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Apoptosis regulator Bcl-2

 BCL2_HUMAN              Reviewed;         239 AA.
P10415; C9JHD5; P10416; Q13842; Q16197;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-APR-1993, sequence version 2.
30-AUG-2017, entry version 224.
RecName: Full=Apoptosis regulator Bcl-2;
Name=BCL2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA).
PubMed=3523487; DOI=10.1073/pnas.83.14.5214;
Tsujimoto Y., Croce C.M.;
"Analysis of the structure, transcripts, and protein products of bcl-
2, the gene involved in human follicular lymphoma.";
Proc. Natl. Acad. Sci. U.S.A. 83:5214-5218(1986).
[2]
SEQUENCE REVISION TO 96; 110 AND 237.
PubMed=1508712; DOI=10.1093/nar/20.16.4187;
Eguchi Y., Ewert D.L., Tsujimoto Y.;
"Isolation and characterization of the chicken bcl-2 gene: expression
in a variety of tissues including lymphoid and neuronal organs in
adult and embryo.";
Nucleic Acids Res. 20:4187-4192(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), AND CHROMOSOMAL
TRANSLOCATION.
PubMed=2875799; DOI=10.1016/0092-8674(86)90362-4;
Cleary M.L., Smith S.D., Sklar J.;
"Cloning and structural analysis of cDNAs for bcl-2 and a hybrid bcl-
2/immunoglobulin transcript resulting from the t(14;18)
translocation.";
Cell 47:19-28(1986).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), AND VARIANT SER-7.
PubMed=2834197;
Seto M., Jaeger U., Hockett R.D., Graninger W., Bennett S.,
Goldman P., Korsmeyer S.J.;
"Alternative promoters and exons, somatic mutation and deregulation of
the Bcl-2-Ig fusion gene in lymphoma.";
EMBO J. 7:123-131(1988).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANT SER-7, AND
CHROMOSOMAL TRANSLOCATION.
PubMed=3285301;
Hua C., Zorn S., Jensen J.P., Coupland R.W., Ko H.S., Wright J.J.,
Bakhshi A.;
"Consequences of the t(14;18) chromosomal translocation in follicular
lymphoma: deregulated expression of a chimeric and mutated BCL-2
gene.";
Oncogene Res. 2:263-275(1988).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT THR-43.
NIEHS SNPs program;
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16177791; DOI=10.1038/nature03983;
Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D.,
Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S.,
Bloom T., Bugalter B., Butler J., Cook A., DeCaprio D., Engels R.,
Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T.,
Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E.,
Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H.,
O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
"DNA sequence and analysis of human chromosome 18.";
Nature 437:551-555(2005).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
TISSUE=Testis;
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).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-131 (ISOFORM ALPHA), AND
VARIANTS NON-HODGKIN LYMPHOMA SER-59 AND ILE-93.
PubMed=1339299;
Tanaka S., Louie D.C., Kant J.A., Reed J.C.;
"Frequent incidence of somatic mutations in translocated BCL2
oncogenes of non-Hodgkin's lymphomas.";
Blood 79:229-237(1992).
[11]
SUBCELLULAR LOCATION.
PubMed=2250705; DOI=10.1038/348334a0;
Hockenbery D., Nunez G., Milliman C., Schreiber R.D., Korsmeyer S.J.;
"Bcl-2 is an inner mitochondrial membrane protein that blocks
programmed cell death.";
Nature 348:334-336(1990).
[12]
INTERACTION WITH BAX, HOMODIMERIZATION, SUBUNIT, AND MUTAGENESIS OF
138-PHE--GLY-141; TRP-144; GLY-145; ARG-146; TRP-188; GLN-190;
ASP-191; ASN-192; 194-GLY--ALA-197 AND GLU-200.
PubMed=8183370; DOI=10.1038/369321a0;
Yin X.-M., Oltvai Z.N., Korsmeyer S.J.;
"BH1 and BH2 domains of Bcl-2 are required for inhibition of apoptosis
and heterodimerization with Bax.";
Nature 369:321-323(1994).
[13]
INTERACTION WITH BAG1.
PubMed=9305631; DOI=10.1093/emboj/16.16.4887;
Takayama S., Bimston D.N., Matsuzawa S.-I., Freeman B.C.,
Aime-Sempe C., Xie Z., Morimoto R.I., Reed J.C.;
"BAG-1 modulates the chaperone activity of Hsp70/Hsc70.";
EMBO J. 16:4887-4896(1997).
[14]
CLEAVAGE BY CASPASES, AND MUTAGENESIS.
PubMed=9395403; DOI=10.1126/science.278.5345.1966;
Cheng E.H.-Y., Kirsch D.G., Clem R.J., Ravi R., Kastan M.B., Bedi A.,
Ueno K., Hardwick J.M.;
"Conversion of Bcl-2 to a Bax-like death effector by caspases.";
Science 278:1966-1968(1997).
[15]
INTERACTION WITH TP53BP2.
PubMed=8668206; DOI=10.1128/MCB.16.7.3884;
Naumovski L., Cleary M.L.;
"The p53-binding protein 53BP2 also interacts with Bcl2 and impedes
cell cycle progression at G2/M.";
Mol. Cell. Biol. 16:3884-3892(1996).
[16]
REVIEW ON PHOSPHORYLATION.
PubMed=11368354; DOI=10.1038/sj/leu/2402090;
Ruvolo P.P., Deng X., May W.S.;
"Phosphorylation of Bcl2 and regulation of apoptosis.";
Leukemia 15:515-522(2001).
[17]
PHOSPHORYLATION BY ASK1/JNK1.
