BAX_HUMAN
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 03-AUG-2022, entry version 229.
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;
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 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 [37]
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 [38]
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 [39]
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 [40]
RP VARIANTS GLU-11; ARG-67 AND VAL-108.
RX PubMed=9531611;
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).
CC -!- FUNCTION: Plays a role in the mitochondrial apoptotic process
CC (PubMed:10772918, PubMed:16113678, PubMed:18948948, PubMed:21199865,
CC PubMed:21458670, PubMed:25609812, PubMed:8358790, PubMed:8521816,
CC PubMed:11060313, PubMed:16199525). Under normal conditions, BAX is
CC largely cytosolic via constant retrotranslocation from mitochondria to
CC the cytosol mediated by BCL2L1/Bcl-xL, which avoids accumulation of
CC toxic BAX levels at the mitochondrial outer membrane (MOM)
CC (PubMed:21458670). Under stress conditions, undergoes a conformation
CC change that causes translocation to the mitochondrion membrane, leading
CC to the release of cytochrome c that then triggers apoptosis
CC (PubMed:11060313, PubMed:16199525, PubMed:10772918, PubMed:16113678,
CC PubMed:18948948, PubMed:21199865, PubMed:21458670, PubMed:25609812,
CC PubMed:8358790, PubMed:8521816). Promotes activation of CASP3, and
CC thereby apoptosis (PubMed:11060313, PubMed:16199525, PubMed:10772918,
CC PubMed:16113678, PubMed:18948948, PubMed:21199865, PubMed:21458670,
CC 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:8358790, 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).
CC {ECO:0000269|PubMed:11060313, ECO:0000269|PubMed:11106734,
CC ECO:0000269|PubMed:11259440, ECO:0000269|PubMed:12732850,
CC ECO:0000269|PubMed:15004026, ECO:0000269|PubMed:15004034,
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=5; IntAct=EBI-516580, EBI-519866;
CC Q07812; Q07812: BAX; NbExp=28; IntAct=EBI-516580, EBI-516580;
CC Q07812; P10415: BCL2; NbExp=14; IntAct=EBI-516580, EBI-77694;
CC Q07812; Q07817-1: BCL2L1; NbExp=21; IntAct=EBI-516580, EBI-287195;
CC Q07812; Q9HD36: BCL2L10; NbExp=2; IntAct=EBI-516580, EBI-2126349;
CC Q07812; O43521: BCL2L11; NbExp=22; IntAct=EBI-516580, EBI-526406;
CC Q07812; Q92843: BCL2L2; NbExp=5; 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=8; 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; 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; P17361: VACWR028; Xeno; NbExp=3; IntAct=EBI-516580, EBI-7115640;
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}. Note=Colocalizes with 14-3-3 proteins in
CC the cytoplasm. Under stress conditions, undergoes a conformation change
CC that causes release from JNK-phosphorylated 14-3-3 proteins and
CC translocation to the mitochondrion membrane. Upon Sendai virus
CC infection, recruited to the mitochondrion through interaction with IRF3
CC (PubMed:25609812). {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;
CC Sequence=VSP_031237;
CC Name=Gamma;
CC IsoId=Q07812-3, Q07815-1;
CC Sequence=VSP_031234, VSP_031236;
CC Name=Delta;
CC IsoId=Q07812-4, P55269-1;
CC 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 -!- SIMILARITY: Belongs to the Bcl-2 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/bax/";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/BAXID128ch19q13.html";
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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_001291431.1. [Q07812-6]
DR RefSeq; NP_004315.1; NM_004324.3. [Q07812-2]
DR RefSeq; NP_620116.1; NM_138761.3. [Q07812-1]
DR RefSeq; NP_620118.1; NM_138763.3. [Q07812-4]
DR RefSeq; NP_620119.2; NM_138764.4. [Q07812-8]
DR RefSeq; XP_016882566.1; XM_017027077.1. [Q07812-7]
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 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 AlphaFoldDB; Q07812; -.
DR BMRB; Q07812; -.
DR SASBDB; Q07812; -.
DR SMR; Q07812; -.
DR BioGRID; 107057; 125.
DR ComplexPortal; CPX-1988; BAX oligomer.
DR CORUM; Q07812; -.
DR DIP; DIP-232N; -.
DR IntAct; Q07812; 79.
DR MINT; Q07812; -.
DR STRING; 9606.ENSP00000293288; -.
DR BindingDB; Q07812; -.
DR ChEMBL; CHEMBL5318; -.
