switches.ELM

Group by :Switch type Motif class Protein Enzyme Pathway Hide inferred Group Index Colouring Info Filtered: PFAM:PF00017 (269 hits) x

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Curated inferred

x Index

Cyclin-dependent kinase 1	Ephrin type-A receptor 3	Ephrin type-B receptor 2
Ephrin type-B receptor 2 (Mus)	Epidermal growth factor receptor	Focal adhesion kinase 1
Glycogen synthase kinase-3 beta	Hepatocyte growth factor receptor	High affinity nerve growth factor receptor
Insulin receptor	Insulin receptor (Rattus)	Insulin-like growth factor 1 receptor
Macrophage-stimulating protein receptor	Neuronal proto-oncogene tyrosine-protein kinase Src (Mus)	Platelet-derived growth factor receptor beta
Protein-tyrosine kinase 2-beta	Proto-oncogene tyrosine-protein kinase LCK (Mus)	Proto-oncogene tyrosine-protein kinase Src
Proto-oncogene tyrosine-protein kinase Src (Rattus)	Proto-oncogene tyrosine-protein kinase receptor Ret	Receptor tyrosine-protein kinase erbB-2
Receptor tyrosine-protein kinase erbB-4	Tyrosine-protein kinase ABL1	Tyrosine-protein kinase ABL1 (Mus)
Tyrosine-protein kinase Blk	Tyrosine-protein kinase CSK	Tyrosine-protein kinase Fgr
Tyrosine-protein kinase Fyn	Tyrosine-protein kinase Fyn (Mus)	Tyrosine-protein kinase JAK1
Tyrosine-protein kinase JAK2	Tyrosine-protein kinase JAK2 (Mus)	Tyrosine-protein kinase JAK3
Tyrosine-protein kinase Lck	Tyrosine-protein kinase Lyn	Tyrosine-protein kinase Lyn (Mus)
Tyrosine-protein kinase SYK	Tyrosine-protein kinase TXK	Tyrosine-protein kinase Yes
Tyrosine-protein kinase ZAP-70	Tyrosine-protein kinase ZAP-70 (Mus)	Vascular endothelial growth factor receptor 3

Motif

Protein

Start

End

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Information

Evidence

Cyclin-dependent kinase 1 - CDK1 - Homo sapiens
LIG_SH2_GRB2	A4_HUMAN	757	760	Cumulative	Rheostatic	While phosphorylation of Y757 in the SH2-binding motif of Amyloid beta A4 protein (APP) induces binding to Growth factor receptor-bound protein 2 (GRB2), additional phosphorylation of T743 further increases the strength of the interaction.	details	Inferred
Ephrin type-A receptor 3 - EPHA3 - Homo sapiens
LIG_SH2_IA	EPHA3_HUMAN	597	606	Binary	Physicochemical compatibility	Phosphorylation of Y602 in the SH2-binding motif of Ephrin type-A receptor 3 (EPHA3) induces binding to the Cytoplasmic protein NCK1 (NCK1) protein.	details	Inferred
Ephrin type-B receptor 2 - EPHB2 - Homo sapiens
LIG_SH2_IB	EPHB2_MOUSE	601	610	Binary	Physicochemical compatibility	Phosphorylation of Y604 in the SH2-binding motif of Ephrin type-B receptor 2 (Ephb2) induces binding to the Adapter molecule crk (CRK) protein.	details	Inferred
LIG_SH2_IB	EPHB2_MOUSE	606	620	Binary	Physicochemical compatibility	Phosphorylation of Y610 in the SH2-binding motif of Ephrin type-B receptor 2 (Ephb2) induces binding to the Adapter molecule crk (CRK) protein.	details	Inferred
LIG_SH2_IB	EPHB2_MOUSE	606	620	Binary	Physicochemical compatibility	Phosphorylation of Y610 in the SH2-binding motif of Ephrin type-B receptor 2 (Ephb2) induces binding to the Adapter molecule crk (CRK) protein.	details	Inferred
LIG_SH2_IB	EPHB2_MOUSE	606	620	Binary	Physicochemical compatibility	Phosphorylation of Y610 in the SH2-binding motif of Ephrin type-B receptor 2 (Ephb2) induces binding to the Adapter molecule crk (CRK) protein.	details	Inferred
Ephrin type-B receptor 2 - EPHB2 - Mus musculus
LIG_SH2_IB	EPHB2_MOUSE	601	610	Binary	Physicochemical compatibility	Phosphorylation of Y604 in the SH2-binding motif of Ephrin type-B receptor 2 (Ephb2) induces binding to the Adapter molecule crk (CRK) protein.	details	Inferred
LIG_SH2_IB	EPHB2_MOUSE	606	620	Binary	Physicochemical compatibility	Phosphorylation of Y610 in the SH2-binding motif of Ephrin type-B receptor 2 (Ephb2) induces binding to the Adapter molecule crk (CRK) protein.	details	Inferred
Epidermal growth factor receptor - EGFR - Homo sapiens
LIG_SH2_IC	EGFR_HUMAN	1092	1100	Binary	Physicochemical compatibility	Phosphorylation of Y1092 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the Growth factor receptor-bound protein 2 (GRB2) protein.	details	Inferred
LIG_SH2_IC	EGFR_HUMAN	1092	1100	Binary	Physicochemical compatibility	Phosphorylation of Y1092 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the Growth factor receptor-bound protein 2 (GRB2) protein.	details	Inferred
LIG_SH2_IE	EGFR_HUMAN	1008	1024	Binary	Physicochemical compatibility	Phosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the Tyrosine-protein kinase JAK2 (JAK2) protein.	details	Inferred
LIG_SH2_ID	EGFR_HUMAN	1008	1024	Binary	Physicochemical compatibility	Phosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the SH2 domain-containing protein 3C (SH2D3C) protein.	details	Inferred
LIG_SH2_ID	EGFR_HUMAN	1008	1024	Binary	Physicochemical compatibility	Phosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the SH2 domain-containing protein 3A (SH2D3A) protein.	details	Inferred
LIG_SH2_III	EGFR_HUMAN	1008	1024	Binary	Physicochemical compatibility	Phosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the Signal transducer and activator of transcription 6 (STAT6) protein.	details	Inferred
LIG_SH2_SRC	EGFR_HUMAN	1016	1019	Binary	Physicochemical compatibility	Phosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-1 (PLCG1).	details	Inferred
LIG_SH2_SRC	EGFR_HUMAN	1016	1019	Binary	Physicochemical compatibility	Phosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to Cytoplasmic protein NCK1 (NCK1).	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	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	Inferred
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	Inferred
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	Inferred
Focal adhesion kinase 1 - PTK2 - Homo sapiens
LIG_SH2_IA	FAK1_HUMAN	389	405	Binary	Physicochemical compatibility	Phosphorylation of Y397 in the SH2-binding motif of Focal adhesion kinase 1 (PTK2) induces binding to the Cytoplasmic protein NCK2 (NCK2) protein.	details	Inferred
LIG_SH2_IA	FAK1_HUMAN	389	405	Binary	Physicochemical compatibility	Phosphorylation of Y397 in the SH2-binding motif of Focal adhesion kinase 1 (PTK2) induces binding to the Cytoplasmic protein NCK2 (NCK2) protein.	details	Inferred
LIG_SH2_SRC	FAK1_HUMAN	397	400	Binary	Physicochemical compatibility	Phosphorylation of Y397 in the SH2-binding motif of Focal adhesion kinase 1 (PTK2) induces binding to Neuronal proto-oncogene tyrosine-protein kinase Src (Src).	details	Inferred
LIG_SH2_SRC	FAK1_HUMAN	397	400	Binary	Physicochemical compatibility	Phosphorylation of Y397 in the SH2-binding motif of Focal adhesion kinase 1 (PTK2) induces binding to Neuronal proto-oncogene tyrosine-protein kinase Src (Src).	details	Inferred
Glycogen synthase kinase-3 beta - GSK3B - Homo sapiens
LIG_SH2_GRB2	A4_HUMAN	757	760	Cumulative	Rheostatic	While phosphorylation of Y757 in the SH2-binding motif of Amyloid beta A4 protein (APP) induces binding to Growth factor receptor-bound protein 2 (GRB2), additional phosphorylation of T743 further increases the strength of the interaction.	details	Inferred
Hepatocyte growth factor receptor - MET - Homo sapiens
LIG_SH2_IC	MET_HUMAN	1351	1360	Binary	Physicochemical compatibility	Phosphorylation of Y1356 in the SH2-binding motif of Hepatocyte growth factor receptor (MET) induces binding to the Growth factor receptor-bound protein 2 (GRB2) protein.	details	Inferred
LIG_SH2_IC	MET_HUMAN	1351	1360	Binary	Physicochemical compatibility	Phosphorylation of Y1356 in the SH2-binding motif of Hepatocyte growth factor receptor (MET) induces binding to the Growth factor receptor-bound protein 2 (GRB2) protein.	details	Inferred
LIG_SH2_IC	MET_HUMAN	1351	1360	Binary	Physicochemical compatibility	Phosphorylation of Y1356 in the SH2-binding motif of Hepatocyte growth factor receptor (MET) induces binding to the Growth factor receptor-bound protein 2 (GRB2) protein.	details	Inferred
LIG_SH2_IC	MET_HUMAN	1351	1360	Binary	Physicochemical compatibility	Phosphorylation of Y1356 in the SH2-binding motif of Hepatocyte growth factor receptor (MET) induces binding to the Growth factor receptor-bound protein 2 (GRB2) protein.	details	Inferred
LIG_SH2_IC	SHC1_HUMAN	423	435	Binary	Physicochemical compatibility	Phosphorylation of Y427 in the SH2-binding motif of SHC-transforming protein 1 (SHC1) induces binding to the Growth factor receptor-bound protein 2 (GRB2) protein.	details	Inferred
LIG_SH2_IA	FAK1_HUMAN	389	405	Binary	Physicochemical compatibility	Phosphorylation of Y397 in the SH2-binding motif of Focal adhesion kinase 1 (PTK2) induces binding to the Cytoplasmic protein NCK2 (NCK2) protein.	details	Inferred
LIG_SH2_SRC	FAK1_HUMAN	397	400	Binary	Physicochemical compatibility	Phosphorylation of Y397 in the SH2-binding motif of Focal adhesion kinase 1 (PTK2) induces binding to Neuronal proto-oncogene tyrosine-protein kinase Src (Src).	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	Inferred
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	Inferred
High affinity nerve growth factor receptor - NTRK1 - Homo sapiens
LIG_SH2_IIB	NTRK1_HUMAN	782	796	Binary	Physicochemical compatibility	Phosphorylation of Y791 in the SH2-binding motif of High affinity nerve growth factor receptor (NTRK1) induces binding to the SHC-transforming protein 1 (SHC1) protein.	details	Inferred
LIG_SH2_IIB	NTRK1_HUMAN	782	796	Binary	Physicochemical compatibility	Phosphorylation of Y791 in the SH2-binding motif of High affinity nerve growth factor receptor (NTRK1) induces binding to the SHC-transforming protein 1 (SHC1) protein.	details	Inferred
