DEPOD - human DEPhOsphorylation Database

Basic Information
Phosphatases
Pathway
Interacting Proteins
Phosphorylating Kinases

Gene Name	LAT (QuickGO)	Interactive visualization of LAT structures (A quick tutorial to explore the interctive visulaization) Representative structure: NA
Synonyms	LAT
Protein Name	LAT
Alternative Name(s)	Linker for activation of T-cells family member 1;36 kDa phospho-tyrosine adapter protein;pp36;p36-38;
Protein Family	noSimilarity_annotations
EntrezGene ID	27040 (Comparitive Toxicogenomics)
UniProt AC (Human)	O43561 (protein sequence)
Enzyme Class	N/A
Molecular Weight	27930 Dalton
Protein Length	262 amino acids (AA)
Genome Browsers	NCBI \| ENSG00000213658 (Ensembl) \| UCSC
Crosslinking annotations	Query our ID-mapping table
Orthologues	Quest For Orthologues (QFO) \| GeneTree
Phosphorylation Network	Visualize

Domain organization, Expression, Diseases

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Localization, Function, Catalytic activity and Sequence

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Motif information from Eukaryotic Linear Motif atlas (ELM)

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Gene Ontology (P: Process; F: Function and C: Component terms)

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KEGG Pathway
Reactome Pathway

Pathway ID	Pathway Name	Pathway Description (KEGG)
hsa04014	Ras signaling pathway	The Ras proteins are GTPases that function as molecular switches for signaling pathways regulating cell proliferation, survival, growth, migration, differentiation or cytoskeletal dynamism. Ras proteins transduce signals from extracellular growth factors by cycling between inactive GDP-bound and active GTP-bound states. The exchange of GTP for GDP on RAS is regulated by guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs). Activated RAS (RAS-GTP) regulates multiple cellular functions through effectors including Raf, phosphatidylinositol 3-kinase (PI3K) and Ral guanine nucleotide-dissociation stimulator (RALGDS).
hsa04015	Rap1 signaling pathway	Rap1 is a small GTPase that controls diverse processes, such as cell adhesion, cell-cell junction formation and cell polarity. Like all G proteins, Rap1 cycles between an inactive GDP-bound and an active GTP-bound conformation. A variety of extracellular signals control this cycle through the regulation of several unique guanine nucleotide exchange factors (GEFs) and GTPase activating proteins (GAPs). Rap1 plays a dominant role in the control of cell-cell and cell-matrix interactions by regulating the function of integrins and other adhesion molecules in various cell types. Rap1 also regulates MAP kinase (MAPK) activity in a manner highly dependent on the context of cell types.
hsa04064	NF-kappa B signaling pathway	Nuclear factor-kappa B (NF-kappa B) is the generic name of a family of transcription factors that function as dimers and regulate genes involved in immunity, inflammation and cell survival. There are several pathways leading to NF-kappa B-activation. The canonical pathway is induced by tumour necrosis factor-alpha (TNF-alpha), interleukin-1 (IL-1) or byproducts of bacterial and viral infections. This pathway relies on IKK- mediated IkappaB-alpha phosphorylation on Ser32 and 36, leading to its degradation, which allows the p50/p65 NF-kappa B dimer to enter the nucleus and activate gene transcription. Atypical pathways are IKK-independent and rely on phosphorylation of IkappaB-alpha on Tyr42 or on Ser residues in IkappaB-alpha PEST domain. The non-canonical pathway is triggered by particular members of the TNFR superfamily, such as lymphotoxin-beta (LT-beta) or BAFF. It involves NIK and IKK-alpha-mediated p100 phosphorylation and processing to p52, resulting in nuclear translocation of p52/RelB heterodimers.
hsa04650	Natural killer cell mediated cytotoxicity	Natural killer (NK) cells are lymphocytes of the innate immune system that are involved in early defenses against both allogeneic (nonself) cells and autologous cells undergoing various forms of stress, such as infection with viruses, bacteria, or parasites or malignant transformation. Although NK cells do not express classical antigen receptors of the immunoglobulin gene family, such as the antibodies produced by B cells or the T cell receptor expressed by T cells, they are equipped with various receptors whose engagement allows them to discriminate between target and nontarget cells. Activating receptors bind ligands on the target cell surface and trigger NK cell activation and target cell lysis. However Inhibitory receptors recognize MHC class I molecules (HLA) and inhibit killing by NK cells by overruling the actions of the activating receptors. This inhibitory signal is lost when the target cells do not express MHC class I and perhaps also in cells infected with virus, which might inhibit MHC class I exprssion or alter its conformation. The mechanism of NK cell killing is the same as that used by the cytotoxic T cells generated in an adaptive immune response; cytotoxic granules are released onto the surface of the bound target cell, and the effector proteins they contain penetrate the cell membrane and induce programmed cell death.
