B2CL1_HUMAN
ID B2CL1_HUMAN Reviewed; 233 AA.
AC Q07817; E1P5L6; Q5CZ89; Q5TE65; Q92976;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 246.
DE RecName: Full=Bcl-2-like protein 1;
DE Short=Bcl2-L-1;
DE AltName: Full=Apoptosis regulator Bcl-X;
GN Name=BCL2L1; Synonyms=BCL2L, BCLX;
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 BCL-X(L) AND BCL-X(S)).
RX PubMed=8358789; DOI=10.1016/0092-8674(93)90508-n;
RA Boise L.H., Gonzalez-Garcia M., Postema C.E., Ding L., Lindsten T.,
RA Turka L.A., Mao X., Nunez G., Thompson C.B.;
RT "bcl-x, a bcl-2-related gene that functions as a dominant regulator of
RT apoptotic cell death.";
RL Cell 74:597-608(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BCL-X(BETA)), AND INTERACTION WITH BAX.
RX PubMed=9675101; DOI=10.1006/bbrc.1998.8907;
RA Ban J., Eckhart L., Weninger W., Mildner M., Tschachler E.;
RT "Identification of a human cDNA encoding a novel Bcl-x isoform.";
RL Biochem. Biophys. Res. Commun. 248:147-152(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM BCL-X(BETA)).
RA Inohara N., Ohta S.;
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BCL-X(L)).
RC TISSUE=Colon carcinoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BCL-X(L)).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [7]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BCL-X(L)).
RC TISSUE=Lung;
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 [9]
RP MUTAGENESIS OF GLY-138, AND HETERODIMERIZATION.
RX PubMed=7644501; DOI=10.1073/pnas.92.17.7834;
RA Sedlak T.W., Oltvai Z.N., Yang E., Wang K., Boise L.H., Thompson C.B.,
RA Korsmeyer S.J.;
RT "Multiple Bcl-2 family members demonstrate selective dimerizations with
RT Bax.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:7834-7838(1995).
RN [10]
RP MUTAGENESIS OF GLY-148; ASP-156; ASP-176 AND ASP-189.
RX PubMed=8596636; DOI=10.1038/379554a0;
RA Cheng E.H.-Y., Levine B., Boise L.H., Thompson C.B., Hardwick J.M.,
RA Korsmeyer S.J.;
RT "Bax-independent inhibition of apoptosis by Bcl-XL.";
RL Nature 379:554-556(1996).
RN [11]
RP CLEAVAGE BY CASPASES, AND MUTAGENESIS OF ASP-61.
RX PubMed=9435230; DOI=10.1073/pnas.95.2.554;
RA Clem R.J., Cheng E.H.-Y., Karp C.L., Kirsch D.G., Ueno K., Takahashi A.,
RA Kastan M.B., Griffin D.E., Earnshaw W.C., Veliuona M.A., Hardwick J.M.;
RT "Modulation of cell death by Bcl-xL through caspase interaction.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:554-559(1998).
RN [12]
RP INTERACTION WITH BAX.
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 [13]
RP INTERACTION WITH IKZF3.
RX PubMed=11714801; DOI=10.4049/jimmunol.167.11.6366;
RA Rebollo A., Ayllon V., Fleischer A., Martinez C.A., Zaballos A.;
RT "The association of Aiolos transcription factor and Bcl-xL is involved in
RT the control of apoptosis.";
RL J. Immunol. 167:6366-6373(2001).
RN [14]
RP INTERACTION WITH BCL2 AND BBC3.
RX PubMed=11463391; DOI=10.1016/s1097-2765(01)00213-1;
RA Yu J., Zhang L., Hwang P.M., Kinzler K.W., Vogelstein B.;
RT "PUMA induces the rapid apoptosis of colorectal cancer cells.";
RL Mol. Cell 7:673-682(2001).
RN [15]
RP INTERACTION WITH SIVA1.
RX PubMed=12011449; DOI=10.1073/pnas.102182299;
RA Xue L., Chu F., Cheng Y., Sun X., Borthakur A., Ramarao M., Pandey P.,
RA Wu M., Schlossman S.F., Prasad K.V.S.;
RT "Siva-1 binds to and inhibits BCL-X(L)-mediated protection against UV
RT radiation-induced apoptosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:6925-6930(2002).
RN [16]
RP INTERACTION WITH PGAM5.
RX PubMed=17046835; DOI=10.1074/jbc.m606539200;
RA Lo S.-C., Hannink M.;
RT "PGAM5, a Bcl-XL-interacting protein, is a novel substrate for the redox-
RT regulated Keap1-dependent ubiquitin ligase complex.";
RL J. Biol. Chem. 281:37893-37903(2006).
RN [17]
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 [18]
RP FUNCTION, AND INTERACTION WITH NLRP1.
RX PubMed=17418785; DOI=10.1016/j.cell.2007.01.045;
RA Bruey J.M., Bruey-Sedano N., Luciano F., Zhai D., Balpai R., Xu C.,
RA Kress C.L., Bailly-Maitre B., Li X., Osterman A., Matsuzawa S.,
RA Terskikh A.V., Faustin B., Reed J.C.;
RT "Bcl-2 and Bcl-XL regulate proinflammatory caspase-1 activation by
RT interaction with NALP1.";
RL Cell 129:45-56(2007).
RN [19]
RP FUNCTION IN APOPTOSIS, PHOSPHORYLATION AT SER-62 BY CDK1, AND SUBCELLULAR
RP LOCATION.
RX PubMed=19917720; DOI=10.1128/mcb.00882-09;
RA Terrano D.T., Upreti M., Chambers T.C.;
RT "Cyclin-dependent kinase 1-mediated Bcl-xL/Bcl-2 phosphorylation acts as a
RT functional link coupling mitotic arrest and apoptosis.";
RL Mol. Cell. Biol. 30:640-656(2010).
RN [20]
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 [21]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-49, AND MUTAGENESIS
RP OF SER-49.
RX PubMed=21840391; DOI=10.1016/j.cellsig.2011.07.017;
RA Wang J., Beauchemin M., Bertrand R.;
RT "Bcl-xL phosphorylation at Ser49 by polo kinase 3 during cell cycle
RT progression and checkpoints.";
RL Cell. Signal. 23:2030-2038(2011).
RN [22]
RP INTERACTION WITH BECN1.
RX PubMed=22498477; DOI=10.4161/auto.19084;
RA Robert G., Gastaldi C., Puissant A., Hamouda A., Jacquel A., Dufies M.,
RA Belhacene N., Colosetti P., Reed J.C., Auberger P., Luciano F.;
RT "The anti-apoptotic Bcl-B protein inhibits BECN1-dependent autophagic cell
RT death.";
RL Autophagy 8:637-649(2012).
RN [23]
RP INTERACTION WITH CLU.
