BAIT

NIK2

NSP-interacting kinase 2, AT3G25560
NSP-interacting kinase 2
GO Process (1)
GO Function (1)
GO Component (0)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Arabidopsis thaliana (Columbia)
PREY

SAC52

F14L17.9, F14L17_9, RPL10, RPL10A, SUPPRESSOR OF ACAULIS 52, ribosomal protein L10, ribosomal protein L10 A, AT1G14320
60S ribosomal protein L10-1
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

The ribosomal protein L10/QM-like protein is a component of the NIK-mediated antiviral signaling.

Rocha CS, Santos AA, Machado JP, Fontes EP

The NIK (NSP-interacting kinase)-mediated antiviral signaling pathway was identified as a virulence target of the begomovirus nuclear shuttle protein (NSP). Here, we further characterized this layer of plant innate defense by identifying the ribosomal protein L10 (rpL10), a QM-like protein, as a downstream effector of the antiviral signaling. Although both ribosomal proteins rpL10 and rpL18 were found to associate with ... [more]

Virology Oct. 25, 2008; 380(2);165-9 [Pubmed: 18789471]

Throughput

  • Low Throughput

Curated By

  • BioGRID