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. | |||||||
BTK_MOUSE | DOC_WW_Pin1_4 | 112 | 117 | Phosphorylation of S115 in the Pin1-binding motif of Tyrosine-protein kinase BTK (Btk) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein. | |||
BTK_MOUSE | DOC_WW_Pin1_4 | 18 | 23 | Phosphorylation of S21 in the Pin1-binding motif of Tyrosine-protein kinase BTK (Btk) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein. |