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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 |
LIG_PTB_Phospho_1 - This phosphorylation-dependent motif binds to Shc-like and IRS-like PTB domains. The pTyr is positioned within a highly basic-charged anchoring pocket. A hydrophobic residue -5 (compared to pY) increases the affinity of the interaction. | |||||||
| EGFR_HUMAN | 1104 | 1110 | Binary | Physicochemical compatibility | Phosphorylation of Y1110 in the PTB-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the Docking protein 1 (DOK1) protein. | ||
| ITB3_HUMAN | 767 | 773 | Binary | Physicochemical compatibility | Phosphorylation of Y773 in the PTB-binding motif of Integrin beta-3 (ITGB3) induces binding to the Docking protein 1 (DOK1) protein. | ||
| ITB3_HUMAN | 767 | 773 | Specificity | Altered binding specificity | Phosphorylation of Y773 in Integrin beta-3 (ITGB3) switches the specificity of ITGB3 from Talin-1 (TLN1) to Docking protein 1 (DOK1), with a 2-fold decrease of the affinity for TLN1 and close to a 400-fold increase of the affinity for DOK1. This switch results in negative regulation of integrin activation. | ||
LIG_SH2_IB - | |||||||
| DOK1_HUMAN | 447 | 454 | Binary | Physicochemical compatibility | Phosphorylation of Y449 in the SH2-binding motif of Docking protein 1 (DOK1) induces binding to the SH2 domain-containing protein 1A (SH2D1A) protein. | ||
LIG_SH2_IIB - | |||||||
| DOK1_HUMAN | 203 | 206 | Binary | Physicochemical compatibility | Phosphorylation of Y203 in the SH2-binding motif of Docking protein 1 (DOK1) induces binding to the Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 1 (INPP5D) protein. | ||