ID BAX_HUMAN Reviewed; 192 AA. AC Q07812; A8K4W1; P55269; Q07814; Q07815; Q8WZ49; Q9NR76; Q9NYG7; Q9UCZ6; AC Q9UCZ7; Q9UQD6; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 10-JUN-2026, entry version 247. DE RecName: Full=Apoptosis regulator BAX; DE AltName: Full=Bcl-2-like protein 4; DE Short=Bcl2-L-4; GN Name=BAX; Synonyms=BCL2L4; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA; BETA AND GAMMA), FUNCTION, RP SUBUNIT, AND SUBCELLULAR LOCATION. RC TISSUE=B-cell; RX PubMed=8358790; DOI=10.1016/0092-8674(93)90509-o; RA Oltvai Z.N., Milliman C.L., Korsmeyer S.J.; RT "Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that RT accelerates programmed cell death."; RL Cell 74:609-619(1993). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DELTA). RX PubMed=7607685; DOI=10.1016/0888-7543(95)80180-t; RA Apte S.S., Mattei M.-G., Olsen B.R.; RT "Mapping of the human BAX gene to chromosome 19q13.3-q13.4 and isolation of RT a novel alternatively spliced transcript, BAX delta."; RL Genomics 26:592-594(1995). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM EPSILON). RC TISSUE=Brain; RX PubMed=9920818; DOI=10.1006/bbrc.1998.0130; RA Shi B., Triebe D., Kajiji S., Iwata K.K., Bruskin A., Mahajna J.; RT "Identification and characterization of baxepsilon, a novel bax variant RT missing the BH2 and the transmembrane domains."; RL Biochem. Biophys. Res. Commun. 254:779-785(1999). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND SIGMA), FUNCTION, RP INTERACTION WITH BCL2A1 AND BCL2L1, AND TISSUE SPECIFICITY. RX PubMed=10772918; DOI=10.1006/bbrc.2000.2537; RA Schmitt E., Paquet C., Beauchemin M., Dever-Bertrand J., Bertrand R.; RT "Characterization of Bax-sigma, a cell death-inducing isoform of Bax."; RL Biochem. Biophys. Res. Commun. 270:868-879(2000). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PSI), AND TISSUE SPECIFICITY. RX PubMed=11912183; DOI=10.1093/hmg/11.6.675; RA Cartron P.F., Oliver L., Martin S., Moreau C., LeCabellec M.T., RA Jezequel P., Meflah K., Vallette F.M.; RT "The expression of a new variant of the pro-apoptotic molecule Bax, Baxpsi, RT is correlated with an increased survival of glioblastoma multiforme RT patients."; RL Hum. Mol. Genet. 11:675-687(2002). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ZETA). RC TISSUE=Ovarian carcinoma; RA Perez R.P., Sanville H.; RT "Bax mRNA splice variant lacking exons 2 and 3."; RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA). RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RG NIEHS SNPs program; RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA). RC TISSUE=Skin; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [11] RP NUCLEOTIDE SEQUENCE [MRNA] OF 63-77 AND 98-118, AND VARIANTS ARG-67 AND RP VAL-108. RX PubMed=7475270; RA Meijerink J.P.P., Smetsers T.F.C.M., Sloetjes A.W., Linders E.H.P., RA Mensink E.J.B.M.; RT "Bax mutations in cell lines derived from hematological malignancies."; RL Leukemia 9:1828-1832(1995). RN [12] RP MUTAGENESIS, AND FUNCTION OF BH3 MOTIF. RX PubMed=8521816; DOI=10.1002/j.1460-2075.1995.tb00246.x; RA Chittenden T., Flemington C., Houghton A.B., Ebb R.G., Gallo G.J., RA Elangovan B., Chinnadurai G., Lutz R.J.; RT "A conserved domain in Bak, distinct from BH1 and BH2, mediates cell death RT and protein binding functions."; RL EMBO J. 14:5589-5596(1995). RN [13] RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-184. RX PubMed=10228148; DOI=10.1093/emboj/18.9.2330; RA Nechushtan A., Smith C.L., Hsu Y.-T., Youle R.J.; RT "Conformation of the Bax C-terminus regulates subcellular location and cell RT death."; RL EMBO J. 18:2330-2341(1999). RN [14] RP FUNCTION, AND INTERACTION WITH MOAP1. RX PubMed=11060313; DOI=10.1074/jbc.m008955200; RA Tan K.O., Tan K.M.L., Chan S.-L., Yee K.S.Y., Bevort M., Ang K.C., Yu V.C.; RT "MAP-1, a novel proapoptotic protein containing a BH3-like motif that RT associates with Bax through its Bcl-2 homology domains."; RL J. Biol. Chem. 276:2802-2807(2001). RN [15] RP INTERACTION WITH SH3GLB1. RX PubMed=11259440; DOI=10.1074/jbc.m101527200; RA Cuddeback S.M., Yamaguchi H., Komatsu K., Miyashita T., Yamada M., Wu C., RA Singh S., Wang H.-G.; RT "Molecular cloning and characterization of Bif-1. A novel Src homology 3 RT domain-containing protein that associates with Bax."; RL J. Biol. Chem. 276:20559-20565(2001). RN [16] RP INTERACTION WITH ADENOVIRUS PROTEIN E1B 19K. RX PubMed=11462023; DOI=10.1128/jvi.75.16.7506-7516.2001; RA Sundararajan R., White E.; RT "E1B 19K blocks Bax oligomerization and tumor necrosis factor alpha- RT mediated apoptosis."; RL J. Virol. 