LIG_SH2_IB	NTRK1_HUMAN	783	796	Binary	Physicochemical compatibility	Phosphorylation of Y791 in the SH2-binding motif of High affinity nerve growth factor receptor (NTRK1) induces binding to the Megakaryocyte-associated tyrosine-protein kinase (MATK) protein.	details	Inferred
LIG_SH2_IB	NTRK1_HUMAN	783	796	Binary	Physicochemical compatibility	Phosphorylation of Y791 in the SH2-binding motif of High affinity nerve growth factor receptor (NTRK1) induces binding to the Megakaryocyte-associated tyrosine-protein kinase (MATK) protein.	details	Inferred
Insulin receptor - INSR - Rattus norvegicus
LIG_SH2_GRB2	IRS1_RAT	895	898	Binary	Physicochemical compatibility	Phosphorylation of Y895 in the SH2-binding motif of Insulin receptor substrate 1 (Irs1) induces binding to the Growth factor receptor-bound protein 2 (Grb2) protein.	details	Inferred
LIG_SH2_IB	CBL_HUMAN	770	780	Binary	Physicochemical compatibility	Phosphorylation of Y774 in the SH2-binding motif of E3 ubiquitin-protein ligase CBL (CBL) induces binding to the Adapter molecule crk (CRK) protein.	details	Inferred
Insulin receptor - INSR - Homo sapiens
LIG_SH2_GRB2	IRS1_RAT	895	898	Binary	Physicochemical compatibility	Phosphorylation of Y895 in the SH2-binding motif of Insulin receptor substrate 1 (Irs1) induces binding to the Growth factor receptor-bound protein 2 (Grb2) protein.	details	Inferred
LIG_SH2_GRB2	IRS1_RAT	895	898	Binary	Physicochemical compatibility	Phosphorylation of Y895 in the SH2-binding motif of Insulin receptor substrate 1 (Irs1) induces binding to the Growth factor receptor-bound protein 2 (Grb2) protein.	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	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	Inferred
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	Inferred
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	Inferred
Insulin-like growth factor 1 receptor - IGF1R - Homo sapiens
LIG_SH2_GRB2	IRS1_RAT	895	898	Binary	Physicochemical compatibility	Phosphorylation of Y895 in the SH2-binding motif of Insulin receptor substrate 1 (Irs1) induces binding to the Growth factor receptor-bound protein 2 (Grb2) protein.	details	Inferred
LIG_SH2_IC	PDPK1_HUMAN	376	379	Binary	Physicochemical compatibility	Phosphorylation of Y376 in the SH2-binding motif of 3-phosphoinositide-dependent protein kinase 1 (PDPK1) induces binding to the Tensin-1 (TNS1) protein.	details	Inferred
Macrophage-stimulating protein receptor - MST1R - Homo sapiens
LIG_SH2_IC	MET_HUMAN	1351	1360	Binary	Physicochemical compatibility	Phosphorylation of Y1356 in the SH2-binding motif of Hepatocyte growth factor receptor (MET) induces binding to the Growth factor receptor-bound protein 2 (GRB2) protein.	details	Inferred
Neuronal proto-oncogene tyrosine-protein kinase Src - SRC - Mus musculus
LIG_SH2_IC	EGFR_HUMAN	1092	1100	Binary	Physicochemical compatibility	Phosphorylation of Y1092 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the Growth factor receptor-bound protein 2 (GRB2) protein.	details	Inferred
LIG_SH2_IA	DAB1_MOUSE	212	228	Binary	Physicochemical compatibility	Phosphorylation of Y220 in the SH2-binding motif of Disabled homolog 1 (Dab1) induces binding to the Cytoplasmic protein NCK2 (NCK2) protein.	details	Inferred
LIG_SH2_IA	DAB1_MOUSE	220	223	Binary	Pre‑translational	Alternative splicing removes the SH2-binding motif of Disabled homolog 1 (Dab1), abrogating binding to Cytoplasmic protein NCK2 (NCK2). NCK2-beta has a clear preference for splice variant 2 (with the YQYI motif) over splice variant 3 (with the YQTI motif). The authors theorise that since Adapter molecule crk (Crk) is directly linked to the C3G-Rap1 pathway, and NCK2-beta is linked to the Breast cancer anti-estrogen resistance protein 1 (Bcar1) (p130Cas) pathway, it is likely that isoforms 2 and 3 connect to different downstream cascades. It was suggested that the ability of different Dab1 isoforms to recruit distinct sets of SH2 domains implies a fine-tuning role of Dab1 splicing in the intricate series of events that underlie neuronal migration (Gao et al. (2012) (here)) (See also Katyal and Godbout (2004) (here) and Gao et al. (2010) (here)).	details	Curated
LIG_SH2_IA	DAB1_MOUSE	220	223	Binary	Pre‑translational	Alternative splicing removes the SH2-binding motif of Disabled homolog 1 (Dab1), abrogating binding to Adapter molecule crk (Crk). Both Adapter molecule crk (Crk) and Crk-like protein (Crkl) bind equally well to variants 2 and 3. The authors theorise that since Adapter molecule crk (Crk) is directly linked to the C3G-Rap1 pathway, and NCK2-beta is linked to the Breast cancer anti-estrogen resistance protein 1 (Bcar1) (p130Cas) pathway, it is likely that isoforms 2 and 3 connect to different downstream cascades. It was suggested that the ability of different Dab1 isoforms to recruit distinct sets of SH2 domains implies a fine-tuning role of Dab1 splicing in the intricate series of events that underlie neuronal migration (Gao et al. (2012) (here)) (See also Katyal and Godbout (2004) (here) and Gao et al. (2010) (here)).	details	Curated
LIG_SH2_SRC	DAB1_MOUSE	198	201	Binary	Pre‑translational	Alternative splicing removes the SH2-binding motif of Disabled homolog 1 (Dab1), abrogating binding to Neuronal proto-oncogene tyrosine-protein kinase Src (Src). Splice variants 2 and 3 (only containing one of the YQxI motifs, i.e. Y185 and Y198) exhibit decreased tyrosine phosphorylation, suggesting both motifs are required for full activation of Dab1. Dab1 is likely to recruit Neuronal proto-oncogene tyrosine-protein kinase Src (Src) via these two YQxI motifs, which subsequently phosphorylates adjacent YxVP motifs (here). This was also suggested for Phosphatidylinositol 3-kinase regulatory subunit alpha (Pik3r1) and Suppressor of cytokine signaling 2 (Socs2). Gao et al. (2012) (here) suggests that the ability of different Dab1 isoforms to recruit distinct sets of SH2 domains allows a fine-tuning role for Dab1 splicing in the intricate series of events that underlie neuronal migration (See also Katyal & Godbout (2004) (here) and Gao et al. (2010) (here)).	details	Curated
LIG_SH2_SRC	DAB1_MOUSE	198	201	Binary	Physicochemical compatibility	Phosphorylation of Y198 in the SH2-binding motif of Disabled homolog 1 (Dab1) induces binding to Neuronal proto-oncogene tyrosine-protein kinase Src (Src).	details	Curated
Platelet-derived growth factor receptor beta - PDGFRB - Homo sapiens
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
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
LIG_SH2_IIA	PGFRB_HUMAN	1018	1029	Binary	Physicochemical compatibility	Phosphorylation of Y1021 in the SH2-binding motif of Platelet-derived growth factor receptor beta (PDGFRB) induces binding to the 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-1 (PLCG1) protein.	details	Inferred
LIG_SH2_IIA	PGFRB_HUMAN	1018	1029	Binary	Physicochemical compatibility	Phosphorylation of Y1021 in the SH2-binding motif of Platelet-derived growth factor receptor beta (PDGFRB) induces binding to the 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-1 (PLCG1) protein.	details	Inferred
Protein-tyrosine kinase 2-beta - PTK2B - Homo sapiens
LIG_SH2_IB	FAK2_HUMAN	394	410	Binary	Physicochemical compatibility	Phosphorylation of Y402 in the SH2-binding motif of Protein-tyrosine kinase 2-beta (PTK2B) induces binding to the Megakaryocyte-associated tyrosine-protein kinase (MATK) protein.	details	Inferred
LIG_SH2_IB	FAK2_HUMAN	394	410	Binary	Physicochemical compatibility	Phosphorylation of Y402 in the SH2-binding motif of Protein-tyrosine kinase 2-beta (PTK2B) induces binding to the Megakaryocyte-associated tyrosine-protein kinase (MATK) protein.	details	Inferred
Proto-oncogene tyrosine-protein kinase LCK - LCK - Mus musculus
LIG_SH2_STAT5	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	Inferred
Proto-oncogene tyrosine-protein kinase Src - SRC - Rattus norvegicus
LIG_SH2_SRC	SRC_HUMAN	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.	details	Inferred
Proto-oncogene tyrosine-protein kinase Src - SRC - Homo sapiens
LIG_SH2_SRC	SRC_HUMAN	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.	details	Inferred
LIG_SH2_SRC	DAG1_HUMAN	892	895	Specificity	Altered binding specificity	Adhesion-dependent phosphorylation of Y892 in Dystroglycan (DAG1) by Src kinase (Proto-oncogene tyrosine-protein kinase Src (SRC)) switches the specificity of DAG1 from the WW domain containing cytoskeletal linker Dystrophin (DMD) to the SH2 domain containing Tyrosine-protein kinase Fyn (FYN).	details	Inferred
LIG_SH2_SRC	DAG1_HUMAN	892	895	Specificity	Altered binding specificity	Adhesion-dependent phosphorylation of Y892 in Dystroglycan (DAG1) by c-Src (SRC) switches the specificity of DAG1 from WW domain containing proteins like Utrophin (UTRN) to SH2 domain containing proteins like Tyrosine-protein kinase CSK (CSK).	details	Inferred
LIG_TYR_ITSM	OX1R_HUMAN	79	86	Avidity‑sensing		Orexin-A induced phosphorylation of the ITSM and ITIM motifs in Orexin receptor type 1 (HCRTR1) allows binding of Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) via its two SH2 domains. Mutation of either tyrosine in the motifs abolishes binding of Tyrosine-protein phosphatase non-receptor type 11 (PTPN11).	details	Inferred
