DEPOD - human DEPhOsphorylation Database

Basic Information
Substrates
Pathway
Interacting Proteins
Phosphorylating Kinases

Gene Name	PTPN6 (QuickGO)	Interactive visualization of PTPN6 structures (A quick tutorial to explore the interactive visualization)
Synonyms	PTPN6, HCP, PTP1C
Protein Name	PTPN6
Alternative Name(s)	Tyrosine-protein phosphatase non-receptor type 6;3.1.3.48;Hematopoietic cell protein-tyrosine phosphatase;Protein-tyrosine phosphatase 1C;PTP-1C;Protein-tyrosine phosphatase SHP-1;SH-PTP1;SHP1
EntrezGene ID	5777 (Comparative Toxicogenomics)
UniProt AC (Human)	P29350 (protein sequence)
Enzyme Class	EC 3.1.3.48 (BRENDA )
Molecular Weight	67561 Dalton
Protein Length	595 amino acids (AA)
Genome Browsers	NCBI \| ENSG00000111679 (Ensembl) \| UCSC
Crosslinking annotations	Query our ID-mapping table
Orthologues	Quest For Orthologues (QFO) \| GeneTree
Classification	Superfamily: Class I Cys-based PTPs --> Family: NR-PTP \| Historic class: Class I Cys-based PTPs --> Classical PTPs --> Non-receptor type PTPs (NR-PTPs) \| CATH ID: 3.90.190.10 \| SCOP Fold: CC1
Phosphatase activity	active \| Catalytic signature motif: HCSAGIGR
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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GO:0001784	F:phosphotyrosine residue binding
GO:0002244	P:hematopoietic progenitor cell differentiation
GO:0002924	P:negative regulation of humoral immune response mediated by circulating immunoglobulin
GO:0004725	F:protein tyrosine phosphatase activity
GO:0005001	F:transmembrane receptor protein tyrosine phosphatase activity
GO:0005576	C:extracellular region
GO:0005634	C:nucleus
GO:0005654	C:nucleoplasm
GO:0005730	C:nucleolus
GO:0005737	C:cytoplasm
GO:0005829	C:cytosol
GO:0005911	C:cell-cell junction
GO:0006470	P:protein dephosphorylation
GO:0006915	P:apoptotic process
GO:0007186	P:G-protein coupled receptor signaling pathway
GO:0008283	P:cell proliferation
GO:0008284	P:positive regulation of cell proliferation
GO:0008285	P:negative regulation of cell proliferation
GO:0014068	P:positive regulation of phosphatidylinositol 3-kinase signaling
GO:0016020	C:membrane
GO:0017124	F:SH3 domain binding
GO:0018108	P:peptidyl-tyrosine phosphorylation
GO:0019221	P:cytokine-mediated signaling pathway
GO:0019901	F:protein kinase binding
GO:0030154	P:cell differentiation
GO:0030168	P:platelet activation
GO:0030220	P:platelet formation
GO:0031295	P:T cell costimulation
GO:0032991	C:protein-containing complex
GO:0033277	P:abortive mitotic cell cycle
GO:0033630	P:positive regulation of cell adhesion mediated by integrin
GO:0035335	P:peptidyl-tyrosine dephosphorylation
GO:0035556	P:intracellular signal transduction
GO:0035580	C:specific granule lumen
GO:0035855	P:megakaryocyte development
GO:0042105	C:alpha-beta T cell receptor complex
GO:0042130	P:negative regulation of T cell proliferation
GO:0042169	F:SH2 domain binding
GO:0042267	P:natural killer cell mediated cytotoxicity
GO:0043312	P:neutrophil degranulation
GO:0043407	P:negative regulation of MAP kinase activity
GO:0045577	P:regulation of B cell differentiation
GO:0050732	P:negative regulation of peptidyl-tyrosine phosphorylation
GO:0050839	F:cell adhesion molecule binding
GO:0050853	P:B cell receptor signaling pathway
GO:0050859	P:negative regulation of B cell receptor signaling pathway
GO:0050860	P:negative regulation of T cell receptor signaling pathway
GO:0050900	P:leukocyte migration
GO:0051279	P:regulation of release of sequestered calcium ion into cytosol
GO:0060338	P:regulation of type I interferon-mediated signaling pathway
GO:0070062	C:extracellular exosome
GO:0070372	P:regulation of ERK1 and ERK2 cascade
GO:0070527	P:platelet aggregation
GO:0071345	P:cellular response to cytokine stimulus
GO:0140031	F:phosphorylation-dependent protein binding
GO:1904724	C:tertiary granule lumen
GO:2000045	P:regulation of G1/S transition of mitotic cell cycle

KEGG Pathway
Reactome Pathway

Pathway ID	Pathway Name	Pathway Description (KEGG)
hsa04520	Adherens junction	Cell-cell adherens junctions (AJs), the most common type of intercellular adhesions, are important for maintaining tissue architecture and cell polarity and can limit cell movement and proliferation. At AJs, E-cadherin serves as an essential cell adhesion molecules (CAMs). The cytoplasmic tail binds beta-catenin, which in turn binds alpha-catenin. Alpha-catenin is associated with F-actin bundles directly and indirectly. The integrity of the cadherin-catenin complex is negatively regulated by phosphorylation of beta-catenin by receptor tyrosine kinases (RTKs) and cytoplasmic tyrosine kinases (Fer, Fyn, Yes, and Src), which leads to dissociation of the cadherin-catenin complex. Integrity of this complex is positively regulated by beta -catenin phosphorylation by casein kinase II, and dephosphorylation by protein tyrosine phosphatases. Changes in the phosphorylation state of beta-catenin affect cell-cell adhesion, cell migration and the level of signaling beta-catenin. Wnt signaling acts as a positive regulator of beta-catenin by inhibiting beta-catenin degradation, which stabilizes beta-catenin, and causes its accumulation. Cadherin may acts as a negative regulator of signaling beta-catenin as it binds beta-catenin at the cell surface and thereby sequesters it from the nucleus. Nectins also function as CAMs at AJs, but are more highly concentrated at AJs than E-cadherin. Nectins transduce signals through Cdc42 and Rac, which reorganize the actin cytoskeleton, regulate the formation of AJs, and strengthen cell-cell adhesion.
hsa04630	Jak-STAT signaling pathway	The Janus kinase/signal transducers and activators of transcription (JAK/STAT) pathway is one of a handful of pleiotropic cascades used to transduce a multitude of signals for development and homeostasis in animals, from humans to flies. In mammals, the JAK/STAT pathway is the principal signaling mechanism for a wide array of cytokines and growth factors. Following the binding of cytokines to their cognate receptor, STATs are activated by members of the JAK family of tyrosine kinases. Once activated, they dimerize and translocate to the nucleus and modulate the expression of target genes. In addition to the activation of STATs, JAKs mediate the recruitment of other molecules such as the MAP kinases, PI3 kinase etc. These molecules process downstream signals via the Ras-Raf-MAP kinase and PI3 kinase pathways which results in the activation of additional transcription factors.
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.
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.
hsa04662	B cell receptor signaling pathway	B cells are an important component of adaptive immunity. They produce and secrete millions of different antibody molecules, each of which recognizes a different (foreign) antigen. The B cell receptor (BCR) is an integral membrane protein complex that is composed of two immunoglobulin (Ig) heavy chains, two Ig light chains and two heterodimers of Ig-alpha and Ig-beta. After BCR ligation by antigen, three main protein tyrosine kinases (PTKs) -the SRC-family kinase LYN, SYK and the TEC-family kinase BTK- are activated. Phosphatidylinositol 3-kinase (PI3K) and phospholipase C-gamma 2 (PLC-gamma 2) are important downstream effectors of BCR signalling. This signalling ultimately results in the expression of immediate early genes that further activate the expression of other genes involved in B cell proliferation, differentiation and Ig production as well as other processes.
hsa05140	Leishmaniasis	Leishmania is an intracellular protozoan parasite of macrophages that causes visceral, mucosal, and cutaneous diseases. The parasite is transmitted to humans by sandflies, where they survive and proliferate intracellularly by deactivating the macrophage. Successful infection of Leishmania is achieved by alteration of signaling events in the host cell, leading to enhanced production of the autoinhibitory molecules like TGF-beta and decreased induction of cytokines such as IL12 for protective immunity. Nitric oxide production is also inhibited. In addition, defective expression of major histocompatibility complex (MHC) genes silences subsequent T cell activation mediated by macrophages, resulting in abnormal immune responses.
hsa05205	Proteoglycans in cancer	Many proteoglycans (PGs) in the tumor microenvironment have been shown to be key macromolecules that contribute to biology of various types of cancer including proliferation, adhesion, angiogenesis and metastasis, affecting tumor progress. The four main types of proteoglycans include hyaluronan (HA), which does not occur as a PG but in free form, heparan sulfate proteoglycans (HSPGs), chondroitin sulfate proteoglycans (CSPGs), dematan sulfate proteoglycans (DSPG) and keratan sulfate proteoglycans (KSPGs) [BR:00535]. Among these proteoglycans such as HA, acting with CD44, promotes tumor cell growth and migration, whereas other proteoglycans such as syndecans (-1~-4), glypican (-1, -3) and perlecan may interact with growth factors, cytokines, morphogens and enzymes through HS chains [BR: 00536], also leading to tumor growth and invasion. In contrast, some of the small leucine-rich proteolgycans, such as decorin and lumican, can function as tumor repressors, and modulate the signaling pathways by the interaction of their core proteins and multiple receptors.

