| http://purl.uniprot.org/citations/20682791 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/20682791 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/20682791 | http://www.w3.org/2000/01/rdf-schema#comment | "Ecm29 is a 200-kDa HEAT repeat protein that binds the 26 S proteasome. Genome-wide two-hybrid screens and mass spectrometry have identified molecular motors, endosomal components, and ubiquitin-proteasome factors as Ecm29-interacting proteins. The C-terminal half of human Ecm29 binds myosins and kinesins; its N-terminal region binds the endocytic proteins, Vps11, Rab11-FIP4, and rabaptin. Whereas full-length FLAG-Ecm29, its C-terminal half, and a small central fragment of Ecm29 remain bound to glycerol-gradient-separated 26 S proteasomes, the N-terminal half of Ecm29 does not. Confocal microscopy showed that Ecm-26 S proteasomes are present on flotillin-positive endosomes, but they are virtually absent from caveolin- and clathrin-decorated endosomes. Expression of the small central fragment of Ecm29 markedly reduces proteasome association with flotillin-positive endosomes. Identification of regions within Ecm29 capable of binding molecular motors, endosomal proteins, and the 26 S proteasome supports the hypothesis that Ecm29 serves as an adaptor for coupling 26 S proteasomes to specific cellular compartments."xsd:string |
| http://purl.uniprot.org/citations/20682791 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m110.154120"xsd:string |
| http://purl.uniprot.org/citations/20682791 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m110.154120"xsd:string |
| http://purl.uniprot.org/citations/20682791 | http://purl.uniprot.org/core/author | "Bell R."xsd:string |
| http://purl.uniprot.org/citations/20682791 | http://purl.uniprot.org/core/author | "Bell R."xsd:string |
| http://purl.uniprot.org/citations/20682791 | http://purl.uniprot.org/core/author | "Gorbea C."xsd:string |
| http://purl.uniprot.org/citations/20682791 | http://purl.uniprot.org/core/author | "Gorbea C."xsd:string |
| http://purl.uniprot.org/citations/20682791 | http://purl.uniprot.org/core/author | "Hughes R.E."xsd:string |
| http://purl.uniprot.org/citations/20682791 | http://purl.uniprot.org/core/author | "Hughes R.E."xsd:string |
| http://purl.uniprot.org/citations/20682791 | http://purl.uniprot.org/core/author | "Pratt G."xsd:string |
| http://purl.uniprot.org/citations/20682791 | http://purl.uniprot.org/core/author | "Pratt G."xsd:string |
| http://purl.uniprot.org/citations/20682791 | http://purl.uniprot.org/core/author | "Rechsteiner M."xsd:string |
| http://purl.uniprot.org/citations/20682791 | http://purl.uniprot.org/core/author | "Rechsteiner M."xsd:string |
| http://purl.uniprot.org/citations/20682791 | http://purl.uniprot.org/core/author | "Sahasrabudhe S."xsd:string |
| http://purl.uniprot.org/citations/20682791 | http://purl.uniprot.org/core/author | "Sahasrabudhe S."xsd:string |
| http://purl.uniprot.org/citations/20682791 | http://purl.uniprot.org/core/author | "Ustrell V."xsd:string |
| http://purl.uniprot.org/citations/20682791 | http://purl.uniprot.org/core/author | "Ustrell V."xsd:string |
| http://purl.uniprot.org/citations/20682791 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
| http://purl.uniprot.org/citations/20682791 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
| http://purl.uniprot.org/citations/20682791 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/20682791 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/20682791 | http://purl.uniprot.org/core/pages | "31616-31633"xsd:string |
| http://purl.uniprot.org/citations/20682791 | http://purl.uniprot.org/core/pages | "31616-31633"xsd:string |