| http://purl.uniprot.org/citations/26524494 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/26524494 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/26524494 | http://www.w3.org/2000/01/rdf-schema#comment | "E3 protein ligases enhance transfer of ubiquitin-like (Ubl) proteins from E2 conjugating enzymes to substrates by stabilizing the thioester-charged E2~Ubl in a closed configuration optimally aligned for nucleophilic attack. Here, we report biochemical and structural data that define the N-terminal domain of the Homo sapiens ZNF451 as the catalytic module for SUMO E3 ligase activity. The ZNF451 catalytic module contains tandem SUMO-interaction motifs (SIMs) bridged by a Pro-Leu-Arg-Pro (PLRP) motif. The first SIM and PLRP motif engage thioester-charged E2~SUMO while the next SIM binds a second molecule of SUMO bound to the back side of E2. We show that ZNF451 is SUMO2 specific and that SUMO modification of ZNF451 may contribute to activity by providing a second molecule of SUMO that interacts with E2. Our results are consistent with ZNF451 functioning as a bona fide SUMO E3 ligase."xsd:string |
| http://purl.uniprot.org/citations/26524494 | http://purl.org/dc/terms/identifier | "doi:10.1038/nsmb.3116"xsd:string |
| http://purl.uniprot.org/citations/26524494 | http://purl.org/dc/terms/identifier | "doi:10.1038/nsmb.3116"xsd:string |
| http://purl.uniprot.org/citations/26524494 | http://purl.uniprot.org/core/author | "Lima C.D."xsd:string |
| http://purl.uniprot.org/citations/26524494 | http://purl.uniprot.org/core/author | "Lima C.D."xsd:string |
| http://purl.uniprot.org/citations/26524494 | http://purl.uniprot.org/core/author | "Cappadocia L."xsd:string |
| http://purl.uniprot.org/citations/26524494 | http://purl.uniprot.org/core/author | "Cappadocia L."xsd:string |
| http://purl.uniprot.org/citations/26524494 | http://purl.uniprot.org/core/author | "Pichler A."xsd:string |
| http://purl.uniprot.org/citations/26524494 | http://purl.uniprot.org/core/author | "Pichler A."xsd:string |
| http://purl.uniprot.org/citations/26524494 | http://purl.uniprot.org/core/date | "2015"xsd:gYear |
| http://purl.uniprot.org/citations/26524494 | http://purl.uniprot.org/core/date | "2015"xsd:gYear |
| http://purl.uniprot.org/citations/26524494 | http://purl.uniprot.org/core/name | "Nat. Struct. Mol. Biol."xsd:string |
| http://purl.uniprot.org/citations/26524494 | http://purl.uniprot.org/core/name | "Nat. Struct. Mol. Biol."xsd:string |
| http://purl.uniprot.org/citations/26524494 | http://purl.uniprot.org/core/pages | "968-975"xsd:string |
| http://purl.uniprot.org/citations/26524494 | http://purl.uniprot.org/core/pages | "968-975"xsd:string |
| http://purl.uniprot.org/citations/26524494 | http://purl.uniprot.org/core/title | "Structural basis for catalytic activation by the human ZNF451 SUMO E3 ligase."xsd:string |
| http://purl.uniprot.org/citations/26524494 | http://purl.uniprot.org/core/title | "Structural basis for catalytic activation by the human ZNF451 SUMO E3 ligase."xsd:string |
| http://purl.uniprot.org/citations/26524494 | http://purl.uniprot.org/core/volume | "22"xsd:string |
| http://purl.uniprot.org/citations/26524494 | http://purl.uniprot.org/core/volume | "22"xsd:string |
| http://purl.uniprot.org/citations/26524494 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/26524494 |
| http://purl.uniprot.org/citations/26524494 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/26524494 |
| http://purl.uniprot.org/citations/26524494 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/26524494 |
| http://purl.uniprot.org/citations/26524494 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/26524494 |