BAIT

BAK1

ATBAK1, ATSERK3, BRI1-associated receptor kinase, ELG, ELONGATED, F17M5.190, F17M5_190, RECEPTOR KINASES LIKE SERK 10, RKS10, SERK3, SOMATIC EMBRYOGENESIS RECEPTOR-LIKE KINASE 3, AT4G33430
Leu-rich receptor Serine/threonine protein kinase BAK1
Arabidopsis thaliana (Columbia)
PREY

KAPP

RAG1, ROOT ATTENUATED GROWTH 1, T24G5.3, kinase associated protein phosphatase, AT5G19280
kinase associated protein phosphatase
GO Process (2)
GO Function (4)
GO Component (2)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Arabidopsis thaliana (Columbia)

Co-crystal Structure

Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.

Publication

Phosphoprotein and phosphopeptide interactions with the FHA domain from Arabidopsis kinase-associated protein phosphatase.

Ding Z, Wang H, Liang X, Morris ER, Gallazzi F, Pandit S, Skolnick J, Walker JC, Van Doren SR

FHA domains are phosphoThr recognition modules found in diverse signaling proteins, including kinase-associated protein phosphatase (KAPP) from Arabidopsis thaliana. The kinase-interacting FHA domain (KI-FHA) of KAPP targets it to function as a negative regulator of some receptor-like kinase (RLK) signaling pathways important in plant development and environmental responses. To aid in the identification of potential binding sites for the KI-FHA ... [more]

Biochemistry Mar. 13, 2007; 46(10);2684-96 [Pubmed: 17302430]

Throughput

  • Low Throughput

Additional Notes

  • nmr

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
BAK1 KAPP
Far Western
Far Western

An interaction is detected between a protein immobilized on a membrane and a purified protein probe.

Low-BioGRID
-

Curated By

  • BioGRID