RX PubMed=21567405; DOI=10.1002/jcp.22836;
RA Kim N., Yoo J.C., Han J.Y., Hwang E.M., Kim Y.S., Jeong E.Y., Sun C.H.,
RA Yi G.S., Roh G.S., Kim H.J., Kang S.S., Cho G.J., Park J.Y., Choi W.S.;
RT "Human nuclear clusterin mediates apoptosis by interacting with Bcl-XL
RT through C-terminal coiled coil domain.";
RL J. Cell. Physiol. 227:1157-1167(2012).
RN [24]
RP INTERACTION WITH RTL10.
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 [25]
RP INTERACTION WITH DNM1L, FUNCTION, AND MUTAGENESIS OF 145-SER--GLY-147 AND
RP 188-TRP--PHE-191.
RX PubMed=23792689; DOI=10.1038/ncb2791;
RA Li H., Alavian K.N., Lazrove E., Mehta N., Jones A., Zhang P.,
RA Licznerski P., Graham M., Uo T., Guo J., Rahner C., Duman R.S.,
RA Morrison R.S., Jonas E.A.;
RT "A Bcl-xL-Drp1 complex regulates synaptic vesicle membrane dynamics during
RT endocytosis.";
RL Nat. Cell Biol. 15:773-785(2013).
RN [26]
RP INTERACTION WITH VDAC1.
RX PubMed=25296756; DOI=10.1074/jbc.m114.567792;
RA Li L., Yao Y.C., Gu X.Q., Che D., Ma C.Q., Dai Z.Y., Li C., Zhou T.,
RA Cai W.B., Yang Z.H., Yang X., Gao G.Q.;
RT "Plasminogen kringle 5 induces endothelial cell apoptosis by triggering a
RT voltage-dependent anion channel 1 (VDAC1) positive feedback loop.";
RL J. Biol. Chem. 289:32628-32638(2014).
RN [27]
RP IDENTIFICATION BY MASS 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 [28]
RP INTERACTION WITH BCL2L11.
RX PubMed=27013495; DOI=10.15252/embr.201541392;
RA Weber A., Heinlein M., Dengjel J., Alber C., Singh P.K., Haecker G.;
RT "The deubiquitinase Usp27x stabilizes the BH3-only protein Bim and enhances
RT apoptosis.";
RL EMBO Rep. 17:724-738(2016).
RN [29]
RP UBIQUITINATION, PROTEASOMAL DEGRADATION, AND INTERACTION WITH RNF183.
RX PubMed=29507230; DOI=10.1073/pnas.1716439115;
RA Wu Y., Li X., Jia J., Zhang Y., Li J., Zhu Z., Wang H., Tang J., Hu J.;
RT "Transmembrane E3 ligase RNF183 mediates ER stress-induced apoptosis by
RT degrading Bcl-xL.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E2762-E2771(2018).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), AND STRUCTURE BY NMR OF 1-209.
RX PubMed=8692274; DOI=10.1038/381335a0;
RA Muchmore S.W., Sattler M., Liang H., Meadows R.P., Harlan J.E., Yoon H.S.,
RA Nettesheim D., Chang B.S., Thompson C.B., Wong S.L., Ng S.L., Fesik S.W.;
RT "X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell
RT death.";
RL Nature 381:335-341(1996).
RN [31]
RP STRUCTURE BY NMR OF 1-209.
RX PubMed=9020082; DOI=10.1126/science.275.5302.983;
RA Sattler M., Liang H., Nettesheim D., Meadows R.P., Harlan J.E.,
RA Eberstadt M., Yoon H.S., Shuker S.B., Chang B.S., Minn A.J., Thompson C.B.,
RA Fesik S.W.;
RT "Structure of Bcl-xL-Bak peptide complex: recognition between regulators of
RT apoptosis.";
RL Science 275:983-986(1997).
RN [32]
RP STRUCTURE BY NMR OF 1-209 IN COMPLEX WITH BAD.
RX PubMed=11206074; DOI=10.1110/ps.9.12.2528;
RA Petros A.M., Nettesheim D.G., Wang Y., Olejniczak E.T., Meadows R.P.,
RA Mack J., Swift K., Matayoshi E.D., Zhang H., Thompson C.B., Fesik S.W.;
RT "Rationale for Bcl-xL/Bad peptide complex formation from structure,
RT mutagenesis, and biophysical studies.";
RL Protein Sci. 9:2528-2534(2000).
RN [33]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1-211.
RX PubMed=14534311; DOI=10.1074/jbc.m306021200;
RA Manion M.K., O'Neill J.W., Giedt C.D., Kim K.M., Zhang K.Y.Z.,
RA Hockenbery D.M.;
RT "Bcl-XL mutations suppress cellular sensitivity to antimycin A.";
RL J. Biol. Chem. 279:2159-2165(2004).
RN [34]
RP STRUCTURE BY NMR OF 1-209.
RX PubMed=15902208; DOI=10.1038/nature03579;
RA Oltersdorf T., Elmore S.W., Shoemaker A.R., Armstrong R.C., Augeri D.J.,
RA Belli B.A., Bruncko M., Deckwerth T.L., Dinges J., Hajduk P.J.,
RA Joseph M.K., Kitada S., Korsmeyer S.J., Kunzer A.R., Letai A., Li C.,
RA Mitten M.J., Nettesheim D.G., Ng S.-C., Nimmer P.M., O'Connor J.M.,
RA Oleksijew A., Petros A.M., Reed J.C., Shen W., Tahir S.K., Thompson C.B.,
RA Tomaselli K.J., Wang B., Wendt M.D., Zhang H., Fesik S.W., Rosenberg S.H.;
RT "An inhibitor of Bcl-2 family proteins induces regression of solid
RT tumours.";
RL Nature 435:677-681(2005).
RN [35]
RP X-RAY CRYSTALLOGRAPHY (3.45 ANGSTROMS) OF 1-211, AND HOMODIMERIZATION.
RX PubMed=16368107; DOI=10.1016/j.jmb.2005.11.032;
RA O'Neill J.W., Manion M.K., Maguire B., Hockenbery D.M.;
RT "BCL-XL dimerization by three-dimensional domain swapping.";
RL J. Mol. Biol. 356:367-381(2006).
RN [36]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 83-209 IN COMPLEX WITH BECN1.
RX PubMed=17337444; DOI=10.1074/jbc.m700492200;
RA Oberstein A., Jeffrey P.D., Shi Y.;
RT "Crystal structure of the Bcl-XL-Beclin 1 peptide complex: Beclin 1 is a
RT novel BH3-only protein.";
RL J. Biol. Chem. 282:13123-13132(2007).
RN [37]
RP STRUCTURE BY NMR OF 1-209.
RX PubMed=17256834; DOI=10.1021/jm061152t;
RA Bruncko M., Oost T.K., Belli B.A., Ding H., Joseph M.K., Kunzer A.,
RA Martineau D., McClellan W.J., Mitten M., Ng S.-C., Nimmer P.M.,
RA Oltersdorf T., Park C.-M., Petros A.M., Shoemaker A.R., Song X., Wang X.,
RA Wendt M.D., Zhang H., Fesik S.W., Rosenberg S.H., Elmore S.W.;
RT "Studies leading to potent, dual inhibitors of Bcl-2 and Bcl-xL.";
RL J. Med. Chem. 50:641-662(2007).
