DEPOD - human DEPhOsphorylation Database

Basic Information
Phosphatases
Pathway
Interacting Proteins
Phosphorylating Kinases

Gene Name	BCL2 (QuickGO)	Interactive visualization of BCL2 structures (A quick tutorial to explore the interctive visulaization) Representative structure: 1YSW
Synonyms	BCL2
Protein Name	BCL2
Alternative Name(s)	Apoptosis regulator Bcl-2;
Protein Family	Belongs to the Bcl-2 family
EntrezGene ID	596 (Comparitive Toxicogenomics)
UniProt AC (Human)	P10415 (protein sequence)
Enzyme Class	N/A
Molecular Weight	26266 Dalton
Protein Length	239 amino acids (AA)
Genome Browsers	NCBI \| ENSG00000171791 (Ensembl) \| UCSC
Crosslinking annotations	Query our ID-mapping table
Orthologues	Quest For Orthologues (QFO) \| GeneTree \| eggNOG - KOG4728 \| eggNOG - ENOG41123S0
Phosphorylation Network	Visualize

Domain organization, Expression, Diseases

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Localization, Function, Catalytic activity and Sequence

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Motif information from Eukaryotic Linear Motif atlas (ELM)

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

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GO:0000209	P:protein polyubiquitination
GO:0001503	P:ossification
GO:0001541	P:ovarian follicle development
GO:0001656	P:metanephros development
GO:0001658	P:branching involved in ureteric bud morphogenesis
GO:0001662	P:behavioral fear response
GO:0001782	P:B cell homeostasis
GO:0001836	P:release of cytochrome c from mitochondria
GO:0001952	P:regulation of cell-matrix adhesion
GO:0002020	F:protease binding
GO:0002320	P:lymphoid progenitor cell differentiation
GO:0002326	P:B cell lineage commitment
GO:0002931	P:response to ischemia
GO:0003014	P:renal system process
GO:0005634	C:nucleus
GO:0005654	C:nucleoplasm
GO:0005737	C:cytoplasm
GO:0005739	C:mitochondrion
GO:0005741	C:mitochondrial outer membrane
GO:0005783	C:endoplasmic reticulum
GO:0005789	C:endoplasmic reticulum membrane
GO:0005829	C:cytosol
GO:0006470	P:protein dephosphorylation
GO:0006582	P:melanin metabolic process
GO:0006808	P:regulation of nitrogen utilization
GO:0006915	P:apoptotic process
GO:0006959	P:humoral immune response
GO:0006974	P:cellular response to DNA damage stimulus
GO:0007015	P:actin filament organization
GO:0007409	P:axonogenesis
GO:0007565	P:female pregnancy
GO:0007569	P:cell aging
GO:0008134	F:transcription factor binding
GO:0008584	P:male gonad development
GO:0008625	P:extrinsic apoptotic signaling pathway via death domain receptors
GO:0008630	P:intrinsic apoptotic signaling pathway in response to DNA damage
GO:0008631	P:intrinsic apoptotic signaling pathway in response to oxidative stress
GO:0009314	P:response to radiation
GO:0009636	P:response to toxic substance
GO:0009791	P:post-embryonic development
GO:0010039	P:response to iron ion
GO:0010224	P:response to UV-B
GO:0010332	P:response to gamma radiation
GO:0010468	P:regulation of gene expression
GO:0010507	P:negative regulation of autophagy
GO:0010523	P:negative regulation of calcium ion transport into cytosol
GO:0010559	P:regulation of glycoprotein biosynthetic process
GO:0014031	P:mesenchymal cell development
GO:0014042	P:positive regulation of neuron maturation
GO:0014911	P:positive regulation of smooth muscle cell migration
GO:0015267	F:channel activity
GO:0016020	C:membrane
GO:0016248	F:channel inhibitor activity
GO:0018105	P:peptidyl-serine phosphorylation
GO:0018107	P:peptidyl-threonine phosphorylation
GO:0019221	P:cytokine-mediated signaling pathway
GO:0021747	P:cochlear nucleus development
GO:0022612	P:gland morphogenesis
GO:0022898	P:regulation of transmembrane transporter activity
GO:0030279	P:negative regulation of ossification
GO:0030307	P:positive regulation of cell growth
GO:0030308	P:negative regulation of cell growth
GO:0030318	P:melanocyte differentiation
GO:0030336	P:negative regulation of cell migration
GO:0030890	P:positive regulation of B cell proliferation
GO:0031069	P:hair follicle morphogenesis
GO:0031103	P:axon regeneration
GO:0031625	F:ubiquitin protein ligase binding
GO:0031647	P:regulation of protein stability
GO:0031965	C:nuclear membrane
GO:0032469	P:endoplasmic reticulum calcium ion homeostasis
GO:0032835	P:glomerulus development
GO:0032848	P:negative regulation of cellular pH reduction
GO:0032991	C:protein-containing complex
GO:0033033	P:negative regulation of myeloid cell apoptotic process
GO:0033077	P:T cell differentiation in thymus
GO:0033138	P:positive regulation of peptidyl-serine phosphorylation
GO:0033689	P:negative regulation of osteoblast proliferation
GO:0034097	P:response to cytokine
GO:0035094	P:response to nicotine
GO:0035265	P:organ growth
GO:0040018	P:positive regulation of multicellular organism growth
GO:0042100	P:B cell proliferation
GO:0042149	P:cellular response to glucose starvation
GO:0042493	P:response to drug
GO:0042542	P:response to hydrogen peroxide
GO:0042802	F:identical protein binding
GO:0042803	F:protein homodimerization activity
GO:0043029	P:T cell homeostasis
GO:0043066	P:negative regulation of apoptotic process
GO:0043085	P:positive regulation of catalytic activity
GO:0043209	C:myelin sheath
GO:0043375	P:CD8-positive
GO:0043496	alpha-beta T cell lineage commitment
GO:0043497	P:regulation of protein homodimerization activity
GO:0043524	P:regulation of protein heterodimerization activity
GO:0043565	P:negative regulation of neuron apoptotic process
GO:0043583	F:sequence-specific DNA binding
GO:0045069	P:ear development
GO:0045636	P:regulation of viral genome replication
GO:0046671	P:positive regulation of melanocyte differentiation
GO:0046902	P:negative regulation of retinal cell programmed cell death
GO:0046930	P:regulation of mitochondrial membrane permeability
GO:0046982	C:pore complex
GO:0048041	F:protein heterodimerization activity
GO:0048536	P:focal adhesion assembly
GO:0048538	P:spleen development
GO:0048546	P:thymus development
GO:0048599	P:digestive tract morphogenesis
GO:0048743	P:oocyte development
GO:0048753	P:positive regulation of skeletal muscle fiber development
GO:0048873	P:pigment granule organization
GO:0050853	P:homeostasis of number of cells within a tissue
GO:0051384	P:B cell receptor signaling pathway
GO:0051402	P:response to glucocorticoid
GO:0051434	P:neuron apoptotic process
GO:0051607	F:BH3 domain binding
GO:0051721	P:defense response to virus
GO:0051881	F:protein phosphatase 2A binding
GO:0051902	P:regulation of mitochondrial membrane potential
GO:0051924	P:negative regulation of mitochondrial depolarization
GO:0070059	P:regulation of calcium ion transport
GO:0071456	P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress
GO:0072593	P:cellular response to hypoxia
GO:0097192	P:reactive oxygen species metabolic process
GO:0098609	P:extrinsic apoptotic signaling pathway in absence of ligand
GO:1900740	P:cell-cell adhesion
GO:1902166	P:positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway
GO:2000134	P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator
GO:2000378	P:negative regulation of G1/S transition of mitotic cell cycle
GO:2000811	P:negative regulation of reactive oxygen species metabolic process
GO:2001234	P:negative regulation of anoikis
GO:2001240	P:negative regulation of apoptotic signaling pathway
GO:2001243	P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand
GO:2001244	P:negative regulation of intrinsic apoptotic signaling pathway