LIG_TYR_ITIM	OX1R_HUMAN	356	361	Avidity‑sensing		Orexin-A induced phosphorylation of the ITSM and ITIM motifs in Orexin receptor type 1 (HCRTR1) allows binding of Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) via its two SH2 domains. Mutation of either tyrosine in the motifs abolishes binding of Tyrosine-protein phosphatase non-receptor type 11 (PTPN11).	details	Inferred
LIG_SH2_IC	PDPK1_HUMAN	376	379	Binary	Physicochemical compatibility	Phosphorylation of Y376 in the SH2-binding motif of 3-phosphoinositide-dependent protein kinase 1 (PDPK1) induces binding to the Tensin-1 (TNS1) protein.	details	Inferred
LIG_SH2_IC	PDPK1_HUMAN	376	379	Binary	Physicochemical compatibility	Phosphorylation of Y376 in the SH2-binding motif of 3-phosphoinositide-dependent protein kinase 1 (PDPK1) induces binding to the Tensin-1 (TNS1) protein.	details	Inferred
LIG_SH2_IE	EGFR_HUMAN	1008	1024	Binary	Physicochemical compatibility	Phosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the Tyrosine-protein kinase JAK2 (JAK2) protein.	details	Inferred
LIG_SH2_IE	EGFR_HUMAN	1008	1024	Binary	Physicochemical compatibility	Phosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the Tyrosine-protein kinase JAK2 (JAK2) protein.	details	Inferred
LIG_SH2_ID	EGFR_HUMAN	1008	1024	Binary	Physicochemical compatibility	Phosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the SH2 domain-containing protein 3C (SH2D3C) protein.	details	Inferred
LIG_SH2_ID	EGFR_HUMAN	1008	1024	Binary	Physicochemical compatibility	Phosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the SH2 domain-containing protein 3C (SH2D3C) protein.	details	Inferred
LIG_SH2_ID	EGFR_HUMAN	1008	1024	Binary	Physicochemical compatibility	Phosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the SH2 domain-containing protein 3A (SH2D3A) protein.	details	Inferred
LIG_SH2_ID	EGFR_HUMAN	1008	1024	Binary	Physicochemical compatibility	Phosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the SH2 domain-containing protein 3A (SH2D3A) protein.	details	Inferred
LIG_SH2_III	EGFR_HUMAN	1008	1024	Binary	Physicochemical compatibility	Phosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the Signal transducer and activator of transcription 6 (STAT6) protein.	details	Inferred
LIG_SH2_III	EGFR_HUMAN	1008	1024	Binary	Physicochemical compatibility	Phosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the Signal transducer and activator of transcription 6 (STAT6) protein.	details	Inferred
LIG_SH2_IB	CBL_HUMAN	770	780	Binary	Physicochemical compatibility	Phosphorylation of Y774 in the SH2-binding motif of E3 ubiquitin-protein ligase CBL (CBL) induces binding to the Adapter molecule crk (CRK) protein.	details	Inferred
LIG_SH2_IC	SHC1_HUMAN	423	435	Binary	Physicochemical compatibility	Phosphorylation of Y427 in the SH2-binding motif of SHC-transforming protein 1 (SHC1) induces binding to the Growth factor receptor-bound protein 2 (GRB2) protein.	details	Inferred
LIG_SH2_IA	FAK1_HUMAN	389	405	Binary	Physicochemical compatibility	Phosphorylation of Y397 in the SH2-binding motif of Focal adhesion kinase 1 (PTK2) induces binding to the Cytoplasmic protein NCK2 (NCK2) protein.	details	Inferred
LIG_SH2_IB	FAK2_HUMAN	394	410	Binary	Physicochemical compatibility	Phosphorylation of Y402 in the SH2-binding motif of Protein-tyrosine kinase 2-beta (PTK2B) induces binding to the Megakaryocyte-associated tyrosine-protein kinase (MATK) protein.	details	Inferred
LIG_SH2_IA	DAB1_MOUSE	212	228	Binary	Physicochemical compatibility	Phosphorylation of Y220 in the SH2-binding motif of Disabled homolog 1 (Dab1) induces binding to the Cytoplasmic protein NCK2 (NCK2) protein.	details	Inferred
LIG_SH2_IA	DAB1_MOUSE	212	228	Binary	Physicochemical compatibility	Phosphorylation of Y220 in the SH2-binding motif of Disabled homolog 1 (Dab1) induces binding to the Cytoplasmic protein NCK2 (NCK2) protein.	details	Inferred
LIG_SH2_III	STA5A_HUMAN	686	702	Binary	Physicochemical compatibility	Phosphorylation of Y694 in the SH2-binding motif of Signal transducer and activator of transcription 5A (STAT5A) induces binding to the Signal transducer and activator of transcription 5B (STAT5B) protein.	details	Inferred
LIG_SH2_III	STA5A_HUMAN	686	702	Binary	Physicochemical compatibility	Phosphorylation of Y694 in the SH2-binding motif of Signal transducer and activator of transcription 5A (STAT5A) induces binding to the Signal transducer and activator of transcription 5B (STAT5B) protein.	details	Inferred
LIG_SH2_IA	DAB1_MOUSE	220	223	Binary	Pre‑translational	Alternative splicing removes the SH2-binding motif of Disabled homolog 1 (Dab1), abrogating binding to Cytoplasmic protein NCK2 (NCK2). NCK2-beta has a clear preference for splice variant 2 (with the YQYI motif) over splice variant 3 (with the YQTI motif). The authors theorise that since Adapter molecule crk (Crk) is directly linked to the C3G-Rap1 pathway, and NCK2-beta is linked to the Breast cancer anti-estrogen resistance protein 1 (Bcar1) (p130Cas) pathway, it is likely that isoforms 2 and 3 connect to different downstream cascades. It was suggested that the ability of different Dab1 isoforms to recruit distinct sets of SH2 domains implies a fine-tuning role of Dab1 splicing in the intricate series of events that underlie neuronal migration (Gao et al. (2012) (here)) (See also Katyal and Godbout (2004) (here) and Gao et al. (2010) (here)).	details	Inferred
LIG_SH2_IA	DAB1_MOUSE	220	223	Binary	Pre‑translational	Alternative splicing removes the SH2-binding motif of Disabled homolog 1 (Dab1), abrogating binding to Cytoplasmic protein NCK2 (NCK2). NCK2-beta has a clear preference for splice variant 2 (with the YQYI motif) over splice variant 3 (with the YQTI motif). The authors theorise that since Adapter molecule crk (Crk) is directly linked to the C3G-Rap1 pathway, and NCK2-beta is linked to the Breast cancer anti-estrogen resistance protein 1 (Bcar1) (p130Cas) pathway, it is likely that isoforms 2 and 3 connect to different downstream cascades. It was suggested that the ability of different Dab1 isoforms to recruit distinct sets of SH2 domains implies a fine-tuning role of Dab1 splicing in the intricate series of events that underlie neuronal migration (Gao et al. (2012) (here)) (See also Katyal and Godbout (2004) (here) and Gao et al. (2010) (here)).	details	Inferred
LIG_SH2_IA	DAB1_MOUSE	232	235	Binary	Pre‑translational	Alternative splicing removes the SH2-binding motif of Disabled homolog 1 (Dab1), abrogating binding to Cytoplasmic protein NCK2 (NCK2). The NCK2-beta has a clear preference for splice variant 2 (with YQYI motif) over splice variant 3 (with YQTI motif). The authors theorise that since Adapter molecule crk (Crk) is directly linked to the C3G-Rap1 pathway, and NCK2-beta is linked to the Breast cancer anti-estrogen resistance protein 1 (Bcar1) (p130Cas) pathway, it is likely that isoforms 2 and 3 connect to different downstream cascades. It was suggested that the ability of different Dab1 isoforms to recruit distinct sets of SH2 domains implies a fine-tuning role of Dab1 splicing in the intricate series of events that underlie neuronal migration (Gao et al. (2012) (here)) (See also Katyal and Godbout (2004) (here) and Gao et al. (2010) (here)).	details	Inferred
LIG_SH2_IA	DAB1_MOUSE	232	235	Binary	Pre‑translational	Alternative splicing removes the SH2-binding motif of Disabled homolog 1 (Dab1), abrogating binding to Cytoplasmic protein NCK2 (NCK2). The NCK2-beta has a clear preference for splice variant 2 (with YQYI motif) over splice variant 3 (with YQTI motif). The authors theorise that since Adapter molecule crk (Crk) is directly linked to the C3G-Rap1 pathway, and NCK2-beta is linked to the Breast cancer anti-estrogen resistance protein 1 (Bcar1) (p130Cas) pathway, it is likely that isoforms 2 and 3 connect to different downstream cascades. It was suggested that the ability of different Dab1 isoforms to recruit distinct sets of SH2 domains implies a fine-tuning role of Dab1 splicing in the intricate series of events that underlie neuronal migration (Gao et al. (2012) (here)) (See also Katyal and Godbout (2004) (here) and Gao et al. (2010) (here)).	details	Inferred
LIG_SH2_IA	DAB1_MOUSE	232	235	Binary	Pre‑translational	Alternative splicing removes the SH2-binding motif of Disabled homolog 1 (Dab1), abrogating binding to Cytoplasmic protein NCK2 (NCK2). The NCK2-beta has a clear preference for splice variant 2 (with YQYI motif) over splice variant 3 (with YQTI motif). The authors theorise that since Adapter molecule crk (Crk) is directly linked to the C3G-Rap1 pathway, and NCK2-beta is linked to the Breast cancer anti-estrogen resistance protein 1 (Bcar1) (p130Cas) pathway, it is likely that isoforms 2 and 3 connect to different downstream cascades. It was suggested that the ability of different Dab1 isoforms to recruit distinct sets of SH2 domains implies a fine-tuning role of Dab1 splicing in the intricate series of events that underlie neuronal migration (Gao et al. (2012) (here)) (See also Katyal and Godbout (2004) (here) and Gao et al. (2010) (here)).	details	Inferred
LIG_SH2_IA	DAB1_MOUSE	220	223	Binary	Pre‑translational	Alternative splicing removes the SH2-binding motif of Disabled homolog 1 (Dab1), abrogating binding to Adapter molecule crk (Crk). Both Adapter molecule crk (Crk) and Crk-like protein (Crkl) bind equally well to variants 2 and 3. The authors theorise that since Adapter molecule crk (Crk) is directly linked to the C3G-Rap1 pathway, and NCK2-beta is linked to the Breast cancer anti-estrogen resistance protein 1 (Bcar1) (p130Cas) pathway, it is likely that isoforms 2 and 3 connect to different downstream cascades. It was suggested that the ability of different Dab1 isoforms to recruit distinct sets of SH2 domains implies a fine-tuning role of Dab1 splicing in the intricate series of events that underlie neuronal migration (Gao et al. (2012) (here)) (See also Katyal and Godbout (2004) (here) and Gao et al. (2010) (here)).	details	Inferred