75:7506-7516(2001). RN [17] RP INTERACTION WITH HUMANIN. RX PubMed=12732850; DOI=10.1038/nature01627; RA Guo B., Zhai D., Cabezas E., Welsh K., Nouraini S., Satterthwait A.C., RA Reed J.C.; RT "Humanin peptide suppresses apoptosis by interfering with Bax activation."; RL Nature 423:456-461(2003). RN [18] RP INTERACTION WITH SFN AND YWHAZ, AND SUBCELLULAR LOCATION. RX PubMed=15071501; DOI=10.1038/sj.emboj.7600194; RA Tsuruta F., Sunayama J., Mori Y., Hattori S., Shimizu S., Tsujimoto Y., RA Yoshioka K., Masuyama N., Gotoh Y.; RT "JNK promotes Bax translocation to mitochondria through phosphorylation of RT 14-3-3 proteins."; RL EMBO J. 23:1889-1899(2004). RN [19] RP INTERACTION WITH NOL3. RX PubMed=15004034; DOI=10.1074/jbc.m400695200; RA Gustafsson A.B., Tsai J.G., Logue S.E., Crow M.T., Gottlieb R.A.; RT "Apoptosis repressor with caspase recruitment domain protects against cell RT death by interfering with Bax activation."; RL J. Biol. Chem. 279:21233-21238(2004). RN [20] RP INTERACTION WITH HHV-5 PROTEIN UL37. RX PubMed=15004026; DOI=10.1074/jbc.m308408200; RA Poncet D., Larochette N., Pauleau A.L., Boya P., Jalil A.A., Cartron P.F., RA Vallette F., Schnebelen C., Bartle L.M., Skaletskaya A., Boutolleau D., RA Martinou J.C., Goldmacher V.S., Kroemer G., Zamzami N.; RT "An anti-apoptotic viral protein that recruits Bax to mitochondria."; RL J. Biol. Chem. 279:22605-22614(2004). RN [21] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CLU. RX PubMed=16113678; DOI=10.1038/ncb1291; RA Zhang H., Kim J.K., Edwards C.A., Xu Z., Taichman R., Wang C.Y.; RT "Clusterin inhibits apoptosis by interacting with activated Bax."; RL Nat. Cell Biol. 7:909-915(2005). RN [22] RP FUNCTION, AND INTERACTION WITH MOAP1. RX PubMed=16199525; DOI=10.1073/pnas.0503524102; RA Tan K.O., Fu N.Y., Sukumaran S.K., Chan S.L., Kang J.H., Poon K.L., RA Chen B.S., Yu V.C.; RT "MAP-1 is a mitochondrial effector of Bax."; RL Proc. Natl. Acad. Sci. U.S.A. 102:14623-14628(2005). RN [23] RP INTERACTION WITH FAIM2/LFG2. RX PubMed=16964429; DOI=10.3892/ijmm.18.4.729; RA Reimers K., Choi C.Y., Mau-Thek E., Vogt P.M.; RT "Sequence analysis shows that Lifeguard belongs to a new evolutionarily RT conserved cytoprotective family."; RL Int. J. Mol. Med. 18:729-734(2006). RN [24] RP INTERACTION WITH GIMAP3 AND GIMAP5. RX PubMed=16509771; DOI=10.1371/journal.pbio.0040103; RA Nitta T., Nasreen M., Seike T., Goji A., Ohigashi I., Miyazaki T., Ohta T., RA Kanno M., Takahama Y.; RT "IAN family critically regulates survival and development of T RT lymphocytes."; RL PLoS Biol. 4:593-605(2006). RN [25] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [26] RP INTERACTION WITH RNF144B. RX PubMed=20300062; DOI=10.1038/emboj.2010.39; RA Benard G., Neutzner A., Peng G., Wang C., Livak F., Youle R.J., RA Karbowski M.; RT "IBRDC2, an IBR-type E3 ubiquitin ligase, is a regulatory factor for Bax RT and apoptosis activation."; RL EMBO J. 29:1458-1471(2010). RN [27] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [28] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH BCL2L1. RX PubMed=21458670; DOI=10.1016/j.cell.2011.02.034; RA Edlich F., Banerjee S., Suzuki M., Cleland M.M., Arnoult D., Wang C., RA Neutzner A., Tjandra N., Youle R.J.; RT "Bcl-x(L) retrotranslocates Bax from the mitochondria into the cytosol."; RL Cell 145:104-116(2011). RN [29] RP INTERACTION WITH BCL2L10. RX PubMed=23235460; DOI=10.1038/cddis.2012.178; RA Rautureau G.J., Yabal M., Yang H., Huang D.C., Kvansakul M., Hinds M.G.; RT "The restricted binding repertoire of Bcl-B leaves Bim as the universal RT BH3-only prosurvival Bcl-2 protein antagonist."; RL Cell Death Dis. 3:e443-e443(2012). RN [30] RP INTERACTION WITH RTL10/BOP. RX PubMed=23055042; DOI=10.1007/s13238-012-2069-7; RA Zhang X., Weng C., Li Y., Wang X., Jiang C., Li X., Xu Y., Chen Q., Pan L., RA Tang H.; RT "Human Bop is a novel BH3-only member of the Bcl-2 protein family."; RL Protein Cell 3:790-801(2012). RN [31] RP FUNCTION, INTERACTION WITH IRF3 AND BCL2, AND SUBCELLULAR LOCATION. RX PubMed=25609812; DOI=10.1128/jvi.02959-14; RA Wei B., Cui Y., Huang Y., Liu H., Li L., Li M., Ruan K.C., Zhou Q., RA Wang C.; RT "Tom70 mediates Sendai virus-induced apoptosis on mitochondria."; RL J. Virol. 89:3804-3818(2015). RN [32] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [33] RP INTERACTION WITH ENTEROVIRUS 71 PROTEIN 2B, AND SUBCELLULAR LOCATION. RX PubMed=27558414; DOI=10.1128/jvi.01499-16; RA Cong H., Du N., Yang Y., Song L., Zhang W., Tien P.; RT "Enterovirus 71 2B induces cell apoptosis by directly inducing the RT conformational activation of the proapoptotic protein Bax."; RL J. Virol. 90:9862-9877(2016). RN [34] RP SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=29531808; DOI=10.1038/s41420-017-0006-5; RA Kuriyama S., Tsuji T., Sakuma T., Yamamoto T., Tanaka M.; RT "PLEKHN1 promotes apoptosis by enhancing Bax-Bak hetero-oligomerization RT through interaction with Bid in human colon cancer."; RL Cell. Death. Discov. 