KEGG Pathway
Reactome Pathway

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.
hsa01524	Platinum drug resistance	Platinum-based drugs cisplatin, carboplatin and oxaliplatin are widely used in the therapy of solid malignancies, including testicular, ovarian, head and neck, colorectal, bladder and lung cancers. The mechanism of action of Platinum-based drugs involves covalent binding to purine DNA bases, which primarily leads to cellular apoptosis. Their clinical success is, however, limited due to severe side effects and intrinsic or acquired resistance to the treatment. Platinum resistance could arise from decreased drug influx, increased drug efflux, intracellular detoxification by glutathione, etc., decreased binding (e.g., due to high intracellular pH), increased DNA repair, decreased mismatch repair, defective apoptosis, and altered oncogene expression.
hsa04064	NF-kappa B signaling pathway	Nuclear factor-kappa B (NF-kappa B) is the generic name of a family of transcription factors that function as dimers and regulate genes involved in immunity, inflammation and cell survival. There are several pathways leading to NF-kappa B-activation. The canonical pathway is induced by tumour necrosis factor-alpha (TNF-alpha), interleukin-1 (IL-1) or byproducts of bacterial and viral infections. This pathway relies on IKK- mediated IkappaB-alpha phosphorylation on Ser32 and 36, leading to its degradation, which allows the p50/p65 NF-kappa B dimer to enter the nucleus and activate gene transcription. Atypical pathways are IKK-independent and rely on phosphorylation of IkappaB-alpha on Tyr42 or on Ser residues in IkappaB-alpha PEST domain. The non-canonical pathway is triggered by particular members of the TNFR superfamily, such as lymphotoxin-beta (LT-beta) or BAFF. It involves NIK and IKK-alpha-mediated p100 phosphorylation and processing to p52, resulting in nuclear translocation of p52/RelB heterodimers.
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.
hsa04071	Sphingolipid signaling pathway	Sphingomyelin (SM) and its metabolic products are now known to have second messenger functions in a variety of cellular signaling pathways. Particularly, the sphingolipid metabolites, ceramide (Cer) and sphingosine-1-phosphate (S1P), have emerged as a new class of potent bioactive molecules. Ceramide can be generated de novo or by hydrolysis of membrane sphingomyelin by sphingomyelinase (SMase). Ceramide is subsequently metabolized by ceramidase to generate sphingosine (Sph) which in turn produces S1P through phosphorylation by sphingosine kinases 1 and 2 (SphK1, 2). Both ceramide and S1P regulate cellular responses to stress, with generally opposing effects. S1P functions as a growth and survival factor, acting as a ligand for a family of G protein-coupled receptors, whereas ceramide activates intrinsic and extrinsic apoptotic pathways through receptor-independent mechanisms.
hsa04115	p53 signaling pathway	p53 activation is induced by a number of stress signals, including DNA damage, oxidative stress and activated oncogenes. The p53 protein is employed as a transcriptional activator of p53-regulated genes. This results in three major outputs; cell cycle arrest, cellular senescence or apoptosis. Other p53-regulated gene functions communicate with adjacent cells, repair the damaged DNA or set up positive and negative feedback loops that enhance or attenuate the functions of the p53 protein and integrate these stress responses with other signal transduction pathways.
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.
hsa04141	Protein processing in endoplasmic reticulum	The endoplasmic reticulum (ER) is a subcellular organelle where proteins are folded with the help of lumenal chaperones. Newly synthesized peptides enter the ER via the sec61 pore and are glycosylated. Correctly folded proteins are packaged into transport vesicles that shuttle them to the Golgi complex. Misfolded proteins are retained within the ER lumen in complex with molecular chaperones. Proteins that are terminally misfolded bind to BiP and are directed toward degradation through the proteasome in a process called ER-associated degradation (ERAD). Accumulation of misfolded proteins in the ER causes ER stress and activates a signaling pathway called the unfolded protein response (UPR). In certain severe situations, however, the protective mechanisms activated by the UPR are not sufficient to restore normal ER function and cells die by apoptosis.
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.
hsa04210	Apoptosis	Apoptosis is a genetically programmed process for the elimination of damaged or redundant cells by activation of caspases (aspartate-specific cysteine proteases). The onset of apoptosis is controlled by numerous interrelating processes. The 'extrinsic' pathway involves stimulation of members of the tumor necrosis factor (TNF) receptor subfamily, such as TNFRI, CD95/Fas or TRAILR (death receptors), located at the cell surface, by their specific ligands, such as TNF-alpha, FasL or TRAIL, respectively. The 'intrinsic' pathway is activated mainly by non-receptor stimuli, such as DNA damage, ER stress, metabolic stress, UV radiation or growth-factor deprivation. The central event in the 'intrinsic' pathway is the mitochondrial outer membrane permeabilization (MOMP), which leads to the release of cytochrome c. These two pathways converge at the level of effector caspases, such as caspase-3 and caspase-7. The third major pathway is initiated by the constituents of cytotoxic granules (e.g. Perforin and Granzyme B) that are released by CTLs (cytotoxic T-cells) and NK (natural killer) cells. Granzyme B, similarly to the caspases, cleaves its substrates after aspartic acid residues, suggesting that this protease has the ability to activate members of the caspase family directly. It is the balance between the pro-apoptotic and anti-apoptotic signals that eventually determines whether cells will undergo apoptosis, survive or proliferate. TNF family of ligands activates anti-apoptotic or cell-survival signals as well as apoptotic signals. NGF and Interleukin-3 promotes the survival, proliferation and differentiation of neurons or hematopoietic cells, respectively. Withdrawal of these growth factors leads to cell death, as described above.
hsa04215	Apoptosis - multiple species	Apoptosis is an evolutionarily conserved process used by multicellular organisms to developmentally regulate cell number or to eliminate cells that are potentially detrimental to the organism. The major players are caspases, caspase inhibitors, members of the Bcl-2 family of pro- and anti-apoptotic proteins and adaptors of the Ced-4/APAF-1 type. Mammals, by comparison with Caenorhabditis and Drosophila, exhibit highly complex extrinsic and intrinsic pathways for apoptosis induction. However, recent analyses of whole genome sequences from cnidarians (e.g. Hydra) suggest that the caspase and Bcl-2 families were already highly complex in cnidarians and that Caenorhabditis and Drosophila lost many of the genes involved in apoptosis.
hsa04217	Necroptosis	Necroptosis is a programmed form of necrosis. It can be initiated by different stimuli, such as tumor necrosis factor (TNF), TNF-related apoptosis-inducing ligand (TRAIL), Fas ligand (FasL), interferon (IFN), LPS, viral DNA or RNA, DNA-damage agent and requires the kinase activity of receptor-interacting protein 1 (RIPK1) and RIPK3. Its execution involves ROS generation, calcium overload, the opening of the mitochondrial permeability transition pore, mitochondrial fission, inflammatory response and chromatinolysis. Necroptosis participates in many pathogenesis of diseases, including neurological diseases, retinal disorders, acute kidney injury, inflammatory diseases and microbial infections.
hsa04261	Adrenergic signaling in cardiomyocytes	Cardiac myocytes express at least six subtypes of adrenergic receptor (AR) which include three subtypes of beta-AR (beta-1, beta-2, beta-3) and three subtypes of the alpha-1-AR (alpha-1A, alpha-1B, and alpha-1C). In the human heart the beta-1-AR is the pre- dominate receptor. Acute sympathetic stimulation of cardiac beta-1-ARs induces positive inotropic and chronotropic effects, the most effective mechanism to acutely increase output of the heart, by coupling to Gs, formation of cAMP by adenylyl cyclase (AC), and PKA- dependent phosphorylation of various target proteins (e.g., ryanodine receptor [RyR]; phospholamban [PLB], troponin I [TnI], and the L-type Ca2+ channel [LTCC]). Chronic beta-1-AR stimulation is detrimental and induces cardiomyocyte hypertrophy and apoptosis. beta-2-AR coupled to Gs exerts a proapoptotic action as well as beta-1-AR, while beta-2-AR coupled to Gi exerts an antiapoptotic action.
hsa04340	Hedgehog signaling pathway	The Hedgehog (Hh) signaling pathway has numerous roles in the control of cell proliferation, tissue patterning, stem cell maintenance and development. The primary cilium is an important center for transduction of the Hedgehog signal in vertebrates. In Hh's absence, the Ptch receptor localizes to the cilium, where it inhibits Smo activation. Gli proteins are phosphorylated by PKA, CKI and GSK3B and partially degraded into truncated Gli repressor form (GliR) that suppresses Hh target gene transcription in the nucleus. In Hh's presence, Ptch disappears from the cilium, and activated Smo contributes to the translocation of the protein complex Gli, Sufu, Kif7 to ciliary tip, where Gli dissociates from the negative regulator Sufu. The production of Gli activator form (GliA) occurs and the increased nuclear accumulation of GliA results in activation transcription of Hh target genes.
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.
hsa04621	NOD-like receptor signaling pathway	Specific families of pattern recognition receptors are responsible for detecting various pathogens and generating innate immune responses. The intracellular NOD-like receptor (NLR) family contains more than 20 members in mammals and plays a pivotal role in the recognition of intracellular ligands. NOD1 and NOD2, two prototypic NLRs, sense the cytosolic presence of the bacterial peptidoglycan fragments that escaped from endosomal compartments, driving the activation of NF-{kappa}B and MAPK, cytokine production and apoptosis. On the other hand, a different set of NLRs induces caspase-1 activation through the assembly of multiprotein complexes called inflammasomes. The activated of caspase-1 regulates maturation of the pro-inflammatory cytokines IL-1B, IL-18 and drives pyroptosis.
hsa04630	Jak-STAT signaling pathway	The Janus kinase/signal transducers and activators of transcription (JAK/STAT) pathway is one of a handful of pleiotropic cascades used to transduce a multitude of signals for development and homeostasis in animals, from humans to flies. In mammals, the JAK/STAT pathway is the principal signaling mechanism for a wide array of cytokines and growth factors. Following the binding of cytokines to their cognate receptor, STATs are activated by members of the JAK family of tyrosine kinases. Once activated, they dimerize and translocate to the nucleus and modulate the expression of target genes. In addition to the activation of STATs, JAKs mediate the recruitment of other molecules such as the MAP kinases, PI3 kinase etc. These molecules process downstream signals via the Ras-Raf-MAP kinase and PI3 kinase pathways which results in the activation of additional transcription factors.
hsa04722	Neurotrophin signaling pathway	Neurotrophins are a family of trophic factors involved in differentiation and survival of neural cells. The neurotrophin family consists of nerve growth factor (NGF), brain derived neurotrophic factor (BDNF), neurotrophin 3 (NT-3), and neurotrophin 4 (NT-4). Neurotrophins exert their functions through engagement of Trk tyrosine kinase receptors or p75 neurotrophin receptor (p75NTR). Neurotrophin/Trk signaling is regulated by connecting a variety of intracellular signaling cascades, which include MAPK pathway, PI-3 kinase pathway, and PLC pathway, transmitting positive signals like enhanced survival and growth. On the other hand, p75NTR transmits both positive and nagative signals. These signals play an important role for neural development and additional higher-order activities such as learning and memory.
hsa04725	Cholinergic synapse	Acetylcholine (ACh) is a neurotransmitter widely distributed in the central (and also peripheral, autonomic and enteric) nervous system (CNS). In the CNS, ACh facilitates many functions, such as learning, memory, attention and motor control. When released in the synaptic cleft, ACh binds to two distinct types of receptors: Ionotropic nicotinic acetylcholine receptors (nAChR) and metabotropic muscarinic acetylcholine receptors (mAChRs). The activation of nAChR by ACh leads to the rapid influx of Na+ and Ca2+ and subsequent cellular depolarization. Activation of mAChRs is relatively slow (milliseconds to seconds) and, depending on the subtypes present (M1-M5), they directly alter cellular homeostasis of phospholipase C, inositol trisphosphate, cAMP, and free calcium. In the cleft, ACh may also be hydrolyzed by acetylcholinesterase (AChE) into choline and acetate. The choline derived from ACh hydrolysis is recovered by a presynaptic high-affinity choline transporter (CHT).
hsa04915	Estrogen signaling pathway	Estrogens are steroid hormones that regulate a plethora of physiological processes in mammals, including reproduction, cardiovascular protection, bone integrity, cellular homeostasis, and behavior. Estrogen mediates its cellular actions through two signaling pathways classified as nuclear-initiated steroid signalingand membrane-initiated steroid signaling. In the nuclearpathway, estrogen binds either ERalpha or ERbeta, which in turn translocates to the nucleus, binds DNA at ERE elements and activates the expression of ERE-dependent genes. In membranepathway, Estrogen can exert its actions through a subpopulation of ER at the plasma membrane (mER) or novel G-protein coupled E2 receptors (GPER). Upon activation of these receptors various signaling pathways (i.e. Ca2+, cAMP, protein kinase cascades) are rapidly activated and ultimately influence downstream transcription factors.
