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. | |||||||
ZAP70_HUMAN | LIG_SH2_IIC | 284 | 300 | Phosphorylation of Y292 in the SH2-binding motif of Tyrosine-protein kinase ZAP-70 (ZAP70) induces binding to the E3 ubiquitin-protein ligase CBL-B (CBLB) protein. | |||
KSYK_HUMAN | LIG_SH2_IIC | 315 | 331 | Phosphorylation of Y323 in the SH2-binding motif of Tyrosine-protein kinase SYK (SYK) induces binding to the E3 ubiquitin-protein ligase CBL-B (CBLB) protein. |