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Statistics
241 human active and 13 inactive phosphatases in total;
194 phosphatases have substrate data;
--------------------------------
336 protein substrates;
83 non-protein substrates;
1215 dephosphorylation interactions;
--------------------------------
299 KEGG pathways;
876 Reactome pathways;
--------------------------------
last scientific update:
11 Mar, 2019
last maintenance update:
01 Sep, 2023
194 phosphatases have substrate data;
--------------------------------
336 protein substrates;
83 non-protein substrates;
1215 dephosphorylation interactions;
--------------------------------
299 KEGG pathways;
876 Reactome pathways;
--------------------------------
last scientific update:
11 Mar, 2019
last maintenance update:
01 Sep, 2023
Top
IGF1R
Gene Name  | IGF1R (QuickGO) | (A quick tutorial to explore the interctive visulaization) Representative structure: 3NW7 |
| Synonyms | IGF1R | |
| Protein Name | IGF1R | |
| Alternative Name(s) | Insulin-like growth factor 1 receptor;2.7.10.1;Insulin-like growth factor I receptor;IGF-I receptor;CD221;Insulin-like growth factor 1 receptor alpha chain;Insulin-like growth factor 1 receptor beta chain; | |
| Protein Family | Belongs to the protein kinase superfamily Tyr proteinkinase family Insulin receptor subfamily | |
| EntrezGene ID | 3480 (Comparitive Toxicogenomics) | |
| UniProt AC (Human) | P08069 (protein sequence) | |
| Enzyme Class | 2.7.10.1 (BRENDA ) | |
| Molecular Weight | 154793 Dalton | |
| Protein Length | 1367 amino acids (AA) | |
| Genome Browsers | NCBI | ENSG00000140443 (Ensembl) | UCSC | |
| Crosslinking annotations | Query our ID-mapping table | |
| Orthologues | Quest For Orthologues (QFO) | GeneTree | eggNOG - KOG4258 | eggNOG - COG0515 | |
| Phosphorylation Network | Visualize | |
| Domain organization, Expression, Diseases | (show / hide) |
| Protein Domain | InterPro | Pfam | SMART | 3D Structure | PDB | DrugPort | ModBase | SwissModel |
| Polypeptide organization (Pfam)  | |||
| Gene Expression | Gene Expression Atlas | Disease | OMIM | DisGeNet | COSMIC | ClinVar |
| Protein-protein interactions | STRING | IntAct | MINT | BioGRID | ||
| Phosphosites | Phospho.ELM | PhosphoSitePlus |
| Localization, Function, Catalytic activity and Sequence | (show / hide) |
| Localization (UniProt annotation) | |||
| Cell membrane | |||
| Function (UniProt annotation) | |||
| Receptor tyrosine kinase which mediates actions ofinsulin-like growth factor 1 (IGF1) Binds IGF1 with high affinityand IGF2 and insulin (INS) with a lower affinity The activatedIGF1R is involved in cell growth and survival control IGF1R iscrucial for tumor transformation and survival of malignant cellLigand binding activates the receptor kinase, leading to receptorautophosphorylation, and tyrosines phosphorylation of multiplesubstrates, that function as signaling adapter proteins including,the insulin-receptor substrates (IRS1/2), Shc and 14-3-3 proteinsPhosphorylation of IRSs proteins lead to the activation of twomain signaling pathways: the PI3K-AKT/PKB pathway and the Ras-MAPKpathway The result of activating the MAPK pathway is increasedcellular proliferation, whereas activating the PI3K pathwayinhibits apoptosis and stimulates protein synthesisPhosphorylated IRS1 can activate the 85 kDa regulatory subunit ofPI3K (PIK3R1), leading to activation of several downstreamsubstrates, including protein AKT/PKB AKT phosphorylation, inturn, enhances protein synthesis through mTOR activation andtriggers the antiapoptotic effects of IGFIR throughphosphorylation and inactivation of BAD In parallel to PI3K-driven signaling, recruitment of Grb2/SOS by phosphorylated IRS1or Shc leads to recruitment of Ras and activation of the ras-MAPKpathway In addition to these two main signaling pathways IGF1Rsignals also through the Janus kinase/signal transducer andactivator of transcription pathway (JAK/STAT) Phosphorylation ofJAK proteins can lead to phosphorylation/activation of signaltransducers and activators of transcription (STAT) proteins Inparticular activation of STAT3, may be essential for thetransforming activity of IGF1R The JAK/STAT pathway activatesgene transcription and may be responsible for the transformingactivity JNK kinases can also be activated by the IGF1R IGF1exerts inhibiting activities on JNK activation via phosphorylationand inhibition of MAP3K5/ASK1, which is able to directly associatewith the IGF1R When present in a hybrid receptor with INSR, binds IGF1PubMed:12138094 shows that hybrid receptors composed of IGF1R andINSR isoform Long are activated with a high affinity by IGF1, withlow affinity by IGF2 and not significantly activated by insulin,and that hybrid receptors composed of IGF1R and INSR isoform Shortare activated by IGF1, IGF2 and insulin In contrast,PubMed:16831875 shows that hybrid receptors composed of IGF1R andINSR isoform Long and hybrid receptors composed of IGF1R and INSRisoform Short have similar binding characteristics, both bind IGF1and have a low affinity for insulin | |||
| Catalytic Activity (UniProt annotation) | |||
| ATP + a [protein]-L-tyrosine = ADP + a[protein]-L-tyrosine phosphate | |||
| Protein Sequence | |||
| MKSGSGGGSPTSLWGLLFLSAALSLWPTSGEICGPGIDIRNDYQQLKRLENCTVIEGYLHILLISKAEDYRSYRFPKLTV ITEYLLLFRVAGLESLGDLFPNLTVIRGWKLFYNYALVIFEMTNLKDIGLYNLRNITRGAIRIEKNADLCYLSTVDWSLI LDAVSNNYIVGNKPPKECGDLCPGTMEEKPMCEKTTINNEYNYRCWTTNRCQKMCPSTCGKRACTENNECCHPECLGSCS APDNDTACVACRHYYYAGVCVPACPPNTYRFEGWRCVDRDFCANILSAESSDSEGFVIHDGECMQECPSGFIRNGSQSMY CIPCEGPCPKVCEEEKKTKTIDSVTSAQMLQGCTIFKGNLLINIRRGNNIASELENFMGLIEVVTGYVKIRHSHALVSLS FLKNLRLILGEEQLEGNYSFYVLDNQNLQQLWDWDHRNLTIKAGKMYFAFNPKLCVSEIYRMEEVTGTKGRQSKGDINTR NNGERASCESDVLHFTSTTTSKNRIIITWHRYRPPDYRDLISFTVYYKEAPFKNVTEYDGQDACGSNSWNMVDVDLPPNK DVEPGILLHGLKPWTQYAVYVKAVTLTMVENDHIRGAKSEILYIRTNASVPSIPLDVLSASNSSSQLIVKWNPPSLPNGN LSYYIVRWQRQPQDGYLYRHNYCSKDKIPIRKYADGTIDIEEVTENPKTEVCGGEKGPCCACPKTEAEKQAEKEEAEYRK VFENFLHNSIFVPRPERKRRDVMQVANTTMSSRSRNTTAADTYNITDPEELETEYPFFESRVDNKERTVISNLRPFTLYR IDIHSCNHEAEKLGCSASNFVFARTMPAEGADDIPGPVTWEPRPENSIFLKWPEPENPNGLILMYEIKYGSQVEDQRECV SRQEYRKYGGAKLNRLNPGNYTARIQATSLSGNGSWTDPVFFYVQAKTGYENFIHLIIALPVAVLLIVGGLVIMLYVFHR KRNNSRLGNGVLYASVNPEYFSAADVYVPDEWEVAREKITMSRELGQGSFGMVYEGVAKGVVKDEPETRVAIKTVNEAAS MRERIEFLNEASVMKEFNCHHVVRLLGVVSQGQPTLVIMELMTRGDLKSYLRSLRPEMENNPVLAPPSLSKMIQMAGEIA DGMAYLNANKFVHRDLAARNCMVAEDFTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMSPESLKDGVFTTYSDVWSFGV VLWEIATLAEQPYQGLSNEQVLRFVMEGGLLDKPDNCPDMLFELMRMCWQYNPKMRPSFLEIISSIKEEMEPGFREVSFY YSEENKLPEPEELDLEPENMESVPLDPSASSSSLPLPDRHSGHKAENGPGPGVLVLRASFDERQPYAHMNGGRKNERALP LPQSSTC | |||
| Motif information from Eukaryotic Linear Motif atlas (ELM) | (show / hide) |
| ELM Motif | Motif Instance
| Description | Motif Regex |
| NA | NA | NA | NA |
| Gene Ontology (P: Process; F: Function and C: Component terms) | (show / hide) | |
| GO:0004713 | F:protein tyrosine kinase activity |
| GO:0005010 | F:insulin-like growth factor-activated receptor activity |
| GO:0005158 | F:insulin receptor binding |
| GO:0005520 | F:insulin-like growth factor binding |
| GO:0005524 | F:ATP binding |
| GO:0005886 | C:plasma membrane |
| GO:0005887 | C:integral component of plasma membrane |
| GO:0006955 | P:immune response |
| GO:0007165 | P:signal transduction |
| GO:0008284 | P:positive regulation of cell proliferation |
| GO:0008286 | P:insulin receptor signaling pathway |
| GO:0014065 | P:phosphatidylinositol 3-kinase signaling |
| GO:0016020 | C:membrane |
| GO:0030335 | P:positive regulation of cell migration |
| GO:0031994 | F:insulin-like growth factor I binding |
| GO:0035867 | C:alphav-beta3 integrin-IGF-1-IGF1R complex |
| GO:0038083 | P:peptidyl-tyrosine autophosphorylation |
| GO:0042802 | F:identical protein binding |
| GO:0043066 | P:negative regulation of apoptotic process |
| GO:0043231 | C:intracellular membrane-bounded organelle |
| GO:0043235 | C:receptor complex |
| GO:0043243 | P:positive regulation of protein complex disassembly |
| GO:0043548 | F:phosphatidylinositol 3-kinase binding |
| GO:0043559 | F:insulin binding |
| GO:0043560 | F:insulin receptor substrate binding |
| GO:0046328 | P:regulation of JNK cascade |
| GO:0046777 | P:protein autophosphorylation |
| GO:0048009 | P:insulin-like growth factor receptor signaling pathway |
| GO:0048015 | P:phosphatidylinositol-mediated signaling |
| GO:0051262 | P:protein tetramerization |
| GO:0051389 | P:inactivation of MAPKK activity |
| GO:0097062 | P:dendritic spine maintenance |
| GO:0097242 | P:amyloid-beta clearance |
| GO:0120162 | P:positive regulation of cold-induced thermogenesis |
| GO:1904646 | P:cellular response to amyloid-beta |
IGF1R is dephosphorylated by following phosphatases:
| Phosphatase Gene Name | Phosphatase UniProt_AC | DephosphoSite and sequence (+/-5) in IGF1R (P08069) | Bioassay Type | PubMed ID | View in Europe PMC | Reliability of the interaction |
| PTPN1 | P18031 | Tyr-1161_MTRDIyETDYY,, Tyr-1165_IYETDyYRKGG, | In vitro and in vivo | 8702689, 23814047, | Europe PMC |  |