Pathway ID	Pathway Name	Pathway Description (Reactome)
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-1433559	Regulation of KIT signaling.	SCF induced proliferation is negatively regulated by various proteins including SHP1, PKC, CBL, SOCS1, SOCS6 and LNK
R-HSA-210990	PECAM1 interactions.	PECAM-1/CD31 is a member of the immunoglobulin superfamily (IgSF) and has been implicated to mediate the adhesion and trans-endothelial migration of T-lymphocytes into the vascular wall, T cell activation and angiogenesis. It has six Ig homology domains within its extracellularly and an ITIM motif within its cytoplasmic region. PECAM-1 mediates cellular interactions by both homophilic and heterophilic interactions. The cytoplasmic domain of PECAM-1 contains tyrosine residues which serves as docking sites for recruitment of cytosolic signaling molecules. Under conditions of platelet activation, PECAM-1 is phosphorylated by Src kinase members. The tyrosine residues 663 and 686 are required for recruitment of the SH2 domain containing PTPs
R-HSA-388841	Costimulation by the CD28 family.	Optimal activation of T-lymphocytes requires at least two signals. A primary one is delivered by the T-cell receptor (TCR) complex after antigen recognition and additional costimulatory signals are delivered by the engagement of costimulatory receptors such as CD28. The best-characterized costimulatory pathways are mediated by a set of cosignaling molecules belonging to the CD28 superfamily, including CD28, CTLA4, ICOS, PD1 and BTLA receptors. These proteins deliver both positive and negative second signals to T-cells by interacting with B7 family ligands expressed on antigen presenting cells. Different subsets of T-cells have very different requirements for costimulation. CD28 family mediated costimulation is not required for all T-cell responses in vivo, and alternative costimulatory pathways also exist. Different receptors of the CD28 family and their ligands have different regulation of expression. CD28 is constitutively expressed on naive T cells whereas CTLA4 expression is dependent on CD28/B7 engagement and the other receptor members ICOS, PD1 and BTLA are induced after initial T-cell stimulation. The positive signals induced by CD28 and ICOS molecules are counterbalanced by other members of the CD28 family, including cytotoxic T-lymphocyte associated antigen (CTLA)4, programmed cell death (PD)1, and B and T lymphocyte attenuator (BTLA), which dampen immune responses. The balance of stimulatory and inhibitory signals is crucial to maximize protective immune responses while maintaining immunological tolerance and preventing autoimmunity. The costimulatory receptors CD28, CTLA4, ICOS and PD1 are composed of single extracellular IgV-like domains, whereas BTLA has one IgC-like domain. Receptors CTLA4, CD28 and ICOS are covalent homodimers, due to an interchain disulphide linkage. The costimulatory ligands B71, B72, B7H2, B7H1 and B7DC, have a membrane proximal IgC-like domain and a membrane distal IgV-like domain that is responsible for receptor binding and dimerization. CD28 and CTLA4 have no known intrinsic enzymatic activity. Instead, engagement by their physiologic ligands B71 and B72 leads to the physical recruitment and activation of downstream T-cell effector molecules
R-HSA-389948	PD-1 signaling.	The Programmed cell death protein 1 (PD-1) is one of the negative regulators of TCR signaling. PD-1 may exert its effects on cell differentiation and survival directly by inhibiting early activation events that are positively regulated by CD28 or indirectly through IL-2. PD-1 ligation inhibits the induction of the cell survival factor Bcl-xL and the expression of transcription factors associated with effector cell function, including GATA-3, Tbet, and Eomes. PD-1 exerts its inhibitory effects by bringing phosphatases SHP-1 and SHP-2 into the immune synapse, leading to dephosphorylation of CD3-zeta chain, PI3K and AKT
R-HSA-391160	Signal regulatory protein family interactions.	Signal regulatory protein alpha (SIRPA, SHPS1, CD172a) is a transmembrane protein expressed mostly on myeloid cells. CD47, a widely expressed transmembrane protein, is a ligand for SIRP alpha, with the two proteins constituting a cell-cell communication system. The interaction of SIRPA with CD47 is important for the regulation of migration and phagocytosis. SIRPA functions as a docking protein to recruit and activate PTPN6 (SHP-1) or PTPN11 (SHP-2) at the cell membrane in response to extracellular stimuli. SIRPA also binds other intracellular proteins including the adaptor molecules Src kinase-associated protein (SKAP2 SKAP55hom/R), Fyn-binding protein/SLP-76-associated phosphoprotein (FYB/SLAP-130) and the tyrosine kinase PYK2. SIRPA also binds the extracellular proteins, surfactant-A (SP-A) and surfactant-D (SP-D). The SIRP family members SIRPB and SIRPG show high sequence similarity and similar extracellular structural topology, including three Ig domains, but their ligand binding topology might differ. SIRPB is expressed on myeloid cells, including monocytes, granulocytes and DCs. It has no known natural ligand. SIRPG can bind CD47 but with lower affinity than SIRPA
R-HSA-432142	Platelet sensitization by LDL.	Physiological concentrations (1g/L) of Low density lipoprotein (LDL) enhance platelet aggregation responses initiated by thrombin, collagen, and ADP. This enhancement involves the rapid phosphorylation of p38 mitogen-activated protein kinase (p38MAPK) at Thr180 and Tyr182. The receptor for LDL is ApoER2, a splice variant of the classical ApoE receptor. ApoER2 stimulation leads to association of the Src family kinase Fgr which is probably responsible for subsequent phosphorylation of p38MAPK. This stimulation is transient because LDL also increases the activity of PECAM-1, which stimulates phosphatases that dephosphorylate p38MAPK
R-HSA-512988	Interleukin-3, Interleukin-5 and GM-CSF signaling.	The Interleukin-3 (IL-3), IL-5 and Granulocyte-macrophage colony stimulating factor (GM-CSF) receptors form a family of heterodimeric receptors that have specific alpha chains but share a common beta subunit, often referred to as the common beta (Bc). Both subunits contain extracellular conserved motifs typical of the cytokine receptor superfamily. The cytoplasmic domains have limited similarity with other cytokine receptors and lack detectable catalytic domains such as tyrosine kinase domains. IL-3 is a 20-26 kDa product of CD4+ T cells that acts on the most immature marrow progenitors. IL-3 is capable of inducing the growth and differentiation of multi-potential hematopoietic stem cells, neutrophils, eosinophils, megakaryocytes, macrophages, lymphoid and erythroid cells. IL-3 has been used to support the proliferation of murine cell lines with properties of multi-potential progenitors, immature myeloid as well as T and pre-B lymphoid cells (Miyajima et al. 1992). IL-5 is a hematopoietic growth factor responsible for the maturation and differentiation of eosinophils. It was originally defined as a T-cell-derived cytokine that triggers activated B cells for terminal differentiation into antibody-secreting plasma cells. It also promotes the generation of cytotoxic T-cells from thymocytes. IL-5 induces the expression of IL-2 receptors (Kouro & Takatsu 2009). GM-CSF is produced by cells (T-lymphocytes, tissue macrophages, endothelial cells, mast cells) found at sites of inflammatory responses. It stimulates the growth and development of progenitors of granulocytes and macrophages, and the production and maturation of dendritic cells. It stimulates myeloblast and monoblast differentiation, synergises with Epo in the proliferation of erythroid and megakaryocytic progenitor cells, acts as an autocrine mediator of growth for some types of acute myeloid leukemia, is a strong chemoattractant for neutrophils and eosinophils. It enhances the activity of neutrophils and macrophages. Under steady-state conditions GM-CSF is not essential for the production of myeloid cells, but it is required for the proper development of alveolar macrophages, otherwise, pulmonary alvelolar proteinosis (PAP) develops. A growing body of evidence suggests that GM-CSF plays a key role in emergency hematopoiesis (predominantly myelopoiesis) in response to infection, including the production of granulocytes and macrophages in the bone marrow and their maintenance, survival, and functional activation at sites of injury or insult (Hercus et al. 2009). All three receptors have alpha chains that bind their specific ligands with low affinity (de Groot et al. 1998). Bc then associates with the alpha chain forming a high affinity receptor (Geijsen et al. 2001), though the in vivo receptor is likely be a higher order multimer as recently demonstrated for the GM-CSF receptor (Hansen et al. 2008). The receptor chains lack intrinsic kinase activity, instead they interact with and activate signaling kinases, notably Janus Kinase 2 (JAK2). These phosphorylate the common beta subunit, allowing recruitment of signaling molecules such as Shc, the phosphatidylinositol 3-kinases (PI3Ks), and the Signal Transducers and Activators of Transcription (STATs). The cytoplasmic domain of Bc has two distinct functional domains: the membrane proximal region mediates the induction of proliferation-associated genes such as c-myc, pim-1 and oncostatin M. This region binds multiple signal-transducing proteins including JAK2 (Quelle et al. 1994), STATs, c-Src and PI3 kinase (Rao and Mufson, 1995). The membrane distal domain is required for cytokine-induced growth inhibition and is necessary for the viability of hematopoietic cells (Inhorn et al. 1995). This region interacts with signal-transducing proteins such as Shc (Inhorn et al. 1995) and SHP and mediates the transcriptional activation of c-fos, c-jun, c-Raf and p70S6K (Reddy et al. 2000).Figure reproduced by permission from Macmillan Publishers Ltd: Leukemia, WL Blalock et al. 13:1109-1166, copyright 1999. Note that residue numbering in this diagram refers to the mature Common beta chain with signal peptide removed