hsa04928	Parathyroid hormone synthesis, secretion and action	Parathyroid hormone (PTH) is a key regulator of calcium and phosphorus homeostasis. The principal regulators of PTH secretion are extracellular ionized calcium (Ca2+) and 1,25-dihydroxyvitamin D (1,25(OH)2D3). Under conditions of dietary Ca restriction, a decrement in serum Ca concentration induces release of PTH from the parathyroid gland. PTH acts on bone and kidney to stimulate bone turnover, increase the circulating levels of 1,25(OH)2D3 and calcium and inhibit the reabsorption of phosphate from the glomerular filtrate. This hormone exerts its actions via binding to the PTH/PTH-related peptide receptor (PTH1R). PTH1R primarily activates two sub-types of heterotrimeric Gproteins: Gs and Gq , which in turn regulate the activity of adenylyl cyclases and phospholipase C (PLC) that control the flow of cAMP/PKA and IP/PKC signaling cascades, respectively.
hsa04933	AGE-RAGE signaling pathway in diabetic complications	Advanced glycation end products (AGEs) are a complex group of compounds produced through the non-enzymatic glycation and oxidation of proteins, lipids and nucleic acids, primarily due to aging and under certain pathologic condition such as huperglycemia. Some of the best chemically characterized AGEs include N-epsilon-carboxy-methyl-lysine (CML), N-epsilon-carboxy-ethyl-lysine (CEL), and Imidazolone. The major receptor for AGEs, known as receptor for advanced glycation end products (RAGE or AGER), belongs to the immunoglobulin superfamily and has been described as a pattern recognition receptor. AGE/RAGE signaling elicits activation of multiple intracellular signal pathways involving NADPH oxidase, protein kinase C, and MAPKs, then resulting in NF-kappaB activity. NF-kappa B promotes the expression of pro-inflammatory cytokines such as IL-1, IL-6 and TNF-alpha and a variety of atherosclerosis-related genes, including VCAM-1, tissue factor, VEGF, and RAGE. In addition, JAK-STAT-mediated and PI3K-Akt-dependent pathways are induced via RAGE, which in turn participate in cell proliferation and apoptosis respectively. Hypoxia-mediated induction of Egr-1 was also shown to require the AGE-RAGE interaction. The results of these signal transductions have been reported to be the possible mechanism that initates diabetic complications.
hsa05014	Amyotrophic lateral sclerosis (ALS)	Amyotrophic lateral sclerosis (ALS) is a progressive, lethal, degenerative disorder of motor neurons. The hallmark of this disease is the selective death of motor neurons in the brain and spinal cord, leading to paralysis of voluntary muscles. Mutant superoxide dismutase 1 (SOD1), as seen in some familial ALS (FALS) cases, is unstable, forming aggregates in the motor neuron cytoplasm, axoplasm and mitochondria. Within mitochondria, mutant SOD1 may interfere with the anti-apoptotic function of Bcl-2, affect mitochondrial import by interfering with the translocation machinery (TOM/TIM), and generate toxic free radicals (ROS). Reactive oxygen species (ROS), produced within mitochondria, inhibit the function of EAAT2, the main glial glutamate transporter protein, responsible for most of the reuptake of synaptically released glutamate. Glutamate excess increases intracellular calcium, which enhances oxidative stress and mitochondrial damage. Mutant SOD1 can also trigger oxidative reactions , which can then cause damage through the formation of hydroxyl radicals or via nitration of tyrosine residues on proteins. Nitration may target neurofilament proteins, affecting axonal transport. Collectively, these mechanisms are predicted to disturb cellular homeostasis, ultimately triggering motor neuron death.
hsa05145	Toxoplasmosis	Toxoplasma gondii is an obligate intracellular parasite that is prevalent worldwide. The tachyzoite form acquired by oral ingestion downmodulates proinflammatory signaling pathways via various mechanisms. During early infection, nuclear translocation of NFkB is temporally blocked and p38 MAPK phosphorylation is prevented, suppressing IL-12 production. Another pathway for IL-12 induction occurs through CCR5 dependent pathway, but parasitic induction of an eicosanoid LXA4 contributes to the downregulation of IL-12. Direct activation of STAT3 by the parasite enhance anti-inflammatory function of IL-10 and TGF beta. T. gondii can cause lifelong chronic infection by establishing an anti-apoptotic environment through induction of bcl-2 or IAPs and by redirecting LDL-mediated cholesterol transport to scavenge nutrients from the host.
hsa05152	Tuberculosis	Tuberculosis, or TB, is an infectious disease caused by Mycobacterium tuberculosis. One third of the world's population is thought to be infected with TB. About 90% of those infected result in latent infections, and about 10% of latent infections develop active diseases when their immune system is impaired due to the age, other diseases such as AIDS or exposure to immunosuppressive drugs. TB is transmitted through the air and primarily attacks the lungs, then it can spread by the circulatory system to other parts of body. Once TB bacilli have entered the host by the respiratory route and infected macrophages in the lungs, they interfere with phagosomal maturation, antigen presentation, apoptosis and host immune system to establish persistent or latent infection.
hsa05161	Hepatitis B	Hepatitis B virus (HBV) is an enveloped virus and contains a partially double-stranded relaxed circular DNA (RC-DNA) genome. After entry into hepatocytes, HBV RC-DNA is transported to the nucleus and converted into a covalently closed circular molecule cccDNA. The cccDNA is the template for transcription of all viral RNAs including the pregenomic RNA (pgRNA), encoding for 7 viral proteins: large, middle, and small envelope proteins (LHBs, MHBs, and SHBs) that form the surface antigen (HBsAg), the core antigen (HBcAg), the e antigen (HBeAg), the HBV polymerase, and the regulatory protein X (HBx). The pgRNA interacts with the viral polymerase protein to initiate the encapsidation into the core particles. Through endoplasmic reticulum, the core particles finish assembling with the envelope proteins and are released. HBV infection leads to a wide spectrum of liver diseases raging from chronic hepatitis, cirrhosis to hepatocellular carcinoma. The mechanism of liver injury is still not clear. However, HBV proteins target host proteins, involved in a variety of functions, thus regulating transcription, cellular signaling cascades, proliferation, differentiation, and apoptosis.
hsa05169	Epstein-Barr virus infection	Epstein-Barr virus (EBV) is a gamma-herpes virus that widely infects human populations predominantly at an early age but remains mostly asymptomatic. EBV has been linked to a wide spectrum of human malignancies, including nasopharyngeal carcinoma and other hematologic cancers, like Hodgkin's lymphoma, Burkitt's lymphoma (BL), B-cell immunoblastic lymphoma in HIV patients, and posttransplant-associated lymphoproliferative diseases. EBV has the unique ability to establish life-long latent infection in primary human B lymphocytes. During latent infection, EBV expresses a small subset of genes, including 6 nuclear antigens (EBNA-1, -2, -3A, -3B, -3C, and -LP), 3 latent membrane proteins (LMP-1, -2A, and -2B), 2 small noncoding RNAs (EBER-1 and 2). On the basis of these latent gene expression, three different latency patterns associated with the types of cancers are recognized.
hsa05170	Human immunodeficiency virus 1 infection	Human immunodeficiency virus type 1 (HIV-1) , the causative agent of AIDS (acquired immunodeficiency syndrome), is a lentivirus belonging to the Retroviridae family. The primary cell surface receptor for HIV-1, the CD4 protein, and the co-receptor for HIV-1, either CCR5 or CXCR4, are found on macrophages and T lymphocytes. At the earliest step, sequential binding of virus envelope (Env) glycoprotein gp120 to CD4 and the co-receptor CCR5 or CXCR4 facilitates HIV-1 entry and has the potential to trigger critical signaling that may favor viral replication. At advanced stages of the disease, HIV-1 infection results in dramatic induction of T-cell (CD4+ T and CD8+ T cell) apoptosis both in infected and uninfected bystander T cells, a hallmark of HIV-1 pathogenesis. On the contrary, macrophages are resistant to the cytopathic effect of HIV-1 and produce virus for longer periods of time.
hsa05200	Pathways in cancer
hsa05206	MicroRNAs in cancer	MicroRNA (miRNA) is a cluster of small non-encoding RNA molecules of 21 - 23 nucleotides in length, which controls gene expression post-transcriptionally either via the degradation of target mRNAs or the inhibition of protein translation. Using high-throughput profiling, dysregulation of miRNAs has been widely observed in different stages of cancer. The upregulation (overexpression) of specific miRNAs could lead to the repression of tumor suppressor gene expression, and conversely the downregulation of specific miRNAs could result in an increase of oncogene expression; both these situations induce subsequent malignant effects on cell proliferation, differentiation, and apoptosis that lead to tumor growth and progress. The miRNA signatures of cancer observed in various studies differ significantly. These inconsistencies occur due to the differences in the study populations and methodologies used. This pathway map shows the summarized results from various studies in 9 cancers, each of which is presented in a review article.
hsa05210	Colorectal cancer	Colorectal cancer (CRC) is the second largest cause of cancer-related deaths in Western countries. CRC arises from the colorectal epithelium as a result of the accumulation of genetic alterations in defined oncogenes and tumour suppressor genes (TSG). Two major mechanisms of genomic instability have been identified in sporadic CRC progression. The first, known as chromosomal instability (CIN), results from a series of genetic changes that involve the activation of oncogenes such as K-ras and inactivation of TSG such as p53, DCC/Smad4, and APC. The second, known as microsatellite instability (MSI), results from inactivation of the DNA mismatch repair genes MLH1 and/or MSH2 by hypermethylation of their promoter, and secondary mutation of genes with coding microsatellites, such as transforming growth factor receptor II (TGF-RII) and BAX. Hereditary syndromes have germline mutations in specific genes (mutation in the tumour suppressor gene APC on chromosome 5q in FAP, mutated DNA mismatch repair genes in HNPCC).
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.
hsa05222	Small cell lung cancer	Lung cancer is a leading cause of cancer death among men and women in industrialized countries. Small cell lung carcinoma (SCLC) is a highly aggressive neoplasm, which accounts for approximately 25% of all lung cancer cases. Molecular mechanisms altered in SCLC include induced expression of oncogene, MYC, and loss of tumorsuppressor genes, such as p53, PTEN, RB, and FHIT. The overexpression of MYC proteins in SCLC is largely a result of gene amplification. Such overexpression leads to more rapid proliferation and loss of terminal differentiation. Mutation or deletion of p53 or PTEN can lead to more rapid proliferation and reduced apoptosis. The retinoblastoma gene RB1 encodes a nuclear phosphoprotein that helps to regulate cell-cycle progression. The fragile histidine triad gene FHIT encodes the enzyme diadenosine triphosphate hydrolase, which is thought to have an indirect role in proapoptosis and cell-cycle control.
hsa05226	Gastric cancer	Gastric cancer (GC) is one of the world's most common cancers. According to Lauren's histological classification gastric cancer is divided into two distinct histological groups - the intestinal and diffuse types. Several genetic changes have been identified in intestinal-type GC. The intestinal metaplasia is characterized by mutations in p53 gene, reduced expression of retinoic acid receptor beta (RAR-beta) and hTERT expression. Gastric adenomas furthermore display mutations in the APC gene, reduced p27 expression and cyclin E amplification. In addition, amplification and overexpression of c-ErbB2, reduced TGF-beta receptor type I (TGFBRI) expression and complete loss of p27 expression are commonly observed in more advanced GC. The main molecular changes observed in diffuse-type GCs include loss of E-cadherin function by mutations in CDH1 and amplification of MET and FGFR2F.
hsa05418	Fluid shear stress and atherosclerosis	Shear stress represents the frictional force that the flow of blood exerts at the endothelial surface of the vessel wall and plays a central role in vascular biology and contributes to the progress of atherosclerosis. Sustained laminar flow with high shear stress upregulates expressions of endothelial cell (EC) genes and proteins that are protective against atherosclerosis. The key shear stress-induced transcription factors that govern the expression of these genes are Kruppel-like factor 2 (KLF2) and nuclear factor erythroid 2-like 2 (Nrf2). On the other hand, disturbed flow with associated reciprocating, low shear stress generally upregulates the EC genes and proteins that promote oxidative and inflammatory states in the artery wall, resulting in atherogenesis. Important transcriptional events that reflect this condition of ECs in disturbed flow include the activation of activator protein 1 (AP-1) and nuclear factor kappaB (NF-kappaB).

