BAIT

CIPK23

ATCIPK23, CBL-interacting protein kinase 23, F12P21.6, F12P21_6, LKS1, LOW-K+-SENSITIVE 1, SNF1-RELATED PROTEIN KINASE 3.23, SnRK3.23, AT1G30270
CBL-interacting serine/threonine-protein kinase 23
GO Process (4)
GO Function (3)
GO Component (5)
Arabidopsis thaliana (Columbia)
PREY

ACT1

AAc1, ARABIDOPSIS ACTIN 1, F13M22.12, F13M22_12, actin 1, AT2G37620
actin 1
GO Process (3)
GO Function (1)
GO Component (6)
Arabidopsis thaliana (Columbia)

Biochemical Activity (Phosphorylation)

An interaction is inferred from the biochemical effect of one protein upon another, for example, GTP-GDP exchange activity or phosphorylation of a substrate by a kinase. The bait protein executes the activity on the substrate hit protein. A Modification value is recorded for interactions of this type with the possible values Phosphorylation, Ubiquitination, Sumoylation, Dephosphorylation, Methylation, Prenylation, Acetylation, Deubiquitination, Proteolytic Processing, Glucosylation, Nedd(Rub1)ylation, Deacetylation, No Modification, Demethylation.

Publication

Phosphorylation of calcineurin B-like (CBL) calcium sensor proteins by their CBL-interacting protein kinases (CIPKs) is required for full activity of CBL-CIPK complexes toward their target proteins.

Hashimoto K, Eckert C, Anschuetz U, Scholz M, Held K, Waadt R, Reyer A, Hippler M, Becker D, Kudla J

Calcineurin B-like proteins (CBLs) represent a family of calcium sensor proteins that interact with a group of serine/threonine kinases designated as CBL-interacting protein kinases (CIPKs). CBL-CIPK complexes are crucially involved in relaying plant responses to many environmental signals and in regulating ion fluxes. However, the biochemical characterization of CBL-CIPK complexes has so far been hampered by low activities of recombinant ... [more]

J. Biol. Chem. Mar. 09, 2012; 287(11);7956-68 [Pubmed: 22253446]

Throughput

  • Low Throughput

Curated By

  • BioGRID