PubMed=10567572; DOI=10.1128/MCB.19.12.8469;
Yamamoto K., Ichijo H., Korsmeyer S.J.;
"BCL-2 is phosphorylated and inactivated by an ASK1/Jun N-terminal
protein kinase pathway normally activated at G(2)/M.";
Mol. Cell. Biol. 19:8469-8478(1999).
[18]
INTERACTION WITH BBC3 AND BCL2L1.
PubMed=11463391; DOI=10.1016/S1097-2765(01)00213-1;
Yu J., Zhang L., Hwang P.M., Kinzler K.W., Vogelstein B.;
"PUMA induces the rapid apoptosis of colorectal cancer cells.";
Mol. Cell 7:673-682(2001).
[19]
INTERACTION WITH BNIPL.
PubMed=12901880; DOI=10.1016/S0006-291X(03)01387-1;
Qin W., Hu J., Guo M., Xu J., Li J., Yao G., Zhou X., Jiang H.,
Zhang P., Shen L., Wan D., Gu J.;
"BNIPL-2, a novel homologue of BNIP-2, interacts with Bcl-2 and
Cdc42GAP in apoptosis.";
Biochem. Biophys. Res. Commun. 308:379-385(2003).
[20]
INTERACTION WITH FKBP8.
PubMed=15733859; DOI=10.1016/j.febslet.2005.01.053;
Kang C.B., Tai J., Chia J., Yoon H.S.;
"The flexible loop of Bcl-2 is required for molecular interaction with
immunosuppressant FK-506 binding protein 38 (FKBP38).";
FEBS Lett. 579:1469-1476(2005).
[21]
INTERACTION WITH RAF1.
PubMed=15849194; DOI=10.1074/jbc.M413374200;
Jin S., Zhuo Y., Guo W., Field J.;
"p21-activated Kinase 1 (Pak1)-dependent phosphorylation of Raf-1
regulates its mitochondrial localization, phosphorylation of BAD, and
Bcl-2 association.";
J. Biol. Chem. 280:24698-24705(2005).
[22]
INTERACTION WITH MRPL41.
PubMed=15547950; DOI=10.1002/jcb.20292;
Chintharlapalli S.R., Jasti M., Malladi S., Parsa K.V.L.,
Ballestero R.P., Gonzalez-Garcia M.;
"BMRP is a Bcl-2 binding protein that induces apoptosis.";
J. Cell. Biochem. 94:611-626(2005).
[23]
INTERACTION WITH FKBP8.
PubMed=17090549; DOI=10.1074/jbc.M606181200;
Portier B.P., Taglialatela G.;
"Bcl-2 localized at the nuclear compartment induces apoptosis after
transient overexpression.";
J. Biol. Chem. 281:40493-40502(2006).
[24]
FUNCTION, INTERACTION WITH NLRP1, DOMAIN, AND MUTAGENESIS OF GLY-145.
PubMed=17418785; DOI=10.1016/j.cell.2007.01.045;
Bruey J.M., Bruey-Sedano N., Luciano F., Zhai D., Balpai R., Xu C.,
Kress C.L., Bailly-Maitre B., Li X., Osterman A., Matsuzawa S.,
Terskikh A.V., Faustin B., Reed J.C.;
"Bcl-2 and Bcl-XL regulate proinflammatory caspase-1 activation by
interaction with NALP1.";
Cell 129:45-56(2007).
[25]
PHOSPHORYLATION AT THR-69; SER-70 AND SER-87 BY MAPK8/JNK1, AND
FUNCTION.
PubMed=18570871; DOI=10.1016/j.molcel.2008.06.001;
Wei Y., Pattingre S., Sinha S., Bassik M., Levine B.;
"JNK1-mediated phosphorylation of Bcl-2 regulates starvation-induced
autophagy.";
Mol. Cell 30:678-688(2008).
[26]
INTERACTION WITH G0S2.
PubMed=19706769; DOI=10.1158/0008-5472.CAN-09-0128;
Welch C., Santra M.K., El-Assaad W., Zhu X., Huber W.E., Keys R.A.,
Teodoro J.G., Green M.R.;
"Identification of a protein, G0S2, that lacks Bcl-2 homology domains
and interacts with and antagonizes Bcl-2.";
Cancer Res. 69:6782-6789(2009).
[27]
INTERACTION WITH PPIF.
PubMed=19228691; DOI=10.1074/jbc.M808750200;
Eliseev R.A., Malecki J., Lester T., Zhang Y., Humphrey J.,
Gunter T.E.;
"Cyclophilin D interacts with Bcl2 and exerts an anti-apoptotic
effect.";
J. Biol. Chem. 284:9692-9699(2009).
[28]
INTERACTION WITH EGLN3.
PubMed=20849813; DOI=10.1016/j.bbrc.2010.09.037;
Liu Y., Huo Z., Yan B., Lin X., Zhou Z.N., Liang X., Zhu W., Liang D.,
Li L., Liu Y., Zhao H., Sun Y., Chen Y.H.;
"Prolyl hydroxylase 3 interacts with Bcl-2 to regulate doxorubicin-
induced apoptosis in H9c2 cells.";
Biochem. Biophys. Res. Commun. 401:231-237(2010).
[29]
UBIQUITINATION BY PRKN.
PubMed=20889974; DOI=10.1074/jbc.M110.101469;
Chen D., Gao F., Li B., Wang H., Xu Y., Zhu C., Wang G.;
"Parkin mono-ubiquitinates Bcl-2 and regulates autophagy.";
J. Biol. Chem. 285:38214-38223(2010).
[30]
INTERACTION WITH RTL10/BOP.
PubMed=23055042; DOI=10.1007/s13238-012-2069-7;
Zhang X., Weng C., Li Y., Wang X., Jiang C., Li X., Xu Y., Chen Q.,
Pan L., Tang H.;
"Human Bop is a novel BH3-only member of the Bcl-2 protein family.";
Protein Cell 3:790-801(2012).