LIG_SH2_IA	DAB1_MOUSE	220	223	Binary	Pre‑translational	Alternative splicing removes the SH2-binding motif of Disabled homolog 1 (Dab1), abrogating binding to Adapter molecule crk (Crk). Both Adapter molecule crk (Crk) and Crk-like protein (Crkl) bind equally well to variants 2 and 3. The authors theorise that since Adapter molecule crk (Crk) is directly linked to the C3G-Rap1 pathway, and NCK2-beta is linked to the Breast cancer anti-estrogen resistance protein 1 (Bcar1) (p130Cas) pathway, it is likely that isoforms 2 and 3 connect to different downstream cascades. It was suggested that the ability of different Dab1 isoforms to recruit distinct sets of SH2 domains implies a fine-tuning role of Dab1 splicing in the intricate series of events that underlie neuronal migration (Gao et al. (2012) (here)) (See also Katyal and Godbout (2004) (here) and Gao et al. (2010) (here)).	details	Inferred
LIG_SH2_IA	DAB1_MOUSE	232	235	Binary	Pre‑translational	Alternative splicing removes the SH2-binding motif of Disabled homolog 1 (Dab1), abrogating binding to Adapter molecule crk (Crk). Both Adapter molecule crk (Crk) and Crk-like protein (Crkl) bind equally well to variants 2 and 3. The authors theorise that since Adapter molecule crk (Crk) is directly linked to the C3G-Rap1 pathway, and NCK2-beta is linked to the Breast cancer anti-estrogen resistance protein 1 (Bcar1) (p130Cas) pathway, it is likely that isoforms 2 and 3 connect to different downstream cascades. It was suggested that the ability of different Dab1 isoforms to recruit distinct sets of SH2 domains implies a fine-tuning role of Dab1 splicing in the intricate series of events that underlie neuronal migration (Gao et al. (2012) (here)) (See also Katyal and Godbout (2004) (here) and Gao et al. (2010) (here)).	details	Inferred
LIG_SH2_IA	DAB1_MOUSE	232	235	Binary	Pre‑translational	Alternative splicing removes the SH2-binding motif of Disabled homolog 1 (Dab1), abrogating binding to Adapter molecule crk (Crk). Both Adapter molecule crk (Crk) and Crk-like protein (Crkl) bind equally well to variants 2 and 3. The authors theorise that since Adapter molecule crk (Crk) is directly linked to the C3G-Rap1 pathway, and NCK2-beta is linked to the Breast cancer anti-estrogen resistance protein 1 (Bcar1) (p130Cas) pathway, it is likely that isoforms 2 and 3 connect to different downstream cascades. It was suggested that the ability of different Dab1 isoforms to recruit distinct sets of SH2 domains implies a fine-tuning role of Dab1 splicing in the intricate series of events that underlie neuronal migration (Gao et al. (2012) (here)) (See also Katyal and Godbout (2004) (here) and Gao et al. (2010) (here)).	details	Inferred
LIG_SH2_IA	DAB1_MOUSE	232	235	Binary	Pre‑translational	Alternative splicing removes the SH2-binding motif of Disabled homolog 1 (Dab1), abrogating binding to Adapter molecule crk (Crk). Both Adapter molecule crk (Crk) and Crk-like protein (Crkl) bind equally well to variants 2 and 3. The authors theorise that since Adapter molecule crk (Crk) is directly linked to the C3G-Rap1 pathway, and NCK2-beta is linked to the Breast cancer anti-estrogen resistance protein 1 (Bcar1) (p130Cas) pathway, it is likely that isoforms 2 and 3 connect to different downstream cascades. It was suggested that the ability of different Dab1 isoforms to recruit distinct sets of SH2 domains implies a fine-tuning role of Dab1 splicing in the intricate series of events that underlie neuronal migration (Gao et al. (2012) (here)) (See also Katyal and Godbout (2004) (here) and Gao et al. (2010) (here)).	details	Inferred
LIG_SH2_SRC	DAB1_MOUSE	198	201	Binary	Pre‑translational	Alternative splicing removes the SH2-binding motif of Disabled homolog 1 (Dab1), abrogating binding to Neuronal proto-oncogene tyrosine-protein kinase Src (Src). Splice variants 2 and 3 (only containing one of the YQxI motifs, i.e. Y185 and Y198) exhibit decreased tyrosine phosphorylation, suggesting both motifs are required for full activation of Dab1. Dab1 is likely to recruit Neuronal proto-oncogene tyrosine-protein kinase Src (Src) via these two YQxI motifs, which subsequently phosphorylates adjacent YxVP motifs (here). This was also suggested for Phosphatidylinositol 3-kinase regulatory subunit alpha (Pik3r1) and Suppressor of cytokine signaling 2 (Socs2). Gao et al. (2012) (here) suggests that the ability of different Dab1 isoforms to recruit distinct sets of SH2 domains allows a fine-tuning role for Dab1 splicing in the intricate series of events that underlie neuronal migration (See also Katyal & Godbout (2004) (here) and Gao et al. (2010) (here)).	details	Inferred
LIG_SH2_SRC	DAB1_MOUSE	198	201	Binary	Pre‑translational	Alternative splicing removes the SH2-binding motif of Disabled homolog 1 (Dab1), abrogating binding to Neuronal proto-oncogene tyrosine-protein kinase Src (Src). Splice variants 2 and 3 (only containing one of the YQxI motifs, i.e. Y185 and Y198) exhibit decreased tyrosine phosphorylation, suggesting both motifs are required for full activation of Dab1. Dab1 is likely to recruit Neuronal proto-oncogene tyrosine-protein kinase Src (Src) via these two YQxI motifs, which subsequently phosphorylates adjacent YxVP motifs (here). This was also suggested for Phosphatidylinositol 3-kinase regulatory subunit alpha (Pik3r1) and Suppressor of cytokine signaling 2 (Socs2). Gao et al. (2012) (here) suggests that the ability of different Dab1 isoforms to recruit distinct sets of SH2 domains allows a fine-tuning role for Dab1 splicing in the intricate series of events that underlie neuronal migration (See also Katyal & Godbout (2004) (here) and Gao et al. (2010) (here)).	details	Inferred
LIG_SH2_IA	DAB1_MOUSE	232	235	Binary	Physicochemical compatibility	Phosphorylation of Y232 in the SH2-binding motif of Disabled homolog 1 (Dab1) induces binding to Cytoplasmic protein NCK2 (NCK2).	details	Inferred
LIG_SH2_IA	DAB1_MOUSE	232	235	Binary	Physicochemical compatibility	Phosphorylation of Y232 in the SH2-binding motif of Disabled homolog 1 (Dab1) induces binding to Cytoplasmic protein NCK2 (NCK2).	details	Inferred
LIG_SH2_IA	DAB1_MOUSE	232	235	Binary	Physicochemical compatibility	Phosphorylation of Y232 in the SH2-binding motif of Disabled homolog 1 (Dab1) induces binding to Cytoplasmic protein NCK2 (NCK2).	details	Inferred
LIG_SH2_IA	DAB1_MOUSE	232	235	Binary	Physicochemical compatibility	Phosphorylation of Y232 in the SH2-binding motif of Disabled homolog 1 (Dab1) induces binding to Adapter molecule crk (Crk).	details	Inferred
LIG_SH2_IA	DAB1_MOUSE	232	235	Binary	Physicochemical compatibility	Phosphorylation of Y232 in the SH2-binding motif of Disabled homolog 1 (Dab1) induces binding to Adapter molecule crk (Crk).	details	Inferred
LIG_SH2_IA	DAB1_MOUSE	232	235	Binary	Physicochemical compatibility	Phosphorylation of Y232 in the SH2-binding motif of Disabled homolog 1 (Dab1) induces binding to Adapter molecule crk (Crk).	details	Inferred
LIG_SH2_SRC	DAB1_MOUSE	198	201	Binary	Physicochemical compatibility	Phosphorylation of Y198 in the SH2-binding motif of Disabled homolog 1 (Dab1) induces binding to Neuronal proto-oncogene tyrosine-protein kinase Src (Src).	details	Inferred
LIG_SH2_SRC	DAB1_MOUSE	198	201	Binary	Physicochemical compatibility	Phosphorylation of Y198 in the SH2-binding motif of Disabled homolog 1 (Dab1) induces binding to Neuronal proto-oncogene tyrosine-protein kinase Src (Src).	details	Inferred
LIG_TYR_ITSM	OX1R_HUMAN	79	86	Avidity‑sensing		Orexin-A induced phosphorylation of the ITSM and ITIM motifs in Orexin receptor type 1 (HCRTR1) allows binding of Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) via its two SH2 domains. Mutation of either tyrosine in the motifs abolishes binding of Tyrosine-protein phosphatase non-receptor type 11 (PTPN11).	details	Inferred
LIG_TYR_ITIM	OX1R_HUMAN	356	361	Avidity‑sensing		Orexin-A induced phosphorylation of the ITSM and ITIM motifs in Orexin receptor type 1 (HCRTR1) allows binding of Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) via its two SH2 domains. Mutation of either tyrosine in the motifs abolishes binding of Tyrosine-protein phosphatase non-receptor type 11 (PTPN11).	details	Inferred
LIG_SH2_SRC	EGFR_HUMAN	1016	1019	Binary	Physicochemical compatibility	Phosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-1 (PLCG1).	details	Inferred
LIG_SH2_SRC	EGFR_HUMAN	1016	1019	Binary	Physicochemical compatibility	Phosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-1 (PLCG1).	details	Inferred
LIG_SH2_SRC	EGFR_HUMAN	1125	1128	Binary	Physicochemical compatibility	Phosphorylation of Y1125 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to Adapter molecule crk (CRK).	details	Inferred
LIG_SH2_SRC	EGFR_HUMAN	1125	1128	Binary	Physicochemical compatibility	Phosphorylation of Y1125 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to Adapter molecule crk (CRK).	details	Inferred
LIG_SH2_SRC	EGFR_HUMAN	1125	1128	Binary	Physicochemical compatibility	Phosphorylation of Y1125 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to Adapter molecule crk (CRK).	details	Inferred
