CLK1
Gene Ontology Biological Process
Gene Ontology Molecular Function
PRKDC
Gene Ontology Biological Process
- DNA repair [TAS]
- cellular protein modification process [TAS]
- cellular response to insulin stimulus [IMP]
- double-strand break repair [TAS]
- double-strand break repair via homologous recombination [IBA]
- double-strand break repair via nonhomologous end joining [TAS]
- innate immune response [TAS]
- negative regulation of protein phosphorylation [ISS]
- peptidyl-serine phosphorylation [IDA]
- positive regulation of transcription from RNA polymerase II promoter [IMP]
- positive regulation of type I interferon production [TAS]
- regulation of circadian rhythm [ISS]
- signal transduction involved in mitotic G1 DNA damage checkpoint [IMP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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
SR protein kinases promote splicing of nonconsensus introns.
Phosphorylation of the spliceosome is essential for RNA splicing, yet how and to what extent kinase signaling affects splicing have not been defined on a genome-wide basis. Using a chemical genetic approach, we show in Schizosaccharomyces pombe that the SR protein kinase Dsk1 is required for efficient splicing of introns with suboptimal splice sites. Systematic substrate mapping in fission yeast ... [more]
Throughput
- High Throughput
Additional Notes
- We labeled HeLa extracts with N6-phenethyl-ATP-gammaS in the presence of either recombinant WT or analog-sensitive Clk1. We then purified thiophosphorylated peptides and identified Clk1 substrates as well as their phosphorylation sites by MS
Curated By
- BioGRID