Pathway ID	Pathway Name	Pathway Description (KEGG)
R-HSA-111447	Activation of BAD and translocation to mitochondria.	The switching on/off of its phosphorylation by growth/survival factors regulates BAD activity. BAD remains sequestered by 14-3-3 scaffold proteins after phosphorylation by Akt1. Calcineurin activates BAD by dephosphorylation
R-HSA-111453	BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members.	Bcl-2 interacts with tBid (Yi et al. 2003), BIM (Puthalakath et al. 1999), PUMA (Nakano and Vousden 2001), NOXA (Oda et al. 2000), BAD (Yang et al. 2005), BMF (Puthalakath et al. 2001), resulting in inactivation of BCL2. Binding of BCL2 to tBID inhibits BID-induced cytochrome C release and apoptosis (Yi et al. 2003). BH3 only proteins associate with and inactivate anti-apoptotic BCL-XL
R-HSA-6785807	Interleukin-4 and Interleukin-13 signaling.	Interleukin-4 (IL4) is a principal regulatory cytokine during the immune response, crucially important in allergy and asthma (Nelms et al. 1999). When resting T cells are antigen-activated and expand in response to Interleukin-2 (IL2), they can differentiate as Type 1 (Th1) or Type 2 (Th2) T helper cells. The outcome is influenced by IL4. Th2 cells secrete IL4, which both stimulates Th2 in an autocrine fashion and acts as a potent B cell growth factor to promote humoral immunity (Nelms et al. 1999). Interleukin-13 (IL13) is an immunoregulatory cytokine secreted predominantly by activated Th2 cells. It is a key mediator in the pathogenesis of allergic inflammation. IL13 shares many functional properties with IL4, stemming from the fact that they share a common receptor subunit. IL13 receptors are expressed on human B cells, basophils, eosinophils, mast cells, endothelial cells, fibroblasts, monocytes, macrophages, respiratory epithelial cells, and smooth muscle cells, but unlike IL4, not T cells. Thus IL13 does not appear to be important in the initial differentiation of CD4 T cells into Th2 cells, rather it is important in the effector phase of allergic inflammation (Hershey et al. 2003).\n\nIL4 and IL13 induce “alternative activation” of macrophages, inducing an anti-inflammatory phenotype by signaling through IL4R alpha in a STAT6 dependent manner. This signaling plays an important role in the Th2 response, mediating anti-parasitic effects and aiding wound healing (Gordon & Martinez 2010, Loke et al. 2002)\n\nThere are two types of IL4 receptor complex (Andrews et al. 2006). Type I IL4R (IL4R1) is predominantly expressed on the surface of hematopoietic cells and consists of IL4R and IL2RG, the common gamma chain. Type II IL4R (IL4R2) is predominantly expressed on the surface of nonhematopoietic cells, it consists of IL4R and IL13RA1 and is also the type II receptor for IL13. (Obiri et al. 1995, Aman et al. 1996, Hilton et al. 1996, Miloux et al. 1997, Zhang et al. 1997). The second receptor for IL13 consists of IL4R and Interleukin-13 receptor alpha 2 (IL13RA2), sometimes called Interleukin-13 binding protein (IL13BP). It has a high affinity receptor for IL13 (Kd = 250 pmol/L) but is not sufficient to render cells responsive to IL13, even in the presence of IL4R (Donaldson et al. 1998). It is reported to exist in soluble form (Zhang et al. 1997) and when overexpressed reduces JAK-STAT signaling (Kawakami et al. 2001). It's function may be to prevent IL13 signalling via the functional IL4R:IL13RA1 receptor. IL13RA2 is overexpressed and enhances cell invasion in some human cancers (Joshi & Puri 2012).The first step in the formation of IL4R1 (IL4:IL4R:IL2RB) is the binding of IL4 with IL4R (Hoffman et al. 1995, Shen et al. 1996, Hage et al. 1999). This is also the first step in formation of IL4R2 (IL4:IL4R:IL13RA1). After the initial binding of IL4 and IL4R, IL2RB binds (LaPorte et al. 2008), to form IL4R1. Alternatively, IL13RA1 binds, forming IL4R2. In contrast, the type II IL13 complex (IL13R2) forms with IL13 first binding to IL13RA1 followed by recruitment of IL4R (Wang et al. 2009).Crystal structures of the IL4:IL4R:IL2RG, IL4:IL4R:IL13RA1 and IL13:IL4R:IL13RA1 complexes have been determined (LaPorte et al. 2008). Consistent with these structures, in monocytes IL4R is tyrosine phosphorylated in response to both IL4 and IL13 (Roy et al. 2002, Gordon & Martinez 2010) while IL13RA1 phosphorylation is induced only by IL13 (Roy et al. 2002, LaPorte et al. 2008) and IL2RG phosphorylation is induced only by IL4 (Roy et al. 2002).Both IL4 receptor complexes signal through Jak/STAT cascades. IL4R is constitutively-associated with JAK2 (Roy et al. 2002) and associates with JAK1 following binding of IL4 (Yin et al. 1994) or IL13 (Roy et al. 2002). IL2RG constitutively associates with JAK3 (Boussiotis et al. 1994, Russell et al. 1994). IL13RA1 constitutively associates with TYK2 (Umeshita-Suyama et al. 2000, Roy et al. 2002, LaPorte et al. 2008, Bhattacharjee et al. 2013). IL4 binding to IL4R1 leads to phosphorylation of JAK1 (but not JAK2) and STAT6 activation (Takeda et al. 1994, Ratthe et al. 2007, Bhattacharjee et al. 2013). IL13 binding increases activating tyrosine-99 phosphorylation of IL13RA1 but not that of IL2RG. IL4 binding to IL2RG leads to its tyrosine phosphorylation (Roy et al. 2002). IL13 binding to IL4R2 leads to TYK2 and JAK2 (but not JAK1) phosphorylation (Roy & Cathcart 1998, Roy et al. 2002).Phosphorylated TYK2 binds and phosphorylates STAT6 and possibly STAT1 (Bhattacharjee et al. 2013). A second mechanism of signal transduction activated by IL4 and IL13 leads to the insulin receptor substrate (IRS) family (Kelly-Welch et al. 2003). IL4R1 associates with insulin receptor substrate 2 and activates the PI3K/Akt and Ras/MEK/Erk pathways involved in cell proliferation, survival and translational control. IL4R2 does not associate with insulin receptor substrate 2 and consequently the PI3K/Akt and Ras/MEK/Erk pathways are not activated (Busch-Dienstfertig & González-Rodríguez 2013)
R-HSA-844455	The NLRP1 inflammasome.	NLRP1 is activated by MDP (Faustin et al. 2007). The NLRP1 inflammasome was the first to be characterized. It was described as a complex containing NALP1, ASC, caspase-1 and caspase-5 (Martinon et al. 2002). Unlike NLRP3, NLRP1 has a C-terminal extension containing a CARD domain, which has been reported to interact directly with procaspase-1, obviating a requirement for ASC (Faustin et al. 2007), though ASC was found to augment the interaction. Mouse NLRP1 has no PYD domain and would therefore not be expected to interact directly with procaspase-1. Like the NLRP3 inflammasome, K+ efflux appears to be essential for caspase-1 activation (Wickliffe et al. 2008). Ribonucleoside triphosphates (NTPs) are required for NALP1-mediated caspase-1 activation with ATP being the most efficient, Mg2+ was also required (Faustin et al. 2007). The human NLRP1 gene has 3 paralogues in mouse that are highly polymorphic. Differences between mouse strains underlie susceptibility to anthrax lethal toxin (Boyden & Dietrich 2006)
R-HSA-9018519	Estrogen-dependent gene expression.	Estrogens mediate their transcriptional effects through interaction with the estrogen receptors, ESR1 (also known as ER alpha) and ESR2 (ER beta). ESR1 and ESR2 share overlapping but distinct functions, with ESR1 playing the primary role in transcriptional activation in most cell types (Hah and Krauss, 2014; Haldosén et al, 2014. The receptors function as ligand-dependent dimers and can activate target genes either through direct binding to an estrogen responsive element (ERE) in the target gene promoter, or indirectly through interaction with another DNA-binding protein such as RUNX1, SP1, AP1 or NF-kappa beta (reviewed in Bai and Gust, 2009; Hah and Krause, 2014). Binding of estrogen receptors to the DNA promotes the assembly of higher order transcriptional complexes containing methyltransferases, histone acetyltransferases and other transcriptional activators, which promote transcription by establishing active chromatin marks and by recruiting general transcription factors and RNA polymerase II. ESR1- and estrogen-dependent recruitment of up to hundreds of coregulators has been demonstrated by varied co-immunoprecipitation and proteomic approaches (Kittler et al, 2013; Mohammed et al, 2013; Foulds et al, 2013; Mohammed et al, 2015; Liu et al, 2014; reviewed in Magnani and Lupien, 2014; Arnal, 2017). In some circumstances, ligand-bound receptors can also promote the assembly of a repression complex at a target gene, and in some cases, heterodimers of ESR1 and ESR2 serve as repressors of ESR1-mediated target gene activation (reviewed in Hah and Kraus, 2014; Arnal et al, 2017). Phosphorylation of the estrogen receptor also modulates its activity, and provides cross-talk between nuclear estrogen-dependent signaling and non-genomic estrogen signaling from the plasma membrane (reviewed in Anbalagan and Rowan, 2015; Halodsèn et al, 2014; Schwartz et al, 2016) A number of recent genome wide studies highlight the breadth of the transcriptional response to estrogen. The number of predicted estrogen-dependent target genes ranges from a couple of hundred (based on microarray studies) to upwards of 10000, based on ChIP-chip or ChIP-seq (Cheung and Kraus, 2010; Kinnis and Kraus, 2008; Lin et al, 2004; Welboren et al, 2009; Ikeda et al, 2015; Lin et al, 2007; Carroll et al, 2006). Many of these predicted sites may not represent transcriptionally productive binding events, however. A study examining ESR1 binding by ChIP-seq in 20 primary breast cancers identified a core of 484 ESR-binding events that were conserved in at least 75% of ER+ tumors, which may represent a more realistic estimate (Ross-Innes et al, 2012). These studies also highlight the long-range effect of estrogen receptor-binding, with distal enhancer or promoter elements regulating the expression of many target genes, often through looping or other higher order chromatin structures (Kittler et al, 2013; reviewed in Dietz and Carroll, 2008; Liu and Cheung, 2014; Magnani and Lupien, 2014). Transcription from a number of estrogen-responsive target genes also appears to be primed by the binding of pioneering transcription factors such as FOXA1, GATA3, PBX1 among others

