Gene Report

Basic Information

Approved Symbol	BAX
Approved Name	BCL2-associated X protein
Symbol Alias	BCL2L4
Location	19q13.3-q13.4
Position	chr19:49458117-49465055 (+)
External Links	Entrez Gene: 581 Ensembl: ENSG00000087088 UCSC: uc002plf.1 HGNC ID: 959
No. of Studies (Positive/Negative)	1(1/0)
Type	Literature-origin

Positive relationships between BAX and MDD (count: 0)

Positive relationships between BAX and other components at different levels (count: 1)

Genetic/epigenetic locus					Protein and other molecule			Cell and molecular pathway			Neural system			Cognition and behavior		Symptoms and signs			Environment

Name in Literature	Level	Approved Name (Name in Literature)	Type	Reference	Research Type	Statistical Result	Relation Description	All
Name in Literature	Related Components
Bax		Stress(stress)	environment	Wang, 2011	animal model		In CMS, there was an increased Bax level in both the hippoca...... In CMS, there was an increased Bax level in both the hippocampus and myocardium. More...

Positive relationship network of BAX in MK4MDD

Network loading ...

Note:
1. The different color of the nodes denotes the level of the nodes.

Genetic/Epigenetic Locus	Protein and Other Molecule	Cell and Molecular Pathway	Neural System	Cognition and Behavior	Symptoms and Signs	Environment	MDD

2. Besides the component related relationships from literature, gene mapped protein and protein mapped gene are also shown in the network. If the mapped gene or protein is not from literature, square node would be used instead of Circle node. Accordingly, the relationship is marked with dot line.
2. User can drag the nodes to rearrange the layout of the network. Click the node will enter the report page of the node. Right-click will show also the menus to link to the report page of the node and remove the node and related edges. Hover the node will show the level of the node and hover the edge will show the evidence/description of the edge.
3. The network is generated using Cytoscape Web

Negative relationships between BAX and MDD (count: 0)

Negative relationships between BAX and other components at different levels (count: 0)

BAX related SNPs in MK4MDD (count: 0)

BAX related proteins in MK4MDD (count: 1)

Approved Name	UniportKB	No. of Studies (Positive/Negative)	Source
Apoptosis regulator BAX	Q07812	0(0/0)	Gene mapped

BAX related GO terms (count: 95)

ID	Name	Type	Evidence
Literature-origin GO terms
GO:0006915	apoptotic process	biological process	IDA[9219694]; TAS

