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Protein

Heat shock protein 90-2

Gene

HSP90-2

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

Functioni

Molecular chaperone. Involved in RPM1-mediated resistance. Component of the RPM1/RAR1/SGT1 complex. May stabilize RPM1 and protect it from SGT1-mediated degradation. Associates with RAR1 which may function as co-chaperone. Possesses ATPase activity (PubMed:14592967, PubMed:19487680). In the absence of heat shock, negatively regulates heat-inducible genes by actively suppressing heat shock transcription factor A1D (HSFA1D) function (PubMed:17965410). Involved in the induction of heat shock transcription factor A2 (HSFA2) expression in response to oxidative stress (PubMed:20147301). Required for stomatal closure and modulates transcriptional and physiological responses to abscisic acid (ABA) (PubMed:21586649). Regulates RPP4-mediated temperature-dependent cell death and defense responses (PubMed:24611624). May assist SGT1B in the formation of SCF E3 ubiquitin ligase complexes that target the immune receptors SNC1, RPS2 and RPS4 for degradation, to regulate receptor levels and avoid autoimmunity (PubMed:24889324).7 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 sitei371 – 3711ATPBy similarity

Regions

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

GO - Molecular functioni

  • ATPase activity Source: UniProtKB
  • ATP binding Source: UniProtKB-KW

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 90-2Curated
Short name:
AtHSP90.2Curated
Short name:
AtHsp90-21 Publication
Alternative name(s):
Heat shock protein 81-2Curated
Short name:
Hsp81-21 Publication
Protein EARLY-RESPONSIVE TO DEHYDRATION 8
Protein LOSS OF RECOGNITION OF AVRRPM1 2
Protein MUTANT SNC1-ENHANCING 121 Publication
Gene namesi
Name:HSP90-21 Publication
Synonyms:ERD8, HSP81-21 Publication, LRA2, MUSE121 Publication
Ordered Locus Names:At5g56030
ORF Names:MDA7.7
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G56030.

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 RPM1-mediated disease resistance.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi11 – 111A → T in hsp90.2-7; No effect on ATPase activity, dimerization and interaction with RAR1. Decreased interaction with SGT1B. 1 Publication
Mutagenesisi33 – 331R → H in muse12; enhances snc1-mediated autoimmune phenotypes. 1 Publication
Mutagenesisi41 – 411D → N in muse12; enhances snc1-mediated autoimmune phenotypes. 1 Publication
Mutagenesisi42 – 421A → T in hsp90.2-6; Loss of RPM1 function and accumulation. Loss of ATPase activity. Loss of dimerization. Loss of interaction with RAR1 and SGT1B. 1 Publication
Mutagenesisi80 – 801D → N in hsp90.2-3/lra2-3; Loss of RPM1 function and accumulation. Loss of ATPase activity. Loss of dimerization. Loss of interaction with RAR1 and SGT1B. 1 Publication
Mutagenesisi95 – 951G → E in hsp90.2-1/lra2-1; Loss of RPM1 function and accumulation. Loss of ATPase activity. Loss of dimerization. Loss of interaction with RAR1 and SGT1B. 1 Publication
Mutagenesisi100 – 1001S → F in hsp90.2-4/lra2-4; Loss of RPM1 function and accumulation. Loss of ATPase activity. Loss of dimerization. Normal interaction with RAR1. Loss of interaction with SGT1B. 1 Publication
Mutagenesisi337 – 3371R → C in hsp90.2-6; Decreased dimerization. Loss of ATPase activity and interaction with RAR1 and SGT1B. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 699699Heat shock protein 90-2PRO_0000062947Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei219 – 2191PhosphoserineBy similarity

Post-translational modificationi

Ubiquitinated.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP55737.
PRIDEiP55737.

PTM databases

iPTMnetiP55737.
SwissPalmiP55737.

Expressioni

Tissue specificityi

Present in all tissues. Most abundantly expressed in roots followed by floral bud clusters, flowers and young fruits.

Inductioni

In contrast to other major heat shock proteins, this one is also expressed at normal growth temperatures. Levels increase only slightly after heat shock.

Gene expression databases

ExpressionAtlasiP55737. baseline and differential.
GenevisibleiP55737. AT.

