|   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: Binary Subtype: Physicochemical compatibility | |||||||
| PTM of a residue in a motif or in its flanking regions alters the physicochemical and/or structural compatibility of the motif with its binding partner. This can either induce or enhance an interaction, or result in inhibition or even abrogation of an interaction. | |||||||
| INAR1_HUMAN | LIG_SH2_IE | 458 | 474 | Phosphorylation of Y466 in the SH2-binding motif of Interferon alpha/beta receptor 1 (IFNAR1) induces binding to the Non-receptor tyrosine-protein kinase TYK2 (TYK2) protein. | |||
| INAR1_HUMAN | LIG_SH2_IE | 473 | 489 | Phosphorylation of Y481 in the SH2-binding motif of Interferon alpha/beta receptor 1 (IFNAR1) induces binding to the Non-receptor tyrosine-protein kinase TYK2 (TYK2) protein. | |||