| Pathway ID | Pathway Name | Pathway Description (KEGG) |
| hsa01521 | EGFR tyrosine kinase inhibitor resistance | EGFR is a tyrosine kinase that participates in the regulation of cellular homeostasis. EGFR also serves as a stimulus for cancer growth. EGFR gene mutations and protein overexpression, both of which activate down- stream pathways, are associated with cancers, especially lung cancer. Several tyrosine kinase inhibitor (TKI) therapies against EGFR are currently administered and are initially effective in cancer patients who have EGFR mutations or aberrant activation of EGFR. However, the development of TKI resistance is common and results in the recurrence of tumors. Studies over the last decade have identified mechanisms that drive resistance to EGFR TKI treatment. Most outstanding mechanisms are: the secondary EGFR mutation (T790M), activation of alternative pathways (c-Met, HGF, AXL), aberrance of the downstream pathways (K-RAS mutations, loss of PTEN), impairment of the EGFR-TKIs-mediated apoptosis pathway (BCL2-like 11/BIM deletion polymorphism), histologic transformation, etc. |
| hsa01522 | Endocrine resistance | Endocrine therapy is a key treatment strategy to control or eradicate hormone-responsive breast cancer. The most commonly used endocrine therapy agents are selective estrogen receptor modulators (SERMs, e.g. tamoxifen), estrogen synthesis inhibitors (e.g. aromatase inhibitors (AIs) such as anastrozole, letrozole, and exemestane), and selective estrogen receptor down-regulators (SERDs, e.g. fulvestrant). However, resistance to these agents has become a major clinical obstacle. Mechanisms of endocrine resistance include loss of ER-alpha expression, altered expression of coactivators or coregulators that play a critical role in ER-mediated gene transcription, ligand-independent growth factor signaling cascades that activate kinases and ER-phosphorylation, altered availability of active tamoxifen metabolites regulated by drug-metabolizing enzymes, such as CYP2D6, and deregulation of the cell cycle and apoptotic machinery. |
| hsa04010 | MAPK signaling pathway | The mitogen-activated protein kinase (MAPK) cascade is a highly conserved module that is involved in various cellular functions, including cell proliferation, differentiation and migration. Mammals express at least four distinctly regulated groups of MAPKs, extracellular signal-related kinases (ERK)-1/2, Jun amino-terminal kinases (JNK1/2/3), p38 proteins (p38alpha/beta/gamma/delta) and ERK5, that are activated by specific MAPKKs: MEK1/2 for ERK1/2, MKK3/6 for the p38, MKK4/7 (JNKK1/2) for the JNKs, and MEK5 for ERK5. Each MAPKK, however, can be activated by more than one MAPKKK, increasing the complexity and diversity of MAPK signalling. Presumably each MAPKKK confers responsiveness to distinct stimuli. For example, activation of ERK1/2 by growth factors depends on the MAPKKK c-Raf, but other MAPKKKs may activate ERK1/2 in response to pro-inflammatory stimuli. |
| hsa04014 | Ras signaling pathway | The Ras proteins are GTPases that function as molecular switches for signaling pathways regulating cell proliferation, survival, growth, migration, differentiation or cytoskeletal dynamism. Ras proteins transduce signals from extracellular growth factors by cycling between inactive GDP-bound and active GTP-bound states. The exchange of GTP for GDP on RAS is regulated by guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs). Activated RAS (RAS-GTP) regulates multiple cellular functions through effectors including Raf, phosphatidylinositol 3-kinase (PI3K) and Ral guanine nucleotide-dissociation stimulator (RALGDS). |
| hsa04015 | Rap1 signaling pathway | Rap1 is a small GTPase that controls diverse processes, such as cell adhesion, cell-cell junction formation and cell polarity. Like all G proteins, Rap1 cycles between an inactive GDP-bound and an active GTP-bound conformation. A variety of extracellular signals control this cycle through the regulation of several unique guanine nucleotide exchange factors (GEFs) and GTPase activating proteins (GAPs). Rap1 plays a dominant role in the control of cell-cell and cell-matrix interactions by regulating the function of integrins and other adhesion molecules in various cell types. Rap1 also regulates MAP kinase (MAPK) activity in a manner highly dependent on the context of cell types. |
| hsa04066 | HIF-1 signaling pathway | Hypoxia-inducible factor 1 (HIF-1) is a transcription factor that functions as a master regulator of oxygen homeostasis. It consists of two subunits: an inducibly-expressed HIF-1alpha subunit and a constitutively-expressed HIF-1beta subunit. Under normoxia, HIF-1 alpha undergoes hydroxylation at specific prolyl residues which leads to an immediate ubiquitination and subsequent proteasomal degradation of the subunit. In contrast, under hypoxia, HIF-1 alpha subunit becomes stable and interacts with coactivators such as p300/CBP to modulate its transcriptional activity. Eventually, HIF-1 acts as a master regulator of numerous hypoxia-inducible genes under hypoxic conditions. The target genes of HIF-1 encode proteins that increase O2 delivery and mediate adaptive responses to O2 deprivation. Despite its name, HIF-1 is induced not only in response to reduced oxygen availability but also by other stimulants, such as nitric oxide, or various growth factors. |
| hsa04068 | FoxO signaling pathway | The forkhead box O (FOXO) family of transcription factors regulates the expression of genes in cellular physiological events including apoptosis, cell-cycle control, glucose metabolism, oxidative stress resistance, and longevity. A central regulatory mechanism of FOXO proteins is phosphorylation by the serine-threonine kinase Akt/protein kinase B (Akt/PKB), downstream of phosphatidylinositol 3-kinase (PI3K), in response to insulin or several growth factors. Phosphorylation at three conserved residues results in the export of FOXO proteins from the nucleus to the cytoplasm, thereby decreasing expression of FOXO target genes. In contrast, the stress-activated c-Jun N-terminal kinase (JNK) and the energy sensing AMP-activated protein kinase (AMPK), upon oxidative and nutrient stress stimuli phosphorylate and activate FoxOs. Aside from PKB, JNK and AMPK, FOXOs are regulated by multiple players through several post-translational modifications, including phosphorylation, but also acetylation, methylation and ubiquitylation. |
| hsa04114 | Oocyte meiosis | During meiosis, a single round of DNA replication is followed by two rounds of chromosome segregation, called meiosis I and meiosis II. At meiosis I, homologous chromosomes recombine and then segregate to opposite poles, while the sister chromatids segregate from each other at meoisis II. In vertebrates, immature oocytes are arrested at the PI (prophase of meiosis I). The resumption of meiosis is stimulated by progesterone, which carries the oocyte through two consecutive M-phases (MI and MII) to a second arrest at MII. The key activity driving meiotic progression is the MPF (maturation-promoting factor), a heterodimer of CDC2 (cell division cycle 2 kinase) and cyclin B. In PI-arrested oocytes, MPF is initially inactive and is activated by the dual-specificity CDC25C phosphatase as the result of new synthesis of Mos induced by progesterone. MPF activation mediates the transition from the PI arrest to MI. The subsequent decrease in MPF levels, required to exit from MI into interkinesis, is induced by a negative feedback loop, where CDC2 brings about the activation of the APC (anaphase-promoting complex), which mediates destruction of cyclin B. Re-activation of MPF for MII requires re-accumulation of high levels of cyclin B as well as the inactivation of the APC by newly synthesized Emi2 and other components of the CSF (cytostatic factor), such as cyclin E or high levels of Mos. CSF antagonizes the ubiquitin ligase activity of the APC, preventing cyclin B destruction and meiotic exit until fertilization occurs. Fertilization triggers a transient increase in cytosolic free Ca2+, which leads to CSF inactivation and cyclin B destruction through the APC. Then eggs are released from MII into the first embryonic cell cycle. |
| hsa04140 | Autophagy - animal | Autophagy (or macroautophagy) is a cellular catabolic pathway involving in protein degradation, organelle turnover, and non-selective breakdown of cytoplasmic components, which is evolutionarily conserved among eukaryotes and exquisitely regulated. This progress initiates with production of the autophagosome, a double-membrane intracellular structure of reticular origin that engulfs cytoplasmic contents and ultimately fuses with lysosomes for cargo degradation. Autophagy is regulated in response to extra- or intracellular stress and signals such as starvation, growth factor deprivation and ER stress. Constitutive level of autophagy plays an important role in cellular homeostasis and maintains quality control of essential cellular components. |
