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 |
DOC_WW_Pin1_4 - The Class IV WW domain interaction motif is recognised primarily by the Pin1 phosphorylation-dependent prolyl isomerase. | |||||||
FAK1_HUMAN | 907 | 912 | Binary | Physicochemical compatibility | Phosphorylation of S910 in the Pin1-binding motif of Focal adhesion kinase 1 (PTK2) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein. | ||
LIG_FAT_LD_1 - The paxillin LD motif is recognized by FAK and other focal adhesion proteins mainly involved in cytoskeletal regulation | |||||||
PAXI_HUMAN | 4 | 12 | Binary | Pre‑translational | Alternative splicing removes the FAK-binding LD motif of Paxillin (PXN), abrogating binding to Focal adhesion kinase 1 (PTK2). | ||
LIG_SH2_IA - | |||||||
FAK1_HUMAN | 389 | 405 | Binary | Physicochemical compatibility | Phosphorylation of Y397 in the SH2-binding motif of Focal adhesion kinase 1 (PTK2) induces binding to the Cytoplasmic protein NCK2 (NCK2) protein. | ||
LIG_SH2_SRC - Src-family Src Homology 2 (SH2) domains binding motif. | |||||||
FAK1_HUMAN | 397 | 400 | Binary | Physicochemical compatibility | Phosphorylation of Y397 in the SH2-binding motif of Focal adhesion kinase 1 (PTK2) induces binding to Neuronal proto-oncogene tyrosine-protein kinase Src (Src). |