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P22953 (MD37E_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable mediator of RNA polymerase II transcription subunit 37e
Alternative name(s):
Heat shock 70 kDa protein 1
Heat shock cognate 70 kDa protein 1
Heat shock cognate protein 70-1
Short name=AtHsc70-1
Heat shock protein 70-1
Short name=AtHsp70-1
Protein EARLY-RESPONSIVE TO DEHYDRATION 2
Gene names
Name:MED37E
Synonyms:ERD2, HSC70-1, HSP70-1, MED37_4
Ordered Locus Names:At5g02500
ORF Names:T22P11.90
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length651 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors By similarity. Ref.13 Ref.17 Ref.19

Heat shock protein probably involved in defense response. Chaperone involved in protein targeting to chloroplasts. May cooperate with SGT1 and HSP90 in R gene-mediated resistance towards the oomycete H.parasitica (downy mildew). Plays a role with WPP-domain proteins in facilitating WIT1 nuclear envelope targeting. Ref.13 Ref.17 Ref.19

In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage By similarity. Ref.13 Ref.17 Ref.19

Subunit structure

Binds to the deubiquitinating enzyme AMSH3. Interacts with SGT1B (via SGS domain). Interacts with OEP61. Interacts with HSFA1A/HSF1. Interacts with BAG3, BAG4 and BAG5. Interacts with WPP1, WPP2 and WIT1. Component of a ternary complex composed of WPP1, HSP70-1 and WIT1. Component of the Mediator complex Probable. Binds to TIR. Ref.9 Ref.12 Ref.15 Ref.16 Ref.17 Ref.19 Ref.20 Ref.21 Ref.23

Subcellular location

Cytoplasm. Nucleus Ref.17 Ref.22.

Tissue specificity

Expressed at a substantial level during normal growth in root, stem, leaf and flower tissues, but not in siliques. Ref.1

Developmental stage

Down-regulated during seed maturation. Up-regulated during germination. Ref.11

Induction

By heat shock, cold, dehydration stress and abscisic acid (ABA). Up-regulated by virus infection. Ref.5 Ref.7 Ref.11 Ref.14

Post-translational modification

Ubiquitinated.

Disruption phenotype

No visible phenotype. Ref.22

Miscellaneous

Plants overexpressing HSC70-1 show disabled immune responses, enhanced tolerance to heat shock and altered plant growth and development.

Sequence similarities

Belongs to the heat shock protein 70 (TC 1.A.33) family. DnaK subfamily. [View classification]

Ontologies

Keywords
   Biological processPlant defense
Stress response
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Nucleotide-binding
   Molecular functionChaperone
   PTMAcetylation
Isopeptide bond
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processdefense response to bacterium

Inferred from mutant phenotype Ref.17. Source: UniProtKB

defense response to fungus

Inferred from mutant phenotype Ref.17. Source: UniProtKB

negative regulation of seed germination

Inferred from mutant phenotype PubMed 21586649. Source: TAIR

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

response to cadmium ion

Inferred from expression pattern PubMed 16502469. Source: TAIR

response to cold

Inferred from expression pattern PubMed 14617066. Source: TAIR

response to heat

Inferred from mutant phenotype Ref.17. Source: UniProtKB

response to virus

Inferred from expression pattern Ref.14. Source: TAIR

stomatal closure

Inferred from mutant phenotype PubMed 21586649. Source: TAIR

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentGolgi apparatus

Inferred from direct assay PubMed 22430844. Source: TAIR

apoplast

Inferred from direct assay PubMed 18538804PubMed 21798377. Source: TAIR

cell wall

Inferred from direct assay PubMed 16287169. Source: TAIR

chloroplast

Inferred from direct assay PubMed 15028209PubMed 18431481. Source: TAIR

cytoplasm

Inferred from direct assay Ref.17. Source: UniProtKB

cytosol

Inferred from direct assay Ref.22. Source: TAIR

cytosolic ribosome

Inferred from direct assay PubMed 15821981. Source: TAIR

membrane

Inferred from direct assay PubMed 17432890. Source: TAIR

nucleolus

Inferred from direct assay PubMed 15496452. Source: TAIR

nucleus

Inferred from direct assay PubMed 14617066Ref.22. Source: TAIR

plasma membrane

Inferred from direct assay PubMed 17317660PubMed 17644812. Source: TAIR

plasmodesma

Inferred from direct assay PubMed 21533090. Source: TAIR

vacuolar membrane

Inferred from direct assay PubMed 17151019. Source: TAIR

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protease binding

Inferred from physical interaction Ref.20. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.17. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SGT1BQ9SUT53EBI-1238845,EBI-1581364

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: P22953-1)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 651650Probable mediator of RNA polymerase II transcription subunit 37e
PRO_0000078344

Amino acid modifications

Modified residue21N-acetylserine Ref.8
Cross-link457Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.18

