BAIT

CBL2

ATCBL2, MDA7.3, MDA7_3, calcineurin B-like protein 2, AT5G55990
calcineurin B-like protein 2
GO Process (2)
GO Function (2)
GO Component (4)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Arabidopsis thaliana (Columbia)
PREY

SOS2

ATSOS2, CBL-INTERACTING PROTEIN KINASE 24, CIPK24, K21B8.3, K21B8_3, SALT OVERLY SENSITIVE 2, SNF1-RELATED PROTEIN KINASE 3.11, SNRK3.11, AT5G35410
CBL-interacting serine/threonine-protein kinase 24
GO Process (1)
GO Function (4)
GO Component (2)

Gene Ontology Biological Process

Gene Ontology Cellular Component

Arabidopsis thaliana (Columbia)

Two-hybrid

Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation.

Publication

Molecular characterization of functional domains in the protein kinase SOS2 that is required for plant salt tolerance.

Guo Y, Halfter U, Ishitani M, Zhu JK

The SOS3 (for SALT OVERLY SENSITIVE3) calcium binding protein and SOS2 protein kinase are required for sodium and potassium ion homeostasis and salt tolerance in Arabidopsis. We have shown previously that SOS3 interacts with and activates the SOS2 protein kinase. We report here the identification of a SOS3 binding motif in SOS2 that also serves as the kinase autoinhibitory domain. ... [more]

Plant Cell Jun. 01, 2001; 13(6);1383-400 [Pubmed: 11402167]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
SOS2 CBL2
Biochemical Activity
Biochemical Activity

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.

Low-BioGRID
1238961
CBL2 SOS2
PCA
PCA

A Protein-Fragment Complementation Assay (PCA) is a protein-protein interaction assay in which a bait protein is expressed as fusion to one of the either N- or C- terminal peptide fragments of a reporter protein and prey protein is expressed as fusion to the complementary N- or C- terminal fragment of the same reporter protein. Interaction of bait and prey proteins bring together complementary fragments, which can then fold into an active reporter, e.g. the split-ubiquitin assay.

Low-BioGRID
-

Curated By

  • BioGRID