hsa04658	Th1 and Th2 cell differentiation	Immunity to different classes of microorganisms is orchestrated by separate lineages of effector T helper (TH)-cells, which differentiate from naive CD4+ precursor cells in response to cues provided by antigen presenting cells (APC) and include T helper type 1 (Th1) and Th2. Th1 cells are characterized by the transcription factor T-bet and signal transducer and activator of transcription (STAT) 4, and the production of IFN-gamma. These cells stimulate strong cell-mediated immune responses, particularly against intracellular pathogens. On the other hand, transcription factors like GATA-3 and STAT6 drive the generation of Th2 cells that produce IL-4, IL-5 and IL-13 and are necessary for inducing the humoral response to combat parasitic helminths (type 2 immunity) and isotype switching to IgG1 and IgE. The balance between Th1/Th2 subsets determines the susceptibility to disease states, where the improper development of Th2 cells can lead to allergy, while an overactive Th1 response can lead to autoimmunity.
hsa04659	Th17 cell differentiation	Interleukin (IL)-17-producing helper T (Th17) cells serve as a subset of CD4+ T cells involved in epithelial cell- and neutrophil mediated immune responses against extracellular microbes and in the pathogenesis of autoimmune diseases. In vivo, Th17 differentiation requires antigen presentation and co-stimulation, and activation of antigen presenting-cells (APCs) to produce TGF-beta, IL-6, IL-1, IL-23 and IL-21. This initial activation results in the activation and up-regulation of STAT3, ROR(gamma)t and other transcriptional factors in CD4+ T cells, which bind to the promoter regions of the IL-17, IL-21 and IL-22 genes and induce IL-17, IL-21 and IL-22. In contrast, the differentiation of Th17 cells and their IL-17 expression are negatively regulated by IL-2, Th2 cytokine IL-4, IL-27 and Th1 cytokine IFN-gamma through STAT5, STAT6 and STAT1 activation, respectively. Retinoid acid and the combination of IL-2 and TGF-beta upregulate Foxp3, which also downregulates cytokines like IL-17 and IL-21. The inhibition of Th17 differentiation may serve as a protective strategy to 'fine-tune' the expression IL-17 so it does not cause excessive inflammation. Thus, balanced differentiation of Th cells is crucial for immunity and host protection.
hsa04660	T cell receptor signaling pathway	Activation of T lymphocytes is a key event for an efficient response of the immune system. It requires the involvement of the T-cell receptor (TCR) as well as costimulatory molecules such as CD28. Engagement of these receptors through the interaction with a foreign antigen associated with major histocompatibility complex molecules and CD28 counter-receptors B7.1/B7.2, respectively, results in a series of signaling cascades. These cascades comprise an array of protein-tyrosine kinases, phosphatases, GTP-binding proteins and adaptor proteins that regulate generic and specialised functions, leading to T-cell proliferation, cytokine production and differentiation into effector cells.
hsa04664	Fc epsilon RI signaling pathway	Fc epsilon RI-mediated signaling pathways in mast cells are initiated by the interaction of antigen (Ag) with IgE bound to the extracellular domain of the alpha chain of Fc epsilon RI. The activation pathways are regulated both positively and negatively by the interactions of numerous signaling molecules. Mast cells that are thus activated release preformed granules which contain biogenic amines (especially histamines) and proteoglycans (especially heparin). The activation of phospholipase A2 causes the release of membrane lipids followed by development of lipid mediators such as leukotrienes (LTC4, LTD4 and LTE4) and prostaglandins (especially PDG2). There is also secretion of cytokines, the most important of which are TNF-alpha, IL-4 and IL-5. These mediators and cytokines contribute to inflammatory responses.
hsa04666	Fc gamma R-mediated phagocytosis	Phagocytosis plays an essential role in host-defense mechanisms through the uptake and destruction of infectious pathogens. Specialized cell types including macrophages, neutrophils, and monocytes take part in this process in higher organisms. After opsonization with antibodies (IgG), foreign extracellular materials are recognized by Fc gamma receptors. Cross-linking of Fc gamma receptors initiates a variety of signals mediated by tyrosine phosphorylation of multiple proteins, which lead through the actin cytoskeleton rearrangements and membrane remodeling to the formation of phagosomes. Nascent phagosomes undergo a process of maturation that involves fusion with lysosomes. The acquisition of lysosomal proteases and release of reactive oxygen species are crucial for digestion of engulfed materials in phagosomes.

