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
CLU
Gene Ontology Biological Process
- blood coagulation [TAS]
- cell morphogenesis [IDA]
- central nervous system myelin maintenance [IMP]
- chaperone-mediated protein complex assembly [IDA]
- chaperone-mediated protein folding [IDA]
- complement activation [TAS]
- intrinsic apoptotic signaling pathway [IDA]
- lipid metabolic process [NAS]
- microglial cell activation [IDA]
- microglial cell proliferation [IDA]
- negative regulation of beta-amyloid formation [IDA]
- negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage [IMP]
- negative regulation of protein homooligomerization [IMP]
- platelet activation [TAS]
- platelet degranulation [TAS]
- positive regulation of NF-kappaB transcription factor activity [IMP]
- positive regulation of apoptotic process [IMP]
- positive regulation of beta-amyloid formation [ISS]
- positive regulation of intrinsic apoptotic signaling pathway [IMP]
- positive regulation of neurofibrillary tangle assembly [IMP]
- positive regulation of neuron death [IDA, IMP]
- positive regulation of nitric oxide biosynthetic process [IDA]
- positive regulation of proteasomal ubiquitin-dependent protein catabolic process [IMP]
- positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process [IMP]
- positive regulation of tau-protein kinase activity [IMP]
- positive regulation of tumor necrosis factor production [IDA]
- protein import [IDA]
- protein stabilization [IDA]
- regulation of beta-amyloid clearance [IDA]
- regulation of neuron death [IDA, IMP]
- regulation of neuronal signal transduction [IMP]
- release of cytochrome c from mitochondria [IC]
- response to misfolded protein [IDA]
- response to virus [IEP]
- reverse cholesterol transport [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
- apical dendrite [IDA]
- blood microparticle [IDA]
- cytoplasm [IDA]
- extracellular matrix [IDA]
- extracellular region [TAS]
- extracellular space [IDA]
- extracellular vesicular exosome [IDA]
- mitochondrion [IDA]
- neurofibrillary tangle [IDA]
- perinuclear region of cytoplasm [IDA]
- platelet alpha granule lumen [TAS]
- spherical high-density lipoprotein particle [IDA]
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