| http://purl.uniprot.org/citations/16376875 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16376875 | http://www.w3.org/2000/01/rdf-schema#comment | "Nucleophosmin (NPM) is a multifunctional phosphoprotein, being involved in ribosome assembly, pre-ribosomal RNA processing, DNA duplication, nucleocytoplasmic protein trafficking, and centrosome duplication. NPM is phosphorylated by several kinases, including nuclear kinase II, casein kinase 2, Polo-like kinase 1 and cyclin-dependent kinases (CDK1 and 2), and these phosphorylations modulate the activity and function of NPM. We have previously identified Thr(199) as the major phosphorylation site of NPM mediated by CDK2/cyclin E (and A), and this phosphorylation is involved in the regulation of centrosome duplication. In this study, we further examined the effect of CDK2-mediated phosphorylation of NPM by using the antibody that specifically recognizes NPM phosphorylated on Thr(199). We found that the phospho-Thr(199) NPM localized to dynamic sub-nuclear structures known as nuclear speckles, which are believed to be the sites of storage and/or assembly of pre-mRNA splicing factors. Phosphorylation on Thr(199) by CDK2/cyclin E (and A) targets NPM to nuclear speckles, and enhances the RNA-binding activity of NPM. Moreover, phospho-Thr(199) NPM, but not unphosphorylated NPM, effectively represses pre-mRNA splicing. These findings indicate the involvement of NPM in the regulation of pre-mRNA processing, and its activity is controlled by CDK2-mediated phosphorylation on Thr(199)."xsd:string |
| http://purl.uniprot.org/citations/16376875 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.febslet.2005.12.022"xsd:string |
| http://purl.uniprot.org/citations/16376875 | http://purl.uniprot.org/core/author | "Kim S.H."xsd:string |
| http://purl.uniprot.org/citations/16376875 | http://purl.uniprot.org/core/author | "Suzuki H."xsd:string |
| http://purl.uniprot.org/citations/16376875 | http://purl.uniprot.org/core/author | "Fukasawa K."xsd:string |
| http://purl.uniprot.org/citations/16376875 | http://purl.uniprot.org/core/author | "Tokuyama Y."xsd:string |
| http://purl.uniprot.org/citations/16376875 | http://purl.uniprot.org/core/author | "Shinmura K."xsd:string |
| http://purl.uniprot.org/citations/16376875 | http://purl.uniprot.org/core/author | "Mayeda A."xsd:string |
| http://purl.uniprot.org/citations/16376875 | http://purl.uniprot.org/core/author | "Tarapore P."xsd:string |
| http://purl.uniprot.org/citations/16376875 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
| http://purl.uniprot.org/citations/16376875 | http://purl.uniprot.org/core/name | "FEBS Lett"xsd:string |
| http://purl.uniprot.org/citations/16376875 | http://purl.uniprot.org/core/pages | "399-409"xsd:string |
| http://purl.uniprot.org/citations/16376875 | http://purl.uniprot.org/core/title | "Thr199 phosphorylation targets nucleophosmin to nuclear speckles and represses pre-mRNA processing."xsd:string |
| http://purl.uniprot.org/citations/16376875 | http://purl.uniprot.org/core/volume | "580"xsd:string |
| http://purl.uniprot.org/citations/16376875 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/16376875 |
| http://purl.uniprot.org/citations/16376875 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/16376875 |
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