Experimental info

Sequence conflict651N → S in CAA54419. Ref.6
Sequence conflict1951S → R in CAA54419. Ref.6
Sequence conflict1951S → T in CAA52684. Ref.2
Sequence conflict3721D → V in CAA54419. Ref.6
Sequence conflict3761A → V in CAA54419. Ref.6
Sequence conflict5071I → V in CAA54419. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 1, 2000. Version 3.
Checksum: BD689BA0C936A420

FASTA65171,358
        10         20         30         40         50         60 
MSGKGEGPAI GIDLGTTYSC VGVWQHDRVE IIANDQGNRT TPSYVAFTDS ERLIGDAAKN 

        70         80         90        100        110        120 
QVAMNPVNTV FDAKRLIGRR FSDSSVQSDM KLWPFKIQAG PADKPMIYVE YKGEEKEFAA 

       130        140        150        160        170        180 
EEISSMVLIK MREIAEAYLG VTIKNAVVTV PAYFNDSQRQ ATKDAGVIAG LNVMRIINEP 

       190        200        210        220        230        240 
TAAAIAYGLD KKATSVGEKN VLIFDLGGGT FDVSLLTIEE GIFEVKATAG DTHLGGEDFD 

       250        260        270        280        290        300 
NRMVNHFVQE FKRKSKKDIT GNPRALRRLR TSCERAKRTL SSTAQTTIEI DSLYEGIDFY 

       310        320        330        340        350        360 
STITRARFEE LNMDLFRKCM EPVEKCLRDA KMDKSTVHDV VLVGGSTRIP KVQQLLQDFF 

       370        380        390        400        410        420 
NGKELCKSIN PDEAVAYGAA VQGAILSGEG NEKVQDLLLL DVTPLSLGLE TAGGVMTTLI 

       430        440        450        460        470        480 
PRNTTIPTKK EQVFSTYSDN QPGVLIQVYE GERARTKDNN LLGKFELSGI PPAPRGVPQI 

       490        500        510        520        530        540 
TVCFDIDANG ILNVSAEDKT TGQKNKITIT NDKGRLSKDE IEKMVQEAEK YKSEDEEHKK 

       550        560        570        580        590        600 
KVEAKNALEN YAYNMRNTIQ DEKIGEKLPA ADKKKIEDSI EQAIQWLEGN QLAEADEFED 