DR TCDB; 1.A.21.1.2; the bcl-2 (bcl-2) family.
DR iPTMnet; Q07812; -.
DR MetOSite; Q07812; -.
DR PhosphoSitePlus; Q07812; -.
DR SwissPalm; Q07812; -.
DR BioMuta; BAX; -.
DR DMDM; 728945; -.
DR EPD; Q07812; -.
DR jPOST; Q07812; -.
DR MassIVE; Q07812; -.
DR MaxQB; Q07812; -.
DR PaxDb; Q07812; -.
DR PeptideAtlas; Q07812; -.
DR PRIDE; 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 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; 2081 antibodies from 51 providers.
DR CPTC; Q07812; 1 antibody.
DR DNASU; 581; -.
DR Ensembl; ENST00000293288.12; ENSP00000293288.8; ENSG00000087088.21. [Q07812-2]
DR Ensembl; ENST00000345358.12; ENSP00000263262.9; ENSG00000087088.21. [Q07812-1]
DR Ensembl; ENST00000354470.7; ENSP00000346461.3; ENSG00000087088.21. [Q07812-4]
DR Ensembl; ENST00000356483.8; ENSP00000348871.4; ENSG00000087088.21. [Q07812-5]
DR Ensembl; ENST00000415969.6; ENSP00000389971.2; ENSG00000087088.21. [Q07812-8]
DR Ensembl; ENST00000515540.5; ENSP00000426328.1; ENSG00000087088.21. [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 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 neXtProt; NX_Q07812; -.
DR OpenTargets; ENSG00000087088; -.
DR PharmGKB; PA25269; -.
DR VEuPathDB; HostDB:ENSG00000087088; -.
DR eggNOG; KOG4728; Eukaryota.
DR GeneTree; ENSGT01050000244872; -.
DR HOGENOM; CLU_3279262_0_0_1; -.
DR InParanoid; Q07812; -.
DR OMA; HFGTPTW; -.
DR OrthoDB; 1218929at2759; -.
DR PhylomeDB; Q07812; -.
DR TreeFam; TF315834; -.
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 BioGRID-ORCS; 581; 29 hits in 1090 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 166 other tissues.
DR ExpressionAtlas; Q07812; baseline and differential.
DR Genevisible; Q07812; HS.
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:0051087; F:chaperone binding; IEA:Ensembl.
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:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:HGNC-UCL.
DR GO; GO:0008635; P:activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c; IDA:HGNC-UCL.
DR GO; GO:0097296; P:activation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0008637; P:apoptotic mitochondrial changes; IDA:HGNC-UCL.
DR GO; GO:0006915; P:apoptotic process; IDA:DIBU.
DR GO; GO:1902262; P:apoptotic process involved in blood vessel morphogenesis; IEA:Ensembl.
DR GO; GO:1902263; P:apoptotic process involved in embryonic digit morphogenesis; IEA:Ensembl.
DR GO; GO:0060057; P:apoptotic process involved in mammary gland involution; IEA:Ensembl.
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:0001782; P:B cell homeostasis; IEA:Ensembl.
DR GO; GO:0002358; P:B cell homeostatic proliferation; IEA:Ensembl.
DR GO; GO:0002352; P:B cell negative selection; IEA:Ensembl.
DR GO; GO:1990117; P:B cell receptor apoptotic signaling pathway; IDA:BHF-UCL.
DR GO; GO:0001974; P:blood vessel remodeling; IEA:Ensembl.
DR GO; GO:0060402; P:calcium ion transport into cytosol; IEA:Ensembl.
DR GO; GO:0034620; P:cellular response to unfolded protein; TAS:ParkinsonsUK-UCL.
DR GO; GO:0034644; P:cellular response to UV; IEA:Ensembl.
DR GO; GO:0098586; P:cellular response to virus; IDA:UniProtKB.
DR GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
DR GO; GO:0045136; P:development of secondary sexual characteristics; IEA:Ensembl.
DR GO; GO:0035234; P:ectopic germ cell programmed cell death; IEA:Ensembl.
DR GO; GO:0032469; P:endoplasmic reticulum calcium ion homeostasis; TAS:UniProtKB.
DR GO; GO:1904019; P:epithelial cell apoptotic process; IEA:Ensembl.
DR GO; GO:0010248; P:establishment or maintenance of transmembrane electrochemical gradient; IDA: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:0009566; P:fertilization; IEA:Ensembl.
DR GO; GO:0007281; P:germ cell development; IEA:Ensembl.