[31]
INTERACTION WITH FBXO10, UBIQUITINATION, AND IDENTIFICATION IN THE
SCF(FBXO10) COMPLEX.
PubMed=23431138; DOI=10.1073/pnas.1217271110;
Chiorazzi M., Rui L., Yang Y., Ceribelli M., Tishbi N., Maurer C.W.,
Ranuncolo S.M., Zhao H., Xu W., Chan W.C., Jaffe E.S., Gascoyne R.D.,
Campo E., Rosenwald A., Ott G., Delabie J., Rimsza L.M., Shaham S.,
Staudt L.M.;
"Related F-box proteins control cell death in Caenorhabditis elegans
and human lymphoma.";
Proc. Natl. Acad. Sci. U.S.A. 110:3943-3948(2013).
[32]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[33]
STRUCTURE BY NMR OF 1-207.
PubMed=11248023; DOI=10.1073/pnas.041619798;
Petros A.M., Medek A., Nettesheim D.G., Kim D.H., Yoon H.S., Swift K.,
Matayoshi E.D., Oltersdorf T., Fesik S.W.;
"Solution structure of the antiapoptotic protein bcl-2.";
Proc. Natl. Acad. Sci. U.S.A. 98:3012-3017(2001).
[34]
STRUCTURE BY NMR OF 45-207.
PubMed=15902208; DOI=10.1038/nature03579;
Oltersdorf T., Elmore S.W., Shoemaker A.R., Armstrong R.C.,
Augeri D.J., Belli B.A., Bruncko M., Deckwerth T.L., Dinges J.,
Hajduk P.J., Joseph M.K., Kitada S., Korsmeyer S.J., Kunzer A.R.,
Letai A., Li C., Mitten M.J., Nettesheim D.G., Ng S.-C., Nimmer P.M.,
O'Connor J.M., Oleksijew A., Petros A.M., Reed J.C., Shen W.,
Tahir S.K., Thompson C.B., Tomaselli K.J., Wang B., Wendt M.D.,
Zhang H., Fesik S.W., Rosenberg S.H.;
"An inhibitor of Bcl-2 family proteins induces regression of solid
tumours.";
Nature 435:677-681(2005).
[35]
STRUCTURE BY NMR OF 44-207.
PubMed=17256834; DOI=10.1021/jm061152t;
Bruncko M., Oost T.K., Belli B.A., Ding H., Joseph M.K., Kunzer A.,
Martineau D., McClellan W.J., Mitten M., Ng S.-C., Nimmer P.M.,
Oltersdorf T., Park C.-M., Petros A.M., Shoemaker A.R., Song X.,
Wang X., Wendt M.D., Zhang H., Fesik S.W., Rosenberg S.H.,
Elmore S.W.;
"Studies leading to potent, dual inhibitors of Bcl-2 and Bcl-xL.";
J. Med. Chem. 50:641-662(2007).
-!- FUNCTION: Suppresses apoptosis in a variety of cell systems
including factor-dependent lymphohematopoietic and neural cells.
Regulates cell death by controlling the mitochondrial membrane
permeability. Appears to function in a feedback loop system with
caspases. Inhibits caspase activity either by preventing the
release of cytochrome c from the mitochondria and/or by binding to
the apoptosis-activating factor (APAF-1). May attenuate
inflammation by impairing NLRP1-inflammasome activation, hence
CASP1 activation and IL1B release (PubMed:17418785).
{ECO:0000269|PubMed:17418785, ECO:0000269|PubMed:18570871}.
-!- SUBUNIT: Forms homodimers, and heterodimers with BAX, BAD, BAK and
Bcl-X(L). Heterodimerization with BAX requires intact BH1 and BH2
motifs, and is necessary for anti-apoptotic activity
(PubMed:8183370). Interacts with EI24 (By similarity). Also
interacts with APAF1, BBC3, BCL2L1, BNIPL, MRPL41 and TP53BP2.
Binding to FKBP8 seems to target BCL2 to the mitochondria and
probably interferes with the binding of BCL2 to its targets.
Interacts with BAG1 in an ATP-dependent manner. Interacts with
RAF1 (the 'Ser-338' and 'Ser-339' phosphorylated form). Interacts
(via the BH4 domain) with EGLN3; the interaction prevents the
formation of the BAX-BCL2 complex and inhibits the anti-apoptotic
activity of BCL2. Interacts with G0S2; this interaction also
prevents the formation of the anti-apoptotic BAX-BCL2 complex.
Interacts with RTL10/BOP. Interacts with the SCF(FBXO10) complex.
