Aldosterone-regulated sodium reabsorption (KEGG - hsa04960)
|
| LIG_SH2_STAT5 | INSR_HUMAN | 1361 | 1364 | Specificity | Domain hiding | PIP3 (1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate), a product of PI3-kinase, binds to the SH2 domains of PI3K (Phosphatidylinositol 3-kinase regulatory subunit alpha (PIK3R1)) and thereby blocks its interaction with tyrosine-phosphorylated SH2 motif containing proteins. | details | Inferred |
Endocytosis (KEGG - hsa04144)
|
| LIG_SH2_STAT5 | ERBB4_HUMAN | 1056 | 1059 | 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. | details | Inferred |
ErbB signaling pathway (KEGG - hsa04012)
|
| LIG_SH2_STAT5 | ERBB4_HUMAN | 1056 | 1059 | 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. | details | Inferred |
| LIG_SH2_IIA | ERBB4_HUMAN | 1056 | 1059 | Binary | Pre‑translational | Alternative splicing removes the SH2-binding motif of Receptor tyrosine-protein kinase erbB-4 (ERBB4), abrogating binding to Phosphatidylinositol 3-kinase regulatory subunit alpha (PIK3R1). The SH2-binding motif overlaps with a WW-binding motif. Binding of these motifs is regulated in a phosphorylation-dependent manner, ensuring ERBB4 is either endocytosed or stabilised. | details | Inferred |
| LIG_SH2_IIA | ERBB4_HUMAN | 1056 | 1059 | Binary | Pre‑translational | Alternative splicing removes the SH2-binding motif of Receptor tyrosine-protein kinase erbB-4 (ERBB4), abrogating binding to Phosphatidylinositol 3-kinase regulatory subunit alpha (PIK3R1). The SH2-binding motif overlaps with a WW-binding motif. Binding of these motifs is regulated in a phosphorylation-dependent manner, ensuring ERBB4 is either endocytosed or stabilised. | details | Inferred |
| LIG_SH2_STAT5 | GAB1_HUMAN | 472 | 475 | Binary | Physicochemical compatibility | Phosphorylation of Y472 in the SH2-binding motif of GRB2-associated-binding protein 1 (GAB1) induces binding to Phosphatidylinositol 3-kinase regulatory subunit alpha (PIK3R1). | details | Curated |
| LIG_SH2_STAT5 | GAB1_HUMAN | 447 | 450 | Binary | Physicochemical compatibility | Phosphorylation of Y447 in the SH2-binding motif of GRB2-associated-binding protein 1 (GAB1) induces binding to Phosphatidylinositol 3-kinase regulatory subunit alpha (PIK3R1). | details | Curated |
Focal adhesion (KEGG - hsa04510)
|
| LIG_SH2_IIA | PGFRB_HUMAN | 751 | 755 | Binary | Physicochemical compatibility | Phosphorylation of Y751 in the SH2-binding motif of Platelet-derived growth factor receptor beta (PDGFRB) induces binding to the Phosphatidylinositol 3-kinase regulatory subunit alpha (PIK3R1) protein. | details | Inferred |
HIF-1 signaling pathway (KEGG - hsa04066)
|
| LIG_SH2_STAT5 | INSR_HUMAN | 1361 | 1364 | Specificity | Domain hiding | PIP3 (1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate), a product of PI3-kinase, binds to the SH2 domains of PI3K (Phosphatidylinositol 3-kinase regulatory subunit alpha (PIK3R1)) and thereby blocks its interaction with tyrosine-phosphorylated SH2 motif containing proteins. | details | Inferred |
Insulin signaling pathway (KEGG - hsa04910)
|
| LIG_SH2_STAT5 | INSR_HUMAN | 1361 | 1364 | Specificity | Domain hiding | PIP3 (1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate), a product of PI3-kinase, binds to the SH2 domains of PI3K (Phosphatidylinositol 3-kinase regulatory subunit alpha (PIK3R1)) and thereby blocks its interaction with tyrosine-phosphorylated SH2 motif containing proteins. | details | Inferred |
PI3K-Akt signaling pathway (KEGG - hsa04151)
|
| LIG_SH2_STAT5 | INSR_HUMAN | 1361 | 1364 | Specificity | Domain hiding | PIP3 (1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate), a product of PI3-kinase, binds to the SH2 domains of PI3K (Phosphatidylinositol 3-kinase regulatory subunit alpha (PIK3R1)) and thereby blocks its interaction with tyrosine-phosphorylated SH2 motif containing proteins. | details | Inferred |
| LIG_SH2_IIA | PGFRB_HUMAN | 751 | 755 | Binary | Physicochemical compatibility | Phosphorylation of Y751 in the SH2-binding motif of Platelet-derived growth factor receptor beta (PDGFRB) induces binding to the Phosphatidylinositol 3-kinase regulatory subunit alpha (PIK3R1) protein. | details | Inferred |
Regulation of actin cytoskeleton (KEGG - hsa04810)
|
| LIG_SH2_IIA | PGFRB_HUMAN | 751 | 755 | Binary | Physicochemical compatibility | Phosphorylation of Y751 in the SH2-binding motif of Platelet-derived growth factor receptor beta (PDGFRB) induces binding to the Phosphatidylinositol 3-kinase regulatory subunit alpha (PIK3R1) protein. | details | Inferred |