| 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. |
| hsa04150 | mTOR signaling pathway | The mammalian (mechanistic) target of rapamycin (mTOR) is a highly conserved serine/threonine protein kinase, which exists in two complexes termed mTOR complex 1 (mTORC1) and 2 (mTORC2). mTORC1 contains mTOR, Raptor, PRAS40, Deptor, mLST8, Tel2 and Tti1. mTORC1 is activated by the presence of growth factors, amino acids, energy status, stress and oxygen levels to regulate several biological processes, including lipid metabolism, autophagy, protein synthesis and ribosome biogenesis. On the other hand, mTORC2, which consists of mTOR, mSin1, Rictor, Protor, Deptor, mLST8, Tel2 and Tti1, responds to growth factors and controls cytoskeletal organization, metabolism and survival. |
| hsa04151 | PI3K-Akt signaling pathway | The phosphatidylinositol 3' -kinase(PI3K)-Akt signaling pathway is activated by many types of cellular stimuli or toxic insults and regulates fundamental cellular functions such as transcription, translation, proliferation, growth, and survival. The binding of growth factors to their receptor tyrosine kinase (RTK) or G protein-coupled receptors (GPCR) stimulates class Ia and Ib PI3K isoforms, respectively. PI3K catalyzes the production of phosphatidylinositol-3,4,5-triphosphate (PIP3) at the cell membrane. PIP3 in turn serves as a second messenger that helps to activate Akt. Once active, Akt can control key cellular processes by phosphorylating substrates involved in apoptosis, protein synthesis, metabolism, and cell cycle. |
| hsa04152 | AMPK signaling pathway | AMP-activated protein kinase (AMPK) is a serine threonine kinase that is highly conserved through evolution. AMPK system acts as a sensor of cellular energy status. It is activated by increases in the cellular AMP:ATP ratio caused by metabolic stresses that either interfere with ATP production (eg, deprivation for glucose or oxygen) or that accelerate ATP consumption (eg, muscle contraction). Several upstream kinases, including liver kinase B1 (LKB1), calcium/calmodulin kinase kinase-beta (CaMKK beta), and TGF-beta-activated kinase-1 (TAK-1), can activate AMPK by phosphorylating a threonine residue on its catalytic alpha-subunit. Once activated, AMPK leads to a concomitant inhibition of energy-consuming biosynthetic pathways, such as protein, fatty acid and glycogen synthesis, and activation of ATP-producing catabolic pathways, such as fatty acid oxidation and glycolysis. |
| hsa04211 | Longevity regulating pathway | Regulation of longevity depends on genetic and environmental factors. Caloric restriction (CR), that is limiting food intake, is recognized in mammals as the best characterized and most reproducible strategy for extending lifespan. Four pathways have been implicated in mediating the CR effect. These are the insulin like growth factor (IGF-1)/insulin signaling pathway, the sirtuin pathway, the adenosine monophosphate (AMP) activated protein kinase (AMPK) pathway and the target of rapamycin (TOR) pathway. The collective response of these pathways to CR is believed to promote cellular fitness and ultimately longevity via activation of autophagy, stress defense mechanisms, and survival pathways while attenuating proinflammatory mediators and cellular growth. Furthermore, there is evidence supporting that life span extension can be achieved with pharmacologic agents that mimic the effects of caloric restriction, such as rapamycin, via mTOR signaling blockade, resveratrol, by activating SIRT1 activity, and metformin, which seems to be a robust stimulator of AMPK activity. As an aging suppressor, Klotho is an important molecule in aging processes and its overexpression results in longevity. |
| hsa04213 | Longevity regulating pathway - multiple species | Aging is a complex process of accumulation of molecular, cellular, and organ damage, leading to loss of function and increased vulnerability to disease and death. Despite the complexity of aging, recent work has shown that dietary restriction (DR) and genetic down-regulation of nutrient-sensing pathways, namely IIS (insulin/insulin-like growth factor signalling) and TOR (target-of- rapamycin) can substantially increase healthy life span of laboratory model organisms. These nutrient signaling pathways are conserved in various organisms. In worms, flies, and mammals, DR reduces signalling through IIS/TOR pathways, deactivating the PI3K/Akt/TOR intracellular signalling cascade and consequently activating the antiaging FOXO family transcription factor(s). In yeast, the effects of DR on life- span extension are associated with reduced activities of the TOR/Sch9 and Ras/PKA pathways and require the serine-threonine kinase Rim15 and transcription factors Gis1 and Msn2/4. These transcription factors (FOXO, DAF-16, Gis1, and Msn2/4) transactivate genes involved in resistance to oxidative stress, energy metabolism, DNA damage repair, glucose metabolism, autophagy and protection of proteins by chaperones. |
| 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. |
| hsa04550 | Signaling pathways regulating pluripotency of stem cells | Pluripotent stem cells (PSCs) are basic cells with an indefinite self-renewal capacity and the potential to generate all the cell types of the three germinal layers. The types of PSCs known to date include embryonic stem (ES) and induced pluripotent stem (iPS) cells. ES cells are derived from the inner cell mass (ICM) of blastocyst-stage embryos. iPS cells are generated by reprogramming somatic cells back to pluripotent state with defined reprogramming factors, Oct4, Sox2, Klf4 and c-Myc (also known as Yamanaka factors). PSCs including ES cells and iPS cells are categorized into two groups by their morphology, gene expression profile and external signal dependence. Conventional mouse-type ES/iPS cells are called 'naive state' cells. They are mainly maintained under the control of LIF and BMP signaling. On the other hand, human-type ES/iPS cells, which are in need of Activin and FGF signaling, are termed 'primed state'. However, these signaling pathways converge towards the activation of a core transcriptional network that is similar in both groups and involves OCt4, Nanog and Sox2. The three transcription factors and their downstream target genes coordinately promote self-renewal and pluripotency. |
| hsa04730 | Long-term depression | Cerebellar long-term depression (LTD), thought to be a molecular and cellular basis for cerebellar learning, is a process involving a decrease in the synaptic strength between parallel fiber (PF) and Purkinje cells (PCs) induced by the conjunctive activation of PFs and climbing fiber (CF). Multiple signal transduction pathways have been shown to be involved in this process. Activation of PFs terminating on spines in dendritic branchlets leads to glutamate release and activation of both AMPA and mGluRs. Activation of CFs, which make multiple synaptic contacts on proximal dendrites, also via AMPA receptors, opens voltage-gated calcium channels (VGCCs) and causes a generalized influx of calcium. These cellular signals, generated from two different synaptic origins, trigger a cascade of events culminating in a phosphorylation-dependent, long-term reduction in AMPA receptor sensitivity at the PF-PC synapse. This may take place either through receptor internalization and/or through receptor desensitization. |
| hsa04913 | Ovarian steroidogenesis | The ovarian steroids, 17-beta estradiol (E2) and progesterone (P4), are critical for normal uterine function, establishment and maintenance of pregnancy, and mammary gland development. Furthermore, the local effects that are essential for normal ovarian physiology are dependent on the endocrine, paracrine, and autocrine actions of E2, P4, and androgens. In most mammals (including humans and mice), ovarian steroidogenesis occurs according to the two-cell/two-gonadotropin theory. This theory describes how granulosa and theca cells work together to make the ovarian steroids. Theca cells respond to LH signaling by increasing the expression of enzymes necessary for the conversion of cholesterol to androgens, such as androstenedione (A) and testosterone (T). Granulosa cells respond to FSH signaling by increasing the expression of enzymes necessary for the conversion of theca-derived androgens into estrogens (E2 and estrone). |
| hsa04914 | Progesterone-mediated oocyte maturation | Xenopus oocytes are naturally arrested at G2 of meiosis I. Exposure to either insulin/IGF-1 or the steroid hormone progesterone breaks this arrest and induces resumption of the two meiotic division cycles and maturation of the oocyte into a mature, fertilizable egg. This process is termed oocyte maturation. The transition is accompanied by an increase in maturation promoting factor (MPF or Cdc2/cyclin B) which precedes germinal vesicle breakdown (GVBD). Most reports point towards the Mos-MEK1-ERK2 pathway [where ERK is an extracellular signal-related protein kinase, MEK is a MAPK/ERK kinase and Mos is a p42(MAPK) activator] and the polo-like kinase/CDC25 pathway as responsible for the activation of MPF in meiosis, most likely triggered by a decrease in cAMP. |