Interacts (via the loop between motifs BH4 and BH3) with NLRP1
(via LRR repeats), but not with NLRP2, NLRP3, NLRP4, PYCARD, nor
MEFV (PubMed:17418785). {ECO:0000250, ECO:0000269|PubMed:11463391,
ECO:0000269|PubMed:12901880, ECO:0000269|PubMed:15547950,
ECO:0000269|PubMed:15733859, ECO:0000269|PubMed:15849194,
ECO:0000269|PubMed:17090549, ECO:0000269|PubMed:17418785,
ECO:0000269|PubMed:19228691, ECO:0000269|PubMed:19706769,
ECO:0000269|PubMed:20849813, ECO:0000269|PubMed:23055042,
ECO:0000269|PubMed:23431138, ECO:0000269|PubMed:8183370,
ECO:0000269|PubMed:8668206, ECO:0000269|PubMed:9305631}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-77694, EBI-77694;
Q9C0C7:AMBRA1; NbExp=10; IntAct=EBI-77694, EBI-2512975;
Q92934:BAD; NbExp=5; IntAct=EBI-77694, EBI-700771;
Q61337:Bad (xeno); NbExp=6; IntAct=EBI-77694, EBI-400328;
Q16611:BAK1; NbExp=3; IntAct=EBI-77694, EBI-519866;
Q07812:BAX; NbExp=11; IntAct=EBI-77694, EBI-516580;
Q9BXH1:BBC3; NbExp=5; IntAct=EBI-77694, EBI-519884;
P51572:BCAP31; NbExp=2; IntAct=EBI-77694, EBI-77683;
O43521:BCL2L11; NbExp=8; IntAct=EBI-77694, EBI-526406;
O43521-1:BCL2L11; NbExp=3; IntAct=EBI-77694, EBI-526416;
O43521-2:BCL2L11; NbExp=4; IntAct=EBI-77694, EBI-526420;
Q9NYF8:BCLAF1; NbExp=2; IntAct=EBI-77694, EBI-437804;
Q14457:BECN1; NbExp=16; IntAct=EBI-77694, EBI-949378;
P55957:BID; NbExp=8; IntAct=EBI-77694, EBI-519672;
Q13323:BIK; NbExp=5; IntAct=EBI-77694, EBI-700794;
Q91ZE9:Bmf (xeno); NbExp=2; IntAct=EBI-77694, EBI-708032;
O60238:BNIP3L; NbExp=2; IntAct=EBI-77694, EBI-849893;
P38398:BRCA1; NbExp=6; IntAct=EBI-77694, EBI-349905;
Q5S007:LRRK2; NbExp=2; IntAct=EBI-4370304, EBI-5323863;
O15151:MDM4; NbExp=4; IntAct=EBI-77694, EBI-398437;
Q96HR8:NAF1; NbExp=2; IntAct=EBI-77694, EBI-2515597;
Q9C000:NLRP1; NbExp=12; IntAct=EBI-77694, EBI-1220518;
P22736:NR4A1; NbExp=7; IntAct=EBI-77694, EBI-721550;
Q13794:PMAIP1; NbExp=3; IntAct=EBI-77694, EBI-707392;
O15304:SIVA1; NbExp=2; IntAct=EBI-77694, EBI-520756;
P04637:TP53; NbExp=5; IntAct=EBI-77694, EBI-366083;
Q13625:TP53BP2; NbExp=13; IntAct=EBI-77694, EBI-77642;
-!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
{ECO:0000269|PubMed:2250705}; Single-pass membrane protein
{ECO:0000269|PubMed:2250705}. Nucleus membrane
{ECO:0000269|PubMed:2250705}; Single-pass membrane protein
{ECO:0000269|PubMed:2250705}. Endoplasmic reticulum membrane
{ECO:0000269|PubMed:2250705}; Single-pass membrane protein
{ECO:0000269|PubMed:2250705}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Alpha;
IsoId=P10415-1; Sequence=Displayed;
Name=Beta;
IsoId=P10415-2; Sequence=VSP_000512;
Note=Ref.1 (AAA51814) sequence is in conflict in position:
199:L->S. {ECO:0000305};
-!- TISSUE SPECIFICITY: Expressed in a variety of tissues.
-!- DOMAIN: BH1 and BH2 domains are required for the interaction with
BAX and for anti-apoptotic activity. {ECO:0000269|PubMed:8183370}.
-!- DOMAIN: The BH4 motif is required for anti-apoptotic activity and
for interaction with RAF1 and EGLN3.
-!- DOMAIN: The loop between motifs BH4 and BH3 is required for the
interaction with NLRP1. {ECO:0000269|PubMed:17418785}.
-!- PTM: Phosphorylation/dephosphorylation on Ser-70 regulates anti-
apoptotic activity. Growth factor-stimulated phosphorylation on
Ser-70 by PKC is required for the anti-apoptosis activity and
occurs during the G2/M phase of the cell cycle. In the absence of
growth factors, BCL2 appears to be phosphorylated by other protein
kinases such as ERKs and stress-activated kinases. Phosphorylated
by MAPK8/JNK1 at Thr-69, Ser-70 and Ser-87, wich stimulates
starvation-induced autophagy. Dephosphorylated by protein
phosphatase 2A (PP2A) (By similarity). {ECO:0000250}.
-!- PTM: Proteolytically cleaved by caspases during apoptosis. The
cleaved protein, lacking the BH4 motif, has pro-apoptotic
activity, causes the release of cytochrome c into the cytosol
promoting further caspase activity. {ECO:0000269|PubMed:9395403}.
-!- PTM: Monoubiquitinated by PRKN, leading to increase its stability.
Ubiquitinated by SCF(FBXO10), leading to its degradation by the
proteasome. {ECO:0000269|PubMed:20889974,
ECO:0000269|PubMed:23431138}.
-!- DISEASE: Note=A chromosomal aberration involving BCL2 has been
found in chronic lymphatic leukemia. Translocation
t(14;18)(q32;q21) with immunoglobulin gene regions. BCL2 mutations
found in non-Hodgkin lymphomas carrying the chromosomal
translocation could be attributed to the Ig somatic hypermutation
mechanism resulting in nucleotide transitions.
{ECO:0000269|PubMed:2875799, ECO:0000269|PubMed:3285301}.
-!- SIMILARITY: Belongs to the Bcl-2 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/BCL2ID49.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/bcl2/";
-!- WEB RESOURCE: Name=Wikipedia; Note=Bcl-2 entry;
URL="https://en.wikipedia.org/wiki/Bcl-2";
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EMBL; M13994; AAA51813.1; ALT_SEQ; mRNA.
EMBL; M13995; AAA51814.1; ALT_SEQ; mRNA.
EMBL; M14745; AAA35591.1; -; mRNA.