R-HSA-5690714	CD22 mediated BCR regulation.	BCR activation is highly regulated and coreceptors like CD22 (SIGLEC2) set a signalling threshold to prevent aberrant immune response and autoimmune disease (Cyster et al. 1997, Han et al. 2005). CD22 is a glycoprotein found on the surface of B cells during restricted stages of development. CD22 is a member of the receptors of the sialic acid-binding Ig-like lectin (Siglec) family which binds specifically to the terminal sequence N-acetylneuraminic acid alpha(2-6) galactose (NeuAc-alpha(2-6)-Gal) present on many B-cell glycoproteins (Powell et al. 1993, Sgroi et al. 1993). CD22 has seven immunoglobulin (Ig)-like extracellular domains and a cytoplasmic tail containing six tyrosines, three of which belong to the inhibitory immunoreceptor tyrosine-based inhibition motifs (ITIMs) sequences. Upon BCR cross-linking CD22 is rapidly tyrosine phosphorylated by the tyrosine kinase Lyn, thereby recruiting and activating tyrosine phosphatase, SHP-1 and inhibiting calcium signalling
R-HSA-6798695	Neutrophil degranulation.	Neutrophils are the most abundant leukocytes (white blood cells), indispensable in defending the body against invading microorganisms. In response to infection, neutrophils leave the circulation and migrate towards the inflammatory focus. They contain several subsets of granules that are mobilized to fuse with the cell membrane or phagosomal membrane, resulting in the exocytosis or exposure of membrane proteins. Traditionally, neutrophil granule constituents are described as antimicrobial or proteolytic, but granules also introduce membrane proteins to the cell surface, changing how the neutrophil responds to its environment (Borregaard et al. 2007). Primed neutrophils actively secrete cytokines and other inflammatory mediators and can present antigens via MHC II, stimulating T-cells (Wright et al. 2010).Granules form during neutrophil differentiation. Granule subtypes can be distinguished by their content but overlap in structure and composition. The differences are believed to be a consequence of changing protein expression and differential timing of granule formation during the terminal processes of neutrophil differentiation, rather than sorting (Le Cabec et al. 1996). The classical granule subsets are Azurophil or primary granules (AG), secondary granules (SG) and gelatinase granules (GG). Neutrophils also contain exocytosable storage cell organelles, storage vesicles (SV), formed by endocytosis they contain many cell-surface markers and extracellular, plasma proteins (Borregaard et al. 1992). Ficolin-1-rich granules (FG) are like GGs highly exocytosable but gelatinase-poor (Rorvig et al. 2009)
R-HSA-877300	Interferon gamma signaling.	Interferon-gamma (IFN-gamma) belongs to the type II interferon family and is secreted by activated immune cells-primarily T and NK cells, but also B-cells and APC. INFG exerts its effect on cells by interacting with the specific IFN-gamma receptor (IFNGR). IFNGR consists of two chains, namely IFNGR1 (also known as the IFNGR alpha chain) and IFNGR2 (also known as the IFNGR beta chain). IFNGR1 is the ligand binding receptor and is required but not sufficient for signal transduction, whereas IFNGR2 do not bind IFNG independently but mainly plays a role in IFNG signaling and is generally the limiting factor in IFNG responsiveness. Both IFNGR chains lack intrinsic kinase/phosphatase activity and thus rely on other signaling proteins like Janus-activated kinase 1 (JAK1), JAK2 and Signal transducer and activator of transcription 1 (STAT-1) for signal transduction. IFNGR complex in its resting state is a preformed tetramer and upon IFNG association undergoes a conformational change. This conformational change induces the phosphorylation and activation of JAK1, JAK2, and STAT1 which in turn induces genes containing the gamma-interferon activation sequence (GAS) in the promoter
R-HSA-877312	Regulation of IFNG signaling.	At least three different classes of negative regulators exist to control the extent of INFG stimulation and signaling. These include the feedback inhibitors belonging to protein family suppressors of cytokine signaling (SOCS), the Scr-homology 2 (SH2)-containing protein tyrosine phosphatases (SHPs), and the protein inhibitors of activated STATs (PIAS). The induction of these regulators seems to be able to stop further signal transduction by inhibiting various steps in IFNG cascade
R-HSA-9008059	Interleukin-37 signaling.	Interleukins (IL) are immunomodulatory proteins that elicit a wide array of responses in cells and tissues. Interleukin 37 (IL37), also known as IL 1F7, is a member of the IL 1 family (Sharma et al. 2008). Isoform b of IL37 (referred just as IL37) is synthesized as a precursor that requires processing (primarily by caspase 1) to attain full receptor agonist or antagonist function (Kumar et al. 2002). Both full length and processed IL37 can bind to the IL 18 binding protein (IL 18BP) and the Interleukin 18 receptor 1 (IL 18R1) (Shi et al. 2003). Upon binding to the IL18R1, IL37 recruits Single Ig IL 1 related receptor (SIGIRR) (Nold-Petry et al. 2015). The IL37:IL18R1 complex can activate phosphorylation of Signal transducer and activator of transcription 3 (STAT3), Tyrosine protein kinase Mer and Phosphatidylinositol 3,4,5 trisphosphate 3 phosphatase and dual specificity protein phosphatase PTEN and can also inhibit Nuclear factor NF kappa B p105 subunit (NFKB) (Nold-Petry et al. 2015). Processed IL37 can be secreted from the cytosol to the extracellular space or translocated into the nucleus (Bulau et al. 2014). Full length IL37 can also be secreted from the cytosol to the extracellular space (Bulau et al. 2014). Processed IL37 can bind with Mothers against decapentaplegic homolog 3 (SMAD3) in the cytosol and then translocate to the nucleus, where it facilitates transcription of Tyrosine protein phosphatase non receptors (PTPNs) (Nold et al. 2010, Luo et al. 2017). These events ultimately lead to suppression of cytokine production in several types of immune cells resulting in reduced inflammation
R-HSA-909733	Interferon alpha/beta signaling.	Type I interferons (IFNs) are composed of various genes including IFN alpha (IFNA), beta (IFNB), omega, epsilon, and kappa. In humans the IFNA genes are composed of more than 13 subfamily genes, whereas there is only one IFNB gene. The large family of IFNA/B proteins all bind to a single receptor which is composed of two distinct chains: IFNAR1 and IFNAR2. The IFNA/B stimulation of the IFNA receptor complex leads to the formation of two transcriptional activator complexes: IFNA-activated-factor (AAF), which is a homodimer of STAT1 and IFN-stimulated gene factor 3 (ISGF3), which comprises STAT1, STAT2 and a member of the IRF family, IRF9/P48. AAF mediates activation of the IRF-1 gene by binding to GAS (IFNG-activated site), whereas ISGF3 activates several IFN-inducible genes including IRF3 and IRF7
R-HSA-912526	Interleukin receptor SHC signaling.	Phosphorylation of Shc at three tyrosine residues, 239, 240 (Gotoh et al. 1996) and 317 (Salcini et al. 1994) involves unidentified tyrosine kinases presumed to be part of the activated receptor complex. These phosphorylated tyrosines subsequently bind SH2 signaling proteins such as Grb2, Gab2 and SHIP that are involved in the regulation of different signaling pathways. Grb2 can associate with the guanosine diphosphate-guanosine triphosphate exchange factor Sos1, leading to Ras activation and regulation of cell proliferation. Downstream signals are mediated via the Raf-MEK-Erk pathway.Grb2 can also associate through Gab2 with PI3K and with SHIP.Figure reproduced from Gu, H. et al. 2000. Mol. Cell. Biol. 20(19):7109-7120Copyright American Society for Microbiology. All Rights Reserved