RN [38]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1-209 IN COMPLEX WITH HEBP2, AND
RP INTERACTION WITH HEBP2.
RX PubMed=21639858; DOI=10.1042/bj20110257;
RA Ambrosi E., Capaldi S., Bovi M., Saccomani G., Perduca M., Monaco H.L.;
RT "Structural changes in the BH3 domain of SOUL protein upon interaction with
RT the anti-apoptotic protein Bcl-xL.";
RL Biochem. J. 438:291-301(2011).
RN [39]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-209 IN COMPLEX WITH BBC3,
RP STRUCTURE BY NMR OF 1-209 IN COMPLEX WITH BBC3, AND INTERACTION WITH BBC3
RP AND TP53.
RX PubMed=23340338; DOI=10.1038/nchembio.1166;
RA Follis A.V., Chipuk J.E., Fisher J.C., Yun M.K., Grace C.R., Nourse A.,
RA Baran K., Ou L., Min L., White S.W., Green D.R., Kriwacki R.W.;
RT "PUMA binding induces partial unfolding within BCL-xL to disrupt p53
RT binding and promote apoptosis.";
RL Nat. Chem. Biol. 9:163-168(2013).
CC -!- FUNCTION: Potent inhibitor of cell death. Inhibits activation of
CC caspases. Appears to regulate cell death by blocking the voltage-
CC dependent anion channel (VDAC) by binding to it and preventing the
CC release of the caspase activator, CYC1, from the mitochondrial
CC membrane. Also acts as a regulator of G2 checkpoint and progression to
CC cytokinesis during mitosis.
CC -!- FUNCTION: Isoform Bcl-X(L) also regulates presynaptic plasticity,
CC including neurotransmitter release and recovery, number of axonal
CC mitochondria as well as size and number of synaptic vesicle clusters.
CC During synaptic stimulation, increases ATP availability from
CC mitochondria through regulation of mitochondrial membrane ATP synthase
CC F(1)F(0) activity and regulates endocytic vesicle retrieval in
CC hippocampal neurons through association with DMN1L and stimulation of
CC its GTPase activity in synaptic vesicles. May attenuate inflammation
CC impairing NLRP1-inflammasome activation, hence CASP1 activation and
CC IL1B release (PubMed:17418785). {ECO:0000269|PubMed:17418785}.
CC -!- FUNCTION: Isoform Bcl-X(S) promotes apoptosis.
CC -!- SUBUNIT: Homodimer. Interacts with BCL2L11 (By similarity). Interacts
CC with BAD. Interacts with PGAM5. Interacts with HEBP2. Interacts with
CC p53/TP53 and BBC3; interaction with BBC3 disrupts the interaction with
CC p53/TP53. Interacts with ATP5F1A and ATP5F1B; the interactions mediate
CC the association of isoform Bcl-X(L) with the mitochondrial membrane ATP
CC synthase F(1)F(0) ATP synthase. Interacts with VDAC1 (PubMed:25296756).
CC Interacts with BCL2L11 (via BH3) (PubMed:27013495). Interacts with
CC RNF183 (PubMed:29507230). Interacts with GIMAP3/IAN4 and GIMAP5/IAN5
CC (PubMed:16509771). Interacts with GIMAP5 and HSPA8/HSC70; the
CC interaction between HSPA8 and BCL2L1 is impaired in the absence of
CC GIMAP5 (By similarity). Interacts with isoform 4 of CLU; this
CC interaction releases and activates BAX and promotes cell death
CC (PubMed:21567405). {ECO:0000250|UniProtKB:P53563,
CC ECO:0000250|UniProtKB:Q64373, ECO:0000269|PubMed:10772918,
CC ECO:0000269|PubMed:11206074, ECO:0000269|PubMed:11463391,
CC ECO:0000269|PubMed:16509771, ECO:0000269|PubMed:17046835,
CC ECO:0000269|PubMed:21567405, ECO:0000269|PubMed:21639858,
CC ECO:0000269|PubMed:23340338, ECO:0000269|PubMed:25296756,
CC ECO:0000269|PubMed:27013495, ECO:0000269|PubMed:29507230,
CC ECO:0000269|PubMed:9675101}.
CC -!- SUBUNIT: [Isoform Bcl-X(L)]: Forms heterodimers with BAX, BAK or BCL2;
CC heterodimerization with BAX does not seem to be required for anti-
CC apoptotic activity (PubMed:7644501). Interacts with isoform 1 of SIVA1;
CC the interaction inhibits the anti-apoptotic activity (PubMed:12011449).
CC Interacts with IKZF3 (PubMed:11714801). Interacts with RTL10/BOP
CC (PubMed:23055042). Interacts with DNM1L and CLTA; DNM1L and BCL2L1
CC isoform BCL-X(L) may form a complex in synaptic vesicles that also
CC contains clathrin and MFF (PubMed:23792689). Interacts (via the loop
CC between motifs BH4 and BH3) with NLRP1 (via LRR repeats), but not with
CC NLRP2, NLRP3, NLRP4, PYCARD, nor MEFV (PubMed:17418785). Interacts with
CC BECN1 (PubMed:22498477, PubMed:17337444). {ECO:0000269|PubMed:11714801,
CC ECO:0000269|PubMed:12011449, ECO:0000269|PubMed:17337444,
CC ECO:0000269|PubMed:17418785, ECO:0000269|PubMed:22498477,
CC ECO:0000269|PubMed:23055042, ECO:0000269|PubMed:23792689,
CC ECO:0000269|PubMed:7644501}.