EMBL; X06487; CAA29778.1; -; mRNA.
EMBL; AY220759; AAO26045.1; -; Genomic_DNA.
EMBL; AC021803; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC022726; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471096; EAW63137.1; -; Genomic_DNA.
EMBL; BC027258; AAH27258.1; -; mRNA.
EMBL; S72602; AAD14111.1; ALT_SEQ; Genomic_DNA.
CCDS; CCDS11981.1; -. [P10415-1]
CCDS; CCDS45882.1; -. [P10415-2]
PIR; B29409; TVHUB1.
PIR; C37332; TVHUA1.
RefSeq; NP_000624.2; NM_000633.2. [P10415-1]
RefSeq; NP_000648.2; NM_000657.2. [P10415-2]
UniGene; Hs.150749; -.
PDB; 1G5M; NMR; -; A=1-34, A=92-207.
PDB; 1GJH; NMR; -; A=1-34, A=92-207.
PDB; 1YSW; NMR; -; A=3-33, A=92-206.
PDB; 2O21; NMR; -; A=3-34, A=92-207.
PDB; 2O22; NMR; -; A=3-34, A=92-207.
PDB; 2O2F; NMR; -; A=8-31, A=92-204.
PDB; 2W3L; X-ray; 2.10 A; A/B=92-206.
PDB; 2XA0; X-ray; 2.70 A; A/B=1-207.
PDB; 4AQ3; X-ray; 2.40 A; A/B/C/D/E/F=1-33, A/B/C/D/E/F=92-207.
PDB; 4IEH; X-ray; 2.10 A; A=1-34, A=92-207.
PDB; 4LVT; X-ray; 2.05 A; A/B=1-34, A/B=92-207.
PDB; 4LXD; X-ray; 1.90 A; A=1-34, A=92-207.
PDB; 4MAN; X-ray; 2.07 A; A/B=1-34, A/B=92-207.
PDB; 5AGW; X-ray; 2.69 A; A/B=1-34, A/B=92-207.
PDB; 5AGX; X-ray; 2.24 A; A/B=1-34, A/B=92-207.
PDB; 5FCG; X-ray; 2.10 A; A=1-207.
PDB; 5JSN; X-ray; 2.10 A; A/C=1-207.
PDBsum; 1G5M; -.
PDBsum; 1GJH; -.
PDBsum; 1YSW; -.
PDBsum; 2O21; -.
PDBsum; 2O22; -.
PDBsum; 2O2F; -.
PDBsum; 2W3L; -.
PDBsum; 2XA0; -.
PDBsum; 4AQ3; -.
PDBsum; 4IEH; -.
PDBsum; 4LVT; -.
PDBsum; 4LXD; -.
PDBsum; 4MAN; -.
PDBsum; 5AGW; -.
PDBsum; 5AGX; -.
PDBsum; 5FCG; -.
PDBsum; 5JSN; -.
DisProt; DP00297; -.
ProteinModelPortal; P10415; -.
SMR; P10415; -.
BioGrid; 107068; 100.
DIP; DIP-1043N; -.
IntAct; P10415; 47.
MINT; MINT-87089; -.
STRING; 9606.ENSP00000329623; -.
BindingDB; P10415; -.
ChEMBL; CHEMBL4860; -.
DrugBank; DB05764; ABT-263.
DrugBank; DB05297; DHA-paclitaxel.
DrugBank; DB01248; Docetaxel.
DrugBank; DB04940; E7389.
DrugBank; DB01050; Ibuprofen.
DrugBank; DB01229; Paclitaxel.
DrugBank; DB01367; Rasagiline.
DrugBank; DB05281; S-8184.
DrugBank; DB11581; Venetoclax.
GuidetoPHARMACOLOGY; 2844; -.
iPTMnet; P10415; -.
PhosphoSitePlus; P10415; -.
BioMuta; BCL2; -.
DMDM; 231632; -.
EPD; P10415; -.
MaxQB; P10415; -.
PaxDb; P10415; -.
PeptideAtlas; P10415; -.
PRIDE; P10415; -.
DNASU; 596; -.
Ensembl; ENST00000333681; ENSP00000329623; ENSG00000171791. [P10415-1]
Ensembl; ENST00000398117; ENSP00000381185; ENSG00000171791. [P10415-1]
Ensembl; ENST00000589955; ENSP00000466417; ENSG00000171791. [P10415-2]
GeneID; 596; -.
KEGG; hsa:596; -.
UCSC; uc002lit.2; human. [P10415-1]
CTD; 596; -.
DisGeNET; 596; -.
GeneCards; BCL2; -.
HGNC; HGNC:990; BCL2.
HPA; CAB000003; -.
HPA; HPA055295; -.
MalaCards; BCL2; -.
MIM; 151430; gene+phenotype.
neXtProt; NX_P10415; -.
OpenTargets; ENSG00000171791; -.
Orphanet; 545; Follicular lymphoma.
Orphanet; 98839; Intravascular large B-cell lymphoma.
PharmGKB; PA25302; -.
eggNOG; KOG4728; Eukaryota.
eggNOG; ENOG41123S0; LUCA.
GeneTree; ENSGT00530000062935; -.
HOGENOM; HOG000056452; -.
HOVERGEN; HBG004472; -.
InParanoid; P10415; -.
KO; K02161; -.
OMA; EWDAGDA; -.
OrthoDB; EOG091G0OCU; -.
PhylomeDB; P10415; -.
TreeFam; TF315834; -.
Reactome; R-HSA-111447; Activation of BAD and translocation to mitochondria.
Reactome; R-HSA-111453; BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members.
Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
Reactome; R-HSA-844455; The NLRP1 inflammasome.
SIGNOR; P10415; -.