4:11-11(2018). RN [35] RP FORMATION OF FIBERS WITH HUMANIN, AND MUTAGENESIS OF 172-THR--GLY-192 AND RP SER-184. RX PubMed=31690630; DOI=10.1074/jbc.ra119.011297; RA Morris D.L., Kastner D.W., Johnson S., Strub M.P., He Y., Bleck C.K.E., RA Lee D.Y., Tjandra N.; RT "Humanin induces conformational changes in the apoptosis regulator BAX and RT sequesters it into fibers, preventing mitochondrial outer-membrane RT permeabilization."; RL J. Biol. Chem. 294:19055-19065(2019). RN [36] RP FUNCTION, DEUBIQUITINATION BY USP12, MUTAGENESIS OF LYS-128; LYS-189 AND RP LYS-190, SUBCELLULAR LOCATION, AND UBIQUITINATION AT LYS-128 AND LYS-190. RX PubMed=36361894; DOI=10.3390/ijms232113107; RA Choi H.S., Lim E.S., Baek K.H.; RT "Deubiquitinating Enzyme USP12 Regulates the Pro-Apoptosis Protein Bax."; RL Int. J. Mol. Sci. 23:0-0(2022). RN [37] RP STRUCTURE BY NMR, SUBCELLULAR LOCATION, AND SUBUNIT. RX PubMed=11106734; DOI=10.1016/s0092-8674(00)00167-7; RA Suzuki M., Youle R.J., Tjandra N.; RT "Structure of Bax: coregulation of dimer formation and intracellular RT localization."; RL Cell 103:645-654(2000). RN [38] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 13-19 IN COMPLEX WITH ANTIBODY RP FRAGMENT. RX PubMed=16946732; DOI=10.1038/sj.cdd.4402025; RA Peyerl F.W., Dai S., Murphy G.A., Crawford F., White J., Marrack P., RA Kappler J.W.; RT "Elucidation of some Bax conformational changes through crystallization of RT an antibody-peptide complex."; RL Cell Death Differ. 14:447-452(2007). RN [39] RP STRUCTURE BY NMR IN COMPLEX WITH BCL2L11, FUNCTION, SUBUNIT, MUTAGENESIS OF RP LYS-21, AND INTERACTION WITH BCL2L11. RX PubMed=18948948; DOI=10.1038/nature07396; RA Gavathiotis E., Suzuki M., Davis M.L., Pitter K., Bird G.H., Katz S.G., RA Tu H.C., Kim H., Cheng E.H., Tjandra N., Walensky L.D.; RT "BAX activation is initiated at a novel interaction site."; RL Nature 455:1076-1081(2008). RN [40] RP X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) OF 48-81 IN COMPLEXES WITH BCL2L1 RP AND MCL1, INTERACTION WITH MCL1; BCL2; BCL2L1 AND BCL2L2, FUNCTION, AND RP MUTAGENESIS OF MET-74. RX PubMed=21199865; DOI=10.1074/jbc.m110.161281; RA Czabotar P.E., Lee E.F., Thompson G.V., Wardak A.Z., Fairlie W.D., RA Colman P.M.; RT "Mutation to Bax beyond the BH3 domain disrupts interactions with pro- RT survival proteins and promotes apoptosis."; RL J. Biol. Chem. 286:7123-7131(2011). RN [41] RP VARIANTS GLU-11; ARG-67 AND VAL-108. RX PubMed=9531611; DOI=10.1182/blood.v91.8.2991.2991_2991_2997; RA Meijerink J.P.P., Mensink E.J.B.M., Wang K., Sedlak T.W., Sloetjes A.W., RA de Witte T., Waksman G., Korsmeyer S.J.; RT "Hematopoietic malignancies demonstrate loss-of-function mutations of RT BAX."; RL Blood 91:2991-2997(1998). RN [42] RP INTERACTION WITH XRCC6. RX PubMed=15023334; DOI=10.1016/s1097-2765(04)00094-2; RA Cohen H.Y., Lavu S., Bitterman K.J., Hekking B., Imahiyerobo T.A., RA Miller C., Frye R., Ploegh H., Kessler B.M., Sinclair D.A.; RT "Acetylation of the C terminus of Ku70 by CBP and PCAF controls Bax- RT mediated apoptosis."; RL Mol. Cell 13:627-638(2004). RN [43] RP UBIQUITINATION. RX PubMed=18362350; DOI=10.1073/pnas.0706700105; RA Amsel A.D., Rathaus M., Kronman N., Cohen H.Y.; RT "Regulation of the proapoptotic factor Bax by Ku70-dependent RT deubiquitylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:5117-5122(2008). CC -!- FUNCTION: Plays a role in the mitochondrial apoptotic process CC (PubMed:10772918, PubMed:11060313, PubMed:16113678, PubMed:16199525, CC PubMed:18948948, PubMed:21199865, PubMed:21458670, PubMed:25609812, CC PubMed:36361894, PubMed:8358790, PubMed:8521816). Under normal CC conditions, BAX is largely cytosolic via constant retrotranslocation CC from mitochondria to the cytosol mediated by BCL2L1/Bcl-xL, which CC avoids accumulation of toxic BAX levels at the mitochondrial outer CC membrane (MOM) (PubMed:21458670). Under stress conditions, undergoes a CC conformation change that causes translocation to the mitochondrion CC membrane, leading to the release of cytochrome c that then triggers CC apoptosis (PubMed:10772918, PubMed:11060313, PubMed:16113678, CC PubMed:16199525, PubMed:18948948, PubMed:21199865, PubMed:21458670, CC PubMed:25609812, PubMed:8358790, PubMed:8521816). Promotes activation CC of CASP3, and thereby apoptosis (PubMed:10772918, PubMed:11060313, CC PubMed:16113678, PubMed:16199525, PubMed:18948948, PubMed:21199865, CC PubMed:21458670, PubMed:25609812, PubMed:8358790, PubMed:8521816). CC {ECO:0000269|PubMed:10772918, ECO:0000269|PubMed:11060313, CC ECO:0000269|PubMed:16113678, ECO:0000269|PubMed:16199525, CC ECO:0000269|PubMed:18948948, ECO:0000269|PubMed:21199865, CC ECO:0000269|PubMed:21458670, ECO:0000269|PubMed:25609812, CC ECO:0000269|PubMed:36361894, ECO:0000269|PubMed:8358790, CC ECO:0000269|PubMed:8521816}. CC -!