CC -!- INTERACTION:
CC Q07817; Q92934: BAD; NbExp=31; IntAct=EBI-78035, EBI-700771;
CC Q07817; Q16611: BAK1; NbExp=27; IntAct=EBI-78035, EBI-519866;
CC Q07817; Q07817: BCL2L1; NbExp=2; IntAct=EBI-78035, EBI-78035;
CC Q07817; O43521: BCL2L11; NbExp=8; IntAct=EBI-78035, EBI-526406;
CC Q07817; P55957: BID; NbExp=2; IntAct=EBI-78035, EBI-519672;
CC Q07817; Q13323: BIK; NbExp=12; IntAct=EBI-78035, EBI-700794;
CC Q07817; Q96LC9: BMF; NbExp=12; IntAct=EBI-78035, EBI-3919268;
CC Q07817; P0C671: BNIP5; NbExp=3; IntAct=EBI-78035, EBI-12806802;
CC Q07817; Q8IYJ2-2: C10orf67; NbExp=3; IntAct=EBI-78035, EBI-13381098;
CC Q07817; Q9GZR5: ELOVL4; NbExp=3; IntAct=EBI-78035, EBI-18535450;
CC Q07817; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-78035, EBI-781551;
CC Q07817; P27469: G0S2; NbExp=3; IntAct=EBI-78035, EBI-3939849;
CC Q07817; P22749: GNLY; NbExp=3; IntAct=EBI-78035, EBI-17844792;
CC Q07817; Q8NBJ4: GOLM1; NbExp=3; IntAct=EBI-78035, EBI-712073;
CC Q07817; Q5T7V8: GORAB; NbExp=3; IntAct=EBI-78035, EBI-3917143;
CC Q07817; Q9H2K0: MTIF3; NbExp=3; IntAct=EBI-78035, EBI-3923617;
CC Q07817; Q9C000: NLRP1; NbExp=9; IntAct=EBI-78035, EBI-1220518;
CC Q07817; Q9H6H4: REEP4; NbExp=3; IntAct=EBI-78035, EBI-7545592;
CC Q07817; Q6NTF9-3: RHBDD2; NbExp=3; IntAct=EBI-78035, EBI-17589229;
CC Q07817; Q7Z5B4-5: RIC3; NbExp=3; IntAct=EBI-78035, EBI-12375429;
CC Q07817; P78317: RNF4; NbExp=3; IntAct=EBI-78035, EBI-2340927;
CC Q07817; O15304: SIVA1; NbExp=2; IntAct=EBI-78035, EBI-520756;
CC Q07817; P37840: SNCA; NbExp=3; IntAct=EBI-78035, EBI-985879;
CC Q07817; Q9H2V7: SPNS1; NbExp=3; IntAct=EBI-78035, EBI-1386527;
CC Q07817; P56557: TMEM50B; NbExp=3; IntAct=EBI-78035, EBI-12366453;
CC Q07817; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-78035, EBI-10180829;
CC Q07817-1; Q92934: BAD; NbExp=6; IntAct=EBI-287195, EBI-700771;
CC Q07817-1; Q16611: BAK1; NbExp=13; IntAct=EBI-287195, EBI-519866;
CC Q07817-1; Q07812: BAX; NbExp=21; IntAct=EBI-287195, EBI-516580;
CC Q07817-1; Q9BXH1: BBC3; NbExp=9; IntAct=EBI-287195, EBI-519884;
CC Q07817-1; Q07817-1: BCL2L1; NbExp=6; IntAct=EBI-287195, EBI-287195;
CC Q07817-1; O43521: BCL2L11; NbExp=10; IntAct=EBI-287195, EBI-526406;
CC Q07817-1; O43521-1: BCL2L11; NbExp=2; IntAct=EBI-287195, EBI-526416;
CC Q07817-1; Q14457: BECN1; NbExp=5; IntAct=EBI-287195, EBI-949378;
CC Q07817-1; P55957: BID; NbExp=7; IntAct=EBI-287195, EBI-519672;
CC Q07817-1; Q13323: BIK; NbExp=4; IntAct=EBI-287195, EBI-700794;
CC Q07817-1; P10909-4: CLU; NbExp=6; IntAct=EBI-287195, EBI-4322678;
CC Q07817-1; O00198: HRK; NbExp=3; IntAct=EBI-287195, EBI-701322;
CC Q07817-1; P42345: MTOR; NbExp=4; IntAct=EBI-287195, EBI-359260;
CC Q07817-1; Q9C000: NLRP1; NbExp=2; IntAct=EBI-287195, EBI-1220518;
CC Q07817-1; Q7L3V2: RTL10; NbExp=3; IntAct=EBI-287195, EBI-10697720;
CC Q07817-1; O15304: SIVA1; NbExp=2; IntAct=EBI-287195, EBI-520756;
CC Q07817-1; O15304-1: SIVA1; NbExp=5; IntAct=EBI-287195, EBI-520766;
CC Q07817-1; P04637: TP53; NbExp=26; IntAct=EBI-287195, EBI-366083;
CC Q07817-1; Q13625: TP53BP2; NbExp=3; IntAct=EBI-287195, EBI-77642;
CC Q07817-1; Q86Y07-1: VRK2; NbExp=2; IntAct=EBI-287195, EBI-1207633;
CC Q07817-1; Q61337: Bad; Xeno; NbExp=3; IntAct=EBI-287195, EBI-400328;
CC Q07817-1; Q99ML1: Bbc3; Xeno; NbExp=3; IntAct=EBI-287195, EBI-727801;
CC Q07817-1; O54918-3: Bcl2l11; Xeno; NbExp=3; IntAct=EBI-287195, EBI-526084;
CC Q07817-1; P30429-2: ced-4; Xeno; NbExp=2; IntAct=EBI-287195, EBI-536271;
CC Q07817-1; Q99MI6: Gimap3; Xeno; NbExp=3; IntAct=EBI-287195, EBI-15572304;
CC Q07817-1; Q8BWF2: Gimap5; Xeno; NbExp=3; IntAct=EBI-287195, EBI-15572348;
CC Q07817-1; P02340: Tp53; Xeno; NbExp=3; IntAct=EBI-287195, EBI-474016;
CC -!- SUBCELLULAR LOCATION: [Isoform Bcl-X(L)]: Mitochondrion inner membrane
CC {ECO:0000250}. Mitochondrion outer membrane {ECO:0000250}.
CC Mitochondrion matrix {ECO:0000250}. Cytoplasmic vesicle, secretory
CC vesicle, synaptic vesicle membrane {ECO:0000250}. Cytoplasm, cytosol
CC {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center,
CC centrosome. Nucleus membrane {ECO:0000250}; Single-pass membrane
CC protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=After
CC neuronal stimulation, translocates from cytosol to synaptic vesicle and
CC mitochondrion membrane in a calmodulin-dependent manner (By
CC similarity). Localizes to the centrosome when phosphorylated at Ser-49.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=Bcl-X(L); Synonyms=Bcl-xL;
CC IsoId=Q07817-1; Sequence=Displayed;
CC Name=Bcl-X(S); Synonyms=Bcl-xS;
CC IsoId=Q07817-2; Sequence=VSP_000515;
CC Name=Bcl-X(beta);
CC IsoId=Q07817-3; Sequence=VSP_000516;
CC -!- TISSUE SPECIFICITY: Bcl-X(S) is expressed at high levels in cells that
CC undergo a high rate of turnover, such as developing lymphocytes. In
CC contrast, Bcl-X(L) is found in tissues containing long-lived
CC postmitotic cells, such as adult brain.
CC -!- DOMAIN: The BH4 motif is required for anti-apoptotic activity. The BH1
CC and BH2 motifs are required for both heterodimerization with other Bcl-
CC 2 family members and for repression of cell death.
CC -!- DOMAIN: The loop between motifs BH4 and BH3 is required for the
CC interaction with NLRP1. {ECO:0000269|PubMed:17418785}.
CC -!- PTM: Proteolytically cleaved by caspases during apoptosis. The cleaved
CC protein, lacking the BH4 motif, has pro-apoptotic activity.
CC {ECO:0000269|PubMed:9435230}.
