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Apoptosis regulator BAX

 BAX_MOUSE               Reviewed;         192 AA.
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
05-DEC-2018, entry version 190.
RecName: Full=Apoptosis regulator BAX;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
PubMed=8358790; DOI=10.1016/0092-8674(93)90509-O;
Oltvai Z.N., Milliman C.L., Korsmeyer S.J.;
"Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that
accelerates programmed cell death.";
Cell 74:609-619(1993).
STRAIN=FVB/N-3; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
PubMed=15383280; DOI=10.1016/j.molcel.2004.08.020;
Nam Y.J., Mani K., Ashton A.W., Peng C.F., Krishnamurthy B.,
Hayakawa Y., Lee P., Korsmeyer S.J., Kitsis R.N.;
"Inhibition of both the extrinsic and intrinsic death pathways through
nonhomotypic death-fold interactions.";
Mol. Cell 15:901-912(2004).
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
Cell 143:1174-1189(2010).
PubMed=18248095; DOI=10.1371/journal.ppat.0040025;
Ku B., Woo J.S., Liang C., Lee K.H., Hong H.S., E X., Kim K.S.,
Jung J.U., Oh B.H.;
"Structural and biochemical bases for the inhibition of autophagy and
apoptosis by viral BCL-2 of murine gamma-herpesvirus 68.";
PLoS Pathog. 4:E25-E25(2008).
PubMed=21060336; DOI=10.1038/cr.2010.149;
Ku B., Liang C., Jung J.U., Oh B.H.;
"Evidence that inhibition of BAX activation by BCL-2 involves its
tight and preferential interaction with the BH3 domain of BAX.";
Cell Res. 21:627-641(2011).
-!- FUNCTION: Accelerates programmed cell death by binding to, and
antagonizing the apoptosis repressor BCL2 or its adenovirus
homolog E1B 19k protein. Under stress conditions, undergoes a
conformation change that causes translocation to the mitochondrion
membrane, leading to the release of cytochrome c that then
triggers apoptosis. Promotes activation of CASP3, and thereby
apoptosis. BAX deficiency leads to lymphoid hyperplasia and male
sterility, because of the cessation of sperm production.
{ECO:0000269|PubMed:21060336, ECO:0000269|PubMed:8358790}.
-!- SUBUNIT: Homodimer. Forms higher oligomers under stress
conditions. Forms heterooligomers with BAK (By similarity).
Interacts with BCL2L11. Interaction with BCL2L11 promotes BAX
oligomerization and association with mitochondrial membranes, with
subsequent release of cytochrome c (PubMed:21060336). Forms
heterodimers with BCL2 (PubMed:8358790, PubMed:21060336). Forms
heterodimers with BCL2L1 isoform Bcl-X(L), BCL2L2, MCL1 and A1.
Interacts with SH3GLB1 and HN. Interacts with SFN and YWHAZ; the
interaction occurs in the cytoplasm. Under stress conditions, JNK-
mediated phosphorylation of SFN and YWHAZ, releases BAX to
mitochondria. Interacts with RNF144B, which regulates the
ubiquitin-dependent stability of BAX. Interacts with CLU under
stress conditions that cause a conformation change leading to BAX
oligomerization and association with mitochondria. Does not
interact with CLU in unstressed cells (By similarity). Interacts
with FAIM2/LFG2 (By similarity). Interacts with BOP (By
similarity). Interacts (via a C-terminal 33 residues) with NOL3
(via CARD domain); inhibits BAX activation and translocationand
consequently cytochrome c release from mitochondria
(PubMed:15383280). {ECO:0000250|UniProtKB:Q07812,
ECO:0000269|PubMed:15383280, ECO:0000269|PubMed:21060336,
-!- SUBUNIT: (Microbial infection) Interacts with gamma-herpesvirus 68
protein vBCL2. {ECO:0000269|PubMed:18248095}.