- SUBUNIT: Homodimer. Forms higher oligomers under stress conditions. CC Forms heterooligomers with BAK (PubMed:29531808). Interacts with CC BCL2L11. Interaction with BCL2L11 promotes BAX oligomerization and CC association with mitochondrial membranes, with subsequent release of CC cytochrome c. Forms heterodimers with BCL2, BCL2L1 isoform Bcl-X(L), CC BCL2L2, MCL1 and A1 (PubMed:25609812). Interacts with SH3GLB1. CC Interacts with humanin; forms fibers with humanin which results in BAX CC conformational changes and sequestering of BAX into the fibers, CC preventing BAX activation (PubMed:12732850, PubMed:31690630). Interacts CC with SFN and YWHAZ; the interaction occurs in the cytoplasm. Under CC stress conditions, JNK-mediated phosphorylation of SFN and YWHAZ, CC releases BAX to mitochondria. Interacts with RNF144B, which regulates CC the ubiquitin-dependent stability of BAX. Interacts with CLU under CC stress conditions that cause a conformation change leading to BAX CC oligomerization and association with mitochondria. Does not interact CC with CLU in unstressed cells. Interacts with FAIM2/LFG2. Interacts with CC RTL10/BOP. Interacts (via a C-terminal 33 residues) with NOL3 (via CARD CC domain); inhibits BAX activation and translocation and consequently CC cytochrome c release from mitochondria. Interacts with GIMAP3/IAN4 and CC GIMAP5/IAN5; this interaction is increased, when cells initiate CC apoptosis upon IL2 withdrawal (PubMed:16509771). Interacts with IRF3; CC the interaction is direct, increases upon Sendai virus infection and CC mediates the formation of the apoptosis complex CC TOMM70:HSP90AA1:IRF3:BAX (PubMed:25609812). Interacts with MOAP1, CC facilitating BAX-dependent mitochondrial outer membrane CC permeabilization and apoptosis (PubMed:11060313, PubMed:16199525). CC Interacts with BCL2L10/BCL-B (PubMed:23235460). Interacts with non- CC acetylated XRCC6/Ku70; this interaction leads to BAX sequestration in CC the cytosol, away from the mitochondria, preventing BAX-mediated CC apoptosis (PubMed:15023334). {ECO:0000269|PubMed:11060313, CC ECO:0000269|PubMed:11106734, ECO:0000269|PubMed:11259440, CC ECO:0000269|PubMed:12732850, ECO:0000269|PubMed:15004026, CC ECO:0000269|PubMed:15004034, ECO:0000269|PubMed:15023334, CC ECO:0000269|PubMed:15071501, ECO:0000269|PubMed:16113678, CC ECO:0000269|PubMed:16199525, ECO:0000269|PubMed:16509771, CC ECO:0000269|PubMed:16946732, ECO:0000269|PubMed:16964429, CC ECO:0000269|PubMed:18948948, ECO:0000269|PubMed:20300062, CC ECO:0000269|PubMed:21199865, ECO:0000269|PubMed:23055042, CC ECO:0000269|PubMed:23235460, ECO:0000269|PubMed:25609812, CC ECO:0000269|PubMed:29531808, ECO:0000269|PubMed:31690630, CC ECO:0000269|PubMed:8358790}. CC -!- SUBUNIT: [Isoform Sigma]: Interacts with BCL2A1 and BCL2L1 isoform Bcl- CC X(L). {ECO:0000269|PubMed:10772918}. CC -!- SUBUNIT: (Microbial infection) Interacts with adenovirus E1B 19K CC protein; this interaction blocks BAX oligomerization (PubMed:11462023). CC {ECO:0000269|PubMed:11462023}. CC -!- SUBUNIT: (Microbial infection) Interacts with human CC cytomegalovirus/HHV-5 protein vMIA/UL37. {ECO:0000269|PubMed:15004026}. CC -!- SUBUNIT: (Microbial infection) Interacts with enterovirus protein 2B; CC this interaction activates BAX-induced apoptosis. CC {ECO:0000269|PubMed:27558414}. CC -!- INTERACTION: CC Q07812; Q16611: BAK1; NbExp=6; IntAct=EBI-516580, EBI-519866; CC Q07812; Q07812: BAX; NbExp=28; IntAct=EBI-516580, EBI-516580; CC Q07812; P10415: BCL2; NbExp=16; IntAct=EBI-516580, EBI-77694; CC Q07812; Q07817-1: BCL2L1; NbExp=21; IntAct=EBI-516580, EBI-287195; CC Q07812; Q9HD36: BCL2L10; NbExp=3; IntAct=EBI-516580, EBI-2126349; CC Q07812; O43521: BCL2L11; NbExp=22; IntAct=EBI-516580, EBI-526406; CC Q07812; Q9HB09: BCL2L12; NbExp=3; IntAct=EBI-516580, EBI-3940897; CC Q07812; Q92843: BCL2L2; NbExp=8; IntAct=EBI-516580, EBI-707714; CC Q07812; P55957: BID; NbExp=17; IntAct=EBI-516580, EBI-519672; CC Q07812; O75460: ERN1; NbExp=2; IntAct=EBI-516580, EBI-371750; CC Q07812; O75031: HSF2BP; NbExp=3; IntAct=EBI-516580, EBI-7116203; CC Q07812; P22001: KCNA3; NbExp=2; IntAct=EBI-516580, EBI-8627664; CC Q07812; Q07820: MCL1; NbExp=11; IntAct=EBI-516580, EBI-1003422; CC Q07812; Q8IVG9: MT-RNR2; NbExp=5; IntAct=EBI-516580, EBI-8643752; CC Q07812; Q9ULZ3: PYCARD; NbExp=7; IntAct=EBI-516580, EBI-751215; CC Q07812; Q7Z419: RNF144B; NbExp=5; IntAct=EBI-516580, EBI-2129982; CC Q07812; Q7L3V2: RTL10; NbExp=2; IntAct=EBI-516580, EBI-10697720; CC Q07812; Q9Y371-1: SH3GLB1; NbExp=2; IntAct=EBI-516580, EBI-5291808; CC Q07812; P37840: SNCA; NbExp=4; IntAct=EBI-516580, EBI-985879; CC Q07812; Q9P2Y5: UVRAG; NbExp=6; IntAct=EBI-516580, EBI-2952704; CC Q07812; P12956: XRCC6; NbExp=2; IntAct=EBI-516580, EBI-353208; CC Q07812; P70444: Bid; Xeno; NbExp=2; IntAct=EBI-516580, EBI-783400; CC Q07812; PRO_0000223236 [P70444]: Bid; Xeno; NbExp=2; IntAct=EBI-516580, EBI-2128640; CC Q07812; Q99MI6: Gimap3; Xeno; NbExp=2; IntAct=EBI-516580, EBI-15572304; CC Q07812; Q8BWF2: Gimap5; Xeno; NbExp=2; IntAct=EBI-516580, EBI-15572348; CC Q07812; P97287: Mcl1; Xeno; NbExp=2; IntAct=EBI-516580, EBI-707292; CC Q07812; P17361: OPG035; Xeno; NbExp=3; IntAct=EBI-516580, EBI-7115640; CC Q07812; P49334: TOM22; Xeno; NbExp=3; IntAct=EBI-516580, EBI-12527; CC Q07812; P23644: TOM40; Xeno; NbExp=2; IntAct=EBI-516580, EBI-12539; CC Q07812; P24391: tom40; Xeno; NbExp=2; IntAct=EBI-516580, EBI-1791540; CC Q07812; P07213: TOM70; Xeno; NbExp=2; IntAct=EBI-516580, EBI-12551; CC Q07812; P16778: UL37; Xeno; NbExp=2; IntAct=EBI-516580, EBI-16026491; CC Q07812; PRO_0000037647 [P26662]; Xeno; NbExp=3; IntAct=EBI-516580, EBI-9099462; CC -!