Pathway ID	Pathway Name	Pathway Description (KEGG)
R-HSA-114604	GPVI-mediated activation cascade.	The GPVI receptor is a complex of the GPVI protein with Fc epsilon R1 gamma (FcR). The Src family kinases Fyn and Lyn constitutively associate with the GPVI-FcR complex in platelets and initiate platelet activation through phosphorylation of the immunoreceptor tyrosine-based activation motif (ITAM) in the FcR gamma chain, leading to binding and activation of the tyrosine kinase Syk. Downstream of Syk, a series of adapter molecules and effectors lead to platelet activation. The GPVI receptor signaling cascade is similar to that of T- and B-cell immune receptors, involving the formation of a signalosome composed of adapter and effector proteins. At the core of the T-cell receptor signalosome is the transmembrane adapter LAT and two cytosolic adapters SLP-76 and Gads. While LAT is essential for signalling to PLCgamma1 downstream of the T-cell receptor, the absence of LAT in platelets only impairs the activation of PLCgamma2, the response to collagen and GPVI receptor ligands remains sufficient to elicit a full aggregation response. In contrast, GPVI signalling is almost entirely abolished in the absence of SLP-76
R-HSA-202433	Generation of second messenger molecules.	In addition to serving as a scaffold via auto-phosphorylation, ZAP-70 also phosphorylates a restricted set of substrates following TCR stimulation - including LAT and SLP-76. These substrates have been recognized to play pivotal role in TCR signaling by releasing second messengers. When phosphorylated, LAT and SLP-76 act as adaptor proteins which serve as nucleation points for the construction of a higher order signalosome: GADS, PLC-gamma1 and GRB2 bind to the LAT on the phosphorylated tyrosine residues (steps 8 and 13). SLP-76 and SOS are then moved to the signalosome by interacting with the SH3 domains of GRB2 and GADS via their proline rich sequences (step 9). Three SLP-76 acidic domain N-term tyrosine residues are phosphorylated by ZAP-70, once SLP-76 binds to GADS (step 10). These phospho-tyrosine residues act as binding sites to the SH2 domains of PLC-gamma1, Vav and Itk (steps 11 and 12). PLC-gamma1 is activated by dual phosphorylation on the tyrosine residues at positions 771, 783 and 1254 by Itk and ZAP-70 (step 14). Phosphorylated PLC-gamma1 subsequently detaches from LAT and SLP-76 and translocates to the plasma membrane by binding to phosphatidylinositol-4,5-bisphosphate (PIP2) via its PH domain (step 15). PLC-gamma1 goes on to hydrolyse PIP2 to second messengers DAG and IP3. These second messengers are involved in PKC and NF-kB activation and calcium mobilization (step 16)
R-HSA-2424491	DAP12 signaling.	In response to receptor ligation, the tyrosine residues in DAP12's immunoreceptor tyrosine-based activation motif (ITAM) are phosphorylated by Src family kinases. These phosphotyrosines form the docking site for the protein tyrosine kinase SYK in myeloid cells and SYK and ZAP70 in NK cells. DAP12-bound SYK autophosphorylates and phosphorylates the scaffolding molecule LAT, recruiting the proximal signaling molecules phosphatidylinositol-3-OH kinase (PI3K), phospholipase-C gamma (PLC-gamma), GADS (GRB2-related adapter downstream of SHC), SLP76 (SH2 domain-containing leukocyte protein of 76 kDa), GRB2:SOS (Growth factor receptor-bound protein 2:Son of sevenless homolog 1) and VAV. All of these intermediate signalling molecules result in the recruitment and activation of kinases AKT, CBL (Casitas B-lineage lymphoma) and ERK (extracellular signal-regulated kinase), and rearrangement of the actin cytoskeleton (actin polymerization) finally leading to cellular activation. PLC-gamma generates the secondary messengers diacylglycerol (DAG) and inositol-1,4,5-trisphosphate (InsP3), leading to activation of protein kinase C (PKC) and calcium mobilization, respectively (Turnbull & Colonna 2007, Klesney-Tait et al. 2006)
