| http://purl.uniprot.org/citations/10196197 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10196197 | http://www.w3.org/2000/01/rdf-schema#comment | "Serine/arginine-rich (SR) proteins play an important role in constitutive and alternative pre-mRNA splicing. The C-terminal arginine-serine domain of these proteins, such as SF2/ASF, mediates protein-protein interactions and is phosphorylated in vivo. Using glutathione S-transferase (GST)-SF2/ASF-affinity chromatography, the SF2/ASF kinase activity was co-purified from HeLa cells with a 95-kDa protein, which was recognized by an anti-SR protein kinase (SRPK) 1 monoclonal antibody. Recombinant SRPK1 and SRPK2 bound to and phosphorylated GST-SF2/ASF in vitro. Phosphopeptide mapping showed that identical sites were phosphorylated in the pull-down kinase reaction with HeLa extracts and by recombinant SRPKs. Epitope-tagged SF2/ASF transiently expressed in COS7 cells co-immunoprecipitated with SRPKs. Deletion analysis mapped the phosphorylation sites to a region containing an (Arg-Ser)8 repeat beginning at residue 204, and far-Western analysis showed that the region is required for binding of SRPKs to SF2/ASF. Further binding studies showed that SRPKs bound unphosphorylated SF2/ASF but did not bind phosphorylated SF2/ASF. Expression of an SRPK2 kinase-inactive mutant caused accumulation of SF2/ASF in the cytoplasm. These results suggest that the formation of complexes between SF2/ASF and SRPKs, which is influenced by the phosphorylation state of SF2/ASF, may have regulatory roles in the assembly and localization of this splicing factor."xsd:string |
| http://purl.uniprot.org/citations/10196197 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.274.16.11125"xsd:string |
| http://purl.uniprot.org/citations/10196197 | http://purl.uniprot.org/core/author | "Okamoto Y."xsd:string |
| http://purl.uniprot.org/citations/10196197 | http://purl.uniprot.org/core/author | "Krainer A.R."xsd:string |
| http://purl.uniprot.org/citations/10196197 | http://purl.uniprot.org/core/author | "Hagiwara M."xsd:string |
| http://purl.uniprot.org/citations/10196197 | http://purl.uniprot.org/core/author | "Mayeda A."xsd:string |
| http://purl.uniprot.org/citations/10196197 | http://purl.uniprot.org/core/author | "Koizumi J."xsd:string |
| http://purl.uniprot.org/citations/10196197 | http://purl.uniprot.org/core/author | "Onogi H."xsd:string |
| http://purl.uniprot.org/citations/10196197 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
| http://purl.uniprot.org/citations/10196197 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/10196197 | http://purl.uniprot.org/core/pages | "11125-11131"xsd:string |
| http://purl.uniprot.org/citations/10196197 | http://purl.uniprot.org/core/title | "The subcellular localization of SF2/ASF is regulated by direct interaction with SR protein kinases (SRPKs)."xsd:string |
| http://purl.uniprot.org/citations/10196197 | http://purl.uniprot.org/core/volume | "274"xsd:string |
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