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 |
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_IB - | |||||||
PAXI_HUMAN | 118 | 121 | Binary | Pre‑translational | Alternative splicing removes the SH2-binding motif of Paxillin (PXN), abrogating binding to Ras GTPase-activating protein 1 (RASA1). | ||
PAXI_HUMAN | 118 | 121 | Binary | Pre‑translational | Alternative splicing removes the SH2-binding motif of Paxillin (PXN), abrogating binding to Adapter molecule crk (CRK). | ||
PAXI_HUMAN | 31 | 34 | Binary | Pre‑translational | Alternative splicing removes the SH2-binding motif of Paxillin (PXN), abrogating binding to Adapter molecule crk (CRK). | ||
PAXI_HUMAN | 118 | 121 | Binary | Pre‑translational | Alternative splicing removes the SH2-binding motif of Paxillin (PXN), abrogating binding to Ras GTPase-activating protein 1 (RASA1). |