R-HSA-912694	Regulation of IFNA signaling.	There are several proteins and mechanisms involved in controlling the extent of ligand stimulation of IFNA/B signaling. These mechanisms can effect every step of the IFNA/B cascade. Dephosphorylation of JAK and STAT by SHP protein phosphatases, inhibition of STAT function in the nucleus by protein inhibitors of activated STATs (PIAS) proteins, inhibition of tyrosine kinase activity of JAKs by SOCS as well as inhibition of JAK and IFNAR2 interaction by UBP43 are few of the negative regulation mechanisms in controling type I IFN signaling
R-HSA-982772	Growth hormone receptor signaling.	Growth hormone (Somatotropin or GH) is a key factor in determining lean body mass, stimulating the growth and metabolism of muscle, bone and cartilage cells, while reducing body fat. It has many other roles; it acts to regulate cell growth, differentiation, apoptosis, and reorganisation of the cytoskeleton, affecting diverse processes such as cardiac function, immune function, brain function, and aging. GH also has insulin-like effects such as stimulating amino acid transport, protein synthesis, glucose transport, and lipogenesis. The growth hormone receptor (GHR) is a a member of the cytokine receptor family. When the dimeric receptor binds GH it undergoes a conformational change which leads to phosphorylation of key tyrosine residues in its cytoplasmic domains and activation of associated tyrosine kinase JAK2. This leads to recruitment of signaling molecules such as STAT5 and Src family kinases such as Lyn leading to ERK activation. The signal is attenuated by association of Suppressor of Cytokine Signaling (SOCS) proteins and SHP phosphatases which bind to or dephosphorylate specific phosphorylated tyrosines on GHR/JAK. The availability of GHR on the cell surface is regulated by at least two processes; internalization and cleavage from the suface by metalloproteases
R-HSA-983695	Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.	Mature B cells express IgM and IgD immunoglobulins which are complexed with Ig-alpha (CD79A, MB-1) and Ig-beta (CD79B, B29) to form the B cell receptor (BCR) (Fu et al. 1974, Fu et al. 1975, Kunkel et al. 1975, Van Noesal et al. 1992, Sanchez et al. 1993, reviewed in Brezski and Monroe 2008). Binding of antigen to the immunoglobulin activates phosphorylation of immunoreceptor tyrosine-based activation motifs (ITAMs) in the cytoplasmic tails of Ig-alpha and Ig-beta by Src family tyrosine kinases, including LYN, FYN, and BLK (Nel et al. 1984, Yamanashi et al. 1991, Flaswinkel and Reth 1994, Saouaf et al. 1994, Hata et al. 1994, Saouaf et al. 1995, reviewed in Gauld and Cambier 2004, reviewed in Harwood and Batista 2010). The protein kinase SYK may also be involved in phosphorylating the ITAMs.The protein kinase SYK binds the phosphorylated immunoreceptor tyrosine-activated motifs (ITAMs) on the cytoplasmic tails of Ig-alpha (CD79A, MB-1) and Ig-beta (CD79B, B29) (Wienands et al. 1995, Rowley et al. 1995, Tsang et al. 2008). The binding causes the activation and autophosphorylation of SYK (Law et al. 1994, Irish et al. 2006, Baldock et al. 2008, Tsang et al. 2008, reviewed in Bradshaw 2010).Activated SYK and other kinases phosphorylate BLNK (SLP-65, BASH) and BCAP. LYN and FYN phosphorylate CD19. Phosphorylated BLNK, BCAP, and CD19 serve as scaffolds which recruit effectors to the plasma membrane and assemble large complexes, the signalosomes. BCAP and CD19 recruit phosphoinositol 3-kinase (PI3K). BLNK recruits phospholipase C gamma (predominantly PLC-gamma2 in B cells, Coggeshall et al. 1992), NCK, BAM32, BTK, VAV1, and SHC. The effectors are phosphorylated by SYK and other kinases.Phosphorylated BCAP recruits PI3K, which is phosphorylated by a SYK-dependent mechanism (Kuwahara et al. 1996) and produces phosphatidylinositol-3,4,5-trisphosphate (PIP3). Phosphorylated CD19 likewise recruits PIP3K. PIP3 recruits BAM32 (Marshall et al. 2000) and BTK (de Weers et al. 1994, Baba et al. 2001) to the plasma membrane via their PH domains. PIP3 also recruits and activates PLC-gamma1 and PLC-gamma2 (Bae et al. 1998). BTK binds phosphorylated BLNK via its SH2 domain (Baba et al. 2001). BTK phosphorylates PLC-gamma2 (Rodriguez et al. 2001), which activates phospholipase activity (Carter et al. 1991, Roifman and Wang 1992, Kim et al. 2004, Sekiya et al. 2004). Phosphorylated BLNK recruits PLC-gamma, VAV, GRB2, and NCK (Fu and Chan 1997, Fu et al. 1998, Chiu et al. 2002).PLC-gamma hydrolyzes phosphatidylinositol-4,5-bisphosphate to yield inositol-1,4,5-trisphosphate (IP3) and diacylglycerol (Carter et al. 1991, Kim et al. 2004). IP3 binds receptors on the endoplasmic reticulum and causes release of Ca2+ ions from the ER into the cytosol. The depletion of calcium from the ER in turn activates STIM1 to interact with ORAI and TRPC1 channels (and possibly other TRP channels) in the plasma membrane, resulting in an influx of extracellular calcium ions (Mori et al. 2002, Muik et al. 2008, Luik et al. 2008, Park et al. 2009)

BioGRID
IntAct
MINT
ALL

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Interacting partner	Detection method	Interaction type	PubMed IDs	Interaction Score	Source
ABL1	Affinity Capture-Western	physical	8692915, (Europe PMC)	NA	BioGRID
AIMP1	Co-fractionation	physical	26344197, (Europe PMC)	NA	BioGRID
BCR	Affinity Capture-MS, Affinity Capture-Western	physical	27432908, 9788431, (Europe PMC)	NA	BioGRID
BLNK	Affinity Capture-Western	physical	11356834, (Europe PMC)	NA	BioGRID
BRIX1	Affinity Capture-MS	physical	27432908, (Europe PMC)	NA	BioGRID
C8orf33	Affinity Capture-MS	physical	27432908, (Europe PMC)	NA	BioGRID
CAV1	Affinity Capture-Western, coimmunoprecipitation, cosedimentation through density gradient	colocalization, physical, physical association	12176037, (Europe PMC)	0.50	BioGRID, IntAct, MINT
CBL	Affinity Capture-Western	physical	12176909, (Europe PMC)	NA	BioGRID
CD22	Affinity Capture-Western, Biochemical Activity, coimmunoprecipitation	association, physical, physical association	10228003, 11356834, 11551923, 8627166, 9890995, (Europe PMC)	0.50	BioGRID, IntAct
CD33	Affinity Capture-Western, Reconstituted Complex, anti bait coimmunoprecipitation, coimmunoprecipitation, enzymatic study, pull down	association, physical, physical association	10206955, 10556798, 17947393, (Europe PMC)	0.77	BioGRID, IntAct, MINT
CD5	Affinity Capture-Western	physical	10082557, (Europe PMC)	NA	BioGRID
CD72	Affinity Capture-Western, Reconstituted Complex	physical	11114375, 12882840, 9590210, (Europe PMC)	NA	BioGRID
CDK1	Biochemical Activity	physical	14699166, (Europe PMC)	NA	BioGRID
CLTCL1	Affinity Capture-MS	physical	27432908, (Europe PMC)	NA	BioGRID
CSF2RB	Affinity Capture-Western, Reconstituted Complex, experimental interaction detection, pull down	association, physical	7528537, 8246974, 9162089, (Europe PMC)	0.47	BioGRID, IntAct, MINT
CTNND1	Affinity Capture-MS, Affinity Capture-Western, Reconstituted Complex	physical	10835420, (Europe PMC)	NA	BioGRID
CXCR4	Affinity Capture-Western	physical	10506573, (Europe PMC)	NA	BioGRID
DARS	Co-fractionation	physical	26344197, (Europe PMC)	NA	BioGRID
DIMT1	Affinity Capture-MS	physical	27432908, (Europe PMC)	NA	BioGRID
DUSP18	Affinity Capture-MS	physical	27880917, (Europe PMC)	NA	BioGRID
EBNA1BP2	Affinity Capture-MS	physical	27432908, (Europe PMC)	NA	BioGRID
EGFR	Affinity Capture-Western, Reconstituted Complex, Two-hybrid, pull down	association, physical	28065597, 7673163, 9733788, (Europe PMC)	0.35	BioGRID, IntAct, MINT
EPOR	Affinity Capture-Western, Reconstituted Complex, affinity chromatography technology, anti bait coimmunoprecipitation, experimental interaction detection, pull down	association, direct interaction, physical, physical association	7228577, 7528537, 7528577, 7889566, (Europe PMC)	0.80	BioGRID, IntAct, MINT
ERBB2	Affinity Capture-Western, Two-hybrid	physical	28065597, (Europe PMC)	NA	BioGRID
ERBB3	Two-hybrid	physical	28065597, (Europe PMC)	NA	BioGRID
ERBB4	Biochemical Activity, Two-hybrid	physical	28065597, (Europe PMC)	NA	BioGRID
FCRL3	Affinity Capture-Western, Reconstituted Complex	physical	12051764, (Europe PMC)	NA	BioGRID
FGFR2	Two-hybrid	physical	28065597, (Europe PMC)	NA	BioGRID
FGFR4	Two-hybrid	physical	28065597, (Europe PMC)	NA	BioGRID
FGFRL1	Affinity Capture-Western	physical	23640895, (Europe PMC)	NA	BioGRID
FHL3	Two-hybrid, two hybrid array, two hybrid prey pooling approach, validated two hybrid	physical, physical association	25416956, (Europe PMC)	0.56	BioGRID, IntAct
GAB2	Affinity Capture-Western	physical	11895767, (Europe PMC)	NA	BioGRID
GADD45GIP1	Affinity Capture-MS	physical	27432908, (Europe PMC)	NA	BioGRID