R-HSA-2454202	Fc epsilon receptor (FCERI) signaling.	Mast cells (MC) are distributed in tissues throughout the human body and have long been recognized as key cells of type I hypersensitivity reactions. They also play important roles in inflammatory and immediate allergic reactions. Activation through FCERI-bound antigen-specific IgE causes release of potent inflammatory mediators, such as histamine, proteases, chemotactic factors, cytokines and metabolites of arachidonic acid that act on the vasculature, smooth muscle, connective tissue, mucous glands and inflammatory cells (Borish & Joseph 1992, Amin 2012, Metcalfe et al. 1993). FCERI is a multimeric cell-surface receptor that binds the Fc fragment of IgE with high affinity. On mast cells and basophils FCERI exists as a tetrameric complex consisting of one alpha-chain, one beta-chain, and two disulfide-bonded gamma-chains, and on dendritic cells, Langerhans cells, macrophages, and eosinophils it exists as a trimeric complex with one alpha-chain and two disulfide-bonded gamma-chains (Wu 2011, Kraft & Kinet 2007). FCERI signaling in mast cells includes a network of signaling molecules and adaptor proteins. These molecules coordinate ultimately leading to effects on degranulation, eicosanoid production, and cytokine and chemokine production and cell migration and adhesion, growth and survival.The first step in FCERI signaling is the phosphorylation of the tyrosine residues in the ITAM of both the beta and the gamma subunits of the FCERI by LYN, which is bound to the FCERI beta-chain. The phosphorylated ITAM then recruits the protein tyrosine kinase SYK (spleen tyrosine kinase) which then phosphorylates the adaptor protein LAT. Phosphorylated LAT (linker for activation of T cells) acts as a scaffolding protein and recruits other cytosolic adaptor molecules GRB2 (growth-factor-receptor-bound protein 2), GADS (GRB2-related adaptor protein), SHC (SRC homology 2 (SH2)-domain-containing transforming protein C) and SLP76 (SH2-domain-containing leukocyte protein of 76 kDa), as well as the exchange factors and adaptor molecules VAV and SOS (son of sevenless homologue), and the signalling enzyme phospholipase C gamma1 (PLC-gamma1). Tyrosoine phosphorylation of enzymes and adaptors, including VAV, SHC GRB2 and SOS stimulate small GTPases such as RAC, RAS and RAF. These pathways lead to activation of the ERK, JNK and p38 MAP kinases, histamine release and cytokine production. FCERI activation also triggers the phosphorylation of PLC-gamma which upon membrane localisation hydrolyse PIP2 to form IP3 and 1,2-diacylglycerol (DAG) - second messengers that release Ca2+ from internal stores and activate PKC, respectively. Degranulation or histamine release follows the activation of PLC-gamma and protein kinase C (PKC) and the increased mobilization of calcium (Ca2+). Receptor aggregation also results in the phosphorylation of adaptor protein NTAL/LAT2 which then recruits GAB2. PI3K associates with phosphorylated GAB2 and catalyses the formation of PIP3 in the membrane, which attracts many PH domain proteins like BTK, PLC-gamma, AKT and PDK. PI3K mediated activation of AKT then regulate the mast cell proliferation, development and survival (Gu et al. 2001)
R-HSA-2871796	FCERI mediated MAPK activation.	Formation of the LAT signaling complex leads to activation of MAPK and production of cytokines. The sequence of events that leads from LAT to cytokine production has not been as clearly defined as the sequence that leads to degranulation. However, the pathways that lead to cytokine production require the guanine-nucleotide-exchange factors SOS and VAV that regulate GDP-GTP exchange of RAS. After its activation, RAS positively regulates the RAF-dependent pathway that leads to phosphorylation and, in part, activation of the mitogen-activated protein kinases (MAPKs) extracellular-signal-regulated kinase 1 (ERK1) and ERK2 (Gilfillan & Tkaczyk 2006)