ChiTaRS; BCL2; human.
EvolutionaryTrace; P10415; -.
GeneWiki; Bcl-2; -.
GenomeRNAi; 596; -.
PMAP-CutDB; P10415; -.
PRO; PR:P10415; -.
Proteomes; UP000005640; Chromosome 18.
Bgee; ENSG00000171791; -.
CleanEx; HS_BCL2; -.
ExpressionAtlas; P10415; baseline and differential.
Genevisible; P10415; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0046930; C:pore complex; IDA:BHF-UCL.
GO; GO:0043234; C:protein complex; IMP:CAFA.
GO; GO:0051434; F:BH3 domain binding; IPI:UniProtKB.
GO; GO:0015267; F:channel activity; IDA:BHF-UCL.
GO; GO:0016248; F:channel inhibitor activity; IDA:BHF-UCL.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0002020; F:protease binding; IDA:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0051721; F:protein phosphatase 2A binding; IEA:Ensembl.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
GO; GO:0008134; F:transcription factor binding; IEA:Ensembl.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0007015; P:actin filament organization; IEA:Ensembl.
GO; GO:0006915; P:apoptotic process; IDA:MGI.
GO; GO:0031103; P:axon regeneration; IEA:Ensembl.
GO; GO:0007409; P:axonogenesis; IEA:Ensembl.
GO; GO:0001782; P:B cell homeostasis; IEA:Ensembl.
GO; GO:0002326; P:B cell lineage commitment; IEA:Ensembl.
GO; GO:0042100; P:B cell proliferation; IDA:MGI.
GO; GO:0050853; P:B cell receptor signaling pathway; IMP:UniProtKB.
GO; GO:0001662; P:behavioral fear response; IEA:Ensembl.
GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IEA:Ensembl.
GO; GO:0043375; P:CD8-positive, alpha-beta T cell lineage commitment; IEA:Ensembl.
GO; GO:0007569; P:cell aging; IEA:Ensembl.
GO; GO:0016049; P:cell growth; IEA:Ensembl.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
GO; GO:0042149; P:cellular response to glucose starvation; IEA:Ensembl.
GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
GO; GO:0071310; P:cellular response to organic substance; IEA:Ensembl.
GO; GO:0021747; P:cochlear nucleus development; IEA:Ensembl.
GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
GO; GO:0048546; P:digestive tract morphogenesis; IEA:Ensembl.
GO; GO:0043583; P:ear development; IEA:Ensembl.
GO; GO:0032469; P:endoplasmic reticulum calcium ion homeostasis; TAS:UniProtKB.
GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IDA:MGI.
GO; GO:0007565; P:female pregnancy; NAS:UniProtKB.
GO; GO:0048041; P:focal adhesion assembly; IEA:Ensembl.
GO; GO:0022612; P:gland morphogenesis; IEA:Ensembl.
GO; GO:0032835; P:glomerulus development; IEA:Ensembl.
GO; GO:0031069; P:hair follicle morphogenesis; IEA:Ensembl.
GO; GO:0048873; P:homeostasis of number of cells within a tissue; IEA:Ensembl.
GO; GO:0006959; P:humoral immune response; TAS:UniProtKB.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IBA:GO_Central.
GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IDA:MGI.
GO; GO:0008631; P:intrinsic apoptotic signaling pathway in response to oxidative stress; IEA:Ensembl.
GO; GO:0002320; P:lymphoid progenitor cell differentiation; IEA:Ensembl.
GO; GO:0008584; P:male gonad development; IEA:Ensembl.
GO; GO:0006582; P:melanin metabolic process; IEA:Ensembl.
GO; GO:0030318; P:melanocyte differentiation; IEA:Ensembl.
GO; GO:0014031; P:mesenchymal cell development; IEA:Ensembl.
GO; GO:0001656; P:metanephros development; IEA:Ensembl.
GO; GO:2000811; P:negative regulation of anoikis; IMP:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IMP:UniProtKB.
GO; GO:0010507; P:negative regulation of autophagy; TAS:UniProtKB.
GO; GO:0010523; P:negative regulation of calcium ion transport into cytosol; IEA:Ensembl.
GO; GO:0030308; P:negative regulation of cell growth; IEA:Ensembl.
GO; GO:0030336; P:negative regulation of cell migration; IEA:Ensembl.
GO; GO:0032848; P:negative regulation of cellular pH reduction; IDA:UniProtKB.
GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IGI:MGI.
GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IEA:Ensembl.
GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IDA:UniProtKB.
GO; GO:0051902; P:negative regulation of mitochondrial depolarization; TAS:UniProtKB.
GO; GO:0033033; P:negative regulation of myeloid cell apoptotic process; IEA:Ensembl.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IDA:MGI.
GO; GO:0030279; P:negative regulation of ossification; IEA:Ensembl.
GO; GO:0033689; P:negative regulation of osteoblast proliferation; IEA:Ensembl.
GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; IEA:Ensembl.
GO; GO:0046671; P:negative regulation of retinal cell programmed cell death; IEA:Ensembl.
GO; GO:0051402; P:neuron apoptotic process; TAS:HGNC.
GO; GO:0048599; P:oocyte development; IEA:Ensembl.
GO; GO:0035265; P:organ growth; IEA:Ensembl.
GO; GO:0001503; P:ossification; IEA:Ensembl.
GO; GO:0001541; P:ovarian follicle development; IEA:Ensembl.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IEA:Ensembl.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; IEA:Ensembl.
GO; GO:0048753; P:pigment granule organization; IEA:Ensembl.
GO; GO:0030890; P:positive regulation of B cell proliferation; IMP:UniProtKB.
GO; GO:0043085; P:positive regulation of catalytic activity; IEA:Ensembl.