GRB2	Affinity Capture-Western, anti tag coimmunoprecipitation, far western blotting, two hybrid	physical, physical association	10660620, 10747947, 11964172, 25535246, 8632004, (Europe PMC)	0.65	BioGRID, IntAct, MINT
H1FX-AS1	Affinity Capture-MS	physical	27432908, (Europe PMC)	NA	BioGRID
HOXA10	Affinity Capture-Western, Biochemical Activity, Reconstituted Complex	physical	12145285, (Europe PMC)	NA	BioGRID
IGF1R	Affinity Capture-Western, Two-hybrid	physical	28065597, (Europe PMC)	NA	BioGRID
IL4R	Affinity Capture-Western, Reconstituted Complex, pull down	association, physical	11714803, 27742835, 9392697, (Europe PMC)	0.53	BioGRID, IntAct, MINT
IL6ST	Affinity Capture-Western	physical	10800945, (Europe PMC)	NA	BioGRID
INSR	Affinity Capture-Western	physical	7512963, (Europe PMC)	NA	BioGRID
JAK1	Biochemical Activity	physical	7629131, (Europe PMC)	NA	BioGRID
JAK2	Affinity Capture-Western	physical	10772872, 8943354, (Europe PMC)	NA	BioGRID
KDR	Two-hybrid, anti bait coimmunoprecipitation	physical, physical association	18377662, 28065597, (Europe PMC)	0.40	BioGRID, IntAct
KIT	Affinity Capture-Western, Reconstituted Complex, anti tag coimmunoprecipitation	physical, physical association	12614164, 7684496, 9528781, (Europe PMC)	0.40	BioGRID, IntAct, MINT
LAIR1	Affinity Capture-Western, Reconstituted Complex, Two-hybrid, coimmunoprecipitation, pull down, two hybrid	association, physical, physical association	10660620, 10764762, 10903717, 11160222, 15703304, 9285412, (Europe PMC)	0.61	BioGRID, IntAct, MINT
LAT	Affinity Capture-Western, FRET	physical	27221712, (Europe PMC)	NA	BioGRID
LCK	Biochemical Activity, Reconstituted Complex, phosphatase assay, protein kinase assay	dephosphorylation reaction, phosphorylation reaction, physical	10617656, 11294838, 19167335, 8114715, (Europe PMC)	0.62	BioGRID, IntAct, MINT
LCP2	Affinity Capture-Western, Reconstituted Complex	physical	8760799, 9765283, (Europe PMC)	NA	BioGRID
LIFR	Affinity Capture-Western	physical	10800945, (Europe PMC)	NA	BioGRID
LILRB1	Affinity Capture-Western, anti bait coimmunoprecipitation	physical, physical association	18802077, 9842885, (Europe PMC)	0.40	BioGRID, IntAct
LILRB2	Affinity Capture-Western, anti bait coimmunoprecipitation	physical, physical association	18802077, 9531263, 9842885, (Europe PMC)	0.40	BioGRID, IntAct
LMTK2	Two-hybrid	physical	28065597, (Europe PMC)	NA	BioGRID
LYN	Reconstituted Complex, anti bait coimmunoprecipitation	physical, physical association	10574931, 22624718, (Europe PMC)	0.40	BioGRID, IntAct
MACROD1	Affinity Capture-MS	physical	27432908, (Europe PMC)	NA	BioGRID
MPIG6B	Affinity Capture-Western	physical	11544253, (Europe PMC)	NA	BioGRID
NMNAT1	Affinity Capture-MS	physical	27432908, (Europe PMC)	NA	BioGRID
NOS1	Affinity Capture-Western	physical	11511520, (Europe PMC)	NA	BioGRID
NSUN7	Affinity Capture-MS	physical	26186194, 28514442, (Europe PMC)	NA	BioGRID
NUDT16	Affinity Capture-MS	physical	27432908, (Europe PMC)	NA	BioGRID
OLIG1	Two-hybrid, two hybrid array, validated two hybrid	physical, physical association	25814554, (Europe PMC)	0.49	BioGRID, IntAct
PA2G4	Affinity Capture-MS	physical	27432908, (Europe PMC)	NA	BioGRID
PAG1	Reconstituted Complex	physical	10790433, (Europe PMC)	NA	BioGRID
PANK4	Co-fractionation	physical	22939629, (Europe PMC)	NA	BioGRID
PECAM1	Affinity Capture-Western, Far Western, Reconstituted Complex, pull down, surface plasmon resonance	association, physical	10350061, 9774457, (Europe PMC)	0.46	BioGRID, IntAct, MINT
PFKP	Co-fractionation	physical	26344197, (Europe PMC)	NA	BioGRID
PIK3R1	Two-hybrid, coimmunoprecipitation, pull down	association, physical	10488096, 11160222, (Europe PMC)	0.46	BioGRID, IntAct, MINT
PILRA	Affinity Capture-Western, Reconstituted Complex, Two-hybrid, anti tag coimmunoprecipitation, surface plasmon resonance, two hybrid	physical, physical association	10660620, 10903717, (Europe PMC)	0.58	BioGRID, IntAct
PLCG1	Affinity Capture-Western	physical	27221712, (Europe PMC)	NA	BioGRID
PLCG2	Affinity Capture-Western, FRET	physical	27221712, (Europe PMC)	NA	BioGRID
PRKCD	Affinity Capture-Western, Biochemical Activity, Reconstituted Complex	physical	11723252, (Europe PMC)	NA	BioGRID
PTK2	Affinity Capture-Luminescence, Two-hybrid, luminescence based mammalian interactome mapping, two hybrid array, validated two hybrid	physical, physical association	25814554, (Europe PMC)	0.57	BioGRID, IntAct
PTK2B	Affinity Capture-Western, Biochemical Activity	physical	10521452, 10747947, (Europe PMC)	NA	BioGRID
PTK7	Two-hybrid	physical	28065597, (Europe PMC)	NA	BioGRID
PTPN11	Affinity Capture-MS	physical	27432908, (Europe PMC)	NA	BioGRID
PTPN12	Affinity Capture-MS	physical	27432908, 28514442, (Europe PMC)	NA	BioGRID
PTPN2	Co-fractionation	physical	26344197, (Europe PMC)	NA	BioGRID
PTPN6	Affinity Capture-MS	physical	27432908, (Europe PMC)	NA	BioGRID
ROR1	Two-hybrid	physical	28065597, (Europe PMC)	NA	BioGRID
ROR2	Two-hybrid	physical	28065597, (Europe PMC)	NA	BioGRID
ROS1	Affinity Capture-Western, Biochemical Activity, Two-hybrid, coimmunoprecipitation, phosphatase assay, pull down	association, dephosphorylation reaction, physical	11266449, 17416557, (Europe PMC)	0.64	BioGRID, IntAct, MINT
RPF2	Affinity Capture-MS	physical	27432908, (Europe PMC)	NA	BioGRID
RPL18A	Affinity Capture-MS	physical	27432908, (Europe PMC)	NA	BioGRID
RPL22L1	Affinity Capture-MS	physical	27432908, (Europe PMC)	NA	BioGRID
RPL30	Affinity Capture-MS	physical	27432908, (Europe PMC)	NA	BioGRID
RPL35A	Affinity Capture-MS	physical	27432908, (Europe PMC)	NA	BioGRID
RPL36AL	Affinity Capture-MS	physical	27432908, (Europe PMC)	NA	BioGRID
RPL37A	Affinity Capture-MS	physical	27432908, (Europe PMC)	NA	BioGRID
RPL7L1	Affinity Capture-MS	physical	27432908, (Europe PMC)	NA	BioGRID
RPP30	Affinity Capture-MS	physical	27432908, (Europe PMC)	NA	BioGRID
RPS10P5	Affinity Capture-MS	physical	27432908, (Europe PMC)	NA	BioGRID
RPS19BP1	Affinity Capture-MS	physical	27432908, (Europe PMC)	NA	BioGRID
RRS1	Affinity Capture-MS	physical	27432908, (Europe PMC)	NA	BioGRID
SAMD4B	Co-fractionation	physical	22939629, (Europe PMC)	NA	BioGRID
SIGLEC11	Affinity Capture-Western	physical	11986327, (Europe PMC)	NA	BioGRID
SIGLEC7	Affinity Capture-Western	physical	15703304, (Europe PMC)	NA	BioGRID
SIGLEC9	Affinity Capture-Western	physical	15703304, (Europe PMC)	NA	BioGRID
SIRPA	Co-crystal Structure, Two-hybrid, two hybrid	physical, physical association	10660565, 10660620, (Europe PMC)	0.37	BioGRID, IntAct
SLAMF6	Affinity Capture-Western, anti bait coimmunoprecipitation	association, physical	11489943, (Europe PMC)	0.35	BioGRID, IntAct
SMAD3	Affinity Capture-MS, tandem affinity purification	physical, physical association	18729074, (Europe PMC)	0.40	BioGRID, IntAct
SOS1	Affinity Capture-Western	physical	8632004, (Europe PMC)	NA	BioGRID
SRC	Biochemical Activity	physical	14699166, (Europe PMC)	NA	BioGRID
SRP14	Affinity Capture-MS	physical	27432908, (Europe PMC)	NA	BioGRID
SRSF5	Affinity Capture-MS	physical	27432908, (Europe PMC)	NA	BioGRID
SSTR2	Affinity Capture-Western	physical	9305905, (Europe PMC)	NA	BioGRID
STAT5B	Affinity Capture-Western	physical	9211920, (Europe PMC)	NA	BioGRID
SYK	Affinity Capture-Western, Biochemical Activity	physical	10072516, 10747947, (Europe PMC)	NA	BioGRID
TREML1	Affinity Capture-Western	physical	12393607, (Europe PMC)	NA	BioGRID
TRIP6	Co-fractionation	physical	26344197, (Europe PMC)	NA	BioGRID
TXN	Affinity Capture-Western	physical	19561639, (Europe PMC)	NA	BioGRID
TYK2	Affinity Capture-Western, Biochemical Activity	physical	7629131, (Europe PMC)	NA	BioGRID
VARS	Co-fractionation	physical	26344197, (Europe PMC)	NA	BioGRID
VAV1	Reconstituted Complex	physical	8632004, (Europe PMC)	NA	BioGRID
ZAP70	Reconstituted Complex	physical	8638162, (Europe PMC)	NA	BioGRID

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Interacting partner	Detection method	Interaction type	PubMed IDs	Interaction Score	Source
BTLA	coimmunoprecipitation	association	14652006, (Europe PMC)	0.35	IntAct, MINT
CAMK1	anti bait coimmunoprecipitation	physical association	25915125, (Europe PMC)	0.40	IntAct
CASP8	anti bait coimmunoprecipitation, anti tag coimmunoprecipitation	physical association	18086677, (Europe PMC)	0.52	IntAct, MINT
CAV1	Affinity Capture-Western, coimmunoprecipitation, cosedimentation through density gradient	colocalization, physical, physical association	12176037, (Europe PMC)	0.50	BioGRID, IntAct, MINT
CD22	Affinity Capture-Western, Biochemical Activity, coimmunoprecipitation	association, physical, physical association	10228003, 11356834, 11551923, 8627166, 9890995, (Europe PMC)	0.50	BioGRID, IntAct
CD244	anti bait coimmunoprecipitation, pull down	association, physical association	11489943, 24642916, (Europe PMC)	0.56	IntAct
CD300A	anti bait coimmunoprecipitation	association	11489943, (Europe PMC)	0.35	IntAct
CD300LF	coimmunoprecipitation	association	15549731, (Europe PMC)	0.35	IntAct, MINT