R-HSA-2871809	FCERI mediated Ca+2 mobilization.	Increase of intracellular calcium in mast cells is most crucial for mast cell degranulation. Elevation of intracellular calcium is achieved by activation of PLC-gamma. Mast cells express both PLC-gamma1 and PLC-gamma2 isoforms and activation of these enzymes leads to conversion of phosphatidylinositol 4,5-bisphosphate (PIP2) into inositol triphosphate (IP3) and diacylglycerol (DAG). The production of IP3 leads to mobilization of intracellular Ca+2, which later results in a sustained Ca+2 flux response that is maintained by an influx of extracellular Ca+2. In addition to degranulation, an increase in intracellular calcium concentration also activates the Ca2+/calmodulin-dependent serine phosphatase calcineurin. Calcineurin dephosphorylates the nuclear factor for T cell activation (NFAT) which exposes nuclear-localization signal sequence triggering translocation of the dephosphorylated NFAT-CaN complex to the nucleus. Once in the nucleus, NFAT regulates the transcription of several cytokine genes (Kambayashi et al. 2007, Hoth & Penner 1992, Ebinu et al. 2000, Siraganian et al)
R-HSA-5673001	RAF/MAP kinase cascade.	The RAS-RAF-MEK-ERK pathway regulates processes such as proliferation, differentiation, survival, senescence and cell motility in response to growth factors, hormones and cytokines, among others. Binding of these stimuli to receptors in the plasma membrane promotes the GEF-mediated activation of RAS at the plasma membrane and initiates the three-tiered kinase cascade of the conventional MAPK cascades. GTP-bound RAS recruits RAF (the MAPK kinase kinase), and promotes its dimerization and activation (reviewed in Cseh et al, 2014; Roskoski, 2010; McKay and Morrison, 2007; Wellbrock et al, 2004). Activated RAF phosphorylates the MAPK kinase proteins MEK1 and MEK2 (also known as MAP2K1 and MAP2K2), which in turn phophorylate the proline-directed kinases ERK1 and 2 (also known as MAPK3 and MAPK1) (reviewed in Roskoski, 2012a, b; Kryiakis and Avruch, 2012). Activated ERK proteins may undergo dimerization and have identified targets in both the nucleus and the cytosol; consistent with this, a proportion of activated ERK protein relocalizes to the nucleus in response to stimuli (reviewed in Roskoski 2012b; Turjanski et al, 2007; Plotnikov et al, 2010; Cargnello et al, 2011). Although initially seen as a linear cascade originating at the plasma membrane and culminating in the nucleus, the RAS/RAF MAPK cascade is now also known to be activated from various intracellular location. Temporal and spatial specificity of the cascade is achieved in part through the interaction of pathway components with numerous scaffolding proteins (reviewed in McKay and Morrison, 2007; Brown and Sacks, 2009). The importance of the RAS/RAF MAPK cascade is highlighted by the fact that components of this pathway are mutated with high frequency in a large number of human cancers. Activating mutations in RAS are found in approximately one third of human cancers, while ~8% of tumors express an activated form of BRAF (Roberts and Der, 2007; Davies et al, 2002; Cantwell-Dorris et al, 2011)

BioGRID
IntAct
MINT
ALL

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Interacting partner	Detection method	Interaction type	PubMed IDs	Interaction Score	Source
CBL	Affinity Capture-Western	physical	16938345, (Europe PMC)	NA	BioGRID
CD247	Affinity Capture-Western	physical	14523017, (Europe PMC)	NA	BioGRID
CD3E	Affinity Capture-Western	physical	14523017, (Europe PMC)	NA	BioGRID
CLYBL	Affinity Capture-Western	physical	11368773, (Europe PMC)	NA	BioGRID
CREB3	Two-hybrid, two hybrid	physical, physical association	21516116, (Europe PMC)	0.37	BioGRID, IntAct, MINT
EGFR	Affinity Capture-Luminescence, PCA, Two-hybrid, luminescence based mammalian interactome mapping, ubiquitin reconstruction	physical, physical association	24658140, 25402006, (Europe PMC)	0.51	BioGRID, IntAct
FCGR1A	Affinity Capture-Western	physical	10781611, (Europe PMC)	NA	BioGRID
FCGR2A	Affinity Capture-Western	physical	10781611, (Europe PMC)	NA	BioGRID
FYN	Biochemical Activity, protein kinase assay	phosphorylation reaction, physical	16938345, (Europe PMC)	0.44	BioGRID, IntAct
