Motif | Protein | Start | End | Switch Type | Switch Subtype | Switch description | Information | Evidence |
Endocytosis (KEGG - hsa04144) | ||||||||
LIG_WW_1 | ERBB4_HUMAN | 1053 | 1056 | Specificity | Altered binding specificity | Phosphorylation-dependent binding of Receptor tyrosine-protein kinase erbB-4 (ERBB4) to the SH2 domains of Phosphatidylinositol 3-kinase regulatory subunit alpha (PIK3R1) results in signaling activation, while binding to the WW domains of E3 ubiquitin-protein ligase Itchy homolog (ITCH) to unphopshorylated ERBB4 results in ubiquitylation, endocytosis and ultimately degradation of ERBB4. | Inferred | |
LIG_WW_1 | ERBB4_HUMAN | 1053 | 1056 | Binary | Pre‑translational | Alternative splicing removes the WW-binding motif of Receptor tyrosine-protein kinase erbB-4 (ERBB4), abrogating binding to E3 ubiquitin-protein ligase Itchy homolog (ITCH). The presence of a WW-binding motif mediates ERBB4 mono-ubiquitination and endocytosis by the WW domain-containing HECT-type E3 ubiquitin ligase ITCH. | Inferred | |
LIG_WW_1 | ERBB4_HUMAN | 1053 | 1056 | Binary | Pre‑translational | Alternative splicing removes the WW-binding motif of Receptor tyrosine-protein kinase erbB-4 (ERBB4), abrogating binding to E3 ubiquitin-protein ligase Itchy homolog (ITCH). The presence of a WW-binding motif mediates ERBB4 mono-ubiquitination and endocytosis by the WW domain-containing HECT-type E3 ubiquitin ligase ITCH. | Inferred | |
ErbB signaling pathway (KEGG - hsa04012) | ||||||||
LIG_WW_1 | ERBB4_HUMAN | 1053 | 1056 | Specificity | Altered binding specificity | Phosphorylation-dependent binding of Receptor tyrosine-protein kinase erbB-4 (ERBB4) to the SH2 domains of Phosphatidylinositol 3-kinase regulatory subunit alpha (PIK3R1) results in signaling activation, while binding to the WW domains of E3 ubiquitin-protein ligase Itchy homolog (ITCH) to unphopshorylated ERBB4 results in ubiquitylation, endocytosis and ultimately degradation of ERBB4. | Inferred |