
R-ATH-3371571. HSF1-dependent transactivation.
R-ATH-844456. The NLRP3 inflammasome.

Names & Taxonomyi

Protein namesi
Recommended name:
Heat shock protein 90-1Curated
Short name:
AtHSP90.1Curated
Short name:
AtHsp90-11 Publication
Alternative name(s):
Heat shock protein 81-1Curated
Short name:
Hsp81-11 Publication
Heat shock protein 83
Gene namesi
Name:HSP90-11 Publication
Synonyms:HSP81-11 Publication, HSP83
Ordered Locus Names:At5g52640
ORF Names:F6N7.13
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G52640.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

No visible phenotype under normal growth condition. In case of infection, plants are altered in RPS2-mediated disease resistance.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 700700Heat shock protein 90-1PRO_0000062946Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei219 – 2191PhosphoserineCombined sources

Post-translational modificationi

Ubiquitinated.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP27323.
PRIDEiP27323.

PTM databases

iPTMnetiP27323.

Expressioni

Tissue specificityi

Expressed constitutively in roots only. After heat treatment, expressed in most tissues. Levels also increase after heavy metal treatment.

Developmental stagei

Expressed in pollen during pollen development, germination and tube growth. Expressed during embryo development and young seedling growth.1 Publication

Inductioni

By heat shock and infection by avirulent and virulent bacterial pathogens (P.syringae).1 Publication

Gene expression databases

ExpressionAtlasiP27323. baseline and differential.
GenevisibleiP27323. AT.

Interactioni

Subunit structurei

Homodimer (PubMed:24036116). Interacts with RAR1 (PubMed:14504384, PubMed:17148606). Interacts with OEP61, OEP64 and OM64 (PubMed:24036116).3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FKBP62Q389314EBI-1778266,EBI-2409351

Protein-protein interaction databases

BioGridi20586. 16 interactions.
DIPiDIP-47087N.
IntActiP27323. 5 interactions.
STRINGi3702.AT5G52640.1.

Structurei

3D structure databases

ProteinModelPortaliP27323.
SMRiP27323. Positions 3-670.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi696 – 7005TPR repeat-binding

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi247 – 2537Poly-Lys

Domaini

The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins.By similarity

Sequence similaritiesi

Belongs to the heat shock protein 90 family.Curated

Phylogenomic databases

eggNOGiKOG0019. Eukaryota.
COG0326. LUCA.
HOGENOMiHOG000031988.
InParanoidiP27323.
KOiK04079.
PhylomeDBiP27323.

Family and domain databases

Gene3Di3.30.565.10. 1 hit.
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.

P27323-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADAETFAFQ AEINQLLSLI INTFYSNKEI FLRELISNSS DALDKIRFES
60 70 80 90 100
LTDKSKLDGQ PELFIRLVPD KSNKTLSIID SGIGMTKADL VNNLGTIARS
110 120 130 140 150
GTKEFMEALQ AGADVSMIGQ FGVGFYSAYL VAEKVVVTTK HNDDEQYVWE
160 170 180 190 200
SQAGGSFTVT RDVDGEPLGR GTKITLFLKD DQLEYLEERR LKDLVKKHSE
210 220 230 240 250
FISYPIYLWT EKTTEKEISD DEDEDEPKKE NEGEVEEVDE EKEKDGKKKK
260 270 280 290 300
KIKEVSHEWE LINKQKPIWL RKPEEITKEE YAAFYKSLTN DWEDHLAVKH
310 320 330 340 350
FSVEGQLEFK AILFVPKRAP FDLFDTRKKL NNIKLYVRRV FIMDNCEELI
360 370 380 390 400
PEYLSFVKGV VDSDDLPLNI SRETLQQNKI LKVIRKNLVK KCIEMFNEIA
410 420 430 440 450
ENKEDYTKFY EAFSKNLKLG IHEDSQNRGK IADLLRYHST KSGDEMTSFK
460 470 480 490 500
DYVTRMKEGQ KDIFYITGES KKAVENSPFL ERLKKRGYEV LYMVDAIDEY
510 520 530 540 550
AVGQLKEYDG KKLVSATKEG LKLEDETEEE KKKREEKKKS FENLCKTIKE
560 570 580 590 600
ILGDKVEKVV VSDRIVDSPC CLVTGEYGWT ANMERIMKAQ ALRDSSMSGY
610 620 630 640 650
MSSKKTMEIN PDNGIMEELR KRAEADKNDK SVKDLVMLLY ETALLTSGFS
660 670 680 690 700
LDEPNTFAAR IHRMLKLGLS IDEDENVEED GDMPELEEDA AEESKMEEVD
Length:700
Mass (Da):80,635
Last modified:December 6, 2002 - v3
Checksum:i5B379E915757EC7B
GO