GAB2	Affinity Capture-Western	physical	11572860, (Europe PMC)	NA	BioGRID
GRAP	Affinity Capture-Western, Reconstituted Complex	physical	12186560, 9489702, (Europe PMC)	NA	BioGRID
GRAP2	Affinity Capture-Western, Reconstituted Complex	physical	10021361, 10224278, (Europe PMC)	NA	BioGRID
GRB2	Affinity Capture-Western, Reconstituted Complex, anti bait coimmunoprecipitation, coimmunoprecipitation, cosedimentation in solution, isothermal titration calorimetry, pull down	association, direct interaction, physical, physical association	10811803, 11368773, 12186560, 16906159, 16938345, 23460737, 8063801, 9489702, (Europe PMC)	0.35, 0.61, 0.71	BioGRID, IntAct, MINT
ITK	Affinity Capture-Western, Biochemical Activity	physical	10506192, 12186560, (Europe PMC)	NA	BioGRID
LCK	Affinity Capture-Western, Biochemical Activity, Co-fractionation, anti bait coimmunoprecipitation, protein kinase assay	association, phosphorylation reaction, physical	14523017, 16938345, (Europe PMC)	0.52	BioGRID, IntAct
LCP2	Affinity Capture-Western, anti bait coimmunoprecipitation	association, physical	23514740, 24584089, (Europe PMC)	0.35	BioGRID, IntAct
LMNA	Two-hybrid	physical	24623722, (Europe PMC)	NA	BioGRID
MAP4K1	Affinity Capture-Western, Co-fractionation	physical	11279207, (Europe PMC)	NA	BioGRID
PIK3R1	Affinity Capture-Western, Reconstituted Complex, coimmunoprecipitation, pull down	association, physical	10811803, 11368773, (Europe PMC)	0.46	BioGRID, IntAct, MINT
PLCG1	Affinity Capture-MS, Affinity Capture-Western, Co-fractionation, FRET, Reconstituted Complex, anti bait coimmunoprecipitation, coimmunoprecipitation, pull down, surface plasmon resonance	association, direct interaction, physical, physical association	10811803, 11368773, 16467851, 16938345, 24642916, 27221712, 9489702, 9729044, (Europe PMC)	0.81	BioGRID, IntAct, MINT
PLCG2	Affinity Capture-Western, FRET, surface plasmon resonance	direct interaction, physical	24642916, 27221712, (Europe PMC)	0.44	BioGRID, IntAct
PTPN1	Biochemical Activity, Co-purification, cosedimentation, phosphatase assay, pull down	colocalization, dephosphorylation reaction, physical, physical association	12857726, (Europe PMC)	0.59	BioGRID, IntAct, MINT
PTPN6	Affinity Capture-Western, FRET	physical	27221712, (Europe PMC)	NA	BioGRID
PTPRJ	Biochemical Activity, biochemical	dephosphorylation reaction, physical	11259588, (Europe PMC)	0.44	BioGRID, IntAct, MINT
SGTA	Two-hybrid, two hybrid array, two hybrid prey pooling approach, validated two hybrid	physical, physical association	25416956, (Europe PMC)	0.49, 0.56	BioGRID, IntAct
SH3BP2	Affinity Capture-Western, Reconstituted Complex, cosedimentation through density gradient	colocalization, physical	11390470, 17306257, 9846481, (Europe PMC)	0.35	BioGRID, IntAct, MINT
SHB	Affinity Capture-Western	physical	10488157, 12084069, (Europe PMC)	NA	BioGRID
SLA	Affinity Capture-Western	physical	10449770, (Europe PMC)	NA	BioGRID
SOS1	Co-localization	physical	16906159, (Europe PMC)	NA	BioGRID
SPRY1	Affinity Capture-Western	physical	19915061, (Europe PMC)	NA	BioGRID
SYK	Biochemical Activity	physical	11368773, (Europe PMC)	NA	BioGRID
TRAF6	Affinity Capture-Western, Co-fractionation	physical	23514740, 25907557, (Europe PMC)	NA	BioGRID
USP12	Proximity Label-MS	physical	26811477, (Europe PMC)	NA	BioGRID
USP19	Affinity Capture-MS	physical	19615732, (Europe PMC)	NA	BioGRID
VAV1	Affinity Capture-Western, Reconstituted Complex	physical	11368773, 12186560, (Europe PMC)	NA	BioGRID
ZAP70	Affinity Capture-Western, Biochemical Activity, Co-localization	physical	11368773, 12186560, 16906159, 23514740, (Europe PMC)	NA	BioGRID
ZHX2	Two-hybrid, two hybrid array	physical, physical association	21988832, (Europe PMC)	0.37	BioGRID, IntAct

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Interacting partner	Detection method	Interaction type	PubMed IDs	Interaction Score	Source
CCDC155	barcode fusion genetics two hybrid, validated two hybrid	physical association	27107012, (Europe PMC)	0.49	IntAct
