Q9LZU4 · CRK4_ARATH

Function

Catalytic activity

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site357-365ATP (UniProtKB | ChEBI)
Binding site379ATP (UniProtKB | ChEBI)
Active site476Proton acceptor

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 Componentmembrane
Molecular FunctionATP binding
Molecular Functionprotein serine kinase activity
Molecular Functionprotein serine/threonine kinase activity
Biological Processdefense response to bacterium
Biological Processprogrammed cell death
Biological Processresponse to salicylic acid

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Cysteine-rich receptor-like protein kinase 4
  • EC number
  • Short names
    Cysteine-rich RLK4

Gene names

    • Name
      CRK4
    • ORF names
      F16L2_70
    • Ordered locus names
      At3g45860

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
    Q9LZU4

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

Membrane
; Single-pass membrane protein

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain17-287Extracellular
Transmembrane288-308Helical
Topological domain309-676Cytoplasmic

Keywords

PTM/Processing

Features

Showing features for signal, chain, glycosylation, modified residue.

TypeIDPosition(s)Description
Signal1-16
ChainPRO_000029505117-676Cysteine-rich receptor-like protein kinase 4
Glycosylation33N-linked (GlcNAc...) asparagine
Glycosylation46N-linked (GlcNAc...) asparagine
Glycosylation64N-linked (GlcNAc...) asparagine
Glycosylation152N-linked (GlcNAc...) asparagine
Glycosylation181N-linked (GlcNAc...) asparagine
Glycosylation243N-linked (GlcNAc...) asparagine
Glycosylation248N-linked (GlcNAc...) asparagine
Glycosylation286N-linked (GlcNAc...) asparagine
Modified residue424Phosphotyrosine
Modified residue516Phosphothreonine
Modified residue524Phosphotyrosine

Keywords

Proteomic databases

PTM databases

Expression

Induction

By salicylic acid (SA) or by a bacterial pathogen infection.

Gene expression databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain31-135Gnk2-homologous 1
Domain146-246Gnk2-homologous 2
Region252-279Disordered
Domain351-631Protein kinase

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CRK subfamily.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    676
  • Mass (Da)
    75,923
  • Last updated
    2000-10-01 v1
  • Checksum
    46DB72413084CC89
MSFFWLFPFLLHLSFADSLSPLSAPVQNFIHLNHSCPSSILTYSRNSTYFTNLKTLLSSLSSRNASYSTGFQTATAGQAPDRVTGLFLCRGDVSQEVCRNCVAFSVKETLYWCPYNKEVVLYYDECMLRYSHRNILSTVTYDGSAILLNGANISSSNQNQVDEFRDLVSSTLNLAAVEAANSSKKFYTRKVITPQPLYLLVQCTPDLTRQDCLRCLQKSIKGMSLYRIGGRFFYPSCNSRYENYSFYNETATRSSSPPSLPPRSTPQQQLKLAPPPLISERGKGRNSSVIIVVVVPIIALLLLFVAFFSLRAKKTRTNYEREPLTEESDDITTAGSLQFDFKAIEAATNKFCETNKLGQGGFGEVYKGIFPSGVQVAVKRLSKTSGQGEREFANEVIVVAKLQHRNLVRLLGFCLERDERILVYEFVPNKSLDYFIFDSTMQSLLDWTRRYKIIGGIARGILYLHQDSRLTIIHRDLKAGNILLGDDMNAKIADFGMARIFGMDQTEANTRRIVGTYGYMSPEYAMYGQFSMKSDVYSFGVLVLEIISGKKNSNVYQMDGTSAGNLVTYTWRLWSNGSPLELVDPSFRDNYRINEVSRCIHIALLCVQEEAEDRPTMSAIVQMLTTSSIALAVPQRPGFFFRSSKHEQVGLVDRLSINTSALCSVDDASITNVTPR

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AL162459
EMBL· GenBank· DDBJ
CAB82810.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002686
EMBL· GenBank· DDBJ
AEE78083.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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