Sequence cautioni

The sequence AAA32822.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAM91104.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAN46890.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AED96244.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAA98082.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAA68885.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti72 – 721S → A in AAA32822 (PubMed:16667903).Curated
Sequence conflicti72 – 721S → P in CAA68885 (PubMed:9426614).Curated
Sequence conflicti175 – 1751T → S in AAA32822 (PubMed:16667903).Curated
Sequence conflicti175 – 1751T → S in CAA68885 (PubMed:9426614).Curated
Sequence conflicti210 – 2101T → I in BAA00615 (PubMed:7697294).Curated
Sequence conflicti241 – 2411E → K in CAA68885 (PubMed:9426614).Curated
Sequence conflicti281 – 2811Y → S in AAA32822 (PubMed:16667903).Curated
Sequence conflicti478 – 4781Missing in CAA68885 (PubMed:9426614).Curated
Sequence conflicti618 – 6181E → D in CAA68885 (PubMed:9426614).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M62984 mRNA. Translation: AAA32822.1. Different initiation.
D00710 Genomic DNA. Translation: BAA00615.1.
Y07613 Genomic DNA. Translation: CAA68885.1. Different initiation.
AB025606 Genomic DNA. Translation: BAA98082.1. Different initiation.
CP002688 Genomic DNA. Translation: AED96244.1. Different initiation.
AY128296 mRNA. Translation: AAM91104.1. Different initiation.
BT001091 mRNA. Translation: AAN46890.1. Different initiation.
PIRiA45508.
RefSeqiNP_200076.1. NM_124642.3.
UniGeneiAt.25471.

Genome annotation databases

EnsemblPlantsiAT5G52640.1; AT5G52640.1; AT5G52640.
GeneIDi835341.
GrameneiAT5G52640.1; AT5G52640.1; AT5G52640.
KEGGiath:AT5G52640.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M62984 mRNA. Translation: AAA32822.1. Different initiation.
D00710 Genomic DNA. Translation: BAA00615.1.
Y07613 Genomic DNA. Translation: CAA68885.1. Different initiation.
AB025606 Genomic DNA. Translation: BAA98082.1. Different initiation.
CP002688 Genomic DNA. Translation: AED96244.1. Different initiation.
AY128296 mRNA. Translation: AAM91104.1. Different initiation.
BT001091 mRNA. Translation: AAN46890.1. Different initiation.
PIRiA45508.
RefSeqiNP_200076.1. NM_124642.3.
UniGeneiAt.25471.

3D structure databases

ProteinModelPortaliP27323.
SMRiP27323. Positions 3-670.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi20586. 16 interactions.
DIPiDIP-47087N.
IntActiP27323. 5 interactions.
STRINGi3702.AT5G52640.1.

PTM databases

iPTMnetiP27323.

Proteomic databases

PaxDbiP27323.
PRIDEiP27323.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G52640.1; AT5G52640.1; AT5G52640.
GeneIDi835341.
GrameneiAT5G52640.1; AT5G52640.1; AT5G52640.
KEGGiath:AT5G52640.

Organism-specific databases

TAIRiAT5G52640.

Phylogenomic databases

eggNOGiKOG0019. Eukaryota.
COG0326. LUCA.
HOGENOMiHOG000031988.
InParanoidiP27323.
KOiK04079.
PhylomeDBiP27323.

