SRPK2
Gene Ontology Biological Process
- RNA splicing [IDA]
- angiogenesis [ISS]
- innate immune response [IC]
- intracellular signal transduction [IDA]
- negative regulation of viral genome replication [IDA]
- nuclear speck organization [ISS]
- positive regulation of cell cycle [ISS]
- positive regulation of cell proliferation [IDA]
- positive regulation of gene expression [ISS]
- positive regulation of neuron apoptotic process [ISS]
- positive regulation of viral genome replication [IDA]
- protein phosphorylation [IDA]
- regulation of mRNA splicing, via spliceosome [TAS]
- spliceosomal complex assembly [IDA]
Gene Ontology Molecular Function
AP1M1
Gene Ontology Biological Process
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 Srpk2. We then purified thiophosphorylated peptides and identified Srpk2 substrates as well as their phosphorylation sites by MS
Curated By
- BioGRID