- SUBCELLULAR LOCATION: [Isoform Alpha]: Mitochondrion outer membrane CC {ECO:0000269|PubMed:25609812, ECO:0000269|PubMed:29531808}; Single-pass CC membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:27558414, CC ECO:0000269|PubMed:29531808}. Nucleus {ECO:0000269|PubMed:36361894}. CC Note=Colocalizes with 14-3-3 proteins in the cytoplasm. Under stress CC conditions, undergoes a conformation change that causes release from CC JNK-phosphorylated 14-3-3 proteins and translocation to the CC mitochondrion membrane. Upon Sendai virus infection, recruited to the CC mitochondrion through interaction with IRF3 (PubMed:25609812). CC {ECO:0000269|PubMed:25609812}. CC -!- SUBCELLULAR LOCATION: [Isoform Beta]: Cytoplasm. CC -!- SUBCELLULAR LOCATION: [Isoform Gamma]: Cytoplasm. CC -!- SUBCELLULAR LOCATION: [Isoform Delta]: Cytoplasm {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=8; CC Name=Alpha; CC IsoId=Q07812-1; Sequence=Displayed; CC Name=Beta; CC IsoId=Q07812-2, Q07814-1; Sequence=VSP_031237; CC Name=Gamma; CC IsoId=Q07812-3, Q07815-1; Sequence=VSP_031234, VSP_031236; CC Name=Delta; CC IsoId=Q07812-4, P55269-1; Sequence=VSP_031235; CC Name=Epsilon; CC IsoId=Q07812-5; Sequence=VSP_031240; CC Name=Zeta; CC IsoId=Q07812-6; Sequence=VSP_031239; CC Name=Psi; CC IsoId=Q07812-7; Sequence=VSP_031238; CC Name=Sigma; CC IsoId=Q07812-8; Sequence=VSP_037475; CC -!- TISSUE SPECIFICITY: Expressed in a wide variety of tissues. Isoform Psi CC is found in glial tumors. Isoform Alpha is expressed in spleen, breast, CC ovary, testis, colon and brain, and at low levels in skin and lung. CC Isoform Sigma is expressed in spleen, breast, ovary, testis, lung, CC colon, brain and at low levels in skin. Isoform Alpha and isoform Sigma CC are expressed in pro-myelocytic leukemia, histiocytic lymphoma, CC Burkitt's lymphoma, T-cell lymphoma, lymphoblastic leukemia, breast CC adenocarcinoma, ovary adenocarcinoma, prostate carcinoma, prostate CC adenocarcinoma, lung carcinoma, epidermoid carcinoma, small cell lung CC carcinoma and colon adenocarcinoma cell lines. CC {ECO:0000269|PubMed:10772918, ECO:0000269|PubMed:11912183}. CC -!- DOMAIN: Intact BH3 motif is required by BIK, BID, BAK, BAD and BAX for CC their pro-apoptotic activity and for their interaction with anti- CC apoptotic members of the Bcl-2 family. {ECO:0000269|PubMed:8521816}. CC -!- PTM: Ubiquitinated in the absence of XRCC6/Ku70 (PubMed:18362350). CC Ubiquitination promotes protein degradation (PubMed:18362350). CC Ubiquitinated on Lys-128 and Lys-190. 'Lys-63'-linked polyubiquitin CC chains on Lys-128 are removed by USP12. {ECO:0000269|PubMed:18362350, CC ECO:0000269|PubMed:36361894}. CC -!- SIMILARITY: Belongs to the Bcl-2 family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/128/BAX"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L22473; AAA03619.1; -; mRNA. DR EMBL; L22474; AAA03620.1; -; mRNA. DR EMBL; L22475; AAA03621.1; -; mRNA. DR EMBL; U19599; AAC50142.1; -; mRNA. DR EMBL; AF007826; AAD22706.1; -; mRNA. DR EMBL; AF247393; AAF71267.1; -; mRNA. DR EMBL; AJ417988; CAD10744.1; -; mRNA. DR EMBL; AF250190; AAF82094.1; -; mRNA. DR EMBL; AK291076; BAF83765.1; -; mRNA. DR EMBL; AY217036; AAO22992.1; -; Genomic_DNA. DR EMBL; CH471177; EAW52418.1; -; Genomic_DNA. DR EMBL; CH471177; EAW52417.1; -; Genomic_DNA. DR EMBL; BC014175; AAH14175.1; -; mRNA. DR CCDS; CCDS12742.1; -. [Q07812-1] DR CCDS; CCDS12743.1; -. [Q07812-4] DR CCDS; CCDS12744.1; -. [Q07812-2] DR CCDS; CCDS12745.2; -. [Q07812-8] DR PIR; A47538; A47538. DR PIR; B47538; B47538. DR PIR; C47538; C47538. DR PIR; I38921; I38921. DR PIR; JC7255; JC7255. DR RefSeq; NP_001278357.1; NM_001291428.1. DR RefSeq; NP_001278360.1; NM_001291431.2. [Q07812-6] DR RefSeq; NP_004315.1; NM_004324.4. [Q07812-2] DR RefSeq; NP_620116.1; NM_138761.4. [Q07812-1] DR RefSeq; NP_620118.1; NM_138763.4. [Q07812-4] DR RefSeq; NP_620119.2; NM_138764.5. [Q07812-8] DR PDB; 1F16; NMR; -; A=1-192. DR PDB; 2G5B; X-ray; 2.30 A; I/J/K/L=13-19. DR PDB; 2K7W; NMR; -; A=1-192. DR PDB; 2LR1; NMR; -; A=1-192. DR PDB; 3PK1; X-ray; 2.49 A; B/D=48-81. DR PDB; 3PL7; X-ray; 2.61 A; C=48-81. DR PDB; 4BD2; X-ray; 2.21 A; A=1-171. DR PDB; 4BD6; X-ray; 2.49 A; A=1-171, C=48-81. DR PDB; 4BD7; X-ray; 2.80 A; A/B/C/D=1-171. DR PDB; 4BD8; X-ray; 2.22 A; A/B/C/D=1-171. DR PDB; 4BDU; X-ray; 3.00 A; A/B/C/D=53-128. DR PDB; 4S0O; X-ray; 1.90 A; A/B=1-192. DR PDB; 4S0P; X-ray; 3.25 A; A/B=1-192. DR PDB; 4UF2; X-ray; 3.00 A; B=50-77. DR PDB; 4ZIE; X-ray; 1.80 A; A=1-166. DR PDB; 4ZIF; X-ray; 2.40 A; A=1-166. DR PDB; 4ZIG; X-ray; 2.20 A; A=1-166. DR PDB; 4ZIH; X-ray; 2.50 A; A=1-164. DR PDB; 4ZII; X-ray; 2.19 