P10417:Bcl2; NbExp=2; IntAct=EBI-700711, EBI-526314;
O43521:BCL2L11 (xeno); NbExp=7; IntAct=EBI-15666406, EBI-526406;
O75460:ERN1 (xeno); NbExp=2; IntAct=EBI-700711, EBI-371750;
-!- SUBCELLULAR LOCATION: Isoform Alpha: Mitochondrion outer membrane
{ECO:0000250|UniProtKB:Q07812}; Single-pass membrane protein
{ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:Q07812}.
Note=Colocalizes with 14-3-3 proteins in the cytoplasm. Under
stress conditions, undergoes a conformation change that causes
release from JNK-phosphorylated 14-3-3 proteins and translocation
to the mitochondrion membrane (By similarity).
-!- SUBCELLULAR LOCATION: Isoform Beta: Cytoplasm {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform Gamma: Cytoplasm {ECO:0000250}.
Event=Alternative splicing; Named isoforms=3;
IsoId=Q07813-1; Sequence=Displayed;
IsoId=Q07813-2; Sequence=Not described;
IsoId=Q07813-3; Sequence=Not described;
-!- TISSUE SPECIFICITY: Expressed in a wide variety of tissues.
-!- DOMAIN: Intact BH3 motif is required by BIK, BID, BAK, BAD and BAX
for their pro-apoptotic activity and for their interaction with
anti-apoptotic members of the Bcl-2 family. {ECO:0000250}.
-!- SIMILARITY: Belongs to the Bcl-2 family. {ECO:0000305}.
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
EMBL; L22472; AAA03622.1; -; mRNA.
EMBL; BC018228; AAH18228.1; -; mRNA.
EMBL; BC053380; AAH53380.1; -; mRNA.
CCDS; CCDS21246.1; -. [Q07813-1]
PIR; D47538; D47538.
RefSeq; NP_031553.1; NM_007527.3. [Q07813-1]
UniGene; Mm.19904; -.
PDB; 2XA0; X-ray; 2.70 A; C/D=52-82.
PDB; 5W62; X-ray; 2.20 A; A=1-192.
PDBsum; 2XA0; -.
PDBsum; 5W62; -.
ProteinModelPortal; Q07813; -.
SMR; Q07813; -.
BioGrid; 198304; 23.
ComplexPortal; CPX-2031; BAX oligomer.
CORUM; Q07813; -.
DIP; DIP-29541N; -.
ELM; Q07813; -.
IntAct; Q07813; 12.
MINT; Q07813; -.
STRING; 10090.ENSMUSP00000033093; -.
ChEMBL; CHEMBL3414407; -.
iPTMnet; Q07813; -.
PhosphoSitePlus; Q07813; -.
SwissPalm; Q07813; -.
EPD; Q07813; -.
PaxDb; Q07813; -.
PeptideAtlas; Q07813; -.
PRIDE; Q07813; -.
TopDownProteomics; Q07813-1; -. [Q07813-1]
Ensembl; ENSMUST00000033093; ENSMUSP00000033093; ENSMUSG00000003873. [Q07813-1]
GeneID; 12028; -.
KEGG; mmu:12028; -.
UCSC; uc009gvh.1; mouse. [Q07813-1]
CTD; 581; -.
MGI; MGI:99702; Bax.
eggNOG; ENOG410IWQJ; Eukaryota.
eggNOG; ENOG4112738; LUCA.
GeneTree; ENSGT00730000111112; -.
HOGENOM; HOG000095178; -.
HOVERGEN; HBG003606; -.
InParanoid; Q07813; -.
KO; K02159; -.
OrthoDB; EOG091G0YWR; -.
PhylomeDB; Q07813; -.
TreeFam; TF315834; -.
Reactome; R-MMU-111457; Release of apoptotic factors from the mitochondria.
Reactome; R-MMU-114294; Activation, translocation and oligomerization of BAX.