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Interacting partner	Detection method	Interaction type	PubMed IDs	Interaction Score	Source
ATG12	Affinity Capture-Western	physical	22152474, (Europe PMC)	NA	BioGRID
ATP2A3	Affinity Capture-Luminescence	physical	9788433, (Europe PMC)	NA	BioGRID
AVEN	Affinity Capture-Western, Two-hybrid	physical	10949025, (Europe PMC)	NA	BioGRID
BAD	Affinity Capture-Western, Far Western, Protein-peptide, Reconstituted Complex, Two-hybrid, anti bait coimmunoprecipitation, enzyme linked immunosorbent assay, surface plasmon resonance, two hybrid	direct interaction, physical, physical association	10611223, 15694340, 15849194, 15990872, 16697956, 17446862, 20603619, 7834748, 9305851, 9388232, 9463381, (Europe PMC)	0.81	BioGRID, IntAct, MINT
BAG1	Reconstituted Complex	physical	9305631, (Europe PMC)	NA	BioGRID
BAG3	Affinity Capture-Western	physical	23341456, (Europe PMC)	NA	BioGRID
BAK1	Affinity Capture-Western, Protein-peptide, anti bait coimmunoprecipitation, fluorescence polarization spectroscopy	direct interaction, physical, physical association	11728179, 14980220, 20836993, 26004684, 9463381, (Europe PMC)	0.61	BioGRID, IntAct
BARD1	Co-localization	physical	26022179, (Europe PMC)	NA	BioGRID
BAX	Affinity Capture-Western, Reconstituted Complex, Two-hybrid, anti bait coimmunoprecipitation, anti tag coimmunoprecipitation, enzyme linked immunosorbent assay, fluorescence microscopy, fluorescence technology	association, colocalization, physical, physical association	10620799, 10716992, 14980220, 15231068, 16642033, 17097560, 17289999, 17525735, 18981409, 21199865, 21458670, 21671007, 21778226, 22262057, 23479509, 26004684, 8358790, 9111042, 9388232, 9463381, (Europe PMC)	0.94	BioGRID, IntAct, MINT
BBC3	Affinity Capture-Western, Protein-peptide, anti tag coimmunoprecipitation, fluorescence polarization spectroscopy, surface plasmon resonance	direct interaction, physical, physical association	11463392, 15694340, 16697956, 17289999, (Europe PMC)	0.40, 0.76	BioGRID, IntAct
BCAP31	Affinity Capture-Western, Reconstituted Complex, coimmunoprecipitation, far western blotting	physical, physical association	9334338, (Europe PMC)	0.52	BioGRID, IntAct
BCL2	Affinity Capture-Western, Reconstituted Complex, anti tag coimmunoprecipitation	physical, physical association	18835031, 9111042, 9463381, (Europe PMC)	0.59	BioGRID, IntAct
BCL2L1	Affinity Capture-MS, Affinity Capture-Western, Protein-peptide, Reconstituted Complex, fluorescence polarization spectroscopy	direct interaction, physical	12137781, 14980220, 18835031, 26186194, 28514442, (Europe PMC)	0.44	BioGRID, IntAct
BCL2L10	Affinity Capture-Western	physical	11278245, (Europe PMC)	NA	BioGRID
BCL2L11	Affinity Capture-MS, Affinity Capture-Western, Protein-peptide, Reconstituted Complex, Two-hybrid, anti bait coimmunoprecipitation, anti tag coimmunoprecipitation, coimmunoprecipitation, fluorescence polarization spectroscopy, surface plasmon resonance	association, direct interaction, physical, physical association	15694340, 16697956, 17074758, 17097560, 17289999, 17692808, 19805519, 20836993, 21199865, 21671007, 23845444, 26004684, 26186194, 28514442, 9430630, 9731710, (Europe PMC)	0.35, 0.70, 0.71, 0.92	BioGRID, IntAct, MINT
BECN1	Affinity Capture-Western, Co-purification, FRET, Reconstituted Complex, Two-hybrid, anti bait coimmunoprecipitation, anti tag coimmunoprecipitation, cosedimentation through density gradient, pull down, two hybrid	association, colocalization, physical, physical association	16179260, 17446862, 18641390, 19050071, 19180116, 19347031, 19959994, 20010695, 20622903, 20711182, 20889974, 21139567, 21358617, 21543763, 21971985, 22622204, 23168911, 23316280, 23479509, 23504944, 23541952, 23564079, 23954414, 24034250, 24472739, 24599950, 25891078, 25984893, 28128446, 29079782, 9765397, (Europe PMC)	0.95	BioGRID, IntAct, MINT
BFAR	Affinity Capture-Western, Two-hybrid	physical	10716992, (Europe PMC)	NA	BioGRID
BID	Affinity Capture-Western, Co-fractionation, Protein-peptide, Reconstituted Complex, anti bait coimmunoprecipitation, anti tag coimmunoprecipitation, coimmunoprecipitation, fluorescence polarization spectroscopy, surface plasmon resonance	association, direct interaction, physical, physical association	12624108, 15520201, 15694340, 16697956, 17289999, 18835031, 19074266, 9463381, (Europe PMC)	0.87	BioGRID, IntAct
BIK	Affinity Capture-Western, Protein-peptide, Two-hybrid, anti bait coimmunoprecipitation, anti tag coimmunoprecipitation, fluorescence polarization spectroscopy, two hybrid array, two hybrid prey pooling approach	direct interaction, physical, physical association	12853473, 15694340, 16697956, 17289999, 9463381, 9488477, (Europe PMC)	0.80	BioGRID, IntAct
BLID	Affinity Capture-Western	physical	20400521, (Europe PMC)	NA	BioGRID
BLK	Reconstituted Complex	physical	9525867, (Europe PMC)	NA	BioGRID
BMF	Affinity Capture-Western, Protein-peptide, anti tag coimmunoprecipitation	physical, physical association	11546872, 16697956, 17289999, (Europe PMC)	0.40	BioGRID, IntAct
BNIP1	Reconstituted Complex	physical	10217402, (Europe PMC)	NA	BioGRID
BNIP2	Reconstituted Complex, Two-hybrid, two hybrid	physical, physical association	10381623, 12901880, 7954800, (Europe PMC)	0.37	BioGRID, IntAct, MINT
BNIP3	Affinity Capture-Western, Two-hybrid, two hybrid	physical, physical association	10381623, 10625696, 23504944, 7954800, (Europe PMC)	0.37	BioGRID, IntAct, MINT
BNIP3L	Affinity Capture-Western, Reconstituted Complex, pull down	direct interaction, physical	10467396, 9973195, (Europe PMC)	0.44	BioGRID, IntAct
BNIPL	Affinity Capture-Western, Two-hybrid	physical	12901880, (Europe PMC)	NA	BioGRID
BRCA1	Affinity Capture-Western, FRET, confocal microscopy, proximity ligation assay	colocalization, physical, physical association	21444675, (Europe PMC)	0.46	BioGRID, IntAct
CAPN2	Biochemical Activity, Reconstituted Complex	physical	12000759, (Europe PMC)	NA	BioGRID
CASP2	Phenotypic Suppression	genetic	11832478, (Europe PMC)	NA	BioGRID
CASP3	Biochemical Activity	physical	11752215, (Europe PMC)	NA	BioGRID
CASP8	Affinity Capture-Western, Phenotypic Suppression, Two-hybrid, two hybrid	genetic, physical, physical association	11406564, 11832478, 16183855, (Europe PMC)	0.37	BioGRID, IntAct
CDK1	Affinity Capture-Western, Biochemical Activity	physical	11326318, 11774038, 9668078, (Europe PMC)	NA	BioGRID
CDK4	Negative Genetic	genetic	28319113, (Europe PMC)	NA	BioGRID
CHUK	Affinity Capture-Western	physical	22262057, (Europe PMC)	NA	BioGRID
CISD2	Affinity Capture-Western	physical	20010695, (Europe PMC)	NA	BioGRID
CRYAB	Affinity Capture-Western	physical	20841355, (Europe PMC)	NA	BioGRID
DYNLL1	Affinity Capture-Western	physical	10198631, (Europe PMC)	NA	BioGRID
FKBP8	Affinity Capture-Western, Far Western, Reconstituted Complex, Two-hybrid, pull down, two hybrid	physical, physical association	12510191, 15733859, 15990872, 17379601, 17942410, (Europe PMC)	0.51	BioGRID, IntAct, MINT
GIMAP5	Affinity Capture-Western	physical	16509771, (Europe PMC)	NA	BioGRID
HIF1A	Affinity Capture-Western	physical	20668552, (Europe PMC)	NA	BioGRID
HNRNPD	Two-hybrid	physical	14769789, (Europe PMC)	NA	BioGRID
HRK	Affinity Capture-Western, Protein-peptide, Two-hybrid	physical	15694340, 9130713, (Europe PMC)	NA	BioGRID
HSP90AA1	Affinity Capture-Western	physical	20668552, 21543763, (Europe PMC)	NA	BioGRID
HSPA1A	Affinity Capture-Western	physical	10354271, (Europe PMC)	NA	BioGRID
IKBKB	Affinity Capture-Western	physical	22262057, (Europe PMC)	NA	BioGRID
IKBKG	Affinity Capture-Western	physical	17363905, (Europe PMC)	NA	BioGRID
IRS1	Affinity Capture-Western	physical	10679027, (Europe PMC)	NA	BioGRID
IRS2	Affinity Capture-Western	physical	10679027, (Europe PMC)	NA	BioGRID
ITLN1	Dosage Rescue	genetic	22647378, (Europe PMC)	NA	BioGRID
ITM2B	Affinity Capture-Western	physical	12082633, (Europe PMC)	NA	BioGRID
ITPR1	Affinity Capture-Western, Reconstituted Complex, anti bait coimmunoprecipitation	physical, physical association	15613488, 19706527, (Europe PMC)	0.40	BioGRID, IntAct
KEAP1	Affinity Capture-Western	physical	24127568, (Europe PMC)	NA	BioGRID
KRAS	Affinity Capture-Western	physical	19433448, (Europe PMC)	NA	BioGRID
MAPK1	Affinity Capture-Western, Biochemical Activity, anti bait coimmunoprecipitation, experimental interaction detection	phosphorylation reaction, physical, physical association	15225643, (Europe PMC)	0.49	BioGRID, IntAct, MINT
MAPK8	Biochemical Activity, experimental interaction detection	phosphorylation reaction, physical	15733859, (Europe PMC)	0.31	BioGRID, IntAct, MINT
MAT2A	Affinity Capture-Western	physical	26416353, (Europe PMC)	NA	BioGRID
MDM4	Affinity Capture-Western, anti bait coimmunoprecipitation	association, physical, physical association	19521340, 24445145, (Europe PMC)	0.50	BioGRID, IntAct, MINT
MEX3D	Two-hybrid	physical	14769789, (Europe PMC)	NA	BioGRID
MOAP1	Affinity Capture-Western	physical	11060313, (Europe PMC)	NA	BioGRID
MYC	Affinity Capture-Western, Co-localization	physical	15210690, (Europe PMC)	NA	BioGRID
NMT2	Affinity Capture-Western, anti bait coimmunoprecipitation	physical, physical association	16530191, (Europe PMC)	0.40	BioGRID, IntAct, MINT
NR4A1	Affinity Capture-Western, Reconstituted Complex, Two-hybrid, anti bait coimmunoprecipitation, anti tag coimmunoprecipitation, circular dichroism, fluorescence polarization spectroscopy	association, direct interaction, physical, physical association	14980220, 16434970, 18835031, (Europe PMC)	0.67	BioGRID, IntAct
PARP1	Reconstituted Complex	physical	11790116, (Europe PMC)	NA	BioGRID
PIN1	Affinity Capture-Western	physical	11326318, (Europe PMC)	NA	BioGRID
PMAIP1	Affinity Capture-Western, Protein-peptide, anti bait coimmunoprecipitation, pull down, surface plasmon resonance	direct interaction, physical, physical association	10807576, 15694340, 21454712, (Europe PMC)	0.52, 0.54	BioGRID, IntAct
PML	Affinity Capture-Western	physical	15231068, (Europe PMC)	NA	BioGRID
PPARA	Affinity Capture-Western, Biochemical Activity	physical	26556865, (Europe PMC)	NA	BioGRID
PPID	Affinity Capture-Western, Reconstituted Complex, Two-hybrid	physical	19228691, (Europe PMC)	NA	BioGRID
PPP1CA	Affinity Capture-Western, antibody array	physical, physical association	17274640, (Europe PMC)	0.40	BioGRID, IntAct
PPP1CB	Affinity Capture-Western, antibody array	physical, physical association	17274640, (Europe PMC)	0.40	BioGRID, IntAct
PPP1CC	Affinity Capture-Western, antibody array	physical, physical association	17274640, (Europe PMC)	0.40	BioGRID, IntAct
PPP2CA	Affinity Capture-Western, Biochemical Activity, Reconstituted Complex, anti bait coimmunoprecipitation, experimental interaction detection	dephosphorylation reaction, physical, physical association	15225643, 9852076, (Europe PMC)	0.49	BioGRID, IntAct, MINT
PPP2R5A	Affinity Capture-Western	physical	11929874, (Europe PMC)	NA	BioGRID
PPP3CA	Affinity Capture-Western	physical	19706527, 9109491, (Europe PMC)	NA	BioGRID
PPP3CC	Reconstituted Complex	physical	15757646, (Europe PMC)	NA	BioGRID
PRKN	Affinity Capture-Western, Reconstituted Complex	physical	20889974, (Europe PMC)	NA	BioGRID
PSEN1	Affinity Capture-Western, Two-hybrid	physical	10521466, (Europe PMC)	NA	BioGRID
RAD9A	Affinity Capture-Western, Two-hybrid	physical	10620799, 18794804, (Europe PMC)	NA	BioGRID
RAF1	Affinity Capture-Western, Reconstituted Complex, Two-hybrid	physical	12488548, 15849194, 8929532, (Europe PMC)	NA	BioGRID
RRAS	Affinity Capture-Western, Two-hybrid	physical	8232588, (Europe PMC)	NA	BioGRID
RTN3	Affinity Capture-Western	physical	17191123, (Europe PMC)	NA	BioGRID
RTN4	Affinity Capture-Western, Two-hybrid	physical	11126360, 17191123, (Europe PMC)	NA	BioGRID
SEPT4	Affinity Capture-Western, PCA, Protein-peptide	physical	29020630, (Europe PMC)	NA	BioGRID
SERPINB8	Affinity Capture-Western	physical	15231068, (Europe PMC)	NA	BioGRID
SMN1	Affinity Capture-Western, Reconstituted Complex, Two-hybrid	physical	9389483, (Europe PMC)	NA	BioGRID
SOD1	Affinity Capture-Western, Reconstituted Complex	physical	15233914, (Europe PMC)	NA	BioGRID
SPNS1	Affinity Capture-Western, anti tag coimmunoprecipitation, confocal microscopy	colocalization, physical, physical association	12815463, (Europe PMC)	0.46	BioGRID, IntAct
SQSTM1	Affinity Capture-Western, Reconstituted Complex	physical	23564079, 25311206, (Europe PMC)	NA	BioGRID
TMBIM6	Affinity Capture-Western	physical	9660918, (Europe PMC)	NA	BioGRID
TOMM20	Reconstituted Complex	physical	9119086, (Europe PMC)	NA	BioGRID
TP53	Affinity Capture-Western, anti bait coimmunoprecipitation	association, physical, physical association	12667443, 19521340, 21597459, 21624955, (Europe PMC)	0.56	BioGRID, IntAct, MINT
TP53AIP1	Affinity Capture-Western	physical	12019168, (Europe PMC)	NA	BioGRID
TP53BP2	Protein-peptide, Reconstituted Complex, Two-hybrid, fluorescence technology, peptide array, proximity ligation assay, surface plasmon resonance	direct interaction, physical	18719108, 8668206, (Europe PMC)	0.65	BioGRID, IntAct
UBE2I	Affinity Capture-Western	physical	26416353, (Europe PMC)	NA	BioGRID
VDAC1	Affinity Capture-Western, anti bait coimmunoprecipitation	physical, physical association	19706527, (Europe PMC)	0.40	BioGRID, IntAct
XIAP	Biochemical Activity, Reconstituted Complex	physical	29020630, (Europe PMC)	NA	BioGRID