CREB3	Two-hybrid, two hybrid	physical, physical association	21516116, (Europe PMC)	0.37	BioGRID, IntAct, MINT
EBI-4399559	anti bait coimmunoprecipitation	physical association	21282648, (Europe PMC)	0.40	IntAct
EGFR	Affinity Capture-Luminescence, PCA, Two-hybrid, luminescence based mammalian interactome mapping, ubiquitin reconstruction	physical, physical association	24658140, 25402006, (Europe PMC)	0.51	BioGRID, IntAct
FYN	Biochemical Activity, protein kinase assay	phosphorylation reaction, physical	16938345, (Europe PMC)	0.44	BioGRID, IntAct
GRB2	Affinity Capture-Western, Reconstituted Complex, anti bait coimmunoprecipitation, coimmunoprecipitation, cosedimentation in solution, isothermal titration calorimetry, pull down	association, direct interaction, physical, physical association	10811803, 11368773, 12186560, 16906159, 16938345, 23460737, 8063801, 9489702, (Europe PMC)	0.35, 0.61, 0.71	BioGRID, IntAct, MINT
LCK	Affinity Capture-Western, Biochemical Activity, Co-fractionation, anti bait coimmunoprecipitation, protein kinase assay	association, phosphorylation reaction, physical	14523017, 16938345, (Europe PMC)	0.52	BioGRID, IntAct
LCP2	Affinity Capture-Western, anti bait coimmunoprecipitation	association, physical	23514740, 24584089, (Europe PMC)	0.35	BioGRID, IntAct
PIK3R1	Affinity Capture-Western, Reconstituted Complex, coimmunoprecipitation, pull down	association, physical	10811803, 11368773, (Europe PMC)	0.46	BioGRID, IntAct, MINT
PLCG1	Affinity Capture-MS, Affinity Capture-Western, Co-fractionation, FRET, Reconstituted Complex, anti bait coimmunoprecipitation, coimmunoprecipitation, pull down, surface plasmon resonance	association, direct interaction, physical, physical association	10811803, 11368773, 16467851, 16938345, 24642916, 27221712, 9489702, 9729044, (Europe PMC)	0.81	BioGRID, IntAct, MINT
PLCG2	Affinity Capture-Western, FRET, surface plasmon resonance	direct interaction, physical	24642916, 27221712, (Europe PMC)	0.44	BioGRID, IntAct
PTPN1	Biochemical Activity, Co-purification, cosedimentation, phosphatase assay, pull down	colocalization, dephosphorylation reaction, physical, physical association	12857726, (Europe PMC)	0.59	BioGRID, IntAct, MINT
PTPRJ	Biochemical Activity, biochemical	dephosphorylation reaction, physical	11259588, (Europe PMC)	0.44	BioGRID, IntAct, MINT
SGTA	Two-hybrid, two hybrid array, two hybrid prey pooling approach, validated two hybrid	physical, physical association	25416956, (Europe PMC)	0.49, 0.56	BioGRID, IntAct
SH3BP2	Affinity Capture-Western, Reconstituted Complex, cosedimentation through density gradient	colocalization, physical	11390470, 17306257, 9846481, (Europe PMC)	0.35	BioGRID, IntAct, MINT
THEMIS	anti bait coimmunoprecipitation, pull down	association	21189249, 23460737, (Europe PMC)	0.35, 0.46	IntAct
ZHX2	Two-hybrid, two hybrid array	physical, physical association	21988832, (Europe PMC)	0.37	BioGRID, IntAct

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Interacting partner	Detection method	Interaction type	PubMed IDs	Interaction Score	Source
CBL	Affinity Capture-Western	physical	16938345, (Europe PMC)	NA	BioGRID
CCDC155	barcode fusion genetics two hybrid, validated two hybrid	physical association	27107012, (Europe PMC)	0.49	IntAct
CD247	Affinity Capture-Western	physical	14523017, (Europe PMC)	NA	BioGRID
CD3E	Affinity Capture-Western	physical	14523017, (Europe PMC)	NA	BioGRID
CLYBL	Affinity Capture-Western	physical	11368773, (Europe PMC)	NA	BioGRID
CREB3	Two-hybrid, two hybrid	physical, physical association	21516116, (Europe PMC)	0.37	BioGRID, IntAct, MINT
EBI-4399559	anti bait coimmunoprecipitation	physical association	21282648, (Europe PMC)	0.40	IntAct
EGFR	Affinity Capture-Luminescence, PCA, Two-hybrid, luminescence based mammalian interactome mapping, ubiquitin reconstruction	physical, physical association	24658140, 25402006, (Europe PMC)	0.51	BioGRID, IntAct
FCGR1A	Affinity Capture-Western	physical	10781611, (Europe PMC)	NA	BioGRID
FCGR2A	Affinity Capture-Western	physical	10781611, (Europe PMC)	NA	BioGRID