Reactome; R-MMU-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
ChiTaRS; Bax; mouse.
PRO; PR:Q07813; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000003873; Expressed in 287 organ(s), highest expression level in fibroblast.
CleanEx; MM_BAX; -.
ExpressionAtlas; Q07813; baseline and differential.
Genevisible; Q07813; MM.
GO; GO:0097144; C:BAX complex; IPI:BHF-UCL.
GO; GO:0097136; C:Bcl-2 family protein complex; ISS:UniProtKB.
GO; GO:0071944; C:cell periphery; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:ParkinsonsUK-UCL.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; ISS:MGI.
GO; GO:0031966; C:mitochondrial membrane; IDA:MGI.
GO; GO:0005741; C:mitochondrial outer membrane; IDA:MGI.
GO; GO:0005757; C:mitochondrial permeability transition pore complex; ISS:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:ParkinsonsUK-UCL.
GO; GO:0005635; C:nuclear envelope; ISO:MGI.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
GO; GO:0046930; C:pore complex; ISS:UniProtKB.
GO; GO:0051400; F:BH domain binding; ISO:MGI.
GO; GO:0051434; F:BH3 domain binding; ISO:MGI.
GO; GO:0015267; F:channel activity; ISS:UniProtKB.
GO; GO:0051087; F:chaperone binding; IPI:ParkinsonsUK-UCL.
GO; GO:0031072; F:heat shock protein binding; ISO:MGI.
GO; GO:0030544; F:Hsp70 protein binding; IDA:ParkinsonsUK-UCL.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0008289; F:lipid binding; ISS:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IPI:MGI.
GO; GO:0042803; F:protein homodimerization activity; IMP:MGI.
GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
GO; GO:0008635; P:activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c; IDA:MGI.
GO; GO:0097296; P:activation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; IMP:MGI.
GO; GO:0008637; P:apoptotic mitochondrial changes; IDA:MGI.
GO; GO:0006915; P:apoptotic process; IDA:MGI.
GO; GO:1902262; P:apoptotic process involved in blood vessel morphogenesis; IGI:MGI.
GO; GO:1902263; P:apoptotic process involved in embryonic digit morphogenesis; IGI:MGI.
GO; GO:0097190; P:apoptotic signaling pathway; IMP:MGI.
GO; GO:0001783; P:B cell apoptotic process; IGI:MGI.
GO; GO:0001782; P:B cell homeostasis; IMP:MGI.
GO; GO:0002358; P:B cell homeostatic proliferation; IMP:MGI.
GO; GO:0002352; P:B cell negative selection; IGI:MGI.
GO; GO:1990117; P:B cell receptor apoptotic signaling pathway; ISO:MGI.
GO; GO:0001974; P:blood vessel remodeling; IGI:MGI.
GO; GO:0008283; P:cell proliferation; IDA:MGI.
GO; GO:0045333; P:cellular respiration; ISO:MGI.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:MGI.
GO; GO:0071310; P:cellular response to organic substance; IDA:MGI.
GO; GO:0034644; P:cellular response to UV; IGI:MGI.
GO; GO:0021987; P:cerebral cortex development; IMP:MGI.
GO; GO:0045136; P:development of secondary sexual characteristics; IMP:MGI.
GO; GO:0035234; P:ectopic germ cell programmed cell death; IMP:MGI.
GO; GO:0010248; P:establishment or maintenance of transmembrane electrochemical gradient; ISS:UniProtKB.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; ISO:MGI.
GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IGI:MGI.
GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IDA:MGI.
GO; GO:0009566; P:fertilization; IGI:MGI.
GO; GO:0007281; P:germ cell development; IGI:MGI.
GO; GO:0006687; P:glycosphingolipid metabolic process; IMP:MGI.
GO; GO:0048872; P:homeostasis of number of cells; IMP:MGI.
GO; GO:0048873; P:homeostasis of number of cells within a tissue; IMP:MGI.