CD33	Affinity Capture-Western, Reconstituted Complex, anti bait coimmunoprecipitation, coimmunoprecipitation, enzymatic study, pull down	association, physical, physical association	10206955, 10556798, 17947393, (Europe PMC)	0.77	BioGRID, IntAct, MINT
CD37	anti bait coimmunoprecipitation	association, physical association	22624718, (Europe PMC)	0.50	IntAct
CDH2	phosphatase assay	dephosphorylation reaction	19167335, (Europe PMC)	0.44	IntAct
CSF2RB	Affinity Capture-Western, Reconstituted Complex, experimental interaction detection, pull down	association, physical	7528537, 8246974, 9162089, (Europe PMC)	0.47	BioGRID, IntAct, MINT
DUSP22	pull down	association	28330616, (Europe PMC)	0.35	IntAct
EGFR	Affinity Capture-Western, Reconstituted Complex, Two-hybrid, pull down	association, physical	28065597, 7673163, 9733788, (Europe PMC)	0.35	BioGRID, IntAct, MINT
EPOR	Affinity Capture-Western, Reconstituted Complex, affinity chromatography technology, anti bait coimmunoprecipitation, experimental interaction detection, pull down	association, direct interaction, physical, physical association	7228577, 7528537, 7528577, 7889566, (Europe PMC)	0.80	BioGRID, IntAct, MINT
ESR1	phosphatase assay	dephosphorylation reaction	7539106, (Europe PMC)	0.44	IntAct, MINT
FCGR2B	proteinchip(r) on a surface-enhanced laser desorption/ionization, affinity chromatography technology, pull down	association, physical association	8577729, 9148918, 9603468, (Europe PMC)	0.67	IntAct, MINT
FHL3	Two-hybrid, two hybrid array, two hybrid prey pooling approach, validated two hybrid	physical, physical association	25416956, (Europe PMC)	0.56	BioGRID, IntAct
GRB2	Affinity Capture-Western, anti tag coimmunoprecipitation, far western blotting, two hybrid	physical, physical association	10660620, 10747947, 11964172, 25535246, 8632004, (Europe PMC)	0.65	BioGRID, IntAct, MINT
IL4R	Affinity Capture-Western, Reconstituted Complex, pull down	association, physical	11714803, 27742835, 9392697, (Europe PMC)	0.53	BioGRID, IntAct, MINT
KDR	Two-hybrid, anti bait coimmunoprecipitation	physical, physical association	18377662, 28065597, (Europe PMC)	0.40	BioGRID, IntAct
KHDRBS1	coimmunoprecipitation	physical association	9045636, (Europe PMC)	0.40	IntAct
KIR2DL1	coimmunoprecipitation, pull down	association	8691146, (Europe PMC)	0.46	IntAct, MINT
KIR2DL3	affinity chromatography technology, coimmunoprecipitation, pull down, surface plasmon resonance	association, direct interaction, physical association	8574854, 8648092, 8691154, 9148918, (Europe PMC)	0.82	IntAct, MINT
KIT	Affinity Capture-Western, Reconstituted Complex, anti tag coimmunoprecipitation	physical, physical association	12614164, 7684496, 9528781, (Europe PMC)	0.40	BioGRID, IntAct, MINT
LAIR1	Affinity Capture-Western, Reconstituted Complex, Two-hybrid, coimmunoprecipitation, pull down, two hybrid	association, physical, physical association	10660620, 10764762, 10903717, 11160222, 15703304, 9285412, (Europe PMC)	0.61	BioGRID, IntAct, MINT
LCK	Biochemical Activity, Reconstituted Complex, phosphatase assay, protein kinase assay	dephosphorylation reaction, phosphorylation reaction, physical	10617656, 11294838, 19167335, 8114715, (Europe PMC)	0.62	BioGRID, IntAct, MINT
LILRB1	Affinity Capture-Western, anti bait coimmunoprecipitation	physical, physical association	18802077, 9842885, (Europe PMC)	0.40	BioGRID, IntAct
LILRB2	Affinity Capture-Western, anti bait coimmunoprecipitation	physical, physical association	18802077, 9531263, 9842885, (Europe PMC)	0.40	BioGRID, IntAct
LILRB3	anti bait coimmunoprecipitation	physical association	18802077, (Europe PMC)	0.40	IntAct
LILRB4	anti bait coimmunoprecipitation	physical association	18802077, (Europe PMC)	0.40	IntAct
LYN	Reconstituted Complex, anti bait coimmunoprecipitation	physical, physical association	10574931, 22624718, (Europe PMC)	0.40	BioGRID, IntAct
MAP3K4	experimental interaction detection, imaging technique	colocalization, dephosphorylation reaction	15601262, (Europe PMC)	0.40	IntAct, MINT
MPIG6B	coimmunoprecipitation	association	11544253, (Europe PMC)	0.35	IntAct, MINT
NFAT5	anti bait coimmunoprecipitation, anti tag coimmunoprecipitation, protein phosphatase assay	dephosphorylation reaction, physical association	20351292, (Europe PMC)	0.60	IntAct
NTRK1	anti bait coimmunoprecipitation	physical association	15557341, (Europe PMC)	0.40	IntAct, MINT
OLIG1	Two-hybrid, two hybrid array, validated two hybrid	physical, physical association	25814554, (Europe PMC)	0.49	BioGRID, IntAct
PDCD1	coimmunoprecipitation	association	15240681, (Europe PMC)	0.35	IntAct, MINT
PDGFRB	phosphatase assay	dephosphorylation reaction	19167335, (Europe PMC)	0.44	IntAct
PECAM1	Affinity Capture-Western, Far Western, Reconstituted Complex, pull down, surface plasmon resonance	association, physical	10350061, 9774457, (Europe PMC)	0.46	BioGRID, IntAct, MINT
PIK3R1	Two-hybrid, coimmunoprecipitation, pull down	association, physical	10488096, 11160222, (Europe PMC)	0.46	BioGRID, IntAct, MINT
PILRA	Affinity Capture-Western, Reconstituted Complex, Two-hybrid, anti tag coimmunoprecipitation, surface plasmon resonance, two hybrid	physical, physical association	10660620, 10903717, (Europe PMC)	0.58	BioGRID, IntAct
PSMC5	pull down	association	28330616, (Europe PMC)	0.35	IntAct
PSMD1	pull down	association	28330616, (Europe PMC)	0.35	IntAct
PSMD11	pull down	association	28330616, (Europe PMC)	0.35	IntAct
PSMD13	pull down	association	28330616, (Europe PMC)	0.35	IntAct
PSMD2	pull down	association	28330616, (Europe PMC)	0.35	IntAct
PSMD3	pull down	association	28330616, (Europe PMC)	0.35	IntAct
PSMD4	pull down	association	28330616, (Europe PMC)	0.35	IntAct
PSMD7	pull down	association	28330616, (Europe PMC)	0.35	IntAct
PTK2	Affinity Capture-Luminescence, Two-hybrid, luminescence based mammalian interactome mapping, two hybrid array, validated two hybrid	physical, physical association	25814554, (Europe PMC)	0.57	BioGRID, IntAct
ROS1	Affinity Capture-Western, Biochemical Activity, Two-hybrid, coimmunoprecipitation, phosphatase assay, pull down	association, dephosphorylation reaction, physical	11266449, 17416557, (Europe PMC)	0.64	BioGRID, IntAct, MINT
SH3BP2	pull down, surface plasmon resonance	association	16649996, (Europe PMC)	0.46	IntAct, MINT
SIGLEC10	biochemical	association	12163025, (Europe PMC)	0.35	IntAct, MINT
SIRPA	Co-crystal Structure, Two-hybrid, two hybrid	physical, physical association	10660565, 10660620, (Europe PMC)	0.37	BioGRID, IntAct
SLAMF6	Affinity Capture-Western, anti bait coimmunoprecipitation	association, physical	11489943, (Europe PMC)	0.35	BioGRID, IntAct
SMAD3	Affinity Capture-MS, tandem affinity purification	physical, physical association	18729074, (Europe PMC)	0.40	BioGRID, IntAct
TFG	pull down	physical association	15557341, (Europe PMC)	0.40	IntAct, MINT
THEMIS	anti bait coimmunoprecipitation, pull down	association, physical association	25535246, (Europe PMC)	0.50	IntAct, MINT
TMEM62	two hybrid pooling approach	physical association	16169070, (Europe PMC)	0.37	IntAct
TNFRSF1A	pull down	association	11786908, (Europe PMC)	0.35	IntAct, MINT

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Interacting partner	Detection method	Interaction type	PubMed IDs	Interaction Score	Source
CASP8	anti bait coimmunoprecipitation, anti tag coimmunoprecipitation	physical association	18086677, (Europe PMC)	0.52	IntAct, MINT
CAV1	Affinity Capture-Western, coimmunoprecipitation, cosedimentation through density gradient	colocalization, physical, physical association	12176037, (Europe PMC)	0.50	BioGRID, IntAct, MINT
CD300LF	coimmunoprecipitation	association	15549731, (Europe PMC)	0.35	IntAct, MINT
CD33	Affinity Capture-Western, Reconstituted Complex, anti bait coimmunoprecipitation, coimmunoprecipitation, enzymatic study, pull down	association, physical, physical association	10206955, 10556798, 17947393, (Europe PMC)	0.77	BioGRID, IntAct, MINT
CSF2RB	Affinity Capture-Western, Reconstituted Complex, experimental interaction detection, pull down	association, physical	7528537, 8246974, 9162089, (Europe PMC)	0.47	BioGRID, IntAct, MINT
EGFR	Affinity Capture-Western, Reconstituted Complex, Two-hybrid, pull down	association, physical	28065597, 7673163, 9733788, (Europe PMC)	0.35	BioGRID, IntAct, MINT
EPOR	Affinity Capture-Western, Reconstituted Complex, affinity chromatography technology, anti bait coimmunoprecipitation, experimental interaction detection, pull down	association, direct interaction, physical, physical association	7228577, 7528537, 7528577, 7889566, (Europe PMC)	0.80	BioGRID, IntAct, MINT
ESR1	phosphatase assay	dephosphorylation reaction	7539106, (Europe PMC)	0.44	IntAct, MINT
FCGR2B	proteinchip(r) on a surface-enhanced laser desorption/ionization, affinity chromatography technology, pull down	association, physical association	8577729, 9148918, 9603468, (Europe PMC)	0.67	IntAct, MINT