LIG_SH2_SRC	EGFR_HUMAN	1125	1128	Binary	Physicochemical compatibility	Phosphorylation of Y1125 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to Adapter molecule crk (CRK).	details	Inferred
LIG_SH2_SRC	EGFR_HUMAN	1016	1019	Binary	Physicochemical compatibility	Phosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to Cytoplasmic protein NCK1 (NCK1).	details	Inferred
LIG_SH2_SRC	EGFR_HUMAN	1016	1019	Binary	Physicochemical compatibility	Phosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to Cytoplasmic protein NCK1 (NCK1).	details	Inferred
LIG_SH2_SRC	FAK1_HUMAN	397	400	Binary	Physicochemical compatibility	Phosphorylation of Y397 in the SH2-binding motif of Focal adhesion kinase 1 (PTK2) induces binding to Neuronal proto-oncogene tyrosine-protein kinase Src (Src).	details	Inferred
Proto-oncogene tyrosine-protein kinase receptor Ret - RET - Homo sapiens
LIG_SH2_IIB	RET_HUMAN	976	985	Binary	Physicochemical compatibility	Phosphorylation of Y981 in the SH2-binding motif of Proto-oncogene tyrosine-protein kinase receptor Ret (RET) induces binding to the SH2B adapter protein 1 (SH2B1) protein.	details	Inferred
LIG_SH2_IIB	RET_HUMAN	976	985	Binary	Physicochemical compatibility	Phosphorylation of Y981 in the SH2-binding motif of Proto-oncogene tyrosine-protein kinase receptor Ret (RET) induces binding to the SH2B adapter protein 1 (SH2B1) protein.	details	Inferred
LIG_SH2_IIB	RET_HUMAN	976	985	Binary	Physicochemical compatibility	Phosphorylation of Y981 in the SH2-binding motif of Proto-oncogene tyrosine-protein kinase receptor Ret (RET) induces binding to the SH2B adapter protein 1 (SH2B1) protein.	details	Inferred
Receptor tyrosine-protein kinase erbB-2 - ERBB2 - Homo sapiens
LIG_SH2_IC	ERBB2_HUMAN	1135	1144	Binary	Physicochemical compatibility	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	Inferred
LIG_SH2_IC	ERBB2_HUMAN	1135	1144	Binary	Physicochemical compatibility	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	Inferred
LIG_SH2_IE	ERBB2_HUMAN	1015	1031	Binary	Physicochemical compatibility	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	Inferred
LIG_SH2_ID	ERBB2_HUMAN	1131	1147	Binary	Physicochemical compatibility	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	Inferred
LIG_SH2_ID	ERBB2_HUMAN	1131	1147	Binary	Physicochemical compatibility	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	Inferred
LIG_SH2_ID	ERBB2_HUMAN	1015	1031	Binary	Physicochemical compatibility	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	Inferred
LIG_SH2_III	ERBB2_HUMAN	1131	1147	Binary	Physicochemical compatibility	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	Inferred
LIG_SH2_III	ERBB2_HUMAN	1131	1147	Binary	Physicochemical compatibility	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	Inferred
Receptor tyrosine-protein kinase erbB-4 - ERBB4 - Homo sapiens
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
Tyrosine-protein kinase ABL1 - ABL1 - Homo sapiens
LIG_SH2_IC	EGFR_HUMAN	1092	1100	Binary	Physicochemical compatibility	Phosphorylation of Y1092 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the Growth factor receptor-bound protein 2 (GRB2) protein.	details	Inferred
LIG_SH2_IE	EGFR_HUMAN	1008	1024	Binary	Physicochemical compatibility	Phosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the Tyrosine-protein kinase JAK2 (JAK2) protein.	details	Inferred
LIG_SH2_ID	EGFR_HUMAN	1008	1024	Binary	Physicochemical compatibility	Phosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the SH2 domain-containing protein 3C (SH2D3C) protein.	details	Inferred
LIG_SH2_ID	EGFR_HUMAN	1008	1024	Binary	Physicochemical compatibility	Phosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the SH2 domain-containing protein 3A (SH2D3A) protein.	details	Inferred
LIG_SH2_III	EGFR_HUMAN	1008	1024	Binary	Physicochemical compatibility	Phosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the Signal transducer and activator of transcription 6 (STAT6) protein.	details	Inferred
LIG_SH2_IC	MET_HUMAN	1351	1360	Binary	Physicochemical compatibility	Phosphorylation of Y1356 in the SH2-binding motif of Hepatocyte growth factor receptor (MET) induces binding to the Growth factor receptor-bound protein 2 (GRB2) protein.	details	Inferred
LIG_SH2_IA	DAB1_MOUSE	212	228	Binary	Physicochemical compatibility	Phosphorylation of Y220 in the SH2-binding motif of Disabled homolog 1 (Dab1) induces binding to the Cytoplasmic protein NCK2 (NCK2) protein.	details	Inferred
LIG_SH2_IA	DAB1_MOUSE	220	223	Binary	Pre‑translational	Alternative splicing removes the SH2-binding motif of Disabled homolog 1 (Dab1), abrogating binding to Cytoplasmic protein NCK2 (NCK2). NCK2-beta has a clear preference for splice variant 2 (with the YQYI motif) over splice variant 3 (with the YQTI motif). The authors theorise that since Adapter molecule crk (Crk) is directly linked to the C3G-Rap1 pathway, and NCK2-beta is linked to the Breast cancer anti-estrogen resistance protein 1 (Bcar1) (p130Cas) pathway, it is likely that isoforms 2 and 3 connect to different downstream cascades. It was suggested that the ability of different Dab1 isoforms to recruit distinct sets of SH2 domains implies a fine-tuning role of Dab1 splicing in the intricate series of events that underlie neuronal migration (Gao et al. (2012) (here)) (See also Katyal and Godbout (2004) (here) and Gao et al. (2010) (here)).	details	Inferred
LIG_SH2_IA	DAB1_MOUSE	232	235	Binary	Pre‑translational	Alternative splicing removes the SH2-binding motif of Disabled homolog 1 (Dab1), abrogating binding to Cytoplasmic protein NCK2 (NCK2). The NCK2-beta has a clear preference for splice variant 2 (with YQYI motif) over splice variant 3 (with YQTI motif). The authors theorise that since Adapter molecule crk (Crk) is directly linked to the C3G-Rap1 pathway, and NCK2-beta is linked to the Breast cancer anti-estrogen resistance protein 1 (Bcar1) (p130Cas) pathway, it is likely that isoforms 2 and 3 connect to different downstream cascades. It was suggested that the ability of different Dab1 isoforms to recruit distinct sets of SH2 domains implies a fine-tuning role of Dab1 splicing in the intricate series of events that underlie neuronal migration (Gao et al. (2012) (here)) (See also Katyal and Godbout (2004) (here) and Gao et al. (2010) (here)).	details	Inferred
LIG_SH2_IA	DAB1_MOUSE	220	223	Binary	Pre‑translational	Alternative splicing removes the SH2-binding motif of Disabled homolog 1 (Dab1), abrogating binding to Adapter molecule crk (Crk). Both Adapter molecule crk (Crk) and Crk-like protein (Crkl) bind equally well to variants 2 and 3. The authors theorise that since Adapter molecule crk (Crk) is directly linked to the C3G-Rap1 pathway, and NCK2-beta is linked to the Breast cancer anti-estrogen resistance protein 1 (Bcar1) (p130Cas) pathway, it is likely that isoforms 2 and 3 connect to different downstream cascades. It was suggested that the ability of different Dab1 isoforms to recruit distinct sets of SH2 domains implies a fine-tuning role of Dab1 splicing in the intricate series of events that underlie neuronal migration (Gao et al. (2012) (here)) (See also Katyal and Godbout (2004) (here) and Gao et al. (2010) (here)).	details	Inferred
LIG_SH2_IA	DAB1_MOUSE	232	235	Binary	Pre‑translational	Alternative splicing removes the SH2-binding motif of Disabled homolog 1 (Dab1), abrogating binding to Adapter molecule crk (Crk). Both Adapter molecule crk (Crk) and Crk-like protein (Crkl) bind equally well to variants 2 and 3. The authors theorise that since Adapter molecule crk (Crk) is directly linked to the C3G-Rap1 pathway, and NCK2-beta is linked to the Breast cancer anti-estrogen resistance protein 1 (Bcar1) (p130Cas) pathway, it is likely that isoforms 2 and 3 connect to different downstream cascades. It was suggested that the ability of different Dab1 isoforms to recruit distinct sets of SH2 domains implies a fine-tuning role of Dab1 splicing in the intricate series of events that underlie neuronal migration (Gao et al. (2012) (here)) (See also Katyal and Godbout (2004) (here) and Gao et al. (2010) (here)).	details	Inferred
LIG_SH2_IA	DAB1_MOUSE	232	235	Binary	Physicochemical compatibility	Phosphorylation of Y232 in the SH2-binding motif of Disabled homolog 1 (Dab1) induces binding to Cytoplasmic protein NCK2 (NCK2).	details	Inferred
LIG_SH2_IA	DAB1_MOUSE	232	235	Binary	Physicochemical compatibility	Phosphorylation of Y232 in the SH2-binding motif of Disabled homolog 1 (Dab1) induces binding to Adapter molecule crk (Crk).	details	Inferred
LIG_SH2_SRC	EGFR_HUMAN	1016	1019	Binary	Physicochemical compatibility	Phosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-1 (PLCG1).	details	Inferred
LIG_SH2_SRC	EGFR_HUMAN	1016	1019	Binary	Physicochemical compatibility	Phosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to Cytoplasmic protein NCK1 (NCK1).	details	Inferred
Tyrosine-protein kinase ABL1 - ABL1 - Mus musculus
LIG_SH2_IB	CBL_HUMAN	770	780	Binary	Physicochemical compatibility	Phosphorylation of Y774 in the SH2-binding motif of E3 ubiquitin-protein ligase CBL (CBL) induces binding to the Adapter molecule crk (CRK) protein.	details	Inferred
Tyrosine-protein kinase Blk - BLK - Homo sapiens
LIG_TYR_ITIM	FCG2B_HUMAN	290	295	Binary	Physicochemical compatibility	Phosphorylation of Y292 in the ITIM motif of Low affinity immunoglobulin gamma Fc region receptor II-b (FCGR2B) induces binding of Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 1 (INPP5D) via its SH2 domain.	details	Inferred