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Interacting partner	Detection method	Interaction type	PubMed IDs	Interaction Score	Source
BAD	Affinity Capture-Western, Far Western, Protein-peptide, Reconstituted Complex, Two-hybrid, anti bait coimmunoprecipitation, enzyme linked immunosorbent assay, surface plasmon resonance, two hybrid	direct interaction, physical, physical association	10611223, 15694340, 15849194, 15990872, 16697956, 17446862, 20603619, 7834748, 9305851, 9388232, 9463381, (Europe PMC)	0.81	BioGRID, IntAct, MINT
BAK1	Affinity Capture-Western, Protein-peptide, anti bait coimmunoprecipitation, fluorescence polarization spectroscopy	direct interaction, physical, physical association	11728179, 14980220, 20836993, 26004684, 9463381, (Europe PMC)	0.61	BioGRID, IntAct
BAX	Affinity Capture-Western, Reconstituted Complex, Two-hybrid, anti bait coimmunoprecipitation, anti tag coimmunoprecipitation, enzyme linked immunosorbent assay, fluorescence microscopy, fluorescence technology	association, colocalization, physical, physical association	10620799, 10716992, 14980220, 15231068, 16642033, 17097560, 17289999, 17525735, 18981409, 21199865, 21458670, 21671007, 21778226, 22262057, 23479509, 26004684, 8358790, 9111042, 9388232, 9463381, (Europe PMC)	0.94	BioGRID, IntAct, MINT
BBC3	Affinity Capture-Western, Protein-peptide, anti tag coimmunoprecipitation, fluorescence polarization spectroscopy, surface plasmon resonance	direct interaction, physical, physical association	11463392, 15694340, 16697956, 17289999, (Europe PMC)	0.40, 0.76	BioGRID, IntAct
BCAP31	Affinity Capture-Western, Reconstituted Complex, coimmunoprecipitation, far western blotting	physical, physical association	9334338, (Europe PMC)	0.52	BioGRID, IntAct
BCL2	Affinity Capture-Western, Reconstituted Complex, anti tag coimmunoprecipitation	physical, physical association	18835031, 9111042, 9463381, (Europe PMC)	0.59	BioGRID, IntAct
BCL2L1	Affinity Capture-MS, Affinity Capture-Western, Protein-peptide, Reconstituted Complex, fluorescence polarization spectroscopy	direct interaction, physical	12137781, 14980220, 18835031, 26186194, 28514442, (Europe PMC)	0.44	BioGRID, IntAct
BCL2L11	Affinity Capture-MS, Affinity Capture-Western, Protein-peptide, Reconstituted Complex, Two-hybrid, anti bait coimmunoprecipitation, anti tag coimmunoprecipitation, coimmunoprecipitation, fluorescence polarization spectroscopy, surface plasmon resonance	association, direct interaction, physical, physical association	15694340, 16697956, 17074758, 17097560, 17289999, 17692808, 19805519, 20836993, 21199865, 21671007, 23845444, 26004684, 26186194, 28514442, 9430630, 9731710, (Europe PMC)	0.35, 0.70, 0.71, 0.92	BioGRID, IntAct, MINT
BCLAF1	anti bait coimmunoprecipitation	association, physical association	23541952, (Europe PMC)	0.50	IntAct
BECN1	Affinity Capture-Western, Co-purification, FRET, Reconstituted Complex, Two-hybrid, anti bait coimmunoprecipitation, anti tag coimmunoprecipitation, cosedimentation through density gradient, pull down, two hybrid	association, colocalization, physical, physical association	16179260, 17446862, 18641390, 19050071, 19180116, 19347031, 19959994, 20010695, 20622903, 20711182, 20889974, 21139567, 21358617, 21543763, 21971985, 22622204, 23168911, 23316280, 23479509, 23504944, 23541952, 23564079, 23954414, 24034250, 24472739, 24599950, 25891078, 25984893, 28128446, 29079782, 9765397, (Europe PMC)	0.95	BioGRID, IntAct, MINT
BECN2	anti tag coimmunoprecipitation	physical association	23954414, (Europe PMC)	0.40	IntAct
BID	Affinity Capture-Western, Co-fractionation, Protein-peptide, Reconstituted Complex, anti bait coimmunoprecipitation, anti tag coimmunoprecipitation, coimmunoprecipitation, fluorescence polarization spectroscopy, surface plasmon resonance	association, direct interaction, physical, physical association	12624108, 15520201, 15694340, 16697956, 17289999, 18835031, 19074266, 9463381, (Europe PMC)	0.87	BioGRID, IntAct
BIK	Affinity Capture-Western, Protein-peptide, Two-hybrid, anti bait coimmunoprecipitation, anti tag coimmunoprecipitation, fluorescence polarization spectroscopy, two hybrid array, two hybrid prey pooling approach	direct interaction, physical, physical association	12853473, 15694340, 16697956, 17289999, 9463381, 9488477, (Europe PMC)	0.80	BioGRID, IntAct
BMF	Affinity Capture-Western, Protein-peptide, anti tag coimmunoprecipitation	physical, physical association	11546872, 16697956, 17289999, (Europe PMC)	0.40	BioGRID, IntAct
BNIP2	Reconstituted Complex, Two-hybrid, two hybrid	physical, physical association	10381623, 12901880, 7954800, (Europe PMC)	0.37	BioGRID, IntAct, MINT
BNIP3	Affinity Capture-Western, Two-hybrid, two hybrid	physical, physical association	10381623, 10625696, 23504944, 7954800, (Europe PMC)	0.37	BioGRID, IntAct, MINT
BNIP3L	Affinity Capture-Western, Reconstituted Complex, pull down	direct interaction, physical	10467396, 9973195, (Europe PMC)	0.44	BioGRID, IntAct
BRCA1	Affinity Capture-Western, FRET, confocal microscopy, proximity ligation assay	colocalization, physical, physical association	21444675, (Europe PMC)	0.46	BioGRID, IntAct
CALR	cosedimentation through density gradient	colocalization	21139567, (Europe PMC)	0.35	IntAct, MINT
CASP8	Affinity Capture-Western, Phenotypic Suppression, Two-hybrid, two hybrid	genetic, physical, physical association	11406564, 11832478, 16183855, (Europe PMC)	0.37	BioGRID, IntAct
FKBP8	Affinity Capture-Western, Far Western, Reconstituted Complex, Two-hybrid, pull down, two hybrid	physical, physical association	12510191, 15733859, 15990872, 17379601, 17942410, (Europe PMC)	0.51	BioGRID, IntAct, MINT
HSPA9	cosedimentation through density gradient	colocalization	21139567, (Europe PMC)	0.35	IntAct, MINT
ITPR1	Affinity Capture-Western, Reconstituted Complex, anti bait coimmunoprecipitation	physical, physical association	15613488, 19706527, (Europe PMC)	0.40	BioGRID, IntAct
LRRK2	protein kinase assay	phosphorylation reaction	25446991, (Europe PMC)	0.44	IntAct
MAPK1	Affinity Capture-Western, Biochemical Activity, anti bait coimmunoprecipitation, experimental interaction detection	phosphorylation reaction, physical, physical association	15225643, (Europe PMC)	0.49	BioGRID, IntAct, MINT
MAPK8	Biochemical Activity, experimental interaction detection	phosphorylation reaction, physical	15733859, (Europe PMC)	0.31	BioGRID, IntAct, MINT
MCL1	cosedimentation through density gradient	colocalization	21139567, (Europe PMC)	0.35	IntAct, MINT
MDM4	Affinity Capture-Western, anti bait coimmunoprecipitation	association, physical, physical association	19521340, 24445145, (Europe PMC)	0.50	BioGRID, IntAct, MINT
NAF1	anti bait coimmunoprecipitation, pull down	direct interaction, physical association	20010695, (Europe PMC)	0.54	IntAct, MINT
NLRP1	anti bait coimmunoprecipitation, anti tag coimmunoprecipitation, confocal microscopy, pull down	association, colocalization, direct interaction, physical association	17418785, 19223583, (Europe PMC)	0.75	IntAct
NMT2	Affinity Capture-Western, anti bait coimmunoprecipitation	physical, physical association	16530191, (Europe PMC)	0.40	BioGRID, IntAct, MINT
NR4A1	Affinity Capture-Western, Reconstituted Complex, Two-hybrid, anti bait coimmunoprecipitation, anti tag coimmunoprecipitation, circular dichroism, fluorescence polarization spectroscopy	association, direct interaction, physical, physical association	14980220, 16434970, 18835031, (Europe PMC)	0.67	BioGRID, IntAct
PMAIP1	Affinity Capture-Western, Protein-peptide, anti bait coimmunoprecipitation, pull down, surface plasmon resonance	direct interaction, physical, physical association	10807576, 15694340, 21454712, (Europe PMC)	0.52, 0.54	BioGRID, IntAct
PPIF	two hybrid	physical association	19228691, (Europe PMC)	0.37	IntAct
PPP1CA	Affinity Capture-Western, antibody array	physical, physical association	17274640, (Europe PMC)	0.40	BioGRID, IntAct
PPP1CB	Affinity Capture-Western, antibody array	physical, physical association	17274640, (Europe PMC)	0.40	BioGRID, IntAct
PPP1CC	Affinity Capture-Western, antibody array	physical, physical association	17274640, (Europe PMC)	0.40	BioGRID, IntAct
PPP2CA	Affinity Capture-Western, Biochemical Activity, Reconstituted Complex, anti bait coimmunoprecipitation, experimental interaction detection	dephosphorylation reaction, physical, physical association	15225643, 9852076, (Europe PMC)	0.49	BioGRID, IntAct, MINT
PPP3R1	fluorescence microscopy, pull down	colocalization, direct interaction	15757646, (Europe PMC)	0.49	IntAct, MINT
RTL10	anti tag coimmunoprecipitation	association	23055042, (Europe PMC)	0.35	IntAct
SIVA1	pull down	physical association	14739602, (Europe PMC)	0.40	IntAct
SPNS1	Affinity Capture-Western, anti tag coimmunoprecipitation, confocal microscopy	colocalization, physical, physical association	12815463, (Europe PMC)	0.46	BioGRID, IntAct
TP53	Affinity Capture-Western, anti bait coimmunoprecipitation	association, physical, physical association	12667443, 19521340, 21597459, 21624955, (Europe PMC)	0.56	BioGRID, IntAct, MINT
TP53BP2	Protein-peptide, Reconstituted Complex, Two-hybrid, fluorescence technology, peptide array, proximity ligation assay, surface plasmon resonance	direct interaction, physical	18719108, 8668206, (Europe PMC)	0.65	BioGRID, IntAct
VDAC1	Affinity Capture-Western, anti bait coimmunoprecipitation	physical, physical association	19706527, (Europe PMC)	0.40	BioGRID, IntAct
VRK2	two hybrid	physical association	16963744, (Europe PMC)	0.37	IntAct

