DEPOD - human DEPhOsphorylation Database

Basic Information
Phosphatases
Pathway
Interacting Proteins
Phosphorylating Kinases

Gene Name	WASL (QuickGO)	Interactive visualization of WASL structures (A quick tutorial to explore the interctive visulaization) Representative structure: 2VCP
Synonyms	WASL
Protein Name	WASL
Alternative Name(s)	Neural Wiskott-Aldrich syndrome protein;N-WASP;
Protein Family	noSimilarity_annotations
EntrezGene ID	8976 (Comparitive Toxicogenomics)
UniProt AC (Human)	O00401 (protein sequence)
Enzyme Class	N/A
Molecular Weight	54827 Dalton
Protein Length	505 amino acids (AA)
Genome Browsers	NCBI \| ENSG00000106299 (Ensembl) \| UCSC
Crosslinking annotations	Query our ID-mapping table
Orthologues	Quest For Orthologues (QFO) \| GeneTree \| eggNOG - KOG3671 \| eggNOG - ENOG4111J0D
Phosphorylation Network	Visualize

Domain organization, Expression, Diseases

(show / hide)

Localization, Function, Catalytic activity and Sequence

(show / hide)

Motif information from Eukaryotic Linear Motif atlas (ELM)

(show / hide)

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

(show / hide)

KEGG Pathway
Reactome Pathway

Pathway ID	Pathway Name	Pathway Description (KEGG)
hsa04062	Chemokine signaling pathway	Inflammatory immune response requires the recruitment of leukocytes to the site of inflammation upon foreign insult. Chemokines are small chemoattractant peptides that provide directional cues for the cell trafficking and thus are vital for protective host response. In addition, chemokines regulate plethora of biological processes of hematopoietic cells to lead cellular activation, differentiation and survival.The chemokine signal is transduced by chemokine receptors (G-protein coupled receptors) expressed on the immune cells. After receptor activation, the alpha- and beta-gamma-subunits of G protein dissociate to activate diverse downstream pathways resulting in cellular polarization and actin reorganization. Various members of small GTPases are involved in this process. Induction of nitric oxide and production of reactive oxygen species are as well regulated by chemokine signal via calcium mobilization and diacylglycerol production.
hsa04144	Endocytosis	Endocytosis is a mechanism for cells to remove ligands, nutrients, and plasma membrane (PM) proteins, and lipids from the cell surface, bringing them into the cell interior. Transmembrane proteins entering through clathrin-dependent endocytosis (CDE) have sequences in their cytoplasmic domains that bind to the APs (adaptor-related protein complexes) and enable their rapid removal from the PM. In addition to APs and clathrin, there are numerous accessory proteins including dynamin. Depending on the various proteins that enter the endosome membrane, these cargoes are sorted to distinct destinations. Some cargoes, such as nutrient receptors, are recycled back to the PM. Ubiquitylated membrane proteins, such as activated growth-factor receptors, are sorted into intraluminal vesicles and eventually end up in the lysosome lumen via multivesicular endosomes (MVEs). There are distinct mechanisms of clathrin-independent endocytosis (CIE) depending upon the cargo and the cell type.
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.
hsa04530	Tight junction	Tight junctions (TJs) are essential for establishing a selectively permeable barrier to diffusion through the paracellular space between neighboring cells. TJs are composed of at least three types of transmembrane protein -occludin, claudin and junctional adhesion molecules (JAMs)- and a cytoplasmic 'plaque' consisting of many different proteins that form large complexes. These are proposed to be involved in junction assembly, barrier regulation, cell polarity, gene transcription, and other pathways.
hsa04666	Fc gamma R-mediated phagocytosis	Phagocytosis plays an essential role in host-defense mechanisms through the uptake and destruction of infectious pathogens. Specialized cell types including macrophages, neutrophils, and monocytes take part in this process in higher organisms. After opsonization with antibodies (IgG), foreign extracellular materials are recognized by Fc gamma receptors. Cross-linking of Fc gamma receptors initiates a variety of signals mediated by tyrosine phosphorylation of multiple proteins, which lead through the actin cytoskeleton rearrangements and membrane remodeling to the formation of phagosomes. Nascent phagosomes undergo a process of maturation that involves fusion with lysosomes. The acquisition of lysosomal proteases and release of reactive oxygen species are crucial for digestion of engulfed materials in phagosomes.
hsa04810	Regulation of actin cytoskeleton
hsa05100	Bacterial invasion of epithelial cells	Many pathogenic bacteria can invade phagocytic and non-phagocytic cells and colonize them intracellularly, then become disseminated to other cells. Invasive bacteria induce their own uptake by non-phagocytic host cells (e.g. epithelial cells) using two mechanisms referred to as zipper model and trigger model. Listeria, Staphylococcus, Streptococcus, and Yersinia are examples of bacteria that enter using the zipper model. These bacteria express proteins on their surfaces that interact with cellular receptors, initiating signalling cascades that result in close apposition of the cellular membrane around the entering bacteria. Shigella and Salmonella are the examples of bacteria entering cells using the trigger model. These bacteria use type III secretion systems to inject protein effectors that interact with the actin cytoskeleton.
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.
hsa05131	Shigellosis	Shigellosis, or bacillary dysentery, is an intestinal infection caused by Shigella, a genus of enterobacteria. Shigella are potential food-borne pathogens that are capable of colonizing the intestinal epithelium by exploiting epithelial-cell functions and circumventing the host innate immune response. During basolateral entry into the host-cell cytoplasm, Shigella deliver a subset of effectors into the host cells through the type III secretion system. The effectors induce membrane ruffling through the stimulation of the Rac1-WAVE-Arp2/3 pathway, enabling bacterial entry into the epithelial cells. During multiplication within the cells, Shigella secrete another subset of effectors. VirG induces actin polymerization at one pole of the bacteria, allowing the bacteria to spread intracellularly and to infect adjacent cells. OspF, OspG and IpaH(9.8) downregulate the production of proinflammatory cytokines such as IL-8, helping bacteria circumvent the innate immune response.
hsa05132	Salmonella infection	Salmonella infection usually presents as a self-limiting gastroenteritis or the more severe typhoid fever and bacteremia. The common disease-causing Salmonella species in human is a single species, Salmonella enterica, which has numerous serovars.Following intestinal colonization Salmonella inject effector proteins into the host cells using a type III secretion system (T3SS), T3SS1. Then a small group of effector proteins induce rearrangement of the actin cytoskeleton resulting in membrane ruffles and rapid internalization of the bacteria.The T3SS2 is responsible for translocating effector proteins that direct Salmonella-containing vacuole (SCV) maturation. The majority of the bacteria are known to survive and replicate in SCV.
hsa05231	Choline metabolism in cancer	Abnormal choline metabolism is emerging as a metabolic hallmark that is associated with oncogenesis and tumour progression. Following transformation, oncogenic signalling via pathways such as the RAS and PI3K-AKT pathways, and transcription factors associated with oncogenesis such as hypoxia-inducible factor 1 (HIF1) mediate overexpression and activation of choline cycle enzymes, which causes increased levels of choline-containing precursors and breakdown products of membrane phospholipids. These products of choline phospholipid metabolism, such as phosphocholine (PCho), diacylglycerol (DAG) and phosphatidic acid, may function as second messengers that are essential for the mitogenic activity of growth factors, particularly in the activation of the ras-raf-1-MAPK cascade and protein kinase C pathway.

