basic mechanisms of sumoylation
| PAG Title | basic mechanisms of sumoylation |
| PAG ID | WAG001469 |
| Type | P |
| Source Link |  BioCarta |
| Publication Reference | NA |
| PAG Description | Like ubiquitin, SUMO (small ubiquitin-related modifier) proteins are small protein tags that are conjugated to proteins to modify their function. The ubiquitin system tags proteins for degradation by the proteosome (see Proteosome pathway) but SUMO conjugation has a range of other functions, stabilizing some proteins and altering their subcellular localization. Sumoylation may also influence ubiquitition and protein stability indirectly. Three different SUMO proteins are conjugated to proteins, SUMO-1, SUMO-2 and SUMO-3. The SUMO-2 and SUMO-3 genes are closely related, with 86% sequence identity while SUMO-1 is less closely related with about 50% sequence identity with SUMO-2 and SUMO-3. These SUMO proteins also have distinct functions, with SUMO-1 conjugated to proteins as a monomer, while SUMO-2 and SUMO-3 are conjugated to proteins as higher molecular weight polymers with SUMO-1 termiting further SUMO addition. SUMO proteins are first activated by adenylation by one enzyme complex (SAE1/SAE2), then transferred to Ubc-9 and filly to the termil amino group of a lysine side chain in target proteins. The same conjugation system appears to work for all three SUMO proteins. |
| Species | Homo sapiens |
| Quality Metric Scores | nCoCo Score: 1,745 |
| Information Content | Rich |
| Other IDs | |
| Base PAG ID | WAG001469 |
| Human Phenotyte Annotation | |
| Curator | PAGER curation team |
| Curator Contact | PAGER-contact@googlegroups.com |
">
Something else? Please send us an email!