GO; GO:0021854; P:hypothalamus development; IMP:MGI.
GO; GO:0007007; P:inner mitochondrial membrane organization; ISO:MGI.
GO; GO:0097193; P:intrinsic apoptotic signaling pathway; ISO:MGI.
GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; IMP:MGI.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IMP:MGI.
GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IGI:MGI.
GO; GO:0001822; P:kidney development; IGI:MGI.
GO; GO:0001776; P:leukocyte homeostasis; IGI:MGI.
GO; GO:0035108; P:limb morphogenesis; IGI:MGI.
GO; GO:0008584; P:male gonad development; IMP:MGI.
GO; GO:0043653; P:mitochondrial fragmentation involved in apoptotic process; ISS:UniProtKB.
GO; GO:0008053; P:mitochondrial fusion; IGI:MGI.
GO; GO:0070584; P:mitochondrion morphogenesis; IGI:MGI.
GO; GO:0002262; P:myeloid cell homeostasis; IGI:MGI.
GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IGI:MGI.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:MGI.
GO; GO:0032471; P:negative regulation of endoplasmic reticulum calcium ion concentration; IGI:MGI.
GO; GO:0048147; P:negative regulation of fibroblast proliferation; IMP:MGI.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IDA:MGI.
GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; IGI:MGI.
GO; GO:0032091; P:negative regulation of protein binding; ISS:UniProtKB.
GO; GO:0007399; P:nervous system development; IMP:MGI.
GO; GO:0051402; P:neuron apoptotic process; IMP:MGI.
GO; GO:0001764; P:neuron migration; IMP:MGI.
GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IGI:MGI.
GO; GO:0007008; P:outer mitochondrial membrane organization; ISO:MGI.
GO; GO:0001541; P:ovarian follicle development; IMP:MGI.
GO; GO:1902512; P:positive regulation of apoptotic DNA fragmentation; ISO:MGI.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:MGI.
GO; GO:0060058; P:positive regulation of apoptotic process involved in mammary gland involution; IMP:MGI.
GO; GO:0002904; P:positive regulation of B cell apoptotic process; IGI:MGI.
GO; GO:0010524; P:positive regulation of calcium ion transport into cytosol; IGI:MGI.
GO; GO:0048087; P:positive regulation of developmental pigmentation; IGI:MGI.
GO; GO:1900103; P:positive regulation of endoplasmic reticulum unfolded protein response; ISS:UniProtKB.
GO; GO:2001241; P:positive regulation of extrinsic apoptotic signaling pathway in absence of ligand; IDA:MGI.
GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IMP:MGI.
GO; GO:1902110; P:positive regulation of mitochondrial membrane permeability involved in apoptotic process; IGI:MGI.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IMP:UniProtKB.
GO; GO:0032461; P:positive regulation of protein oligomerization; ISS:UniProtKB.
GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; ISS:UniProtKB.
GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; IMP:MGI.
GO; GO:0048597; P:post-embryonic camera-type eye morphogenesis; IGI:MGI.
GO; GO:0009791; P:post-embryonic development; IGI:MGI.
GO; GO:0051259; P:protein complex oligomerization; ISO:MGI.
GO; GO:0051260; P:protein homooligomerization; IDA:MGI.
GO; GO:0001844; P:protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; IMP:MGI.
GO; GO:0051726; P:regulation of cell cycle; IGI:MGI.
GO; GO:0043281; P:regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:MGI.
GO; GO:0033599; P:regulation of mammary gland epithelial cell proliferation; IMP:MGI.
GO; GO:1902108; P:regulation of mitochondrial membrane permeability involved in apoptotic process; IGI:MGI.
GO; GO:1902445; P:regulation of mitochondrial membrane permeability involved in programmed necrotic cell death; IMP:MGI.
GO; GO:0043523; P:regulation of neuron apoptotic process; IMP:MGI.