CC -!- PTM: Phosphorylated on Ser-62 by CDK1. This phosphorylation is partial
CC in normal mitotic cells, but complete in G2-arrested cells upon DNA-
CC damage, thus promoting subsequent apoptosis probably by triggering
CC caspases-mediated proteolysis. Phosphorylated by PLK3, leading to
CC regulate the G2 checkpoint and progression to cytokinesis during
CC mitosis. Phosphorylation at Ser-49 appears during the S phase and G2,
CC disappears rapidly in early mitosis during prometaphase, metaphase and
CC early anaphase, and re-appears during telophase and cytokinesis.
CC {ECO:0000269|PubMed:19917720, ECO:0000269|PubMed:21840391}.
CC -!- PTM: Ubiquitinated by RNF183 during prolonged ER stress, leading to
CC degradation by the proteosome. {ECO:0000269|PubMed:29507230}.
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="http://atlasgeneticsoncology.org/Genes/BCL2L1ID129ch20q11.html";
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DR EMBL; Z23115; CAA80661.1; -; mRNA.
DR EMBL; Z23116; CAA80662.1; -; mRNA.
DR EMBL; U72398; AAB17354.1; -; Genomic_DNA.
DR EMBL; CR936637; CAI56777.1; -; mRNA.
DR EMBL; BT007208; AAP35872.1; -; mRNA.
DR EMBL; AL117381; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL160175; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW76424.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW76425.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW76429.1; -; Genomic_DNA.
DR EMBL; BC019307; AAH19307.1; -; mRNA.
DR CCDS; CCDS13188.1; -. [Q07817-2]
DR CCDS; CCDS13189.1; -. [Q07817-1]
DR PIR; B47537; B47537.
DR PIR; JE0203; JE0203.
DR RefSeq; NP_001182.1; NM_001191.3. [Q07817-2]
DR RefSeq; NP_001304848.1; NM_001317919.1. [Q07817-1]
DR RefSeq; NP_001304849.1; NM_001317920.1. [Q07817-1]
DR RefSeq; NP_001304850.1; NM_001317921.1. [Q07817-1]
DR RefSeq; NP_001309168.1; NM_001322239.1. [Q07817-1]
DR RefSeq; NP_001309169.1; NM_001322240.1. [Q07817-1]
DR RefSeq; NP_001309171.1; NM_001322242.1. [Q07817-1]
DR RefSeq; NP_612815.1; NM_138578.2. [Q07817-1]
DR RefSeq; XP_011527266.1; XM_011528964.2. [Q07817-1]
DR RefSeq; XP_016883482.1; XM_017027993.1. [Q07817-1]
DR PDB; 1BXL; NMR; -; A=1-209.
DR PDB; 1G5J; NMR; -; A=1-209.
DR PDB; 1LXL; NMR; -; A=1-209.
DR PDB; 1MAZ; X-ray; 2.20 A; A=1-209.
DR PDB; 1R2D; X-ray; 1.95 A; A=1-211.
DR PDB; 1R2E; X-ray; 2.10 A; A=1-211.
DR PDB; 1R2G; X-ray; 2.70 A; A=1-211.
DR PDB; 1R2H; X-ray; 2.20 A; A=1-211.
DR PDB; 1R2I; X-ray; 2.00 A; A=1-211.
DR PDB; 1YSG; NMR; -; A=1-209.
DR PDB; 1YSI; NMR; -; A=1-209.
DR PDB; 1YSN; NMR; -; A=1-209.
DR PDB; 2B48; X-ray; 3.45 A; A=1-211.
DR PDB; 2LP8; NMR; -; A=1-209.
DR PDB; 2LPC; NMR; -; A=1-209.
DR PDB; 2M03; NMR; -; A=1-209.
DR PDB; 2M04; NMR; -; A=1-209.
DR PDB; 2ME8; NMR; -; A=1-209.
DR PDB; 2ME9; NMR; -; A=1-209.
DR PDB; 2MEJ; NMR; -; A=1-209.
DR PDB; 2O1Y; NMR; -; A=1-209.
DR PDB; 2O2M; NMR; -; A=2-20, A=83-196.
DR PDB; 2O2N; NMR; -; A=2-20, A=83-196.
DR PDB; 2P1L; X-ray; 2.50 A; A/C/E/G=1-209.
DR PDB; 2PON; NMR; -; B=1-196.
DR PDB; 2YJ1; X-ray; 2.24 A; A/C=1-209.
DR PDB; 2YQ6; X-ray; 1.80 A; A=1-209.
DR PDB; 2YQ7; X-ray; 1.90 A; A=1-209.
DR PDB; 2YXJ; X-ray; 2.20 A; A/B=1-209.
DR PDB; 3CVA; X-ray; 2.70 A; X=1-211.
DR PDB; 3FDL; X-ray; 1.78 A; A=1-209.
DR PDB; 3FDM; X-ray; 2.26 A; A/B/C=1-209.
DR PDB; 3INQ; X-ray; 2.00 A; A/B=1-209.
DR PDB; 3IO8; X-ray; 2.30 A; A/C=1-209.
DR PDB; 3PL7; X-ray; 2.61 A; A/B=1-209.
DR PDB; 3QKD; X-ray; 2.02 A; A/B=1-209.
DR PDB; 3R85; X-ray; 1.95 A; A/B/C/D=1-197.
DR PDB; 3SP7; X-ray; 1.40 A; A=1-209.
DR PDB; 3SPF; X-ray; 1.70 A; A=1-209.
DR PDB; 3WIZ; X-ray; 2.45 A; A/B=1-209.
DR PDB; 3ZK6; X-ray; 2.48 A; A/B=1-209.
DR PDB; 3ZLN; X-ray; 2.29 A; A=1-209.
DR PDB; 3ZLO; X-ray; 2.60 A; A=1-209.
DR PDB; 3ZLR; X-ray; 2.03 A; A/B=1-209.
DR PDB; 4A1U; X-ray; 1.54 A; A=1-209.
DR PDB; 4A1W; X-ray; 2.50 A; A/B/C/D=1-209.
DR PDB; 4AQ3; X-ray; 2.40 A; A/B/C/D/E/F=29-44.
DR PDB; 4BPK; X-ray; 1.76 A; A/B=1-209.
DR PDB; 4C52; X-ray; 2.05 A; A/B=1-209.
DR PDB; 4C5D; X-ray; 2.30 A; A/B=1-209.
DR PDB; 4CIN; X-ray; 2.69 A; A/B=1-209, C/D=79-102.
DR PDB; 4EHR; X-ray; 2.09 A; A=1-209.
DR PDB; 4HNJ; X-ray; 2.90 A; A/B=1-209.
DR PDB; 4IEH; X-ray; 2.10 A; A=29-44.
DR PDB; 4PPI; X-ray; 2.85 A; A=1-209.
DR PDB; 4QVE; X-ray; 2.05 A; A=1-209.
DR PDB; 4QVF; X-ray; 1.53 A; A=1-209.
DR PDB; 4QVX; X-ray; 2.10 A; A/B=1-23, A/B=83-209.
DR PDB; 4TUH; X-ray; 1.80 A; A/B/C/D/E/F/G/H=1-209.
DR PDB; 4Z9V; X-ray; 2.10 A; A/B=1-208.
