Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Combined Automated Annotation using Multiple IEA Methods
Nuclear protein phosphatases with Kelch-repeat domains modulate the response to brassinosteroids in Arabidopsis.
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BES1 is subject to antagonistic phosphorylation (by BIN2) and dephosphorylation (by BSU1) in the nucleus, i.e. BSU1 acts on BES1 as a phosphatase substrate.
"Our data indicate that BES1 is subject to antagonistic phosphorylation and dephosphorylation reactions in the nucleus"
Nucleocytoplasmic shuttling of BZR1 mediated by phosphorylation is essential in Arabidopsis brassinosteroid signaling.
Proteomic profiling of tandem affinity purified 14-3-3 protein complexes in Arabidopsis thaliana.
The CDG1 kinase mediates brassinosteroid signal transduction from BRI1 receptor kinase to BSU1 phosphatase and GSK3-like kinase BIN2.
Brassinosteroid signal transduction from cell-surface receptor kinases to nuclear transcription factors.