| http://purl.uniprot.org/citations/24108357 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/24108357 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/24108357 | http://www.w3.org/2000/01/rdf-schema#comment | "The AMP-activated protein kinase (AMPK) is a major stress sensor of mammalian cells. AMPK's homolog in the yeast Saccharomyces cerevisiae, the SNF1 protein kinase, is a central regulator of carbon metabolism that inhibits the Snf3/Rgt2-Rgt1 glucose sensing pathway and activates genes involved in respiration. We present evidence that glucose induces modification of the Snf1 catalytic subunt of SNF1 with the small ubiquitin-like modifier protein SUMO, catalyzed by the SUMO (E3) ligase Mms21. Our results suggest that SUMOylation of Snf1 inhibits its function in two ways: by interaction of SUMO attached to lysine 549 with a SUMO-interacting sequence motif located near the active site of Snf1, and by targeting Snf1 for destruction via the Slx5-Slx8 (SUMO-directed) ubiquitin ligase. These findings reveal another way SNF1 function is regulated in response to carbon source."xsd:string |
| http://purl.uniprot.org/citations/24108357 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.1304839110"xsd:string |
| http://purl.uniprot.org/citations/24108357 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.1304839110"xsd:string |
| http://purl.uniprot.org/citations/24108357 | http://purl.uniprot.org/core/author | "Johnston M."xsd:string |
| http://purl.uniprot.org/citations/24108357 | http://purl.uniprot.org/core/author | "Johnston M."xsd:string |
| http://purl.uniprot.org/citations/24108357 | http://purl.uniprot.org/core/author | "Simpson-Lavy K.J."xsd:string |
| http://purl.uniprot.org/citations/24108357 | http://purl.uniprot.org/core/author | "Simpson-Lavy K.J."xsd:string |
| http://purl.uniprot.org/citations/24108357 | http://purl.uniprot.org/core/date | "2013"xsd:gYear |
| http://purl.uniprot.org/citations/24108357 | http://purl.uniprot.org/core/date | "2013"xsd:gYear |
| http://purl.uniprot.org/citations/24108357 | http://purl.uniprot.org/core/name | "Proc. Natl. Acad. Sci. U.S.A."xsd:string |
| http://purl.uniprot.org/citations/24108357 | http://purl.uniprot.org/core/name | "Proc. Natl. Acad. Sci. U.S.A."xsd:string |
| http://purl.uniprot.org/citations/24108357 | http://purl.uniprot.org/core/pages | "17432-17437"xsd:string |
| http://purl.uniprot.org/citations/24108357 | http://purl.uniprot.org/core/pages | "17432-17437"xsd:string |
| http://purl.uniprot.org/citations/24108357 | http://purl.uniprot.org/core/title | "Sumoylation regulates the SNF1 protein kinase."xsd:string |
| http://purl.uniprot.org/citations/24108357 | http://purl.uniprot.org/core/title | "Sumoylation regulates the SNF1 protein kinase."xsd:string |
| http://purl.uniprot.org/citations/24108357 | http://purl.uniprot.org/core/volume | "110"xsd:string |
| http://purl.uniprot.org/citations/24108357 | http://purl.uniprot.org/core/volume | "110"xsd:string |
| http://purl.uniprot.org/citations/24108357 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/24108357 |
| http://purl.uniprot.org/citations/24108357 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/24108357 |
| http://purl.uniprot.org/citations/24108357 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/24108357 |
| http://purl.uniprot.org/citations/24108357 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/24108357 |
| http://purl.uniprot.org/uniprot/P06782 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/24108357 |
| http://purl.uniprot.org/uniprot/P38632#attribution-C12E82DB36DD28CE30B1A7C33B372457 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/24108357 |