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Interacting partner	Detection method	Interaction type	PubMed IDs	Interaction Score	Source
BAD	Affinity Capture-Western, Far Western, Protein-peptide, Reconstituted Complex, Two-hybrid, anti bait coimmunoprecipitation, enzyme linked immunosorbent assay, surface plasmon resonance, two hybrid	direct interaction, physical, physical association	10611223, 15694340, 15849194, 15990872, 16697956, 17446862, 20603619, 7834748, 9305851, 9388232, 9463381, (Europe PMC)	0.81	BioGRID, IntAct, MINT
BAX	Affinity Capture-Western, Reconstituted Complex, Two-hybrid, anti bait coimmunoprecipitation, anti tag coimmunoprecipitation, enzyme linked immunosorbent assay, fluorescence microscopy, fluorescence technology	association, colocalization, physical, physical association	10620799, 10716992, 14980220, 15231068, 16642033, 17097560, 17289999, 17525735, 18981409, 21199865, 21458670, 21671007, 21778226, 22262057, 23479509, 26004684, 8358790, 9111042, 9388232, 9463381, (Europe PMC)	0.94	BioGRID, IntAct, MINT
BCL2L11	Affinity Capture-MS, Affinity Capture-Western, Protein-peptide, Reconstituted Complex, Two-hybrid, anti bait coimmunoprecipitation, anti tag coimmunoprecipitation, coimmunoprecipitation, fluorescence polarization spectroscopy, surface plasmon resonance	association, direct interaction, physical, physical association	15694340, 16697956, 17074758, 17097560, 17289999, 17692808, 19805519, 20836993, 21199865, 21671007, 23845444, 26004684, 26186194, 28514442, 9430630, 9731710, (Europe PMC)	0.35, 0.70, 0.71, 0.92	BioGRID, IntAct, MINT
BECN1	Affinity Capture-Western, Co-purification, FRET, Reconstituted Complex, Two-hybrid, anti bait coimmunoprecipitation, anti tag coimmunoprecipitation, cosedimentation through density gradient, pull down, two hybrid	association, colocalization, physical, physical association	16179260, 17446862, 18641390, 19050071, 19180116, 19347031, 19959994, 20010695, 20622903, 20711182, 20889974, 21139567, 21358617, 21543763, 21971985, 22622204, 23168911, 23316280, 23479509, 23504944, 23541952, 23564079, 23954414, 24034250, 24472739, 24599950, 25891078, 25984893, 28128446, 29079782, 9765397, (Europe PMC)	0.95	BioGRID, IntAct, MINT
BNIP2	Reconstituted Complex, Two-hybrid, two hybrid	physical, physical association	10381623, 12901880, 7954800, (Europe PMC)	0.37	BioGRID, IntAct, MINT
BNIP3	Affinity Capture-Western, Two-hybrid, two hybrid	physical, physical association	10381623, 10625696, 23504944, 7954800, (Europe PMC)	0.37	BioGRID, IntAct, MINT
CALR	cosedimentation through density gradient	colocalization	21139567, (Europe PMC)	0.35	IntAct, MINT
FKBP8	Affinity Capture-Western, Far Western, Reconstituted Complex, Two-hybrid, pull down, two hybrid	physical, physical association	12510191, 15733859, 15990872, 17379601, 17942410, (Europe PMC)	0.51	BioGRID, IntAct, MINT
HSPA9	cosedimentation through density gradient	colocalization	21139567, (Europe PMC)	0.35	IntAct, MINT
MAPK1	Affinity Capture-Western, Biochemical Activity, anti bait coimmunoprecipitation, experimental interaction detection	phosphorylation reaction, physical, physical association	15225643, (Europe PMC)	0.49	BioGRID, IntAct, MINT
MAPK8	Biochemical Activity, experimental interaction detection	phosphorylation reaction, physical	15733859, (Europe PMC)	0.31	BioGRID, IntAct, MINT
MCL1	cosedimentation through density gradient	colocalization	21139567, (Europe PMC)	0.35	IntAct, MINT
MDM4	Affinity Capture-Western, anti bait coimmunoprecipitation	association, physical, physical association	19521340, 24445145, (Europe PMC)	0.50	BioGRID, IntAct, MINT
NAF1	anti bait coimmunoprecipitation, pull down	direct interaction, physical association	20010695, (Europe PMC)	0.54	IntAct, MINT
NMT2	Affinity Capture-Western, anti bait coimmunoprecipitation	physical, physical association	16530191, (Europe PMC)	0.40	BioGRID, IntAct, MINT
PPP2CA	Affinity Capture-Western, Biochemical Activity, Reconstituted Complex, anti bait coimmunoprecipitation, experimental interaction detection	dephosphorylation reaction, physical, physical association	15225643, 9852076, (Europe PMC)	0.49	BioGRID, IntAct, MINT
PPP3R1	fluorescence microscopy, pull down	colocalization, direct interaction	15757646, (Europe PMC)	0.49	IntAct, MINT
TP53	Affinity Capture-Western, anti bait coimmunoprecipitation	association, physical, physical association	12667443, 19521340, 21597459, 21624955, (Europe PMC)	0.56	BioGRID, IntAct, MINT