DR GO; GO:0006687; P:glycosphingolipid metabolic process; IEA:Ensembl.
DR GO; GO:0048873; P:homeostasis of number of cells within a tissue; IEA:Ensembl.
DR GO; GO:0021854; P:hypothalamus development; IEA:Ensembl.
DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; IDA:HGNC-UCL.
DR GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; IEA:Ensembl.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IBA:GO_Central.
DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IMP:UniProtKB.
DR GO; GO:0001822; P:kidney development; IEA:Ensembl.
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:0070584; P:mitochondrion morphogenesis; IEA:Ensembl.
DR GO; GO:0097049; P:motor neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0002262; P:myeloid cell homeostasis; IEA:Ensembl.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0032471; P:negative regulation of endoplasmic reticulum calcium ion concentration; IEA:Ensembl.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; IEA:Ensembl.
DR GO; GO:0010917; P:negative regulation of mitochondrial membrane potential; IDA:UniProtKB.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
DR GO; GO:0032091; P:negative regulation of protein binding; IDA:UniProtKB.
DR GO; GO:0001764; P:neuron migration; IEA:Ensembl.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl.
DR GO; GO:0001541; P:ovarian follicle development; IEA:Ensembl.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IEA:Ensembl.
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:0060058; P:positive regulation of apoptotic process involved in mammary gland involution; IEA:Ensembl.
DR GO; GO:0002904; P:positive regulation of B cell apoptotic process; IEA:Ensembl.
DR GO; GO:0010524; P:positive regulation of calcium ion transport into cytosol; IEA:Ensembl.
DR GO; GO:0048087; P:positive regulation of developmental pigmentation; IEA:Ensembl.
DR GO; GO:1900103; P:positive regulation of endoplasmic reticulum unfolded protein response; IMP:UniProtKB.
DR GO; GO:1904037; P:positive regulation of epithelial cell apoptotic process; IEA:Ensembl.
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:2000673; P:positive regulation of motor neuron apoptotic process; IEA:Ensembl.
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:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; IEA:Ensembl.
DR GO; GO:2000243; P:positive regulation of reproductive process; IEA:Ensembl.
DR GO; GO:0048597; P:post-embryonic camera-type eye morphogenesis; IEA:Ensembl.
DR GO; GO:0001844; P:protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0042981; P:regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:Ensembl.
DR GO; GO:0033599; P:regulation of mammary gland epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:1902445; P:regulation of mitochondrial membrane permeability involved in programmed necrotic cell death; IEA:Ensembl.
DR GO; GO:0051881; P:regulation of mitochondrial membrane potential; IDA:HGNC-UCL.
DR GO; GO:0006808; P:regulation of nitrogen utilization; IEA:Ensembl.
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:0051209; P:release of sequestered calcium ion into cytosol; IEA:Ensembl.
DR GO; GO:0048678; P:response to axon injury; IEA:Ensembl.
DR GO; GO:0010332; P:response to gamma radiation; IEA:Ensembl.
DR GO; GO:0009651; P:response to salt stress; IEA:Ensembl.
DR GO; GO:0009636; P:response to toxic substance; IDA:HGNC-UCL.
DR GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
DR GO; GO:0046666; P:retinal cell programmed cell death; IEA:Ensembl.
DR GO; GO:0060011; P:Sertoli cell proliferation; IEA:Ensembl.
DR GO; GO:0048515; P:spermatid differentiation; IEA:Ensembl.
DR GO; GO:0097435; P:supramolecular fiber organization; IDA:UniProtKB.
DR GO; GO:0001777; P:T cell homeostatic proliferation; IEA:Ensembl.
DR GO; GO:0070242; P:thymocyte apoptotic process; IEA:Ensembl.
DR GO; GO:0060068; P:vagina development; IEA:Ensembl.
DR CDD; cd06845; Bcl-2_like; 1.
DR DisProt; DP02540; -.
DR Gene3D; 1.10.437.10; -; 1.
DR InterPro; IPR026304; BAX.
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; PTHR11256; 1.
DR PANTHER; PTHR11256:SF42; PTHR11256:SF42; 1.
DR Pfam; PF00452; Bcl-2; 1.
DR PRINTS; PR01862; BCL2FAMILY.
DR SMART; SM00337; BCL; 1.
DR SUPFAM; SSF56854; SSF56854; 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; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Tumor suppressor.
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 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 Bcl-
FT 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 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 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 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..147
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