DR PDB; 5AGW; X-ray; 2.69 A; A/B=29-44.
DR PDB; 5AGX; X-ray; 2.24 A; A/B=29-44.
DR PDB; 5B1Z; X-ray; 2.15 A; A/B=1-209.
DR PDB; 5C3G; X-ray; 2.45 A; A=83-209.
DR PDB; 5FMJ; X-ray; 2.43 A; A=1-209.
DR PDB; 5FMK; X-ray; 1.73 A; A=1-209.
DR PDB; 5VAY; X-ray; 1.80 A; A/B/C/D=29-44.
DR PDB; 5VX3; X-ray; 1.95 A; A/C/E/G=1-209.
DR PDB; 6BF2; NMR; -; A=1-209.
DR PDB; 6DCN; X-ray; 2.44 A; A/B=1-26, A/B=83-208.
DR PDB; 6DCO; X-ray; 2.20 A; A/B=1-26, A/B=83-208.
DR PDB; 6F46; NMR; -; A=202-233.
DR PDB; 6HJL; X-ray; 2.20 A; A=83-197, B/E/F=83-195.
DR PDB; 6IJQ; NMR; -; B=1-209.
DR PDB; 6LHD; X-ray; 2.50 A; A/B=2-201.
DR PDB; 6O0K; X-ray; 1.62 A; A=29-44.
DR PDB; 6O0L; X-ray; 2.20 A; A/C=29-44.
DR PDB; 6O0M; X-ray; 1.75 A; A=29-44.
DR PDB; 6O0O; X-ray; 2.00 A; A/C=29-44.
DR PDB; 6O0P; X-ray; 1.80 A; A=29-44.
DR PDB; 6RNU; X-ray; 2.40 A; A/B=1-209.
DR PDB; 6ST2; X-ray; 1.79 A; A/B=1-209.
DR PDB; 6UVC; X-ray; 1.90 A; A/B=1-209.
DR PDB; 6UVD; X-ray; 2.15 A; A/B=1-209.
DR PDB; 6UVE; X-ray; 2.87 A; A/B/C=1-209.
DR PDB; 6UVF; X-ray; 2.24 A; A/B/C/D/E/F/G/H/I/J/K/L=1-209.
DR PDB; 6UVG; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J/K/L=1-209.
DR PDB; 6UVH; X-ray; 2.19 A; A/B/C/D=1-209.
DR PDB; 6VWC; X-ray; 1.60 A; A/B=1-25, A/B=83-209.
DR PDB; 6X7I; Other; -; A=206-233.
DR PDB; 6YLI; X-ray; 1.90 A; A/C=1-209.
DR PDB; 6ZHC; X-ray; 1.92 A; DDD=1-209.
DR PDB; 7CA4; X-ray; 2.70 A; A=1-211.
DR PDB; 7JGV; X-ray; 2.05 A; A/B=1-209.
DR PDB; 7JGW; X-ray; 1.30 A; A=1-209.
DR PDB; 7LH7; X-ray; 1.41 A; A/B=1-25, A/B=83-209.
DR PDBsum; 1BXL; -.
DR PDBsum; 1G5J; -.
DR PDBsum; 1LXL; -.
DR PDBsum; 1MAZ; -.
DR PDBsum; 1R2D; -.
DR PDBsum; 1R2E; -.
DR PDBsum; 1R2G; -.
DR PDBsum; 1R2H; -.
DR PDBsum; 1R2I; -.
DR PDBsum; 1YSG; -.
DR PDBsum; 1YSI; -.
DR PDBsum; 1YSN; -.
DR PDBsum; 2B48; -.
DR PDBsum; 2LP8; -.
DR PDBsum; 2LPC; -.
DR PDBsum; 2M03; -.
DR PDBsum; 2M04; -.
DR PDBsum; 2ME8; -.
DR PDBsum; 2ME9; -.
DR PDBsum; 2MEJ; -.
DR PDBsum; 2O1Y; -.
DR PDBsum; 2O2M; -.
DR PDBsum; 2O2N; -.
DR PDBsum; 2P1L; -.
DR PDBsum; 2PON; -.
DR PDBsum; 2YJ1; -.
DR PDBsum; 2YQ6; -.
DR PDBsum; 2YQ7; -.
DR PDBsum; 2YXJ; -.
DR PDBsum; 3CVA; -.
DR PDBsum; 3FDL; -.
DR PDBsum; 3FDM; -.
DR PDBsum; 3INQ; -.
DR PDBsum; 3IO8; -.
DR PDBsum; 3PL7; -.
DR PDBsum; 3QKD; -.
DR PDBsum; 3R85; -.
DR PDBsum; 3SP7; -.
DR PDBsum; 3SPF; -.
DR PDBsum; 3WIZ; -.
DR PDBsum; 3ZK6; -.
DR PDBsum; 3ZLN; -.
DR PDBsum; 3ZLO; -.
DR PDBsum; 3ZLR; -.
DR PDBsum; 4A1U; -.
DR PDBsum; 4A1W; -.
DR PDBsum; 4AQ3; -.
DR PDBsum; 4BPK; -.
DR PDBsum; 4C52; -.
DR PDBsum; 4C5D; -.
DR PDBsum; 4CIN; -.
DR PDBsum; 4EHR; -.
DR PDBsum; 4HNJ; -.
DR PDBsum; 4IEH; -.
DR PDBsum; 4PPI; -.
DR PDBsum; 4QVE; -.
DR PDBsum; 4QVF; -.
DR PDBsum; 4QVX; -.
DR PDBsum; 4TUH; -.
DR PDBsum; 4Z9V; -.
DR PDBsum; 5AGW; -.
DR PDBsum; 5AGX; -.
DR PDBsum; 5B1Z; -.
DR PDBsum; 5C3G; -.
DR PDBsum; 5FMJ; -.
DR PDBsum; 5FMK; -.
DR PDBsum; 5VAY; -.
DR PDBsum; 5VX3; -.
DR PDBsum; 6BF2; -.
DR PDBsum; 6DCN; -.
DR PDBsum; 6DCO; -.
DR PDBsum; 6F46; -.
DR PDBsum; 6HJL; -.
DR PDBsum; 6IJQ; -.
DR PDBsum; 6LHD; -.
DR PDBsum; 6O0K; -.
DR PDBsum; 6O0L; -.
DR PDBsum; 6O0M; -.
DR PDBsum; 6O0O; -.
DR PDBsum; 6O0P; -.
DR PDBsum; 6RNU; -.
DR PDBsum; 6ST2; -.
DR PDBsum; 6UVC; -.
DR PDBsum; 6UVD; -.
DR PDBsum; 6UVE; -.
DR PDBsum; 6UVF; -.
DR PDBsum; 6UVG; -.
DR PDBsum; 6UVH; -.
DR PDBsum; 6VWC; -.
DR PDBsum; 6X7I; -.
DR PDBsum; 6YLI; -.
DR PDBsum; 6ZHC; -.
DR PDBsum; 7CA4; -.
