DEPOD - human DEPhOsphorylation Database

Basic Information
Phosphatases
Pathway
Interacting Proteins
Phosphorylating Kinases

Gene Name	FYN (QuickGO)	Interactive visualization of FYN structures (A quick tutorial to explore the interctive visulaization) Representative structure: 1NYG
Synonyms	FYN
Protein Name	FYN
Alternative Name(s)	Tyrosine-protein kinase Fyn;2.7.10.2;Proto-oncogene Syn;Proto-oncogene c-Fyn;Src-like kinase;SLK;p59-Fyn;
Protein Family	Belongs to the protein kinase superfamily Tyr proteinkinase family SRC subfamily
EntrezGene ID	2534 (Comparitive Toxicogenomics)
UniProt AC (Human)	P06241 (protein sequence)
Enzyme Class	2.7.10.2 (BRENDA )
Molecular Weight	60762 Dalton
Protein Length	537 amino acids (AA)
Genome Browsers	NCBI \| ENSG00000010810 (Ensembl) \| UCSC
Crosslinking annotations	Query our ID-mapping table
Orthologues	Quest For Orthologues (QFO) \| GeneTree \| eggNOG - KOG0197 \| eggNOG - COG0515
Phosphorylation Network	Visualize

Domain organization, Expression, Diseases

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Localization, Function, Catalytic activity and Sequence

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Localization (UniProt annotation)
Cytoplasm Nucleus Cell membraneNote=Present and active in lipid rafts Palmitoylation is crucialfor proper trafficking
Function (UniProt annotation)
Non-receptor tyrosine-protein kinase that plays a rolein many biological processes including regulation of cell growthand survival, cell adhesion, integrin-mediated signaling,cytoskeletal remodeling, cell motility, immune response and axonguidance Inactive FYN is phosphorylated on its C-terminal tailwithin the catalytic domain Following activation by PKA, theprotein subsequently associates with PTK2/FAK1, allowing PTK2/FAK1phosphorylation, activation and targeting to focal adhesionsInvolved in the regulation of cell adhesion and motility throughphosphorylation of CTNNB1 (beta-catenin) and CTNND1 (delta-catenin) Regulates cytoskeletal remodeling by phosphorylatingseveral proteins including the actin regulator WAS and themicrotubule-associated proteins MAP2 and MAPT Promotes cellsurvival by phosphorylating AGAP2/PIKE-A and preventing itsapoptotic cleavage Participates in signal transduction pathwaysthat regulate the integrity of the glomerular slit diaphragm (anessential part of the glomerular filter of the kidney) byphosphorylating several slit diaphragm components including NPHS1,KIRREL1 and TRPC6 Plays a role in neural processes byphosphorylating DPYSL2, a multifunctional adapter protein withinthe central nervous system, ARHGAP32, a regulator for Rho familyGTPases implicated in various neural functions, and SNCA, a smallpre-synaptic protein Participates in the downstream signalingpathways that lead to T-cell differentiation and proliferationfollowing T-cell receptor (TCR) stimulation PhosphorylatesPTK2B/PYK2 in response to T-cell receptor activation Alsoparticipates in negative feedback regulation of TCR signalingthrough phosphorylation of PAG1, thereby promoting interactionbetween PAG1 and CSK and recruitment of CSK to lipid rafts CSKmaintains LCK and FYN in an inactive form Promotes CD28-inducedphosphorylation of VAV1
Catalytic Activity (UniProt annotation)
ATP + a [protein]-L-tyrosine = ADP + a[protein]-L-tyrosine phosphate
Protein Sequence
MGCVQCKDKEATKLTEERDGSLNQSSGYRYGTDPTPQHYPSFGVTSIPNYNNFHAAGGQGLTVFGGVNSSSHTGTLRTRG GTGVTLFVALYDYEARTEDDLSFHKGEKFQILNSSEGDWWEARSLTTGETGYIPSNYVAPVDSIQAEEWYFGKLGRKDAE RQLLSFGNPRGTFLIRESETTKGAYSLSIRDWDDMKGDHVKHYKIRKLDNGGYYITTRAQFETLQQLVQHYSERAAGLCC RLVVPCHKGMPRLTDLSVKTKDVWEIPRESLQLIKRLGNGQFGEVWMGTWNGNTKVAIKTLKPGTMSPESFLEEAQIMKK LKHDKLVQLYAVVSEEPIYIVTEYMNKGSLLDFLKDGEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGN GLICKIADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQVE RGYRMPCPQDCPISLHELMIHCWKKDPEERPTFEYLQSFLEDYFTATEPQYQPGENL

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:0000165	P:MAPK cascade
GO:0000304	P:response to singlet oxygen
GO:0001764	P:neuron migration
GO:0002223	P:stimulatory C-type lectin receptor signaling pathway
GO:0002250	P:adaptive immune response
GO:0003015	P:heart process
GO:0004713	F:protein tyrosine kinase activity
GO:0004715	F:non-membrane spanning protein tyrosine kinase activity
GO:0005088	F:Ras guanyl-nucleotide exchange factor activity
GO:0005524	F:ATP binding
GO:0005634	C:nucleus
GO:0005739	C:mitochondrion
GO:0005768	C:endosome
GO:0005829	C:cytosol
GO:0005884	C:actin filament
GO:0005886	C:plasma membrane
GO:0006468	P:protein phosphorylation
GO:0006816	P:calcium ion transport
GO:0007169	P:transmembrane receptor protein tyrosine kinase signaling pathway
GO:0007411	P:axon guidance
GO:0007417	P:central nervous system development
GO:0007596	P:blood coagulation
GO:0007612	P:learning
GO:0007631	P:feeding behavior
GO:0008360	P:regulation of cell shape
GO:0010629	P:negative regulation of gene expression
GO:0010730	P:negative regulation of hydrogen peroxide biosynthetic process
GO:0010976	P:positive regulation of neuron projection development
GO:0014068	P:positive regulation of phosphatidylinositol 3-kinase signaling
GO:0014069	C:postsynaptic density
GO:0016477	P:cell migration
GO:0018108	P:peptidyl-tyrosine phosphorylation
GO:0019221	P:cytokine-mediated signaling pathway
GO:0019899	F:enzyme binding
GO:0030154	P:cell differentiation
GO:0030168	P:platelet activation
GO:0030425	C:dendrite
GO:0030900	P:forebrain development
GO:0031234	C:extrinsic component of cytoplasmic side of plasma membrane
GO:0031295	P:T cell costimulation
GO:0031397	P:negative regulation of protein ubiquitination
GO:0031802	F:type 5 metabotropic glutamate receptor binding
GO:0035556	P:intracellular signal transduction
GO:0036120	P:cellular response to platelet-derived growth factor stimulus
GO:0038083	P:peptidyl-tyrosine autophosphorylation
GO:0038096	P:Fc-gamma receptor signaling pathway involved in phagocytosis
GO:0042110	P:T cell activation
GO:0042127	P:regulation of cell proliferation
GO:0042177	P:negative regulation of protein catabolic process
GO:0042531	P:positive regulation of tyrosine phosphorylation of STAT protein
GO:0042542	P:response to hydrogen peroxide
GO:0042608	F:T cell receptor binding
GO:0042609	F:CD4 receptor binding
GO:0042610	F:CD8 receptor binding
GO:0042802	F:identical protein binding
GO:0042981	P:regulation of apoptotic process
GO:0043014	F:alpha-tubulin binding
GO:0043123	P:positive regulation of I-kappaB kinase/NF-kappaB signaling
GO:0043524	P:negative regulation of neuron apoptotic process
GO:0043548	F:phosphatidylinositol 3-kinase binding
GO:0044297	C:cell body
GO:0044325	F:ion channel binding
GO:0045087	P:innate immune response
GO:0045121	C:membrane raft
GO:0045471	P:response to ethanol
GO:0046872	F:metal ion binding
GO:0046875	F:ephrin receptor binding
GO:0046934	F:phosphatidylinositol-4,5-bisphosphate 3-kinase activity
GO:0048010	P:vascular endothelial growth factor receptor signaling pathway
GO:0048013	P:ephrin receptor signaling pathway
GO:0048156	F:tau protein binding
GO:0048471	C:perinuclear region of cytoplasm
GO:0048813	P:dendrite morphogenesis
GO:0050690	P:regulation of defense response to virus by virus
GO:0050730	P:regulation of peptidyl-tyrosine phosphorylation
GO:0050798	P:activated T cell proliferation
GO:0050804	P:modulation of chemical synaptic transmission
GO:0050852	P:T cell receptor signaling pathway
GO:0050900	P:leukocyte migration
GO:0050966	P:detection of mechanical stimulus involved in sensory perception of pain
GO:0051428	F:peptide hormone receptor binding
GO:0051897	P:positive regulation of protein kinase B signaling
GO:0070851	F:growth factor receptor binding
GO:0071375	P:cellular response to peptide hormone stimulus
GO:0071560	P:cellular response to transforming growth factor beta stimulus
GO:0090314	P:positive regulation of protein targeting to membrane
GO:0097038	C:perinuclear endoplasmic reticulum
GO:0097062	P:dendritic spine maintenance
GO:0097386	C:glial cell projection
GO:0097718	F:disordered domain specific binding
GO:0098685	C:Schaffer collateral - CA1 synapse
GO:0098978	C:glutamatergic synapse
GO:0099092	C:postsynaptic density
GO:1900182	intracellular component
GO:1900449	P:positive regulation of protein localization to nucleus
GO:1901216	P:regulation of glutamate receptor signaling pathway
GO:1902951	P:positive regulation of neuron death
GO:1903202	P:negative regulation of dendritic spine maintenance
GO:1903997	P:negative regulation of oxidative stress-induced cell death
GO:1904645	P:positive regulation of non-membrane spanning protein tyrosine kinase activity
GO:1905232	P:response to amyloid-beta
GO:1905430	P:cellular response to L-glutamate
GO:1905477	P:cellular response to glycine
GO:1905664	P:positive regulation of protein localization to membrane
GO:2001056	P:regulation of calcium ion import across plasma membrane
GO:2001240	P:positive regulation of cysteine-type endopeptidase activity

KEGG Pathway
Reactome Pathway

Pathway ID	Pathway Name	Pathway Description (KEGG)
hsa04071	Sphingolipid signaling pathway	Sphingomyelin (SM) and its metabolic products are now known to have second messenger functions in a variety of cellular signaling pathways. Particularly, the sphingolipid metabolites, ceramide (Cer) and sphingosine-1-phosphate (S1P), have emerged as a new class of potent bioactive molecules. Ceramide can be generated de novo or by hydrolysis of membrane sphingomyelin by sphingomyelinase (SMase). Ceramide is subsequently metabolized by ceramidase to generate sphingosine (Sph) which in turn produces S1P through phosphorylation by sphingosine kinases 1 and 2 (SphK1, 2). Both ceramide and S1P regulate cellular responses to stress, with generally opposing effects. S1P functions as a growth and survival factor, acting as a ligand for a family of G protein-coupled receptors, whereas ceramide activates intrinsic and extrinsic apoptotic pathways through receptor-independent mechanisms.
hsa04072	Phospholipase D signaling pathway	Phospholipase D (PLD) is an essential enzyme responsible for the production of the lipid second messenger phosphatidic acid (PA), which is involved in fundamental cellular processes, including membrane trafficking, actin cytoskeleton remodeling, cell proliferation and cell survival. PLD activity can be stimulated by a large number of cell surface receptors and is elaborately regulated by intracellular factors, including protein kinase C isoforms, small GTPases of the ARF, Rho and Ras families and the phosphoinositide, phosphatidylinositol 4,5-bisphosphate (PIP2). The PLD-produced PA activates signaling proteins and acts as a node within the membrane to which signaling proteins translocate. Several signaling proteins, including Raf-1 and mTOR, directly bind PA to mediate translocation or activation, respectively.
hsa04360	Axon guidance	Axon guidance represents a key stage in the formation of neuronal network. Axons are guided by a variety of guidance factors, such as netrins, ephrins, Slits, and semaphorins. These guidance cues are read by growth cone receptors, and signal transduction pathways downstream of these receptors converge onto the Rho GTPases to elicit changes in cytoskeletal organization that determine which way the growth cone will turn.
hsa04380	Osteoclast differentiation	The osteoclasts, multinucleared cells originating from the hematopoietic monocyte-macrophage lineage, are responsible for bone resorption. Osteoclastogenesis is mainly regulated by signaling pathways activated by RANK and immune receptors, whose ligands are expressed on the surface of osteoblasts. Signaling from RANK changes gene expression patterns through transcription factors like NFATc1 and characterizes the active osteoclast.
hsa04510	Focal adhesion	Cell-matrix adhesions play essential roles in important biological processes including cell motility, cell proliferation, cell differentiation, regulation of gene expression and cell survival. At the cell-extracellular matrix contact points, specialized structures are formed and termed focal adhesions, where bundles of actin filaments are anchored to transmembrane receptors of the integrin family through a multi-molecular complex of junctional plaque proteins. Some of the constituents of focal adhesions participate in the structural link between membrane receptors and the actin cytoskeleton, while others are signalling molecules, including different protein kinases and phosphatases, their substrates, and various adapter proteins. Integrin signaling is dependent upon the non-receptor tyrosine kinase activities of the FAK and src proteins as well as the adaptor protein functions of FAK, src and Shc to initiate downstream signaling events. These signalling events culminate in reorganization of the actin cytoskeleton; a prerequisite for changes in cell shape and motility, and gene expression. Similar morphological alterations and modulation of gene expression are initiated by the binding of growth factors to their respective receptors, emphasizing the considerable crosstalk between adhesion- and growth factor-mediated signalling.
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.
hsa04611	Platelet activation	Platelets play a key and beneficial role for primary hemostasis on the disruption of the integrity of vessel wall. Platelet adhesion and activation at sites of vascular wall injury is initiated by adhesion to adhesive macromolecules, such as collagen and von Willebrand factor (vWF), or by soluble platelet agonists, such as ADP, thrombin, and thromboxane A2. Different receptors are stimulated by various agonists, almost converging in increasing intracellular Ca2+ concentration that stimulate platelet shape change and granule secretion and ultimately induce the inside-outsignaling process leading to activation of the ligand-binding function of integrin alpha IIb beta 3. Binding of alpha IIb beta 3 to its ligands, mainly fibrinogen, mediates platelet adhesion and aggregation and triggers outside-insignaling, resulting in platelet spreading, additional granule secretion, stabilization of platelet adhesion and aggregation, and clot retraction.
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.
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.
hsa04725	Cholinergic synapse	Acetylcholine (ACh) is a neurotransmitter widely distributed in the central (and also peripheral, autonomic and enteric) nervous system (CNS). In the CNS, ACh facilitates many functions, such as learning, memory, attention and motor control. When released in the synaptic cleft, ACh binds to two distinct types of receptors: Ionotropic nicotinic acetylcholine receptors (nAChR) and metabotropic muscarinic acetylcholine receptors (mAChRs). The activation of nAChR by ACh leads to the rapid influx of Na+ and Ca2+ and subsequent cellular depolarization. Activation of mAChRs is relatively slow (milliseconds to seconds) and, depending on the subtypes present (M1-M5), they directly alter cellular homeostasis of phospholipase C, inositol trisphosphate, cAMP, and free calcium. In the cleft, ACh may also be hydrolyzed by acetylcholinesterase (AChE) into choline and acetate. The choline derived from ACh hydrolysis is recovered by a presynaptic high-affinity choline transporter (CHT).
hsa05020	Prion diseases	Prion diseases, also termed transmissible spongiform encephalopathies (TSEs), are a group of fatal neurodegenerative diseases that affect humans and a number of other animal species. The etiology of these diseases is thought to be associated with the conversion of a normal protein, PrPC, into an infectious, pathogenic form, PrPSc. The conversion is induced by prion infections (for example, variant Creutzfeldt-Jakob disease (vCJD), iatrogenic CJD, Kuru), mutations (familial CJD, Gerstmann-Straussler-Scheinker syndrome, fatal familial insomnia (FFI)) or unknown factors (sporadic CJD (sCJD)), and is thought to occur after PrPC has reached the plasma membrane or is re-internalized for degradation. The PrPSc form shows greater protease resistance than PrPC and accumulates in affected individuals, often in the form of extracellular plaques. Pathways that may lead to neuronal death comprise oxidative stress, regulated activation of complement, ubiquitin-proteasome and endosomal-lysosomal systems, synaptic alterations and dendritic atrophy, corticosteroid response, and endoplasmic reticulum stress. In addition, the conformational transition could lead to the lost of a beneficial activity of the natively folded protein, PrPC.
hsa05130	Pathogenic Escherichia coli infection	Enteropathogenic E. coli (EPEC) and enterohemorrhagic E. coli (EHEC) are closely related pathogenic strains of Escherichia coli. The hallmark of EPEC/EHEC infections [DS:H00278 H00277] is induction of attaching and effacing (A/E) lesions that damage intestinal epithelial cells. The capacity to form A/E lesions is encoded mainly by the locus of enterocyte effacement (LEE) pathogenicity island. Tir, Map, EspF, EspG are known LEE-encoded effector proteins secreted via the type III secretion system, which is also LEE-encoded, into the host cell. EPEC and EHEC Tir's link the extracellular bacterium to the cell cytoskeleton. Map and EspF are involved in mitochondrion membrane permeabilization. EspG interacts with tubulins and stimulates microtubule destabilization. LEE-encoded adhesin or intimin (Eae) is exported via the general secretory pathway to the periplasm, where it is inserted into the outer membrane. In addition to Tir, two potential host cell-carried intimin receptors, beta1 integrin (ITGB1) and nucleolin (NCL), have so far been identified. The distinguishing feature of EHEC is the elaboration of Shiga-like toxin (Stx). Stx cleaves ribosomal RNA, thereby disrupting protein synthesis and killing the intoxicated epithelial or endothelial cells.
hsa05162	Measles	Measles virus (MV) is highly contagious virus that leads infant death worldwide. Humans are the unique natural reservoir for this virus. It causes severe immunosuppression favouring secondary bacterial infections. Several MV proteins have been suggested to disturb host immunity. After infection of host lymphoid cells via SLAM, MV inhibits cytokine response by direct interference with host signaling systems. Three proteins (P, V, and C) associate with Jak/STAT proteins in interferon-triggered pathway and other important proteins related to apoptosis. Interaction between MV and host brings about the shift towards a Th2 response by decreasing IL-12 production and induces lymphopenia by suppressing cell proliferation.
hsa05416	Viral myocarditis	Myocarditis is a cardiac disease associated with inflammation and injury of the myocardium. It results from various etiologies, both noninfectious and infectious, but coxsackievirus B3 (CVB3) is still considered the dominant etiological agent. Myocarditis may be caused by direct cytopathic effects of virus, a pathologic immune response to persistent virus, or autoimmunity triggered by the viral infection. The virus enters the myocyte through internalization of the coxsackie-adenoviral receptor (CAR) and its coreceptor, decay-accelerating factor (DAF). Viral proteases cleave various proteins in the host cell. One example is viral protease 2A, which cleaves eukaryote initiation factor 4G (eIF4G) and the dystrophin protein, resulting in a complete shutdown of cap-dependent RNA translation and cytoskeletal destruction in infected cardiomyocytes, respectively. CVB3 also cleaves the member of the Bcl-2 family Bid, leading to apoptosis. CVB3 infection also induces the cleavage of cyclin D protein through a proteasome-dependent pathway, leading to the host cell-growth arrest. Viral infection and necrosis of myocytes may lead to the release of intracellular antigens, resulting in activation of self-reactive T cells. CVB infection is a significant cause of dilated cardiomyopathy (DCM) as well as myocarditis. Epidemiologically, myocarditis underlies a significant portion of patients with DCM.