GRB2	Affinity Capture-Western, anti tag coimmunoprecipitation, far western blotting, two hybrid	physical, physical association	10660620, 10747947, 11964172, 25535246, 8632004, (Europe PMC)	0.65	BioGRID, IntAct, MINT
IL4R	Affinity Capture-Western, Reconstituted Complex, pull down	association, physical	11714803, 27742835, 9392697, (Europe PMC)	0.53	BioGRID, IntAct, MINT
KIR2DL1	coimmunoprecipitation, pull down	association	8691146, (Europe PMC)	0.46	IntAct, MINT
KIR2DL3	affinity chromatography technology, coimmunoprecipitation, pull down, surface plasmon resonance	association, direct interaction, physical association	8574854, 8648092, 8691154, 9148918, (Europe PMC)	0.82	IntAct, MINT
KIT	Affinity Capture-Western, Reconstituted Complex, anti tag coimmunoprecipitation	physical, physical association	12614164, 7684496, 9528781, (Europe PMC)	0.40	BioGRID, IntAct, MINT
LAIR1	Affinity Capture-Western, Reconstituted Complex, Two-hybrid, coimmunoprecipitation, pull down, two hybrid	association, physical, physical association	10660620, 10764762, 10903717, 11160222, 15703304, 9285412, (Europe PMC)	0.61	BioGRID, IntAct, MINT
LCK	Biochemical Activity, Reconstituted Complex, phosphatase assay, protein kinase assay	dephosphorylation reaction, phosphorylation reaction, physical	10617656, 11294838, 19167335, 8114715, (Europe PMC)	0.62	BioGRID, IntAct, MINT
MAP3K4	experimental interaction detection, imaging technique	colocalization, dephosphorylation reaction	15601262, (Europe PMC)	0.40	IntAct, MINT
MPIG6B	coimmunoprecipitation	association	11544253, (Europe PMC)	0.35	IntAct, MINT
NTRK1	anti bait coimmunoprecipitation	physical association	15557341, (Europe PMC)	0.40	IntAct, MINT
PDCD1	coimmunoprecipitation	association	15240681, (Europe PMC)	0.35	IntAct, MINT
PECAM1	Affinity Capture-Western, Far Western, Reconstituted Complex, pull down, surface plasmon resonance	association, physical	10350061, 9774457, (Europe PMC)	0.46	BioGRID, IntAct, MINT
PIK3R1	Two-hybrid, coimmunoprecipitation, pull down	association, physical	10488096, 11160222, (Europe PMC)	0.46	BioGRID, IntAct, MINT
ROS1	Affinity Capture-Western, Biochemical Activity, Two-hybrid, coimmunoprecipitation, phosphatase assay, pull down	association, dephosphorylation reaction, physical	11266449, 17416557, (Europe PMC)	0.64	BioGRID, IntAct, MINT
SH3BP2	pull down, surface plasmon resonance	association	16649996, (Europe PMC)	0.46	IntAct, MINT
SIGLEC10	biochemical	association	12163025, (Europe PMC)	0.35	IntAct, MINT
TFG	pull down	physical association	15557341, (Europe PMC)	0.40	IntAct, MINT
THEMIS	anti bait coimmunoprecipitation, pull down	association, physical association	25535246, (Europe PMC)	0.50	IntAct, MINT
TNFRSF1A	pull down	association	11786908, (Europe PMC)	0.35	IntAct, MINT

Visualize Download

Interacting partner	Detection method	Interaction type	PubMed IDs	Interaction Score	Source
ABL1	Affinity Capture-Western	physical	8692915, (Europe PMC)	NA	BioGRID
AIMP1	Co-fractionation	physical	26344197, (Europe PMC)	NA	BioGRID
ANXA1	anti bait coimmunoprecipitation	association	23754495, (Europe PMC)	0.35	IntAct
BCR	Affinity Capture-MS, Affinity Capture-Western	physical	27432908, 9788431, (Europe PMC)	NA	BioGRID
BLNK	Affinity Capture-Western	physical	11356834, (Europe PMC)	NA	BioGRID
BRIX1	Affinity Capture-MS	physical	27432908, (Europe PMC)	NA	BioGRID
BTLA	coimmunoprecipitation	association	14652006, (Europe PMC)	0.35	IntAct, MINT
C8orf33	Affinity Capture-MS	physical	27432908, (Europe PMC)	NA	BioGRID
CAMK1	anti bait coimmunoprecipitation	physical association	25915125, (Europe PMC)	0.40	IntAct
CASP8	anti bait coimmunoprecipitation, anti tag coimmunoprecipitation	physical association	18086677, (Europe PMC)	0.52	IntAct, MINT
CAV1	Affinity Capture-Western, coimmunoprecipitation, cosedimentation through density gradient	colocalization, physical, physical association	12176037, (Europe PMC)	0.50	BioGRID, IntAct, MINT
CBL	Affinity Capture-Western	physical	12176909, (Europe PMC)	NA	BioGRID
CD22	Affinity Capture-Western, Biochemical Activity, coimmunoprecipitation	association, physical, physical association	10228003, 11356834, 11551923, 8627166, 9890995, (Europe PMC)	0.50	BioGRID, IntAct
CD244	anti bait coimmunoprecipitation, pull down	association, physical association	11489943, 24642916, (Europe PMC)	0.56	IntAct
CD300A	anti bait coimmunoprecipitation	association	11489943, (Europe PMC)	0.35	IntAct
CD300LF	coimmunoprecipitation	association	15549731, (Europe PMC)	0.35	IntAct, MINT
CD33	Affinity Capture-Western, Reconstituted Complex, anti bait coimmunoprecipitation, coimmunoprecipitation, enzymatic study, pull down	association, physical, physical association	10206955, 10556798, 17947393, (Europe PMC)	0.77	BioGRID, IntAct, MINT
CD37	anti bait coimmunoprecipitation	association, physical association	22624718, (Europe PMC)	0.50	IntAct
CD5	Affinity Capture-Western	physical	10082557, (Europe PMC)	NA	BioGRID
CD72	Affinity Capture-Western, Reconstituted Complex	physical	11114375, 12882840, 9590210, (Europe PMC)	NA	BioGRID
CDH2	phosphatase assay	dephosphorylation reaction	19167335, (Europe PMC)	0.44	IntAct
CDK1	Biochemical Activity	physical	14699166, (Europe PMC)	NA	BioGRID
CLTCL1	Affinity Capture-MS	physical	27432908, (Europe PMC)	NA	BioGRID
CSF2RB	Affinity Capture-Western, Reconstituted Complex, experimental interaction detection, pull down	association, physical	7528537, 8246974, 9162089, (Europe PMC)	0.47	BioGRID, IntAct, MINT
CTNND1	Affinity Capture-MS, Affinity Capture-Western, Reconstituted Complex	physical	10835420, (Europe PMC)	NA	BioGRID
CXCR4	Affinity Capture-Western	physical	10506573, (Europe PMC)	NA	BioGRID
DARS	Co-fractionation	physical	26344197, (Europe PMC)	NA	BioGRID
DIMT1	Affinity Capture-MS	physical	27432908, (Europe PMC)	NA	BioGRID
DUSP18	Affinity Capture-MS	physical	27880917, (Europe PMC)	NA	BioGRID
DUSP22	pull down	association	28330616, (Europe PMC)	0.35	IntAct
EBNA1BP2	Affinity Capture-MS	physical	27432908, (Europe PMC)	NA	BioGRID
EGFR	Affinity Capture-Western, Reconstituted Complex, Two-hybrid, pull down	association, physical	28065597, 7673163, 9733788, (Europe PMC)	0.35	BioGRID, IntAct, MINT
EPOR	Affinity Capture-Western, Reconstituted Complex, affinity chromatography technology, anti bait coimmunoprecipitation, experimental interaction detection, pull down	association, direct interaction, physical, physical association	7228577, 7528537, 7528577, 7889566, (Europe PMC)	0.80	BioGRID, IntAct, MINT
ERBB2	Affinity Capture-Western, Two-hybrid	physical	28065597, (Europe PMC)	NA	BioGRID
ERBB3	Two-hybrid	physical	28065597, (Europe PMC)	NA	BioGRID
ERBB4	Biochemical Activity, Two-hybrid	physical	28065597, (Europe PMC)	NA	BioGRID
ESR1	phosphatase assay	dephosphorylation reaction	7539106, (Europe PMC)	0.44	IntAct, MINT
FCGR2B	proteinchip(r) on a surface-enhanced laser desorption/ionization, affinity chromatography technology, pull down	association, physical association	8577729, 9148918, 9603468, (Europe PMC)	0.67	IntAct, MINT
FCRL3	Affinity Capture-Western, Reconstituted Complex	physical	12051764, (Europe PMC)	NA	BioGRID
FGFR2	Two-hybrid	physical	28065597, (Europe PMC)	NA	BioGRID
FGFR4	Two-hybrid	physical	28065597, (Europe PMC)	NA	BioGRID
FGFRL1	Affinity Capture-Western	physical	23640895, (Europe PMC)	NA	BioGRID
FHL3	Two-hybrid, two hybrid array, two hybrid prey pooling approach, validated two hybrid	physical, physical association	25416956, (Europe PMC)	0.56	BioGRID, IntAct
GAB2	Affinity Capture-Western	physical	11895767, (Europe PMC)	NA	BioGRID
GADD45GIP1	Affinity Capture-MS	physical	27432908, (Europe PMC)	NA	BioGRID
GRB2	Affinity Capture-Western, anti tag coimmunoprecipitation, far western blotting, two hybrid	physical, physical association	10660620, 10747947, 11964172, 25535246, 8632004, (Europe PMC)	0.65	BioGRID, IntAct, MINT
H1FX-AS1	Affinity Capture-MS	physical	27432908, (Europe PMC)	NA	BioGRID
HOXA10	Affinity Capture-Western, Biochemical Activity, Reconstituted Complex	physical	12145285, (Europe PMC)	NA	BioGRID
IGF1R	Affinity Capture-Western, Two-hybrid	physical	28065597, (Europe PMC)	NA	BioGRID
IL4R	Affinity Capture-Western, Reconstituted Complex, pull down	association, physical	11714803, 27742835, 9392697, (Europe PMC)	0.53	BioGRID, IntAct, MINT
IL6ST	Affinity Capture-Western	physical	10800945, (Europe PMC)	NA	BioGRID
INSR	Affinity Capture-Western	physical	7512963, (Europe PMC)	NA	BioGRID
JAK1	Biochemical Activity	physical	7629131, (Europe PMC)	NA	BioGRID
JAK2	Affinity Capture-Western	physical	10772872, 8943354, (Europe PMC)	NA	BioGRID
KDR	Two-hybrid, anti bait coimmunoprecipitation	physical, physical association	18377662, 28065597, (Europe PMC)	0.40	BioGRID, IntAct
KHDRBS1	coimmunoprecipitation	physical association	9045636, (Europe PMC)	0.40	IntAct
KIR2DL1	coimmunoprecipitation, pull down	association	8691146, (Europe PMC)	0.46	IntAct, MINT