DR PDBsum; 7JGV; -.
DR PDBsum; 7JGW; -.
DR PDBsum; 7LH7; -.
DR AlphaFoldDB; Q07817; -.
DR BMRB; Q07817; -.
DR SMR; Q07817; -.
DR BioGRID; 107070; 224.
DR ComplexPortal; CPX-1983; BAD:BCL-XL complex. [Q07817-1]
DR ComplexPortal; CPX-1985; BIM:BCL-XL complex. [Q07817-1]
DR ComplexPortal; CPX-1987; PUMA:BCL-XL complex. [Q07817-1]
DR ComplexPortal; CPX-1991; BID:BCL-XL complex. [Q07817-1]
DR ComplexPortal; CPX-298; BCL-XL complex. [Q07817-1]
DR ComplexPortal; CPX-860; BAK1-Bcl-X complex. [Q07817-1]
DR CORUM; Q07817; -.
DR DIP; DIP-30916N; -.
DR ELM; Q07817; -.
DR IntAct; Q07817; 109.
DR MINT; Q07817; -.
DR STRING; 9606.ENSP00000302564; -.
DR BindingDB; Q07817; -.
DR ChEMBL; CHEMBL4625; -.
DR DrugBank; DB07108; 4'-FLUORO-1,1'-BIPHENYL-4-CARBOXYLIC ACID.
DR DrugBank; DB13044; Gossypol.
DR DrugCentral; Q07817; -.
DR GuidetoPHARMACOLOGY; 2845; -.
DR TCDB; 1.A.21.1.1; the bcl-2 (bcl-2) family.
DR iPTMnet; Q07817; -.
DR PhosphoSitePlus; Q07817; -.
DR BioMuta; BCL2L1; -.
DR DMDM; 728955; -.
DR EPD; Q07817; -.
DR jPOST; Q07817; -.
DR MassIVE; Q07817; -.
DR MaxQB; Q07817; -.
DR PaxDb; Q07817; -.
DR PeptideAtlas; Q07817; -.
DR PRIDE; Q07817; -.
DR ProteomicsDB; 58537; -. [Q07817-1]
DR ProteomicsDB; 58538; -. [Q07817-2]
DR ProteomicsDB; 58539; -. [Q07817-3]
DR TopDownProteomics; Q07817-1; -. [Q07817-1]
DR TopDownProteomics; Q07817-2; -. [Q07817-2]
DR Antibodypedia; 3430; 2028 antibodies from 52 providers.
DR CPTC; Q07817; 3 antibodies.
DR DNASU; 598; -.
DR Ensembl; ENST00000307677.5; ENSP00000302564.4; ENSG00000171552.14. [Q07817-1]
DR Ensembl; ENST00000376055.9; ENSP00000365223.4; ENSG00000171552.14. [Q07817-2]
DR Ensembl; ENST00000376062.6; ENSP00000365230.2; ENSG00000171552.14. [Q07817-1]
DR Ensembl; ENST00000420488.6; ENSP00000390760.2; ENSG00000171552.14. [Q07817-1]
DR Ensembl; ENST00000422920.2; ENSP00000411252.2; ENSG00000171552.14. [Q07817-2]
DR Ensembl; ENST00000434194.2; ENSP00000401173.2; ENSG00000171552.14. [Q07817-1]
DR Ensembl; ENST00000439267.2; ENSP00000389688.2; ENSG00000171552.14. [Q07817-1]
DR Ensembl; ENST00000456404.6; ENSP00000395545.2; ENSG00000171552.14. [Q07817-1]
DR Ensembl; ENST00000676582.1; ENSP00000503725.1; ENSG00000171552.14. [Q07817-1]
DR Ensembl; ENST00000676942.1; ENSP00000504536.1; ENSG00000171552.14. [Q07817-1]
DR Ensembl; ENST00000677194.1; ENSP00000504387.1; ENSG00000171552.14. [Q07817-1]
DR Ensembl; ENST00000678563.1; ENSP00000504237.1; ENSG00000171552.14. [Q07817-1]
DR GeneID; 598; -.
DR KEGG; hsa:598; -.
DR MANE-Select; ENST00000307677.5; ENSP00000302564.4; NM_138578.3; NP_612815.1.
DR UCSC; uc002wwl.4; human. [Q07817-1]
DR CTD; 598; -.
DR DisGeNET; 598; -.
DR GeneCards; BCL2L1; -.
DR HGNC; HGNC:992; BCL2L1.
DR HPA; ENSG00000171552; Low tissue specificity.
DR MIM; 600039; gene.
DR neXtProt; NX_Q07817; -.
DR OpenTargets; ENSG00000171552; -.
DR PharmGKB; PA76; -.
DR VEuPathDB; HostDB:ENSG00000171552; -.
DR eggNOG; KOG4728; Eukaryota.
DR GeneTree; ENSGT01050000244953; -.
DR InParanoid; Q07817; -.
DR OMA; SPNRTDG; -.
DR PhylomeDB; Q07817; -.
DR TreeFam; TF315834; -.
DR PathwayCommons; Q07817; -.
DR Reactome; R-HSA-111453; BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members.
DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
DR Reactome; R-HSA-844455; The NLRP1 inflammasome.
DR Reactome; R-HSA-9648002; RAS processing.
DR Reactome; R-HSA-9702518; STAT5 activation downstream of FLT3 ITD mutants.
DR SignaLink; Q07817; -.
DR SIGNOR; Q07817; -.
DR BioGRID-ORCS; 598; 528 hits in 1091 CRISPR screens.
DR ChiTaRS; BCL2L1; human.
DR EvolutionaryTrace; Q07817; -.
DR GeneWiki; BCL2-like_1_(gene); -.
DR GenomeRNAi; 598; -.
DR Pharos; Q07817; Tchem.
DR PRO; PR:Q07817; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q07817; protein.
DR Bgee; ENSG00000171552; Expressed in right lung and 200 other tissues.
DR ExpressionAtlas; Q07817; baseline and differential.
DR Genevisible; Q07817; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0097136; C:Bcl-2 family protein complex; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:HGNC-UCL.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0097143; C:PUMA-BCL-xl complex; IPI:ComplexPortal.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051434; F:BH3 domain binding; IPI:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046982; F:protein heterodimerization activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0008637; P:apoptotic mitochondrial changes; TAS:ProtInc.
DR GO; GO:0071839; P:apoptotic process in bone marrow cell; IEA:Ensembl.
DR GO; GO:0071312; P:cellular response to alkaloid; IEA:Ensembl.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
DR GO; GO:0071480; P:cellular response to gamma radiation; IEA:Ensembl.
DR GO; GO:0051607; P:defense response to virus; IDA:DIBU.
DR GO; GO:0097048; P:dendritic cell apoptotic process; IEA:Ensembl.
DR GO; GO:0044565; P:dendritic cell proliferation; IEA:Ensembl.
DR GO; GO:0035234; P:ectopic germ cell programmed cell death; IEA:Ensembl.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0050673; P:epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IBA:GO_Central.
