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| Domain hiding | Altered binding specificity | Motif hiding | Composite binding site formation |
| Uncategorised | Rheostatic | Allostery | Avidity-sensing |
| Physicochemical compatibility | Pre-translational | Competition |
| Protein | Start | End | Switch Type | Switch Subtype | Switch Description | Information |
TRG_NLS_MonoExtC_3 - Monopartite variant of the classical basically charged NLS. C-extended version. | |||||||
| PHO4_YEAST | 156 | 161 | Binary | Physicochemical compatibility | Phosphorylation of S152 adjacent to the NLS of Phosphate system positive regulatory protein PHO4 (PHO4) by the Pho80-Pho85 CDK-Cyclin complex inhibits nuclear import this protein by blocking its interaction with Importin subunit beta-3 (PSE1). Upon phosphate starvation, Pho81 inhibits the Pho80-Pho85 complex, leading to translocation of Phosphate system positive regulatory protein PHO4 (PHO4) to the nucleus, where it regulates expression of phosphate-responsive genes. | ||
| MDM2_HUMAN | 181 | 187 | Binary | Pre‑translational | Alternative splicing removes the nuclear localisation signal (NLS) of E3 ubiquitin-protein ligase Mdm2 (MDM2), abrogating binding to Importin subunit alpha-1 (KPNA1). The exclusion from the nucleus is not complete however, as another NLS (466-473) is speculated to target splice variants to the nucleus, however, to the annotator it seems more likely that splice variants can dimerise with full-length MDM2 and be simultaneously transported into nucleus. | ||