Q9FIR9 · LSU2_ARATH

Function

function

May be involved in defense responses monitoring (PubMed:21798943).
Probably implicated into osmotic stress signaling (PubMed:23517122).

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
Biological Processcellular oxidant detoxification
Biological Processcellular response to sulfur starvation
Biological Processchloroplast organization
Biological Processdefense response to bacterium
Biological Processdefense response to oomycetes
Biological Processpositive regulation of DNA-templated transcription
Biological Processregulation of defense response
Biological Processregulation of response to osmotic stress
Biological Processresponse to salt stress

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Protein RESPONSE TO LOW SULFUR 2
  • Alternative names
    • Protein ENHANCED DE-ETIOLATION 6

Gene names

    • Name
      LSU2
    • Synonyms
      END6
    • ORF names
      MXC17.2
    • Ordered locus names
      At5g24660

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
    Q9FIR9

Proteomes

Organism-specific databases

Genome annotation databases

Phenotypes & Variants

Disruption phenotype

Enhanced tolerance to osmotic stress (PubMed:23517122).
Increased susceptibility to pathogens such as P.syringae and H.arabidopsidis (PubMed:21798943).

Variants

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

The viewer provides 9 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_00004376931-94Protein RESPONSE TO LOW SULFUR 2

Proteomic databases

Expression

Induction

By stressful environmental conditions such as salt stress, AgNO3, and sulfur deficiency (PubMed:15842617, PubMed:25628631).
Induced during oxidative stress (PubMed:25628631).
Accumulates at the beginning of an extended night, which may indicate that it is induced by carbon starvation and in response to sugar (PubMed:25628631).
Induced by a combination of light and plastid signaling (PubMed:22383539).

Gene expression databases

Structure

Family & Domains

Features

Showing features for domain, coiled coil.

TypeIDPosition(s)Description
Domain14-61Death
Coiled coil15-63

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    94
  • Mass (Da)
    10,679
  • Last updated
    2001-03-01 v1
  • Checksum
    D8869AEDAA0378D5
MGKGGNYVTVAASEVDELRRKNGEMEKAVEEMKKEMLQLWRRTQVAEEAEERLCSQLAELEAESLDQARDYHSRIIFLMNELSRLSSDSASASP

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB016881
EMBL· GenBank· DDBJ
BAB09648.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002688
EMBL· GenBank· DDBJ
AED93346.1
EMBL· GenBank· DDBJ
Genomic DNA
AK118602
EMBL· GenBank· DDBJ
BAC43201.1
EMBL· GenBank· DDBJ
mRNA
BT004681
EMBL· GenBank· DDBJ
AAO42927.1
EMBL· GenBank· DDBJ
mRNA
AY086698
EMBL· GenBank· DDBJ
AAM63752.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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