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

CIPK9

CBL-interacting protein kinase 9, F6F3.28, PKS6, PROTEIN KINASE 6, SNF1-RELATED PROTEIN KINASE 3.12, SnRK3.12, AT1G01140
CBL-interacting serine/threonine-protein kinase 9
Arabidopsis thaliana (Columbia)

Reconstituted Complex

An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator.

Publication

A protein kinase CIPK9 interacts with calcium sensor CBL3 and regulates K+ homeostasis under low-K+ stress in Arabidopsis.

Liu LL, Ren HM, Chen LQ, Wang Y, Wu WH

Potassium (K(+)) is an essential macronutrient for plant growth and development. The previous studies have demonstrated that CBL1/9 (Calcineurin B-Like protein 1 or 9) and CIPK23 (CBL-Interacting Protein Kinase 23) regulate K(+) uptake in Arabidopsis roots by modulating K(+) channel AKT1 (Arabidopsis K(+) Transporter 1). In this study, we show that the protein kinase CIPK9 interacts with the calcium sensor ... [more]

Plant Physiol. Oct. 29, 2012; 0(0); [Pubmed: 23109687]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
CBL2 CIPK9
FRET
FRET

An interaction is inferred when close proximity of interaction partners is detected by fluorescence resonance energy transfer between pairs of fluorophore-labeled molecules, such as occurs between CFP (donor) and YFP (acceptor) fusion proteins.

Low-BioGRID
1238178
CBL2 CIPK9
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
-
CIPK9 CBL2
Two-hybrid
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.

High-BioGRID
-
CBL2 CIPK9
Two-hybrid
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.

Low-BioGRID
-
CIPK9 CBL2
Two-hybrid
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.

Low-BioGRID
-
CBL2 CIPK9
Two-hybrid
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.

Low-BioGRID
-

Curated By

  • BioGRID