|  Domain hiding
|  Altered binding specificity
|  Motif hiding
|  Composite binding site formation
|  Physicochemical compatibility
|Type: Binary Subtype: Physicochemical compatibility
|Type: Specificity Subtype: Altered binding specificity
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.
|Phosphorylation of T743 adjacent to the PTB-binding motif of Amyloid beta A4 protein (APP) reduces the affinity for Amyloid beta A4 precursor protein-binding family B member 1 (APBB1).
Type: Specificity Subtype: Altered binding specificity
|The balance of the competition for overlapping or adjacent, mutually exclusive interaction interfaces is tipped in favor of one of the interactors by PTM-dependent modulation of the intrinsic affinity of a binding region. Multiple, successive PTMs allow sequential switching of different binding partners in an ordered manner by step-wise alteration of binding specificity.
|Phosphorylation of Y757 in APP (Amyloid beta A4 protein (APP)) switches its specificity from PTB domain containing proteins, like Amyloid beta A4 precursor protein-binding family B member 1 (APBB1), which is involved in trafficking and processing of APP, to SH2 domain containing proteins, such as Growth factor receptor-bound protein 2 (GRB2).