| http://purl.uniprot.org/citations/10958799 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10958799 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10958799 | http://www.w3.org/2000/01/rdf-schema#comment | "PDZ domains play a pivotal role in the synaptic localization of ion channels, receptors, signaling enzymes, and cell adhesion molecules. These domains mediate protein-protein interactions via the recognition of a conserved sequence motif at the extreme C terminus of their target proteins. By means of a yeast two-hybrid screen using the C terminus of the G protein-coupled alpha-latrotoxin receptor CL1 as bait, three PDZ domain proteins of the Shank family were identified. These proteins belong to a single protein family characterized by a common domain organization. The PDZ domain is highly conserved among the family members, significantly different from other known PDZ domains, and specifically binds to the C terminus of CL1. Shank1 and CL1 are expressed primarily in brain, and both proteins co-enrich in the postsynaptic density. Furthermore, Shank1 induces a clustering of CL1 in transfected cells, strongly supporting an interaction of both proteins in vivo."xsd:string |
| http://purl.uniprot.org/citations/10958799 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m006448200"xsd:string |
| http://purl.uniprot.org/citations/10958799 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m006448200"xsd:string |
| http://purl.uniprot.org/citations/10958799 | http://purl.uniprot.org/core/author | "Suedhof T.C."xsd:string |
| http://purl.uniprot.org/citations/10958799 | http://purl.uniprot.org/core/author | "Suedhof T.C."xsd:string |
| http://purl.uniprot.org/citations/10958799 | http://purl.uniprot.org/core/author | "Stahl B."xsd:string |
| http://purl.uniprot.org/citations/10958799 | http://purl.uniprot.org/core/author | "Stahl B."xsd:string |
| http://purl.uniprot.org/citations/10958799 | http://purl.uniprot.org/core/author | "Tobaben S."xsd:string |
| http://purl.uniprot.org/citations/10958799 | http://purl.uniprot.org/core/author | "Tobaben S."xsd:string |
| http://purl.uniprot.org/citations/10958799 | http://purl.uniprot.org/core/date | "2000"xsd:gYear |
| http://purl.uniprot.org/citations/10958799 | http://purl.uniprot.org/core/date | "2000"xsd:gYear |
| http://purl.uniprot.org/citations/10958799 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/10958799 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/10958799 | http://purl.uniprot.org/core/pages | "36204-36210"xsd:string |
| http://purl.uniprot.org/citations/10958799 | http://purl.uniprot.org/core/pages | "36204-36210"xsd:string |
| http://purl.uniprot.org/citations/10958799 | http://purl.uniprot.org/core/title | "The G protein-coupled receptor CL1 interacts directly with proteins of the Shank family."xsd:string |
| http://purl.uniprot.org/citations/10958799 | http://purl.uniprot.org/core/title | "The G protein-coupled receptor CL1 interacts directly with proteins of the Shank family."xsd:string |
| http://purl.uniprot.org/citations/10958799 | http://purl.uniprot.org/core/volume | "275"xsd:string |
| http://purl.uniprot.org/citations/10958799 | http://purl.uniprot.org/core/volume | "275"xsd:string |
| http://purl.uniprot.org/citations/10958799 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/10958799 |
| http://purl.uniprot.org/citations/10958799 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/10958799 |
| http://purl.uniprot.org/citations/10958799 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/10958799 |
| http://purl.uniprot.org/citations/10958799 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/10958799 |