http://purl.uniprot.org/citations/9860131 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/9860131 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/9860131 | http://www.w3.org/2000/01/rdf-schema#comment | "Mint 1 and 2 are proteins that bind to munc18-1, an essential component of the synaptic vesicle fusion machinery, and are detectably expressed only in neurons [Okamoto and Südhof, J. Biol. Chem. 272, 31459-31464 (1997)]. Mint 1 and 2 are composed of a variable N-terminal region that includes a conserved munc18-1-binding site, and a constant C-terminal region that contains one PTB and two PDZ domains. We have now identified a third mint isoform, mint 3. Similar to mint 1 and 2, the C-terminal half of mint 3 is composed of one PTB domain and two PDZ domains. However, in contrast to mint 1 and 2, mint 3 lacks an N-terminal munc18-binding domain and does not interact with munc18-1 in yeast two-hybrid assays. Mint 3 is ubiquitously expressed in all tissues, with lowest levels in brain and testis whereas mint 1 and 2 appear to be brain-specific. Our data suggest that mints form a diverse family of proteins with specialized neuronal and ubiquitous isoforms."xsd:string |
http://purl.uniprot.org/citations/9860131 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0171-9335(98)80103-9"xsd:string |
http://purl.uniprot.org/citations/9860131 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0171-9335(98)80103-9"xsd:string |
http://purl.uniprot.org/citations/9860131 | http://purl.uniprot.org/core/author | "Okamoto M."xsd:string |
http://purl.uniprot.org/citations/9860131 | http://purl.uniprot.org/core/author | "Okamoto M."xsd:string |
http://purl.uniprot.org/citations/9860131 | http://purl.uniprot.org/core/author | "Suedhof T.C."xsd:string |
http://purl.uniprot.org/citations/9860131 | http://purl.uniprot.org/core/author | "Suedhof T.C."xsd:string |
http://purl.uniprot.org/citations/9860131 | http://purl.uniprot.org/core/date | "1998"xsd:gYear |
http://purl.uniprot.org/citations/9860131 | http://purl.uniprot.org/core/date | "1998"xsd:gYear |
http://purl.uniprot.org/citations/9860131 | http://purl.uniprot.org/core/name | "Eur. J. Cell Biol."xsd:string |
http://purl.uniprot.org/citations/9860131 | http://purl.uniprot.org/core/name | "Eur. J. Cell Biol."xsd:string |
http://purl.uniprot.org/citations/9860131 | http://purl.uniprot.org/core/pages | "161-165"xsd:string |
http://purl.uniprot.org/citations/9860131 | http://purl.uniprot.org/core/pages | "161-165"xsd:string |
http://purl.uniprot.org/citations/9860131 | http://purl.uniprot.org/core/title | "Mint 3: a ubiquitous mint isoform that does not bind to munc18-1 or -2."xsd:string |
http://purl.uniprot.org/citations/9860131 | http://purl.uniprot.org/core/title | "Mint 3: a ubiquitous mint isoform that does not bind to munc18-1 or -2."xsd:string |
http://purl.uniprot.org/citations/9860131 | http://purl.uniprot.org/core/volume | "77"xsd:string |
http://purl.uniprot.org/citations/9860131 | http://purl.uniprot.org/core/volume | "77"xsd:string |
http://purl.uniprot.org/citations/9860131 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/9860131 |
http://purl.uniprot.org/citations/9860131 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/9860131 |
http://purl.uniprot.org/citations/9860131 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/9860131 |
http://purl.uniprot.org/citations/9860131 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/9860131 |
http://purl.uniprot.org/uniprot/O70248 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/9860131 |
http://purl.uniprot.org/embl-cds/AAC17978.1 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/9860131 |