ID	Name	Type	Evidence
Gene mapped GO terms
GO:0009566	fertilization	biological process	IEA
GO:0005757	mitochondrial permeability transition pore complex	cellular component	IDA[9843949]
GO:0044445	cytosolic part	cellular component	IEA
GO:0001777	T cell homeostatic proliferation	biological process	IEA
GO:1990009	retinal cell apoptotic process	biological process	IMP[10702418]
GO:0051259	protein oligomerization	biological process	IDA[19074440]
GO:0007281	germ cell development	biological process	IEA
GO:0035234	germ cell programmed cell death	biological process	IEA
GO:0006808	regulation of nitrogen utilization	biological process	IEA
GO:0001836	release of cytochrome c from mitochondria	biological process	IDA[9843949]
GO:0001822	kidney development	biological process	IEA
GO:0042803	protein homodimerization activity	molecular function	IDA[16608847]; IPI[9111042]
GO:0002352	B cell negative selection	biological process	IEA
GO:0002262	myeloid cell homeostasis	biological process	IEA
GO:0043653	mitochondrial fragmentation involved in apoptotic process	biological process	IDA[12499352]
GO:0002904	positive regulation of B cell apoptotic process	biological process	IEA
GO:0010332	response to gamma radiation	biological process	IEA
GO:0005789	endoplasmic reticulum membrane	cellular component	IDA[16424160]
GO:0008637	apoptotic mitochondrial changes	biological process	IDA[9843949]
GO:0045136	development of secondary sexual characteristics	biological process	IEA
GO:0097193	intrinsic apoptotic signaling pathway	biological process	IDA[16462759]
GO:0033137	negative regulation of peptidyl-serine phosphorylation	biological process	IEA
GO:0048597	post-embryonic camera-type eye morphogenesis	biological process	IEA
GO:0060068	vagina development	biological process	IEA
GO:0009636	response to toxin	biological process	IDA[16307838]
GO:0030264	nuclear fragmentation involved in apoptotic nuclear change	biological process	IMP[11350920]
GO:0001782	B cell homeostasis	biological process	IEA
GO:0008635	activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c	biological process	IDA[15214043]
GO:0032976	release of matrix enzymes from mitochondria	biological process	IDA[9843949]
GO:0046982	protein heterodimerization activity	molecular function	IPI[9111042]
GO:0043496	regulation of protein homodimerization activity	biological process	IDA[9111042]
GO:0048678	response to axon injury	biological process	IEA
GO:0006974	response to DNA damage stimulus	biological process	IEA
GO:0048515	spermatid differentiation	biological process	IEA
GO:0043497	regulation of protein heterodimerization activity	biological process	IPI[9111042]
GO:0035108	limb morphogenesis	biological process	IEA
GO:1900103	positive regulation of endoplasmic reticulum unfolded protein response	biological process	IMP[16645094]
GO:0001541	ovarian follicle development	biological process	IEA
GO:0046666	retinal cell programmed cell death	biological process	IEA
GO:0008289	lipid binding	molecular function	IDA[14522999]
GO:0048087	positive regulation of developmental pigmentation	biological process	IEA
GO:0005515	protein binding	molecular function	IPI[16113678]
GO:0032091	negative regulation of protein binding	biological process	IDA[9388232]
GO:0097136	Bcl-2 family protein complex	cellular component	IDA
GO:0071310	cellular response to organic substance	biological process	IEA
GO:0060011	Sertoli cell proliferation	biological process	IEA
GO:0005634	nucleus	cellular component	IMP[15102863]
GO:0001974	blood vessel remodeling	biological process	IEA
GO:0043525	positive regulation of neuron apoptotic process	biological process	IDA[15637643]
GO:0009651	response to salt stress	biological process	IEA
GO:0010248	establishment or maintenance of transmembrane electrochemical gradient	biological process	IDA[9843949]
GO:0048147	negative regulation of fibroblast proliferation	biological process	IEA
GO:0001101	response to acid	biological process	IEA
GO:0001844	protein insertion into mitochondrial membrane involved in apoptotic signaling pathway	biological process	IEA
GO:0005739	mitochondrion	cellular component	IDA[17823127]
GO:0051434	BH3 domain binding	molecular function	IDA; IPI[17052454]
GO:0033599	regulation of mammary gland epithelial cell proliferation	biological process	IEA
GO:0060058	positive regulation of apoptotic process involved in mammary gland involution	biological process	IEA
GO:0042802	identical protein binding	molecular function	IPI[16113678]
GO:0005783	endoplasmic reticulum	cellular component	IDA[16424160]
GO:0006309	apoptotic DNA fragmentation	biological process	IMP[11350920]
GO:0005741	mitochondrial outer membrane	cellular component	TAS
GO:2001244	positive regulation of intrinsic apoptotic signaling pathway	biological process	IMP[14963330]
GO:0019048	virus-host interaction	biological process	IEA
GO:0043065	positive regulation of apoptotic process	biological process	IMP[17289999]
GO:0032461	positive regulation of protein oligomerization	biological process	IDA[19805544]
GO:0042475	odontogenesis of dentin-containing tooth	biological process	IEA
GO:0051402	neuron apoptotic process	biological process	IEA
GO:0006917	induction of apoptosis	biological process	IDA[11912183]; IMP[11350920]; NAS[9920818]
GO:0006927	transformed cell apoptotic process	biological process	IMP[10739008]
GO:0006922	cleavage of lamin involved in execution phase of apoptosis	biological process	IMP[11350920]
GO:0006919	activation of cysteine-type endopeptidase activity involved in apoptotic process	biological process	IDA[11912183]; IMP[11350920]
GO:0001783	B cell apoptotic process	biological process	IDA[16424160]
GO:0002358	B cell homeostatic proliferation	biological process	IEA
GO:0043524	negative regulation of neuron apoptotic process	biological process	IEA
GO:0051281	positive regulation of release of sequestered calcium ion into cytosol	biological process	IEA
GO:0008053	mitochondrial fusion	biological process	IDA[14769861]
GO:0005829	cytosol	cellular component	IDA[17823127]; TAS
GO:0070059	intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress	biological process	IMP[16645094]
GO:0006687	glycosphingolipid metabolic process	biological process	IEA
GO:0097190	apoptotic signaling pathway	biological process	IDA[16424160]
GO:0046930	pore complex	cellular component	IDA[9219694]
GO:0021987	cerebral cortex development	biological process	IEA
GO:0051260	protein homooligomerization	biological process	IDA[14522999]
GO:0015267	channel activity	molecular function	IDA[9219694]
GO:0090200	positive regulation of release of cytochrome c from mitochondria	biological process	IDA[14963330]
GO:0032471	reduction of endoplasmic reticulum calcium ion concentration	biological process	IEA
GO:0021854	hypothalamus development	biological process	IEA
GO:0060041	retina development in camera-type eye	biological process	IEA
GO:0051881	regulation of mitochondrial membrane potential	biological process	IDA[9843949]
GO:0034644	cellular response to UV	biological process	IEA
GO:0051726	regulation of cell cycle	biological process	IEA
GO:0001764	neuron migration	biological process	IEA
GO:0048873	homeostasis of number of cells within a tissue	biological process	IEA

BAX related KEGG pathways (count: 8)

ID	Name	Brief Description	Full Description
Gene mapped KEGG pathways
hsa05200	pathways in_cancer	Pathways in cancer
hsa05014	amyotrophic lateral_sclerosis_als	Amyotrophic lateral sclerosis (ALS)	Amyotrophic lateral sclerosis (ALS) is a progressive, lethal...... 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 amyotrophic lateral sclerosis (FALS) cases, may be toxic because it 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) via aberrant superoxide chemistry. These changes may then result in abnormal mitochondrial energy metabolism, Ca2+ handling, and release of pro-apoptotic factors. 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 causes neurotoxicity by increasing intracellular calcium, which enhances oxidative stress and mitochondrial damage. Mutant SOD1 can also trigger oxidative reactions by various means including by increasing levels of peroxynitrite, which can then cause damage through the formation of hydroxyl radicals or via nitration of tyrosine residues on proteins. Nitration may target neurofilament proteins, disrupting their phosphorylation and affecting axonal transport. Collectively, these mechanisms (or a combination thereof) are predicted to disturb cellular homeostasis (within glial and/or motor neurons), ultimately triggering motor neuron death. More...
hsa05016	huntingtons disease	Huntington's disease	Huntington disease (HD) is an autosomal-dominant neurodegene...... Huntington disease (HD) is an autosomal-dominant neurodegenerative disorder that primarily affects medium spiny striatal neurons (MSN). HD is caused by a CAG repeat expansion in the IT15 gene, which results in a long stretch of polyglutamine close to the amino-terminus of the HD protein huntingtin (Htt). Mutant Htt (mHtt) has effects both in the cytoplasm and in the nucleus. In the cytoplasm, full-length mHtt can interfere with BDNF vesicular transport on microtubules. This mutant protein also may lead to abnormal endocytosis and secretion in neurons, because normal Htt form a complex with the proteins Hip1, clathrin and AP2 that are involved in endocytosis. In addition, mHtt affects Ca2+ signaling by sensitizing InsP3R1 to activation by InsP3, stimulating NR2B/NR1 NMDAR activity, and destabilizing mitochondrial Ca2+ handling. As a result, stimulation of glutamate receptors leads to supranormal Ca2+ responses in HD MSN and mitochondrial Ca2+ overload. The mHtt translocates to the nucleus, where it forms intranuclear inclusions, though they are not primarily responsible for toxicity. Nuclear toxicity is believed to be caused by interference with gene transcription, leading to loss of transcription of neuroprotective molecules such as BDNF. While mHtt binds to p53 and upregulates levels of nuclear p53 as well as p53 transcriptional activity. Augmented p53 mediates mitochondrial dysfunction. More...
hsa05210	colorectal cancer	Colorectal cancer	Classically, colorectal cancer (CRC) has been believed to de...... Classically, colorectal cancer (CRC) has been believed to develop from normal mucosa through the premalignant adenoma by the step-wise accumulation of mutations. All CRC display either microsatellite instability (MSI) or chromosome instability (CIN). MSI occurs in 15% of colon cancers and results from inactivation of the DNA mismatch repair (MMR) system by either MMR gene mutations or hypermethylation of the MLH1 promoter. MSI promotes tumorigenesis through generating mutations in target genes that possess coding microsatellite repeats, such as beta-catenin, TGFBR2 and BAX. CIN is found in the majority of colon cancers and leads to a different pattern of gene alterations that contribute to tumor formation. Genes involved in CIN are those coding for APC, K-ras, SMAD4 and p53. More...
hsa04210	apoptosis	Apoptosis	Apoptosis is a genetically controlled mechanisms of cell dea...... Apoptosis is a genetically controlled mechanisms of cell death involved in the regulation of tissue homeostasis. The 2 major pathways of apoptosis are the extrinsic (Fas and other TNFR superfamily members and ligands) and the intrinsic (mitochondria-associated) pathways, both of which are found in the cytoplasm. The extrinsic pathway is triggered by death receptor engagement, which initiates a signaling cascade mediated by caspase-8 activation. Caspase-8 both feeds directly into caspase-3 activation and stimulates the release of cytochrome c by the mitochondria. Caspase-3 activation leads to the degradation of cellular proteins necessary to maintain cell survival and integrity. The intrinsic pathway occurs when various apoptotic stimuli trigger the release of cytochrome c from the mitochondria (independently of caspase-8 activation). Cytochrome c interacts with Apaf-1 and caspase-9 to promote the activation of caspase-3. Recent studies point to the ER as a third subcellular compartment implicated in apoptotic execution. Alterations in Ca2+ homeostasis and accumulation of misfolded proteins in the ER cause ER stress. Prolonged ER stress can result in the activation of BAD and/or caspase-12, and execute apoptosis. More...
hsa04115	p53 signaling_pathway	p53 signaling pathway	p53 activation is induced by a number of stress signals, inc...... 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. More...
hsa05020	prion diseases	Prion diseases	Prion diseases, also termed transmissible spongiform encepha...... Prion diseases, also termed transmissible spongiform encephalopathies (TSEs), are a group of fatal neurodegenerative diseases that affect humans and a number of other animal species. The etiology of these diseases is thought to be associated with the conversion of a normal protein, PrPC, into an infectious, pathogenic form, PrPSc. The conversion is induced by prion infections (for example, variant Creutzfeldt-Jakob disease (vCJD), iatrogenic CJD, Kuru), mutations (familial CJD, Gerstmann-Straussler-Scheinker syndrome, fatal familial insomnia (FFI)) or unknown factors (sporadic CJD (sCJD)), and is thought to occur after PrPC has reached the plasma membrane or is re-internalized for degradation. The PrPSc form shows greater protease resistance than PrPC and accumulates in affected individuals, often in the form of extracellular plaques. Pathways that may lead to neuronal death comprise oxidative stress, regulated activation of complement, ubiquitin-proteasome and endosomal-lysosomal systems, synaptic alterations and dendritic atrophy, corticosteroid response, and endoplasmic reticulum stress. In addition, the conformational transition could lead to the lost of a beneficial activity of the natively folded protein, PrPC. More...
hsa04722	neurotrophin signaling_pathway	Neurotrophin signaling pathway	Neurotrophins are a family of trophic factors involved in di...... 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. More...

BAX related BioCarta pathways (count: 6)

ID	Name	Brief Description	Full Description
Gene mapped BioCarta pathways
MITOCHONDRIA_PATHWAY	mitochondria pathway	Role of Mitochondria in Apoptotic Signaling	Mitochondria participate in apoptotic signaling pathways thr...... Mitochondria participate in apoptotic signaling pathways through the release of mitochondrial proteins into the cytoplasm. Cytochrome c, a key protein in electron transport, is released from mitochondria in response to apoptotic signals, and activates Apaf-1, a protease released from mitochondria. Activated Apaf-1 activates caspase-9 and the rest of the caspase pathway. Smac/DIABLO is released from mitochondria and inhibits IAP proteins that normally interact with caspase-9 to inhibit apoptosis. Apoptosis regulation by Bcl-2 family proteins occurs as family members form complexes that enter the mitochondrial membrane, regulating the release of cytochrome c and other proteins. TNF family receptor that cause apoptosis directly activate the caspase cascade, but can also activate Bid, a Bcl-2 family member, which activates mitochondria-mediated apoptosis. Bax, another Bcl-2 family member, is activated by this pathway to localize to the mitochondrial membrane and increase its permeability, releasing cytochre c and other mitochondrial proteins. Bcl-2 and Bcl-xL prevent pore formation, blocking apoptosis. AIF (Apoptosis inducing factor) is another mitochondrial factor that is released into the cytoplasm to induce apoptosis. AIF-induced apoptosis is important during development but is not caspase dependent. More...
CHEMICAL_PATHWAY	chemical pathway	Apoptotic Signaling in Response to DNA Damage	The cellular activation of the caspase cascade resulting in ...... The cellular activation of the caspase cascade resulting in cell death is triggered by chemical damage to DNA which stimulates a sequence resulting in the cleavage of Bid in a manner similar to the binding of so called death-receptors or directly initiates the permeability transition of the mitochondrial membrane. The permiability transition releases several factors including cytochrome c, AIF and other factors in to the cytoplasm. Cytochrome c, a key protein in electron transport, is released from mitochondria in response to apoptotic signals, and activates Apaf-1, a protease released from mitochondria. Activated Apaf-1 activates caspase-9 and the rest of the caspase cascade. The caspases are a class of cysteine proteases that includes several representatives involved in apoptosis. The caspases convey the apoptotic signal in a proteolytic cascade, with caspases cleaving and activating other caspases that then degrade other cellular targets that lead to cell death. More...
BAD_PATHWAY	bad pathway	Regulation of BAD phosphorylation	The function of the pro-apoptotic molecule BAD is regulated ...... The function of the pro-apoptotic molecule BAD is regulated by phosphorylation of three sites (ser 112,136 and 155). Phosphorylation at these sites results in loss of the ability of BAD to heterodimerize with the survival proteins BCL-XL or BCL-2. Phosphorylated BAD binds to 14-3-3 and is sequestered in the cytoplasm. While ser-136 phosphorylation is concordant with the activation of Akt, Ser-112 phosphorylation requires activation of the Ras-MAPK pathway. BAD Ser 155 was found to be a major site of phosphorylation induced following stimulation by growth factors and prevented by protein kinase A inhibitors. More...
P53HYPOXIA_PATHWAY	p53hypoxia pathway	Hypoxia and p53 in the Cardiovascular system	Hypoxic stress, like DNA damage, induces p53 protein accumul...... Hypoxic stress, like DNA damage, induces p53 protein accumulation and p53-dependent apoptosis in oncogenically transformed cells. Unlike DNA damage, hypoxia does not induce p53-dependent cell cycle arrest, suggesting that p53 activity is differentially regulated by these two stresses. Hypoxia induces p53 protein accumulation, but in contrast to DNA damage, hypoxia fails to induce endogenous downstream p53 effector mRNAs and proteins, such as p21, Bax, CIP1, WAF1 etc. Hypoxia does not inhibit the induction of p53 target genes by ionizing radiation, indicating that p53-dependent