Pathway ID	Pathway Name	Pathway Description (KEGG)
R-HSA-2029482	Regulation of actin dynamics for phagocytic cup formation.	The actin cytoskeleton is fundamental for phagocytosis and members of the Rho family GTPases RAC and CDC42 are involved in actin cytoskeletal regulation leading to pseudopod extension. Active RAC and CDC42 exert their action through the members of WASP family proteins (WASP/N-WASP/WAVE) and ARP2/3 complex. Actin filaments move from the bottom toward the top of the phagocytic cup during pseudopod extension
R-HSA-203641	NOSTRIN mediated eNOS trafficking.	eNOS traffic inducer (NOSTRIN) is a novel 506-amino acid eNOS-interacting protein. Along with a decrease in eNOS activity, NOSTRIN causes translocation of eNOS from the plasma membrane to intracellular vesicular structures. NOSTRIN functions as an adaptor protein through homotrimerization and recruitment of eNOS, dynamin-2, and N-WASP to its SH3 domain. Studies indicated that NOSTRIN may facilitate vesicle fission and endocytosis of eNOS by coordinating the function of dynamin and N-WASP, which in turn, recruits the Arp2/3 complex, initiating actin filament polymerization. Overall, this process is thought to occur via caveolar endocytosis
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-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-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-5663213	RHO GTPases Activate WASPs and WAVEs.	WASP and WAVE proteins belong to the Wiskott-Aldrich Syndrome protein family, with recessive mutations in the founding member WASP being responsible for the X-linked recessive immunodeficieny known as the Wiskott-Aldrich Syndrome. WASP proteins include WASP and WASL (N-WASP). WAVE proteins include WASF1 (WAVE1), WASF2 (WAVE2) and WASF3 (WAVE3). WASPs and WAVEs contain a VCA domain (consisting of WH2 and CA subdomains) at the C-terminus, responsible for binding to G-actin (WH2 subdomain) and the actin-associated ARP2/3 complex (CA subdomain). WASPs contain a WH1 (WASP homology 1) domain at the N-terminus, responsible for binding to WIPs (WASP-interacting proteins). A RHO GTPase binding domain (GBD) is located in the N-terminal half of WASPs and C-terminally located in WAVEs. RHO GTPases activate WASPs by disrupting the autoinhibitory interaction between the GBD and VCA domains, which allows WASPs to bind actin and the ARP2/3 complex and act as nucleation promoting factors in actin polymerization. WAVEs have the WAVE/SCAR homology domain (WHD/SHD) at the N-terminus, which binds ABI, NCKAP1, CYFIP2 and BRK1 to form the WAVE regulatory complex (WRC). Binding of the RAC1:GTP to the GBD of WAVEs most likely induces a conformational change in the WRC that allows activating phosphorylation of WAVEs by ABL1, thus enabling them to function as nucleation promoting factors in actin polymerization through binding G-actin and the ARP2/3 complex (Reviewed by Lane et al. 2014)
R-HSA-8856828	Clathrin-mediated endocytosis.	Clathrin-mediated endocytosis (CME) is one of a number of process that control the uptake of material from the plasma membrane, and leads to the formation of clathrin-coated vesicles (Pearse et al, 1975; reviewed in Robinson, 2015; McMahon and Boucrot, 2011; Kirchhausen et al, 2014). CME contributes to signal transduction by regulating the cell surface expression and signaling of receptor tyrosine kinases (RTKs) and G-protein coupled receptors (GPCRs). Most RTKs exhibit a robust increase in internalization rate after binding specific ligands; however, some RTKs may also exhibit significant ligand-independent internalization (reviewed in Goh and Sorkin, 2013). CME controls RTK and GPCR signaling by organizing signaling both within the plasma membrane and on endosomes (reviewed in Eichel et al, 2016; Garay et al, 2015; Vieira et al, 1996; Sorkin and von Zastrow, 2014; Di Fiori and von Zastrow, 2014; Barbieri et al, 2016). CME also contributes to the uptake of material such as metabolites, hormones and other proteins from the extracellular space, and regulates membrane composition by recycling membrane components and/or targeting them for degradation. Clathrin-mediated endocytosis involves initiation of clathrin-coated pit (CCP) formation, cargo selection, coat assembly and stabilization, membrane scission and vesicle uncoating. Although for simplicity in this pathway, the steps leading to a mature CCP are represented in a linear and temporally distinct fashion, the formation of a clathrin-coated vesicle is a highly heterogeneous process and clear temporal boundaries between these processes may not exist (see for instance Taylor et al, 2011; Antonescu et al, 2011; reviewed in Kirchhausen et al, 2014). Cargo selection in particular is a critical aspect of the formation of a mature and stable CCP, and many of the proteins involved in the initiation and maturation of a CCP contribute to cargo selection and are themselves stabilized upon incorporation of cargo into the nascent vesicle (reviewed in Kirchhausen et al, 2014; McMahon and Boucrot, 2011).Although the clathrin triskelion was identified early as a major component of the coated vesicles, clathrin does not bind directly to membranes or to the endocytosed cargo. Vesicle formation instead relies on many proteins and adaptors that can bind the plasma membrane and interact with cargo molecules. Cargo selection depends on the recognition of endocytic signals in cytoplasmic tails of the cargo proteins by adaptors that interact with components of the vesicle's inner coat. The classic adaptor for clathrin-coated vesicles is the tetrameric AP-2 complex, which along with clathrin was identified early as a major component of the coat. Some cargo indeed bind directly to AP-2, but subsequent work has revealed a large family of proteins collectively known as CLASPs (clathrin- associated sorting proteins) that mediate the recruitment of diverse cargo into the emerging clathrin-coated vesicles (reviewed in Traub and Bonifacino, 2013). Many of these CLASP proteins themselves interact with AP-2 and clathrin, coordinating cargo recruitment with coat formation (Schmid et al, 2006; Edeling et al, 2006; reviewed in Traub and Bonifacino, 2013; Kirchhausen et al, 2014). Initiation of CCP formation is also influenced by lipid composition, regulated by clathrin-associated phosphatases and kinases (reviewed in Picas et al, 2016). The plasma membrane is enriched in PI(4,5)P2. Many of the proteins involved in initiating clathrin-coated pit formation bind to PI(4,5)P2 and induce membrane curvature through their BAR domains (reviewed in McMahon and Boucrot, 2011; Daumke et al, 2014). Epsin also contributes to early membrane curvature through its Epsin N-terminal homology (ENTH) domain, which promotes membrane curvature by inserting into the lipid bilayer (Ford et al, 2002). Following initiation, some CCPs progress to formation of vesicles, while others undergo disassembly at the cell surface without producing vesicles (Ehrlich et al, 2004; Loerke et al, 2009; Loerke et al, 2011; Aguet et al, 2013; Taylor et al, 2011). The assembly and stabilization of nascent CCPs is regulated by several proteins and lipids (Mettlen et al, 2009; Antonescu et al, 2011).Maturation of the emerging clathrin-coated vesicle is accompanied by further changes in the lipid composition of the membrane and increased membrane curvature, promoted by the recruitment of N-BAR domain containing proteins (reviewed in Daumke et al, 2014; Ferguson and De Camilli, 2012; Picas et al, 2016). Some N-BAR domain containing proteins also contribute to the recruitment of the large GTPase dynamin, which is responsible for scission of the mature vesicle from the plasma membrane (Koh et al, 2007; Lundmark and Carlsson, 2003; Soulet et al, 2005; David et al, 1996; Owen et al, 1998; Shupliakov et al, 1997; Taylor et al, 2011; Ferguson et al, 2009; Aguet et al, 2013; Posor et al, 2013; Chappie et al, 2010; Shnyrova et al, 2013; reviewed in Mettlen et al, 2009; Daumke et al, 2014). After vesicle scission, the clathrin coat is dissociated from the new vesicle by the ATPase HSPA8 (also known as HSC70) and its DNAJ cofactor auxilin, priming the vesicle for fusion with a subsequent endocytic compartment and releasing clathrin for reuse (reviewed in McMahon and Boucrot, 2011; Sousa and Laufer, 2015)

BioGRID
IntAct
MINT
ALL

Visualize Download

Interacting partner	Detection method	Interaction type	PubMed IDs	Interaction Score	Source
ABI2	Co-fractionation, two hybrid array, two hybrid prey pooling approach	physical, physical association	26344197, (Europe PMC)	0.49	BioGRID, IntAct
ACTBL2	Affinity Capture-MS	physical	28514442, (Europe PMC)	NA	BioGRID
ACTG1	Co-crystal Structure, Reconstituted Complex	physical	22847007, (Europe PMC)	NA	BioGRID
ACTR2	Protein-peptide, coimmunoprecipitation	physical, physical association	12732638, 15834156, (Europe PMC)	0.40	BioGRID, IntAct, MINT
ACTR3	Protein-peptide, pull down	physical, physical association	12732638, 17028176, (Europe PMC)	0.40	BioGRID, IntAct
APBB1	Reconstituted Complex	physical	16055720, (Europe PMC)	NA	BioGRID
APP	Reconstituted Complex	physical	21832049, (Europe PMC)	NA	BioGRID
ARPC1B	Affinity Capture-Western, pull down	direct interaction, physical, physical association	11943145, 15894313, (Europe PMC)	0.61	BioGRID, IntAct, MINT
ARPC3	Two-hybrid, two hybrid array, two hybrid prey pooling approach, validated two hybrid	physical, physical association	25416956, (Europe PMC)	0.70	BioGRID, IntAct
ASPA	Affinity Capture-MS	physical	28514442, (Europe PMC)	NA	BioGRID
ATG4C	Affinity Capture-MS	physical	28514442, (Europe PMC)	NA	BioGRID
BAIAP2	Affinity Capture-MS, Two-hybrid, anti tag coimmunoprecipitation, two hybrid	association, physical, physical association	21988832, 26496610, (Europe PMC)	0.55	BioGRID, IntAct
BCHE	Affinity Capture-MS	physical	28514442, (Europe PMC)	NA	BioGRID
BIN1	Reconstituted Complex	physical	25262827, (Europe PMC)	NA	BioGRID
CDC42	Reconstituted Complex, Two-hybrid, coimmunoprecipitation, phosphatase assay, protein kinase assay, two hybrid, two hybrid pooling approach	phosphorylation reaction, physical, physical association	10781580, 11331876, 15834156, 16293614, 20936779, 21311754, 9422512, (Europe PMC)	0.37, 0.75	BioGRID, IntAct, MINT
CTTN	Affinity Capture-Western, Far Western, fluorescence microscopy	colocalization, physical	11830518, 12672817, 18344974, (Europe PMC)	0.27	BioGRID, IntAct, MINT
DNMBP	Affinity Capture-MS, isothermal titration calorimetry, x-ray crystallography	direct interaction, physical	14506234, 24332715, (Europe PMC)	0.56	BioGRID, IntAct
EGFR	PCA, Two-hybrid, ubiquitin reconstruction	physical, physical association	24658140, 25402006, (Europe PMC)	0.37	BioGRID, IntAct
ELAVL1	Affinity Capture-RNA	physical	19322201, (Europe PMC)	NA	BioGRID
FCHSD2	Two-hybrid, two hybrid	physical, physical association	21988832, (Europe PMC)	0.37	BioGRID, IntAct
FNBP1	Co-fractionation, Reconstituted Complex	physical	16418535, 22939629, (Europe PMC)	NA	BioGRID
FNBP1L	Co-fractionation, Reconstituted Complex	physical	16418535, 26344197, (Europe PMC)	NA	BioGRID
GRB2	Affinity Capture-MS, Reconstituted Complex, Two-hybrid, anti tag coimmunoprecipitation, barcode fusion genetics two hybrid, peptide array, two hybrid array, two hybrid pooling approach, two hybrid prey pooling approach, validated two hybrid	association, physical, physical association	10781580, 17474147, 20936779, 21706016, 25416956, 27107012, 28514442, (Europe PMC)	0.86	BioGRID, IntAct
GSN	Co-crystal Structure	physical	16531231, (Europe PMC)	NA	BioGRID
HP	Two-hybrid, two hybrid	physical, physical association	21988832, (Europe PMC)	0.37	BioGRID, IntAct
HSP90AA1	Reconstituted Complex	physical	15791211, (Europe PMC)	NA	BioGRID
HSP90AB1	Reconstituted Complex	physical	15791211, (Europe PMC)	NA	BioGRID
IPO5	Two-hybrid, two hybrid	physical, physical association	21988832, (Europe PMC)	0.37	BioGRID, IntAct
IQGAP1	Affinity Capture-Western	physical	24639526, (Europe PMC)	NA	BioGRID
ITSN1	Reconstituted Complex, coimmunoprecipitation, imaging technique, pull down	colocalization, direct interaction, physical, physical association	11584276, 18539136, (Europe PMC)	0.70	BioGRID, IntAct, MINT
ITSN2	Two-hybrid	physical	22558309, (Europe PMC)	NA	BioGRID
LCK	Biochemical Activity, protein kinase assay	phosphorylation reaction, physical	16293614, (Europe PMC)	0.44	BioGRID, IntAct
