LIG_SH2_STAT5 - STAT5 Src Homology 2 (SH2) domain binding motif. |
| LAT_HUMAN | 161 | 164 | Binary | Physicochemical compatibility | Phosphorylation of Y161 in the SH2-binding motif of Linker for activation of T-cells family member 1 (LAT) induces binding to the 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-1 (PLCG1) protein. | details |
| CTLA4_MOUSE | 201 | 204 | Specificity | Altered binding specificity | Dephosphorylation of Y201 of Cytotoxic T-lymphocyte protein 4 (Ctla4) switches the specificity of Ctla4 from SH2 domain-containing proteins like Tyrosine-protein phosphatase non-receptor type 11 (Ptpn11) to the AP-2 complex mu subunit (AP-2 complex subunit mu (Ap2m1)), thereby switching from inhibitory signal transmission and negative regulation of T cell responses to internalization and inactivation of Ctla4. | details |
| 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 |
| 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 |
| STA5A_HUMAN | 694 | 697 | Binary | Pre‑translational | Alternative splicing removes the regulatory Y694 residue of Signal transducer and activator of transcription 5A (STAT5A). The phosphorylation of Y694 by Proto-oncogene tyrosine-protein kinase Src (SRC) has been shown to be essential for DNA binding. This event acts as an important regulatory mechanism (See Clark et al. (2005) (here) and Okutani et al. (2001) (here)). The exact function of Y694 remains uncertain as is binding to STAT5 in dimer. The STAT5A-DeltaE18 does not enter nucleus upon PRLR stimulation. | details |
| PRLR_HUMAN | 342 | 345 | Binary | Pre‑translational | Alternative Splicing removes the degron motif of Prolactin receptor (PRLR), abrogating binding to Signal transducer and activator of transcription 5A (STAT5A). The PRLR S1a (Isoform Short form 1a of Prolactin receptor (PRLR)) and S1b and (Isoform Short form 1b of Prolactin receptor (PRLR)) isoforms were unable to mediate the transcriptional activation of the beta-casein promoter via the JAK-STAT5 pathway. Therefore these two splice variants act as dominant negatives on the full-length version LF (Isoform 1 of Prolactin receptor (PRLR)). Another study showed that different splice variants of heterodimers (e.g. LF/S1a, LF/S1b) that were able to induce JAK2 phosphorylation but not further signalling events due to lack of STAT recruitment (Qazi et al. (2006) (here)). | details |
| 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 |
| 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 |
