P22953 · HS701_ARATH

Function

function

In cooperation with other chaperones, Hsp70s are key components that facilitate folding of de novo synthesized proteins, assist translocation of precursor proteins into organelles, and are responsible for degradation of damaged protein under stress conditions (Probable). 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 Hyaloperonospora parasitica (downy mildew). Plays a role with WPP-domain proteins in facilitating WIT1 nuclear envelope targeting (PubMed:12805626, PubMed:18065690, PubMed:19617588).
Modulates stomatal aperture in response to various environmental conditions and physiological responses to the hormone abscisic acid (ABA) (PubMed:21586649).

Miscellaneous

Plants overexpressing HSP70-1 show disabled immune responses, enhanced tolerance to heat shock and altered plant growth and development (PubMed:12805626).
Plants overexpressing HSP70-1 are hypersensitive to abscisic acid (ABA) in seed germination assays, and are compromised in the dark- and ABA-induced stomatal closure (PubMed:21586649).

GO annotations

all annotationsall molecular functionnucleotide bindingmolecular_functionnucleic acid bindingdna bindingchromatin bindingdna-binding transcription factor activityrna bindingcytoskeletal motor activitycatalytic activitynuclease activitysignaling receptor bindingstructural molecule activitytransporter activitybindingprotein bindingtranslation factor activity, rna bindinglipid bindingkinase activitytransferase activityhydrolase activityoxygen bindingenzyme regulator activitycarbohydrate bindingsignaling receptor activitytranslation regulator activitytranscription regulator activityother molecular functionall biological processcarbohydrate metabolic processgeneration of precursor metabolites and energynucleobase-containing compound metabolic processdna metabolic processtranslationlipid metabolic processtransportresponse to stresscell cyclecell communicationsignal transductioncell-cell signalingmulticellular organism developmentcircadian rhythmbiological_processmetabolic processcatabolic processbiosynthetic processresponse to light stimulusresponse to external stimulustropismresponse to biotic stimulusresponse to abiotic stimulusresponse to endogenous stimulusembryo developmentpost-embryonic developmentfruit ripeningabscissionpollinationflower developmentcellular processprogrammed cell deathphotosynthesiscellular component organizationcell growthprotein metabolic processcellular homeostasissecondary metabolic processreproductive processcell differentiationprotein modification processgrowthepigenetic regulation of gene expressionresponse to chemicalanatomical structure developmentregulation of molecular functionother biological processall cellular componentcellular_componentextracellular regioncell wallintracellular anatomical structurenucleusnuclear envelopenucleoplasmnucleoluscytoplasmmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuscytosolribosomecytoskeletonplasma membranechloroplastplastidthylakoidmembraneexternal encapsulating structureother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentapoplast
Cellular Componentchloroplast
Cellular Componentcytoplasm
Cellular Componentcytosol
Cellular Componentcytosolic ribosome
Cellular ComponentGolgi apparatus
Cellular Componentnucleolus
Cellular Componentnucleus
Cellular Componentplant-type cell wall
Cellular Componentplant-type vacuole
Cellular Componentplasma membrane
Cellular Componentplasmodesma
Molecular FunctionATP binding
Molecular FunctionATP-dependent protein folding chaperone
Molecular FunctionmRNA binding
Molecular Functionprotease binding
Biological Processdefense response to bacterium
Biological Processdefense response to fungus
Biological Processdefense response to other organism
Biological Processheat acclimation
Biological Processnegative regulation of seed germination
Biological Processresponse to heat
Biological Processresponse to virus
Biological Processstomatal closure

Keywords

Enzyme and pathway databases

Protein family/group databases

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

Names & Taxonomy

Protein names

  • Recommended name
    Heat shock 70 kDa protein 1
  • Alternative names
    • Heat shock cognate 70 kDa protein 1
    • Heat shock cognate protein 70-1
      (AtHsc70-1
      )
    • Heat shock protein 70-1
      (AtHsp70-1
      )
    • Protein EARLY-RESPONSIVE TO DEHYDRATION 2

Gene names

    • Name
      HSP70-1
    • Synonyms
      ERD2
      , HSC70-1
      , MED37_4
      , MED37E
    • ORF names
      T22P11.90
    • Ordered locus names
      At5g02500

Organism names

  • Taxonomic identifier
  • Strains
    • cv. Columbia
    • cv. Ostwestfalen
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis

Accessions

  • Primary accession
    P22953
  • Secondary accessions
    • Q93VU6
    • Q9LZ52

Proteomes

Organism-specific databases

Genome annotation databases

Phenotypes & Variants

Disruption phenotype

No visible phenotype under normal growth conditions (PubMed:21418353, PubMed:26408532, PubMed:28004282).
The double mutants hsp70-1 and hsp70-4 exhibit accelerated bolting, flowering, and branching, small round shape and flat leaf blades, thin stems and short siliques (PubMed:28004282).
The double mutants hsp70-1 and hsp70-4 exhibit reduced tolerance to abiotic stresses, such as heat, cold, salt and osmotic shock (PubMed:28004282).