| hsa05200 | Pathways in cancer | |
| hsa05202 | Transcriptional misregulation in cancer | In tumor cells, genes encoding transcription factors (TFs) are often amplified, deleted, rearranged via chromosomal translocation and inversion, or subjected to point mutations that result in a gain- or loss-of- function. In hematopoietic cancers and solid tumors, the translocations and inversions increase or deregulate transcription of the oncogene. Recurrent chromosome translocations generate novel fusion oncoproteins, which are common in myeloid cancers and soft-tissue sarcomas. The fusion proteins have aberrant transcriptional function compared to their wild-type counterparts. These fusion transcription factors alter expression of target genes, and thereby result in a variety of altered cellular properties that contribute to the tumourigenic process. |
| hsa05205 | Proteoglycans in cancer | Many proteoglycans (PGs) in the tumor microenvironment have been shown to be key macromolecules that contribute to biology of various types of cancer including proliferation, adhesion, angiogenesis and metastasis, affecting tumor progress. The four main types of proteoglycans include hyaluronan (HA), which does not occur as a PG but in free form, heparan sulfate proteoglycans (HSPGs), chondroitin sulfate proteoglycans (CSPGs), dematan sulfate proteoglycans (DSPG) and keratan sulfate proteoglycans (KSPGs) [BR:00535]. Among these proteoglycans such as HA, acting with CD44, promotes tumor cell growth and migration, whereas other proteoglycans such as syndecans (-1~-4), glypican (-1, -3) and perlecan may interact with growth factors, cytokines, morphogens and enzymes through HS chains [BR: 00536], also leading to tumor growth and invasion. In contrast, some of the small leucine-rich proteolgycans, such as decorin and lumican, can function as tumor repressors, and modulate the signaling pathways by the interaction of their core proteins and multiple receptors. |
| hsa05214 | Glioma | Gliomas are the most common of the primary brain tumors and account for more than 40% of all central nervous system neoplasms. Gliomas include tumours that are composed predominantly of astrocytes (astrocytomas), oligodendrocytes (oligodendrogliomas), mixtures of various glial cells (for example,oligoastrocytomas) and ependymal cells (ependymomas). The most malignant form of infiltrating astrocytoma - glioblastoma multiforme (GBM) - is one of the most aggressive human cancers. GBM may develop de novo (primary glioblastoma) or by progression from low-grade or anaplastic astrocytoma (secondary glioblastoma). Primary glioblastomas develop in older patients and typically show genetic alterations (EGFR amplification, p16/INK4a deletion, and PTEN mutations) at frequencies of 24-34%. Secondary glioblastomas develop in younger patients and frequently show overexpression of PDGF and CDK4 as well as p53 mutations (65%) and loss of Rb playing major roles in such transformations. Loss of PTEN has been implicated in both pathways, although it is much more common in the pathogenesis of primary GBM. |
| hsa05215 | Prostate cancer | Prostate cancer constitutes a major health problem in Western countries. It is the most frequently diagnosed cancer among men and the second leading cause of male cancer deaths. The identification of key molecular alterations in prostate-cancer cells implicates carcinogen defenses (GSTP1), growth-factor-signaling pathways (NKX3.1, PTEN, and p27), and androgens (AR) as critical determinants of the phenotype of prostate-cancer cells. Glutathione S-transferases (GSTP1) are detoxifying enzymes. Cells of prostatic intraepithelial neoplasia, devoid of GSTP1, undergo genomic damage mediated by carcinogens. NKX3.1, PTEN, and p27 regulate the growth and survival of prostate cells in the normal prostate. Inadequate levels of PTEN and NKX3.1 lead to a reduction in p27 levels and to increased proliferation and decreased apoptosis. Androgen receptor (AR) is a transcription factor that is normally activated by its androgen ligand. During androgen withdrawal therapy, the AR signal transduction pathway also could be activated by amplification of the AR gene, by AR gene mutations, or by altered activity of AR coactivators. Through these mechanisms, tumor cells lead to the emergence of androgen-independent prostate cancer. |
| hsa05218 | Melanoma | Melanoma is a form of skin cancer that has a poor prognosis and which is on the rise in Western populations. Melanoma arises from the malignant transformation of pigment-producing cells, melanocytes. The only known environmental risk factor is exposure to ultraviolet (UV) light and in people with fair skin the risk is greatly increased. Melanoma pathogenesis is also driven by genetic factors. Oncogenic NRAS mutations activate both effector pathways Raf-MEK-ERK and PI3K-Akt. The Raf-MEK-ERK pathway may also be activated via mutations in the BRAF gene. The PI3K-Akt pathway may be activated through loss or mutation of the inhibitory tumor suppressor gene PTEN. These mutations arise early during melanoma pathogenesis and are preserved throughout tumor progression. Melanoma development has been shown to be strongly associated with inactivation of the p16INK4a/cyclin dependent kinases 4 and 6/retinoblastoma protein (p16INK4a/CDK4,6/pRb) and p14ARF/human double minute 2/p53 (p14ARF/HMD2/p53) tumor suppressor pathways. MITF and TP53 are implicated in further melanoma progression. |
| hsa05224 | Breast cancer | Breast cancer is the leading cause of cancer death among women worldwide. The vast majority of breast cancers are carcinomas that originate from cells lining the milk-forming ducts of the mammary gland. The molecular subtypes of breast cancer, which are based on the presence or absence of hormone receptors (estrogen and progesterone subtypes) and human epidermal growth factor receptor-2 (HER2), include: hormone receptor positive and HER2 negative (luminal A subtype), hormone receptor positive and HER2 positive (luminal B subtype), hormone receptor negative and HER2 positive (HER2 positive), and hormone receptor negative and HER2 negative (basal-like or triple-negative breast cancers (TNBCs)). Hormone receptor positive breast cancers are largely driven by the estrogen/ER pathway. In HER2 positive breast tumours, HER2 activates the PI3K/AKT and the RAS/RAF/MAPK pathways, and stimulate cell growth, survival and differentiation. In patients suffering from TNBC, the deregulation of various signalling pathways (Notch and Wnt/beta-catenin), EGFR protein have been confirmed. In the case of breast cancer only 8% of all cancers are hereditary, a phenomenon linked to genetic changes in BRCA1 or BRCA2. Somatic mutations in only three genes (TP53, PIK3CA and GATA3) occurred at >10% incidence across all breast cancers. |
| hsa05225 | Hepatocellular carcinoma | Hepatocellular carcinoma (HCC) is a major type of primary liver cancer and one of the rare human neoplasms etiologically linked to viral factors. It has been shown that, after HBV/HCV infection and alcohol or aflatoxin B1 exposure, genetic and epigenetic changes occur. The recurrent mutated genes were found to be highly enriched in multiple key driver signaling processes, including telomere maintenance, TP53, cell cycle regulation, the Wnt/beta-catenin pathway (CTNNB1 and AXIN1), the phosphatidylinositol-3 kinase (PI3K)/AKT/mammalian target of rapamycin (mTOR) pathway. Recent studies using whole-exome sequencing have revealed recurrent mutations in new driver genes involved in the chromatin remodelling (ARID1A and ARID2) and the oxidative stress (NFE2L2) pathways. |
| Pathway ID | Pathway Name | Pathway Description (KEGG) |
| R-HSA-2404192 | Signaling by Type 1 Insulin-like Growth Factor 1 Receptor (IGF1R). | Binding of IGF1 (IGF-I) or IGF2 (IGF-II) to the extracellular alpha peptides of the type 1 insulin-like growth factor receptor (IGF1R) triggers the activation of two major signaling pathways: the SOS-RAS-RAF-MAPK (ERK) pathway and the PI3K-PKB (AKT) pathway (recently reviewed in Pavelic et al. 2007, Chitnis et al. 2008, Maki et al. 2010, Parella et al. 2010, Annunziata et al. 2011, Siddle et al. 2012, Holzenberger 2012) |
| R-HSA-2428928 | IRS-related events triggered by IGF1R. | The phosphorylated type 1 insulin-like growth factor receptor phosphorylates IR1, IRS2, IRS4 and possibly other IRS/DOK family members (reviewed in Pavelic et al. 2007, Chitnis et al. 2008, Maki et al. 2010, Parrella et al. 2010, Siddle et al. 2012). The phosphorylated IRS proteins serve as scaffolds that bind the effector molecules PI3K and GRB2:SOS. PI3K then activates PKB (AKT) signaling while GRB2:SOS activates RAS-RAF-MAPK signaling |
| R-HSA-2428933 | SHC-related events triggered by IGF1R. | Phosphorylated IGF1R binds and phosphorylates SHC1 (reviewed in Pavelic et al. 2007, Chitnis et al. 2008, Maki et al. 2010, Parrella et al. 2010, Siddle et al. 2012). Phosphorylated SHC then binds GRB:SOS, which activates RAS-RAF-MAPK signaling |
| Interacting partner | Detection method | Interaction type | PubMed IDs | Interaction Score | Source |
| APP | Reconstituted Complex | physical | 21832049, (Europe PMC) | NA | BioGRID |
| ARHGEF12 | Affinity Capture-Western, Reconstituted Complex, Two-hybrid, anti bait coimmunoprecipitation, anti tag coimmunoprecipitation, imaging technique, pull down | colocalization, direct interaction, physical, physical association | 11724822, (Europe PMC) | 0.65 | BioGRID, IntAct, MINT |
| ARRB1 | Affinity Capture-Western, anti bait coimmunoprecipitation | physical, physical association | 15878855, 21685939, (Europe PMC) | 0.40 | BioGRID, IntAct |
| ARRB2 | Affinity Capture-Western | physical | 15878855, 19165858, 23188799, (Europe PMC) | NA | BioGRID |
| BAP1 | Two-hybrid, two hybrid array | physical, physical association | 25640309, (Europe PMC) | 0.37 | BioGRID, IntAct, MINT |
| CAMP | Affinity Capture-Western, Reconstituted Complex | physical | 21685939, (Europe PMC) | NA | BioGRID |
| CBL | Affinity Capture-Western, Biochemical Activity | physical | 18632619, (Europe PMC) | NA | BioGRID |
| CDKN1B | Negative Genetic | genetic | 28319113, (Europe PMC) | NA | BioGRID |
| CDKN2A | Negative Genetic | genetic | 28319113, (Europe PMC) | NA | BioGRID |
| CHEK1 | Negative Genetic | genetic | 28319113, (Europe PMC) | NA | BioGRID |
| CRKL | Co-localization, proximity ligation assay | physical, physical association | 25241761, (Europe PMC) | 0.40 | BioGRID, IntAct |
| CSK | Affinity Capture-Western, Two-hybrid, anti bait coimmunoprecipitation, coimmunoprecipitation, two hybrid | association, physical, physical association | 10026153, (Europe PMC) | 0.57 | BioGRID, IntAct, MINT |
| CYP17A1 | Two-hybrid, two hybrid array | physical, physical association | 25640309, (Europe PMC) | 0.37 | BioGRID, IntAct, MINT |
| DUPD1 | Two-hybrid | physical | 28065597, (Europe PMC) | NA | BioGRID |
| DUSP10 | Two-hybrid | physical | 28065597, (Europe PMC) | NA | BioGRID |
| DUSP14 | Two-hybrid | physical | 28065597, (Europe PMC) | NA | BioGRID |
| DUSP15 | Two-hybrid | physical | 28065597, (Europe PMC) | NA | BioGRID |
| DUSP18 | Two-hybrid | physical | 28065597, (Europe PMC) | NA | BioGRID |
| DUSP19 | Two-hybrid | physical | 28065597, (Europe PMC) | NA | BioGRID |
| DUSP21 | Two-hybrid | physical | 28065597, (Europe PMC) | NA | BioGRID |
| DUSP26 | Two-hybrid | physical | 28065597, (Europe PMC) | NA | BioGRID |
| EEA1 | Affinity Capture-Western | physical | 18632619, (Europe PMC) | NA | BioGRID |
| EGFR | Affinity Capture-Western | physical | 17047074, 17307140, (Europe PMC) | NA | BioGRID |
| EHD1 | Reconstituted Complex | physical | 11423532, (Europe PMC) | NA | BioGRID |
| ERBB2 | Affinity Capture-Western | physical | 17307140, (Europe PMC) | NA | BioGRID |
| ESR1 | Affinity Capture-Western | physical | 14764897, 16113100, 24051437, (Europe PMC) | NA | BioGRID |
| FBXO6 | Affinity Capture-MS | physical | 22268729, (Europe PMC) | NA | BioGRID |
| FDPS | Co-fractionation | physical | 26344197, (Europe PMC) | NA | BioGRID |
| FFAR2 | Two-hybrid, two hybrid array | physical, physical association | 21988832, (Europe PMC) | 0.37 | BioGRID, IntAct |
| GNAI1 | Affinity Capture-Western | physical | 10644671, (Europe PMC) | NA | BioGRID |
| GRB10 | Affinity Capture-Western, Reconstituted Complex, Two-hybrid, pull down, two hybrid | direct interaction, physical, physical association | 12697834, 19165858, 8764099, 8776723, 9506989, (Europe PMC) | 0.53 | BioGRID, IntAct, MINT |
| GRB14 | Two-hybrid, two hybrid, two hybrid array | physical, physical association | 21988832, (Europe PMC) | 0.49 | BioGRID, IntAct |
| HDAC6 | Negative Genetic | genetic | 28319113, (Europe PMC) | NA | BioGRID |
| HNRNPL | Affinity Capture-RNA | physical | 28611215, (Europe PMC) | NA | BioGRID |
| HOXC6 | Two-hybrid, two hybrid array | physical, physical association | 25640309, (Europe PMC) | 0.37 | BioGRID, IntAct, MINT |
| HSP90AA1 | Affinity Capture-Luminescence | physical | 22939624, (Europe PMC) | NA | BioGRID |
| IGF1 | Reconstituted Complex, affinity technology, competition binding, mass spectrometry study of hydrogen/deuterium exchange, surface plasmon resonance, x-ray crystallography | direct interaction, physical, physical association | 1852007, 21645859, 26027733, 8452530, (Europe PMC) | 0.78 | BioGRID, IntAct |
| IGFBP3 | Co-purification | physical | 9389554, (Europe PMC) | NA | BioGRID |
| IL13RA2 | Two-hybrid, two hybrid array | physical, physical association | 25640309, (Europe PMC) | 0.37 | BioGRID, IntAct, MINT |
| ILKAP | Two-hybrid | physical | 28065597, (Europe PMC) | NA | BioGRID |
| IRS1 | Affinity Capture-Western, Two-hybrid, two hybrid | physical, physical association | 10082579, 7541045, 7559507, 8776723, (Europe PMC) | 0.37 | BioGRID, IntAct |
| JAK1 | Reconstituted Complex | physical | 9492017, (Europe PMC) | NA | BioGRID |
| KCNIP3 | Two-hybrid, two hybrid array, two hybrid prey pooling approach, validated two hybrid | physical, physical association | 25416956, (Europe PMC) | 0.70 | BioGRID, IntAct |
| KLK5 | Two-hybrid | physical | 25640309, (Europe PMC) | NA | BioGRID |
| LYPD3 | Two-hybrid, two hybrid array | physical, physical association | 25640309, (Europe PMC) | 0.37 | BioGRID, IntAct, MINT |
| LYZL2 | Affinity Capture-MS | physical | 28514442, (Europe PMC) | NA | BioGRID |
| MDM2 | Affinity Capture-Western, Biochemical Activity, Co-localization, display technology, proximity ligation assay | physical, physical association | 12821780, 18632619, 19165858, 20195357, 25241761, 28092675, (Europe PMC) | 0.59 | BioGRID, IntAct |
| MPZL2 | Affinity Capture-Western | physical | 28065597, (Europe PMC) | NA | BioGRID |
| MTA3 | Two-hybrid, two hybrid array | physical, physical association | 25640309, (Europe PMC) | 0.37 | BioGRID, IntAct, MINT |
| MTOR | Negative Genetic | genetic | 28319113, (Europe PMC) | NA | BioGRID |
| NAT2 | Two-hybrid, two hybrid array | physical, physical association | 25640309, (Europe PMC) | 0.37 | BioGRID, IntAct, MINT |
| NEDD4 | Affinity Capture-Western, Biochemical Activity | physical | 12697834, 18632619, 19165858, (Europe PMC) | NA | BioGRID |
| NTRK1 | Affinity Capture-MS | physical | 25921289, (Europe PMC) | NA | BioGRID |
| PHB2 | Affinity Capture-Western | physical | 24051437, (Europe PMC) | NA | BioGRID |
| PIK3R1 | Co-localization, coimmunoprecipitation, proximity ligation assay, pull down, two hybrid | association, physical, physical association | 25241761, 7589433, 7642582, 8603569, (Europe PMC) | 0.75 | BioGRID, IntAct, MINT |
| PIK3R3 | Affinity Capture-Western, Co-localization, Reconstituted Complex, anti bait coimmunoprecipitation, proximity ligation assay | physical, physical association | 17360667, 25241761, 9415396, (Europe PMC) | 0.59 | BioGRID, IntAct |
| PPM1A | Affinity Capture-Western, Two-hybrid | physical | 28065597, (Europe PMC) | NA | BioGRID |
| PPM1F | Affinity Capture-Western | physical | 28065597, (Europe PMC) | NA | BioGRID |
| PRKDC | Negative Genetic | genetic | 28319113, (Europe PMC) | NA | BioGRID |
| PTK2 | Affinity Capture-Western | physical | 10082579, (Europe PMC) | NA | BioGRID |
| PTPN1 | Affinity Capture-Western, bioluminescence resonance energy transfer, coimmunoprecipitation | physical, physical association | 15976035, 16926280, 8999839, (Europe PMC) | 0.70 | BioGRID, IntAct, MINT |
| PTPN11 | Affinity Capture-Western, Reconstituted Complex, Two-hybrid, beta galactosidase complementation, pull down, two hybrid | association, physical, physical association | 10082579, 28065597, 7642582, 8895367, (Europe PMC) | 0.62 | BioGRID, IntAct, MINT |
| PTPN12 | Two-hybrid | physical | 28065597, (Europe PMC) | NA | BioGRID |
| PTPN6 | Affinity Capture-Western, Two-hybrid | physical | 28065597, (Europe PMC) | NA | BioGRID |
| PTPN7 | Two-hybrid | physical | 28065597, (Europe PMC) | NA | BioGRID |
| PTPRR | Two-hybrid | physical | 28065597, (Europe PMC) | NA | BioGRID |
| PXN | Affinity Capture-Western | physical | 10082579, (Europe PMC) | NA | BioGRID |
| RACK1 | Affinity Capture-Western | physical | 11884618, 20871634, (Europe PMC) | NA | BioGRID |
| RASA1 | Affinity Capture-Western, Reconstituted Complex, pull down | association, physical | 7642582, (Europe PMC) | 0.35 | BioGRID, IntAct, MINT |
| RPL11 | Two-hybrid, two hybrid array | physical, physical association | 21988832, (Europe PMC) | 0.37 | BioGRID, IntAct |
| RUVBL1 | Co-fractionation | physical | 22939629, (Europe PMC) | NA | BioGRID |
| SH2B1 | Two-hybrid | physical | 15767667, (Europe PMC) | NA | BioGRID |
| SHC1 | Affinity Capture-Western, Two-hybrid, far western blotting, two hybrid | physical, physical association | 14764897, 15629149, 16113100, 24051437, 7541045, 7559507, 8776723, (Europe PMC) | 0.37, 0.51 | BioGRID, IntAct |
| SLAMF1 | Affinity Capture-MS | physical | 28514442, (Europe PMC) | NA | BioGRID |
| SLC23A3 | Affinity Capture-Western, pull down | physical, physical association | 20368287, (Europe PMC) | 0.40 | BioGRID, IntAct |
| SNAP29 | Affinity Capture-Western | physical | 11423532, (Europe PMC) | NA | BioGRID |
| SOCS1 | Two-hybrid | physical | 9727029, (Europe PMC) | NA | BioGRID |
| SOCS2 | Affinity Capture-Western, Reconstituted Complex, Two-hybrid | physical | 9727029, (Europe PMC) | NA | BioGRID |
| SOCS3 | Affinity Capture-Western, Reconstituted Complex, Two-hybrid | physical | 11071852, (Europe PMC) | NA | BioGRID |
| SSH1 | Affinity Capture-Western | physical | 28065597, (Europe PMC) | NA | BioGRID |
| STAT3 | Co-localization | physical | 25241761, (Europe PMC) | NA | BioGRID |
| STYX | Two-hybrid | physical | 28065597, (Europe PMC) | NA | BioGRID |
| SYVN1 | Affinity Capture-Western | physical | 26536657, (Europe PMC) | NA | BioGRID |
| THRSP | Two-hybrid, two hybrid array | physical, physical association | 25640309, (Europe PMC) | 0.37 | BioGRID, IntAct, MINT |
| TP53 | Affinity Capture-Western | physical | 19165858, (Europe PMC) | NA | BioGRID |
| TRIM25 | Affinity Capture-RNA, Two-hybrid, two hybrid array | physical, physical association | 25640309, 29117863, (Europe PMC) | 0.37 | BioGRID, IntAct, MINT |
| UBQLN1 | Affinity Capture-MS, Affinity Capture-Western | physical | 28075048, (Europe PMC) | NA | BioGRID |
| UNC5CL | Affinity Capture-MS | physical | 28514442, (Europe PMC) | NA | BioGRID |
| VAV3 | Affinity Capture-Western | physical | 11094073, (Europe PMC) | NA | BioGRID |
| VPS45 | Two-hybrid, two hybrid array | physical, physical association | 25640309, (Europe PMC) | 0.37 | BioGRID, IntAct, MINT |
| YWHAB | Reconstituted Complex, anti bait coimmunoprecipitation, coimmunoprecipitation, pull down, two hybrid | association, direct interaction, physical, physical association | 14651979, 15629149, 17353931, 9581554, (Europe PMC) | 0.83 | BioGRID, IntAct, MINT |
| YWHAE | Reconstituted Complex, Two-hybrid, experimental interaction detection, pull down, two hybrid | association, direct interaction, physical, physical association | 9111084, (Europe PMC) | 0.54 | BioGRID, IntAct, MINT |
| YWHAG | Affinity Capture-MS, anti bait coimmunoprecipitation, coimmunoprecipitation | physical, physical association | 15324660, 17353931, (Europe PMC) | 0.59 | BioGRID, IntAct, MINT |
| Interacting partner | Detection method | Interaction type | PubMed IDs | Interaction Score | Source |
| ARHGEF12 | Affinity Capture-Western, Reconstituted Complex, Two-hybrid, anti bait coimmunoprecipitation, anti tag coimmunoprecipitation, imaging technique, pull down | colocalization, direct interaction, physical, physical association | 11724822, (Europe PMC) | 0.65 | BioGRID, IntAct, MINT |
| ARRB1 | Affinity Capture-Western, anti bait coimmunoprecipitation | physical, physical association | 15878855, 21685939, (Europe PMC) | 0.40 | BioGRID, IntAct |
| BAP1 | Two-hybrid, two hybrid array | physical, physical association | 25640309, (Europe PMC) | 0.37 | BioGRID, IntAct, MINT |
| CAMP | anti bait coimmunoprecipitation, enzyme linked immunosorbent assay | physical association | 21685939, (Europe PMC) | 0.52 | IntAct |
| CDH3 | anti bait coimmunoprecipitation | physical association | 21317933, (Europe PMC) | 0.40 | IntAct |
| CRK | two hybrid | physical association | 15522217, (Europe PMC) | 0.37 | IntAct |
| CRKL | Co-localization, proximity ligation assay | physical, physical association | 25241761, (Europe PMC) | 0.40 | BioGRID, IntAct |
| CSK | Affinity Capture-Western, Two-hybrid, anti bait coimmunoprecipitation, coimmunoprecipitation, two hybrid | association, physical, physical association | 10026153, (Europe PMC) | 0.57 | BioGRID, IntAct, MINT |
| CTNNB1 | anti bait coimmunoprecipitation | association, physical association | 22261717, (Europe PMC) | 0.50 | IntAct, MINT |
| CYP17A1 | Two-hybrid, two hybrid array | physical, physical association | 25640309, (Europe PMC) | 0.37 | BioGRID, IntAct, MINT |
| FFAR2 | Two-hybrid, two hybrid array | physical, physical association | 21988832, (Europe PMC) | 0.37 | BioGRID, IntAct |
| GRB10 | Affinity Capture-Western, Reconstituted Complex, Two-hybrid, pull down, two hybrid | direct interaction, physical, physical association | 12697834, 19165858, 8764099, 8776723, 9506989, (Europe PMC) | 0.53 | BioGRID, IntAct, MINT |
| GRB14 | Two-hybrid, two hybrid, two hybrid array | physical, physical association | 21988832, (Europe PMC) | 0.49 | BioGRID, IntAct |
| HOXC6 | Two-hybrid, two hybrid array | physical, physical association | 25640309, (Europe PMC) | 0.37 | BioGRID, IntAct, MINT |
| HSP90AB1 | luminescence based mammalian interactome mapping | physical association | 22939624, (Europe PMC) | 0.40 | IntAct |
| IGF1 | Reconstituted Complex, affinity technology, competition binding, mass spectrometry study of hydrogen/deuterium exchange, surface plasmon resonance, x-ray crystallography | direct interaction, physical, physical association | 1852007, 21645859, 26027733, 8452530, (Europe PMC) | 0.78 | BioGRID, IntAct |
| IGF1R | anti tag coimmunoprecipitation, comigration in sds page, molecular sieving, protein kinase assay, static light scattering | association, covalent binding, direct interaction, phosphorylation reaction, physical association | 11448933, 17586502, 21645859, (Europe PMC) | 0.80 | IntAct, MINT |
| IL13RA2 | Two-hybrid, two hybrid array | physical, physical association | 25640309, (Europe PMC) | 0.37 | BioGRID, IntAct, MINT |
| IRS1 | Affinity Capture-Western, Two-hybrid, two hybrid | physical, physical association | 10082579, 7541045, 7559507, 8776723, (Europe PMC) | 0.37 | BioGRID, IntAct |
| IRS2 | two hybrid | physical association | 8662806, (Europe PMC) | 0.37 | IntAct, MINT |
| KCNIP3 | Two-hybrid, two hybrid array, two hybrid prey pooling approach, validated two hybrid | physical, physical association | 25416956, (Europe PMC) | 0.70 | BioGRID, IntAct |
| KLK5 | two hybrid array | physical association | 25640309, (Europe PMC) | 0.37 | IntAct, MINT |
| LEF1 | anti bait coimmunoprecipitation, anti tag coimmunoprecipitation | association, physical association | 22261717, (Europe PMC) | 0.58 | IntAct, MINT |
| LYPD3 | Two-hybrid, two hybrid array | physical, physical association | 25640309, (Europe PMC) | 0.37 | BioGRID, IntAct, MINT |
| MDM2 | Affinity Capture-Western, Biochemical Activity, Co-localization, display technology, proximity ligation assay | physical, physical association | 12821780, 18632619, 19165858, 20195357, 25241761, 28092675, (Europe PMC) | 0.59 | BioGRID, IntAct |
| MTA3 | Two-hybrid, two hybrid array | physical, physical association | 25640309, (Europe PMC) | 0.37 | BioGRID, IntAct, MINT |
| NAT2 | Two-hybrid, two hybrid array | physical, physical association | 25640309, (Europe PMC) | 0.37 | BioGRID, IntAct, MINT |
| PIK3R1 | Co-localization, coimmunoprecipitation, proximity ligation assay, pull down, two hybrid | association, physical, physical association | 25241761, 7589433, 7642582, 8603569, (Europe PMC) | 0.75 | BioGRID, IntAct, MINT |
| PIK3R2 | two hybrid | physical association | 7541045, (Europe PMC) | 0.37 | IntAct |
| PIK3R3 | Affinity Capture-Western, Co-localization, Reconstituted Complex, anti bait coimmunoprecipitation, proximity ligation assay | physical, physical association | 17360667, 25241761, 9415396, (Europe PMC) | 0.59 | BioGRID, IntAct |
| PTPN1 | Affinity Capture-Western, bioluminescence resonance energy transfer, coimmunoprecipitation | physical, physical association | 15976035, 16926280, 8999839, (Europe PMC) | 0.70 | BioGRID, IntAct, MINT |
| PTPN11 | Affinity Capture-Western, Reconstituted Complex, Two-hybrid, beta galactosidase complementation, pull down, two hybrid | association, physical, physical association | 10082579, 28065597, 7642582, 8895367, (Europe PMC) | 0.62 | BioGRID, IntAct, MINT |
| RASA1 | Affinity Capture-Western, Reconstituted Complex, pull down | association, physical | 7642582, (Europe PMC) | 0.35 | BioGRID, IntAct, MINT |
| RPL11 | Two-hybrid, two hybrid array | physical, physical association | 21988832, (Europe PMC) | 0.37 | BioGRID, IntAct |
| SHC1 | Affinity Capture-Western, Two-hybrid, far western blotting, two hybrid | physical, physical association | 14764897, 15629149, 16113100, 24051437, 7541045, 7559507, 8776723, (Europe PMC) | 0.37, 0.51 | BioGRID, IntAct |
| SLC23A3 | Affinity Capture-Western, pull down | physical, physical association | 20368287, (Europe PMC) | 0.40 | BioGRID, IntAct |
| STAT3 | proximity ligation assay | physical association | 25241761, (Europe PMC) | 0.40 | IntAct |
| TAGLN | anti bait coimmunoprecipitation | physical association | 22245152, (Europe PMC) | 0.40 | IntAct, MINT |
| THRSP | Two-hybrid, two hybrid array | physical, physical association | 25640309, (Europe PMC) | 0.37 | BioGRID, IntAct, MINT |
| TRIM25 | Affinity Capture-RNA, Two-hybrid, two hybrid array | physical, physical association | 25640309, 29117863, (Europe PMC) | 0.37 | BioGRID, IntAct, MINT |