LIG_TYR_ITIM	FCG2B_HUMAN	290	295	Binary	Physicochemical compatibility	Phosphorylation of Y292 in the ITIM motif of Low affinity immunoglobulin gamma Fc region receptor II-b (FCGR2B) induces binding of Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 1 (INPP5D) via its SH2 domain.	details	Inferred
LIG_TYR_ITAM	FCG2A_HUMAN	285	307	Avidity‑sensing		Phosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).	details	Inferred
LIG_TYR_ITAM	FCG2A_HUMAN	285	307	Avidity‑sensing		Phosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).	details	Inferred
LIG_TYR_ITAM	FCG2A_HUMAN	285	307	Avidity‑sensing		Phosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).	details	Inferred
LIG_TYR_ITAM	FCG2A_HUMAN	285	307	Avidity‑sensing		Phosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).	details	Inferred
LIG_TYR_ITAM	FCG2A_HUMAN	285	307	Avidity‑sensing		Phosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).	details	Inferred
LIG_TYR_ITAM	FCG2A_HUMAN	285	307	Avidity‑sensing		Phosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).	details	Inferred
LIG_TYR_ITAM	FCG2A_HUMAN	285	307	Avidity‑sensing		Phosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).	details	Inferred
LIG_TYR_ITAM	FCG2A_HUMAN	285	307	Avidity‑sensing		Phosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).	details	Inferred
Tyrosine-protein kinase CSK - CSK - Homo sapiens
LIG_SH2_SRC	SRC_HUMAN	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.	details	Inferred
LIG_SH2_SRC	SRC_HUMAN	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.	details	Inferred
Tyrosine-protein kinase Fgr - FGR - Homo sapiens
LIG_SH2_IA	FAK1_HUMAN	389	405	Binary	Physicochemical compatibility	Phosphorylation of Y397 in the SH2-binding motif of Focal adhesion kinase 1 (PTK2) induces binding to the Cytoplasmic protein NCK2 (NCK2) protein.	details	Inferred
LIG_SH2_SRC	FAK1_HUMAN	397	400	Binary	Physicochemical compatibility	Phosphorylation of Y397 in the SH2-binding motif of Focal adhesion kinase 1 (PTK2) induces binding to Neuronal proto-oncogene tyrosine-protein kinase Src (Src).	details	Inferred
Tyrosine-protein kinase Fyn - FYN - Mus musculus
LIG_SH2_GRB2	IRS1_RAT	895	898	Binary	Physicochemical compatibility	Phosphorylation of Y895 in the SH2-binding motif of Insulin receptor substrate 1 (Irs1) induces binding to the Growth factor receptor-bound protein 2 (Grb2) protein.	details	Inferred
LIG_SH2_STAT5	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	Inferred
LIG_TYR_ITAM	FCG2A_HUMAN	285	307	Avidity‑sensing		Phosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).	details	Inferred
LIG_TYR_ITAM	FCG2A_HUMAN	285	307	Avidity‑sensing		Phosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).	details	Inferred
Tyrosine-protein kinase Fyn - FYN - Homo sapiens
LIG_TYR_ITIM	FCG2B_HUMAN	290	295	Binary	Physicochemical compatibility	Phosphorylation of Y292 in the ITIM motif of Low affinity immunoglobulin gamma Fc region receptor II-b (FCGR2B) induces binding of Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 1 (INPP5D) via its SH2 domain.	details	Inferred
LIG_TYR_ITSM	SLAF1_HUMAN	277	284	Binary	Physicochemical compatibility	Phosphorylation of Y281 in the ITSM motif of Signaling lymphocytic activation molecule (SLAMF1) induces binding of Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) via one of its SH2 domains.	details	Inferred
LIG_TYR_ITSM	SLAF1_HUMAN	277	284	Binary	Physicochemical compatibility	Phosphorylation of Y281 in the ITSM motif of Signaling lymphocytic activation molecule (SLAMF1) induces binding of Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) via one of its SH2 domains.	details	Inferred
LIG_TYR_ITSM	SLAF1_HUMAN	323	330	Binary	Physicochemical compatibility	Phosphorylation of Y327 in the ITSM motif of Signaling lymphocytic activation molecule (SLAMF1) induces binding of Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) via one of its SH2 domains.	details	Inferred
LIG_TYR_ITSM	SLAF1_HUMAN	323	330	Binary	Physicochemical compatibility	Phosphorylation of Y327 in the ITSM motif of Signaling lymphocytic activation molecule (SLAMF1) induces binding of Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) via one of its SH2 domains.	details	Inferred
LIG_SH2_GRB2	A4_HUMAN	757	760	Cumulative	Rheostatic	While phosphorylation of Y757 in the SH2-binding motif of Amyloid beta A4 protein (APP) induces binding to Growth factor receptor-bound protein 2 (GRB2), additional phosphorylation of T743 further increases the strength of the interaction.	details	Inferred
LIG_TYR_ITAM	CD3E_HUMAN	185	202	Specificity	Altered binding specificity	Phosphorylation of T-cell surface glycoprotein CD3 epsilon chain (CD3E) by Lck (Tyrosine-protein kinase Lck (LCK)) during T cell activation switches the specificity of CD3E from SH3 domain containing proteins like Epidermal growth factor receptor kinase substrate 8-like protein 1 (EPS8L1) to SH2 domain containing proteins like Tyrosine-protein kinase ZAP-70 (ZAP70).	details	Inferred
LIG_TYR_ITAM	CD3E_HUMAN	185	202	Specificity	Altered binding specificity	Phosphorylation of T-cell surface glycoprotein CD3 epsilon chain (CD3E) by Lck (Tyrosine-protein kinase Lck (LCK)) during T cell activation switches the specificity of CD3E from SH3 domain containing proteins like Epidermal growth factor receptor kinase substrate 8-like protein 1 (EPS8L1) to SH2 domain containing proteins like Tyrosine-protein kinase ZAP-70 (ZAP70).	details	Inferred
LIG_SH2_GRB2	A4_HUMAN	757	760	Specificity	Altered binding specificity	Phosphorylation of Y757 in APP (Amyloid beta A4 protein (APP)) switches its specificity from PTB domain containing proteins, like Amyloid beta A4 precursor protein-binding family B member 1 (APBB1), which is involved in trafficking and processing of APP, to SH2 domain containing proteins, such as Growth factor receptor-bound protein 2 (GRB2).	details	Inferred
LIG_TYR_ITAM	CD3E_HUMAN	185	202	Avidity‑sensing		Phosphorylation of Y188 and Y199 in the ITAM motif of T-cell surface glycoprotein CD3 epsilon chain (CD3E) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).	details	Inferred
LIG_TYR_ITAM	CD3E_HUMAN	185	202	Avidity‑sensing		Phosphorylation of Y188 and Y199 in the ITAM motif of T-cell surface glycoprotein CD3 epsilon chain (CD3E) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).	details	Inferred
LIG_TYR_ITAM	CD3E_HUMAN	185	202	Avidity‑sensing		Phosphorylation of Y188 and Y199 in the ITAM motif of T-cell surface glycoprotein CD3 epsilon chain (CD3E) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).	details	Inferred
LIG_TYR_ITAM	CD3E_HUMAN	185	202	Avidity‑sensing		Phosphorylation of Y188 and Y199 in the ITAM motif of T-cell surface glycoprotein CD3 epsilon chain (CD3E) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).	details	Inferred
LIG_TYR_ITAM	CD3Z_HUMAN	108	126	Avidity‑sensing		Phosphorylation of Y111 and Y123 in the ITAM motif of T-cell surface glycoprotein CD3 zeta chain (CD247) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase ZAP-70 (ZAP70).	details	Inferred
LIG_TYR_ITAM	CD3Z_HUMAN	108	126	Avidity‑sensing		Phosphorylation of Y111 and Y123 in the ITAM motif of T-cell surface glycoprotein CD3 zeta chain (CD247) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase ZAP-70 (ZAP70).	details	Inferred
LIG_TYR_ITAM	CD3Z_HUMAN	108	126	Avidity‑sensing		Phosphorylation of Y111 and Y123 in the ITAM motif of T-cell surface glycoprotein CD3 zeta chain (CD247) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase ZAP-70 (ZAP70).	details	Inferred
LIG_TYR_ITAM	CD3Z_HUMAN	108	126	Avidity‑sensing		Phosphorylation of Y111 and Y123 in the ITAM motif of T-cell surface glycoprotein CD3 zeta chain (CD247) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase ZAP-70 (ZAP70).	details	Inferred
LIG_TYR_ITAM	FCG2A_HUMAN	285	307	Avidity‑sensing		Phosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).	details	Inferred
LIG_TYR_ITAM	FCG2A_HUMAN	285	307	Avidity‑sensing		Phosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).	details	Inferred
LIG_TYR_ITAM	FCG2A_HUMAN	285	307	Avidity‑sensing		Phosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).	details	Inferred
LIG_TYR_ITAM	FCG2A_HUMAN	285	307	Avidity‑sensing		Phosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).	details	Inferred
LIG_TYR_ITAM	FCG2A_HUMAN	285	307	Avidity‑sensing		Phosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).	details	Inferred
LIG_TYR_ITAM	FCG2A_HUMAN	285	307	Avidity‑sensing		Phosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).	details	Inferred
LIG_SH2_IB	CBL_HUMAN	770	780	Binary	Physicochemical compatibility	Phosphorylation of Y774 in the SH2-binding motif of E3 ubiquitin-protein ligase CBL (CBL) induces binding to the Adapter molecule crk (CRK) protein.	details	Inferred
LIG_SH2_IB	CBL_HUMAN	770	780	Binary	Physicochemical compatibility	Phosphorylation of Y774 in the SH2-binding motif of E3 ubiquitin-protein ligase CBL (CBL) induces binding to the Adapter molecule crk (CRK) protein.	details	Inferred
LIG_SH2_IB	SLAF1_HUMAN	276	286	Binary	Physicochemical compatibility	Phosphorylation of Y281 in the SH2-binding motif of Signaling lymphocytic activation molecule (SLAMF1) induces binding to the SH2 domain-containing protein 1A (SH2D1A) protein.	details	Inferred
LIG_SH2_IB	SLAF1_HUMAN	276	286	Binary	Physicochemical compatibility	Phosphorylation of Y281 in the SH2-binding motif of Signaling lymphocytic activation molecule (SLAMF1) induces binding to the SH2 domain-containing protein 1A (SH2D1A) protein.	details	Inferred