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-1227986	Signaling by ERBB2.	ERBB2, also known as HER2 or NEU, is a receptor tyrosine kinase (RTK) belonging to the EGFR family. ERBB2 possesses an extracellular domain that does not bind any known ligand, contrary to other EGFR family members, a single transmembrane domain, and an intracellular domain consisting of an active kinase and a C-tail with multiple tyrosine phosphorylation sites. Inactive ERBB2 is associated with a chaperone heat shock protein 90 (HSP90) and its co-chaperone CDC37 (Xu et al. 2001, Citri et al. 2004, Xu et al. 2005). In addition, ERBB2 is associated with ERBB2IP (also known as ERBIN or LAP2), a protein responsible for proper localization of ERBB2. In epithelial cells, ERBB2IP restricts expression of ERBB2 to basolateral plasma membrane regions (Borg et al. 2000).\nERBB2 becomes activated by forming a heterodimer with another ligand-activated EGFR family member, either EGFR, ERBB3 or ERBB4, which is accompanied by dissociation of chaperoning proteins HSP90 and CDC37 (Citri et al. 2004), as well as ERBB2IP (Borg et al. 2000) from ERBB2. ERBB2 heterodimers function to promote cell proliferation, cell survival and differentiation, depending on the cellular context. ERBB2 can also be activated by homodimerization when it is overexpressed, in cancer for example. \nIn cells expressing both ERBB2 and EGFR, EGF stimulation of EGFR leads to formation of both ERBB2:EGFR heterodimers (Wada et al. 1990, Karunagaran et al. 1996) and EGFR homodimers. Heterodimers of ERBB2 and EGFR trans-autophosphorylate on twelve tyrosine residues, six in the C-tail of EGFR and six in the C-tail of ERBB2 - Y1023, Y1139, Y1196, Y1221, Y1222 and Y1248 (Margolis et al. 1989, Hazan et al. 1990,Walton et al. 1990, Helin et al. 1991, Ricci et al. 1995, Pinkas-Kramarski 1996). Phosphorylated tyrosine residues in the C-tail of EGFR and ERBB2 serve as docking sites for downstream signaling molecules. Three key signaling pathways activated by ERBB2:EGFR heterodimers are RAF/MAP kinase cascade, PI3K-induced AKT signaling, and signaling by phospholipase C gamma (PLCG1). Downregulation of EGFR signaling is mediated by ubiquitin ligase CBL, and is shown under Signaling by EGFR.\nIn cells expressing ERBB2 and ERBB3, ERBB3 activated by neuregulin NRG1 or NRG2 binding (Tzahar et al. 1994) forms a heterodimer with ERBB2 (Pinkas-Kramarski et al. 1996, Citri et al. 2004). ERBB3 is the only EGFR family member with no kinase activity, and can only function in heterodimers, with ERBB2 being its preferred heterodimerization partner. After heterodimerization, ERBB2 phosphorylates ten tyrosine residues in the C-tail of ERBB3, Y1054, Y1197, Y1199, Y1222, Y1224, Y1260, Y1262, Y1276, Y1289 and Y1328 (Prigent et al. 1994, Pinkas-Kramarski et al. 1996, Vijapurkar et al. 2003, Li et al. 2007) that subsequently serve as docking sites for downstream signaling molecules, resulting in activation of PI3K-induced AKT signaling and RAF/MAP kinase cascade. Signaling by ERBB3 is downregulated by the action of RNF41 ubiquitin ligase, also known as NRDP1. \nIn cells expressing ERBB2 and ERBB4, ligand stimulated ERBB4 can either homodimerize or form heterodimers with ERBB2 (Li et al. 2007), resulting in trans-autophosphorylation of ERBB2 and ERBB4 on C-tail tyrosine residues that will subsequently serve as docking sites for downstream signaling molecules, leading to activation of RAF/MAP kinase cascade and, in the case of ERBB4 CYT1 isoforms, PI3K-induced AKT signaling (Hazan et al. 1990, Cohen et al. 1996, Li et al. 2007, Kaushansky et al. 2008). Signaling by ERBB4 is downregulated by the action of WWP1 and ITCH ubiquitin ligases, and is shown under Signaling by ERBB4
R-HSA-1257604	PIP3 activates AKT signaling.	Signaling by AKT is one of the key outcomes of receptor tyrosine kinase (RTK) activation. AKT is activated by the cellular second messenger PIP3, a phospholipid that is generated by PI3K. In ustimulated cells, PI3K class IA enzymes reside in the cytosol as inactive heterodimers composed of p85 regulatory subunit and p110 catalytic subunit. In this complex, p85 stabilizes p110 while inhibiting its catalytic activity. Upon binding of extracellular ligands to RTKs, receptors dimerize and undergo autophosphorylation. The regulatory subunit of PI3K, p85, is recruited to phosphorylated cytosolic RTK domains either directly or indirectly, through adaptor proteins, leading to a conformational change in the PI3K IA heterodimer that relieves inhibition of the p110 catalytic subunit. Activated PI3K IA phosphorylates PIP2, converting it to PIP3; this reaction is negatively regulated by PTEN phosphatase. PIP3 recruits AKT to the plasma membrane, allowing TORC2 to phosphorylate a conserved serine residue of AKT. Phosphorylation of this serine induces a conformation change in AKT, exposing a conserved threonine residue that is then phosphorylated by PDPK1 (PDK1). Phosphorylation of both the threonine and the serine residue is required to fully activate AKT. The active AKT then dissociates from PIP3 and phosphorylates a number of cytosolic and nuclear proteins that play important roles in cell survival and metabolism. For a recent review of AKT signaling, please refer to Manning and Cantley, 2007
R-HSA-1433557	Signaling by SCF-KIT.	Stem cell factor (SCF) is a growth factor with membrane bound and soluble forms. It is expressed by fibroblasts and endothelial cells throughout the body, promoting proliferation, migration, survival and differentiation of hematopoetic progenitors, melanocytes and germ cells.(Linnekin 1999, Ronnstrand 2004, Lennartsson and Ronnstrand 2006). The receptor for SCF is KIT, a tyrosine kinase receptor (RTK) closely related to the receptors for platelet derived growth factor receptor, colony stimulating factor 1 (Linnekin 1999) and Flt3 (Rosnet et al. 1991). Four isoforms of c-Kit have been identified in humans. Alternative splicing results in isoforms of KIT differing in the presence or absence of four residues (GNNK) in the extracellular region. This occurs due to the use of an alternate 5' splice donor site. These GNNK+ and GNNK- variants are co-expressed in most tissues; the GNNK- form predominates and was more strongly tyrosine-phosphorylated and more rapidly internalized (Ronnstrand 2004). There are also splice variants that arise from alternative usage of splice acceptor site resulting in the presence or absence of a serine residue (Crosier et al., 1993). Finally, there is an alternative shorter transcript of KIT expressed in postmeiotic germ cells in the testis which encodes a truncated KIT consisting only of the second part of the kinase domain and thus lackig the extracellular and transmembrane domains as well as the first part of the kinase domain (Rossi et al. 1991). Binding of SCF homodimers to KIT results in KIT homodimerization followed by activation of its intrinsic tyrosine kinase activity. KIT stimulation activates a wide array of signalling pathways including MAPK, PI3K and JAK/STAT (Reber et al. 2006, Ronnstrand 2004). Defects of KIT in humans are associated with different genetic diseases and also in several types of cancers like mast cell leukaemia, germ cell tumours, certain subtypes of malignant melanoma and gastrointestinal tumours
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-164944	Nef and signal transduction.	Nef interferes with cellular signal transduction pathways in a number of ways. Nef is associated with lipid rafts through its amino-terminal myristoylation and a proline-rich SH3-binding domain. These cholesterol-rich membrane microdomains appear to concentrate potent signaling mediators. Nef was found to complex with and activate serine/threonine protein kinase PAK-2, which may contribute to activation of infected cells. In vitro, HIV-infected T cells produce enhanced levels of interleukin-2 during activation. When expressed in macrophages, Nef intersects the CD40L signaling pathway inducing secretion of chemokines and other factors that attract resting T cells and promote their infection by HIV
R-HSA-202733	Cell surface interactions at the vascular wall.	Leukocyte extravasation is a rigorously controlled process that guides white cell movement from the vascular lumen to sites of tissue inflammation. The powerful adhesive interactions that are required for leukocytes to withstand local flow at the vessel wall is a multistep process mediated by different adhesion molecules. Platelets adhered to injured vessel walls form strong adhesive substrates for leukocytes. For instance, the initial tethering and rolling of leukocytes over the site of injury are mediated by reversible binding of selectins to their cognate cell-surface glycoconjugates. \r\n\r\nEndothelial cells are tightly connected through various proteins, which regulate the organization of the junctional complex and bind to cytoskeletal proteins or cytoplasmic interaction partners that allow the transfer of intracellular signals. An important role for these junctional proteins in governing the transendothelial migration of leukocytes under normal or inflammatory conditions has been established. \r\n\r\nThis pathway describes some of the key interactions that assist in the process of platelet and leukocyte interaction with the endothelium, in response to injury
R-HSA-2029481	FCGR activation.	Cross-linking of FCGRs with IgG coated immune complexes results in tyrosine phosphorylation of the immuno tyrosine activation motif (ITAMs) of the rececptor by membrane-bound tyrosine kinases of the SRC family. The phosphorylated ITAM tyrosines serve as docking sites for Src homology 2 (SH2) domain-containing SYK kinase. Recruitment and activation of SYK is critical for FCGR-mediated signaling in phagocytosis, but the exact role of SYK in this process is unclear. Activated SYK then transmits downstream signals leading to actin polymerization and particle internalization
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-2219530	Constitutive Signaling by Aberrant PI3K in Cancer.	Signaling by PI3K/AKT is frequently constitutively activated in cancer via gain-of-function mutations in one of the two PI3K subunits - PI3KCA (encoding the catalytic subunit p110alpha) or PIK3R1 (encoding the regulatory subunit p85alpha). Gain-of-function mutations activate PI3K signaling by diverse mechanisms. Mutations affecting the helical domain of PIK3CA and mutations affecting nSH2 and iSH2 domains of PIK3R1 impair inhibitory interactions between these two subunits while preserving their association. Mutations in the catalytic domain of PIK3CA enable the kinase to achieve an active conformation. PI3K complexes with gain-of-function mutations therefore produce PIP3 and activate downstream AKT in the absence of growth factors (Huang et al. 2007, Zhao et al. 2005, Miled et al. 2007, Horn et al. 2008, Sun et al. 2010, Jaiswal et al. 2009, Zhao and Vogt 2010, Urick et al. 2011)
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-2682334	EPH-Ephrin signaling.	During the development process cell migration and adhesion are the main forces involved in morphing the cells into critical anatomical structures. The ability of a cell to migrate to its correct destination depends heavily on signaling at the cell membrane. Erythropoietin producing hepatocellular carcinoma (EPH) receptors and their ligands, the ephrins (EPH receptors interacting proteins, EFNs), orchestrates the precise control necessary to guide a cell to its destination. They are expressed in all tissues of a developing embryo and are involved in multiple developmental processes such as axon guidance, cardiovascular and skeletal development and tissue patterning. In addition, EPH receptors and EFNs are expressed in developing and mature synapses in the nervous system, where they may have a role in regulating synaptic plasticity and long-term potentiation. Activation of EPHB receptors in neurons induces the rapid formation and enlargement of dendritic spines, as well as rapid synapse maturation (Dalva et al. 2007). On the other hand, EPHA4 activation leads to dendritic spine elimination (Murai et al. 2003, Fu et al. 2007).EPH receptors are the largest known family of receptor tyrosine kinases (RTKs), with fourteen total receptors divided into either A- or B-subclasses: EPHA (1-8 and 10) and EPHB (1-4 and 6). EPH receptors can have overlapping functions, and loss of one receptor can be partially compensated for by another EPH receptor that has similar expression pattern and ligand-binding specificities. EPH receptors have an N-terminal extracellular domain through which they bind to ephrin ligands, a short transmembrane domain, and an intracellular cytoplasmic signaling structure containing a canonical tyrosine kinase catalytic domain as well as other protein interaction sites. Ephrins are also sub-divided into an A-subclass (A1-A5), which are tethered to the plasma membrane by a glycosylphosphatidylinositol (GPI) anchor, and a B-subclass (B1-B3), members of which have a transmembrane domain and a short, highly conserved cytoplasmic tail lacking endogenous catalytic activity. The interaction between EPH receptors and its ligands requires cell-cell interaction since both molecules are membrane-bound. Close contact between EPH receptors and EFNs is required for signaling to occur. EPH/EFN-initiated signaling occurs bi-directionally into either EPH- or EFN-expressing cells or axons. Signaling into the EPH receptor-expressing cell is referred as the forward signal and signaling into the EFN-expressing cell, the reverse signal. (Dalva et al. 2000, Grunwald et al. 2004, Davy & Robbins 2000, Cowan et al
R-HSA-2730905	Role of LAT2/NTAL/LAB on calcium mobilization.	The lipid raft resident adaptor molecules LAT1 and Non-T cell activation linker (NTAL), also known as linker for activation of B cells (LAB)/LAT2 are known participants in the regulation of mast cell calcium responses. Both LAT and NTAL are expressed and phosphorylated following engagement of FCERI on mast cells. NTAL is functionally and topographically different from LAT. There is a considerable debate on the role of NTAL in mast cell. Depending on the circumstances, NTAL appears to have a dual role as positive and negative regulator of MC responses elicited via FCERI. Studies conducted in bone marrow-derived mast cells (BMMCs) of mice lacking NTAL displayed enhanced FCERI-mediated tyrosine phosphorylation of several substrates, calcium response, degranulation, and cytokine production. This indicated that NTAL negatively regulates FCERI-mediated degranulation. However, in mice lacking both LAT and NTAL showed severe block in FCERI-mediated signaling than BMMCs deficient in LAT alone, suggesting that NTAL also shares a redundant function with LAT to play a positive role (Draberova et al. 2007, Orr & McVicar. 2011, Zhu et al. 2004, Volna et al. 2004)
R-HSA-373753	Nephrin family interactions.	Nephrin (NPHS1) is a member of the Super-IgG-Molecule family and is most prominently expressed in kidney podocytes. It is a major if not the most important structural component of the slit diaphragm, a modified adherens junction inbetween these cells. NPHS1 has an extracellular domain that contains eight distal IgG like domains and one proximal fibronectin type III domain, a transmembrane domain and a short intracellular domain. NPHS1 molecules show both homophilic and heterophilic interactions. Among heterophilic interaction partners, slit diaphragm proteins such as Kin of IRRE-like protein 1 (KIRREL, Nephrin-like protein 1, NEPH1), KIRREL3 (NEPH2) and KIRREL2 (NEPH3) were shown to stabilize the slit diaphragm structure. Intracellularly Podocin (NPHS2), CD2 associated protein (CD2AP) and adherins junction associated proteins like IQGAP, MAGI, CASK and spectrins all interact with NPHS1. Hence it seems to play a major role in organizing the molecular structure of the slit diaphragm itself and via its binding partners links it to the actin cytoskeleton. NPHS1 tyrosine phosphorylation by the Src kinase FYN initiates the PI3K-AKT signaling cascade, which seems to promote antiapoptotic signals
R-HSA-375165	NCAM signaling for neurite out-growth.	The neural cell adhesion molecule, NCAM, is a member of the immunoglobulin (Ig) superfamily and is involved in a variety of cellular processes of importance for the formation and maintenance of the nervous system. The role of NCAM in neural differentiation and synaptic plasticity is presumed to depend on the modulation of intracellular signal transduction cascades. NCAM based signaling complexes can initiate downstream intracellular signals by at least two mechanisms: (1) activation of FGFR and (2) formation of intracellular signaling complexes by direct interaction with cytoplasmic interaction partners such as Fyn and FAK. Tyrosine kinases Fyn and FAK interact with NCAM and undergo phosphorylation and this transiently activates the MAPK, ERK 1 and 2, cAMP response element binding protein (CREB) and transcription factors ELK and NFkB. CREB activates transcription of genes which are important for axonal growth, survival, and synaptic plasticity in neurons.NCAM1 mediated intracellular signal transduction is represented in the figure below. The Ig domains in NCAM1 are represented in orange ovals and Fn domains in green squares. The tyrosine residues susceptible to phosphorylation are represented in red circles and their positions are numbered. Phosphorylation is represented by red arrows and dephosphorylation by yellow. Ig, Immunoglobulin domain; Fn, Fibronectin domain; Fyn, Proto-oncogene tyrosine-protein kinase Fyn; FAK, focal adhesion kinase; RPTPalpha, Receptor-type tyrosine-protein phosphatase; Grb2, Growth factor receptor-bound protein 2; SOS, Son of sevenless homolog; Raf, RAF proto-oncogene serine/threonine-protein kinase; MEK, MAPK and ERK kinase; ERK, Extracellular signal-regulated kinase; MSK1, Mitogen and stress activated protein kinase 1; CREB, Cyclic AMP-responsive element-binding protein; CRE, cAMP response elements
R-HSA-389356	CD28 co-stimulation.	In naive T cells, CD28 costimulation enhances cell cycle entry, potently stimulates expression of both the mitogenic lymphokine interleukin-2 (IL-2) and its receptor, and stimulates the activation of an antiapoptotic program. CD28 engages with one or both members of the B7 receptor family, B7.1 and B7.2. Upon ligand binding the tyrosines and proline-rich motifs present in the cytoplasmic tail of CD28 are phosphorylated by Lck or Fyn. Upon phosphorylation CD28 recruits and induces phosphorylation and activation of a more restricted set of intracellular signaling components that, together with those mobilized by the TCR, contribute to convert membrane-based biochemical and biophysical changes into gene activation events. Proteins like PI3K, Vav-1, Tec and Itk kinases, AKT, and the Dok-1 adaptor have been identified as elements of the CD28 signaling pathway by biochemical or genetic approaches or both
R-HSA-389357	CD28 dependent PI3K/Akt signaling.	PI3Ks can be activated by a number of different receptors, including the TcR (T cell receptor), co-stimulatory receptors (CD28), cytokine receptors and chemokine receptors. However, the specific roles of PI3Ks downstream of these receptors vary. CD28 contains the YMNM consensus PI3K-binding motif, and PI3K recruitment by CD28 contributes to or complements TCR-dependent PI3K signaling. Activation of PI3K promotes PIP3 production at the plasma membrane and several potential target molecules for this phospholipid have been implicated in PI3K pathways downstream of the TcR and CD28. Of these targets, at least Vav and Akt have been implicated in CD28 costimulation of T cell activation. AKT/PKB connects PI3K to signaling pathways that promote cytokine transcription, survival, cell-cycle entry and growth
