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Literature summary extracted from

  • Horn, M.A.; Walker, J.C.
    Biochemical properties of the autophosphorylation of RLK5, a receptor-like protein kinase from Arabidopsis thaliana (1994), Biochim. Biophys. Acta, 1208, 65-74.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.10.2 expression of the catalytic domain as two different recombinant fusion proteins in Escherichia coli Arabidopsis thaliana

Protein Variants

EC Number Protein Variants Comment Organism
2.7.10.2 K711E substitution in the catalytic domain of RLK5 results in the catalytically inactive protein Arabidopsis thaliana

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.7.10.2 membrane RLK5 protein contains an extracellular domain that has 21 tandemly repeated leucine-rich motifs linked, via a transmembrane hydrophobic region Arabidopsis thaliana 16020
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.10.2 Mg2+ significantly greater activity in the presence of Mn2+ than Mg2+ Arabidopsis thaliana
2.7.10.2 Mn2+ significantly greater activity in the presence of Mn2+ than Mg2+ Arabidopsis thaliana

Organism

EC Number Organism UniProt Comment Textmining
2.7.10.2 Arabidopsis thaliana P47735
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.7.10.2 phosphoprotein several sites in the catalytic domain are phosphorylated Arabidopsis thaliana

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.10.2 ATP + a protein autophosphorylation Arabidopsis thaliana ADP + a phosphoprotein
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.10.2 receptor-like protein kinase 5 precursor
-
 Arabidopsis thaliana
2.7.10.2 RLK5
-
 Arabidopsis thaliana