Enzyme and pathway databases

ReactomeiR-ATH-3371511. HSF1 activation.
R-ATH-3371568. Attenuation phase.
R-ATH-3371571. HSF1-dependent transactivation.
R-ATH-844456. The NLRP3 inflammasome.

Miscellaneous databases

PROiP27323.

Gene expression databases

ExpressionAtlasiP27323. baseline and differential.
GenevisibleiP27323. AT.

Family and domain databases

Gene3Di3.30.565.10. 1 hit.
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. "Sequence and expression of a HSP83 from Arabidopsis thaliana."
    Conner T.W., Lafayette P.R., Nagao R.T., Key J.L.
    Plant Physiol. 94:1689-1695(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Columbia.
    Tissue: Leaf.
  2. "Analysis of tissue-specific expression of Arabidopsis thaliana HSP90-family gene HSP81."
    Yabe N., Takahashi T., Komeda Y.
    Plant Cell Physiol. 35:1207-1219(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: cv. Columbia.
    Tissue: Seed.
  3. "Genomic organization of hsp90 gene family in Arabidopsis."
    Milioni D., Hatzopoulos P.
    Plant Mol. Biol. 35:955-961(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: cv. Landsberg erecta.
  4. "Structural analysis of Arabidopsis thaliana chromosome 5. XI."
    Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H., Tabata S.
    Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  5. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  6. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  7. "The Hsp90 family of proteins in Arabidopsis thaliana."
    Krishna P., Gloor G.
    Cell Stress Chaperones 6:238-246(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, NOMENCLATURE.
  8. "HSP90 interacts with RAR1 and SGT1 and is essential for RPS2-mediated disease resistance in Arabidopsis."
    Takahashi A., Casais C., Ichimura K., Shirasu K.
    Proc. Natl. Acad. Sci. U.S.A. 100:11777-11782(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RAR1, INDUCTION, DISRUPTION PHENOTYPE.
  9. "Tight regulation of expression of two Arabidopsis cytosolic Hsp90 genes during embryo development."
    Prasinos C., Krampis K., Samakovli D., Hatzopoulos P.
    J. Exp. Bot. 56:633-644(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.
  10. "RAR1, a central player in plant immunity, is targeted by Pseudomonas syringae effector AvrB."
    Shang Y., Li X., Cui H., He P., Thilmony R., Chintamanani S., Zwiesler-Vollick J., Gopalan S., Tang X., Zhou J.M.
    Proc. Natl. Acad. Sci. U.S.A. 103:19200-19205(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAR1.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Root.
  12. "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana."
    Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., Rathjen J.P., Peck S.C.
    J. Proteomics 72:439-451(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: cv. Columbia.
  13. "Tandem affinity purification and mass spectrometric analysis of ubiquitylated proteins in Arabidopsis."
    Saracco S.A., Hansson M., Scalf M., Walker J.M., Smith L.M., Vierstra R.D.
    Plant J. 59:344-358(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS].
  14. "Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
    Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
    Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Quantification of interaction strengths between chaperones and tetratricopeptide repeat domain-containing membrane proteins."
    Schweiger R., Soll J., Jung K., Heermann R., Schwenkert S.
    J. Biol. Chem. 288:30614-30625(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: HOMODIMERIZATION, INTERACTION WITH OEP61; OEP64 AND OM64.
  16. "Structural and functional differences of cytosolic 90-kDa heat-shock proteins (Hsp90s) in Arabidopsis thaliana."
    Cha J.Y., Ahn G., Kim J.Y., Kang S.B., Kim M.R., Su'udi M., Kim W.Y., Son D.
    Plant Physiol. Biochem. 70:368-373(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiHS901_ARATH
AccessioniPrimary (citable) accession number: P27323
Secondary accession number(s): Q03930
, Q8H0Z5, Q96268, Q9LTF3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: December 6, 2002
Last modified: June 8, 2016
This is version 142 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. 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.