A; A=1-170. DR PDB; 5W5X; X-ray; 2.50 A; A=1-192. DR PDB; 5W5Z; X-ray; 2.00 A; A=32-192. DR PDB; 5W60; X-ray; 1.80 A; A=1-192. DR PDB; 5W61; X-ray; 2.30 A; A=1-192. DR PDB; 6EB6; X-ray; 2.02 A; A=1-192. DR PDB; 6L8V; NMR; -; A/B=53-128. DR PDB; 6L95; NMR; -; A/B=166-192. DR PDB; 6TRR; X-ray; 2.12 A; B=50-77. DR PDB; 6XY6; X-ray; 2.91 A; B/D/F/H/J/L/N/P=50-77. DR PDB; 7ADT; X-ray; 2.21 A; C/U=50-77. DR PDB; 8G1T; X-ray; 2.09 A; A/B/C/D/E/F/G/H=53-128. DR PDB; 8SPE; X-ray; 2.30 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d=53-128. DR PDB; 8SPF; X-ray; 2.20 A; A/B/C/D/E/F=53-128. DR PDB; 8SPZ; X-ray; 2.40 A; A/B/C/D=53-128. DR PDB; 8SRX; X-ray; 2.09 A; B/D=53-128. DR PDB; 8SRY; X-ray; 2.40 A; B/D=53-128. DR PDB; 8SVK; X-ray; 2.25 A; A/B/C/D=53-128. DR PDB; 9IXU; EM; 3.19 A; A/B/C/D/E/F/G/H=1-192. DR PDBsum; 1F16; -. DR PDBsum; 2G5B; -. DR PDBsum; 2K7W; -. DR PDBsum; 2LR1; -. DR PDBsum; 3PK1; -. DR PDBsum; 3PL7; -. DR PDBsum; 4BD2; -. DR PDBsum; 4BD6; -. DR PDBsum; 4BD7; -. DR PDBsum; 4BD8; -. DR PDBsum; 4BDU; -. DR PDBsum; 4S0O; -. DR PDBsum; 4S0P; -. DR PDBsum; 4UF2; -. DR PDBsum; 4ZIE; -. DR PDBsum; 4ZIF; -. DR PDBsum; 4ZIG; -. DR PDBsum; 4ZIH; -. DR PDBsum; 4ZII; -. DR PDBsum; 5W5X; -. DR PDBsum; 5W5Z; -. DR PDBsum; 5W60; -. DR PDBsum; 5W61; -. DR PDBsum; 6EB6; -. DR PDBsum; 6L8V; -. DR PDBsum; 6L95; -. DR PDBsum; 6TRR; -. DR PDBsum; 6XY6; -. DR PDBsum; 7ADT; -. DR PDBsum; 8G1T; -. DR PDBsum; 8SPE; -. DR PDBsum; 8SPF; -. DR PDBsum; 8SPZ; -. DR PDBsum; 8SRX; -. DR PDBsum; 8SRY; -. DR PDBsum; 8SVK; -. DR PDBsum; 9IXU; -. DR AlphaFoldDB; Q07812; -. DR BMRB; Q07812; -. DR EMDB; EMD-60977; -. DR SASBDB; Q07812; -. DR SMR; Q07812; -. DR BioGRID; 107057; 153. DR ComplexPortal; CPX-1988; BAX oligomer. DR CORUM; Q07812; -. DR DIP; DIP-232N; -. DR FunCoup; Q07812; 1141. DR IntAct; Q07812; 88. DR MINT; Q07812; -. DR NDEx; IQUERY-CP-BAX; 72 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000293288; -. DR BindingDB; Q07812; -. DR ChEMBL; CHEMBL5318; -. DR DrugBank; DB12756; TAK-901. DR DrugBank; DB16447; Thymoquinone. DR TCDB; 1.A.21.1.2; the bcl-2 (bcl-2) family. DR GlyGen; Q07812; 2 sites, 1 O-linked glycan (1 site). DR iPTMnet; Q07812; -. DR MetOSite; Q07812; -. DR PhosphoSitePlus; Q07812; -. DR SwissPalm; Q07812; -. DR BioMuta; BAX; -. DR DMDM; 728945; -. DR jPOST; Q07812; -. DR MassIVE; Q07812; -. DR PaxDb; 9606-ENSP00000293288; -. DR PeptideAtlas; Q07812; -. DR ProteomicsDB; 58529; -. [Q07812-1] DR ProteomicsDB; 58530; -. [Q07812-2] DR ProteomicsDB; 58531; -. [Q07812-3] DR ProteomicsDB; 58532; -. [Q07812-4] DR ProteomicsDB; 58533; -. [Q07812-5] DR ProteomicsDB; 58534; -. [Q07812-6] DR ProteomicsDB; 58535; -. [Q07812-7] DR ProteomicsDB; 58536; -. [Q07812-8] DR Pumba; Q07812; -. DR TopDownProteomics; Q07812-1; -. [Q07812-1] DR TopDownProteomics; Q07812-2; -. [Q07812-2] DR TopDownProteomics; Q07812-5; -. [Q07812-5] DR TopDownProteomics; Q07812-6; -. [Q07812-6] DR TopDownProteomics; Q07812-8; -. [Q07812-8] DR ABCD; Q07812; 22 sequenced antibodies. DR Antibodypedia; 3777; 2180 antibodies from 54 providers. DR CPTC; Q07812; 1 antibody. DR DNASU; 581; -. DR Ensembl; ENST00000293288.12; ENSP00000293288.8; ENSG00000087088.22. [Q07812-2] DR Ensembl; ENST00000345358.12; ENSP00000263262.9; ENSG00000087088.22. [Q07812-1] DR Ensembl; ENST00000354470.7; ENSP00000346461.3; ENSG00000087088.22. [Q07812-4] DR Ensembl; ENST00000356483.8; ENSP00000348871.4; ENSG00000087088.22. [Q07812-5] DR Ensembl; ENST00000415969.6; ENSP00000389971.2; ENSG00000087088.22. [Q07812-8] DR Ensembl; ENST00000515540.5; ENSP00000426328.1; ENSG00000087088.22. [Q07812-3] DR GeneID; 581; -. DR KEGG; hsa:581; -. DR MANE-Select; ENST00000345358.12; ENSP00000263262.9; NM_138761.4; NP_620116.1. DR UCSC; uc002plf.2; human. [Q07812-1] DR AGR; HGNC:959; -. DR CIViC; 581; 2 evidence items across 3 molecular profiles. DR ClinPGx; PA25269; -. DR CTD; 581; -. DR DisGeNET; 581; -. DR GeneCards; BAX; -. DR HGNC; HGNC:959; BAX. DR HPA; ENSG00000087088; Low tissue specificity. DR MalaCards; BAX; -. DR MIM; 600040; gene. DR OpenTargets; ENSG00000087088; -. DR VEuPathDB; HostDB:ENSG00000087088; -. DR eggNOG; KOG4728; Eukaryota. DR GeneTree; ENSGT01130000278292; -. DR HOGENOM; CLU_3279262_0_0_1; -. DR InParanoid; Q07812; -. DR OMA; QCCGDSE; -. DR OrthoDB; 6080198at2759; -. DR PAN-GO; Q07812; 7 GO annotations based on evolutionary models. DR PhylomeDB; Q07812; -. DR PathwayCommons; Q07812; -. DR Reactome; R-HSA-111457; Release of apoptotic factors from the mitochondria. DR Reactome; R-HSA-114294; Activation, translocation and oligomerization of BAX. DR Reactome; R-HSA-5620971; Pyroptosis. DR Reactome; R-HSA-6803204; TP53 Regulates Transcription of Genes Involved in Cytochrome C Release. DR Reactome; R-HSA-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest. DR Reactome; R-HSA-8878166; Transcriptional regulation by RUNX2. DR Reactome; R-HSA-9603505; NTRK3 as a dependence receptor. DR SignaLink; Q07812; -. DR SIGNOR; Q07812; -. DR Agora; ENSG00000087088; -. DR BioGRID-ORCS; 581; 32 hits in 1176 CRISPR screens. DR ChiTaRS; BAX; human. DR EvolutionaryTrace; Q07812; -. DR GeneWiki; Bcl-2-associated_X_protein; -. DR GenomeRNAi; 581; -. DR Pharos; Q07812; Tchem. DR PRO; PR:Q07812; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; Q07812; protein. DR Bgee; ENSG00000087088; Expressed in mucosa of transverse colon and 168 other cell types or tissues. DR ExpressionAtlas; Q07812; baseline and differential. DR GO; GO:0097145; C:BAK complex; IDA:ARUK-UCL. DR GO; GO:0097144; C:BAX complex; IDA:UniProtKB. DR GO; GO:0097136; C:Bcl-2 family protein complex; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HGNC-UCL. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:HGNC-UCL. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB. DR GO; GO:0005757; C:mitochondrial permeability transition pore complex; IDA:HGNC-UCL. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0005635; C:nuclear envelope; IDA:AgBase. DR GO; GO:0005634; C:nucleus; IDA:AgBase. DR GO; GO:0046930; C:pore complex; IDA:BHF-UCL. DR GO; GO:0051434; F:BH3 domain binding; IDA:UniProtKB. DR GO; GO:0015267; F:channel activity; IDA:BHF-UCL. DR GO; GO:0030544; F:Hsp70 protein binding; IEA:Ensembl. DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB. DR GO; GO:0008289; F:lipid binding; IDA:HGNC-UCL. DR GO; GO:0046982; F:protein heterodimerization activity; IPI:HGNC-UCL. DR GO; GO:0042803; F:protein homodimerization activity; IDA:HGNC-UCL. DR GO; GO:0008637; P:apoptotic mitochondrial changes; IDA:HGNC-UCL. DR GO; GO:0006915; P:apoptotic process; IDA:DIBU. DR GO; GO:0097190; P:apoptotic signaling pathway; IDA:HGNC-UCL. DR GO; GO:0001783; P:B cell apoptotic process; IDA:HGNC-UCL. DR GO; GO:1990117; P:B cell receptor apoptotic signaling pathway; IDA:BHF-UCL. DR GO; GO:0034620; P:cellular response to unfolded protein; TAS:ParkinsonsUK-UCL. DR GO; GO:0098586; P:cellular response to virus; IDA:UniProtKB. DR GO; GO:0032469; P:endoplasmic reticulum calcium ion homeostasis; TAS:UniProtKB. DR GO; GO:0010248; P:establishment or maintenance of transmembrane electrochemical gradient; IDA:HGNC-UCL. DR GO; GO:0097194; P:execution phase of apoptosis; IMP:HGNC-UCL. DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IDA:BHF-UCL. DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IBA:GO_Central. DR GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IC:BHF-UCL. DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; IDA:HGNC-UCL. DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IDA:HGNC-UCL. DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; TAS:ParkinsonsUK-UCL. DR GO; GO:0043653; P:mitochondrial fragmentation involved in apoptotic process; IDA:HGNC-UCL. DR GO; GO:0008053; P:mitochondrial fusion; IDA:HGNC-UCL. DR GO; GO:0010917; P:negative regulation of mitochondrial membrane potential; IDA:UniProtKB. DR GO; GO:0032091; P:negative regulation of protein binding; IDA:UniProtKB. DR GO; GO:1902512; P:positive regulation of apoptotic DNA fragmentation; IMP:BHF-UCL. DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB. DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IMP:UniProtKB. DR GO; GO:1903896; P:positive regulation of IRE1-mediated unfolded protein response; TAS:ParkinsonsUK-UCL. DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; IDA:HGNC-UCL. DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; IDA:UniProtKB. DR GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; IDA:UniProtKB. DR GO; GO:0042981; P:regulation of apoptotic process; IDA:UniProtKB. DR GO; GO:0051881; P:regulation of mitochondrial membrane potential; IDA:HGNC-UCL. DR GO; GO:0001836; P:release of cytochrome c from mitochondria; IDA:UniProtKB. DR GO; GO:0032976; P:release of matrix enzymes from mitochondria; IDA:HGNC-UCL. DR GO; GO:0009636; P:response to toxic substance; IDA:HGNC-UCL. DR GO; GO:0097435; P:supramolecular fiber organization; IDA:UniProtKB. DR CDD; cd06845; Bcl-2_like; 1. DR DisProt; DP02540; -. DR FunFam; 1.10.437.10:FF:000004; apoptosis regulator BAX isoform X2; 1. DR Gene3D; 1.10.437.10; Blc2-like; 1. DR InterPro; IPR036834; Bcl-2-like_sf. DR InterPro; IPR046371; Bcl-2_BH1-3. DR InterPro; IPR026298; Bcl-2_fam. DR InterPro; IPR002475; Bcl2-like. DR InterPro; IPR020717; Bcl2_BH1_motif_CS. DR InterPro; IPR020726; Bcl2_BH2_motif_CS. DR InterPro; IPR020728; Bcl2_BH3_motif_CS. DR PANTHER; PTHR11256:SF42; APOPTOSIS REGULATOR BAX; 1. DR PANTHER; PTHR11256; BCL-2 RELATED; 1. DR Pfam; PF00452; Bcl-2; 1. DR PRINTS; PR01862; BCL2FAMILY. DR SMART; SM00337; BCL; 1. DR SUPFAM; SSF56854; Bcl-2 inhibitors of programmed cell death; 1. DR PROSITE; PS50062; BCL2_FAMILY; 1. DR PROSITE; PS01080; BH1; 1. DR PROSITE; PS01258; BH2; 1. DR PROSITE; PS01259; BH3; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Apoptosis; Cytoplasm; KW Host-virus interaction; Isopeptide bond; Membrane; Mitochondrion; KW Mitochondrion outer