Domain hiding |   Altered binding specificity |   Motif hiding |   Composite binding site formation |
  Uncategorised |   Rheostatic |   Allostery |   Avidity-sensing |
  Physicochemical compatibility |   Pre-translational |   Competition |
Type: Binary Subtype: Physicochemical compatibility | Type: Binary Subtype: Pre‑translational |
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. | |||||||
DAB1_HUMAN | LIG_SH2_IB | 211 | 230 | Phosphorylation of Y220 in the SH2-binding motif of Disabled homolog 1 (DAB1) induces binding to the Adapter molecule crk (CRK) protein. | |||
CBL_HUMAN | LIG_SH2_IB | 770 | 780 | Phosphorylation of Y774 in the SH2-binding motif of E3 ubiquitin-protein ligase CBL (CBL) induces binding to the Adapter molecule crk (CRK) protein. | |||
BCAR1_HUMAN | LIG_SH2_IB | 358 | 368 | Phosphorylation of Y362 in the SH2-binding motif of Breast cancer anti-estrogen resistance protein 1 (BCAR1) induces binding to the Adapter molecule crk (CRK) protein. | |||
EPHB2_MOUSE | LIG_SH2_IB | 601 | 610 | Phosphorylation of Y604 in the SH2-binding motif of Ephrin type-B receptor 2 (Ephb2) induces binding to the Adapter molecule crk (CRK) protein. | |||
EPHB2_MOUSE | LIG_SH2_IB | 606 | 620 | Phosphorylation of Y610 in the SH2-binding motif of Ephrin type-B receptor 2 (Ephb2) induces binding to the Adapter molecule crk (CRK) protein. | |||
EGFR_HUMAN | LIG_SH2_SRC | 1125 | 1128 | Phosphorylation of Y1125 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to Adapter molecule crk (CRK). | |||
Type: Binary Subtype: Pre‑translational | |||||||
Pre-translational mechanisms such as alternative splicing, alternative promoter-usage and/or RNA editing result in inclusion or removal of exons that contain an entire or partial motif. | |||||||
PAXI_HUMAN | LIG_SH2_IB | 118 | 121 | Alternative splicing removes the SH2-binding motif of Paxillin (PXN), abrogating binding to Adapter molecule crk (CRK). | |||
PAXI_HUMAN | LIG_SH2_IB | 31 | 34 | Alternative splicing removes the SH2-binding motif of Paxillin (PXN), abrogating binding to Adapter molecule crk (CRK). |