Interactioni

Subunit structurei

Homodimer (PubMed:19487680, PubMed:24036116). Interacts with RPM1, RAR1 and SGT1B (PubMed:14592967, PubMed:19487680). Interacts with OEP61, OEP64 and OM64 (PubMed:24036116). Interacts with HSFA1D (PubMed:17965410).4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CAM4P258542EBI-1235834,EBI-1235664
CAM6Q035092EBI-1235834,EBI-1236097
CAM7P592202EBI-1235834,EBI-1236031
CML9Q9S7442EBI-1235834,EBI-1236048

Protein-protein interaction databases

BioGridi20945. 16 interactions.
DIPiDIP-51470N.
IntActiP55737. 9 interactions.
STRINGi3702.AT5G56010.1.

Structurei

3D structure databases

ProteinModelPortaliP55737.
SMRiP55737. Positions 3-668.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi695 – 6995TPR repeat-binding

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi222 – 2265Poly-Glu
Compositional biasi246 – 2527Poly-Lys
Compositional biasi529 – 5324Poly-Lys
Compositional biasi670 – 6734Poly-Asp

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.
InParanoidiP55737.
PhylomeDBiP55737.

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.

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: P55737-1) [UniParc]FASTAAdd to basket

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
MADAETFAFQ AEINQLLSLI INTFYSNKEI FLRELISNSS DALDKIRFES
60 70 80 90 100
LTDKSKLDGQ PELFIHIIPD KTNNTLTIID SGIGMTKADL VNNLGTIARS
110 120 130 140 150
GTKEFMEALA AGADVSMIGQ FGVGFYSAYL VADKVVVTTK HNDDEQYVWE
160 170 180 190 200
SQAGGSFTVT RDTSGETLGR GTKMVLYLKE DQLEYLEERR LKDLVKKHSE
210 220 230 240 250
FISYPISLWI EKTIEKEISD DEEEEEKKDE EGKVEEVDEE KEKEEKKKKK
260 270 280 290 300
IKEVSHEWDL VNKQKPIWMR KPEEINKEEY AAFYKSLSND WEEHLAVKHF
310 320 330 340 350
SVEGQLEFKA ILFVPKRAPF DLFDTKKKPN NIKLYVRRVF IMDNCEDIIP
360 370 380 390 400
EYLGFVKGIV DSEDLPLNIS RETLQQNKIL KVIRKNLVKK CLELFFEIAE
410 420 430 440 450
NKEDYNKFYE AFSKNLKLGI HEDSQNRTKI AELLRYHSTK SGDELTSLKD
460 470 480 490 500
YVTRMKEGQN DIFYITGESK KAVENSPFLE KLKKKGIEVL YMVDAIDEYA
510 520 530 540 550
IGQLKEFEGK KLVSATKEGL KLDETEDEKK KKEELKEKFE GLCKVIKDVL
560 570 580 590 600
GDKVEKVIVS DRVVDSPCCL VTGEYGWTAN MERIMKAQAL RDSSMAGYMS
610 620 630 640 650
SKKTMEINPE NSIMDELRKR ADADKNDKSV KDLVLLLFET ALLTSGFSLD
660 670 680 690
EPNTFGSRIH RMLKLGLSID DDDAVEADAE MPPLEDDADA EGSKMEEVD
Length:699
Mass (Da):80,064
Last modified:November 1, 1997 - v1
Checksum:i78A6E490AE48E508
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti657 – 6571S → N in AAN31859 (PubMed:14593172).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB011476 Genomic DNA. Translation: BAB09285.1.
CP002688 Genomic DNA. Translation: AED96711.1.
AY062750 mRNA. Translation: AAL32828.1.
AY128805 mRNA. Translation: AAM91205.1.
BT000717 mRNA. Translation: AAN31859.1.
BT001944 mRNA. Translation: AAN71943.1.
BT002535 mRNA. Translation: AAO00895.1.
RefSeqiNP_200414.1. NM_124985.4. [P55737-1]
UniGeneiAt.25243.
At.27546.
At.45945.

Genome annotation databases

EnsemblPlantsiAT5G56030.1; AT5G56030.1; AT5G56030. [P55737-1]
GeneIDi835701.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB011476 Genomic DNA. Translation: BAB09285.1.
CP002688 Genomic DNA. Translation: AED96711.1.
AY062750 mRNA. Translation: AAL32828.1.
AY128805 mRNA. Translation: AAM91205.1.
BT000717 mRNA. Translation: AAN31859.1.
BT001944 mRNA. Translation: AAN71943.1.
BT002535 mRNA. Translation: AAO00895.1.
RefSeqiNP_200414.1. NM_124985.4. [P55737-1]
UniGeneiAt.25243.
At.27546.
At.45945.

