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.
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ERBB2_HUMAN | LIG_SH2_IC | 1135 | 1144 | Phosphorylation of Y1139 in the SH2-binding motif of Receptor tyrosine-protein kinase erbB-2 (ERBB2) induces binding to the Growth factor receptor-bound protein 7 (GRB7) protein. | details |
ERBB2_HUMAN | LIG_SH2_IE | 1015 | 1031 | Phosphorylation of Y1023 in the SH2-binding motif of Receptor tyrosine-protein kinase erbB-2 (ERBB2) induces binding to the Tyrosine-protein kinase JAK1 (JAK1) protein. | details |
ERBB2_HUMAN | LIG_SH2_IE | 1015 | 1031 | Phosphorylation of Y1023 in the SH2-binding motif of Receptor tyrosine-protein kinase erbB-2 (ERBB2) induces binding to the Tyrosine-protein kinase JAK2 (JAK2) protein. | details |
ERBB2_HUMAN | LIG_SH2_ID | 1131 | 1147 | Phosphorylation of Y1139 in the SH2-binding motif of Receptor tyrosine-protein kinase erbB-2 (ERBB2) induces binding to the Breast cancer anti-estrogen resistance protein 3 (BCAR3) protein. | details |
ERBB2_HUMAN | LIG_SH2_ID | 1015 | 1031 | Phosphorylation of Y1023 in the SH2-binding motif of Receptor tyrosine-protein kinase erbB-2 (ERBB2) induces binding to the SH2 domain-containing protein 3A (SH2D3A) protein. | details |
ERBB2_HUMAN | LIG_SH2_III | 1131 | 1147 | Phosphorylation of Y1139 in the SH2-binding motif of Receptor tyrosine-protein kinase erbB-2 (ERBB2) induces binding to the Signal transducer and activator of transcription 6 (STAT6) protein. | details |