R-HSA-389359	CD28 dependent Vav1 pathway.	CD28 binds to several intracellular proteins including PI3 kinase, Grb-2, Gads and ITK. Grb-2 specifically co-operates with Vav-1 in the up-regulation of NFAT/AP-1 transcription. CD28 costimulation resulted in a prolonged and sustained phosphorylation and membrane localization of Vav1 in comparison to T-cell receptor activation alone. Tyrosine-phosphorylated Vav1 is an early point of integration between the signaling routes triggered by the T-cell receptor and CD28.Vav1 transduces TCR and co-stimulatory signals to multiple biochemical pathways and several cytoskeleton-dependent processes. The products of Vav1 activation, Rac1 and Cdc42, in turn activate the mitogen-activated protein kinases JNK and p38. Vav1 is also required for TCR-induced calcium flux, activation of the ERK MAP kinase pathway, activation of the NF-kB transcription factor, inside-out activation of the integrin LFA-1, TCR clustering, and polarisation of the T cell
R-HSA-389513	CTLA4 inhibitory signaling.	CTLA4 is one of the best studied inhibitory receptors of the CD28 superfamily. CTLA4 inhibits Tcell activation by reducing IL2 production and IL2 expression, and by arresting T cells at the G1 phase of the cell cycle. CTLA-4 expressed by a T cell subpopulation exerts a dominant control on the proliferation of other T cells, which limits autoreactivity. CTLA4 also blocks CD28 signals by competing for the ligands B71 and B72 in the limited space between T cells and antigenpresenting cells. Though the mechanism is obscure, CTLA4 may also propagate inhibitory signals that actively counter those produced by CD28. CTLA4 can also function in a ligand-independent manner.?CTLA-4 regulates the activation of pathogenic T cells by directly modulating T cell receptor signaling (i.e. TCR-zeta chain phosphorylation) as well as downstream biochemical signals (i.e. ERK activation). The cytoplasmic region of CTLA4 contains a tyrosine motif YVKM and a proline rich region. After TCR stimulation, it undergoes tyrosine phosphorylation by src kinases, inducing surface retention
R-HSA-3928662	EPHB-mediated forward signaling.	Multiple EPHB receptors contribute directly to dendritic spine development and morphogenesis. These are more broadly involved in post-synaptic development through activation of focal adhesion kinase (FAK) and Rho family GTPases and their GEFs. Dendritic spine morphogenesis is a vital part of the process of synapse formation and maturation during CNS development. Dendritic spine morphogenesis is characterized by filopodia shortening followed by the formation of mature mushroom-shaped spines (Moeller et al. 2006). EPHBs control neuronal morphology and motility by modulation of the actin cytoskeleton. EPHBs control dendritic filopodia motility, enabling synapse formation. EPHBs exert these effects through interacting with the guanine exchange factors (GEFs) such as intersectin and kalirin. The intersectin-CDC42-WASP-actin and kalirin-RAC-PAK-actin pathways have been proposed to regulate the EPHB receptor mediated morphogenesis and maturation of dendritic spines in cultured hippocampal and cortical neurons (Irie & Yamaguchi 2002, Penzes et al. 2003). EPHBs are also involved in the regulation of dendritic spine morphology through FAK which activates the RHOA-ROCK-LIMK-1 pathway to suppress cofilin activity and inhibit cofilin-mediated dendritic spine remodeling (Shi et al. 2009)
R-HSA-3928663	EPHA-mediated growth cone collapse.	EPH/Ephrin signaling is coupled to Rho family GTPases such as Rac, Rho and Cdc42 that connect bidirectional receptor-ligand interactions to changes in the actin cytoskeleton (Noren & Pasquale 2004, Groeger & Nobes 2007). RHOA regulates actin dynamics and is involved in EPHA-induced growth cone collapse. This is mediated by ephexins. Ephexin, a guanine nucleotide exchange factor for Rho GTPases, interacts with the EPHA kinase domain and its subsequent activation differentially affects Rho GTPases, such that RHOA is activated, whereas Cdc42 and Rac1 are inhibited. Activation of RHOA, and inhibition of Cdc42 and Rac, shifts actin cytoskeleton to increased contraction and reduced expansion leading to growth-cone collapse (Shamah et al. 2001, Sahin et al. 2005). The activation of EPH receptors in growing neurons typically, but not always, leads to a growth cone collapse response and retraction from an ephrin-expressing substrate (Poliakov et al. 2004, Pasquale 2005). EPHA-mediated repulsive responses prevent axons from growing into regions of excessive ephrin-A concentration, such as the posterior end of the superior colliculus (Pasquale 2005)
R-HSA-3928664	Ephrin signaling.	The interaction between ephrin (EFN) ligands and EPH receptors results not only in forward signaling through the EPH receptor, but also in 'reverse' signaling through the EFN ligand itself. Reverse signaling through EFNB is required for correct spine morphogenesis and proper path-finding of corpus callosum and dorsal retinal axons. The molecular mechanism by which EFNBs transduce a reverse signal involves phosphorylation of multiple, conserved tyrosines on the intracellular domain of B-type ephrins, facilitating binding of the SH2/SH3 domain adaptor protein GRB4 and subsequent cytoskeletal remodeling (Bruckner et al. 1997, Cowan & Henkemeyer 2001, Lu et al. 2001). The other mechanism of reverse signaling involves the C-terminus PSD-95/Dlg/ZO-1 (PDZ)-binding motif of EFNBs which recruits various PDZ domain containing proteins. Phosphorylation and PDZ-dependent reverse signaling by ephrin-B1 have each been proposed to play important roles in multiple contexts in development and disease (Bush & Soriano 2009)
R-HSA-3928665	EPH-ephrin mediated repulsion of cells.	Despite high-affinity multimeric interaction between EPHs and ephrins (EFNs), the cellular response to EPH-EFN engagement is usually repulsion between the two cells and signal termination. These repulsive responses induce an EPH receptor-expressing cell to retract from an ephrin-expressing cell after establishing initial contact. The repulsive responses mediated by EPH receptors in the growth cone at the leading edge of extending axons and in axonal collateral branches contribute to the formation of selective neuronal connections. It is unclear how high affinity trans-cellular interactions between EPHs and ephrins are broken to convert adhesion into repulsion. Two possible mechanisms have been proposed for the repulsion of EPH-EFN bearing cells: the first one involves regulated cleavage of ephrin ligands or EPH receptors by transmembrane proteases following cell-cell contact, while the second one is rapid endocytosis of whole EPH:EFN complexes during the retraction of the interacting cells or neuronal growth cones (Egea & Klein 2007, Janes et al. 2005). RAC also plays an essential role during growth cone collapse by promoting actin polymerization that drives membrane internalization by endocytosis (Marston et al. 2003)
R-HSA-399954	Sema3A PAK dependent Axon repulsion.	Activated Rac1 bound to plexin-A might modulate actin dynamics through the sequential phosphorylation and activation of PAK, LIMK1 and cofilin
R-HSA-399955	SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.	Sema3A, a prototypical semaphorin, acts as a chemorepellent or a chemoattractant for axons by activating a receptor complex comprising neuropilin-1 as the ligand-binding subunit and plexin-A1 as the signal-transducing subunit. Sema3A inhibits cell migration by inhibiting integrin ligand-binding activity
R-HSA-399956	CRMPs in Sema3A signaling.	CRMPs are a small family of plexinA-interacting cytosolic phosphoproteins identified as mediators of Sema3A signaling and neuronal differentiation. After Sema3A activation Plexin-A bound CRMP's undergo phosphorylation by Cdk5, GSK3beta and Fes kinases. Phosphorylation of CRMPs by these kinases blocks the ability of CRMP to bind to tubulin dimers, subsequently induces depolymerization of F-actin, and ultimately leads to growth cone collapse
R-HSA-418885	DCC mediated attractive signaling.	The DCC family includes DCC and neogenin in vertebrates. DCC is required for netrin-induced axon attraction. DCC is a transmembrane protein lacking any identifiable catalytic activity. Protein tyrosine kinase 2/FAK and src family kinases bind constitutively to the cytoplasmic domain of DCC and their activation couples to downstream intracellular signaling complex that directs the organization of actin
R-HSA-4420097	VEGFA-VEGFR2 Pathway.	Angiogenesis is the formation of new blood vessels from preexisting vasculature. One of the most important proangiogenic factors is vascular endothelial growth factor (VEGF). VEGF exerts its biologic effect through interaction with transmembrane tyrosine kinase receptors VEGFR, selectively expressed on vascular endothelial cells. VEGFA signaling through VEGFR2 is the major pathway that activates angiogenesis by inducing the proliferation, survival, sprouting and migration of endothelial cells (ECs), and also by increasing endothelial permeability (Lohela et al. 2009, Shibuya & Claesson-Welsh 2006, Claesson-Welsh & Welsh, 2013). The critical role of VEGFR2 in vascular development is highlighted by the fact that VEGFR2-/- mice die at E8.5-9.5 due to defective development of blood islands, endothelial cells and haematopoietic cells (Shalaby et al. 1995)
R-HSA-5621480	Dectin-2 family.	Dendritic cell-associated C-type lectin-2 (Dectin-2) family of C-type lectin receptors (CLRs) includes Dectin-2 (CLEC6A), blood dendritic antigen 2 (BDCA2/CLEC4C), macrophage C-type lectin (MCL/CLEC4D), Dendritic cell immunoreceptor (DCIR/CLEC4A) and macrophage inducible C-type lectin (Mincle/CLEC4E). These receptors possesses a single extracellular conserved C-type lectin domain (CTLD) with a short cytoplasmic tail that induces intracellular signalling indirectly by binding with the FCERG (High affinity immunoglobulin epsilon receptor subunit gamma) except for DCIR that has a longer cytoplasmic tail with an integral inhibitory signalling motif (Graham & Brown. 2009, Kerschera et al. 2013). CLEC6A (Dectin-2) binds to high mannose containing pathogen-associated molecular patterns (PAMPs) expressed by fungal hyphae, and CLEC4E (mincle) binds to alpha-mannaosyl PAMPs on fungal, mycobacterial and necrotic cell ligands. Both signaling pathways lead to Toll-like receptor (TLR)-independent production of cytokines such as tumor necrosis factor (TNF) and interleukin 6 (IL6). Similarities with Dectin-1 (CLC7A) signaling pathway suggests that both these CLRs couple SYK activation to NF-kB activation using a complex involving CARD9, BCL10 and MALT1 (Geijtenbeek & Gringhuis 2009)
R-HSA-5621575	CD209 (DC-SIGN) signaling.	CD209 (also called as DC-SIGN (DC-specific intracellular adhesion molecule-3-grabbing non-integrin)) is a type II transmembrane C-type lectin receptor preferentially expressed on dendritic cells (DCs). CD209 functions as a pattern recognition receptor (PRR) that recognises several microorganisms and pathogens, contributing to generation of pathogen-tailored immune responses (Gringhuis & Geijtenbeek 2010, den Dunnen et al. 2009, Svajger et al. 2010). CD209 interacts with different mannose-expressing pathogens such as Mycobacterium tuberculosis and HIV-1 (Gringhuis et al. 2007, Geijtenbeek et al. 2000a). It also acts as an adhesion receptor that interacts with ICAM2 (intracellular adhesion molecule-2) on endothelial cells and ICAM3 on T cells (Geijtenbeek et al. 2000b,c). \nCD209 functions not only as an independent PRR, but is also implicated in the modulation of Toll-like receptor (TLR) signaling at the level of the transcription factor NF-kB (Gringhuis et al. 2009). CLEC7A (Dectin-1) and CD209 (DC-SIGN) signalling modulates Toll-like receptor (TLR) signalling through the kinase RAF1 that is independent of the SYK pathway but integrated with it at the level of NF-kB activation. The activation of RAF1 by CLEC7A or CD209 does not lead to activation of extracellular signal-regulated kinase 1 (ERK1)/2 or Mitogen-activated protein kinase kinase 1 (MEK1)/2 but leads to the phosphorylation and subsequent acetylation of RELA (p65). RELA phosphorylated on S276 not only positively regulates the activity of p65 through acetylation of p65, but also represses RELB activity by sequestering active RELB into inactive p65-RELB dimers that do not bind DNA (Gringhuis et al. 2007, Svajger et al. 2010, Jacque et al. 2005). RAF1-dependent signaling pathway is crucial in dectin-1 mediated immunity as it modulates both the canonical (promoting p65 phosphorylation and acetylation) and non-canonical (forming inactive p65-RELB dimers) NK-kB activation
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)
R-HSA-6811558	PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.	Phosphatidylinositol-5-phosphate (PI5P) may modulate PI3K/AKT signaling in several ways. PI5P is used as a substrate for production of phosphatidylinositol-4,5-bisphosphate, PI(4,5)P2 (Rameh et al. 1997, Clarke et al. 2008, Clarke et al. 2010, Clarke and Irvine 2013, Clarke et al. 2015), which serves as a substrate for activated PI3K, resulting in the production of PIP3 (Mandelker et al. 2009, Burke et al. 2011). The majority of PI(4,5)P2 in the cell, however, is produced from the phosphatidylinositol-4-phosphate (PI4P) substrate (Zhang et al. 1997, Di Paolo et al. 2002, Oude Weernink et al. 2004, Halstead et al. 2006, Oude Weernink et al. 2007). PIP3 is necessary for the activating phosphorylation of AKT. AKT1 can be deactivated by the protein phosphatase 2A (PP2A) complex that contains a regulatory subunit B56-beta (PPP2R5B) or B56-gamma (PPP2R5C). PI5P inhibits AKT1 dephosphorylation by PP2A through an unknown mechanism (Ramel et al. 2009). Increased PI5P levels correlate with inhibitory phosphorylation(s) of the PP2A complex. MAPK1 (ERK2) and MAPK3 (ERK1) are involved in inhibitory phosphorylation of PP2A, in a process that involves IER3 (IEX-1) (Letourneux et al. 2006, Rocher et al. 2007). It is uncertain, however, whether PI5P is in any way involved in ERK-mediated phosphorylation of PP2A or if it regulates another PP2A kinase
R-HSA-75892	Platelet Adhesion to exposed collagen.	Initiation of platelet adhesion is the first step in the formation of the platelet plug. Circulating platelets are arrested and subsequently activated by exposed collagen and vWF. It is not entirely clear which type of collagen is responsible for adhesion and activation; collagen types I and III are abundant in vascular epithelia but several other types incluing IV are present (Farndale 2006). Several collagen binding proteins are expressed on platelets, including integrin alpha2 beta1, GPVI, and GPIV. Integrin alpha2 beta1, known on leukocytes as VLA-2, is the major platelet collagen receptor (Kunicki et al. 1988). It requires Mg2+ to interact with collagen and may require initiation mediated by the activation of integrin alphaIIb beta3 (van de Walle 2007). Binding occurs via the alpha2 subunit I domain to a collagen motif with the sequence Gly-Phe-Hyp-Gly-Glu-Arg (Emsley 2000). Binding of collagen to alpha2 beta1 generates intracellular signals that contribute to platelet activation. These facilitate the engagement of the lower-affinity collagen receptor, GPVI (Keely 1996), the key receptor involved in collagen-induced platelet activation. The GPVI receptor is a complex of the GPVI protein with a dimer of Fc epsilon R1 gamma (FceRI gamma). The Src family kinases Fyn and Lyn constitutively associate with the GPVI:FceRIgamma complex in platelets and initiate platelet activation through phosphorylation of the immunoreceptor tyrosine-based activation motif (ITAM) in FceRI gamma, leading to binding and activation of the tyrosine kinase Syk. Downstream of Syk, a series of adapter molecules and effectors lead to platelet activation. vWF protein is a polymeric structure of variable size. It is secreted in two directions, by the endothelium basolaterally and into the bloodstream. Shear-induced aggregation is achieved when vWF binds via its A1 domain to GPIb (part of GPIb-IX-V), and via its A3 domain mediating collagen binding to the subendothelium. The interaction between vWF and GPIb is regulated by shear force; an increase in the shear stress results in a corresponding increase in the affinity of vWF for GPIb
R-HSA-8866376	Reelin signalling pathway.	Reelin (RELN) is an extracellular, multifunctional signal glycoprotein that controls not only the positioning of neurons in the developing brain, but also their growth, maturation, and synaptic activity in the adult brain (Stranahan et al. 2013). Abnormal Reelin expression in the brain is implicated in a number of neuropsychiatric disorders including autism, schizophrenia, bipolar disorder and Alzheimer's disease (Folsom & Fatemi 2013)
R-HSA-9032500	Activated NTRK2 signals through FYN.	In mouse brain, Fyn activation downstream of Bdnf-induced Ntrk2 (TrkB) signaling results in increased protein levels of AMPA receptor subunits Gria2 (GluR2), Gria3 (GluR3) and Gria1 (GluR1) without change in mRNA levels (Narisawa-Saito et al. 1999). BDNF-mediated activation of NTRK2 increases phosphorylation of voltage gated sodium channels by FYN, resulting in decrease of sodium currents (Ahn et al. 2007). FYN activation downstream of NTRK2 is implicated in olygodendrocyte myelination and contributes to BDNF-induced activation of ERK1/2 (MAPK3/1) through an unknown mechanism (Peckham et al. 2015). Besides acting downstream of NTRK2, FYN and other SRC kinases, activated by other receptors such as GPCRs, may phosphorylate NTRK2 and enhance its catalytic activity (Rajagopal and Chao 2006, Huang and McNamara 2010)
R-HSA-9032759	NTRK2 activates RAC1.	DOCK3-mediated activation of RAC1 downstream of BDNF-induced signaling by NTRK2 (TRKB) plays a role in axonal growth and regeneration. DOCK3 can be recruited to the plasma membrane to activate RAC1 by binding to NTRK-associated FYN (Namekata et al. 2010). Alternatively, DOCK3 can, upon poorly elucidated RHOG activation by the BDNF:NTRK2 complex, bind to the RHOG:GTP complex and activate RAC1 in an ELMO1-dependent manner (Namekata et al. 2012)
R-HSA-912631	Regulation of signaling by CBL.	Cbl is an E3 ubiquitin-protein ligase that negatively regulates signaling pathways by targeting proteins for ubiquitination and proteasomal degradation (Rao et al. 2002). Cbl negatively regulates PI3K via this mechanism (Dufour et al. 2008). The binding of Cbl to the p85 subunit of PI3K is mediated at least in part by tyrosine phosphorylation at Y731 (Dufour et al. 2008). Fyn and the related kinases Hck and Lyn are known to be associated with Cbl (Anderson et al. 1997, Hunter et al. 1999). Fyn is proven capable of Cbl Y731 phosphorylation (Hunter et al. 1999).The association of Fyn and Cbl has been described as constitutive (Hunter et al. 1999). CBL further associates with the p85 subunit of PI3K (Hartley et al. 1995, Anderson et al. 1997, Hunter et al. 1997), this also described as constitutive and mediated by the SH3 domain of p85. Binding of the SH2 domain of p85 to a specific phosphorylation site in Cbl is postulated to explain the the increase in Cbl/p85 association seen in activated cells (Panchamoorthy et al 1996) which negatively regulates PI3K activity (Fang et al. 2001). The negative effect of increased Cbl-PI3K interaction is mediated by Y731 of Cbl. Cbl binding increases PI3K ubiquitination and proteasome degradation (Dufour et al. 2008).Cbl is constitutively associated with Grb in resting hematopoietic cells (Anderson et al. 1997, Odai et al. 1995, Park et al. 1998, Panchamoorthy et al. 1996). Both the SH2 and SH3 domains of Grb2 are involved. Cbl has 2 distinct C-terminal domains, proximal and distal. The proximal domain binds Grb2 in resting and stimulated cells, and in stimulated cells also binds Shc. The distal domain binds the adaptor protein CRKL. Tyrosine phosphorylation of Cbl in response to IL-3 releases the SH3 domain of Grb2 which then is free to bind other molecules (Park et al. 1998). Cbl is tyrosine phosphorylated in response to many cytokines including IL-3, IL-2 (Gesbert et al. 1998) and IL-4 (Ueno et al. 1998)
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)