3D structure databases

ProteinModelPortaliP55737.
SMRiP55737. Positions 3-668.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi20945. 16 interactions.
DIPiDIP-51470N.
IntActiP55737. 9 interactions.
STRINGi3702.AT5G56010.1.

PTM databases

iPTMnetiP55737.
SwissPalmiP55737.

Proteomic databases

PaxDbiP55737.
PRIDEiP55737.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G56030.1; AT5G56030.1; AT5G56030. [P55737-1]
GeneIDi835701.

Organism-specific databases

TAIRiAT5G56030.

Phylogenomic databases

eggNOGiKOG0019. Eukaryota.
COG0326. LUCA.
HOGENOMiHOG000031988.
InParanoidiP55737.
PhylomeDBiP55737.

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

PROiP55737.

Gene expression databases

ExpressionAtlasiP55737. baseline and differential.
GenevisibleiP55737. 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. "Isolation and analysis of the expression of two genes for the 81-kilodalton heat-shock proteins from Arabidopsis."
    Takahashi T., Naito S., Komeda Y.
    Plant Physiol. 99:383-390(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: cv. Columbia.
    Tissue: Seedling.
  2. "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence features of the regions of 1,381,565 bp covered by twenty one physically assigned P1 and TAC clones."
    Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N., Tabata S.
    DNA Res. 5:131-145(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "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.
  5. "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.
  6. "Cytosolic HSP90 associates with and modulates the Arabidopsis RPM1 disease resistance protein."
    Hubert D.A., Tornero P., Belkhadir Y., Krishna P., Takahashi A., Shirasu K., Dangl J.L.
    EMBO J. 22:5679-5689(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RPM1; RAR1 AND SGT1B, DISRUPTION PHENOTYPE, MUTAGENESIS OF ASP-80; GLY-95 AND SER-100.
  7. "Cytosolic HSP90 regulates the heat shock response that is responsible for heat acclimation in Arabidopsis thaliana."
    Yamada K., Fukao Y., Hayashi M., Fukazawa M., Suzuki I., Nishimura M.
    J. Biol. Chem. 282:37794-37804(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HSFA1D.
  8. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: cv. Columbia.
  9. "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].
  10. "Specific Arabidopsis HSP90.2 alleles recapitulate RAR1 cochaperone function in plant NB-LRR disease resistance protein regulation."
    Hubert D.A., He Y., McNulty B.C., Tornero P., Dangl J.L.
    Proc. Natl. Acad. Sci. U.S.A. 106:9556-9563(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RAR1 AND SGT1B, MUTAGENESIS OF ALA-11; ALA-42 AND ARG-337.
  11. "The 26S proteasome function and Hsp90 activity involved in the regulation of HsfA2 expression in response to oxidative stress."
    Nishizawa-Yokoi A., Tainaka H., Yoshida E., Tamoi M., Yabuta Y., Shigeoka S.
    Plant Cell Physiol. 51:486-496(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "The cytosolic/nuclear HSC70 and HSP90 molecular chaperones are important for stomatal closure and modulate abscisic acid-dependent physiological responses in Arabidopsis."
    Clement M., Leonhardt N., Droillard M.J., Reiter I., Montillet J.L., Genty B., Lauriere C., Nussaume L., Noel L.D.
    Plant Physiol. 156:1481-1492(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "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.
  14. "Arabidopsis HSP90 protein modulates RPP4-mediated temperature-dependent cell death and defense responses."
    Bao F., Huang X., Zhu C., Zhang X., Li X., Yang S.
    New Phytol. 202:1320-1334(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. "HSP90s are required for NLR immune receptor accumulation in Arabidopsis."
    Huang S., Monaghan J., Zhong X., Lin L., Sun T., Dong O.X., Li X.
    Plant J. 79:427-439(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ARG-33 AND ASP-41.

Entry informationi

Entry nameiHS902_ARATH
AccessioniPrimary (citable) accession number: P55737
Secondary accession number(s): Q8H158
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: May 11, 2016
This is version 134 of the entry and version 1 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.