http://purl.uniprot.org/citations/9182529 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/9182529 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/9182529 | http://www.w3.org/2000/01/rdf-schema#comment | "Src homology 3 (SH3) domains are conserved modules which participate in protein interaction by recognizing proline-rich motifs on target molecules. To identify new SH3-containing proteins, we performed a two-hybrid screen with a proline-rich region of human SOS-1. One of the specific SOS-1 interacting clones that were isolated from a mouse brain cDNA library defines a new protein that was named amphiphysin 2 because of its homology to the previously reported amphiphysin. Amphiphysin 2 is expressed in a number of mouse tissues through multiple RNA transcripts. Here, we report the amino acid sequence of a brain form of amphiphysin 2 (BRAMP2) encoded by a 2. 5-kilobase mRNA. BRAMP2 associates in vitro with elements of the endocytosis machinery such as alpha-adaptin and dynamin. On a biosensor surface, the BRAMP2/dynamin interaction appeared to be direct and partly dependent on a proline-rich sequence of dynamin. Association with dynamin was also observed in PC12 cells after cell stimulation with nerve growth factor, suggesting that amphiphysin 2 may be connected to receptor-dependent signaling pathways. This hypothesis is strengthened by the ability of BRAMP2 to interact with the p21(ras) exchange factor SOS, in vitro, as a possible point of interconnection between the endocytic and signaling pathways."xsd:string |
http://purl.uniprot.org/citations/9182529 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.272.24.15101"xsd:string |
http://purl.uniprot.org/citations/9182529 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.272.24.15101"xsd:string |
http://purl.uniprot.org/citations/9182529 | http://purl.uniprot.org/core/author | "Camonis J.H."xsd:string |
http://purl.uniprot.org/citations/9182529 | http://purl.uniprot.org/core/author | "Camonis J.H."xsd:string |
http://purl.uniprot.org/citations/9182529 | http://purl.uniprot.org/core/author | "Cussac D."xsd:string |
http://purl.uniprot.org/citations/9182529 | http://purl.uniprot.org/core/author | "Cussac D."xsd:string |
http://purl.uniprot.org/citations/9182529 | http://purl.uniprot.org/core/author | "Berger R."xsd:string |
http://purl.uniprot.org/citations/9182529 | http://purl.uniprot.org/core/author | "Berger R."xsd:string |
http://purl.uniprot.org/citations/9182529 | http://purl.uniprot.org/core/author | "Leprince C."xsd:string |
http://purl.uniprot.org/citations/9182529 | http://purl.uniprot.org/core/author | "Leprince C."xsd:string |
http://purl.uniprot.org/citations/9182529 | http://purl.uniprot.org/core/author | "Romero F."xsd:string |
http://purl.uniprot.org/citations/9182529 | http://purl.uniprot.org/core/author | "Romero F."xsd:string |
http://purl.uniprot.org/citations/9182529 | http://purl.uniprot.org/core/author | "Tavitian A."xsd:string |
http://purl.uniprot.org/citations/9182529 | http://purl.uniprot.org/core/author | "Tavitian A."xsd:string |
http://purl.uniprot.org/citations/9182529 | http://purl.uniprot.org/core/author | "Vayssiere B."xsd:string |
http://purl.uniprot.org/citations/9182529 | http://purl.uniprot.org/core/author | "Vayssiere B."xsd:string |
http://purl.uniprot.org/citations/9182529 | http://purl.uniprot.org/core/date | "1997"xsd:gYear |
http://purl.uniprot.org/citations/9182529 | http://purl.uniprot.org/core/date | "1997"xsd:gYear |
http://purl.uniprot.org/citations/9182529 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
http://purl.uniprot.org/citations/9182529 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
http://purl.uniprot.org/citations/9182529 | http://purl.uniprot.org/core/pages | "15101-15105"xsd:string |
http://purl.uniprot.org/citations/9182529 | http://purl.uniprot.org/core/pages | "15101-15105"xsd:string |