GO; GO:0030307; P:positive regulation of cell growth; IDA:MGI.
GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; TAS:Reactome.
GO; GO:0045636; P:positive regulation of melanocyte differentiation; IEA:Ensembl.
GO; GO:0040018; P:positive regulation of multicellular organism growth; IEA:Ensembl.
GO; GO:0014042; P:positive regulation of neuron maturation; IEA:Ensembl.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
GO; GO:1900740; P:positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; TAS:Reactome.
GO; GO:0048743; P:positive regulation of skeletal muscle fiber development; IEA:Ensembl.
GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IEA:Ensembl.
GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
GO; GO:0006470; P:protein dephosphorylation; IEA:Ensembl.
GO; GO:0000209; P:protein polyubiquitination; IDA:MGI.
GO; GO:0072593; P:reactive oxygen species metabolic process; IEA:Ensembl.
GO; GO:0051924; P:regulation of calcium ion transport; IDA:MGI.
GO; GO:0001952; P:regulation of cell-matrix adhesion; IEA:Ensembl.
GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl.
GO; GO:0010559; P:regulation of glycoprotein biosynthetic process; IEA:Ensembl.
GO; GO:0046902; P:regulation of mitochondrial membrane permeability; ISS:HGNC.
GO; GO:0051881; P:regulation of mitochondrial membrane potential; ISS:HGNC.
GO; GO:0006808; P:regulation of nitrogen utilization; IEA:Ensembl.
GO; GO:0043497; P:regulation of protein heterodimerization activity; IDA:UniProtKB.
GO; GO:0043496; P:regulation of protein homodimerization activity; IDA:UniProtKB.
GO; GO:0031647; P:regulation of protein stability; IEA:Ensembl.
GO; GO:0022898; P:regulation of transmembrane transporter activity; IDA:BHF-UCL.
GO; GO:0045069; P:regulation of viral genome replication; IEA:Ensembl.
GO; GO:0001836; P:release of cytochrome c from mitochondria; ISS:HGNC.
GO; GO:0003014; P:renal system process; IEA:Ensembl.
GO; GO:0034097; P:response to cytokine; IDA:MGI.
GO; GO:0042493; P:response to drug; IDA:MGI.
GO; GO:0010332; P:response to gamma radiation; IEA:Ensembl.
GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
GO; GO:0010039; P:response to iron ion; IDA:UniProtKB.
GO; GO:0002931; P:response to ischemia; IEA:Ensembl.
GO; GO:0035094; P:response to nicotine; IDA:UniProtKB.
GO; GO:0009314; P:response to radiation; NAS:UniProtKB.
GO; GO:0009636; P:response to toxic substance; IDA:HGNC.
GO; GO:0010224; P:response to UV-B; IEA:Ensembl.
GO; GO:0016337; P:single organismal cell-cell adhesion; IEA:Ensembl.
GO; GO:0048536; P:spleen development; IEA:Ensembl.
GO; GO:0033077; P:T cell differentiation in thymus; IEA:Ensembl.
GO; GO:0043029; P:T cell homeostasis; IEA:Ensembl.
GO; GO:0048538; P:thymus development; IEA:Ensembl.
InterPro; IPR013278; Apop_reg_Bcl2.
InterPro; IPR002475; Bcl2-like.
InterPro; IPR004725; Bcl2/BclX.
InterPro; IPR020717; Bcl2_BH1_motif_CS.
InterPro; IPR020726; Bcl2_BH2_motif_CS.
InterPro; IPR020728; Bcl2_BH3_motif_CS.
InterPro; IPR003093; Bcl2_BH4.
InterPro; IPR020731; Bcl2_BH4_motif_CS.
InterPro; IPR026298; Blc2_fam.
PANTHER; PTHR11256; PTHR11256; 1.
PANTHER; PTHR11256:SF55; PTHR11256:SF55; 1.
Pfam; PF00452; Bcl-2; 1.
Pfam; PF02180; BH4; 1.
PRINTS; PR01863; APOPREGBCL2.
PRINTS; PR01862; BCL2FAMILY.
SMART; SM00265; BH4; 1.
SUPFAM; SSF56854; SSF56854; 1.
TIGRFAMs; TIGR00865; bcl-2; 1.
PROSITE; PS50062; BCL2_FAMILY; 1.
PROSITE; PS01080; BH1; 1.
PROSITE; PS01258; BH2; 1.
PROSITE; PS01259; BH3; 1.
PROSITE; PS01260; BH4_1; 1.
PROSITE; PS50063; BH4_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Apoptosis;
Chromosomal rearrangement; Complete proteome; Disease mutation;
Endoplasmic reticulum; Membrane; Mitochondrion;
Mitochondrion outer membrane; Nucleus; Phosphoprotein; Polymorphism;
Proto-oncogene; Reference proteome; Transmembrane;
Transmembrane helix; Ubl conjugation.
CHAIN 1 239 Apoptosis regulator Bcl-2.
/FTId=PRO_0000143048.
TRANSMEM 212 233 Helical. {ECO:0000255}.
MOTIF 10 30 BH4.
MOTIF 93 107 BH3.
MOTIF 136 155 BH1.
MOTIF 187 202 BH2.
SITE 34 35 Cleavage; by caspase-3.
MOD_RES 69 69 Phosphothreonine; by MAPK8.
{ECO:0000269|PubMed:18570871}.
MOD_RES 70 70 Phosphoserine; by MAPK8 and PKC.
{ECO:0000269|PubMed:18570871}.
MOD_RES 87 87 Phosphoserine; by MAPK8.
{ECO:0000269|PubMed:18570871}.
VAR_SEQ 196 239 DAFVELYGPSMRPLFDFSWLSLKTLLSLALVGACITLGAYL
GHK -> VGALGDVSLG (in isoform Beta).
