| http://purl.uniprot.org/citations/10339567 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10339567 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10339567 | http://www.w3.org/2000/01/rdf-schema#comment | "Cas ligand with multiple Src homology (SH) 3 domains (CMS) is an ubiquitously expressed signal transduction molecule that interacts with the focal adhesion protein p130(Cas). CMS contains three SH3 in its NH2 terminus and proline-rich sequences in its center region. The latter sequences mediate the binding to the SH3 domains of p130(Cas), Src-family kinases, p85 subunit of phosphatidylinositol 3-kinase, and Grb2. The COOH-terminal region contains putative actin binding sites and a coiled-coil domain that mediates homodimerization of CMS. CMS is a cytoplasmic protein that colocalizes with F-actin and p130(Cas) to membrane ruffles and leading edges of cells. Ectopic expression of CMS in COS-7 cells resulted in alteration in arrangement of the actin cytoskeleton. We observed a diffuse distribution of actin in small dots and less actin fiber formation. Altogether, these features suggest that CMS functions as a scaffolding molecule with a specialized role in regulation of the actin cytoskeleton."xsd:string |
| http://purl.uniprot.org/citations/10339567 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.96.11.6211"xsd:string |
| http://purl.uniprot.org/citations/10339567 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.96.11.6211"xsd:string |
| http://purl.uniprot.org/citations/10339567 | http://purl.uniprot.org/core/author | "Hanafusa H."xsd:string |
| http://purl.uniprot.org/citations/10339567 | http://purl.uniprot.org/core/author | "Hanafusa H."xsd:string |
| http://purl.uniprot.org/citations/10339567 | http://purl.uniprot.org/core/author | "Ishimaru S."xsd:string |
| http://purl.uniprot.org/citations/10339567 | http://purl.uniprot.org/core/author | "Ishimaru S."xsd:string |
| http://purl.uniprot.org/citations/10339567 | http://purl.uniprot.org/core/author | "Georgescu M.M."xsd:string |
| http://purl.uniprot.org/citations/10339567 | http://purl.uniprot.org/core/author | "Georgescu M.M."xsd:string |
| http://purl.uniprot.org/citations/10339567 | http://purl.uniprot.org/core/author | "Kirsch K.H."xsd:string |
| http://purl.uniprot.org/citations/10339567 | http://purl.uniprot.org/core/author | "Kirsch K.H."xsd:string |
| http://purl.uniprot.org/citations/10339567 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
| http://purl.uniprot.org/citations/10339567 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
| http://purl.uniprot.org/citations/10339567 | http://purl.uniprot.org/core/name | "Proc. Natl. Acad. Sci. U.S.A."xsd:string |
| http://purl.uniprot.org/citations/10339567 | http://purl.uniprot.org/core/name | "Proc. Natl. Acad. Sci. U.S.A."xsd:string |
| http://purl.uniprot.org/citations/10339567 | http://purl.uniprot.org/core/pages | "6211-6216"xsd:string |
| http://purl.uniprot.org/citations/10339567 | http://purl.uniprot.org/core/pages | "6211-6216"xsd:string |
| http://purl.uniprot.org/citations/10339567 | http://purl.uniprot.org/core/title | "CMS: an adapter molecule involved in cytoskeletal rearrangements."xsd:string |
| http://purl.uniprot.org/citations/10339567 | http://purl.uniprot.org/core/title | "CMS: an adapter molecule involved in cytoskeletal rearrangements."xsd:string |
| http://purl.uniprot.org/citations/10339567 | http://purl.uniprot.org/core/volume | "96"xsd:string |
| http://purl.uniprot.org/citations/10339567 | http://purl.uniprot.org/core/volume | "96"xsd:string |
| http://purl.uniprot.org/citations/10339567 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/10339567 |
| http://purl.uniprot.org/citations/10339567 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/10339567 |