LSM1	Co-fractionation	physical	22939629, (Europe PMC)	NA	BioGRID
NCK1	Affinity Capture-MS, Far Western, Reconstituted Complex, anti tag coimmunoprecipitation, peptide array, pull down	association, physical, physical association	11340081, 16595635, 17474147, 26496610, (Europe PMC)	0.50, 0.56	BioGRID, IntAct
NCK2	Affinity Capture-MS, Two-hybrid, two hybrid array, two hybrid prey pooling approach, validated two hybrid	physical, physical association	25416956, 26186194, 26871637, 28514442, (Europe PMC)	0.72	BioGRID, IntAct
NTRK1	Affinity Capture-MS	physical	25921289, (Europe PMC)	NA	BioGRID
PACSIN1	Reconstituted Complex	physical	11082044, (Europe PMC)	NA	BioGRID
PACSIN2	Reconstituted Complex, two hybrid array, two hybrid prey pooling approach	physical, physical association	11082044, (Europe PMC)	0.49	BioGRID, IntAct
PACSIN3	Reconstituted Complex, two hybrid array, two hybrid prey pooling approach	physical, physical association	11082044, (Europe PMC)	0.49	BioGRID, IntAct
PFN1	Affinity Capture-Western, Reconstituted Complex	physical	10867004, 9822597, (Europe PMC)	NA	BioGRID
PRPF40A	Reconstituted Complex	physical	16055720, (Europe PMC)	NA	BioGRID
PSTPIP1	Reconstituted Complex	physical	16418535, (Europe PMC)	NA	BioGRID
PTK6	Two-hybrid, two hybrid array, two hybrid prey pooling approach, validated two hybrid	physical, physical association	25416956, (Europe PMC)	0.56	BioGRID, IntAct
RHOJ	Two-hybrid, two hybrid array, two hybrid prey pooling approach, validated two hybrid	physical, physical association	25416956, (Europe PMC)	0.70	BioGRID, IntAct
RHOQ	Reconstituted Complex, Two-hybrid	physical	12456725, (Europe PMC)	NA	BioGRID
RNF8	Two-hybrid	physical	21516116, 25416956, (Europe PMC)	NA	BioGRID
RPL7AP66	Two-hybrid	physical	21988832, (Europe PMC)	NA	BioGRID
SDCBP	Two-hybrid, two hybrid array, two hybrid prey pooling approach, validated two hybrid	physical, physical association	25416956, (Europe PMC)	0.70	BioGRID, IntAct
SH3KBP1	Affinity Capture-MS	physical	19531213, (Europe PMC)	NA	BioGRID
SKA1	Affinity Capture-MS, anti tag coimmunoprecipitation	association, physical	26496610, (Europe PMC)	0.35	BioGRID, IntAct
SNX9	Reconstituted Complex, anti tag coimmunoprecipitation, pull down	physical, physical association	18388313, (Europe PMC)	0.52	BioGRID, IntAct, MINT
SORBS3	Affinity Capture-Western, anti tag coimmunoprecipitation	physical, physical association	16483316, 18662323, (Europe PMC)	0.59	BioGRID, IntAct, MINT
SRC	Biochemical Activity	physical	15791211, (Europe PMC)	NA	BioGRID
TRIP10	Co-fractionation, Reconstituted Complex, anti bait coimmunoprecipitation, two hybrid array, two hybrid prey pooling approach	physical, physical association	16418535, 20940394, 26344197, (Europe PMC)	0.40, 0.49	BioGRID, IntAct
VIPR1	Reconstituted Complex	physical	10867004, (Europe PMC)	NA	BioGRID
WASF1	Co-fractionation	physical	26344197, (Europe PMC)	NA	BioGRID
WASF2	Co-fractionation	physical	22939629, 26344197, (Europe PMC)	NA	BioGRID
WASF3	Co-fractionation	physical	26344197, (Europe PMC)	NA	BioGRID
WIPF1	Affinity Capture-MS, Affinity Capture-Western, Reconstituted Complex, Two-hybrid, anti bait coimmunoprecipitation, two hybrid, two hybrid array, two hybrid fragment pooling approach, two hybrid prey pooling approach, validated two hybrid	physical, physical association	11331876, 12372256, 16582881, 23414517, 25416956, 28514442, (Europe PMC)	0.81	BioGRID, IntAct, MINT
WIPF2	Affinity Capture-MS, Co-fractionation, two hybrid array, two hybrid fragment pooling approach, two hybrid prey pooling approach	physical, physical association	22939629, 23414517, 28514442, (Europe PMC)	0.62	BioGRID, IntAct
WIPF3	Affinity Capture-MS, two hybrid fragment pooling approach	physical, physical association	23414517, 28514442, (Europe PMC)	0.37	BioGRID, IntAct
WWOX	Affinity Capture-MS	physical	24550385, (Europe PMC)	NA	BioGRID
ZNF395	Two-hybrid, two hybrid	physical, physical association	21988832, (Europe PMC)	0.37	BioGRID, IntAct
ZNF638	Co-fractionation	physical	22939629, (Europe PMC)	NA	BioGRID

Visualize Download

Interacting partner	Detection method	Interaction type	PubMed IDs	Interaction Score	Source
ABI2	Co-fractionation, two hybrid array, two hybrid prey pooling approach	physical, physical association	26344197, (Europe PMC)	0.49	BioGRID, IntAct
ACTR2	Protein-peptide, coimmunoprecipitation	physical, physical association	12732638, 15834156, (Europe PMC)	0.40	BioGRID, IntAct, MINT
ACTR3	Protein-peptide, pull down	physical, physical association	12732638, 17028176, (Europe PMC)	0.40	BioGRID, IntAct
ARPC1B	Affinity Capture-Western, pull down	direct interaction, physical, physical association	11943145, 15894313, (Europe PMC)	0.61	BioGRID, IntAct, MINT
ARPC2	pull down	physical association	24132237, (Europe PMC)	0.40	IntAct
ARPC3	Two-hybrid, two hybrid array, two hybrid prey pooling approach, validated two hybrid	physical, physical association	25416956, (Europe PMC)	0.70	BioGRID, IntAct
BAIAP2	Affinity Capture-MS, Two-hybrid, anti tag coimmunoprecipitation, two hybrid	association, physical, physical association	21988832, 26496610, (Europe PMC)	0.55	BioGRID, IntAct
BAIAP2L1	nuclear magnetic resonance	physical association	22921828, (Europe PMC)	0.40	IntAct
CD44	anti bait coimmunoprecipitation	association	17092940, (Europe PMC)	0.35	IntAct
CDC42	Reconstituted Complex, Two-hybrid, coimmunoprecipitation, phosphatase assay, protein kinase assay, two hybrid, two hybrid pooling approach	phosphorylation reaction, physical, physical association	10781580, 11331876, 15834156, 16293614, 20936779, 21311754, 9422512, (Europe PMC)	0.37, 0.75	BioGRID, IntAct, MINT
CIB1	anti bait coimmunoprecipitation, anti tag coimmunoprecipitation, surface plasmon resonance, two hybrid	direct interaction, physical association	16582881, (Europe PMC)	0.63	IntAct, MINT
CRK	coimmunoprecipitation	physical association	15834156, (Europe PMC)	0.40	IntAct, MINT
CTTN	Affinity Capture-Western, Far Western, fluorescence microscopy	colocalization, physical	11830518, 12672817, 18344974, (Europe PMC)	0.27	BioGRID, IntAct, MINT
DNMBP	Affinity Capture-MS, isothermal titration calorimetry, x-ray crystallography	direct interaction, physical	14506234, 24332715, (Europe PMC)	0.56	BioGRID, IntAct
EBI-16429374	two hybrid array, two hybrid prey pooling approach, validated two hybrid	physical association	26871637, (Europe PMC)	0.56	IntAct
EEF1D	display technology	physical association	20195357, (Europe PMC)	0.40	IntAct
EGFR	PCA, Two-hybrid, ubiquitin reconstruction	physical, physical association	24658140, 25402006, (Europe PMC)	0.37	BioGRID, IntAct
EP300	two hybrid	physical association	21988832, (Europe PMC)	0.37	IntAct
FCHSD2	Two-hybrid, two hybrid	physical, physical association	21988832, (Europe PMC)	0.37	BioGRID, IntAct
GRB2	Affinity Capture-MS, Reconstituted Complex, Two-hybrid, anti tag coimmunoprecipitation, barcode fusion genetics two hybrid, peptide array, two hybrid array, two hybrid pooling approach, two hybrid prey pooling approach, validated two hybrid	association, physical, physical association	10781580, 17474147, 20936779, 21706016, 25416956, 27107012, 28514442, (Europe PMC)	0.86	BioGRID, IntAct
HP	Two-hybrid, two hybrid	physical, physical association	21988832, (Europe PMC)	0.37	BioGRID, IntAct
IPO5	Two-hybrid, two hybrid	physical, physical association	21988832, (Europe PMC)	0.37	BioGRID, IntAct
ITCH	two hybrid fragment pooling approach	physical association	23414517, (Europe PMC)	0.37	IntAct
ITGA2	anti bait coimmunoprecipitation	physical association	16582881, (Europe PMC)	0.40	IntAct, MINT
ITGB1BP2	two hybrid fragment pooling approach	physical association	23414517, (Europe PMC)	0.37	IntAct
ITSN1	Reconstituted Complex, coimmunoprecipitation, imaging technique, pull down	colocalization, direct interaction, physical, physical association	11584276, 18539136, (Europe PMC)	0.70	BioGRID, IntAct, MINT
LCK	Biochemical Activity, protein kinase assay	phosphorylation reaction, physical	16293614, (Europe PMC)	0.44	BioGRID, IntAct
NCK1	Affinity Capture-MS, Far Western, Reconstituted Complex, anti tag coimmunoprecipitation, peptide array, pull down	association, physical, physical association	11340081, 16595635, 17474147, 26496610, (Europe PMC)	0.50, 0.56	BioGRID, IntAct
NCK2	Affinity Capture-MS, Two-hybrid, two hybrid array, two hybrid prey pooling approach, validated two hybrid	physical, physical association	25416956, 26186194, 26871637, 28514442, (Europe PMC)	0.72	BioGRID, IntAct
PACSIN2	Reconstituted Complex, two hybrid array, two hybrid prey pooling approach	physical, physical association	11082044, (Europe PMC)	0.49	BioGRID, IntAct
PACSIN3	Reconstituted Complex, two hybrid array, two hybrid prey pooling approach	physical, physical association	11082044, (Europe PMC)	0.49	BioGRID, IntAct
PTK6	Two-hybrid, two hybrid array, two hybrid prey pooling approach, validated two hybrid	physical, physical association	25416956, (Europe PMC)	0.56	BioGRID, IntAct
PTPN2	phosphatase assay	dephosphorylation reaction	16293614, (Europe PMC)	0.44	IntAct
RHOJ	Two-hybrid, two hybrid array, two hybrid prey pooling approach, validated two hybrid	physical, physical association	25416956, (Europe PMC)	0.70	BioGRID, IntAct
RNF8	two hybrid, two hybrid array, two hybrid prey pooling approach, validated two hybrid	physical association	21516116, 25416956, (Europe PMC)	0.76	IntAct, MINT
ROBO4	two hybrid	physical association	18948384, (Europe PMC)	0.37	IntAct
SDCBP	Two-hybrid, two hybrid array, two hybrid prey pooling approach, validated two hybrid	physical, physical association	25416956, (Europe PMC)	0.70	BioGRID, IntAct
SKA1	Affinity Capture-MS, anti tag coimmunoprecipitation	association, physical	26496610, (Europe PMC)	0.35	BioGRID, IntAct
SNX9	Reconstituted Complex, anti tag coimmunoprecipitation, pull down	physical, physical association	18388313, (Europe PMC)	0.52	BioGRID, IntAct, MINT
SORBS3	Affinity Capture-Western, anti tag coimmunoprecipitation	physical, physical association	16483316, 18662323, (Europe PMC)	0.59	BioGRID, IntAct, MINT
TNNT3	two hybrid fragment pooling approach	physical association	23414517, (Europe PMC)	0.37	IntAct
TRIP10	Co-fractionation, Reconstituted Complex, anti bait coimmunoprecipitation, two hybrid array, two hybrid prey pooling approach	physical, physical association	16418535, 20940394, 26344197, (Europe PMC)	0.40, 0.49	BioGRID, IntAct
WIPF1	Affinity Capture-MS, Affinity Capture-Western, Reconstituted Complex, Two-hybrid, anti bait coimmunoprecipitation, two hybrid, two hybrid array, two hybrid fragment pooling approach, two hybrid prey pooling approach, validated two hybrid	physical, physical association	11331876, 12372256, 16582881, 23414517, 25416956, 28514442, (Europe PMC)	0.81	BioGRID, IntAct, MINT
WIPF2	Affinity Capture-MS, Co-fractionation, two hybrid array, two hybrid fragment pooling approach, two hybrid prey pooling approach	physical, physical association	22939629, 23414517, 28514442, (Europe PMC)	0.62	BioGRID, IntAct
WIPF3	Affinity Capture-MS, two hybrid fragment pooling approach	physical, physical association	23414517, 28514442, (Europe PMC)	0.37	BioGRID, IntAct
WWP1	two hybrid fragment pooling approach	physical association	23414517, (Europe PMC)	0.37	IntAct
ZNF395	Two-hybrid, two hybrid	physical, physical association	21988832, (Europe PMC)	0.37	BioGRID, IntAct