{ECO:0000303|PubMed:3523487}.
/FTId=VSP_000512.
VARIANT 7 7 T -> S. {ECO:0000269|PubMed:2834197,
ECO:0000269|PubMed:3285301}.
/FTId=VAR_000827.
VARIANT 43 43 A -> T (in dbSNP:rs1800477).
{ECO:0000269|Ref.6}.
/FTId=VAR_014716.
VARIANT 59 59 P -> S (in non-Hodgkin lymphoma; somatic
mutation). {ECO:0000269|PubMed:1339299}.
/FTId=VAR_000828.
VARIANT 93 93 V -> I (in non-Hodgkin lymphoma; somatic
mutation). {ECO:0000269|PubMed:1339299}.
/FTId=VAR_000829.
MUTAGEN 34 34 D->A: Abolishes cleavage by caspase-3.
MUTAGEN 64 64 D->A: No effect on cleavage by caspase-3.
MUTAGEN 138 141 FRDG->AAAA: Loss of BAX-binding and of
anti-apoptotic activity.
{ECO:0000269|PubMed:8183370}.
MUTAGEN 144 144 W->A: Loss of BAX-binding and of anti-
apoptotic activity; when associated with
A-145 and A146.
{ECO:0000269|PubMed:8183370}.
MUTAGEN 145 145 G->A: Loss of BAX-binding and of anti-
apoptotic activity. No effect on NLRP1-
induced IL1B release, nor on
homodimerization. Loss of BAX-binding and
of anti-apoptotic activity; when
associated with A-145 and A146.
{ECO:0000269|PubMed:17418785,
ECO:0000269|PubMed:8183370}.
MUTAGEN 145 145 G->E: Loss of BAX-binding and of anti-
apoptotic activity. No effect on
homodimerization.
{ECO:0000269|PubMed:17418785,
ECO:0000269|PubMed:8183370}.
MUTAGEN 146 146 R->A: Loss of BAX-binding and of anti-
apoptotic activity; when associated with
A-144 and A145.
{ECO:0000269|PubMed:8183370}.
MUTAGEN 188 188 W->A: Loss of BAX-binding and of anti-
apoptotic activity. No effect on
homodimerization.
{ECO:0000269|PubMed:8183370}.
MUTAGEN 190 190 Q->L: Partial loss of BAX-binding and 50%
decrease in anti-apoptotic activity; when
associated with A-191 and A-192. No
effect on homodimerization; when
associated with L-190 and A-191.
{ECO:0000269|PubMed:8183370}.
MUTAGEN 191 191 D->A: No effect on BAX-binding, nor on
anti-apoptotic activity. Partial loss of
BAX-binding and 50% decrease in anti-
apoptotic activity; when associated with
L-190 and A-192. No effect on
homodimerization; when associated with L-
190 and A-191.
{ECO:0000269|PubMed:8183370}.
MUTAGEN 192 192 N->A: Partial loss of BAX-binding and 50%
decrease in anti-apoptotic activity; when
associated with L-190 and A-191. No
effect on homodimerization; when
associated with L-190 and A-191.
{ECO:0000269|PubMed:8183370}.
MUTAGEN 194 197 Missing: Loss of BAX-binding and of anti-
apoptotic activity. May also affect
protein stability.
{ECO:0000269|PubMed:8183370}.
MUTAGEN 200 200 E->A: Partial loss of BAX-binding and 50%
decrease in anti-apoptotic activity.
{ECO:0000269|PubMed:8183370}.
CONFLICT 48 48 I -> F (in Ref. 4; CAA29778).
{ECO:0000305}.
CONFLICT 59 59 P -> T (in Ref. 3; AAA35591).
{ECO:0000305}.
CONFLICT 96 96 T -> A (in Ref. 10; AAD14111).
{ECO:0000305}.
CONFLICT 110 110 R -> G (in Ref. 10; AAD14111).
{ECO:0000305}.
CONFLICT 117 117 S -> R (in Ref. 3; AAA35591).
{ECO:0000305}.
CONFLICT 129 129 R -> C (in Ref. 4; CAA29778).
{ECO:0000305}.
HELIX 11 25 {ECO:0000244|PDB:4LXD}.
TURN 32 34 {ECO:0000244|PDB:1G5M}.
HELIX 93 107 {ECO:0000244|PDB:4LXD}.
HELIX 109 118 {ECO:0000244|PDB:4LXD}.
TURN 123 125 {ECO:0000244|PDB:4LXD}.
HELIX 126 137 {ECO:0000244|PDB:4LXD}.
TURN 138 140 {ECO:0000244|PDB:4LXD}.
HELIX 144 163 {ECO:0000244|PDB:4LXD}.
HELIX 169 184 {ECO:0000244|PDB:4LXD}.
HELIX 186 191 {ECO:0000244|PDB:4LXD}.
HELIX 194 202 {ECO:0000244|PDB:4LXD}.
HELIX 203 205 {ECO:0000244|PDB:2XA0}.
SEQUENCE 239 AA; 26266 MW; 3C49F2B714DC9CCB CRC64;
MAHAGRTGYD NREIVMKYIH YKLSQRGYEW DAGDVGAAPP GAAPAPGIFS SQPGHTPHPA
ASRDPVARTS PLQTPAAPGA AAGPALSPVP PVVHLTLRQA GDDFSRRYRR DFAEMSSQLH
LTPFTARGRF ATVVEELFRD GVNWGRIVAF FEFGGVMCVE SVNREMSPLV DNIALWMTEY
LNRHLHTWIQ DNGGWDAFVE LYGPSMRPLF DFSWLSLKTL LSLALVGACI TLGAYLGHK


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