| http://purl.uniprot.org/citations/22889169 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/22889169 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/22889169 | http://www.w3.org/2000/01/rdf-schema#comment | "Vps74p, a member of the GOLPH3 protein family, binds directly to coatomer and the cytoplasmic tails of a subset of Golgi-resident glycosyltransferases to mediate their Golgi retention. We identify a cluster of arginine residues at the N-terminal end of GOLPH3 proteins that are necessary and sufficient to mediate coatomer binding. While loss of coatomer binding renders Vps74p non-functional for glycosyltransferase retention, the Golgi membrane-binding capabilities of the mutant protein are not significantly reduced. We establish that the oligomerization status and phosphatidylinositol-4-phosphate-binding properties of Vps74p largely account for the membrane-binding capacity of the protein and identify an Arf1p-Vps74p interaction as a potential contributing factor in Vps74p Golgi membrane association."xsd:string |
| http://purl.uniprot.org/citations/22889169 | http://purl.org/dc/terms/identifier | "doi:10.1111/j.1600-0854.2012.01403.x"xsd:string |
| http://purl.uniprot.org/citations/22889169 | http://purl.org/dc/terms/identifier | "doi:10.1111/j.1600-0854.2012.01403.x"xsd:string |
| http://purl.uniprot.org/citations/22889169 | http://purl.uniprot.org/core/author | "Chen L."xsd:string |
| http://purl.uniprot.org/citations/22889169 | http://purl.uniprot.org/core/author | "Chen L."xsd:string |
| http://purl.uniprot.org/citations/22889169 | http://purl.uniprot.org/core/author | "Banfield D.K."xsd:string |
| http://purl.uniprot.org/citations/22889169 | http://purl.uniprot.org/core/author | "Banfield D.K."xsd:string |
| http://purl.uniprot.org/citations/22889169 | http://purl.uniprot.org/core/author | "Tu L."xsd:string |
| http://purl.uniprot.org/citations/22889169 | http://purl.uniprot.org/core/author | "Tu L."xsd:string |
| http://purl.uniprot.org/citations/22889169 | http://purl.uniprot.org/core/date | "2012"xsd:gYear |
| http://purl.uniprot.org/citations/22889169 | http://purl.uniprot.org/core/date | "2012"xsd:gYear |
| http://purl.uniprot.org/citations/22889169 | http://purl.uniprot.org/core/name | "Traffic"xsd:string |
| http://purl.uniprot.org/citations/22889169 | http://purl.uniprot.org/core/name | "Traffic"xsd:string |
| http://purl.uniprot.org/citations/22889169 | http://purl.uniprot.org/core/pages | "1496-1507"xsd:string |
| http://purl.uniprot.org/citations/22889169 | http://purl.uniprot.org/core/pages | "1496-1507"xsd:string |
| http://purl.uniprot.org/citations/22889169 | http://purl.uniprot.org/core/title | "A conserved N-terminal arginine-motif in GOLPH3-family proteins mediates binding to coatomer."xsd:string |
| http://purl.uniprot.org/citations/22889169 | http://purl.uniprot.org/core/title | "A conserved N-terminal arginine-motif in GOLPH3-family proteins mediates binding to coatomer."xsd:string |
| http://purl.uniprot.org/citations/22889169 | http://purl.uniprot.org/core/volume | "13"xsd:string |
| http://purl.uniprot.org/citations/22889169 | http://purl.uniprot.org/core/volume | "13"xsd:string |
| http://purl.uniprot.org/citations/22889169 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/22889169 |
| http://purl.uniprot.org/citations/22889169 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/22889169 |
| http://purl.uniprot.org/citations/22889169 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/22889169 |
| http://purl.uniprot.org/citations/22889169 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/22889169 |