LIG_SH2_IB	SLAF1_HUMAN	273	286	Binary	Physicochemical compatibility	Phosphorylation of Y281 in the SH2-binding motif of Signaling lymphocytic activation molecule (SLAMF1) induces binding to the SH2 domain-containing protein 1B (Sh2d1b) protein.	details	Inferred
LIG_SH2_IB	SLAF1_HUMAN	273	286	Binary	Physicochemical compatibility	Phosphorylation of Y281 in the SH2-binding motif of Signaling lymphocytic activation molecule (SLAMF1) induces binding to the SH2 domain-containing protein 1B (Sh2d1b) protein.	details	Inferred
Tyrosine-protein kinase JAK1 - JAK1 - Homo sapiens
LIG_SH2_III	INGR1_HUMAN	457	461	Binary	Physicochemical compatibility	Phosphorylation of Y457 in the SH2-binding motif of Interferon gamma receptor 1 (IFNGR1) induces binding to the Signal transducer and activator of transcription 1-alpha/beta (STAT1) protein.	details	Inferred
Tyrosine-protein kinase JAK2 - JAK2 - Homo sapiens
LIG_SH2_STAT5	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	Inferred
LIG_SH2_STAT5	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	Inferred
LIG_SH2_III	EPOR_HUMAN	360	376	Binary	Physicochemical compatibility	Phosphorylation of Y368 in the SH2-binding motif of Erythropoietin receptor (EPOR) induces binding to the Signal transducer and activator of transcription 5B (STAT5B) protein.	details	Inferred
LIG_SH2_III	JAK2_MOUSE	804	820	Binary	Physicochemical compatibility	Phosphorylation of Y813 in the SH2-binding motif of Tyrosine-protein kinase JAK2 (Jak2) induces binding to the Signal transducer and activator of transcription 5B (Stat5b) protein.	details	Inferred
LIG_SH2_III	STA5A_HUMAN	686	702	Binary	Physicochemical compatibility	Phosphorylation of Y694 in the SH2-binding motif of Signal transducer and activator of transcription 5A (STAT5A) induces binding to the Signal transducer and activator of transcription 5B (STAT5B) protein.	details	Inferred
LIG_SH2_III	STA5A_HUMAN	686	702	Binary	Physicochemical compatibility	Phosphorylation of Y694 in the SH2-binding motif of Signal transducer and activator of transcription 5A (STAT5A) induces binding to the Signal transducer and activator of transcription 5B (STAT5B) protein.	details	Inferred
Tyrosine-protein kinase JAK2 - JAK2 - Mus musculus
LIG_SH2_III	JAK2_MOUSE	804	820	Binary	Physicochemical compatibility	Phosphorylation of Y813 in the SH2-binding motif of Tyrosine-protein kinase JAK2 (Jak2) induces binding to the Signal transducer and activator of transcription 5B (Stat5b) protein.	details	Inferred
Tyrosine-protein kinase JAK3 - JAK3 - Homo sapiens
LIG_SH2_III	STA5A_HUMAN	686	702	Binary	Physicochemical compatibility	Phosphorylation of Y694 in the SH2-binding motif of Signal transducer and activator of transcription 5A (STAT5A) induces binding to the Signal transducer and activator of transcription 5B (STAT5B) protein.	details	Inferred
Tyrosine-protein kinase Lck - LCK - Homo sapiens
LIG_SH2_STAT5	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	Inferred
LIG_TYR_ITAM	CD3Z_HUMAN	139	156	Avidity‑sensing		Phosphorylation of Y142 and Y153 in the ITAM motif of T-cell surface glycoprotein CD3 zeta chain (CD247) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase ZAP-70 (ZAP70).	details	Inferred
LIG_TYR_ITAM	CD3Z_HUMAN	139	156	Avidity‑sensing		Phosphorylation of Y142 and Y153 in the ITAM motif of T-cell surface glycoprotein CD3 zeta chain (CD247) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase ZAP-70 (ZAP70).	details	Inferred
LIG_SH2_IA	IL2RB_HUMAN	409	428	Binary	Physicochemical compatibility	Phosphorylation of Y418 in the SH2-binding motif of Interleukin-2 receptor subunit beta (IL2RB) induces binding to the Tyrosine-protein kinase Lck (LCK) protein.	details	Inferred
LIG_SH2_IA	IL2RB_HUMAN	409	428	Binary	Physicochemical compatibility	Phosphorylation of Y418 in the SH2-binding motif of Interleukin-2 receptor subunit beta (IL2RB) induces binding to the Tyrosine-protein kinase Lck (LCK) protein.	details	Inferred
LIG_SH2_III	IL2RB_HUMAN	531	540	Binary	Physicochemical compatibility	Phosphorylation of Y536 in the SH2-binding motif of Interleukin-2 receptor subunit beta (IL2RB) induces binding to the Signal transducer and activator of transcription 5A (STAT5A) protein.	details	Inferred
LIG_SH2_III	IL2RB_HUMAN	531	540	Binary	Physicochemical compatibility	Phosphorylation of Y536 in the SH2-binding motif of Interleukin-2 receptor subunit beta (IL2RB) induces binding to the Signal transducer and activator of transcription 5A (STAT5A) protein.	details	Inferred
LIG_SH2_III	IL2RB_HUMAN	528	544	Binary	Physicochemical compatibility	Phosphorylation of Y536 in the SH2-binding motif of Interleukin-2 receptor subunit beta (IL2RB) induces binding to the Signal transducer and activator of transcription 5B (STAT5B) protein.	details	Inferred
LIG_SH2_III	IL2RB_HUMAN	528	544	Binary	Physicochemical compatibility	Phosphorylation of Y536 in the SH2-binding motif of Interleukin-2 receptor subunit beta (IL2RB) induces binding to the Signal transducer and activator of transcription 5B (STAT5B) protein.	details	Inferred
LIG_SH2_IIB	VAV_HUMAN	165	180	Binary	Physicochemical compatibility	Phosphorylation of Y174 in the SH2-binding motif of Proto-oncogene vav (VAV1) induces binding to the SH2 domain-containing adapter protein B (SHB) protein.	details	Inferred
LIG_SH2_IB	CBL_HUMAN	770	780	Binary	Physicochemical compatibility	Phosphorylation of Y774 in the SH2-binding motif of E3 ubiquitin-protein ligase CBL (CBL) induces binding to the Adapter molecule crk (CRK) protein.	details	Inferred
LIG_SH2_IIB	LCP2_HUMAN	105	118	Binary	Physicochemical compatibility	Phosphorylation of Y113 in the SH2-binding motif of Lymphocyte cytosolic protein 2 (LCP2) induces binding to the SH2 domain-containing adapter protein B (SHB) protein.	details	Inferred
LIG_SH2_IIB	LCP2_HUMAN	105	118	Binary	Physicochemical compatibility	Phosphorylation of Y113 in the SH2-binding motif of Lymphocyte cytosolic protein 2 (LCP2) induces binding to the SH2 domain-containing adapter protein B (SHB) protein.	details	Inferred
LIG_SH2_IIB	LCP2_HUMAN	120	133	Binary	Physicochemical compatibility	Phosphorylation of Y128 in the SH2-binding motif of Lymphocyte cytosolic protein 2 (LCP2) induces binding to the SH2 domain-containing adapter protein B (SHB) protein.	details	Inferred
LIG_SH2_IIB	LCP2_HUMAN	120	133	Binary	Physicochemical compatibility	Phosphorylation of Y128 in the SH2-binding motif of Lymphocyte cytosolic protein 2 (LCP2) induces binding to the SH2 domain-containing adapter protein B (SHB) protein.	details	Inferred
LIG_SH2_IIB	LCP2_HUMAN	137	150	Binary	Physicochemical compatibility	Phosphorylation of Y145 in the SH2-binding motif of Lymphocyte cytosolic protein 2 (LCP2) induces binding to the SH2 domain-containing adapter protein B (SHB) protein.	details	Inferred
LIG_SH2_III	STA5A_HUMAN	686	702	Binary	Physicochemical compatibility	Phosphorylation of Y694 in the SH2-binding motif of Signal transducer and activator of transcription 5A (STAT5A) induces binding to the Signal transducer and activator of transcription 5B (STAT5B) protein.	details	Inferred
Tyrosine-protein kinase Lyn - LYN - Homo sapiens
LIG_TYR_ITIM	FCG2B_HUMAN	290	295	Binary	Physicochemical compatibility	Phosphorylation of Y292 in the ITIM motif of Low affinity immunoglobulin gamma Fc region receptor II-b (FCGR2B) induces binding of Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 1 (INPP5D) via its SH2 domain.	details	Inferred
LIG_TYR_ITIM	FCG2B_HUMAN	290	295	Binary	Physicochemical compatibility	Phosphorylation of Y292 in the ITIM motif of Low affinity immunoglobulin gamma Fc region receptor II-b (FCGR2B) induces binding of Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 1 (INPP5D) via its SH2 domain.	details	Inferred
LIG_TYR_ITSM	SLAF1_HUMAN	323	330	Binary	Physicochemical compatibility	Phosphorylation of Y327 in the ITSM motif of Signaling lymphocytic activation molecule (SLAMF1) induces binding of Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) via one of its SH2 domains.	details	Inferred
LIG_TYR_ITSM	SLAF1_HUMAN	323	330	Binary	Physicochemical compatibility	Phosphorylation of Y327 in the ITSM motif of Signaling lymphocytic activation molecule (SLAMF1) induces binding of Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) via one of its SH2 domains.	details	Inferred
LIG_TYR_ITAM	FCG2A_HUMAN	285	307	Avidity‑sensing		Phosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).	details	Inferred
LIG_TYR_ITAM	FCG2A_HUMAN	285	307	Avidity‑sensing		Phosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).	details	Inferred
LIG_TYR_ITAM	FCG2A_HUMAN	285	307	Avidity‑sensing		Phosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).	details	Inferred
LIG_TYR_ITAM	FCG2A_HUMAN	285	307	Avidity‑sensing		Phosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).	details	Inferred
LIG_TYR_ITAM	FCG2A_HUMAN	285	307	Avidity‑sensing		Phosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).	details	Inferred
LIG_TYR_ITAM	FCG2A_HUMAN	285	307	Avidity‑sensing		Phosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).	details	Inferred
LIG_SH2_III	EPOR_HUMAN	360	376	Binary	Physicochemical compatibility	Phosphorylation of Y368 in the SH2-binding motif of Erythropoietin receptor (EPOR) induces binding to the Signal transducer and activator of transcription 5B (STAT5B) protein.	details	Inferred
LIG_SH2_III	STA5A_HUMAN	686	702	Binary	Physicochemical compatibility	Phosphorylation of Y694 in the SH2-binding motif of Signal transducer and activator of transcription 5A (STAT5A) induces binding to the Signal transducer and activator of transcription 5B (STAT5B) protein.	details	Inferred