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Interacting partner	Detection method	Interaction type	PubMed IDs	Interaction Score	Source
ACBD7	Affinity Capture-MS	physical	28514442, (Europe PMC)	NA	BioGRID
ADAM15	Reconstituted Complex, filter binding, pull down	physical, physical association	11741929, 16374509, (Europe PMC)	0.59	BioGRID, IntAct, MINT
ADD2	Affinity Capture-Western, Reconstituted Complex	physical	11526103, (Europe PMC)	NA	BioGRID
ANKRD12	Affinity Capture-MS	physical	26186194, (Europe PMC)	NA	BioGRID
ANLN	Affinity Capture-MS, anti tag coimmunoprecipitation	association, physical	26496610, (Europe PMC)	0.35	BioGRID, IntAct
ARHGAP32	Affinity Capture-Western, Reconstituted Complex, Two-hybrid, anti bait coimmunoprecipitation, anti tag coimmunoprecipitation, pull down, two hybrid	direct interaction, physical, physical association	12788081, (Europe PMC)	0.63	BioGRID, IntAct
ATXN1	Two-hybrid, two hybrid	physical, physical association	16713569, (Europe PMC)	0.37	BioGRID, IntAct
BCAR1	Affinity Capture-Western, Reconstituted Complex, Two-hybrid, coimmunoprecipitation, peptide array, pull down, two hybrid array, two hybrid prey pooling approach	association, physical, physical association	10739664, 17474147, 9188452, 9360983, (Europe PMC)	0.49, 0.62	BioGRID, IntAct, MINT
BCL3	Reconstituted Complex, pull down	physical, physical association	16099425, 9576921, (Europe PMC)	0.40	BioGRID, IntAct, MINT
BTK	Reconstituted Complex	physical	8058772, (Europe PMC)	NA	BioGRID
C7orf25	Two-hybrid, two hybrid	physical, physical association	21900206, (Europe PMC)	0.37	BioGRID, IntAct, MINT
C8orf33	Two-hybrid, two hybrid	physical, physical association	21900206, (Europe PMC)	0.37	BioGRID, IntAct, MINT
CAV1	Co-fractionation	physical	9252391, (Europe PMC)	NA	BioGRID
CBL	Affinity Capture-Western, Biochemical Activity, Reconstituted Complex, Two-hybrid, anti bait coimmunoprecipitation, coimmunoprecipitation, competition binding, experimental interaction detection, pull down, two hybrid array	phosphorylation reaction, physical, physical association	10629042, 10829062, 12231245, 12244174, 12941616, 15190072, 15208330, 15556646, 16503409, 17094785, 25814554, 7642581, 7782294, 8621719, 8626543, 8662998, 8900205, 8995358, 9311917, 9535867, (Europe PMC)	0.37, 0.80	BioGRID, IntAct, MINT
CBLB	Two-hybrid, two hybrid array, two hybrid prey pooling approach	physical, physical association	25814554, (Europe PMC)	0.62	BioGRID, IntAct
CBLC	Affinity Capture-Western, Reconstituted Complex	physical	10571044, (Europe PMC)	NA	BioGRID
CCDC8	Affinity Capture-MS	physical	24711643, (Europe PMC)	NA	BioGRID
CCNL2	Affinity Capture-MS	physical	26186194, 28514442, (Europe PMC)	NA	BioGRID
CD2	Reconstituted Complex, anti bait coimmunoprecipitation, experimental interaction detection, pull down	phosphorylation reaction, physical, physical association	9677430, (Europe PMC)	0.57	BioGRID, IntAct, MINT
CD226	Affinity Capture-Western	physical	10591186, (Europe PMC)	NA	BioGRID
CD244	Affinity Capture-Western, anti bait coimmunoprecipitation	association, physical	15169881, 23346089, (Europe PMC)	0.35	BioGRID, IntAct
CD36	Affinity Capture-Western	physical	1715582, 7521304, (Europe PMC)	NA	BioGRID
CD3G	Affinity Capture-Western	physical	16888650, (Europe PMC)	NA	BioGRID
CD44	Affinity Capture-Western, Co-fractionation	physical	9573028, (Europe PMC)	NA	BioGRID
CD5	Affinity Capture-Western	physical	21757751, (Europe PMC)	NA	BioGRID
CDC37	Affinity Capture-MS, luminescence based mammalian interactome mapping	physical, physical association	25036637, 28514442, (Europe PMC)	0.40	BioGRID, IntAct
CDH1	Affinity Capture-Western, Reconstituted Complex	physical	12640114, (Europe PMC)	NA	BioGRID
CDK1	Affinity Capture-Western	physical	8910336, (Europe PMC)	NA	BioGRID
CHRNA7	Affinity Capture-Western	physical	11278378, (Europe PMC)	NA	BioGRID
CLTC	Biochemical Activity	physical	17785434, (Europe PMC)	NA	BioGRID
CMA1	Protein-peptide	physical	22653218, (Europe PMC)	NA	BioGRID
CSF1R	Affinity Capture-Western, Reconstituted Complex, pull down	association, physical	7681396, (Europe PMC)	0.35	BioGRID, IntAct, MINT
CSK	Affinity Capture-Western, pull down	association, physical	7524477, 8262983, (Europe PMC)	0.35	BioGRID, IntAct, MINT
CTLA4	Affinity Capture-Western, Co-localization, proximity ligation assay	physical, physical association	25241761, 9712716, (Europe PMC)	0.40	BioGRID, IntAct
CTNNB1	Biochemical Activity, Co-localization, proximity ligation assay	physical, physical association	12640114, 25241761, (Europe PMC)	0.40	BioGRID, IntAct
CTNND1	Affinity Capture-Western, Biochemical Activity	physical	12640114, 12835311, (Europe PMC)	NA	BioGRID
DAG1	Affinity Capture-Western, Reconstituted Complex, peptide array	physical, physical association	11724572, 17474147, (Europe PMC)	0.40	BioGRID, IntAct
DLG4	Affinity Capture-Western	physical	12419528, 9892651, (Europe PMC)	NA	BioGRID
EFS	Biochemical Activity, Reconstituted Complex, Two-hybrid, two hybrid array, two hybrid prey pooling approach, validated two hybrid	physical, physical association	12471123, 25416956, (Europe PMC)	0.49, 0.56	BioGRID, IntAct
ENO1	Biochemical Activity	physical	11078745, 14530346, (Europe PMC)	NA	BioGRID
EPHA3	Reconstituted Complex	physical	9632142, (Europe PMC)	NA	BioGRID
EPHA4	Affinity Capture-Western	physical	12084815, (Europe PMC)	NA	BioGRID
EPHA8	Affinity Capture-Western, Reconstituted Complex	physical	10498895, (Europe PMC)	NA	BioGRID
EPHB3	Reconstituted Complex	physical	9674711, (Europe PMC)	NA	BioGRID
FAS	Affinity Capture-Western, cosedimentation through density gradient	colocalization, physical	17159908, 8626376, (Europe PMC)	0.35	BioGRID, IntAct, MINT
FASLG	Co-localization, Protein-peptide, Reconstituted Complex, phage display, proximity ligation assay	direct interaction, physical, physical association	11741599, 17164290, 19807924, 25241761, 7589480, (Europe PMC)	0.61	BioGRID, IntAct
FGFR2	Affinity Capture-Western	physical	15190072, (Europe PMC)	NA	BioGRID
FRK	Affinity Capture-Western	physical	10229084, (Europe PMC)	NA	BioGRID
FYB1	Affinity Capture-Western, Reconstituted Complex, Two-hybrid	physical	10229084, 25814554, 7504057, 9207119, 9748251, (Europe PMC)	NA	BioGRID
FYN	Biochemical Activity, Co-crystal Structure, protein kinase assay	phosphorylation reaction, physical	11157475, 14993658, 27001024, 7687536, (Europe PMC)	0.62	BioGRID, IntAct, MINT
GAB3	Reconstituted Complex	physical	11739737, (Europe PMC)	NA	BioGRID
GJB7	Affinity Capture-MS	physical	28514442, (Europe PMC)	NA	BioGRID
GNB1	Affinity Capture-Western	physical	19917775, (Europe PMC)	NA	BioGRID
GNG2	Affinity Capture-Western	physical	19917775, (Europe PMC)	NA	BioGRID
GP6	Reconstituted Complex	physical	11943772, (Europe PMC)	NA	BioGRID
GRASP	Biochemical Activity	physical	15173175, (Europe PMC)	NA	BioGRID
GRB10	Biochemical Activity	physical	10871840, (Europe PMC)	NA	BioGRID
GRIN1	Biochemical Activity	physical	9670010, (Europe PMC)	NA	BioGRID
GRIN2A	Affinity Capture-Western, Reconstituted Complex	physical	10458595, 12419528, 12932824, 9892651, (Europe PMC)	NA	BioGRID
GRIN2B	Biochemical Activity, Reconstituted Complex	physical	10458595, 9670010, (Europe PMC)	NA	BioGRID
GRM1	Affinity Capture-Western	physical	15173175, (Europe PMC)	NA	BioGRID
HOXB5	Affinity Capture-MS	physical	26186194, 28514442, (Europe PMC)	NA	BioGRID
HSP90AA1	Affinity Capture-Luminescence, Affinity Capture-MS, Affinity Capture-Western	physical	16888650, 22939624, 28514442, (Europe PMC)	NA	BioGRID
HSP90AA4P	Affinity Capture-MS	physical	28514442, (Europe PMC)	NA	BioGRID
HSP90AB1	Affinity Capture-MS, anti tag coimmunoprecipitation, luminescence based mammalian interactome mapping	physical, physical association	22939624, 28514442, (Europe PMC)	0.52	BioGRID, IntAct
HSP90AB3P	Affinity Capture-MS	physical	28514442, (Europe PMC)	NA	BioGRID
HSP90AB4P	Affinity Capture-MS	physical	28514442, (Europe PMC)	NA	BioGRID
IFITM3	Affinity Capture-Western	physical	23055554, (Europe PMC)	NA	BioGRID
IKBKG	Affinity Capture-Western	physical	23131831, (Europe PMC)	NA	BioGRID
IL1B	Reconstituted Complex	physical	9230816, (Europe PMC)	NA	BioGRID
IL7R	Affinity Capture-Western	physical	7515933, (Europe PMC)	NA	BioGRID
ITCH	Affinity Capture-Western, Reconstituted Complex	physical	16387660, (Europe PMC)	NA	BioGRID
ITK	Reconstituted Complex	physical	10636929, 8810341, (Europe PMC)	NA	BioGRID
JAK2	Affinity Capture-Western, Reconstituted Complex	physical	10551884, (Europe PMC)	NA	BioGRID
KCNA2	Affinity Capture-Western	physical	11149959, (Europe PMC)	NA	BioGRID
KCNA4	Affinity Capture-Western	physical	11149959, (Europe PMC)	NA	BioGRID
KCNA5	Affinity Capture-Western	physical	11149959, (Europe PMC)	NA	BioGRID
KDM1A	Two-hybrid, two hybrid	physical, physical association	23455924, (Europe PMC)	0.37	BioGRID, IntAct, MINT
KHDRBS1	Affinity Capture-Western, Biochemical Activity, Protein-peptide, Reconstituted Complex	physical	11960376, 15190072, 16888650, 22745667, 9045636, (Europe PMC)	NA	BioGRID
LAT	Biochemical Activity, protein kinase assay	phosphorylation reaction, physical	16938345, (Europe PMC)	0.44	BioGRID, IntAct
LIMK1	Affinity Capture-MS, anti tag coimmunoprecipitation	association, physical	26496610, (Europe PMC)	0.35	BioGRID, IntAct
LRRIQ1	Affinity Capture-MS	physical	28514442, (Europe PMC)	NA	BioGRID
MAG	Reconstituted Complex	physical	7525550, (Europe PMC)	NA	BioGRID
MAP2	Affinity Capture-Western, coimmunoprecipitation, experimental interaction detection	phosphorylation reaction, physical	11546790, 15536091, (Europe PMC)	0.31, 0.44	BioGRID, IntAct, MINT
MAPRE1	Affinity Capture-MS, anti tag coimmunoprecipitation	association, physical	26496610, (Europe PMC)	0.35	BioGRID, IntAct
MAPT	Affinity Capture-Western, Biochemical Activity, Reconstituted Complex, pull down, surface plasmon resonance	direct interaction, physical, physical association	11826099, 16115884, 21692989, (Europe PMC)	0.40, 0.44	BioGRID, IntAct, MINT
MCAM	Affinity Capture-Western	physical	9756930, (Europe PMC)	NA	BioGRID
MED21	Affinity Capture-MS	physical	28514442, (Europe PMC)	NA	BioGRID
MED28	Affinity Capture-Western, anti bait coimmunoprecipitation, peptide array, protein kinase assay, pull down, two hybrid	association, phosphorylation reaction, physical, physical association	16899217, 16964398, (Europe PMC)	0.74	BioGRID, IntAct, MINT
MS4A1	Affinity Capture-Western	physical	7545683, (Europe PMC)	NA	BioGRID
MTUS2	Affinity Capture-MS	physical	28514442, (Europe PMC)	NA	BioGRID
MYH9	Affinity Capture-MS, anti tag coimmunoprecipitation	association, physical	26496610, (Europe PMC)	0.35	BioGRID, IntAct
MYO18A	Affinity Capture-MS, anti tag coimmunoprecipitation	association, physical	26496610, (Europe PMC)	0.35	BioGRID, IntAct
NDFIP2	Affinity Capture-Western	physical	20534535, (Europe PMC)	NA	BioGRID
NEDD4	Biochemical Activity, Reconstituted Complex	physical	19953087, (Europe PMC)	NA	BioGRID
NEDD9	Affinity Capture-Western	physical	9360983, (Europe PMC)	NA	BioGRID
NMT1	Biochemical Activity	physical	11594778, (Europe PMC)	NA	BioGRID
NOS1AP	Two-hybrid, two hybrid array	physical, physical association	25814554, (Europe PMC)	0.37	BioGRID, IntAct
NPHS1	Affinity Capture-Western, Biochemical Activity, Reconstituted Complex	physical	12668668, 12846735, (Europe PMC)	NA	BioGRID
NR3C1	Affinity Capture-Western	physical	16888650, (Europe PMC)	NA	BioGRID
NTRK2	Affinity Capture-Western, Reconstituted Complex	physical	9648856, (Europe PMC)	NA	BioGRID
PAG1	Affinity Capture-Western, Reconstituted Complex, anti bait coimmunoprecipitation, coimmunoprecipitation, peptide array	association, physical, physical association	10790433, 18056706, 23866081, (Europe PMC)	0.62	BioGRID, IntAct, MINT
PCDHGC3	Affinity Capture-MS	physical	28514442, (Europe PMC)	NA	BioGRID
PDE4D	Far Western	physical	10571082, (Europe PMC)	NA	BioGRID
PECAM1	Affinity Capture-Western	physical	10858437, (Europe PMC)	NA	BioGRID
PIK3R1	Reconstituted Complex, mammalian protein protein interaction trap	physical, physical association	25416956, 8294442, (Europe PMC)	0.37	BioGRID, IntAct
PIK3R2	Reconstituted Complex	physical	1334406, (Europe PMC)	NA	BioGRID
PIK3R3	Two-hybrid, two hybrid array	physical, physical association	25814554, (Europe PMC)	0.37	BioGRID, IntAct
PLCG2	Reconstituted Complex	physical	8395016, (Europe PMC)	NA	BioGRID
PMS2	Affinity Capture-MS	physical	26496610, (Europe PMC)	NA	BioGRID
PRKCD	Co-localization, anti bait coimmunoprecipitation, enzyme linked immunosorbent assay, protein kinase assay, proximity ligation assay	phosphorylation reaction, physical, physical association	10383400, 12721299, 25241761, (Europe PMC)	0.75	BioGRID, IntAct
PRKCI	Affinity Capture-MS	physical	28514442, (Europe PMC)	NA	BioGRID
PRKCQ	Affinity Capture-Western, Biochemical Activity, Reconstituted Complex, Two-hybrid, anti bait coimmunoprecipitation, enzyme linked immunosorbent assay, protein kinase assay, pull down, two hybrid	phosphorylation reaction, physical, physical association	10383400, (Europe PMC)	0.66	BioGRID, IntAct
PRMT6	Two-hybrid, two hybrid	physical, physical association	23455924, (Europe PMC)	0.37	BioGRID, IntAct, MINT
PRUNE2	Affinity Capture-MS	physical	28514442, (Europe PMC)	NA	BioGRID
PTK2	Affinity Capture-Western, Co-crystal Structure	physical	11278857, 12558988, (Europe PMC)	NA	BioGRID
PTK2B	Affinity Capture-Western, Biochemical Activity, Reconstituted Complex, coimmunoprecipitation, pull down	association, physical	10229084, 10867021, 9091579, 9104812, (Europe PMC)	0.46	BioGRID, IntAct, MINT
PTPN11	Affinity Capture-Western	physical	10212213, 11157475, (Europe PMC)	NA	BioGRID
PTPN5	Affinity Capture-Western	physical	11983687, (Europe PMC)	NA	BioGRID
PTPRA	Affinity Capture-Western	physical	9535845, (Europe PMC)	NA	BioGRID
PTPRD	Affinity Capture-MS	physical	28514442, (Europe PMC)	NA	BioGRID
PXN	Affinity Capture-Western	physical	10804218, (Europe PMC)	NA	BioGRID
RACK1	Affinity Capture-Western, Reconstituted Complex	physical	11943848, 12524444, (Europe PMC)	NA	BioGRID
RAF1	Affinity Capture-Western, Reconstituted Complex	physical	7517401, (Europe PMC)	NA	BioGRID
RPL10	Reconstituted Complex	physical	12138090, (Europe PMC)	NA	BioGRID
RPS6KA1	Affinity Capture-MS	physical	28514442, (Europe PMC)	NA	BioGRID
RPS6KA2	Affinity Capture-MS	physical	28514442, (Europe PMC)	NA	BioGRID
RPS6KA3	Affinity Capture-MS	physical	28514442, (Europe PMC)	NA	BioGRID
SDC3	Reconstituted Complex	physical	9553134, (Europe PMC)	NA	BioGRID
SH2D1A	Affinity Capture-Western, Reconstituted Complex, anti tag coimmunoprecipitation, mammalian protein protein interaction trap	physical, physical association	12458214, 12545174, 16983070, 25416956, (Europe PMC)	0.37, 0.40	BioGRID, IntAct
SH3BP2	Two-hybrid	physical	9846481, (Europe PMC)	NA	BioGRID
SH3KBP1	Affinity Capture-Western	physical	15707590, (Europe PMC)	NA	BioGRID
SIT1	Affinity Capture-Western	physical	10209036, (Europe PMC)	NA	BioGRID
SKAP1	Affinity Capture-Western, Reconstituted Complex, coimmunoprecipitation	association, physical	10229084, 12171928, 9195899, 9748251, (Europe PMC)	0.35	BioGRID, IntAct, MINT
SKAP2	Affinity Capture-Western, Biochemical Activity	physical	12893833, 9837776, (Europe PMC)	NA	BioGRID
SLAMF1	Reconstituted Complex	physical	12545174, (Europe PMC)	NA	BioGRID
SLC25A11	Affinity Capture-MS	physical	26186194, (Europe PMC)	NA	BioGRID
SLC25A41	Affinity Capture-MS	physical	26186194, 28514442, (Europe PMC)	NA	BioGRID
SLC4A8	Affinity Capture-MS	physical	28514442, (Europe PMC)	NA	BioGRID
SNCA	Biochemical Activity	physical	11078745, 11162638, 15033366, (Europe PMC)	NA	BioGRID
SOCS1	Reconstituted Complex	physical	10022833, (Europe PMC)	NA	BioGRID
SOS1	Reconstituted Complex, peptide array	physical, physical association	17474147, 9856337, (Europe PMC)	0.40	BioGRID, IntAct
SRC	Affinity Capture-MS, Affinity Capture-Western, Protein-peptide, anti bait coimmunoprecipitation	physical, physical association	16966330, 19711372, 28514442, 9169421, (Europe PMC)	0.40	BioGRID, IntAct, MINT
STAT3	Reconstituted Complex	physical	12244095, (Europe PMC)	NA	BioGRID
SUV39H1	Two-hybrid, two hybrid	physical, physical association	23455924, (Europe PMC)	0.37	BioGRID, IntAct, MINT
SYK	Affinity Capture-Western, Reconstituted Complex	physical	9535867, (Europe PMC)	NA	BioGRID
TCAP	Two-hybrid, two hybrid array	physical, physical association	21988832, (Europe PMC)	0.37	BioGRID, IntAct
THY1	Affinity Capture-Western	physical	1351058, (Europe PMC)	NA	BioGRID
TMEM132A	Affinity Capture-MS, anti tag coimmunoprecipitation	association, physical	26496610, (Europe PMC)	0.35	BioGRID, IntAct
TMEM185A	Affinity Capture-MS	physical	26186194, 28514442, (Europe PMC)	NA	BioGRID
TNF	Reconstituted Complex	physical	9230816, (Europe PMC)	NA	BioGRID
TNFRSF10B	Affinity Capture-MS	physical	28514442, (Europe PMC)	NA	BioGRID
TNFRSF1A	Co-fractionation	physical	12753742, (Europe PMC)	NA	BioGRID
TNK2	Affinity Capture-Western, Reconstituted Complex	physical	11087735, (Europe PMC)	NA	BioGRID
TNNT1	Two-hybrid, two hybrid	physical, physical association	21900206, (Europe PMC)	0.37	BioGRID, IntAct, MINT
TOM1L1	Affinity Capture-Western, Reconstituted Complex	physical	11711534, 20182632, (Europe PMC)	NA	BioGRID
TRAF6	Reconstituted Complex	physical	22447928, (Europe PMC)	NA	BioGRID
TRAT1	Reconstituted Complex	physical	10790433, (Europe PMC)	NA	BioGRID
TRPC6	Affinity Capture-Western, Biochemical Activity, Reconstituted Complex	physical	14761972, (Europe PMC)	NA	BioGRID
TRPV4	Affinity Capture-Western	physical	12538589, (Europe PMC)	NA	BioGRID
TSNAX	Affinity Capture-MS, anti tag coimmunoprecipitation	association, physical	26496610, (Europe PMC)	0.35	BioGRID, IntAct
TUBA3C	Affinity Capture-Western, Reconstituted Complex	physical	11826099, (Europe PMC)	NA	BioGRID
TYK2	Affinity Capture-Western, Reconstituted Complex	physical	9196040, (Europe PMC)	NA	BioGRID
UHRF2	Far Western, antibody array	physical, physical association	21952639, (Europe PMC)	0.40	BioGRID, IntAct
UNC119	Affinity Capture-Western, Reconstituted Complex	physical	14757743, (Europe PMC)	NA	BioGRID
VAV1	Affinity Capture-Western, Two-hybrid	physical	11262396, 9822663, (Europe PMC)	NA	BioGRID
VAV2	Two-hybrid	physical	11262396, (Europe PMC)	NA	BioGRID
WAS	Affinity Capture-Western, Biochemical Activity, Reconstituted Complex, anti bait coimmunoprecipitation, experimental interaction detection, pull down	direct interaction, phosphorylation reaction, physical, physical association	10532312, 12431372, 14707117, 7565724, 8805332, (Europe PMC)	0.70	BioGRID, IntAct, MINT
WBP11	Two-hybrid, two hybrid array, two hybrid prey pooling approach, validated two hybrid	physical, physical association	25416956, (Europe PMC)	0.56	BioGRID, IntAct
YES1	Affinity Capture-MS, Affinity Capture-Western	physical	12640114, 28514442, (Europe PMC)	NA	BioGRID
ZAP70	Affinity Capture-Western, Phenotypic Enhancement	genetic, physical	7760813, (Europe PMC)	NA	BioGRID
ZNFX1	Affinity Capture-MS, anti tag coimmunoprecipitation	association, physical	26496610, (Europe PMC)	0.35	BioGRID, IntAct