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 12 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain.

TypeIDPosition(s)Description
Initiator methionine1Removed
Modified residue2N-acetylserine
ChainPRO_00000783442-651Heat shock 70 kDa protein 1

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed at a substantial level during normal growth in root, stem, leaf and flower tissues, but not in siliques (PubMed:8049382).
Expressed in cotyledons, leaves, stems, vascular bundles, roots, stigmas and anthers (PubMed:28004282).

Induction

Induced by heat shock and cold (PubMed:11402207).
Induced by dehydration stress and abscisic acid (ABA) (PubMed:8075396).
Up-regulated by viral infection (PubMed:15805473).

Developmental stage

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

Gene expression databases

Interaction

Subunit

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. Binds to TIR.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY P22953SGT1B Q9SUT53EBI-1238845, EBI-1581364

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region618-651Disordered

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete

This entry describes 1 isoforms produced by Alternative splicing. A number of isoforms are produced. According to EST sequences.

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.

  • Length
    651
  • Mass (Da)
    71,358
  • Last updated
    2000-12-01 v3
  • Checksum
    BD689BA0C936A420
MSGKGEGPAIGIDLGTTYSCVGVWQHDRVEIIANDQGNRTTPSYVAFTDSERLIGDAAKNQVAMNPVNTVFDAKRLIGRRFSDSSVQSDMKLWPFKIQAGPADKPMIYVEYKGEEKEFAAEEISSMVLIKMREIAEAYLGVTIKNAVVTVPAYFNDSQRQATKDAGVIAGLNVMRIINEPTAAAIAYGLDKKATSVGEKNVLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDNRMVNHFVQEFKRKSKKDITGNPRALRRLRTSCERAKRTLSSTAQTTIEIDSLYEGIDFYSTITRARFEELNMDLFRKCMEPVEKCLRDAKMDKSTVHDVVLVGGSTRIPKVQQLLQDFFNGKELCKSINPDEAVAYGAAVQGAILSGEGNEKVQDLLLLDVTPLSLGLETAGGVMTTLIPRNTTIPTKKEQVFSTYSDNQPGVLIQVYEGERARTKDNNLLGKFELSGIPPAPRGVPQITVCFDIDANGILNVSAEDKTTGQKNKITITNDKGRLSKDEIEKMVQEAEKYKSEDEEHKKKVEAKNALENYAYNMRNTIQDEKIGEKLPAADKKKIEDSIEQAIQWLEGNQLAEADEFEDKMKELESICNPIIAKMYQGAGGEAGGPGASGMDDDAPPASGGAGPKIEEVD

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
F4KCE5F4KCE5_ARATHHSC70-1521

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict65in Ref. 6; CAA54419
Sequence conflict195in Ref. 6; CAA54419
Sequence conflict195in Ref. 2; CAA52684
Sequence conflict372in Ref. 6; CAA54419
Sequence conflict376in Ref. 6; CAA54419
Sequence conflict507in Ref. 6; CAA54419

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X74604
EMBL· GenBank· DDBJ
CAA52684.1
EMBL· GenBank· DDBJ
mRNA
AL162971
EMBL· GenBank· DDBJ
CAB85987.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002688
EMBL· GenBank· DDBJ
AED90480.1
EMBL· GenBank· DDBJ
Genomic DNA
AY035123
EMBL· GenBank· DDBJ
AAK59628.2
EMBL· GenBank· DDBJ
mRNA
AY057481
EMBL· GenBank· DDBJ
AAL09715.1
EMBL· GenBank· DDBJ
mRNA
AY120747
EMBL· GenBank· DDBJ
AAM53305.1
EMBL· GenBank· DDBJ
mRNA
BT002754
EMBL· GenBank· DDBJ
AAO22583.1
EMBL· GenBank· DDBJ
mRNA
AH001335
EMBL· GenBank· DDBJ
AAA32819.1
EMBL· GenBank· DDBJ
Genomic DNA
X77199
EMBL· GenBank· DDBJ
CAA54419.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any 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. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp