Bcl-2-associated X Protein

Bcl-2-associated X Protein

Identifiers Symbols BAX; BCL2L4 External IDs OMIM: 600040 MGI: 99702 HomoloGene: 7242 ChEMBL: 5318 GeneCards: BAX Gene

Gene Ontology
Molecular function protein binding
lipid binding
channel activity
identical protein binding
protein homodimerization activity
protein heterodimerization activity
BH3 domain binding
Cellular component nucleus
mitochondrion
mitochondrial outer membrane
mitochondrial permeability transition pore complex
endoplasmic reticulum
endoplasmic reticulum membrane
cytosol
cytosolic part
pore complex
Bcl-2 family protein complex
Biological process response to acid
ovarian follicle development
neuron migration
T cell homeostatic proliferation
B cell homeostasis
B cell apoptotic process
kidney development
release of cytochrome c from mitochondria
protein insertion into mitochondrial membrane involved in apoptotic signaling pathway
blood vessel remodeling
myeloid cell homeostasis
B cell negative selection
B cell homeostatic proliferation
positive regulation of B cell apoptotic process
apoptotic DNA fragmentation
glycosphingolipid metabolic process
regulation of nitrogen utilization
apoptotic process
induction of apoptosis
activation of cysteine-type endopeptidase activity involved in apoptotic process
cleavage of lamin involved in execution phase of apoptosis
transformed cell apoptotic process
response to DNA damage stimulus
germ cell development
mitochondrial fusion
activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c
apoptotic mitochondrial changes
fertilization
response to toxin
response to salt stress
establishment or maintenance of transmembrane electrochemical gradient
response to gamma radiation
virus-host interaction
hypothalamus development
cerebral cortex development
nuclear fragmentation involved in apoptotic nuclear change
negative regulation of protein binding
positive regulation of protein oligomerization
reduction of endoplasmic reticulum calcium ion concentration
release of matrix enzymes from mitochondria
negative regulation of peptidyl-serine phosphorylation
regulation of mammary gland epithelial cell proliferation
cellular response to UV
limb morphogenesis
germ cell programmed cell death
odontogenesis of dentin-containing tooth
positive regulation of apoptotic process
regulation of protein homodimerization activity
regulation of protein heterodimerization activity
negative regulation of neuron apoptotic process
positive regulation of neuron apoptotic process
mitochondrial fragmentation involved in apoptotic process
development of secondary sexual characteristics
retinal cell programmed cell death
positive regulation of developmental pigmentation
negative regulation of fibroblast proliferation
spermatid differentiation
post-embryonic camera-type eye morphogenesis
response to axon injury
homeostasis of number of cells within a tissue
protein oligomerization
protein homooligomerization
positive regulation of release of sequestered calcium ion into cytosol
neuron apoptotic process
regulation of cell cycle
regulation of mitochondrial membrane potential
Sertoli cell proliferation
retina development in camera-type eye
positive regulation of apoptotic process involved in mammary gland involution
vagina development
intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress
cellular response to organic substance
positive regulation of release of cytochrome c from mitochondria
apoptotic signaling pathway
intrinsic apoptotic signaling pathway
positive regulation of endoplasmic reticulum unfolded protein response
positive regulation of intrinsic apoptotic signaling pathway
Sources: Amigo / QuickGO
RNA expression pattern More reference expression data Orthologs Species Human Mouse Entrez 581 12028 Ensembl ENSG00000087088 ENSMUSG00000003873 UniProt Q07812 Q07813 RefSeq (mRNA) NM_004324.3 NM_007527.3 RefSeq (protein) NP_004315.1 NP_031553.1 Location (UCSC) Chr 19:
49.46 – 49.47 Mb Chr 7:
45.46 – 45.47 Mb PubMed search

The Bcl-2–associated X protein, or Bax is a protein of the Bcl-2 gene family. It promotes apoptosis by competing with Bcl-2 proper.

The BAX gene was the first identified pro-apoptotic member of the Bcl-2 protein family. Bcl-2 family members share one or more of the four characteristic domains of homology entitled the Bcl-2 homology (BH) domains (named BH1, BH2, BH3 and BH4), and can form hetero- or homodimers. Bcl-2 proteins act as anti- or pro-apoptotic regulators that are involved in a wide variety of cellular activities. Orthologs of the BAX gene have been identified in most mammals for which complete genome data are available.

Bax is a pro-apoptotic Bcl-2 protein containing BH1, BH2 and BH3 domains. In healthy mammalian cells, the majority of BAX is found in the cytosol, but upon initiation of apoptotic signaling, Bax undergoes a conformation shift, and inserts into organelle membranes, primarily the outer mitochondrial membrane. Bax is believed to interact with, and induce the opening of the mitochondrial voltage-dependent anion channel, VDAC. Alternatively, growing evidence suggest that activated Bax and/or Bak form an oligomeric pore, MAC in the outer membrane. This results in the release of cytochrome c and other pro-apoptotic factors from the mitochondria, often referred to as mitochondrial outer membrane permeabilization, leading to activation of caspases. This defines a direct role for Bax in mitochondrial outer membrane permeabilization, a role common to the Bcl-2 proteins containing the BH1, BH2 and BH3 domains.

The expression of BAX is upregulated by the tumor suppressor protein p53, and BAX has been shown to be involved in p53-mediated apoptosis. The p53 protein is a transcription factor that, when activated as part of the cell's response to stress, regulates many downstream target genes, including BAX. Wild-type p53 has been demonstrated to upregulate the transcription of a chimeric reporter plasmid utilizing the consensus promoter sequence of BAX approximately 50-fold over mutant p53. Thus it is likely that p53 promotes BAX's apoptotic faculties in vivo as a primary transcription factor. However, p53 also has a transcription-independent role in apoptosis. In particular, p53 interacts with Bax, promoting its activation as well as its insertion into the mitochondrial membrane.

Read more about Bcl-2-associated X Protein:  Interactions

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