Visualize Download

Interacting partner	Detection method	Interaction type	PubMed IDs	Interaction Score	Source
ABL1	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
ABL2	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
ADAM15	Reconstituted Complex, filter binding, pull down	physical, physical association	11741929, 16374509, (Europe PMC)	0.59	BioGRID, IntAct, MINT
AIRE	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
AKAP6	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
ANLN	Affinity Capture-MS, anti tag coimmunoprecipitation	association, physical	26496610, (Europe PMC)	0.35	BioGRID, IntAct
APOL5	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
ARHGAP32	Affinity Capture-Western, Reconstituted Complex, Two-hybrid, anti bait coimmunoprecipitation, anti tag coimmunoprecipitation, pull down, two hybrid	direct interaction, physical, physical association	12788081, (Europe PMC)	0.63	BioGRID, IntAct
ARHGAP33	anti bait coimmunoprecipitation, two hybrid	physical association	16777849, (Europe PMC)	0.51	IntAct
ARHGEF11	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
ASAP1	enzyme linked immunosorbent assay, peptide array	direct interaction, physical association	16636290, 17474147, (Europe PMC)	0.61	IntAct, MINT
ASAP2	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
ASB16	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
ATXN1	Two-hybrid, two hybrid	physical, physical association	16713569, (Europe PMC)	0.37	BioGRID, IntAct
BAZ2A	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
BCAR1	Affinity Capture-Western, Reconstituted Complex, Two-hybrid, coimmunoprecipitation, peptide array, pull down, two hybrid array, two hybrid prey pooling approach	association, physical, physical association	10739664, 17474147, 9188452, 9360983, (Europe PMC)	0.49, 0.62	BioGRID, IntAct, MINT
BCL3	Reconstituted Complex, pull down	physical, physical association	16099425, 9576921, (Europe PMC)	0.40	BioGRID, IntAct, MINT
BET1	proximity-dependent biotin identification	association	29568061, (Europe PMC)	0.35	IntAct
BMP8B	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
BRCA2	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
BRPF3	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
C6	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
C7orf25	Two-hybrid, two hybrid	physical, physical association	21900206, (Europe PMC)	0.37	BioGRID, IntAct, MINT
C8orf33	Two-hybrid, two hybrid	physical, physical association	21900206, (Europe PMC)	0.37	BioGRID, IntAct, MINT
CACNA1F	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
CAST	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
CBL	Affinity Capture-Western, Biochemical Activity, Reconstituted Complex, Two-hybrid, anti bait coimmunoprecipitation, coimmunoprecipitation, competition binding, experimental interaction detection, pull down, two hybrid array	phosphorylation reaction, physical, physical association	10629042, 10829062, 12231245, 12244174, 12941616, 15190072, 15208330, 15556646, 16503409, 17094785, 25814554, 7642581, 7782294, 8621719, 8626543, 8662998, 8900205, 8995358, 9311917, 9535867, (Europe PMC)	0.37, 0.80	BioGRID, IntAct, MINT
CBLB	Two-hybrid, two hybrid array, two hybrid prey pooling approach	physical, physical association	25814554, (Europe PMC)	0.62	BioGRID, IntAct
CCKBR	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
CCR10	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
CD2	Reconstituted Complex, anti bait coimmunoprecipitation, experimental interaction detection, pull down	phosphorylation reaction, physical, physical association	9677430, (Europe PMC)	0.57	BioGRID, IntAct, MINT
CD244	Affinity Capture-Western, anti bait coimmunoprecipitation	association, physical	15169881, 23346089, (Europe PMC)	0.35	BioGRID, IntAct
CD2AP	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
CDC27	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
CDC37	Affinity Capture-MS, luminescence based mammalian interactome mapping	physical, physical association	25036637, 28514442, (Europe PMC)	0.40	BioGRID, IntAct
CDCP1	anti bait coimmunoprecipitation	association	21233420, (Europe PMC)	0.35	IntAct
CDKL5	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
CELSR3	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
CENPA	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
CENPV	pull down	physical association	19930468, (Europe PMC)	0.40	IntAct, MINT
CHAF1A	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
CKAP5	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
CNTFR	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
CNTNAP1	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
CSF1R	Affinity Capture-Western, Reconstituted Complex, pull down	association, physical	7681396, (Europe PMC)	0.35	BioGRID, IntAct, MINT
CSK	Affinity Capture-Western, pull down	association, physical	7524477, 8262983, (Europe PMC)	0.35	BioGRID, IntAct, MINT
CSMD2	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
CTLA4	Affinity Capture-Western, Co-localization, proximity ligation assay	physical, physical association	25241761, 9712716, (Europe PMC)	0.40	BioGRID, IntAct
CTNNB1	Biochemical Activity, Co-localization, proximity ligation assay	physical, physical association	12640114, 25241761, (Europe PMC)	0.40	BioGRID, IntAct
CYP4F2	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
DAB2	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
DAG1	Affinity Capture-Western, Reconstituted Complex, peptide array	physical, physical association	11724572, 17474147, (Europe PMC)	0.40	BioGRID, IntAct
DCBLD2	pull down	physical association	23770091, (Europe PMC)	0.40	IntAct, MINT
DDX41	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
DKKL1	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
DLGAP1	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
DLGAP2	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
DLGAP3	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
DLGAP4	peptide array, two hybrid array, two hybrid prey pooling approach	physical association	17474147, (Europe PMC)	0.40, 0.49	IntAct
DLX4	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
DNASE1L2	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
DNM3	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
DOCK1	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
DOCK3	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
DUSP15	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
EFS	Biochemical Activity, Reconstituted Complex, Two-hybrid, two hybrid array, two hybrid prey pooling approach, validated two hybrid	physical, physical association	12471123, 25416956, (Europe PMC)	0.49, 0.56	BioGRID, IntAct
EPB41L3	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
EPS15	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
ERBB2	nuclear magnetic resonance, surface plasmon resonance	direct interaction	24815698, (Europe PMC)	0.56	IntAct, MINT
EXTL3	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
F2RL2	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
FAM110A	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
FANCA	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
FAS	Affinity Capture-Western, cosedimentation through density gradient	colocalization, physical	17159908, 8626376, (Europe PMC)	0.35	BioGRID, IntAct, MINT
FASLG	Co-localization, Protein-peptide, Reconstituted Complex, phage display, proximity ligation assay	direct interaction, physical, physical association	11741599, 17164290, 19807924, 25241761, 7589480, (Europe PMC)	0.61	BioGRID, IntAct
FCGR2B	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
FCGR2C	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
FLNA	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
FLNC	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
FLT1	anti bait coimmunoprecipitation	physical association	12509223, (Europe PMC)	0.40	IntAct
FN1	enzyme linked immunosorbent assay, surface plasmon resonance	direct interaction	17130124, (Europe PMC)	0.56	IntAct, MINT
FOXF2	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
FYB1	coimmunoprecipitation, peptide array, pull down, two hybrid array, validated two hybrid	association, direct interaction, physical association	10409671, 17474147, 25814554, 9207119, (Europe PMC)	0.49, 0.82	IntAct, MINT
FYN	Biochemical Activity, Co-crystal Structure, protein kinase assay	phosphorylation reaction, physical	11157475, 14993658, 27001024, 7687536, (Europe PMC)	0.62	BioGRID, IntAct, MINT
G3BP1	anti tag coimmunoprecipitation	physical association	15743820, (Europe PMC)	0.40	IntAct, MINT
GABBR1	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
GAD1	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
GCFC2	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
GNS	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
GP6	anti bait coimmunoprecipitation, phage display, pull down	association, physical association	1715582, 19940238, (Europe PMC)	0.52, 0.56	IntAct
GPR45	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
GPR63	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
GSTZ1	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
GTF3A	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
GUCY2D	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
HAVCR2	anti bait coimmunoprecipitation, pull down	association	26492563, (Europe PMC)	0.46	IntAct
HCN2	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
HCN4	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
HDAC6	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
HEXA	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
HNRNPR	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
HOXC8	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
HSP90AB1	Affinity Capture-MS, anti tag coimmunoprecipitation, luminescence based mammalian interactome mapping	physical, physical association	22939624, 28514442, (Europe PMC)	0.52	BioGRID, IntAct
HTR6	anti bait coimmunoprecipitation, anti tag coimmunoprecipitation, pull down, two hybrid	direct interaction, physical association	17189269, (Europe PMC)	0.63	IntAct
IL3RA	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
ISG20L2	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
KDM1A	Two-hybrid, two hybrid	physical, physical association	23455924, (Europe PMC)	0.37	BioGRID, IntAct, MINT
KDR	anti tag coimmunoprecipitation	physical association	16966330, (Europe PMC)	0.40	IntAct, MINT
KHDRBS1	coimmunoprecipitation, pull down, two hybrid	direct interaction, physical association	22641034, 7516469, 9045636, (Europe PMC)	0.74	IntAct, MINT
KMT2B	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
LAT	Biochemical Activity, protein kinase assay	phosphorylation reaction, physical	16938345, (Europe PMC)	0.44	BioGRID, IntAct
LCP2	pull down	physical association	15929943, (Europe PMC)	0.40	IntAct, MINT
LIMK1	Affinity Capture-MS, anti tag coimmunoprecipitation	association, physical	26496610, (Europe PMC)	0.35	BioGRID, IntAct
LRBA	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
LTBP2	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
MAP2	Affinity Capture-Western, coimmunoprecipitation, experimental interaction detection	phosphorylation reaction, physical	11546790, 15536091, (Europe PMC)	0.31, 0.44	BioGRID, IntAct, MINT
MAP4K1	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
MAP4K5	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
MAPRE1	Affinity Capture-MS, anti tag coimmunoprecipitation	association, physical	26496610, (Europe PMC)	0.35	BioGRID, IntAct
MAPT	Affinity Capture-Western, Biochemical Activity, Reconstituted Complex, pull down, surface plasmon resonance	direct interaction, physical, physical association	11826099, 16115884, 21692989, (Europe PMC)	0.40, 0.44	BioGRID, IntAct, MINT
MED14	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
MED28	Affinity Capture-Western, anti bait coimmunoprecipitation, peptide array, protein kinase assay, pull down, two hybrid	association, phosphorylation reaction, physical, physical association	16899217, 16964398, (Europe PMC)	0.74	BioGRID, IntAct, MINT
MEPE	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
MKI67	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
MOS	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
MYH9	Affinity Capture-MS, anti tag coimmunoprecipitation	association, physical	26496610, (Europe PMC)	0.35	BioGRID, IntAct
MYO18A	Affinity Capture-MS, anti tag coimmunoprecipitation	association, physical	26496610, (Europe PMC)	0.35	BioGRID, IntAct
NBEA	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
NCK1	anti bait coimmunoprecipitation	physical association	16966330, (Europe PMC)	0.40	IntAct, MINT
NCKAP5	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
NCKIPSD	mammalian protein protein interaction trap, peptide array	physical association	17474147, 25416956, (Europe PMC)	0.57	IntAct
NEK8	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
NELFB	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
NFASC	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
NFS1	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
NKX2-1	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
NOS1AP	Two-hybrid, two hybrid array	physical, physical association	25814554, (Europe PMC)	0.37	BioGRID, IntAct
NPVF	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
NR5A1	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
OCRL	anti tag coimmunoprecipitation	association	25107275, (Europe PMC)	0.35	IntAct, MINT
ORC1	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
PAG1	Affinity Capture-Western, Reconstituted Complex, anti bait coimmunoprecipitation, coimmunoprecipitation, peptide array	association, physical, physical association	10790433, 18056706, 23866081, (Europe PMC)	0.62	BioGRID, IntAct, MINT
PAK2	filter binding	physical association	16374509, (Europe PMC)	0.40	IntAct, MINT
PAX3	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
PAX7	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
PDCD6IP	isothermal titration calorimetry, nuclear magnetic resonance, pull down, two hybrid, x ray scattering	direct interaction, physical association	22641034, (Europe PMC)	0.67	IntAct, MINT
PDGFRB	coimmunoprecipitation, pull down	association	1661130, 7685273, 7687537, (Europe PMC)	0.64	IntAct, MINT
PDIA2	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
PIK3R1	Reconstituted Complex, mammalian protein protein interaction trap	physical, physical association	25416956, 8294442, (Europe PMC)	0.37	BioGRID, IntAct
PIK3R3	Two-hybrid, two hybrid array	physical, physical association	25814554, (Europe PMC)	0.37	BioGRID, IntAct
PKD1	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
PMS2	anti tag coimmunoprecipitation	association	26496610, (Europe PMC)	0.35	IntAct
POLD1	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
PPP1R12A	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
PPP1R3D	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
PRICKLE3	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
PRKCD	Co-localization, anti bait coimmunoprecipitation, enzyme linked immunosorbent assay, protein kinase assay, proximity ligation assay	phosphorylation reaction, physical, physical association	10383400, 12721299, 25241761, (Europe PMC)	0.75	BioGRID, IntAct
PRKCQ	Affinity Capture-Western, Biochemical Activity, Reconstituted Complex, Two-hybrid, anti bait coimmunoprecipitation, enzyme linked immunosorbent assay, protein kinase assay, pull down, two hybrid	phosphorylation reaction, physical, physical association	10383400, (Europe PMC)	0.66	BioGRID, IntAct
PRMT6	Two-hybrid, two hybrid	physical, physical association	23455924, (Europe PMC)	0.37	BioGRID, IntAct, MINT
PRX	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
PTK2B	Affinity Capture-Western, Biochemical Activity, Reconstituted Complex, coimmunoprecipitation, pull down	association, physical	10229084, 10867021, 9091579, 9104812, (Europe PMC)	0.46	BioGRID, IntAct, MINT
PTPN4	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
PTPRE	anti tag coimmunoprecipitation	physical association	14980517, (Europe PMC)	0.40	IntAct, MINT
RAPGEF1	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
RIMS1	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
RIMS2	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
RIN3	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
RP1L1	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
RPP38	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
RRAS	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
RTN4	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
SCARF2	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
SELENON {ECO:0000303\|PubMed:27645994,	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
SEMA7A	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
SF3B4	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
SH2D1A	Affinity Capture-Western, Reconstituted Complex, anti tag coimmunoprecipitation, mammalian protein protein interaction trap	physical, physical association	12458214, 12545174, 16983070, 25416956, (Europe PMC)	0.37, 0.40	BioGRID, IntAct
SHANK3	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
SHC1	pull down	direct interaction	7516469, (Europe PMC)	0.44	IntAct, MINT
SHROOM2	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
SKAP1	Affinity Capture-Western, Reconstituted Complex, coimmunoprecipitation	association, physical	10229084, 12171928, 9195899, 9748251, (Europe PMC)	0.35	BioGRID, IntAct, MINT
SLC24A1	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
SNX12	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
SNX17	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
SNX3	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
SNX8	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
SOS1	Reconstituted Complex, peptide array	physical, physical association	17474147, 9856337, (Europe PMC)	0.40	BioGRID, IntAct
SOS2	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
SP1	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
SPHK1	anti bait coimmunoprecipitation	direct interaction	16316995, (Europe PMC)	0.44	IntAct
SPHK2	anti bait coimmunoprecipitation	direct interaction	16316995, (Europe PMC)	0.44	IntAct
SRC	Affinity Capture-MS, Affinity Capture-Western, Protein-peptide, anti bait coimmunoprecipitation	physical, physical association	16966330, 19711372, 28514442, 9169421, (Europe PMC)	0.40	BioGRID, IntAct, MINT
SUV39H1	Two-hybrid, two hybrid	physical, physical association	23455924, (Europe PMC)	0.37	BioGRID, IntAct, MINT
SUV39H2	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
SYNJ2	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
TCAP	Two-hybrid, two hybrid array	physical, physical association	21988832, (Europe PMC)	0.37	BioGRID, IntAct
TDRD1	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
TGOLN2	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
TMEM132A	Affinity Capture-MS, anti tag coimmunoprecipitation	association, physical	26496610, (Europe PMC)	0.35	BioGRID, IntAct
TMPO	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
TNNT1	Two-hybrid, two hybrid	physical, physical association	21900206, (Europe PMC)	0.37	BioGRID, IntAct, MINT
TRAIP	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
TRIM39	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
TSKS	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
TSNAX	Affinity Capture-MS, anti tag coimmunoprecipitation	association, physical	26496610, (Europe PMC)	0.35	BioGRID, IntAct
TULP1	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
TULP4	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
UHRF2	Far Western, antibody array	physical, physical association	21952639, (Europe PMC)	0.40	BioGRID, IntAct
VPS13A	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
WAS	Affinity Capture-Western, Biochemical Activity, Reconstituted Complex, anti bait coimmunoprecipitation, experimental interaction detection, pull down	direct interaction, phosphorylation reaction, physical, physical association	10532312, 12431372, 14707117, 7565724, 8805332, (Europe PMC)	0.70	BioGRID, IntAct, MINT
WBP11	Two-hybrid, two hybrid array, two hybrid prey pooling approach, validated two hybrid	physical, physical association	25416956, (Europe PMC)	0.56	BioGRID, IntAct
WIPF1	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
WNK2	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
XRCC1	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
ZNFX1	Affinity Capture-MS, anti tag coimmunoprecipitation	association, physical	26496610, (Europe PMC)	0.35	BioGRID, IntAct