GO; GO:0006808; P:regulation of nitrogen utilization; IGI:MGI.
GO; GO:0043497; P:regulation of protein heterodimerization activity; ISO:MGI.
GO; GO:0043496; P:regulation of protein homodimerization activity; ISS:UniProtKB.
GO; GO:0001836; P:release of cytochrome c from mitochondria; IDA:MGI.
GO; GO:0032976; P:release of matrix enzymes from mitochondria; ISS:UniProtKB.
GO; GO:0048678; P:response to axon injury; IMP:MGI.
GO; GO:0010332; P:response to gamma radiation; IMP:MGI.
GO; GO:0010212; P:response to ionizing radiation; IMP:MGI.
GO; GO:0009651; P:response to salt stress; IGI:MGI.
GO; GO:0009636; P:response to toxic substance; IMP:MGI.
GO; GO:0009611; P:response to wounding; IMP:MGI.
GO; GO:0060041; P:retina development in camera-type eye; IMP:MGI.
GO; GO:0046666; P:retinal cell programmed cell death; IMP:MGI.
GO; GO:0060011; P:Sertoli cell proliferation; IGI:MGI.
GO; GO:0007548; P:sex differentiation; IMP:MGI.
GO; GO:0048515; P:spermatid differentiation; IMP:MGI.
GO; GO:0007283; P:spermatogenesis; IMP:MGI.
GO; GO:0001777; P:T cell homeostatic proliferation; IMP:MGI.
GO; GO:0070242; P:thymocyte apoptotic process; IGI:MGI.
GO; GO:0060068; P:vagina development; IGI:MGI.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
Gene3D; 1.10.437.10; -; 1.
InterPro; IPR026304; BAX.
InterPro; IPR002475; Bcl2-like.
InterPro; IPR020717; Bcl2_BH1_motif_CS.
InterPro; IPR020726; Bcl2_BH2_motif_CS.
InterPro; IPR020728; Bcl2_BH3_motif_CS.
InterPro; IPR036834; Blc2-like_sf.
InterPro; IPR026298; Blc2_fam.
PANTHER; PTHR11256; PTHR11256; 1.
PANTHER; PTHR11256:SF42; PTHR11256:SF42; 1.
Pfam; PF00452; Bcl-2; 1.
SUPFAM; SSF56854; SSF56854; 1.
PROSITE; PS01080; BH1; 1.
PROSITE; PS01258; BH2; 1.
PROSITE; PS01259; BH3; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Apoptosis;
Complete proteome; Cytoplasm; Host-virus interaction; Membrane;
Mitochondrion; Mitochondrion outer membrane; Reference proteome;
Transmembrane; Transmembrane helix.
CHAIN 1 192 Apoptosis regulator BAX.
TRANSMEM 172 192 Helical. {ECO:0000255}.
MOTIF 59 73 BH3.
MOTIF 98 118 BH1.
MOTIF 150 165 BH2.
MOD_RES 1 1 N-acetylmethionine.
HELIX 16 34 {ECO:0000244|PDB:5W62}.
HELIX 54 70 {ECO:0000244|PDB:5W62}.
HELIX 74 81 {ECO:0000244|PDB:5W62}.
HELIX 88 99 {ECO:0000244|PDB:5W62}.
TURN 100 102 {ECO:0000244|PDB:5W62}.
HELIX 107 124 {ECO:0000244|PDB:5W62}.
HELIX 131 147 {ECO:0000244|PDB:5W62}.
HELIX 149 154 {ECO:0000244|PDB:5W62}.
TURN 155 158 {ECO:0000244|PDB:5W62}.
HELIX 159 165 {ECO:0000244|PDB:5W62}.
HELIX 170 172 {ECO:0000244|PDB:5W62}.
HELIX 173 188 {ECO:0000244|PDB:5W62}.
SEQUENCE 192 AA; 21395 MW; D2E0B3566579FAFF CRC64;

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