Tyrosine-protein kinase Lyn - LYN - Mus musculus
LIG_TYR_ITAM	FCG2A_HUMAN	285	307	Avidity‑sensing		Phosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).	details	Inferred
LIG_TYR_ITAM	FCG2A_HUMAN	285	307	Avidity‑sensing		Phosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).	details	Inferred
LIG_SH2_III	STA5A_HUMAN	686	702	Binary	Physicochemical compatibility	Phosphorylation of Y694 in the SH2-binding motif of Signal transducer and activator of transcription 5A (STAT5A) induces binding to the Signal transducer and activator of transcription 5B (STAT5B) protein.	details	Inferred
Tyrosine-protein kinase SYK - SYK - Homo sapiens
LIG_TYR_ITAM	FCG2A_HUMAN	285	307	Avidity‑sensing		Phosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).	details	Inferred
LIG_TYR_ITAM	FCG2A_HUMAN	285	307	Avidity‑sensing		Phosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).	details	Inferred
LIG_TYR_ITAM	FCG2A_HUMAN	285	307	Avidity‑sensing		Phosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).	details	Inferred
LIG_TYR_ITAM	FCG2A_HUMAN	285	307	Avidity‑sensing		Phosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).	details	Inferred
LIG_TYR_ITAM	FCG2A_HUMAN	285	307	Avidity‑sensing		Phosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).	details	Inferred
LIG_TYR_ITAM	FCG2A_HUMAN	285	307	Avidity‑sensing		Phosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).	details	Inferred
LIG_SH2_IB	CBL_HUMAN	770	780	Binary	Physicochemical compatibility	Phosphorylation of Y774 in the SH2-binding motif of E3 ubiquitin-protein ligase CBL (CBL) induces binding to the Adapter molecule crk (CRK) protein.	details	Inferred
LIG_SH2_IB	CBL_HUMAN	770	780	Binary	Physicochemical compatibility	Phosphorylation of Y774 in the SH2-binding motif of E3 ubiquitin-protein ligase CBL (CBL) induces binding to the Adapter molecule crk (CRK) protein.	details	Inferred
LIG_SH2_IC	SHC1_HUMAN	423	435	Binary	Physicochemical compatibility	Phosphorylation of Y427 in the SH2-binding motif of SHC-transforming protein 1 (SHC1) induces binding to the Growth factor receptor-bound protein 2 (GRB2) protein.	details	Inferred
LIG_SH2_IIB	M4K1_HUMAN	372	391	Binary	Physicochemical compatibility	Phosphorylation of Y381 in the SH2-binding motif of Mitogen-activated protein kinase kinase kinase kinase 1 (MAP4K1) induces binding to the B-cell linker protein (BLNK) protein.	details	Inferred
LIG_SH2_IIB	LCP2_HUMAN	105	118	Binary	Physicochemical compatibility	Phosphorylation of Y113 in the SH2-binding motif of Lymphocyte cytosolic protein 2 (LCP2) induces binding to the SH2 domain-containing adapter protein B (SHB) protein.	details	Inferred
LIG_SH2_IIB	LCP2_HUMAN	105	118	Binary	Physicochemical compatibility	Phosphorylation of Y113 in the SH2-binding motif of Lymphocyte cytosolic protein 2 (LCP2) induces binding to the SH2 domain-containing adapter protein B (SHB) protein.	details	Inferred
LIG_SH2_IIB	LCP2_HUMAN	120	133	Binary	Physicochemical compatibility	Phosphorylation of Y128 in the SH2-binding motif of Lymphocyte cytosolic protein 2 (LCP2) induces binding to the SH2 domain-containing adapter protein B (SHB) protein.	details	Inferred
LIG_SH2_IIB	LCP2_HUMAN	120	133	Binary	Physicochemical compatibility	Phosphorylation of Y128 in the SH2-binding motif of Lymphocyte cytosolic protein 2 (LCP2) induces binding to the SH2 domain-containing adapter protein B (SHB) protein.	details	Inferred
LIG_SH2_IB	FAK2_HUMAN	394	410	Binary	Physicochemical compatibility	Phosphorylation of Y402 in the SH2-binding motif of Protein-tyrosine kinase 2-beta (PTK2B) induces binding to the Megakaryocyte-associated tyrosine-protein kinase (MATK) protein.	details	Inferred
LIG_SH2_III	STA5A_HUMAN	686	702	Binary	Physicochemical compatibility	Phosphorylation of Y694 in the SH2-binding motif of Signal transducer and activator of transcription 5A (STAT5A) induces binding to the Signal transducer and activator of transcription 5B (STAT5B) protein.	details	Inferred
Tyrosine-protein kinase TXK - TXK - Homo sapiens
LIG_SH2_IIB	LCP2_HUMAN	137	150	Binary	Physicochemical compatibility	Phosphorylation of Y145 in the SH2-binding motif of Lymphocyte cytosolic protein 2 (LCP2) induces binding to the SH2 domain-containing adapter protein B (SHB) protein.	details	Inferred
Tyrosine-protein kinase Yes - YES1 - Homo sapiens
LIG_SH2_IB	CBL_HUMAN	770	780	Binary	Physicochemical compatibility	Phosphorylation of Y774 in the SH2-binding motif of E3 ubiquitin-protein ligase CBL (CBL) induces binding to the Adapter molecule crk (CRK) protein.	details	Inferred
Tyrosine-protein kinase ZAP-70 - ZAP70 - Mus musculus
LIG_SH2_GRB2	LAT_MOUSE	175	178	Binary	Physicochemical compatibility	Phosphorylation of Y175 in the SH2-binding motif of Linker for activation of T-cells family member 1 (Lat) induces binding to the Growth factor receptor-bound protein 2 (Grb2) protein.	details	Inferred
LIG_SH2_GRB2	LAT_MOUSE	195	198	Binary	Physicochemical compatibility	Phosphorylation of Y195 in the SH2-binding motif of Linker for activation of T-cells family member 1 (Lat) induces binding to the Growth factor receptor-bound protein 2 (Grb2) protein.	details	Inferred
LIG_SH2_GRB2	LAT_MOUSE	235	238	Binary	Physicochemical compatibility	Phosphorylation of Y235 in the SH2-binding motif of Linker for activation of T-cells family member 1 (Lat) induces binding to the Growth factor receptor-bound protein 2 (Grb2) protein.	details	Inferred
Tyrosine-protein kinase ZAP-70 - ZAP70 - Homo sapiens
LIG_SH2_GRB2	LAT_MOUSE	175	178	Binary	Physicochemical compatibility	Phosphorylation of Y175 in the SH2-binding motif of Linker for activation of T-cells family member 1 (Lat) induces binding to the Growth factor receptor-bound protein 2 (Grb2) protein.	details	Inferred
LIG_SH2_GRB2	LAT_MOUSE	195	198	Binary	Physicochemical compatibility	Phosphorylation of Y195 in the SH2-binding motif of Linker for activation of T-cells family member 1 (Lat) induces binding to the Growth factor receptor-bound protein 2 (Grb2) protein.	details	Inferred
LIG_SH2_GRB2	LAT_MOUSE	235	238	Binary	Physicochemical compatibility	Phosphorylation of Y235 in the SH2-binding motif of Linker for activation of T-cells family member 1 (Lat) induces binding to the Growth factor receptor-bound protein 2 (Grb2) protein.	details	Inferred
LIG_SH2_IC	SHC1_HUMAN	423	435	Binary	Physicochemical compatibility	Phosphorylation of Y427 in the SH2-binding motif of SHC-transforming protein 1 (SHC1) induces binding to the Growth factor receptor-bound protein 2 (GRB2) protein.	details	Inferred
LIG_SH2_IIB	LCP2_HUMAN	105	118	Binary	Physicochemical compatibility	Phosphorylation of Y113 in the SH2-binding motif of Lymphocyte cytosolic protein 2 (LCP2) induces binding to the SH2 domain-containing adapter protein B (SHB) protein.	details	Inferred
LIG_SH2_IIB	LCP2_HUMAN	105	118	Binary	Physicochemical compatibility	Phosphorylation of Y113 in the SH2-binding motif of Lymphocyte cytosolic protein 2 (LCP2) induces binding to the SH2 domain-containing adapter protein B (SHB) protein.	details	Inferred
LIG_SH2_IIB	LCP2_HUMAN	105	118	Binary	Physicochemical compatibility	Phosphorylation of Y113 in the SH2-binding motif of Lymphocyte cytosolic protein 2 (LCP2) induces binding to the SH2 domain-containing adapter protein B (SHB) protein.	details	Inferred
LIG_SH2_IIB	LCP2_HUMAN	105	118	Binary	Physicochemical compatibility	Phosphorylation of Y113 in the SH2-binding motif of Lymphocyte cytosolic protein 2 (LCP2) induces binding to the SH2 domain-containing adapter protein B (SHB) protein.	details	Inferred
LIG_SH2_IIB	LCP2_HUMAN	120	133	Binary	Physicochemical compatibility	Phosphorylation of Y128 in the SH2-binding motif of Lymphocyte cytosolic protein 2 (LCP2) induces binding to the SH2 domain-containing adapter protein B (SHB) protein.	details	Inferred
LIG_SH2_IIB	LCP2_HUMAN	120	133	Binary	Physicochemical compatibility	Phosphorylation of Y128 in the SH2-binding motif of Lymphocyte cytosolic protein 2 (LCP2) induces binding to the SH2 domain-containing adapter protein B (SHB) protein.	details	Inferred
LIG_SH2_IIB	LCP2_HUMAN	120	133	Binary	Physicochemical compatibility	Phosphorylation of Y128 in the SH2-binding motif of Lymphocyte cytosolic protein 2 (LCP2) induces binding to the SH2 domain-containing adapter protein B (SHB) protein.	details	Inferred
LIG_SH2_IIB	LCP2_HUMAN	120	133	Binary	Physicochemical compatibility	Phosphorylation of Y128 in the SH2-binding motif of Lymphocyte cytosolic protein 2 (LCP2) induces binding to the SH2 domain-containing adapter protein B (SHB) protein.	details	Inferred
LIG_SH2_IIB	LCP2_HUMAN	137	150	Binary	Physicochemical compatibility	Phosphorylation of Y145 in the SH2-binding motif of Lymphocyte cytosolic protein 2 (LCP2) induces binding to the SH2 domain-containing adapter protein B (SHB) protein.	details	Inferred
LIG_SH2_IIB	LCP2_HUMAN	137	150	Binary	Physicochemical compatibility	Phosphorylation of Y145 in the SH2-binding motif of Lymphocyte cytosolic protein 2 (LCP2) induces binding to the SH2 domain-containing adapter protein B (SHB) protein.	details	Inferred
Vascular endothelial growth factor receptor 3 - FLT4 - Homo sapiens
LIG_SH2_IC	SHC1_HUMAN	423	435	Binary	Physicochemical compatibility	Phosphorylation of Y427 in the SH2-binding motif of SHC-transforming protein 1 (SHC1) induces binding to the Growth factor receptor-bound protein 2 (GRB2) protein.	details	Inferred