membrane; Nucleus; Proteomics identification; KW Reference proteome; Transmembrane; Transmembrane helix; Tumor suppressor; KW Ubl conjugation. FT CHAIN 1..192 FT /note="Apoptosis regulator BAX" FT /id="PRO_0000143053" FT TRANSMEM 172..192 FT /note="Helical" FT /evidence="ECO:0000255" FT MOTIF 59..73 FT /note="BH3" FT /evidence="ECO:0000269|PubMed:8521816" FT MOTIF 98..118 FT /note="BH1" FT MOTIF 150..165 FT /note="BH2" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:25944712" FT CROSSLNK 128 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000269|PubMed:36361894" FT CROSSLNK 190 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000269|PubMed:36361894" FT VAR_SEQ 1..78 FT /note="Missing (in isoform Zeta)" FT /evidence="ECO:0000303|Ref.6" FT /id="VSP_031239" FT VAR_SEQ 1..19 FT /note="Missing (in isoform Psi)" FT /evidence="ECO:0000303|PubMed:11912183" FT /id="VSP_031238" FT VAR_SEQ 12..41 FT /note="GPTSSEQIMKTGALLLQGFIQDRAGRMGGE -> VSSRIEQGEWGGRHPSWP FT WTRCLRMRPPRS (in isoform Gamma)" FT /evidence="ECO:0000303|PubMed:8358790" FT /id="VSP_031234" FT VAR_SEQ 30..78 FT /note="Missing (in isoform Delta)" FT /evidence="ECO:0000303|PubMed:7607685" FT /id="VSP_031235" FT VAR_SEQ 42..192 FT /note="Missing (in isoform Gamma)" FT /evidence="ECO:0000303|PubMed:8358790" FT /id="VSP_031236" FT VAR_SEQ 125..192 FT /note="LCTKVPELIRTIMGWTLDFLRERLLGWIQDQGGWDGLLSYFGTPTWQTVTIF FT VAGVLTASLTIWKKMG -> GVKWRDLGSLQPLPPGFKRFTCLSIPRSWDYRPCAPRCR FT N (in isoform Epsilon)" FT /evidence="ECO:0000303|PubMed:9920818" FT /id="VSP_031240" FT VAR_SEQ 159..192 FT /note="DGLLSYFGTPTWQTVTIFVAGVLTASLTIWKKMG -> VRLLKPPHPHHRAL FT TTAPAPPSLPPATPLGPWAFWSRSQWCPLPIFRSSDVVYNAFSLRV (in isoform FT Beta)" FT /evidence="ECO:0000303|PubMed:8358790" FT /id="VSP_031237" FT VAR_SEQ 159..171 FT /note="Missing (in isoform Sigma)" FT /evidence="ECO:0000303|PubMed:10772918" FT /id="VSP_037475" FT VARIANT 11 FT /note="G -> E (in a plasmacytoma cell line; FT dbSNP:rs555248599)" FT /evidence="ECO:0000269|PubMed:9531611" FT /id="VAR_013575" FT VARIANT 39 FT /note="G -> R (in dbSNP:rs36017265)" FT /id="VAR_047053" FT VARIANT 67 FT /note="G -> R (in a T-cell acute lymphoblastic leukemia FT cell line; loss of heterodimerization with Bcl-2 or FT Bcl-X(L); dbSNP:rs398122513)" FT /evidence="ECO:0000269|PubMed:7475270, FT ECO:0000269|PubMed:9531611" FT /id="VAR_007809" FT VARIANT 108 FT /note="G -> V (in a Burkitt lymphoma; loss of FT homodimerization)" FT /evidence="ECO:0000269|PubMed:7475270, FT ECO:0000269|PubMed:9531611" FT /id="VAR_013576" FT MUTAGEN 21 FT /note="K->E: Reduces interaction with BCL2L11, FT homooligomerization and triggering of apoptosis." FT /evidence="ECO:0000269|PubMed:18948948" FT MUTAGEN 74 FT /note="M->D,E: Strongly reduced interaction with MCL1, FT BCL2, BCL2L1 and BCL2L2. No effect on cytochrome c release FT and subsequent apoptosis triggered by etoposide." FT /evidence="ECO:0000269|PubMed:21199865" FT MUTAGEN 128 FT /note="K->R: Partial loss of polyubiquitination." FT /evidence="ECO:0000269|PubMed:36361894" FT MUTAGEN 172..192 FT /note="Missing: Enhanced fiber formation with humanin." FT /evidence="ECO:0000269|PubMed:31690630" FT MUTAGEN 184 FT /note="S->D,E,H,K: Constitutive cytoplasmic location." FT /evidence="ECO:0000269|PubMed:10228148" FT MUTAGEN 184 FT /note="S->V: Constitutive mitochondrial location. Enhanced FT fiber formation with humanin." FT /evidence="ECO:0000269|PubMed:10228148, FT ECO:0000269|PubMed:31690630" FT MUTAGEN 189 FT /note="K->R: No loss of polyubiquitination." FT /evidence="ECO:0000269|PubMed:36361894" FT MUTAGEN 190 FT /note="K->R: Partial loss of polyubiquitination." FT /evidence="ECO:0000269|PubMed:36361894" FT TURN 2..4 FT /evidence="ECO:0007829|PDB:2K7W" FT STRAND 10..14 FT /evidence="ECO:0007829|PDB:1F16" FT HELIX 16..34 FT /evidence="ECO:0007829|PDB:4ZIE" FT HELIX 36..38 FT /evidence="ECO:0007829|PDB:2K7W" FT STRAND 39..41 FT /evidence="ECO:0007829|PDB:5W60" FT HELIX 43..45 FT /evidence="ECO:0007829|PDB:5W60" FT HELIX 48..51 FT /evidence="ECO:0007829|PDB:4ZIE" FT HELIX 54..71 FT /evidence="ECO:0007829|PDB:4ZIE" FT HELIX 74..82 FT /evidence="ECO:0007829|PDB:4ZIE" FT STRAND 85..87 FT /evidence="ECO:0007829|PDB:5W60" FT HELIX 88..99 FT /evidence="ECO:0007829|PDB:4ZIE" FT TURN 100..102 FT /evidence="ECO:0007829|PDB:4ZIE" FT HELIX 107..143 FT /evidence="ECO:0007829|PDB:4ZIE" FT HELIX 144..148 FT /evidence="ECO:0007829|PDB:4ZIE" FT HELIX 149..154 FT /evidence="ECO:0007829|PDB:4ZIE" FT TURN 155..158 FT /evidence="ECO:0007829|PDB:4ZIE" FT HELIX 159..164 FT /evidence="ECO:0007829|PDB:4ZIE" FT TURN 167..169 FT /evidence="ECO:0007829|PDB:5W60" FT HELIX 170..187 FT /evidence="ECO:0007829|PDB:5W60" SQ SEQUENCE 192 AA; 21184 MW; 6C0CDB0A7DEE4994 CRC64; MDGSGEQPRG GGPTSSEQIM KTGALLLQGF IQDRAGRMGG EAPELALDPV PQDASTKKLS ECLKRIGDEL DSNMELQRMI AAVDTDSPRE VFFRVAADMF SDGNFNWGRV VALFYFASKL VLKALCTKVP ELIRTIMGWT LDFLRERLLG WIQDQGGWDG LLSYFGTPTW QTVTIFVAGV LTASLTIWKK MG //