Visualize Download

Interacting partner	Detection method	Interaction type	PubMed IDs	Interaction Score	Source
ADAM15	Reconstituted Complex, filter binding, pull down	physical, physical association	11741929, 16374509, (Europe PMC)	0.59	BioGRID, IntAct, MINT
ASAP1	enzyme linked immunosorbent assay, peptide array	direct interaction, physical association	16636290, 17474147, (Europe PMC)	0.61	IntAct, MINT
BCAR1	Affinity Capture-Western, Reconstituted Complex, Two-hybrid, coimmunoprecipitation, peptide array, pull down, two hybrid array, two hybrid prey pooling approach	association, physical, physical association	10739664, 17474147, 9188452, 9360983, (Europe PMC)	0.49, 0.62	BioGRID, IntAct, MINT
BCL3	Reconstituted Complex, pull down	physical, physical association	16099425, 9576921, (Europe PMC)	0.40	BioGRID, IntAct, MINT
C7orf25	Two-hybrid, two hybrid	physical, physical association	21900206, (Europe PMC)	0.37	BioGRID, IntAct, MINT
C8orf33	Two-hybrid, two hybrid	physical, physical association	21900206, (Europe PMC)	0.37	BioGRID, IntAct, MINT
CBL	Affinity Capture-Western, Biochemical Activity, Reconstituted Complex, Two-hybrid, anti bait coimmunoprecipitation, coimmunoprecipitation, competition binding, experimental interaction detection, pull down, two hybrid array	phosphorylation reaction, physical, physical association	10629042, 10829062, 12231245, 12244174, 12941616, 15190072, 15208330, 15556646, 16503409, 17094785, 25814554, 7642581, 7782294, 8621719, 8626543, 8662998, 8900205, 8995358, 9311917, 9535867, (Europe PMC)	0.37, 0.80	BioGRID, IntAct, MINT
CD2	Reconstituted Complex, anti bait coimmunoprecipitation, experimental interaction detection, pull down	phosphorylation reaction, physical, physical association	9677430, (Europe PMC)	0.57	BioGRID, IntAct, MINT
CENPV	pull down	physical association	19930468, (Europe PMC)	0.40	IntAct, MINT
CSF1R	Affinity Capture-Western, Reconstituted Complex, pull down	association, physical	7681396, (Europe PMC)	0.35	BioGRID, IntAct, MINT
CSK	Affinity Capture-Western, pull down	association, physical	7524477, 8262983, (Europe PMC)	0.35	BioGRID, IntAct, MINT
DCBLD2	pull down	physical association	23770091, (Europe PMC)	0.40	IntAct, MINT
ERBB2	nuclear magnetic resonance, surface plasmon resonance	direct interaction	24815698, (Europe PMC)	0.56	IntAct, MINT
FAS	Affinity Capture-Western, cosedimentation through density gradient	colocalization, physical	17159908, 8626376, (Europe PMC)	0.35	BioGRID, IntAct, MINT
FN1	enzyme linked immunosorbent assay, surface plasmon resonance	direct interaction	17130124, (Europe PMC)	0.56	IntAct, MINT
FYB1	coimmunoprecipitation, peptide array, pull down, two hybrid array, validated two hybrid	association, direct interaction, physical association	10409671, 17474147, 25814554, 9207119, (Europe PMC)	0.49, 0.82	IntAct, MINT
FYN	Biochemical Activity, Co-crystal Structure, protein kinase assay	phosphorylation reaction, physical	11157475, 14993658, 27001024, 7687536, (Europe PMC)	0.62	BioGRID, IntAct, MINT
G3BP1	anti tag coimmunoprecipitation	physical association	15743820, (Europe PMC)	0.40	IntAct, MINT
KDM1A	Two-hybrid, two hybrid	physical, physical association	23455924, (Europe PMC)	0.37	BioGRID, IntAct, MINT
KDR	anti tag coimmunoprecipitation	physical association	16966330, (Europe PMC)	0.40	IntAct, MINT
KHDRBS1	coimmunoprecipitation, pull down, two hybrid	direct interaction, physical association	22641034, 7516469, 9045636, (Europe PMC)	0.74	IntAct, MINT
LCP2	pull down	physical association	15929943, (Europe PMC)	0.40	IntAct, MINT
MAP2	Affinity Capture-Western, coimmunoprecipitation, experimental interaction detection	phosphorylation reaction, physical	11546790, 15536091, (Europe PMC)	0.31, 0.44	BioGRID, IntAct, MINT
MAPT	Affinity Capture-Western, Biochemical Activity, Reconstituted Complex, pull down, surface plasmon resonance	direct interaction, physical, physical association	11826099, 16115884, 21692989, (Europe PMC)	0.40, 0.44	BioGRID, IntAct, MINT
MED28	Affinity Capture-Western, anti bait coimmunoprecipitation, peptide array, protein kinase assay, pull down, two hybrid	association, phosphorylation reaction, physical, physical association	16899217, 16964398, (Europe PMC)	0.74	BioGRID, IntAct, MINT
NCK1	anti bait coimmunoprecipitation	physical association	16966330, (Europe PMC)	0.40	IntAct, MINT
OCRL	anti tag coimmunoprecipitation	association	25107275, (Europe PMC)	0.35	IntAct, MINT
PAG1	Affinity Capture-Western, Reconstituted Complex, anti bait coimmunoprecipitation, coimmunoprecipitation, peptide array	association, physical, physical association	10790433, 18056706, 23866081, (Europe PMC)	0.62	BioGRID, IntAct, MINT
PAK2	filter binding	physical association	16374509, (Europe PMC)	0.40	IntAct, MINT
PDCD6IP	isothermal titration calorimetry, nuclear magnetic resonance, pull down, two hybrid, x ray scattering	direct interaction, physical association	22641034, (Europe PMC)	0.67	IntAct, MINT
PDGFRB	coimmunoprecipitation, pull down	association	1661130, 7685273, 7687537, (Europe PMC)	0.64	IntAct, MINT
PRMT6	Two-hybrid, two hybrid	physical, physical association	23455924, (Europe PMC)	0.37	BioGRID, IntAct, MINT
PTK2B	Affinity Capture-Western, Biochemical Activity, Reconstituted Complex, coimmunoprecipitation, pull down	association, physical	10229084, 10867021, 9091579, 9104812, (Europe PMC)	0.46	BioGRID, IntAct, MINT
PTPRE	anti tag coimmunoprecipitation	physical association	14980517, (Europe PMC)	0.40	IntAct, MINT
SHC1	pull down	direct interaction	7516469, (Europe PMC)	0.44	IntAct, MINT
SKAP1	Affinity Capture-Western, Reconstituted Complex, coimmunoprecipitation	association, physical	10229084, 12171928, 9195899, 9748251, (Europe PMC)	0.35	BioGRID, IntAct, MINT
SRC	Affinity Capture-MS, Affinity Capture-Western, Protein-peptide, anti bait coimmunoprecipitation	physical, physical association	16966330, 19711372, 28514442, 9169421, (Europe PMC)	0.40	BioGRID, IntAct, MINT
SUV39H1	Two-hybrid, two hybrid	physical, physical association	23455924, (Europe PMC)	0.37	BioGRID, IntAct, MINT
TNNT1	Two-hybrid, two hybrid	physical, physical association	21900206, (Europe PMC)	0.37	BioGRID, IntAct, MINT
WAS	Affinity Capture-Western, Biochemical Activity, Reconstituted Complex, anti bait coimmunoprecipitation, experimental interaction detection, pull down	direct interaction, phosphorylation reaction, physical, physical association	10532312, 12431372, 14707117, 7565724, 8805332, (Europe PMC)	0.70	BioGRID, IntAct, MINT