KIR2DL3	affinity chromatography technology, coimmunoprecipitation, pull down, surface plasmon resonance	association, direct interaction, physical association	8574854, 8648092, 8691154, 9148918, (Europe PMC)	0.82	IntAct, MINT
KIT	Affinity Capture-Western, Reconstituted Complex, anti tag coimmunoprecipitation	physical, physical association	12614164, 7684496, 9528781, (Europe PMC)	0.40	BioGRID, IntAct, MINT
LAIR1	Affinity Capture-Western, Reconstituted Complex, Two-hybrid, coimmunoprecipitation, pull down, two hybrid	association, physical, physical association	10660620, 10764762, 10903717, 11160222, 15703304, 9285412, (Europe PMC)	0.61	BioGRID, IntAct, MINT
LAT	Affinity Capture-Western, FRET	physical	27221712, (Europe PMC)	NA	BioGRID
LCK	Biochemical Activity, Reconstituted Complex, phosphatase assay, protein kinase assay	dephosphorylation reaction, phosphorylation reaction, physical	10617656, 11294838, 19167335, 8114715, (Europe PMC)	0.62	BioGRID, IntAct, MINT
LCP2	Affinity Capture-Western, Reconstituted Complex	physical	8760799, 9765283, (Europe PMC)	NA	BioGRID
LIFR	Affinity Capture-Western	physical	10800945, (Europe PMC)	NA	BioGRID
LILRB1	Affinity Capture-Western, anti bait coimmunoprecipitation	physical, physical association	18802077, 9842885, (Europe PMC)	0.40	BioGRID, IntAct
LILRB2	Affinity Capture-Western, anti bait coimmunoprecipitation	physical, physical association	18802077, 9531263, 9842885, (Europe PMC)	0.40	BioGRID, IntAct
LILRB3	anti bait coimmunoprecipitation	physical association	18802077, (Europe PMC)	0.40	IntAct
LILRB4	anti bait coimmunoprecipitation	physical association	18802077, (Europe PMC)	0.40	IntAct
LMTK2	Two-hybrid	physical	28065597, (Europe PMC)	NA	BioGRID
LYN	Reconstituted Complex, anti bait coimmunoprecipitation	physical, physical association	10574931, 22624718, (Europe PMC)	0.40	BioGRID, IntAct
MACROD1	Affinity Capture-MS	physical	27432908, (Europe PMC)	NA	BioGRID
MAP3K4	experimental interaction detection, imaging technique	colocalization, dephosphorylation reaction	15601262, (Europe PMC)	0.40	IntAct, MINT
MPIG6B	Affinity Capture-Western	physical	11544253, (Europe PMC)	NA	BioGRID
MPIG6B	coimmunoprecipitation	association	11544253, (Europe PMC)	0.35	IntAct, MINT
NFAT5	anti bait coimmunoprecipitation, anti tag coimmunoprecipitation, protein phosphatase assay	dephosphorylation reaction, physical association	20351292, (Europe PMC)	0.60	IntAct
NMNAT1	Affinity Capture-MS	physical	27432908, (Europe PMC)	NA	BioGRID
NOS1	Affinity Capture-Western	physical	11511520, (Europe PMC)	NA	BioGRID
NSUN7	Affinity Capture-MS	physical	26186194, 28514442, (Europe PMC)	NA	BioGRID
NTRK1	anti bait coimmunoprecipitation	physical association	15557341, (Europe PMC)	0.40	IntAct, MINT
NUDT16	Affinity Capture-MS	physical	27432908, (Europe PMC)	NA	BioGRID
OLIG1	Two-hybrid, two hybrid array, validated two hybrid	physical, physical association	25814554, (Europe PMC)	0.49	BioGRID, IntAct
PA2G4	Affinity Capture-MS	physical	27432908, (Europe PMC)	NA	BioGRID
PAG1	Reconstituted Complex	physical	10790433, (Europe PMC)	NA	BioGRID
PANK4	Co-fractionation	physical	22939629, (Europe PMC)	NA	BioGRID
PDCD1	coimmunoprecipitation	association	15240681, (Europe PMC)	0.35	IntAct, MINT
PDGFRB	phosphatase assay	dephosphorylation reaction	19167335, (Europe PMC)	0.44	IntAct
PECAM1	Affinity Capture-Western, Far Western, Reconstituted Complex, pull down, surface plasmon resonance	association, physical	10350061, 9774457, (Europe PMC)	0.46	BioGRID, IntAct, MINT
PFKP	Co-fractionation	physical	26344197, (Europe PMC)	NA	BioGRID
PIK3R1	Two-hybrid, coimmunoprecipitation, pull down	association, physical	10488096, 11160222, (Europe PMC)	0.46	BioGRID, IntAct, MINT
PILRA	Affinity Capture-Western, Reconstituted Complex, Two-hybrid, anti tag coimmunoprecipitation, surface plasmon resonance, two hybrid	physical, physical association	10660620, 10903717, (Europe PMC)	0.58	BioGRID, IntAct
PLCG1	Affinity Capture-Western	physical	27221712, (Europe PMC)	NA	BioGRID
PLCG2	Affinity Capture-Western, FRET	physical	27221712, (Europe PMC)	NA	BioGRID
PRKCD	Affinity Capture-Western, Biochemical Activity, Reconstituted Complex	physical	11723252, (Europe PMC)	NA	BioGRID
PSMC5	pull down	association	28330616, (Europe PMC)	0.35	IntAct
PSMD1	pull down	association	28330616, (Europe PMC)	0.35	IntAct
PSMD11	pull down	association	28330616, (Europe PMC)	0.35	IntAct
PSMD13	pull down	association	28330616, (Europe PMC)	0.35	IntAct
PSMD2	pull down	association	28330616, (Europe PMC)	0.35	IntAct
PSMD3	pull down	association	28330616, (Europe PMC)	0.35	IntAct
PSMD4	pull down	association	28330616, (Europe PMC)	0.35	IntAct
PSMD7	pull down	association	28330616, (Europe PMC)	0.35	IntAct
PTK2	Affinity Capture-Luminescence, Two-hybrid, luminescence based mammalian interactome mapping, two hybrid array, validated two hybrid	physical, physical association	25814554, (Europe PMC)	0.57	BioGRID, IntAct
PTK2B	Affinity Capture-Western, Biochemical Activity	physical	10521452, 10747947, (Europe PMC)	NA	BioGRID
PTK7	Two-hybrid	physical	28065597, (Europe PMC)	NA	BioGRID
PTPN11	Affinity Capture-MS	physical	27432908, (Europe PMC)	NA	BioGRID
PTPN12	Affinity Capture-MS	physical	27432908, 28514442, (Europe PMC)	NA	BioGRID
PTPN2	Co-fractionation	physical	26344197, (Europe PMC)	NA	BioGRID
PTPN6	Affinity Capture-MS	physical	27432908, (Europe PMC)	NA	BioGRID
ROR1	Two-hybrid	physical	28065597, (Europe PMC)	NA	BioGRID
ROR2	Two-hybrid	physical	28065597, (Europe PMC)	NA	BioGRID
ROS1	Affinity Capture-Western, Biochemical Activity, Two-hybrid, coimmunoprecipitation, phosphatase assay, pull down	association, dephosphorylation reaction, physical	11266449, 17416557, (Europe PMC)	0.64	BioGRID, IntAct, MINT
RPF2	Affinity Capture-MS	physical	27432908, (Europe PMC)	NA	BioGRID
RPL18A	Affinity Capture-MS	physical	27432908, (Europe PMC)	NA	BioGRID
RPL22L1	Affinity Capture-MS	physical	27432908, (Europe PMC)	NA	BioGRID
RPL30	Affinity Capture-MS	physical	27432908, (Europe PMC)	NA	BioGRID
RPL35A	Affinity Capture-MS	physical	27432908, (Europe PMC)	NA	BioGRID
RPL36AL	Affinity Capture-MS	physical	27432908, (Europe PMC)	NA	BioGRID
RPL37A	Affinity Capture-MS	physical	27432908, (Europe PMC)	NA	BioGRID
RPL7L1	Affinity Capture-MS	physical	27432908, (Europe PMC)	NA	BioGRID
RPP30	Affinity Capture-MS	physical	27432908, (Europe PMC)	NA	BioGRID
RPS10P5	Affinity Capture-MS	physical	27432908, (Europe PMC)	NA	BioGRID
RPS19BP1	Affinity Capture-MS	physical	27432908, (Europe PMC)	NA	BioGRID
RRS1	Affinity Capture-MS	physical	27432908, (Europe PMC)	NA	BioGRID
SAMD4B	Co-fractionation	physical	22939629, (Europe PMC)	NA	BioGRID
SH3BP2	pull down, surface plasmon resonance	association	16649996, (Europe PMC)	0.46	IntAct, MINT
SIGLEC10	biochemical	association	12163025, (Europe PMC)	0.35	IntAct, MINT
SIGLEC11	Affinity Capture-Western	physical	11986327, (Europe PMC)	NA	BioGRID
SIGLEC7	Affinity Capture-Western	physical	15703304, (Europe PMC)	NA	BioGRID
SIGLEC9	Affinity Capture-Western	physical	15703304, (Europe PMC)	NA	BioGRID
SIRPA	Co-crystal Structure, Two-hybrid, two hybrid	physical, physical association	10660565, 10660620, (Europe PMC)	0.37	BioGRID, IntAct
SLAMF6	Affinity Capture-Western, anti bait coimmunoprecipitation	association, physical	11489943, (Europe PMC)	0.35	BioGRID, IntAct
SMAD3	Affinity Capture-MS, tandem affinity purification	physical, physical association	18729074, (Europe PMC)	0.40	BioGRID, IntAct
SOS1	Affinity Capture-Western	physical	8632004, (Europe PMC)	NA	BioGRID
SRC	Biochemical Activity	physical	14699166, (Europe PMC)	NA	BioGRID
SRP14	Affinity Capture-MS	physical	27432908, (Europe PMC)	NA	BioGRID
SRSF5	Affinity Capture-MS	physical	27432908, (Europe PMC)	NA	BioGRID
SSTR2	Affinity Capture-Western	physical	9305905, (Europe PMC)	NA	BioGRID
STAT5B	Affinity Capture-Western	physical	9211920, (Europe PMC)	NA	BioGRID
SYK	Affinity Capture-Western, Biochemical Activity	physical	10072516, 10747947, (Europe PMC)	NA	BioGRID
TFG	pull down	physical association	15557341, (Europe PMC)	0.40	IntAct, MINT
THEMIS	anti bait coimmunoprecipitation, pull down	association, physical association	25535246, (Europe PMC)	0.50	IntAct, MINT
TMEM62	two hybrid pooling approach	physical association	16169070, (Europe PMC)	0.37	IntAct
TNFRSF1A	pull down	association	11786908, (Europe PMC)	0.35	IntAct, MINT
TREML1	Affinity Capture-Western	physical	12393607, (Europe PMC)	NA	BioGRID
TRIP6	Co-fractionation	physical	26344197, (Europe PMC)	NA	BioGRID
TXN	Affinity Capture-Western	physical	19561639, (Europe PMC)	NA	BioGRID
TYK2	Affinity Capture-Western, Biochemical Activity	physical	7629131, (Europe PMC)	NA	BioGRID
VARS	Co-fractionation	physical	26344197, (Europe PMC)	NA	BioGRID
VAV1	Reconstituted Complex	physical	8632004, (Europe PMC)	NA	BioGRID
ZAP70	Reconstituted Complex	physical	8638162, (Europe PMC)	NA	BioGRID

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PTPN6

Download FASTA sequences of PTPN6-substrates in Humans