Visualize Download

Interacting partner	Detection method	Interaction type	PubMed IDs	Interaction Score	Source
ARPC1B	Affinity Capture-Western, pull down	direct interaction, physical, physical association	11943145, 15894313, (Europe PMC)	0.61	BioGRID, IntAct, MINT
CDC42	Reconstituted Complex, Two-hybrid, coimmunoprecipitation, phosphatase assay, protein kinase assay, two hybrid, two hybrid pooling approach	phosphorylation reaction, physical, physical association	10781580, 11331876, 15834156, 16293614, 20936779, 21311754, 9422512, (Europe PMC)	0.37, 0.75	BioGRID, IntAct, MINT
CIB1	anti bait coimmunoprecipitation, anti tag coimmunoprecipitation, surface plasmon resonance, two hybrid	direct interaction, physical association	16582881, (Europe PMC)	0.63	IntAct, MINT
CRK	coimmunoprecipitation	physical association	15834156, (Europe PMC)	0.40	IntAct, MINT
CTTN	Affinity Capture-Western, Far Western, fluorescence microscopy	colocalization, physical	11830518, 12672817, 18344974, (Europe PMC)	0.27	BioGRID, IntAct, MINT
ITGA2	anti bait coimmunoprecipitation	physical association	16582881, (Europe PMC)	0.40	IntAct, MINT
ITSN1	Reconstituted Complex, coimmunoprecipitation, imaging technique, pull down	colocalization, direct interaction, physical, physical association	11584276, 18539136, (Europe PMC)	0.70	BioGRID, IntAct, MINT
RNF8	two hybrid, two hybrid array, two hybrid prey pooling approach, validated two hybrid	physical association	21516116, 25416956, (Europe PMC)	0.76	IntAct, MINT
SNX9	Reconstituted Complex, anti tag coimmunoprecipitation, pull down	physical, physical association	18388313, (Europe PMC)	0.52	BioGRID, IntAct, MINT
SORBS3	Affinity Capture-Western, anti tag coimmunoprecipitation	physical, physical association	16483316, 18662323, (Europe PMC)	0.59	BioGRID, IntAct, MINT
WIPF1	Affinity Capture-MS, Affinity Capture-Western, Reconstituted Complex, Two-hybrid, anti bait coimmunoprecipitation, two hybrid, two hybrid array, two hybrid fragment pooling approach, two hybrid prey pooling approach, validated two hybrid	physical, physical association	11331876, 12372256, 16582881, 23414517, 25416956, 28514442, (Europe PMC)	0.81	BioGRID, IntAct, MINT

Visualize Download

Interacting partner	Detection method	Interaction type	PubMed IDs	Interaction Score	Source
ABI1	Co-fractionation	physical	26344197, (Europe PMC)	NA	BioGRID
ABI2	Co-fractionation, two hybrid array, two hybrid prey pooling approach	physical, physical association	26344197, (Europe PMC)	0.49	BioGRID, IntAct
ACTBL2	Affinity Capture-MS	physical	28514442, (Europe PMC)	NA	BioGRID
ACTG1	Co-crystal Structure, Reconstituted Complex	physical	22847007, (Europe PMC)	NA	BioGRID
ACTR2	Protein-peptide, coimmunoprecipitation	physical, physical association	12732638, 15834156, (Europe PMC)	0.40	BioGRID, IntAct, MINT
ACTR3	Protein-peptide, pull down	physical, physical association	12732638, 17028176, (Europe PMC)	0.40	BioGRID, IntAct
APBB1	Reconstituted Complex	physical	16055720, (Europe PMC)	NA	BioGRID
APP	Reconstituted Complex	physical	21832049, (Europe PMC)	NA	BioGRID
ARPC1B	Affinity Capture-Western, pull down	direct interaction, physical, physical association	11943145, 15894313, (Europe PMC)	0.61	BioGRID, IntAct, MINT
ARPC2	pull down	physical association	24132237, (Europe PMC)	0.40	IntAct
ARPC3	Two-hybrid, two hybrid array, two hybrid prey pooling approach, validated two hybrid	physical, physical association	25416956, (Europe PMC)	0.70	BioGRID, IntAct
ASPA	Affinity Capture-MS	physical	28514442, (Europe PMC)	NA	BioGRID
ATG4C	Affinity Capture-MS	physical	28514442, (Europe PMC)	NA	BioGRID
BAIAP2	Affinity Capture-MS, Two-hybrid, anti tag coimmunoprecipitation, two hybrid	association, physical, physical association	21988832, 26496610, (Europe PMC)	0.55	BioGRID, IntAct
BAIAP2L1	nuclear magnetic resonance	physical association	22921828, (Europe PMC)	0.40	IntAct
BCHE	Affinity Capture-MS	physical	28514442, (Europe PMC)	NA	BioGRID
BIN1	Reconstituted Complex	physical	25262827, (Europe PMC)	NA	BioGRID
CD44	anti bait coimmunoprecipitation	association	17092940, (Europe PMC)	0.35	IntAct
CDC42	Reconstituted Complex, Two-hybrid, coimmunoprecipitation, phosphatase assay, protein kinase assay, two hybrid, two hybrid pooling approach	phosphorylation reaction, physical, physical association	10781580, 11331876, 15834156, 16293614, 20936779, 21311754, 9422512, (Europe PMC)	0.37, 0.75	BioGRID, IntAct, MINT
CIB1	anti bait coimmunoprecipitation, anti tag coimmunoprecipitation, surface plasmon resonance, two hybrid	direct interaction, physical association	16582881, (Europe PMC)	0.63	IntAct, MINT
CRK	coimmunoprecipitation	physical association	15834156, (Europe PMC)	0.40	IntAct, MINT
CTTN	Affinity Capture-Western, Far Western, fluorescence microscopy	colocalization, physical	11830518, 12672817, 18344974, (Europe PMC)	0.27	BioGRID, IntAct, MINT
DNMBP	Affinity Capture-MS, isothermal titration calorimetry, x-ray crystallography	direct interaction, physical	14506234, 24332715, (Europe PMC)	0.56	BioGRID, IntAct
EBI-16429374	two hybrid array, two hybrid prey pooling approach, validated two hybrid	physical association	26871637, (Europe PMC)	0.56	IntAct
EEF1D	display technology	physical association	20195357, (Europe PMC)	0.40	IntAct
EGFR	PCA, Two-hybrid, ubiquitin reconstruction	physical, physical association	24658140, 25402006, (Europe PMC)	0.37	BioGRID, IntAct
ELAVL1	Affinity Capture-RNA	physical	19322201, (Europe PMC)	NA	BioGRID
EP300	two hybrid	physical association	21988832, (Europe PMC)	0.37	IntAct
FCHSD2	Two-hybrid, two hybrid	physical, physical association	21988832, (Europe PMC)	0.37	BioGRID, IntAct
FNBP1	Co-fractionation, Reconstituted Complex	physical	16418535, 22939629, (Europe PMC)	NA	BioGRID
FNBP1L	Co-fractionation, Reconstituted Complex	physical	16418535, 26344197, (Europe PMC)	NA	BioGRID
GRB2	Affinity Capture-MS, Reconstituted Complex, Two-hybrid, anti tag coimmunoprecipitation, barcode fusion genetics two hybrid, peptide array, two hybrid array, two hybrid pooling approach, two hybrid prey pooling approach, validated two hybrid	association, physical, physical association	10781580, 17474147, 20936779, 21706016, 25416956, 27107012, 28514442, (Europe PMC)	0.86	BioGRID, IntAct
GSN	Co-crystal Structure	physical	16531231, (Europe PMC)	NA	BioGRID
HP	Two-hybrid, two hybrid	physical, physical association	21988832, (Europe PMC)	0.37	BioGRID, IntAct
HSP90AA1	Reconstituted Complex	physical	15791211, (Europe PMC)	NA	BioGRID
HSP90AB1	Reconstituted Complex	physical	15791211, (Europe PMC)	NA	BioGRID
IPO5	Two-hybrid, two hybrid	physical, physical association	21988832, (Europe PMC)	0.37	BioGRID, IntAct
IQGAP1	Affinity Capture-Western	physical	24639526, (Europe PMC)	NA	BioGRID
ITCH	two hybrid fragment pooling approach	physical association	23414517, (Europe PMC)	0.37	IntAct
ITGA2	anti bait coimmunoprecipitation	physical association	16582881, (Europe PMC)	0.40	IntAct, MINT
ITGB1BP2	two hybrid fragment pooling approach	physical association	23414517, (Europe PMC)	0.37	IntAct
ITSN1	Reconstituted Complex, coimmunoprecipitation, imaging technique, pull down	colocalization, direct interaction, physical, physical association	11584276, 18539136, (Europe PMC)	0.70	BioGRID, IntAct, MINT
ITSN2	Two-hybrid	physical	22558309, (Europe PMC)	NA	BioGRID
LCK	Biochemical Activity, protein kinase assay	phosphorylation reaction, physical	16293614, (Europe PMC)	0.44	BioGRID, IntAct
LSM1	Co-fractionation	physical	22939629, (Europe PMC)	NA	BioGRID
NCK1	Affinity Capture-MS, Far Western, Reconstituted Complex, anti tag coimmunoprecipitation, peptide array, pull down	association, physical, physical association	11340081, 16595635, 17474147, 26496610, (Europe PMC)	0.50, 0.56	BioGRID, IntAct
NCK2	Affinity Capture-MS, Two-hybrid, two hybrid array, two hybrid prey pooling approach, validated two hybrid	physical, physical association	25416956, 26186194, 26871637, 28514442, (Europe PMC)	0.72	BioGRID, IntAct
NTRK1	Affinity Capture-MS	physical	25921289, (Europe PMC)	NA	BioGRID
PACSIN1	Reconstituted Complex	physical	11082044, (Europe PMC)	NA	BioGRID
PACSIN2	Reconstituted Complex, two hybrid array, two hybrid prey pooling approach	physical, physical association	11082044, (Europe PMC)	0.49	BioGRID, IntAct
PACSIN3	Reconstituted Complex, two hybrid array, two hybrid prey pooling approach	physical, physical association	11082044, (Europe PMC)	0.49	BioGRID, IntAct
PFN1	Affinity Capture-Western, Reconstituted Complex	physical	10867004, 9822597, (Europe PMC)	NA	BioGRID
PRPF40A	Reconstituted Complex	physical	16055720, (Europe PMC)	NA	BioGRID
PSTPIP1	Reconstituted Complex	physical	16418535, (Europe PMC)	NA	BioGRID
PTK6	Two-hybrid, two hybrid array, two hybrid prey pooling approach, validated two hybrid	physical, physical association	25416956, (Europe PMC)	0.56	BioGRID, IntAct
PTPN2	phosphatase assay	dephosphorylation reaction	16293614, (Europe PMC)	0.44	IntAct
RHOJ	Two-hybrid, two hybrid array, two hybrid prey pooling approach, validated two hybrid	physical, physical association	25416956, (Europe PMC)	0.70	BioGRID, IntAct
RHOQ	Reconstituted Complex, Two-hybrid	physical	12456725, (Europe PMC)	NA	BioGRID
RNF8	Two-hybrid	physical	21516116, 25416956, (Europe PMC)	NA	BioGRID
RNF8	two hybrid, two hybrid array, two hybrid prey pooling approach, validated two hybrid	physical association	21516116, 25416956, (Europe PMC)	0.76	IntAct, MINT
ROBO4	two hybrid	physical association	18948384, (Europe PMC)	0.37	IntAct
RPL7AP66	Two-hybrid	physical	21988832, (Europe PMC)	NA	BioGRID
SDCBP	Two-hybrid, two hybrid array, two hybrid prey pooling approach, validated two hybrid	physical, physical association	25416956, (Europe PMC)	0.70	BioGRID, IntAct
SH3KBP1	Affinity Capture-MS	physical	19531213, (Europe PMC)	NA	BioGRID
SKA1	Affinity Capture-MS, anti tag coimmunoprecipitation	association, physical	26496610, (Europe PMC)	0.35	BioGRID, IntAct
SNX9	Reconstituted Complex, anti tag coimmunoprecipitation, pull down	physical, physical association	18388313, (Europe PMC)	0.52	BioGRID, IntAct, MINT
SORBS3	Affinity Capture-Western, anti tag coimmunoprecipitation	physical, physical association	16483316, 18662323, (Europe PMC)	0.59	BioGRID, IntAct, MINT
SRC	Biochemical Activity	physical	15791211, (Europe PMC)	NA	BioGRID
TNNT3	two hybrid fragment pooling approach	physical association	23414517, (Europe PMC)	0.37	IntAct
TRIP10	Co-fractionation, Reconstituted Complex, anti bait coimmunoprecipitation, two hybrid array, two hybrid prey pooling approach	physical, physical association	16418535, 20940394, 26344197, (Europe PMC)	0.40, 0.49	BioGRID, IntAct
VIPR1	Reconstituted Complex	physical	10867004, (Europe PMC)	NA	BioGRID
WASF1	Co-fractionation	physical	26344197, (Europe PMC)	NA	BioGRID
WASF2	Co-fractionation	physical	22939629, 26344197, (Europe PMC)	NA	BioGRID
WASF3	Co-fractionation	physical	26344197, (Europe PMC)	NA	BioGRID
WIPF1	Affinity Capture-MS, Affinity Capture-Western, Reconstituted Complex, Two-hybrid, anti bait coimmunoprecipitation, two hybrid, two hybrid array, two hybrid fragment pooling approach, two hybrid prey pooling approach, validated two hybrid	physical, physical association	11331876, 12372256, 16582881, 23414517, 25416956, 28514442, (Europe PMC)	0.81	BioGRID, IntAct, MINT
WIPF2	Affinity Capture-MS, Co-fractionation, two hybrid array, two hybrid fragment pooling approach, two hybrid prey pooling approach	physical, physical association	22939629, 23414517, 28514442, (Europe PMC)	0.62	BioGRID, IntAct
WIPF3	Affinity Capture-MS, two hybrid fragment pooling approach	physical, physical association	23414517, 28514442, (Europe PMC)	0.37	BioGRID, IntAct
WWOX	Affinity Capture-MS	physical	24550385, (Europe PMC)	NA	BioGRID
WWP1	two hybrid fragment pooling approach	physical association	23414517, (Europe PMC)	0.37	IntAct
ZNF395	Two-hybrid, two hybrid	physical, physical association	21988832, (Europe PMC)	0.37	BioGRID, IntAct
ZNF638	Co-fractionation	physical	22939629, (Europe PMC)	NA	BioGRID

Top

WASL