       610        620        630        640        650 
KMKELESICN PIIAKMYQGA GGEAGGPGAS GMDDDAPPAS GGAGPKIEEV D 

« Hide

References

« Hide 'large scale' references
[1]"Isolation of a cDNA encoding a 70 kDa heat-shock cognate protein expressed in vegetative tissues of Arabidopsis thaliana."
Wu S.H., Wang C., Chen J., Lin B.-L.
Plant Mol. Biol. 25:577-583(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Strain: cv. Columbia.
[2]"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K. expand/collapse author list , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
Nature 408:823-826(2000) [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. expand/collapse author list , 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]"Characterization of an hsp70 cognate gene family in Arabidopsis."
Wu C.H., Caspar T., Browse J., Lindquist S., Somerville C.R.
Plant Physiol. 88:731-740(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-120, INDUCTION.
[6]King K.
Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 15-651.
Strain: cv. Ostwestfalen.
Tissue: Leaf.
[7]"Cloning of cDNAs for genes that are early-responsive to dehydration stress (ERDs) in Arabidopsis thaliana L.: identification of three ERDs as HSP cognate genes."
Kiyosue T., Yamaguchi-shinozaki K., Shinozaki K.
Plant Mol. Biol. 25:791-798(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY DEHYDRATION STRESS AND ABA.
[8]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[9]"The nucleotide sequence of a cDNA encoding the AtTIR, a TIR-like resistance protein in Arabidopsis thaliana."
Kroczynska B., Ciesielski A., Stachnik K.
Plant Gene Register PGR99-172
Cited for: INTERACTION WITH TIR.
Strain: cv. Columbia.
[10]"Genomic analysis of the Hsp70 superfamily in Arabidopsis thaliana."
Lin B.L., Wang J.S., Liu H.C., Chen R.W., Meyer Y., Barakat A., Delseny M.
Cell Stress Chaperones 6:201-208(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE FAMILY, NOMENCLATURE.
[11]"Comprehensive expression profile analysis of the Arabidopsis Hsp70 gene family."
Sung D.Y., Vierling E., Guy C.L.
Plant Physiol. 126:789-800(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: DNAK GENE SUBFAMILY, INDUCTION, DEVELOPMENTAL STAGE.
[12]"Interaction between Arabidopsis heat shock transcription factor 1 and 70 kDa heat shock proteins."
Kim B.H., Schoeffl F.
J. Exp. Bot. 53:371-375(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HSFA1A/HSF1.
[13]"Physiological and molecular assessment of altered expression of Hsc70-1 in Arabidopsis. Evidence for pleiotropic consequences."
Sung D.Y., Guy C.L.
Plant Physiol. 132:979-987(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[14]"Virus induction of heat shock protein 70 reflects a general response to protein accumulation in the plant cytosol."
Aparicio F., Thomas C.L., Lederer C., Niu Y., Wang D., Maule A.J.
Plant Physiol. 138:529-536(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[15]"AtBAG6, a novel calmodulin-binding protein, induces programmed cell death in yeast and plants."
Kang C.H., Jung W.Y., Kang Y.H., Kim J.Y., Kim D.G., Jeong J.C., Baek D.W., Jin J.B., Lee J.Y., Kim M.O., Chung W.S., Mengiste T., Koiwa H., Kwak S.S., Bahk J.D., Lee S.Y., Nam J.S., Yun D.J., Cho M.J.
Cell Death Differ. 13:84-95(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BAG3 AND BAG5.
[16]"Identification and functional characterization of the BAG protein family in Arabidopsis thaliana."
Doukhanina E.V., Chen S., van der Zalm E., Godzik A., Reed J., Dickman M.B.
J. Biol. Chem. 281:18793-18801(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BAG4.
[17]"Interaction between SGT1 and cytosolic/nuclear HSC70 chaperones regulates Arabidopsis immune responses."
Noel L.D., Cagna G., Stuttmann J., Wirthmueller L., Betsuyaku S., Witte C.P., Bhat R., Pochon N., Colby T., Parker J.E.
Plant Cell 19:4061-4076(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SGT1B, SUBCELLULAR LOCATION.
[18]"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] AT LYS-457.
[19]"WPP-domain proteins mimic the activity of the HSC70-1 chaperone in preventing mistargeting of RanGAP1-anchoring protein WIT1."
Brkljacic J., Zhao Q., Meier I.
Plant Physiol. 151:142-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH WPP1; WPP2 AND WIT1, FUNCTION.
[20]"The deubiquitinating enzyme AMSH3 is required for intracellular trafficking and vacuole biogenesis in Arabidopsis thaliana."
Isono E., Katsiarimpa A., Mueller I.K., Anzenberger F., Stierhof Y.-D., Geldner N., Chory J., Schwechheimer C.
Plant Cell 22:1826-1837(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AMSH3.
[21]"OEP61 is a chaperone receptor at the plastid outer envelope."
von Loeffelholz O., Kriechbaumer V., Ewan R.A., Jonczyk R., Lehmann S., Young J.C., Abell B.M.
Biochem. J. 438:143-153(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH OEP61.
[22]"AtHsp70-15-deficient Arabidopsis plants are characterized by reduced growth, a constitutive cytosolic protein response and enhanced resistance to TuMV."
Jungkunz I., Link K., Vogel F., Voll L.M., Sonnewald S., Sonnewald U.
Plant J. 66:983-995(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
[23]"The Mediator complex in plants: structure, phylogeny, and expression profiling of representative genes in a dicot (Arabidopsis) and a monocot (rice) during reproduction and abiotic stress."
Mathur S., Vyas S., Kapoor S., Tyagi A.K.
Plant Physiol. 157:1609-1627(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION, SUBUNIT, NOMENCLATURE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X74604 mRNA. Translation: CAA52684.1.
AL162971 Genomic DNA. Translation: CAB85987.1.
CP002688 Genomic DNA. Translation: AED90480.1.
AY035123 mRNA. Translation: AAK59628.2.
AY057481 mRNA. Translation: AAL09715.1.
AY120747 mRNA. Translation: AAM53305.1.
BT002754 mRNA. Translation: AAO22583.1.
M23108, M23105 Genomic DNA. Translation: AAA32819.1.
X77199 Genomic DNA. Translation: CAA54419.1.
PIRS46302.
T48271.
RefSeqNP_195870.1. NM_120328.4. [P22953-1]
UniGeneAt.23663.

3D structure databases

ProteinModelPortalP22953.
SMRP22953. Positions 6-619.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid16298. 17 interactions.
IntActP22953. 9 interactions.
MINTMINT-8061914.

Protein family/group databases

TCDB1.A.33.1.1. the cation channel-forming heat shock protein-70 (hsp70) family.

2D gel databases

SWISS-2DPAGEP22953.
World-2DPAGE0003:P22953.

Proteomic databases

PaxDbP22953.
PRIDEP22953.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G02500.1; AT5G02500.1; AT5G02500. [P22953-1]
GeneID831020.
KEGGath:AT5G02500.

Organism-specific databases

TAIRAT5G02500.

Phylogenomic databases

eggNOGCOG0443.
HOGENOMHOG000228135.
InParanoidP22953.
KOK03283.
OMAFEDSAVQ.
PhylomeDBP22953.

Enzyme and pathway databases

BioCycARA:GQT-225-MONOMER.
ARA:GQT-44-MONOMER.

Gene expression databases

GenevestigatorP22953.

Family and domain databases

Gene3D1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProIPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSPR00301. HEATSHOCK70.
SUPFAMSSF100920. SSF100920. 1 hit.
SSF100934. SSF100934. 1 hit.
PROSITEPS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMD37E_ARATH
AccessionPrimary (citable) accession number: P22953
Secondary accession number(s): Q93VU6, Q9LZ52
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: December 1, 2000
Last modified: July 9, 2014
This is version 132 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names