| http://purl.uniprot.org/citations/20810653 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/20810653 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/20810653 | http://www.w3.org/2000/01/rdf-schema#comment | "The Slit-Robo GTPase-activating proteins (srGAPs) are critical for neuronal migration through inactivation of Rho GTPases Cdc42, Rac1, and RhoA. Here we report that srGAP2 physically interacts with protein arginine methyltransferase 5 (PRMT5). srGAP2 localizes to the cytoplasm and plasma membrane protrusion. srGAP2 knockdown reduces cell adhesion spreading and increases cell migration, but has no effect on cell proliferation. PRMT5 binds to the N terminus of srGAP2 (225-538 aa) and methylates its C-terminal arginine residue Arg-927. The methylation mutant srGAP2-R927A fails to rescue the cell spreading rate, is unable to localize to the plasma membrane leading edge, and perturbs srGAP2 homodimer formation mediated by the F-BAR domain. These results suggest that srGAP2 arginine methylation plays important roles in cell spreading and cell migration through influencing membrane protrusion."xsd:string |
| http://purl.uniprot.org/citations/20810653 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m110.153429"xsd:string |
| http://purl.uniprot.org/citations/20810653 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m110.153429"xsd:string |
| http://purl.uniprot.org/citations/20810653 | http://purl.uniprot.org/core/author | "Guo S."xsd:string |
| http://purl.uniprot.org/citations/20810653 | http://purl.uniprot.org/core/author | "Guo S."xsd:string |
| http://purl.uniprot.org/citations/20810653 | http://purl.uniprot.org/core/author | "Bao S."xsd:string |
| http://purl.uniprot.org/citations/20810653 | http://purl.uniprot.org/core/author | "Bao S."xsd:string |
| http://purl.uniprot.org/citations/20810653 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
| http://purl.uniprot.org/citations/20810653 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
| http://purl.uniprot.org/citations/20810653 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/20810653 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/20810653 | http://purl.uniprot.org/core/pages | "35133-35141"xsd:string |
| http://purl.uniprot.org/citations/20810653 | http://purl.uniprot.org/core/pages | "35133-35141"xsd:string |
| http://purl.uniprot.org/citations/20810653 | http://purl.uniprot.org/core/title | "srGAP2 arginine methylation regulates cell migration and cell spreading through promoting dimerization."xsd:string |
| http://purl.uniprot.org/citations/20810653 | http://purl.uniprot.org/core/title | "srGAP2 arginine methylation regulates cell migration and cell spreading through promoting dimerization."xsd:string |
| http://purl.uniprot.org/citations/20810653 | http://purl.uniprot.org/core/volume | "285"xsd:string |
| http://purl.uniprot.org/citations/20810653 | http://purl.uniprot.org/core/volume | "285"xsd:string |
| http://purl.uniprot.org/citations/20810653 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/20810653 |
| http://purl.uniprot.org/citations/20810653 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/20810653 |
| http://purl.uniprot.org/citations/20810653 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/20810653 |
| http://purl.uniprot.org/citations/20810653 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/20810653 |
| http://purl.uniprot.org/uniprot/O75044 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/20810653 |
| http://purl.uniprot.org/uniprot/O14744 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/20810653 |