Visualize Download

Interacting partner	Detection method	Interaction type	PubMed IDs	Interaction Score	Source
ABI1	array technology	direct interaction	20598684, (Europe PMC)	0.44	IntAct, MINT
ABL1	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
ABL2	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
ACBD7	Affinity Capture-MS	physical	28514442, (Europe PMC)	NA	BioGRID
ADAM15	Reconstituted Complex, filter binding, pull down	physical, physical association	11741929, 16374509, (Europe PMC)	0.59	BioGRID, IntAct, MINT
ADD2	Affinity Capture-Western, Reconstituted Complex	physical	11526103, (Europe PMC)	NA	BioGRID
AIRE	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
AKAP6	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
ANKRD12	Affinity Capture-MS	physical	26186194, (Europe PMC)	NA	BioGRID
ANLN	Affinity Capture-MS, anti tag coimmunoprecipitation	association, physical	26496610, (Europe PMC)	0.35	BioGRID, IntAct
APOL5	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
ARHGAP32	Affinity Capture-Western, Reconstituted Complex, Two-hybrid, anti bait coimmunoprecipitation, anti tag coimmunoprecipitation, pull down, two hybrid	direct interaction, physical, physical association	12788081, (Europe PMC)	0.63	BioGRID, IntAct
ARHGAP33	anti bait coimmunoprecipitation, two hybrid	physical association	16777849, (Europe PMC)	0.51	IntAct
ARHGEF11	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
ASAP1	enzyme linked immunosorbent assay, peptide array	direct interaction, physical association	16636290, 17474147, (Europe PMC)	0.61	IntAct, MINT
ASAP2	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
ASB16	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
ATXN1	Two-hybrid, two hybrid	physical, physical association	16713569, (Europe PMC)	0.37	BioGRID, IntAct
BAZ2A	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
BCAR1	Affinity Capture-Western, Reconstituted Complex, Two-hybrid, coimmunoprecipitation, peptide array, pull down, two hybrid array, two hybrid prey pooling approach	association, physical, physical association	10739664, 17474147, 9188452, 9360983, (Europe PMC)	0.49, 0.62	BioGRID, IntAct, MINT
BCL3	Reconstituted Complex, pull down	physical, physical association	16099425, 9576921, (Europe PMC)	0.40	BioGRID, IntAct, MINT
BET1	proximity-dependent biotin identification	association	29568061, (Europe PMC)	0.35	IntAct
BMP8B	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
BRCA2	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
BRPF3	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
BTK	Reconstituted Complex	physical	8058772, (Europe PMC)	NA	BioGRID
C6	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
C7orf25	Two-hybrid, two hybrid	physical, physical association	21900206, (Europe PMC)	0.37	BioGRID, IntAct, MINT
C8orf33	Two-hybrid, two hybrid	physical, physical association	21900206, (Europe PMC)	0.37	BioGRID, IntAct, MINT
CACNA1F	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
CAST	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
CAV1	Co-fractionation	physical	9252391, (Europe PMC)	NA	BioGRID
CBL	Affinity Capture-Western, Biochemical Activity, Reconstituted Complex, Two-hybrid, anti bait coimmunoprecipitation, coimmunoprecipitation, competition binding, experimental interaction detection, pull down, two hybrid array	phosphorylation reaction, physical, physical association	10629042, 10829062, 12231245, 12244174, 12941616, 15190072, 15208330, 15556646, 16503409, 17094785, 25814554, 7642581, 7782294, 8621719, 8626543, 8662998, 8900205, 8995358, 9311917, 9535867, (Europe PMC)	0.37, 0.80	BioGRID, IntAct, MINT
CBLB	Two-hybrid, two hybrid array, two hybrid prey pooling approach	physical, physical association	25814554, (Europe PMC)	0.62	BioGRID, IntAct
CBLC	Affinity Capture-Western, Reconstituted Complex	physical	10571044, (Europe PMC)	NA	BioGRID
CCDC8	Affinity Capture-MS	physical	24711643, (Europe PMC)	NA	BioGRID
CCKBR	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
CCNL2	Affinity Capture-MS	physical	26186194, 28514442, (Europe PMC)	NA	BioGRID
CCR10	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
CD2	Reconstituted Complex, anti bait coimmunoprecipitation, experimental interaction detection, pull down	phosphorylation reaction, physical, physical association	9677430, (Europe PMC)	0.57	BioGRID, IntAct, MINT
CD226	Affinity Capture-Western	physical	10591186, (Europe PMC)	NA	BioGRID
CD244	Affinity Capture-Western, anti bait coimmunoprecipitation	association, physical	15169881, 23346089, (Europe PMC)	0.35	BioGRID, IntAct
CD2AP	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
CD36	Affinity Capture-Western	physical	1715582, 7521304, (Europe PMC)	NA	BioGRID
CD3G	Affinity Capture-Western	physical	16888650, (Europe PMC)	NA	BioGRID
CD44	Affinity Capture-Western, Co-fractionation	physical	9573028, (Europe PMC)	NA	BioGRID
CD5	Affinity Capture-Western	physical	21757751, (Europe PMC)	NA	BioGRID
CDC27	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
CDC37	Affinity Capture-MS, luminescence based mammalian interactome mapping	physical, physical association	25036637, 28514442, (Europe PMC)	0.40	BioGRID, IntAct
CDCP1	anti bait coimmunoprecipitation	association	21233420, (Europe PMC)	0.35	IntAct
CDH1	Affinity Capture-Western, Reconstituted Complex	physical	12640114, (Europe PMC)	NA	BioGRID
CDK1	Affinity Capture-Western	physical	8910336, (Europe PMC)	NA	BioGRID
CDKL5	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
CELSR3	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
CENPA	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
CENPV	pull down	physical association	19930468, (Europe PMC)	0.40	IntAct, MINT
CHAF1A	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
CHRNA7	Affinity Capture-Western	physical	11278378, (Europe PMC)	NA	BioGRID
CKAP5	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
CLTC	Biochemical Activity	physical	17785434, (Europe PMC)	NA	BioGRID
CMA1	Protein-peptide	physical	22653218, (Europe PMC)	NA	BioGRID
CNTFR	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
CNTNAP1	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
CSF1R	Affinity Capture-Western, Reconstituted Complex, pull down	association, physical	7681396, (Europe PMC)	0.35	BioGRID, IntAct, MINT
CSK	Affinity Capture-Western, pull down	association, physical	7524477, 8262983, (Europe PMC)	0.35	BioGRID, IntAct, MINT
CSMD2	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
CTLA4	Affinity Capture-Western, Co-localization, proximity ligation assay	physical, physical association	25241761, 9712716, (Europe PMC)	0.40	BioGRID, IntAct
CTNNB1	Biochemical Activity, Co-localization, proximity ligation assay	physical, physical association	12640114, 25241761, (Europe PMC)	0.40	BioGRID, IntAct
CTNND1	Affinity Capture-Western, Biochemical Activity	physical	12640114, 12835311, (Europe PMC)	NA	BioGRID
CYP4F2	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
DAB2	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
DAG1	Affinity Capture-Western, Reconstituted Complex, peptide array	physical, physical association	11724572, 17474147, (Europe PMC)	0.40	BioGRID, IntAct
DCBLD2	pull down	physical association	23770091, (Europe PMC)	0.40	IntAct, MINT
DDX41	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
DKKL1	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
DLG4	Affinity Capture-Western	physical	12419528, 9892651, (Europe PMC)	NA	BioGRID
DLGAP1	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
DLGAP2	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
DLGAP3	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
DLGAP4	peptide array, two hybrid array, two hybrid prey pooling approach	physical association	17474147, (Europe PMC)	0.40, 0.49	IntAct
DLX4	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
DNASE1L2	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
DNM3	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
DOCK1	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
DOCK3	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
DUSP15	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
EFS	Biochemical Activity, Reconstituted Complex, Two-hybrid, two hybrid array, two hybrid prey pooling approach, validated two hybrid	physical, physical association	12471123, 25416956, (Europe PMC)	0.49, 0.56	BioGRID, IntAct
ENO1	Biochemical Activity	physical	11078745, 14530346, (Europe PMC)	NA	BioGRID
EPB41L3	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
EPHA3	Reconstituted Complex	physical	9632142, (Europe PMC)	NA	BioGRID
EPHA4	Affinity Capture-Western	physical	12084815, (Europe PMC)	NA	BioGRID
EPHA8	Affinity Capture-Western, Reconstituted Complex	physical	10498895, (Europe PMC)	NA	BioGRID
EPHB3	Reconstituted Complex	physical	9674711, (Europe PMC)	NA	BioGRID
EPS15	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
ERBB2	nuclear magnetic resonance, surface plasmon resonance	direct interaction	24815698, (Europe PMC)	0.56	IntAct, MINT
EXTL3	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
F2RL2	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
FAM110A	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
FANCA	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
FAS	Affinity Capture-Western, cosedimentation through density gradient	colocalization, physical	17159908, 8626376, (Europe PMC)	0.35	BioGRID, IntAct, MINT
FASLG	Co-localization, Protein-peptide, Reconstituted Complex, phage display, proximity ligation assay	direct interaction, physical, physical association	11741599, 17164290, 19807924, 25241761, 7589480, (Europe PMC)	0.61	BioGRID, IntAct
FCGR2B	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
FCGR2C	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
FGFR2	Affinity Capture-Western	physical	15190072, (Europe PMC)	NA	BioGRID
FLNA	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
FLNC	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
FLT1	anti bait coimmunoprecipitation	physical association	12509223, (Europe PMC)	0.40	IntAct
FN1	enzyme linked immunosorbent assay, surface plasmon resonance	direct interaction	17130124, (Europe PMC)	0.56	IntAct, MINT
FOXF2	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
FRK	Affinity Capture-Western	physical	10229084, (Europe PMC)	NA	BioGRID
FYB1	Affinity Capture-Western, Reconstituted Complex, Two-hybrid	physical	10229084, 25814554, 7504057, 9207119, 9748251, (Europe PMC)	NA	BioGRID
FYB1	coimmunoprecipitation, peptide array, pull down, two hybrid array, validated two hybrid	association, direct interaction, physical association	10409671, 17474147, 25814554, 9207119, (Europe PMC)	0.49, 0.82	IntAct, MINT
FYN	Biochemical Activity, Co-crystal Structure, protein kinase assay	phosphorylation reaction, physical	11157475, 14993658, 27001024, 7687536, (Europe PMC)	0.62	BioGRID, IntAct, MINT
G3BP1	anti tag coimmunoprecipitation	physical association	15743820, (Europe PMC)	0.40	IntAct, MINT
GAB3	Reconstituted Complex	physical	11739737, (Europe PMC)	NA	BioGRID
GABBR1	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
GAD1	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
GCFC2	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
GJB7	Affinity Capture-MS	physical	28514442, (Europe PMC)	NA	BioGRID
GNB1	Affinity Capture-Western	physical	19917775, (Europe PMC)	NA	BioGRID
GNG2	Affinity Capture-Western	physical	19917775, (Europe PMC)	NA	BioGRID
GNS	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
GP6	Reconstituted Complex	physical	11943772, (Europe PMC)	NA	BioGRID
GP6	anti bait coimmunoprecipitation, phage display, pull down	association, physical association	1715582, 19940238, (Europe PMC)	0.52, 0.56	IntAct
GPR45	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
GPR63	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
GRASP	Biochemical Activity	physical	15173175, (Europe PMC)	NA	BioGRID
GRB10	Biochemical Activity	physical	10871840, (Europe PMC)	NA	BioGRID
GRIN1	Biochemical Activity	physical	9670010, (Europe PMC)	NA	BioGRID
GRIN2A	Affinity Capture-Western, Reconstituted Complex	physical	10458595, 12419528, 12932824, 9892651, (Europe PMC)	NA	BioGRID
GRIN2B	Biochemical Activity, Reconstituted Complex	physical	10458595, 9670010, (Europe PMC)	NA	BioGRID
GRM1	Affinity Capture-Western	physical	15173175, (Europe PMC)	NA	BioGRID
GSTZ1	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
GTF3A	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
GUCY2D	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
HAVCR2	anti bait coimmunoprecipitation, pull down	association	26492563, (Europe PMC)	0.46	IntAct
HCN2	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
HCN4	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
HDAC6	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
HEXA	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
HNRNPR	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
HOXB5	Affinity Capture-MS	physical	26186194, 28514442, (Europe PMC)	NA	BioGRID
HOXC8	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
HSP90AA1	Affinity Capture-Luminescence, Affinity Capture-MS, Affinity Capture-Western	physical	16888650, 22939624, 28514442, (Europe PMC)	NA	BioGRID
HSP90AA4P	Affinity Capture-MS	physical	28514442, (Europe PMC)	NA	BioGRID
HSP90AB1	Affinity Capture-MS, anti tag coimmunoprecipitation, luminescence based mammalian interactome mapping	physical, physical association	22939624, 28514442, (Europe PMC)	0.52	BioGRID, IntAct
HSP90AB3P	Affinity Capture-MS	physical	28514442, (Europe PMC)	NA	BioGRID
HSP90AB4P	Affinity Capture-MS	physical	28514442, (Europe PMC)	NA	BioGRID
HTR6	anti bait coimmunoprecipitation, anti tag coimmunoprecipitation, pull down, two hybrid	direct interaction, physical association	17189269, (Europe PMC)	0.63	IntAct
IFITM3	Affinity Capture-Western	physical	23055554, (Europe PMC)	NA	BioGRID
IKBKG	Affinity Capture-Western	physical	23131831, (Europe PMC)	NA	BioGRID
IL1B	Reconstituted Complex	physical	9230816, (Europe PMC)	NA	BioGRID
IL3RA	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
IL7R	Affinity Capture-Western	physical	7515933, (Europe PMC)	NA	BioGRID
ISG20L2	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
ITCH	Affinity Capture-Western, Reconstituted Complex	physical	16387660, (Europe PMC)	NA	BioGRID
ITK	Reconstituted Complex	physical	10636929, 8810341, (Europe PMC)	NA	BioGRID
JAK2	Affinity Capture-Western, Reconstituted Complex	physical	10551884, (Europe PMC)	NA	BioGRID
KCNA2	Affinity Capture-Western	physical	11149959, (Europe PMC)	NA	BioGRID
KCNA4	Affinity Capture-Western	physical	11149959, (Europe PMC)	NA	BioGRID
KCNA5	Affinity Capture-Western	physical	11149959, (Europe PMC)	NA	BioGRID
KDM1A	Two-hybrid, two hybrid	physical, physical association	23455924, (Europe PMC)	0.37	BioGRID, IntAct, MINT
KDR	anti tag coimmunoprecipitation	physical association	16966330, (Europe PMC)	0.40	IntAct, MINT
KHDRBS1	Affinity Capture-Western, Biochemical Activity, Protein-peptide, Reconstituted Complex	physical	11960376, 15190072, 16888650, 22745667, 9045636, (Europe PMC)	NA	BioGRID
KHDRBS1	coimmunoprecipitation, pull down, two hybrid	direct interaction, physical association	22641034, 7516469, 9045636, (Europe PMC)	0.74	IntAct, MINT