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Interacting partner	Detection method	Interaction type	PubMed IDs	Interaction Score	Source
ATG12	Affinity Capture-Western	physical	22152474, (Europe PMC)	NA	BioGRID
ATP2A3	Affinity Capture-Luminescence	physical	9788433, (Europe PMC)	NA	BioGRID
AVEN	Affinity Capture-Western, Two-hybrid	physical	10949025, (Europe PMC)	NA	BioGRID
BAD	Affinity Capture-Western, Far Western, Protein-peptide, Reconstituted Complex, Two-hybrid, anti bait coimmunoprecipitation, enzyme linked immunosorbent assay, surface plasmon resonance, two hybrid	direct interaction, physical, physical association	10611223, 15694340, 15849194, 15990872, 16697956, 17446862, 20603619, 7834748, 9305851, 9388232, 9463381, (Europe PMC)	0.81	BioGRID, IntAct, MINT
BAG1	Reconstituted Complex	physical	9305631, (Europe PMC)	NA	BioGRID
BAG3	Affinity Capture-Western	physical	23341456, (Europe PMC)	NA	BioGRID
BAK1	Affinity Capture-Western, Protein-peptide, anti bait coimmunoprecipitation, fluorescence polarization spectroscopy	direct interaction, physical, physical association	11728179, 14980220, 20836993, 26004684, 9463381, (Europe PMC)	0.61	BioGRID, IntAct
BARD1	Co-localization	physical	26022179, (Europe PMC)	NA	BioGRID
BAX	Affinity Capture-Western, Reconstituted Complex, Two-hybrid, anti bait coimmunoprecipitation, anti tag coimmunoprecipitation, enzyme linked immunosorbent assay, fluorescence microscopy, fluorescence technology	association, colocalization, physical, physical association	10620799, 10716992, 14980220, 15231068, 16642033, 17097560, 17289999, 17525735, 18981409, 21199865, 21458670, 21671007, 21778226, 22262057, 23479509, 26004684, 8358790, 9111042, 9388232, 9463381, (Europe PMC)	0.94	BioGRID, IntAct, MINT
BBC3	Affinity Capture-Western, Protein-peptide, anti tag coimmunoprecipitation, fluorescence polarization spectroscopy, surface plasmon resonance	direct interaction, physical, physical association	11463392, 15694340, 16697956, 17289999, (Europe PMC)	0.40, 0.76	BioGRID, IntAct
BCAP31	Affinity Capture-Western, Reconstituted Complex, coimmunoprecipitation, far western blotting	physical, physical association	9334338, (Europe PMC)	0.52	BioGRID, IntAct
BCL2	Affinity Capture-Western, Reconstituted Complex, anti tag coimmunoprecipitation	physical, physical association	18835031, 9111042, 9463381, (Europe PMC)	0.59	BioGRID, IntAct
BCL2L1	Affinity Capture-MS, Affinity Capture-Western, Protein-peptide, Reconstituted Complex, fluorescence polarization spectroscopy	direct interaction, physical	12137781, 14980220, 18835031, 26186194, 28514442, (Europe PMC)	0.44	BioGRID, IntAct
BCL2L10	Affinity Capture-Western	physical	11278245, (Europe PMC)	NA	BioGRID
BCL2L11	Affinity Capture-MS, Affinity Capture-Western, Protein-peptide, Reconstituted Complex, Two-hybrid, anti bait coimmunoprecipitation, anti tag coimmunoprecipitation, coimmunoprecipitation, fluorescence polarization spectroscopy, surface plasmon resonance	association, direct interaction, physical, physical association	15694340, 16697956, 17074758, 17097560, 17289999, 17692808, 19805519, 20836993, 21199865, 21671007, 23845444, 26004684, 26186194, 28514442, 9430630, 9731710, (Europe PMC)	0.35, 0.70, 0.71, 0.92	BioGRID, IntAct, MINT
BCLAF1	anti bait coimmunoprecipitation	association, physical association	23541952, (Europe PMC)	0.50	IntAct
BECN1	Affinity Capture-Western, Co-purification, FRET, Reconstituted Complex, Two-hybrid, anti bait coimmunoprecipitation, anti tag coimmunoprecipitation, cosedimentation through density gradient, pull down, two hybrid	association, colocalization, physical, physical association	16179260, 17446862, 18641390, 19050071, 19180116, 19347031, 19959994, 20010695, 20622903, 20711182, 20889974, 21139567, 21358617, 21543763, 21971985, 22622204, 23168911, 23316280, 23479509, 23504944, 23541952, 23564079, 23954414, 24034250, 24472739, 24599950, 25891078, 25984893, 28128446, 29079782, 9765397, (Europe PMC)	0.95	BioGRID, IntAct, MINT
BECN2	anti tag coimmunoprecipitation	physical association	23954414, (Europe PMC)	0.40	IntAct
BFAR	Affinity Capture-Western, Two-hybrid	physical	10716992, (Europe PMC)	NA	BioGRID
BID	Affinity Capture-Western, Co-fractionation, Protein-peptide, Reconstituted Complex, anti bait coimmunoprecipitation, anti tag coimmunoprecipitation, coimmunoprecipitation, fluorescence polarization spectroscopy, surface plasmon resonance	association, direct interaction, physical, physical association	12624108, 15520201, 15694340, 16697956, 17289999, 18835031, 19074266, 9463381, (Europe PMC)	0.87	BioGRID, IntAct
BIK	Affinity Capture-Western, Protein-peptide, Two-hybrid, anti bait coimmunoprecipitation, anti tag coimmunoprecipitation, fluorescence polarization spectroscopy, two hybrid array, two hybrid prey pooling approach	direct interaction, physical, physical association	12853473, 15694340, 16697956, 17289999, 9463381, 9488477, (Europe PMC)	0.80	BioGRID, IntAct
BLID	Affinity Capture-Western	physical	20400521, (Europe PMC)	NA	BioGRID
BLK	Reconstituted Complex	physical	9525867, (Europe PMC)	NA	BioGRID
BMF	Affinity Capture-Western, Protein-peptide, anti tag coimmunoprecipitation	physical, physical association	11546872, 16697956, 17289999, (Europe PMC)	0.40	BioGRID, IntAct
BNIP1	Reconstituted Complex	physical	10217402, (Europe PMC)	NA	BioGRID
BNIP2	Reconstituted Complex, Two-hybrid, two hybrid	physical, physical association	10381623, 12901880, 7954800, (Europe PMC)	0.37	BioGRID, IntAct, MINT
BNIP3	Affinity Capture-Western, Two-hybrid, two hybrid	physical, physical association	10381623, 10625696, 23504944, 7954800, (Europe PMC)	0.37	BioGRID, IntAct, MINT
BNIP3L	Affinity Capture-Western, Reconstituted Complex, pull down	direct interaction, physical	10467396, 9973195, (Europe PMC)	0.44	BioGRID, IntAct
BNIPL	Affinity Capture-Western, Two-hybrid	physical	12901880, (Europe PMC)	NA	BioGRID
BRCA1	Affinity Capture-Western, FRET, confocal microscopy, proximity ligation assay	colocalization, physical, physical association	21444675, (Europe PMC)	0.46	BioGRID, IntAct
CALR	cosedimentation through density gradient	colocalization	21139567, (Europe PMC)	0.35	IntAct, MINT
CAPN2	Biochemical Activity, Reconstituted Complex	physical	12000759, (Europe PMC)	NA	BioGRID
CASP2	Phenotypic Suppression	genetic	11832478, (Europe PMC)	NA	BioGRID
CASP3	Biochemical Activity	physical	11752215, (Europe PMC)	NA	BioGRID
CASP8	Affinity Capture-Western, Phenotypic Suppression, Two-hybrid, two hybrid	genetic, physical, physical association	11406564, 11832478, 16183855, (Europe PMC)	0.37	BioGRID, IntAct
CDK1	Affinity Capture-Western, Biochemical Activity	physical	11326318, 11774038, 9668078, (Europe PMC)	NA	BioGRID
CDK4	Negative Genetic	genetic	28319113, (Europe PMC)	NA	BioGRID
CHUK	Affinity Capture-Western	physical	22262057, (Europe PMC)	NA	BioGRID
CISD2	Affinity Capture-Western	physical	20010695, (Europe PMC)	NA	BioGRID
CRYAB	Affinity Capture-Western	physical	20841355, (Europe PMC)	NA	BioGRID
DYNLL1	Affinity Capture-Western	physical	10198631, (Europe PMC)	NA	BioGRID
FKBP8	Affinity Capture-Western, Far Western, Reconstituted Complex, Two-hybrid, pull down, two hybrid	physical, physical association	12510191, 15733859, 15990872, 17379601, 17942410, (Europe PMC)	0.51	BioGRID, IntAct, MINT
GIMAP5	Affinity Capture-Western	physical	16509771, (Europe PMC)	NA	BioGRID
HIF1A	Affinity Capture-Western	physical	20668552, (Europe PMC)	NA	BioGRID
HNRNPD	Two-hybrid	physical	14769789, (Europe PMC)	NA	BioGRID
HRK	Affinity Capture-Western, Protein-peptide, Two-hybrid	physical	15694340, 9130713, (Europe PMC)	NA	BioGRID
HSP90AA1	Affinity Capture-Western	physical	20668552, 21543763, (Europe PMC)	NA	BioGRID
HSPA1A	Affinity Capture-Western	physical	10354271, (Europe PMC)	NA	BioGRID
HSPA9	cosedimentation through density gradient	colocalization	21139567, (Europe PMC)	0.35	IntAct, MINT
IKBKB	Affinity Capture-Western	physical	22262057, (Europe PMC)	NA	BioGRID
IKBKG	Affinity Capture-Western	physical	17363905, (Europe PMC)	NA	BioGRID
IRS1	Affinity Capture-Western	physical	10679027, (Europe PMC)	NA	BioGRID
IRS2	Affinity Capture-Western	physical	10679027, (Europe PMC)	NA	BioGRID
ITLN1	Dosage Rescue	genetic	22647378, (Europe PMC)	NA	BioGRID
ITM2B	Affinity Capture-Western	physical	12082633, (Europe PMC)	NA	BioGRID
ITPR1	Affinity Capture-Western, Reconstituted Complex, anti bait coimmunoprecipitation	physical, physical association	15613488, 19706527, (Europe PMC)	0.40	BioGRID, IntAct
KEAP1	Affinity Capture-Western	physical	24127568, (Europe PMC)	NA	BioGRID
KRAS	Affinity Capture-Western	physical	19433448, (Europe PMC)	NA	BioGRID
LRRK2	protein kinase assay	phosphorylation reaction	25446991, (Europe PMC)	0.44	IntAct
MAPK1	Affinity Capture-Western, Biochemical Activity, anti bait coimmunoprecipitation, experimental interaction detection	phosphorylation reaction, physical, physical association	15225643, (Europe PMC)	0.49	BioGRID, IntAct, MINT
MAPK8	Biochemical Activity, experimental interaction detection	phosphorylation reaction, physical	15733859, (Europe PMC)	0.31	BioGRID, IntAct, MINT
MAT2A	Affinity Capture-Western	physical	26416353, (Europe PMC)	NA	BioGRID
MCL1	cosedimentation through density gradient	colocalization	21139567, (Europe PMC)	0.35	IntAct, MINT
MDM4	Affinity Capture-Western, anti bait coimmunoprecipitation	association, physical, physical association	19521340, 24445145, (Europe PMC)	0.50	BioGRID, IntAct, MINT
MEX3D	Two-hybrid	physical	14769789, (Europe PMC)	NA	BioGRID
MOAP1	Affinity Capture-Western	physical	11060313, (Europe PMC)	NA	BioGRID
MYC	Affinity Capture-Western, Co-localization	physical	15210690, (Europe PMC)	NA	BioGRID
NAF1	anti bait coimmunoprecipitation, pull down	direct interaction, physical association	20010695, (Europe PMC)	0.54	IntAct, MINT
NLRP1	anti bait coimmunoprecipitation, anti tag coimmunoprecipitation, confocal microscopy, pull down	association, colocalization, direct interaction, physical association	17418785, 19223583, (Europe PMC)	0.75	IntAct
NMT2	Affinity Capture-Western, anti bait coimmunoprecipitation	physical, physical association	16530191, (Europe PMC)	0.40	BioGRID, IntAct, MINT
NR4A1	Affinity Capture-Western, Reconstituted Complex, Two-hybrid, anti bait coimmunoprecipitation, anti tag coimmunoprecipitation, circular dichroism, fluorescence polarization spectroscopy	association, direct interaction, physical, physical association	14980220, 16434970, 18835031, (Europe PMC)	0.67	BioGRID, IntAct
PARP1	Reconstituted Complex	physical	11790116, (Europe PMC)	NA	BioGRID
PIN1	Affinity Capture-Western	physical	11326318, (Europe PMC)	NA	BioGRID
PMAIP1	Affinity Capture-Western, Protein-peptide, anti bait coimmunoprecipitation, pull down, surface plasmon resonance	direct interaction, physical, physical association	10807576, 15694340, 21454712, (Europe PMC)	0.52, 0.54	BioGRID, IntAct
PML	Affinity Capture-Western	physical	15231068, (Europe PMC)	NA	BioGRID
PPARA	Affinity Capture-Western, Biochemical Activity	physical	26556865, (Europe PMC)	NA	BioGRID
PPID	Affinity Capture-Western, Reconstituted Complex, Two-hybrid	physical	19228691, (Europe PMC)	NA	BioGRID
PPIF	two hybrid	physical association	19228691, (Europe PMC)	0.37	IntAct
PPP1CA	Affinity Capture-Western, antibody array	physical, physical association	17274640, (Europe PMC)	0.40	BioGRID, IntAct
PPP1CB	Affinity Capture-Western, antibody array	physical, physical association	17274640, (Europe PMC)	0.40	BioGRID, IntAct
PPP1CC	Affinity Capture-Western, antibody array	physical, physical association	17274640, (Europe PMC)	0.40	BioGRID, IntAct
PPP2CA	Affinity Capture-Western, Biochemical Activity, Reconstituted Complex, anti bait coimmunoprecipitation, experimental interaction detection	dephosphorylation reaction, physical, physical association	15225643, 9852076, (Europe PMC)	0.49	BioGRID, IntAct, MINT
PPP2R5A	Affinity Capture-Western	physical	11929874, (Europe PMC)	NA	BioGRID
PPP3CA	Affinity Capture-Western	physical	19706527, 9109491, (Europe PMC)	NA	BioGRID
PPP3CC	Reconstituted Complex	physical	15757646, (Europe PMC)	NA	BioGRID
PPP3R1	fluorescence microscopy, pull down	colocalization, direct interaction	15757646, (Europe PMC)	0.49	IntAct, MINT
PRKN	Affinity Capture-Western, Reconstituted Complex	physical	20889974, (Europe PMC)	NA	BioGRID
PSEN1	Affinity Capture-Western, Two-hybrid	physical	10521466, (Europe PMC)	NA	BioGRID
RAD9A	Affinity Capture-Western, Two-hybrid	physical	10620799, 18794804, (Europe PMC)	NA	BioGRID
RAF1	Affinity Capture-Western, Reconstituted Complex, Two-hybrid	physical	12488548, 15849194, 8929532, (Europe PMC)	NA	BioGRID
RRAS	Affinity Capture-Western, Two-hybrid	physical	8232588, (Europe PMC)	NA	BioGRID
RTL10	anti tag coimmunoprecipitation	association	23055042, (Europe PMC)	0.35	IntAct
RTN3	Affinity Capture-Western	physical	17191123, (Europe PMC)	NA	BioGRID
RTN4	Affinity Capture-Western, Two-hybrid	physical	11126360, 17191123, (Europe PMC)	NA	BioGRID
SEPT4	Affinity Capture-Western, PCA, Protein-peptide	physical	29020630, (Europe PMC)	NA	BioGRID
SERPINB8	Affinity Capture-Western	physical	15231068, (Europe PMC)	NA	BioGRID
SIVA1	pull down	physical association	14739602, (Europe PMC)	0.40	IntAct
SMN1	Affinity Capture-Western, Reconstituted Complex, Two-hybrid	physical	9389483, (Europe PMC)	NA	BioGRID
SOD1	Affinity Capture-Western, Reconstituted Complex	physical	15233914, (Europe PMC)	NA	BioGRID
SPNS1	Affinity Capture-Western, anti tag coimmunoprecipitation, confocal microscopy	colocalization, physical, physical association	12815463, (Europe PMC)	0.46	BioGRID, IntAct
SQSTM1	Affinity Capture-Western, Reconstituted Complex	physical	23564079, 25311206, (Europe PMC)	NA	BioGRID
TMBIM6	Affinity Capture-Western	physical	9660918, (Europe PMC)	NA	BioGRID
TOMM20	Reconstituted Complex	physical	9119086, (Europe PMC)	NA	BioGRID
TP53	Affinity Capture-Western, anti bait coimmunoprecipitation	association, physical, physical association	12667443, 19521340, 21597459, 21624955, (Europe PMC)	0.56	BioGRID, IntAct, MINT
TP53AIP1	Affinity Capture-Western	physical	12019168, (Europe PMC)	NA	BioGRID
TP53BP2	Protein-peptide, Reconstituted Complex, Two-hybrid, fluorescence technology, peptide array, proximity ligation assay, surface plasmon resonance	direct interaction, physical	18719108, 8668206, (Europe PMC)	0.65	BioGRID, IntAct
UBE2I	Affinity Capture-Western	physical	26416353, (Europe PMC)	NA	BioGRID
VDAC1	Affinity Capture-Western, anti bait coimmunoprecipitation	physical, physical association	19706527, (Europe PMC)	0.40	BioGRID, IntAct
VRK2	two hybrid	physical association	16963744, (Europe PMC)	0.37	IntAct
XIAP	Biochemical Activity, Reconstituted Complex	physical	29020630, (Europe PMC)	NA	BioGRID

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BCL2