Domain hiding |   Altered binding specificity |   Motif hiding |   Composite binding site formation |
  Uncategorised |   Rheostatic |   Allostery |   Avidity-sensing |
  Physicochemical compatibility |   Pre-translational |   Competition |
Motif | Start | End | Switch Type | Switch Subtype | Switch Description | Information |
Disintegrin and metalloproteinase domain-containing protein 15 - ADAM15 -  Homo sapiens | |||||||
LIG_SH3_2 | 767 | 772 | Binary | Pre‑translational | Alternative splicing removes the SH3-binding motif of Disintegrin and metalloproteinase domain-containing protein 15 (ADAM15), abrogating binding to Proto-oncogene tyrosine-protein kinase Src (SRC). The overexpression of this splice variant has been linked to clinical aggressiveness of breast cancer. | ||
Guanine nucleotide-binding protein subunit beta-2-like 1 - Gnb2l1 -  Rattus norvegicus | |||||||
LIG_SH2_IA | 241 | 250 | Binary | Physicochemical compatibility | Phosphorylation of Y246 in the SH2-binding motif of Guanine nucleotide-binding protein subunit beta-2-like 1 (Gnb2l1) induces binding to the Proto-oncogene tyrosine-protein kinase Src (SRC) protein. | ||
Neural cell adhesion molecule L1 - L1CAM -  Homo sapiens | |||||||
TRG_ENDOCYTIC_2 | 1176 | 1179 | Binary | Physicochemical compatibility | Phosphorylation of Y1176 by Proto-oncogene tyrosine-protein kinase Src (SRC) in the endocytosis motif of Neural cell adhesion molecule L1 (L1CAM) inhibits binding to AP-2 complex subunit mu (AP2M1). | ||
TRG_ENDOCYTIC_2 | 1176 | 1179 | Binary | Physicochemical compatibility | Phosphorylation of Y1176 in the endocytotic motif of Neural cell adhesion molecule L1 (L1CAM) by Proto-oncogene tyrosine-protein kinase Src (SRC) abolishes binding to the AP-2 complex subunit mu (AP2M1) and thereby inhibits internalisation of Neural cell adhesion molecule L1 (L1CAM). | ||
Proto-oncogene tyrosine-protein kinase Src - SRC -  Homo sapiens | |||||||
LIG_SH2_SRC | 530 | 533 | Binary | Physicochemical compatibility | Phosphorylation of Y530 in the SH2-binding motif of Proto-oncogene tyrosine-protein kinase Src (SRC) induces an intramolecular interaction with the SH2 domain of Proto-oncogene tyrosine-protein kinase Src (SRC) resulting in inhibition of its activity and preventing intermolecular interactions of its SH2 domain. |