transactivation requires a DNA damage-inducible signal that is lacking under hypoxic treatment alone. The phosphatidylinositol 3-OH-kinase-Akt pathway inhibits p53-mediated transcription and apoptosis. Mdm2, a ubiquitin ligase for p53, plays a central role in regulation of the stability of p53 and serves as a good substrate for Akt. Mdm-2 targets the p53 tumor suppressor for ubiquitin-dependent degradation by the proteasome, but, in addition, the p53 transcription factor induces Mdm-2, thus, establishing a feedback loop. Hypoxia or DNA damage by abrogating binding of HIF-1 with VHL and p53 with Mdm-2, respectively, leads to stabilization and accumulation transcriptionally active HIF-1 and p53. At the molecular level, DNA damage induces the interaction of p53 with the transcriptional activator p300 as well as with the transcriptional corepressor mSin3A. In contrast, hypoxia primarily induces an interaction of p53 with mSin3A, but not with p300. More...
CERAMIDE_PATHWAY	ceramide pathway	Ceramide Signaling Pathway	Over 1,000 papers and reviews have been written about the ro...... Over 1,000 papers and reviews have been written about the role of ceramide in the production of programmed cell death or apoptosis. Ceramide is a sphingosine-based lipid-signaling molecule involved in the regulation of cellular differentiation, proliferation, and apoptosis. This diagram represents some of the current understanding of the cascades that couple ceramide to specific signaling pathways. These cascades illustrate that ceramide can be a growth stimulus or proapototic signal. The ultimate ceramide action is determined within the context of other stimuli and by the subcellular topology of its production and is cell-type specific. There are 2 forms of sphingomyelinase, acid (acid-sphingomyelinase:A-SMase) and neutral (neutral-sphingomyelinase N-SMase), that can produce ceramide. TNF-alpha can stimulate either form of sphingomyelinase as can other death receptors. Different domanis of TNF-alpha stimulate the different Smases. N-SMase stimulation is enhanced by the receptor for activated-C kinase 1 (RACK1). The activity of each form is dependent on the local intracellular pH. In the illustration the forms are seperated to reduce confusion however ceramide produced by either method can stimulate either cascade depending on the presence of specific co-factors and activators. A-SMase has been recognized as one of the required molecules to mediate proapoptotic signalling in cell death induced by a diverse array of stresses such as H2O2, Heat, UV exposure and Radiation. ROS generation in mitochondria activates caspase-3 via cooperation of cytochrome c, Aif and caspase-9 and stimulates or increases ceramide generation through A-SMase in a proaptotic activation cycle. Caspase-3 further increases its own activation by proteolytically cleaving ceramide inhibited catalase which is an inhibitor of ROS generation. Ceramide-activated protein kinase(CARK) also known as Kinase Supressor of RAS (KSR) activity is in some cases the switch point in the balance between proapoptotic and antiapoptotic signals and is also cell-type specific. In endothelial cells for example the activation of KSR is required for apoptosis. In contrast in epithelial cells activation of KSR is required for cell proliferation. An additional switch point is the availability of Bad in the cell. Activation of KSR leads to further mitocondrial stimulation or association with RAS and activation of the Raf1 cascade leading to proliferation or differentiation. More...
P53_PATHWAY	p53 pathway	p53 Signaling Pathway	p53 is a transcription factor who's activity is regulated by...... p53 is a transcription factor who's activity is regulated by phosphorylation. The function is p53 is to keep the cell from progressing through the cell cycle if there is damage to DNA present. It may do this in multiple ways from holding the cell at a checkpoint until repairs can be made to causing the cell to enter apoptosis if the damage cannot be repaired. The critical role of p53 is evidenced by the fact that it is mutated in a very large fraction of tumors from nearly all sources. More...