FYN	Biochemical Activity, protein kinase assay	phosphorylation reaction, physical	16938345, (Europe PMC)	0.44	BioGRID, IntAct
GAB2	Affinity Capture-Western	physical	11572860, (Europe PMC)	NA	BioGRID
GRAP	Affinity Capture-Western, Reconstituted Complex	physical	12186560, 9489702, (Europe PMC)	NA	BioGRID
GRAP2	Affinity Capture-Western, Reconstituted Complex	physical	10021361, 10224278, (Europe PMC)	NA	BioGRID
GRB2	Affinity Capture-Western, Reconstituted Complex, anti bait coimmunoprecipitation, coimmunoprecipitation, cosedimentation in solution, isothermal titration calorimetry, pull down	association, direct interaction, physical, physical association	10811803, 11368773, 12186560, 16906159, 16938345, 23460737, 8063801, 9489702, (Europe PMC)	0.35, 0.61, 0.71	BioGRID, IntAct, MINT
ITK	Affinity Capture-Western, Biochemical Activity	physical	10506192, 12186560, (Europe PMC)	NA	BioGRID
LCK	Affinity Capture-Western, Biochemical Activity, Co-fractionation, anti bait coimmunoprecipitation, protein kinase assay	association, phosphorylation reaction, physical	14523017, 16938345, (Europe PMC)	0.52	BioGRID, IntAct
LCP2	Affinity Capture-Western, anti bait coimmunoprecipitation	association, physical	23514740, 24584089, (Europe PMC)	0.35	BioGRID, IntAct
LMNA	Two-hybrid	physical	24623722, (Europe PMC)	NA	BioGRID
MAP4K1	Affinity Capture-Western, Co-fractionation	physical	11279207, (Europe PMC)	NA	BioGRID
PIK3R1	Affinity Capture-Western, Reconstituted Complex, coimmunoprecipitation, pull down	association, physical	10811803, 11368773, (Europe PMC)	0.46	BioGRID, IntAct, MINT
PLCG1	Affinity Capture-MS, Affinity Capture-Western, Co-fractionation, FRET, Reconstituted Complex, anti bait coimmunoprecipitation, coimmunoprecipitation, pull down, surface plasmon resonance	association, direct interaction, physical, physical association	10811803, 11368773, 16467851, 16938345, 24642916, 27221712, 9489702, 9729044, (Europe PMC)	0.81	BioGRID, IntAct, MINT
PLCG2	Affinity Capture-Western, FRET, surface plasmon resonance	direct interaction, physical	24642916, 27221712, (Europe PMC)	0.44	BioGRID, IntAct
PTPN1	Biochemical Activity, Co-purification, cosedimentation, phosphatase assay, pull down	colocalization, dephosphorylation reaction, physical, physical association	12857726, (Europe PMC)	0.59	BioGRID, IntAct, MINT
PTPN6	Affinity Capture-Western, FRET	physical	27221712, (Europe PMC)	NA	BioGRID
PTPRJ	Biochemical Activity, biochemical	dephosphorylation reaction, physical	11259588, (Europe PMC)	0.44	BioGRID, IntAct, MINT
SGTA	Two-hybrid, two hybrid array, two hybrid prey pooling approach, validated two hybrid	physical, physical association	25416956, (Europe PMC)	0.49, 0.56	BioGRID, IntAct
SH3BP2	Affinity Capture-Western, Reconstituted Complex, cosedimentation through density gradient	colocalization, physical	11390470, 17306257, 9846481, (Europe PMC)	0.35	BioGRID, IntAct, MINT
SHB	Affinity Capture-Western	physical	10488157, 12084069, (Europe PMC)	NA	BioGRID
SLA	Affinity Capture-Western	physical	10449770, (Europe PMC)	NA	BioGRID
SOS1	Co-localization	physical	16906159, (Europe PMC)	NA	BioGRID
SPRY1	Affinity Capture-Western	physical	19915061, (Europe PMC)	NA	BioGRID
SYK	Biochemical Activity	physical	11368773, (Europe PMC)	NA	BioGRID
THEMIS	anti bait coimmunoprecipitation, pull down	association	21189249, 23460737, (Europe PMC)	0.35, 0.46	IntAct
TRAF6	Affinity Capture-Western, Co-fractionation	physical	23514740, 25907557, (Europe PMC)	NA	BioGRID
USP12	Proximity Label-MS	physical	26811477, (Europe PMC)	NA	BioGRID
USP19	Affinity Capture-MS	physical	19615732, (Europe PMC)	NA	BioGRID
VAV1	Affinity Capture-Western, Reconstituted Complex	physical	11368773, 12186560, (Europe PMC)	NA	BioGRID
ZAP70	Affinity Capture-Western, Biochemical Activity, Co-localization	physical	11368773, 12186560, 16906159, 23514740, (Europe PMC)	NA	BioGRID
ZHX2	Two-hybrid, two hybrid array	physical, physical association	21988832, (Europe PMC)	0.37	BioGRID, IntAct

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