Domain hiding |   Altered binding specificity |   Motif hiding |   Composite binding site formation |
  Uncategorised |   Rheostatic |   Allostery |   Avidity-sensing |
  Physicochemical compatibility |   Pre-translational |   Competition |
Importin subunit alpha (Saccharomyces) | Large T antigen (Simian) | Regulatory protein SWI6 (Saccharomyces) |
Motif | Start | End | Switch Type | Switch Subtype | Switch Description | Information |
Importin subunit alpha - SRP1 -  Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | |||||||
TRG_NLS_Bipartite_1 | 44 | 58 | Specificity | Domain hiding | An intramolecular interaction between the importin beta-binding (IBB) domain and the NLS-binding pocket of Importin subunit alpha (SRP1) prevents binding of NLS cargo (e.g. Large T antigen) in the absence of Importin subunit beta-1 (KAP95) by hiding of the NLS-binding pocket. Binding of the IBB of Importin subunit alpha (SRP1) to Importin subunit beta-1 (KAP95) relieves this auto-inhibitory interaction and increases the affinity of Importin subunit alpha (SRP1) for NLS cargo. | ||
Large T antigen - -  Simian virus 40 | |||||||
TRG_NLS_MonoExtN_4 | 126 | 132 | Specificity | Domain hiding | An intramolecular interaction between the importin beta-binding (IBB) domain and the NLS-binding pocket of Importin subunit alpha (SRP1) prevents binding of NLS cargo (e.g. Large T antigen) in the absence of Importin subunit beta-1 (KAP95) by hiding of the NLS-binding pocket. Binding of the IBB of Importin subunit alpha (SRP1) to Importin subunit beta-1 (KAP95) relieves this auto-inhibitory interaction and increases the affinity of Importin subunit alpha (SRP1) for NLS cargo. | ||
Regulatory protein SWI6 - SWI6 -  Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | |||||||
TRG_NLS_MonoExtN_4 | 161 | 167 | Binary | Physicochemical compatibility | Phosphorylation of S160 adjacent to the NLS of Regulatory protein SWI6 (SWI6) decreases nuclear import of this protein by decreasing the affinity for Importin subunit alpha (SRP1). |