KMT2B	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
LAT	Biochemical Activity, protein kinase assay	phosphorylation reaction, physical	16938345, (Europe PMC)	0.44	BioGRID, IntAct
LCP2	pull down	physical association	15929943, (Europe PMC)	0.40	IntAct, MINT
LIMK1	Affinity Capture-MS, anti tag coimmunoprecipitation	association, physical	26496610, (Europe PMC)	0.35	BioGRID, IntAct
LRBA	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
LRRIQ1	Affinity Capture-MS	physical	28514442, (Europe PMC)	NA	BioGRID
LTBP2	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
MAG	Reconstituted Complex	physical	7525550, (Europe PMC)	NA	BioGRID
MAP2	Affinity Capture-Western, coimmunoprecipitation, experimental interaction detection	phosphorylation reaction, physical	11546790, 15536091, (Europe PMC)	0.31, 0.44	BioGRID, IntAct, MINT
MAP4K1	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
MAP4K5	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
MAPRE1	Affinity Capture-MS, anti tag coimmunoprecipitation	association, physical	26496610, (Europe PMC)	0.35	BioGRID, IntAct
MAPT	Affinity Capture-Western, Biochemical Activity, Reconstituted Complex, pull down, surface plasmon resonance	direct interaction, physical, physical association	11826099, 16115884, 21692989, (Europe PMC)	0.40, 0.44	BioGRID, IntAct, MINT
MCAM	Affinity Capture-Western	physical	9756930, (Europe PMC)	NA	BioGRID
MED14	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
MED21	Affinity Capture-MS	physical	28514442, (Europe PMC)	NA	BioGRID
MED28	Affinity Capture-Western, anti bait coimmunoprecipitation, peptide array, protein kinase assay, pull down, two hybrid	association, phosphorylation reaction, physical, physical association	16899217, 16964398, (Europe PMC)	0.74	BioGRID, IntAct, MINT
MEPE	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
MKI67	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
MOS	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
MS4A1	Affinity Capture-Western	physical	7545683, (Europe PMC)	NA	BioGRID
MTUS2	Affinity Capture-MS	physical	28514442, (Europe PMC)	NA	BioGRID
MYH9	Affinity Capture-MS, anti tag coimmunoprecipitation	association, physical	26496610, (Europe PMC)	0.35	BioGRID, IntAct
MYO18A	Affinity Capture-MS, anti tag coimmunoprecipitation	association, physical	26496610, (Europe PMC)	0.35	BioGRID, IntAct
NBEA	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
NCK1	anti bait coimmunoprecipitation	physical association	16966330, (Europe PMC)	0.40	IntAct, MINT
NCKAP5	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
NCKIPSD	mammalian protein protein interaction trap, peptide array	physical association	17474147, 25416956, (Europe PMC)	0.57	IntAct
NDFIP2	Affinity Capture-Western	physical	20534535, (Europe PMC)	NA	BioGRID
NEDD4	Biochemical Activity, Reconstituted Complex	physical	19953087, (Europe PMC)	NA	BioGRID
NEDD9	Affinity Capture-Western	physical	9360983, (Europe PMC)	NA	BioGRID
NEK8	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
NELFB	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
NFASC	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
NFS1	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
NKX2-1	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
NMT1	Biochemical Activity	physical	11594778, (Europe PMC)	NA	BioGRID
NOS1AP	Two-hybrid, two hybrid array	physical, physical association	25814554, (Europe PMC)	0.37	BioGRID, IntAct
NPHS1	Affinity Capture-Western, Biochemical Activity, Reconstituted Complex	physical	12668668, 12846735, (Europe PMC)	NA	BioGRID
NPVF	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
NR3C1	Affinity Capture-Western	physical	16888650, (Europe PMC)	NA	BioGRID
NR5A1	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
NTRK2	Affinity Capture-Western, Reconstituted Complex	physical	9648856, (Europe PMC)	NA	BioGRID
OCRL	anti tag coimmunoprecipitation	association	25107275, (Europe PMC)	0.35	IntAct, MINT
ORC1	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
PAG1	Affinity Capture-Western, Reconstituted Complex, anti bait coimmunoprecipitation, coimmunoprecipitation, peptide array	association, physical, physical association	10790433, 18056706, 23866081, (Europe PMC)	0.62	BioGRID, IntAct, MINT
PAK2	filter binding	physical association	16374509, (Europe PMC)	0.40	IntAct, MINT
PAX3	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
PAX7	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
PCDHGC3	Affinity Capture-MS	physical	28514442, (Europe PMC)	NA	BioGRID
PDCD6IP	isothermal titration calorimetry, nuclear magnetic resonance, pull down, two hybrid, x ray scattering	direct interaction, physical association	22641034, (Europe PMC)	0.67	IntAct, MINT
PDE4D	Far Western	physical	10571082, (Europe PMC)	NA	BioGRID
PDGFRB	coimmunoprecipitation, pull down	association	1661130, 7685273, 7687537, (Europe PMC)	0.64	IntAct, MINT
PDIA2	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
PECAM1	Affinity Capture-Western	physical	10858437, (Europe PMC)	NA	BioGRID
PIK3R1	Reconstituted Complex, mammalian protein protein interaction trap	physical, physical association	25416956, 8294442, (Europe PMC)	0.37	BioGRID, IntAct
PIK3R2	Reconstituted Complex	physical	1334406, (Europe PMC)	NA	BioGRID
PIK3R3	Two-hybrid, two hybrid array	physical, physical association	25814554, (Europe PMC)	0.37	BioGRID, IntAct
PKD1	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
PLCG2	Reconstituted Complex	physical	8395016, (Europe PMC)	NA	BioGRID
PMS2	Affinity Capture-MS	physical	26496610, (Europe PMC)	NA	BioGRID
PMS2	anti tag coimmunoprecipitation	association	26496610, (Europe PMC)	0.35	IntAct
POLD1	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
PPP1R12A	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
PPP1R3D	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
PRICKLE3	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
PRKCD	Co-localization, anti bait coimmunoprecipitation, enzyme linked immunosorbent assay, protein kinase assay, proximity ligation assay	phosphorylation reaction, physical, physical association	10383400, 12721299, 25241761, (Europe PMC)	0.75	BioGRID, IntAct
PRKCI	Affinity Capture-MS	physical	28514442, (Europe PMC)	NA	BioGRID
PRKCQ	Affinity Capture-Western, Biochemical Activity, Reconstituted Complex, Two-hybrid, anti bait coimmunoprecipitation, enzyme linked immunosorbent assay, protein kinase assay, pull down, two hybrid	phosphorylation reaction, physical, physical association	10383400, (Europe PMC)	0.66	BioGRID, IntAct
PRMT6	Two-hybrid, two hybrid	physical, physical association	23455924, (Europe PMC)	0.37	BioGRID, IntAct, MINT
PRUNE2	Affinity Capture-MS	physical	28514442, (Europe PMC)	NA	BioGRID
PRX	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
PTK2	Affinity Capture-Western, Co-crystal Structure	physical	11278857, 12558988, (Europe PMC)	NA	BioGRID
PTK2B	Affinity Capture-Western, Biochemical Activity, Reconstituted Complex, coimmunoprecipitation, pull down	association, physical	10229084, 10867021, 9091579, 9104812, (Europe PMC)	0.46	BioGRID, IntAct, MINT
PTPN11	Affinity Capture-Western	physical	10212213, 11157475, (Europe PMC)	NA	BioGRID
PTPN4	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
PTPN5	Affinity Capture-Western	physical	11983687, (Europe PMC)	NA	BioGRID
PTPRA	Affinity Capture-Western	physical	9535845, (Europe PMC)	NA	BioGRID
PTPRD	Affinity Capture-MS	physical	28514442, (Europe PMC)	NA	BioGRID
PTPRE	anti tag coimmunoprecipitation	physical association	14980517, (Europe PMC)	0.40	IntAct, MINT
PXN	Affinity Capture-Western	physical	10804218, (Europe PMC)	NA	BioGRID
RACK1	Affinity Capture-Western, Reconstituted Complex	physical	11943848, 12524444, (Europe PMC)	NA	BioGRID
RAF1	Affinity Capture-Western, Reconstituted Complex	physical	7517401, (Europe PMC)	NA	BioGRID
RAPGEF1	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
RIMS1	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
RIMS2	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
RIN3	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
RP1L1	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
RPL10	Reconstituted Complex	physical	12138090, (Europe PMC)	NA	BioGRID
RPP38	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
RPS6KA1	Affinity Capture-MS	physical	28514442, (Europe PMC)	NA	BioGRID
RPS6KA2	Affinity Capture-MS	physical	28514442, (Europe PMC)	NA	BioGRID
RPS6KA3	Affinity Capture-MS	physical	28514442, (Europe PMC)	NA	BioGRID
RRAS	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
RTN4	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
SCARF2	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
SDC3	Reconstituted Complex	physical	9553134, (Europe PMC)	NA	BioGRID
SELENON {ECO:0000303\|PubMed:27645994,	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
SEMA7A	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
SF3B4	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
SH2D1A	Affinity Capture-Western, Reconstituted Complex, anti tag coimmunoprecipitation, mammalian protein protein interaction trap	physical, physical association	12458214, 12545174, 16983070, 25416956, (Europe PMC)	0.37, 0.40	BioGRID, IntAct
SH3BP2	Two-hybrid	physical	9846481, (Europe PMC)	NA	BioGRID
SH3KBP1	Affinity Capture-Western	physical	15707590, (Europe PMC)	NA	BioGRID
SHANK3	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
SHC1	pull down	direct interaction	7516469, (Europe PMC)	0.44	IntAct, MINT
SHROOM2	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
SIT1	Affinity Capture-Western	physical	10209036, (Europe PMC)	NA	BioGRID
SKAP1	Affinity Capture-Western, Reconstituted Complex, coimmunoprecipitation	association, physical	10229084, 12171928, 9195899, 9748251, (Europe PMC)	0.35	BioGRID, IntAct, MINT
SKAP2	Affinity Capture-Western, Biochemical Activity	physical	12893833, 9837776, (Europe PMC)	NA	BioGRID
SLAMF1	Reconstituted Complex	physical	12545174, (Europe PMC)	NA	BioGRID
SLC24A1	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
SLC25A11	Affinity Capture-MS	physical	26186194, (Europe PMC)	NA	BioGRID
SLC25A41	Affinity Capture-MS	physical	26186194, 28514442, (Europe PMC)	NA	BioGRID
SLC4A8	Affinity Capture-MS	physical	28514442, (Europe PMC)	NA	BioGRID
SNCA	Biochemical Activity	physical	11078745, 11162638, 15033366, (Europe PMC)	NA	BioGRID
SNX12	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
SNX17	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
SNX3	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
SNX8	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
SOCS1	Reconstituted Complex	physical	10022833, (Europe PMC)	NA	BioGRID
SOS1	Reconstituted Complex, peptide array	physical, physical association	17474147, 9856337, (Europe PMC)	0.40	BioGRID, IntAct
SOS2	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
SP1	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
SPHK1	anti bait coimmunoprecipitation	direct interaction	16316995, (Europe PMC)	0.44	IntAct
SPHK2	anti bait coimmunoprecipitation	direct interaction	16316995, (Europe PMC)	0.44	IntAct
SRC	Affinity Capture-MS, Affinity Capture-Western, Protein-peptide, anti bait coimmunoprecipitation	physical, physical association	16966330, 19711372, 28514442, 9169421, (Europe PMC)	0.40	BioGRID, IntAct, MINT
STAT3	Reconstituted Complex	physical	12244095, (Europe PMC)	NA	BioGRID
SUV39H1	Two-hybrid, two hybrid	physical, physical association	23455924, (Europe PMC)	0.37	BioGRID, IntAct, MINT
SUV39H2	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
SYK	Affinity Capture-Western, Reconstituted Complex	physical	9535867, (Europe PMC)	NA	BioGRID
SYNJ2	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
TCAP	Two-hybrid, two hybrid array	physical, physical association	21988832, (Europe PMC)	0.37	BioGRID, IntAct
TDRD1	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
TGOLN2	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
THY1	Affinity Capture-Western	physical	1351058, (Europe PMC)	NA	BioGRID
TMEM132A	Affinity Capture-MS, anti tag coimmunoprecipitation	association, physical	26496610, (Europe PMC)	0.35	BioGRID, IntAct
TMEM185A	Affinity Capture-MS	physical	26186194, 28514442, (Europe PMC)	NA	BioGRID
TMPO	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
TNF	Reconstituted Complex	physical	9230816, (Europe PMC)	NA	BioGRID
TNFRSF10B	Affinity Capture-MS	physical	28514442, (Europe PMC)	NA	BioGRID
TNFRSF1A	Co-fractionation	physical	12753742, (Europe PMC)	NA	BioGRID
TNK2	Affinity Capture-Western, Reconstituted Complex	physical	11087735, (Europe PMC)	NA	BioGRID
TNNT1	Two-hybrid, two hybrid	physical, physical association	21900206, (Europe PMC)	0.37	BioGRID, IntAct, MINT
TOM1L1	Affinity Capture-Western, Reconstituted Complex	physical	11711534, 20182632, (Europe PMC)	NA	BioGRID
TRAF6	Reconstituted Complex	physical	22447928, (Europe PMC)	NA	BioGRID
TRAIP	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
TRAT1	Reconstituted Complex	physical	10790433, (Europe PMC)	NA	BioGRID
TRIM39	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
TRPC6	Affinity Capture-Western, Biochemical Activity, Reconstituted Complex	physical	14761972, (Europe PMC)	NA	BioGRID
TRPV4	Affinity Capture-Western	physical	12538589, (Europe PMC)	NA	BioGRID
TSKS	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
TSNAX	Affinity Capture-MS, anti tag coimmunoprecipitation	association, physical	26496610, (Europe PMC)	0.35	BioGRID, IntAct
TUBA3C	Affinity Capture-Western, Reconstituted Complex	physical	11826099, (Europe PMC)	NA	BioGRID
TULP1	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
TULP4	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
TYK2	Affinity Capture-Western, Reconstituted Complex	physical	9196040, (Europe PMC)	NA	BioGRID
UHRF2	Far Western, antibody array	physical, physical association	21952639, (Europe PMC)	0.40	BioGRID, IntAct
UNC119	Affinity Capture-Western, Reconstituted Complex	physical	14757743, (Europe PMC)	NA	BioGRID
VAV1	Affinity Capture-Western, Two-hybrid	physical	11262396, 9822663, (Europe PMC)	NA	BioGRID
VAV2	Two-hybrid	physical	11262396, (Europe PMC)	NA	BioGRID
VPS13A	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
WAS	Affinity Capture-Western, Biochemical Activity, Reconstituted Complex, anti bait coimmunoprecipitation, experimental interaction detection, pull down	direct interaction, phosphorylation reaction, physical, physical association	10532312, 12431372, 14707117, 7565724, 8805332, (Europe PMC)	0.70	BioGRID, IntAct, MINT
WBP11	Two-hybrid, two hybrid array, two hybrid prey pooling approach, validated two hybrid	physical, physical association	25416956, (Europe PMC)	0.56	BioGRID, IntAct
WIPF1	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
WNK2	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
XRCC1	peptide array	physical association	17474147, (Europe PMC)	0.40	IntAct
YES1	Affinity Capture-MS, Affinity Capture-Western	physical	12640114, 28514442, (Europe PMC)	NA	BioGRID
ZAP70	Affinity Capture-Western, Phenotypic Enhancement	genetic, physical	7760813, (Europe PMC)	NA	BioGRID
ZNFX1	Affinity Capture-MS, anti tag coimmunoprecipitation	association, physical	26496610, (Europe PMC)	0.35	BioGRID, IntAct

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