Please send any suggestions/comments to: switches@elm.eu.org
| Domain hiding | Altered binding specificity | Motif hiding | Composite binding site formation |
| Uncategorised | Rheostatic | Allostery | Avidity-sensing |
| Physicochemical compatibility | Pre-translational | Competition |
| Protein | Motif | Start | End | Switch description | Information |
Type: Uncategorised Subtype: Uncategorised | |||||||
| Switches that have unique regulatory mechanisms. As more instances accumulate these switches may be worthy of a novel switch type | |||||||
| WASP_HUMAN | LIG_GBD_WASP_1 | 466 | 476 | Phosphorylation of Wiskott-Aldrich syndrome protein (WAS) at Y291 by Src kinases, e.g. , destabilises the auto-inhibitory intramolecular interaction of Wiskott-Aldrich syndrome protein (WAS). | |||
Type: Binary Subtype: Allostery | |||||||
| The binding properties of a motif or a motif-binding domain are modulated indirectly by allosteric effects resulting from PTM or effector binding at a site that is distinct from the actual interaction interface. | |||||||
| WASP_HUMAN | LIG_GBD_WASP_1 | 466 | 476 | Binding of Cell division control protein 42 homolog (CDC42) to Wiskott-Aldrich syndrome protein (WAS) allosterically relieves an auto-inhibitory intramolecular interaction in Wiskott-Aldrich syndrome protein (WAS), which becomes active. | |||
| WASP_HUMAN | LIG_GBD_WASP_1 | 466 | 476 | Binding of 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate to Wiskott-Aldrich syndrome protein (WAS) allosterically relieves an auto-inhibitory intramolecular interaction in Wiskott-Aldrich syndrome protein (WAS), which becomes active. | |||