Domain hiding |   Altered binding specificity |   Motif hiding |   Composite binding site formation |
  Uncategorised |   Rheostatic |   Allostery |   Avidity-sensing |
  Physicochemical compatibility |   Pre-translational |   Competition |
Type: Binary Subtype: Allostery | Type: Binary Subtype: Physicochemical compatibility | Type: Cumulative Subtype: Rheostatic |
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. | |||||||
EGFR_HUMAN | LIG_TKB | 1069 | 1074 | Phosphorylation of Y1069 in Epidermal growth factor receptor (EGFR) is necessary for binding to the TKB domain of E3 ubiquitin-protein ligase CBL (CBL). | |||
EGFR_HUMAN | LIG_PTB_Phospho_1 | 1104 | 1110 | Phosphorylation of Y1110 in the PTB-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the Docking protein 1 (DOK1) protein. | |||
EGFR_HUMAN | LIG_SH2_IC | 1092 | 1100 | Phosphorylation of Y1092 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the Growth factor receptor-bound protein 2 (GRB2) protein. | |||
EGFR_HUMAN | LIG_SH2_IE | 1011 | 1020 | Phosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the Ras and Rab interactor 1 (RIN1) protein. | |||
EGFR_HUMAN | LIG_SH2_IE | 1191 | 1200 | Phosphorylation of Y1197 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the Ras and Rab interactor 1 (RIN1) protein. | |||
EGFR_HUMAN | LIG_SH2_IE | 1008 | 1024 | Phosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the Tyrosine-protein kinase JAK1 (JAK1) protein. | |||
EGFR_HUMAN | LIG_SH2_IE | 1008 | 1024 | Phosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the Tyrosine-protein kinase JAK2 (JAK2) protein. | |||
EGFR_HUMAN | LIG_SH2_ID | 1008 | 1024 | Phosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the SH2 domain-containing protein 3C (SH2D3C) protein. | |||
EGFR_HUMAN | LIG_SH2_ID | 1008 | 1024 | Phosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the SH2 domain-containing protein 3A (SH2D3A) protein. | |||
EGFR_HUMAN | LIG_SH2_III | 1008 | 1024 | Phosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the Signal transducer and activator of transcription 6 (STAT6) protein. | |||
EGFR_HUMAN | LIG_SH2_SRC | 1016 | 1019 | Phosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-1 (PLCG1). | |||
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). | |||
EGFR_HUMAN | LIG_SH2_SRC | 1016 | 1019 | Phosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to Cytoplasmic protein NCK1 (NCK1). | |||
Type: Cumulative Subtype: Rheostatic | |||||||
Rheostatic switches gradually alter the affinity of a motif for a single binding partner by addition of multiple PTMs that additively contribute to this modulation. Additional modifications can either strengthen or weaken an interaction. | |||||||
EGFR_HUMAN | LIG_TKB | 1069 | 1074 | While phosphorylation of Y1069 induces binding, additional phosphorylation of S1070 and S1071 in the TKB-binding motif of Epidermal growth factor receptor (EGFR) gradually lowers its binding affinity for E3 ubiquitin-protein ligase CBL (CBL). | |||
Type: Binary Subtype: Allostery | |||||||
The binding properties of a motif or a motif-binding domain are modulated indirectly by allosteric effects resulting from PTM or effector binding at a site that is distinct from the actual interaction interface. | |||||||
EGFR_HUMAN | TRG_ENDOCYTIC_2 | 998 | 1001 | Binding of 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate to the AP-2 complex alpha, beta and mu subunits exposes a binding site on the AP-2 complex subunit mu (AP2M1) subunit for recruitment of Epidermal growth factor receptor (EGFR) via an endocytosis motif. |