BAX related Reactome pathways (count: 2)

ID	Name	Description
Gene mapped Reactome pathways
REACT_578	apoptosis	Apoptosis is a distinct form of cell death that is functiona...... Apoptosis is a distinct form of cell death that is functionally and morphologically different from necrosis. Nuclear chromatin condensation, cytoplasmic shrinking, dilated endoplasmic reticulum, and membrane blebbing characterize apoptosis in general. Mitochondria remain morphologically unchanged. In 1972 Kerr et al introduced the concept of apoptosis as a distinct form of cell-death, and the mechanisms of various apoptotic pathways are still being revealed today. The two principal pathways of apoptosis are (1) the Bcl-2 inhibitable or intrinsic pathway induced by various forms of stress like intracellular damage, developmental cues, and external stimuli and (2) the caspase 8/10 dependent or extrinsic pathway initiated by the engagement of death receptors The caspase 8/10 dependent or extrinsic pathway is a death receptor mediated mechanism that results in the activation of caspase-8 and caspase-10. Activation of death receptors like Fas/CD95, TNFR1, and the TRAIL receptor is promoted by the TNF family of ligands including FASL (APO1L OR CD95L), TNF, LT-alpha, LT-beta, CD40L, LIGHT, RANKL, BLYS/BAFF, and APO2L/TRAIL. These ligands are released in response to microbial infection, or as part of the cellular, humoral immunity responses during the formation of lymphoid organs, activation of dendritic cells, stimulation or survival of T, B, and natural killer (NK) cells, cytotoxic response to viral infection or oncogenic transformation. The Bcl-2 inhibitable or intrinsic pathway of apoptosis is a stress-inducible process, and acts through the activation of caspase-9 via Apaf-1 and cytochrome c. The rupture of the mitochondrial membrane, a rapid process involving some of the Bcl-2 family proteins, releases these molecules into the cytoplasm. Examples of cellular processes that may induce the intrinsic pathway in response to various damage signals include: auto reactivity in lymphocytes, cytokine deprivation, calcium flux or cellular damage by cytotoxic drugs like taxol, deprivation of nutrients like glucose and growth factors like EGF, anoikis, transactivation of target genes by tumor suppressors including p53. In many non-immune cells, death signals initiated by the extrinsic pathway are amplified by connections to the intrinsic pathway. The connecting link appears to be the truncated BID (tBID) protein a proteolytic cleavage product mediated by caspase-8 or other enzymes. More...
REACT_964	intrinsic pathway_for_apoptosis	The intrinsic (Bcl-2 inhibitable or mitochondrial) pathway o...... The intrinsic (Bcl-2 inhibitable or mitochondrial) pathway of apoptosis functions in response to various types of intracellular stress including growth factor withdrawal, DNA damage, unfolding stresses in the endoplasmic reticulum and death receptor stimulation. Following the reception of stress signals, proapoptotic BCL-2 family proteins are activated and subsequently interact with and inactivate antiapoptotic BCL-2 proteins. This interaction leads to the destabilization of the mitochondrial membrane and release of apoptotic factors. These factors induce the caspase proteolytic cascade, chromatin condensation, and DNA fragmentation, ultimately leading to cell death. The key players in the Intrinsic pathway are the Bcl-2 family of proteins that are critical death regulators residing immediately upstream of mitochondria. The Bcl-2 family consists of both anti- and proapoptotic members that possess conserved alpha-helices with sequence conservation clustered in BCL-2 Homology (BH) domains. Proapoptotic members are organized as follows: 1. Multidomain BAX family proteins such as BAX, BAK etc. that display sequence conservation in their BH1-3 regions. These proteins act downstream in mitochondrial disruption. 2. BH3-only proteins such as BID,BAD, NOXA, PUMA,BIM, and BMF have only the short BH3 motif. These act upstream in the pathway, detecting developmental death cues or intracellular damage. Anti-apoptotic members like Bcl-2, Bcl-XL and their relatives exhibit homology in all segments BH1-4. One of the critical functions of BCL-2/BCL-XL proteins is to maintain the integrity of the mitochondrial outer membrane. More...

BAX related interactors from protein-protein interaction data in HPRD (count: 19)

Gene	Interactor	Interactor in MK4MDD?	Experiment Type	PMID
BAX	BCL2	No	in vitro;in vivo;yeast 2-hybrid	9111042 , 8358790 , 9463381 , 16642033 , 17097560 , 15231068
BAX	BAK1	No	in vivo	11571294
BAX	SFN	No	in vivo	11574543
BAX	PPP1CA	No	in vitro;in vivo	17274640
BAX	BCL2L1	Yes	in vitro;in vivo;yeast 2-hybrid	11283018 , 9111042 , 9153240 , 9742125 , 15131699
BAX	BCL2L10	No	in vivo	11278245
BAX	PMAIP1	No	in vivo	15705586
BAX	NOL3	No	in vivo	15383280
BAX	MOAP1	No	in vitro;in vivo	11060313
BAX	YWHAQ	No	in vitro;in vivo	12426317
BAX	BCL2A1	No	in vivo;yeast 2-hybrid	10753914
BAX	VDAC1	No	in vitro	12767928 , 9843949
BAX	BID	No	in vivo;yeast 2-hybrid	15574335
BAX	ERN1	No	in vitro;in vivo	16645094
BAX	KCNA3	No	in vivo	18818304
BAX	SH3GLB1	No	in vitro;in vivo;yeast 2-hybrid	11259440 , 11161816
BAX	SLC25A4	No	in vivo;yeast 2-hybrid	9748162
BAX	BBC3	No	yeast 2-hybrid	15574335
BAX	MCL1	No	in vitro	10837489 , 15077116

Gene Report

Literature-origin GO terms

Gene mapped GO terms

Gene mapped KEGG pathways

Gene mapped BioCarta pathways

Gene mapped Reactome pathways