Q9STH1 · HSOP3_ARATH

Function

function

Mediates the association of the molecular chaperones HSP70 and HSP90. Mediates nuclear encoded chloroplast preproteins binding to HSP90 prior to chloroplastic sorting (By similarity).
Involved in acclimation to heat

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 Componentcytosol
Cellular Componentnucleus
Molecular FunctionHsp90 protein binding
Molecular Functionpreprotein binding
Biological Processchaperone-mediated protein complex assembly
Biological Processheat acclimation

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Hsp70-Hsp90 organizing protein 3
  • Short names
    AtHop3

Gene names

    • Name
      HOP3
    • ORF names
      T4C9.240
    • Ordered locus names
      At4g12400

Organism names

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

Accessions

  • Primary accession
    Q9STH1
  • Secondary accessions
    • B9DG66
    • F4JQM6
    • Q8L724

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

Keywords

Phenotypes & Variants

Disruption phenotype

Decreased thermotolerance after a long recovery (2 days) under nonstress conditions following an acclimation heat treatment.

Variants

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

The viewer provides 113 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004267031-558Hsp70-Hsp90 organizing protein 3

Post-translational modification

Phosphorylated.
Acetylated.

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Co-chaperone that forms a complex with HSP70 and HSP90 and preproteins (e.g. chloroplast preproteins) (By similarity).

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for repeat, domain, region, compositional bias, motif.

TypeIDPosition(s)Description
Repeat2-35TPR 1
Repeat37-69TPR 2
Repeat70-103TPR 3
Domain131-170STI1 1
Repeat136-173TPR 4
Region191-232Disordered
Compositional bias193-232Basic and acidic residues
Motif227-244Bipartite nuclear localization signal
Repeat230-263TPR 5
Repeat265-297TPR 6
Repeat305-342TPR 7
Repeat369-402TPR 8
Repeat404-436TPR 9
Repeat437-470TPR 10
Domain507-546STI1 2

Domain

The tetratricopeptide repeat (TPR) domain, forming a carboxylate clamp (CC), mediates interaction with the highly conserved 'EEVD' motif at the C-terminal ends of HSP90 and HSP70.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

Q9STH1-1

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
    558
  • Mass (Da)
    63,706
  • Last updated
    2000-05-01 v1
  • Checksum
    47010D35F0F98DB9
MAEEAKSKGNAAFSSGDYATAITHFTEAINLSPTNHILYSNRSASYASLHRYEEALSDAKKTIELKPDWSKGYSRLGAAFIGLSKFDEAVDSYKKGLEIDPSNEMLKSGLADASRSRVSSKSNPFVDAFQGKEMWEKLTADPGTRVYLEQDDFVKTMKEIQRNPNNLNLYMKDKRVMKALGVLLNVKFGGSSGEDTEMKEADERKEPEPEMEPMELTEEERQKKERKEKALKEKGEGNVAYKKKDFGRAVEHYTKAMELDDEDISYLTNRAAVYLEMGKYEECIEDCDKAVERGRELRSDFKMIARALTRKGSALVKMARCSKDFEPAIETFQKALTEHRNPDTLKKLNDAEKVKKELEQQEYFDPTIAEEEREKGNGFFKEQKYPEAVKHYSEAIKRNPNDVRAYSNRAACYTKLGALPEGLKDAEKCIELDPSFTKGYSRKGAIQFFMKEYDKAMETYQEGLKHDPKNQEFLDGVRRCVEQINKASRGDLTPEELKERQAKAMQDPEVQNILSDPVMRQVLVDFQENPKAAQEHMKNPMVMNKIQKLVSAGIVQVR

Q9STH1-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Features

Showing features for sequence conflict, compositional bias, alternative sequence.

TypeIDPosition(s)Description
Sequence conflict98in Ref. 4; BAH19733
Compositional bias193-232Basic and acidic residues
Sequence conflict374in Ref. 3; AAM98143
Alternative sequenceVSP_053940523-530in isoform 2
Alternative sequenceVSP_053941531-558in isoform 2

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AL080318
EMBL· GenBank· DDBJ
CAB45987.1
EMBL· GenBank· DDBJ
Genomic DNA
AL161534
EMBL· GenBank· DDBJ
CAB78283.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002687
EMBL· GenBank· DDBJ
AEE83125.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002687
EMBL· GenBank· DDBJ
AEE83126.1
EMBL· GenBank· DDBJ
Genomic DNA
AY140001
EMBL· GenBank· DDBJ
AAM98143.1
EMBL· GenBank· DDBJ
mRNA
AK317040
EMBL· GenBank· DDBJ
BAH19733.1
EMBL· GenBank· DDBJ
mRNA

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