| VPS45 | Two-hybrid, two hybrid array | physical, physical association | 25640309, (Europe PMC) | 0.37 | BioGRID, IntAct, MINT |
| YWHAB | Reconstituted Complex, anti bait coimmunoprecipitation, coimmunoprecipitation, pull down, two hybrid | association, direct interaction, physical, physical association | 14651979, 15629149, 17353931, 9581554, (Europe PMC) | 0.83 | BioGRID, IntAct, MINT |
| YWHAE | Reconstituted Complex, Two-hybrid, experimental interaction detection, pull down, two hybrid | association, direct interaction, physical, physical association | 9111084, (Europe PMC) | 0.54 | BioGRID, IntAct, MINT |
| YWHAG | Affinity Capture-MS, anti bait coimmunoprecipitation, coimmunoprecipitation | physical, physical association | 15324660, 17353931, (Europe PMC) | 0.59 | BioGRID, IntAct, MINT |
| YWHAZ | coimmunoprecipitation | association | 9581554, (Europe PMC) | 0.35 | IntAct, MINT |
| Interacting partner | Detection method | Interaction type | PubMed IDs | Interaction Score | Source |
| BAP1 | Two-hybrid, two hybrid array | physical, physical association | 25640309, (Europe PMC) | 0.37 | BioGRID, IntAct, MINT |
| CSK | Affinity Capture-Western, Two-hybrid, anti bait coimmunoprecipitation, coimmunoprecipitation, two hybrid | association, physical, physical association | 10026153, (Europe PMC) | 0.57 | BioGRID, IntAct, MINT |
| CTNNB1 | anti bait coimmunoprecipitation | association, physical association | 22261717, (Europe PMC) | 0.50 | IntAct, MINT |
| CYP17A1 | Two-hybrid, two hybrid array | physical, physical association | 25640309, (Europe PMC) | 0.37 | BioGRID, IntAct, MINT |
| GRB10 | Affinity Capture-Western, Reconstituted Complex, Two-hybrid, pull down, two hybrid | direct interaction, physical, physical association | 12697834, 19165858, 8764099, 8776723, 9506989, (Europe PMC) | 0.53 | BioGRID, IntAct, MINT |
| HOXC6 | Two-hybrid, two hybrid array | physical, physical association | 25640309, (Europe PMC) | 0.37 | BioGRID, IntAct, MINT |
| IGF1R | anti tag coimmunoprecipitation, comigration in sds page, molecular sieving, protein kinase assay, static light scattering | association, covalent binding, direct interaction, phosphorylation reaction, physical association | 11448933, 17586502, 21645859, (Europe PMC) | 0.80 | IntAct, MINT |
| IL13RA2 | Two-hybrid, two hybrid array | physical, physical association | 25640309, (Europe PMC) | 0.37 | BioGRID, IntAct, MINT |
| IRS2 | two hybrid | physical association | 8662806, (Europe PMC) | 0.37 | IntAct, MINT |
| KLK5 | two hybrid array | physical association | 25640309, (Europe PMC) | 0.37 | IntAct, MINT |
| LEF1 | anti bait coimmunoprecipitation, anti tag coimmunoprecipitation | association, physical association | 22261717, (Europe PMC) | 0.58 | IntAct, MINT |
| LYPD3 | Two-hybrid, two hybrid array | physical, physical association | 25640309, (Europe PMC) | 0.37 | BioGRID, IntAct, MINT |
| MTA3 | Two-hybrid, two hybrid array | physical, physical association | 25640309, (Europe PMC) | 0.37 | BioGRID, IntAct, MINT |
| NAT2 | Two-hybrid, two hybrid array | physical, physical association | 25640309, (Europe PMC) | 0.37 | BioGRID, IntAct, MINT |
| PIK3R1 | Co-localization, coimmunoprecipitation, proximity ligation assay, pull down, two hybrid | association, physical, physical association | 25241761, 7589433, 7642582, 8603569, (Europe PMC) | 0.75 | BioGRID, IntAct, MINT |
| PTPN1 | Affinity Capture-Western, bioluminescence resonance energy transfer, coimmunoprecipitation | physical, physical association | 15976035, 16926280, 8999839, (Europe PMC) | 0.70 | BioGRID, IntAct, MINT |
| PTPN11 | Affinity Capture-Western, Reconstituted Complex, Two-hybrid, beta galactosidase complementation, pull down, two hybrid | association, physical, physical association | 10082579, 28065597, 7642582, 8895367, (Europe PMC) | 0.62 | BioGRID, IntAct, MINT |
| RASA1 | Affinity Capture-Western, Reconstituted Complex, pull down | association, physical | 7642582, (Europe PMC) | 0.35 | BioGRID, IntAct, MINT |
| TAGLN | anti bait coimmunoprecipitation | physical association | 22245152, (Europe PMC) | 0.40 | IntAct, MINT |
| THRSP | Two-hybrid, two hybrid array | physical, physical association | 25640309, (Europe PMC) | 0.37 | BioGRID, IntAct, MINT |
| TRIM25 | Affinity Capture-RNA, Two-hybrid, two hybrid array | physical, physical association | 25640309, 29117863, (Europe PMC) | 0.37 | BioGRID, IntAct, MINT |
| VPS45 | Two-hybrid, two hybrid array | physical, physical association | 25640309, (Europe PMC) | 0.37 | BioGRID, IntAct, MINT |
| YWHAB | Reconstituted Complex, anti bait coimmunoprecipitation, coimmunoprecipitation, pull down, two hybrid | association, direct interaction, physical, physical association | 14651979, 15629149, 17353931, 9581554, (Europe PMC) | 0.83 | BioGRID, IntAct, MINT |
| YWHAE | Reconstituted Complex, Two-hybrid, experimental interaction detection, pull down, two hybrid | association, direct interaction, physical, physical association | 9111084, (Europe PMC) | 0.54 | BioGRID, IntAct, MINT |
| YWHAG | Affinity Capture-MS, anti bait coimmunoprecipitation, coimmunoprecipitation | physical, physical association | 15324660, 17353931, (Europe PMC) | 0.59 | BioGRID, IntAct, MINT |
| YWHAZ | coimmunoprecipitation | association | 9581554, (Europe PMC) | 0.35 | IntAct, MINT |
| Interacting partner | Detection method | Interaction type | PubMed IDs | Interaction Score | Source |
| APP | Reconstituted Complex | physical | 21832049, (Europe PMC) | NA | BioGRID |
| ARHGEF12 | Affinity Capture-Western, Reconstituted Complex, Two-hybrid, anti bait coimmunoprecipitation, anti tag coimmunoprecipitation, imaging technique, pull down | colocalization, direct interaction, physical, physical association | 11724822, (Europe PMC) | 0.65 | BioGRID, IntAct, MINT |
| ARRB1 | Affinity Capture-Western, anti bait coimmunoprecipitation | physical, physical association | 15878855, 21685939, (Europe PMC) | 0.40 | BioGRID, IntAct |
| ARRB2 | Affinity Capture-Western | physical | 15878855, 19165858, 23188799, (Europe PMC) | NA | BioGRID |
| BAP1 | Two-hybrid, two hybrid array | physical, physical association | 25640309, (Europe PMC) | 0.37 | BioGRID, IntAct, MINT |
| CAMP | Affinity Capture-Western, Reconstituted Complex | physical | 21685939, (Europe PMC) | NA | BioGRID |
| CAMP | anti bait coimmunoprecipitation, enzyme linked immunosorbent assay | physical association | 21685939, (Europe PMC) | 0.52 | IntAct |
| CBL | Affinity Capture-Western, Biochemical Activity | physical | 18632619, (Europe PMC) | NA | BioGRID |
| CDH3 | anti bait coimmunoprecipitation | physical association | 21317933, (Europe PMC) | 0.40 | IntAct |
| CDKN1B | Negative Genetic | genetic | 28319113, (Europe PMC) | NA | BioGRID |
| CDKN2A | Negative Genetic | genetic | 28319113, (Europe PMC) | NA | BioGRID |
| CHEK1 | Negative Genetic | genetic | 28319113, (Europe PMC) | NA | BioGRID |
| CRK | two hybrid | physical association | 15522217, (Europe PMC) | 0.37 | IntAct |
| CRKL | Co-localization, proximity ligation assay | physical, physical association | 25241761, (Europe PMC) | 0.40 | BioGRID, IntAct |
| CSK | Affinity Capture-Western, Two-hybrid, anti bait coimmunoprecipitation, coimmunoprecipitation, two hybrid | association, physical, physical association | 10026153, (Europe PMC) | 0.57 | BioGRID, IntAct, MINT |
| CTNNB1 | anti bait coimmunoprecipitation | association, physical association | 22261717, (Europe PMC) | 0.50 | IntAct, MINT |
| CYP17A1 | Two-hybrid, two hybrid array | physical, physical association | 25640309, (Europe PMC) | 0.37 | BioGRID, IntAct, MINT |
| DUPD1 | Two-hybrid | physical | 28065597, (Europe PMC) | NA | BioGRID |
| DUSP10 | Two-hybrid | physical | 28065597, (Europe PMC) | NA | BioGRID |
| DUSP14 | Two-hybrid | physical | 28065597, (Europe PMC) | NA | BioGRID |
| DUSP15 | Two-hybrid | physical | 28065597, (Europe PMC) | NA | BioGRID |
| DUSP18 | Two-hybrid | physical | 28065597, (Europe PMC) | NA | BioGRID |
| DUSP19 | Two-hybrid | physical | 28065597, (Europe PMC) | NA | BioGRID |
| DUSP21 | Two-hybrid | physical | 28065597, (Europe PMC) | NA | BioGRID |
| DUSP26 | Two-hybrid | physical | 28065597, (Europe PMC) | NA | BioGRID |
| EEA1 | Affinity Capture-Western | physical | 18632619, (Europe PMC) | NA | BioGRID |
| EGFR | Affinity Capture-Western | physical | 17047074, 17307140, (Europe PMC) | NA | BioGRID |
| EHD1 | Reconstituted Complex | physical | 11423532, (Europe PMC) | NA | BioGRID |
| ERBB2 | Affinity Capture-Western | physical | 17307140, (Europe PMC) | NA | BioGRID |
| ESR1 | Affinity Capture-Western | physical | 14764897, 16113100, 24051437, (Europe PMC) | NA | BioGRID |
| FBXO6 | Affinity Capture-MS | physical | 22268729, (Europe PMC) | NA | BioGRID |
| FDPS | Co-fractionation | physical | 26344197, (Europe PMC) | NA | BioGRID |
| FFAR2 | Two-hybrid, two hybrid array | physical, physical association | 21988832, (Europe PMC) | 0.37 | BioGRID, IntAct |
| GNAI1 | Affinity Capture-Western | physical | 10644671, (Europe PMC) | NA | BioGRID |
| GRB10 | Affinity Capture-Western, Reconstituted Complex, Two-hybrid, pull down, two hybrid | direct interaction, physical, physical association | 12697834, 19165858, 8764099, 8776723, 9506989, (Europe PMC) | 0.53 | BioGRID, IntAct, MINT |
| GRB14 | Two-hybrid, two hybrid, two hybrid array | physical, physical association | 21988832, (Europe PMC) | 0.49 | BioGRID, IntAct |
| HDAC6 | Negative Genetic | genetic | 28319113, (Europe PMC) | NA | BioGRID |
| HNRNPL | Affinity Capture-RNA | physical | 28611215, (Europe PMC) | NA | BioGRID |
| HOXC6 | Two-hybrid, two hybrid array | physical, physical association | 25640309, (Europe PMC) | 0.37 | BioGRID, IntAct, MINT |
| HSP90AA1 | Affinity Capture-Luminescence | physical | 22939624, (Europe PMC) | NA | BioGRID |
| HSP90AB1 | luminescence based mammalian interactome mapping | physical association | 22939624, (Europe PMC) | 0.40 | IntAct |
| IGF1 | Reconstituted Complex, affinity technology, competition binding, mass spectrometry study of hydrogen/deuterium exchange, surface plasmon resonance, x-ray crystallography | direct interaction, physical, physical association | 1852007, 21645859, 26027733, 8452530, (Europe PMC) | 0.78 | BioGRID, IntAct |
| IGF1R | anti tag coimmunoprecipitation, comigration in sds page, molecular sieving, protein kinase assay, static light scattering | association, covalent binding, direct interaction, phosphorylation reaction, physical association | 11448933, 17586502, 21645859, (Europe PMC) | 0.80 | IntAct, MINT |
| IGFBP3 | Co-purification | physical | 9389554, (Europe PMC) | NA | BioGRID |
| IL13RA2 | Two-hybrid, two hybrid array | physical, physical association | 25640309, (Europe PMC) | 0.37 | BioGRID, IntAct, MINT |
| ILKAP | Two-hybrid | physical | 28065597, (Europe PMC) | NA | BioGRID |
| IRS1 | Affinity Capture-Western, Two-hybrid, two hybrid | physical, physical association | 10082579, 7541045, 7559507, 8776723, (Europe PMC) | 0.37 | BioGRID, IntAct |
| IRS2 | two hybrid | physical association | 8662806, (Europe PMC) | 0.37 | IntAct, MINT |
| JAK1 | Reconstituted Complex | physical | 9492017, (Europe PMC) | NA | BioGRID |
| KCNIP3 | Two-hybrid, two hybrid array, two hybrid prey pooling approach, validated two hybrid | physical, physical association | 25416956, (Europe PMC) | 0.70 | BioGRID, IntAct |
| KLK5 | Two-hybrid | physical | 25640309, (Europe PMC) | NA | BioGRID |
| KLK5 | two hybrid array | physical association | 25640309, (Europe PMC) | 0.37 | IntAct, MINT |
| LEF1 | anti bait coimmunoprecipitation, anti tag coimmunoprecipitation | association, physical association | 22261717, (Europe PMC) | 0.58 | IntAct, MINT |
| LYPD3 | Two-hybrid, two hybrid array | physical, physical association | 25640309, (Europe PMC) | 0.37 | BioGRID, IntAct, MINT |
| LYZL2 | Affinity Capture-MS | physical | 28514442, (Europe PMC) | NA | BioGRID |
| MDM2 | Affinity Capture-Western, Biochemical Activity, Co-localization, display technology, proximity ligation assay | physical, physical association | 12821780, 18632619, 19165858, 20195357, 25241761, 28092675, (Europe PMC) | 0.59 | BioGRID, IntAct |
| MPZL2 | Affinity Capture-Western | physical | 28065597, (Europe PMC) | NA | BioGRID |
| MTA3 | Two-hybrid, two hybrid array | physical, physical association | 25640309, (Europe PMC) | 0.37 | BioGRID, IntAct, MINT |
| MTOR | Negative Genetic | genetic | 28319113, (Europe PMC) | NA | BioGRID |
| NAT2 | Two-hybrid, two hybrid array | physical, physical association | 25640309, (Europe PMC) | 0.37 | BioGRID, IntAct, MINT |
| NEDD4 | Affinity Capture-Western, Biochemical Activity | physical | 12697834, 18632619, 19165858, (Europe PMC) | NA | BioGRID |
| NTRK1 | Affinity Capture-MS | physical | 25921289, (Europe PMC) | NA | BioGRID |
| PHB2 | Affinity Capture-Western | physical | 24051437, (Europe PMC) | NA | BioGRID |
| PIK3R1 | Co-localization, coimmunoprecipitation, proximity ligation assay, pull down, two hybrid | association, physical, physical association | 25241761, 7589433, 7642582, 8603569, (Europe PMC) | 0.75 | BioGRID, IntAct, MINT |
| PIK3R2 | two hybrid | physical association | 7541045, (Europe PMC) | 0.37 | IntAct |
| PIK3R3 | Affinity Capture-Western, Co-localization, Reconstituted Complex, anti bait coimmunoprecipitation, proximity ligation assay | physical, physical association | 17360667, 25241761, 9415396, (Europe PMC) | 0.59 | BioGRID, IntAct |
| PPM1A | Affinity Capture-Western, Two-hybrid | physical | 28065597, (Europe PMC) | NA | BioGRID |
| PPM1F | Affinity Capture-Western | physical | 28065597, (Europe PMC) | NA | BioGRID |
| PRKDC | Negative Genetic | genetic | 28319113, (Europe PMC) | NA | BioGRID |
| PTK2 | Affinity Capture-Western | physical | 10082579, (Europe PMC) | NA | BioGRID |
| PTPN1 | Affinity Capture-Western, bioluminescence resonance energy transfer, coimmunoprecipitation | physical, physical association | 15976035, 16926280, 8999839, (Europe PMC) | 0.70 | BioGRID, IntAct, MINT |
| PTPN11 | Affinity Capture-Western, Reconstituted Complex, Two-hybrid, beta galactosidase complementation, pull down, two hybrid | association, physical, physical association | 10082579, 28065597, 7642582, 8895367, (Europe PMC) | 0.62 | BioGRID, IntAct, MINT |
| PTPN12 | Two-hybrid | physical | 28065597, (Europe PMC) | NA | BioGRID |
| PTPN6 | Affinity Capture-Western, Two-hybrid | physical | 28065597, (Europe PMC) | NA | BioGRID |
| PTPN7 | Two-hybrid | physical | 28065597, (Europe PMC) | NA | BioGRID |
| PTPRR | Two-hybrid | physical | 28065597, (Europe PMC) | NA | BioGRID |
| PXN | Affinity Capture-Western | physical | 10082579, (Europe PMC) | NA | BioGRID |
| RACK1 | Affinity Capture-Western | physical | 11884618, 20871634, (Europe PMC) | NA | BioGRID |
| RASA1 | Affinity Capture-Western, Reconstituted Complex, pull down | association, physical | 7642582, (Europe PMC) | 0.35 | BioGRID, IntAct, MINT |
| RPL11 | Two-hybrid, two hybrid array | physical, physical association | 21988832, (Europe PMC) | 0.37 | BioGRID, IntAct |
| RUVBL1 | Co-fractionation | physical | 22939629, (Europe PMC) | NA | BioGRID |
| SH2B1 | Two-hybrid | physical | 15767667, (Europe PMC) | NA | BioGRID |
| SHC1 | Affinity Capture-Western, Two-hybrid, far western blotting, two hybrid | physical, physical association | 14764897, 15629149, 16113100, 24051437, 7541045, 7559507, 8776723, (Europe PMC) | 0.37, 0.51 | BioGRID, IntAct |
| SLAMF1 | Affinity Capture-MS | physical | 28514442, (Europe PMC) | NA | BioGRID |
| SLC23A3 | Affinity Capture-Western, pull down | physical, physical association | 20368287, (Europe PMC) | 0.40 | BioGRID, IntAct |
| SNAP29 | Affinity Capture-Western | physical | 11423532, (Europe PMC) | NA | BioGRID |
| SOCS1 | Two-hybrid | physical | 9727029, (Europe PMC) | NA | BioGRID |
| SOCS2 | Affinity Capture-Western, Reconstituted Complex, Two-hybrid | physical | 9727029, (Europe PMC) | NA | BioGRID |
| SOCS3 | Affinity Capture-Western, Reconstituted Complex, Two-hybrid | physical | 11071852, (Europe PMC) | NA | BioGRID |
| SSH1 | Affinity Capture-Western | physical | 28065597, (Europe PMC) | NA | BioGRID |
| STAT3 | Co-localization | physical | 25241761, (Europe PMC) | NA | BioGRID |
| STAT3 | proximity ligation assay | physical association | 25241761, (Europe PMC) | 0.40 | IntAct |
| STYX | Two-hybrid | physical | 28065597, (Europe PMC) | NA | BioGRID |
| SYVN1 | Affinity Capture-Western | physical | 26536657, (Europe PMC) | NA | BioGRID |
| TAGLN | anti bait coimmunoprecipitation | physical association | 22245152, (Europe PMC) | 0.40 | IntAct, MINT |
| THRSP | Two-hybrid, two hybrid array | physical, physical association | 25640309, (Europe PMC) | 0.37 | BioGRID, IntAct, MINT |
| TP53 | Affinity Capture-Western | physical | 19165858, (Europe PMC) | NA | BioGRID |
| TRIM25 | Affinity Capture-RNA, Two-hybrid, two hybrid array | physical, physical association | 25640309, 29117863, (Europe PMC) | 0.37 | BioGRID, IntAct, MINT |
| UBQLN1 | Affinity Capture-MS, Affinity Capture-Western | physical | 28075048, (Europe PMC) | NA | BioGRID |
| UNC5CL | Affinity Capture-MS | physical | 28514442, (Europe PMC) | NA | BioGRID |
| VAV3 | Affinity Capture-Western | physical | 11094073, (Europe PMC) | NA | BioGRID |
| VPS45 | Two-hybrid, two hybrid array | physical, physical association | 25640309, (Europe PMC) | 0.37 | BioGRID, IntAct, MINT |
| YWHAB | Reconstituted Complex, anti bait coimmunoprecipitation, coimmunoprecipitation, pull down, two hybrid | association, direct interaction, physical, physical association | 14651979, 15629149, 17353931, 9581554, (Europe PMC) | 0.83 | BioGRID, IntAct, MINT |
| YWHAE | Reconstituted Complex, Two-hybrid, experimental interaction detection, pull down, two hybrid | association, direct interaction, physical, physical association | 9111084, (Europe PMC) | 0.54 | BioGRID, IntAct, MINT |
| YWHAG | Affinity Capture-MS, anti bait coimmunoprecipitation, coimmunoprecipitation | physical, physical association | 15324660, 17353931, (Europe PMC) | 0.59 | BioGRID, IntAct, MINT |
| YWHAZ | coimmunoprecipitation | association | 9581554, (Europe PMC) | 0.35 | IntAct, MINT |