DR GO; GO:0009566; P:fertilization; IEA:Ensembl.
DR GO; GO:0007281; P:germ cell development; IEA:Ensembl.
DR GO; GO:0097284; P:hepatocyte apoptotic process; IEA:Ensembl.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IBA:GO_Central.
DR GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR GO; GO:0070584; P:mitochondrion morphogenesis; IEA:Ensembl.
DR GO; GO:2000811; P:negative regulation of anoikis; IMP:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0010507; P:negative regulation of autophagy; TAS:UniProtKB.
DR GO; GO:2000669; P:negative regulation of dendritic cell apoptotic process; IEA:Ensembl.
DR GO; GO:0051093; P:negative regulation of developmental process; IEA:Ensembl.
DR GO; GO:1902236; P:negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; IDA:UniProtKB.
DR GO; GO:1900118; P:negative regulation of execution phase of apoptosis; IDA:UniProtKB.
DR GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; TAS:BHF-UCL.
DR GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; IDA:MGI.
DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IDA:BHF-UCL.
DR GO; GO:1902230; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage; IDA:BHF-UCL.
DR GO; GO:1901029; P:negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; IDA:ComplexPortal.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; IDA:BHF-UCL.
DR GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; IDA:ComplexPortal.
DR GO; GO:2000242; P:negative regulation of reproductive process; IEA:Ensembl.
DR GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0001541; P:ovarian follicle development; IEA:Ensembl.
DR GO; GO:0032946; P:positive regulation of mononuclear cell proliferation; IEA:Ensembl.
DR GO; GO:0032465; P:regulation of cytokinesis; IMP:UniProtKB.
DR GO; GO:0040008; P:regulation of growth; IEA:Ensembl.
DR GO; GO:0046902; P:regulation of mitochondrial membrane permeability; IDA:HGNC-UCL.
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:HGNC-UCL.
DR GO; GO:0046898; P:response to cycloheximide; IEA:Ensembl.
DR GO; GO:0034097; P:response to cytokine; IDA:MGI.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR GO; GO:0019050; P:suppression by virus of host apoptotic process; IDA:MGI.
DR CDD; cd06845; Bcl-2_like; 1.
DR DisProt; DP00298; -.
DR Gene3D; 1.10.437.10; -; 1.
DR InterPro; IPR013279; Apop_reg_BclX.
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; IPR004725; Bcl2/BclX.
DR InterPro; IPR020717; Bcl2_BH1_motif_CS.
DR InterPro; IPR020726; Bcl2_BH2_motif_CS.
DR InterPro; IPR020728; Bcl2_BH3_motif_CS.
DR InterPro; IPR003093; Bcl2_BH4.
DR InterPro; IPR020731; Bcl2_BH4_motif_CS.
DR PANTHER; PTHR11256; PTHR11256; 1.
DR PANTHER; PTHR11256:SF12; PTHR11256:SF12; 1.
DR Pfam; PF00452; Bcl-2; 1.
DR Pfam; PF02180; BH4; 1.
DR PRINTS; PR01864; APOPREGBCLX.
DR PRINTS; PR01862; BCL2FAMILY.
DR SMART; SM00337; BCL; 1.
DR SMART; SM00265; BH4; 1.
DR SUPFAM; SSF56854; SSF56854; 1.
DR TIGRFAMs; TIGR00865; bcl-2; 1.
DR PROSITE; PS50062; BCL2_FAMILY; 1.
DR PROSITE; PS01080; BH1; 1.
DR PROSITE; PS01258; BH2; 1.
DR PROSITE; PS01259; BH3; 1.
DR PROSITE; PS01260; BH4_1; 1.
DR PROSITE; PS50063; BH4_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Apoptosis; Cytoplasm;
KW Cytoplasmic vesicle; Cytoskeleton; Endocytosis; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Mitochondrion outer membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Synapse; Transmembrane;
KW Transmembrane helix; Ubl conjugation.
FT CHAIN 1..233
FT /note="Bcl-2-like protein 1"
FT /id="PRO_0000143062"
FT TRANSMEM 210..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 28..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 4..24
FT /note="BH4"
FT MOTIF 86..100
FT /note="BH3"
FT MOTIF 129..148
FT /note="BH1"
FT MOTIF 180..195
FT /note="BH2"
FT SITE 61..62
FT /note="Cleavage; by caspase-1"
FT MOD_RES 49
FT /note="Phosphoserine; by PLK3"
FT /evidence="ECO:0000269|PubMed:21840391"
FT MOD_RES 62
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000269|PubMed:19917720"
FT VAR_SEQ 126..188
FT /note="Missing (in isoform Bcl-X(S))"
FT /evidence="ECO:0000305"
FT /id="VSP_000515"
FT VAR_SEQ 189..233
FT /note="DTFVELYGNNAAAESRKGQERFNRWFLTGMTVAGVVLLGSLFSRK -> VRT
FT KPLVCPFSLASGQRSPTALLLYLFLLCWVIVGDVDS (in isoform Bcl-
FT X(beta))"
FT /evidence="ECO:0000305"
FT /id="VSP_000516"
FT MUTAGEN 49
FT /note="S->A: Less stable at G2 checkpoint after DNA
FT damage."
FT /evidence="ECO:0000269|PubMed:21840391"
FT MUTAGEN 61
FT /note="D->A: No cleavage by caspase-1 nor by caspase-3."
FT /evidence="ECO:0000269|PubMed:9435230"
FT MUTAGEN 131..133
FT /note="FRD->VRA: No heterodimerization with BAX."
FT /evidence="ECO:0000269|PubMed:8596636"
FT MUTAGEN 135..137
FT /note="VNW->AIL: Loss of anti-apoptotic activity."
FT /evidence="ECO:0000269|PubMed:8596636"
FT MUTAGEN 138..140
FT /note="GRI->ELN: Loss of anti-apoptotic activity."
FT /evidence="ECO:0000269|PubMed:8596636"
FT MUTAGEN 138
FT /note="G->A: No heterodimerization with BAX."
FT /evidence="ECO:0000269|PubMed:7644501"
FT MUTAGEN 145..147
FT /note="SFG->YCC: Decreases interaction with DNM1L, no
FT effect on endocytosis enhancement."
FT /evidence="ECO:0000269|PubMed:23792689"
FT MUTAGEN 148
FT /note="G->E: No heterodimerization with BAX."
FT /evidence="ECO:0000269|PubMed:8596636"
FT MUTAGEN 156
FT /note="D->A: No effect on caspase-1 cleavage."
FT /evidence="ECO:0000269|PubMed:8596636"
FT MUTAGEN 176
FT /note="D->A: No effect on caspase-1 cleavage."
FT /evidence="ECO:0000269|PubMed:8596636"
FT MUTAGEN 188..191
FT /note="WDTF->SVTC: Abolishes interaction with DNM1L and
FT endocytosis enhancement."
FT /evidence="ECO:0000269|PubMed:23792689"
FT MUTAGEN 188..189
FT /note="WD->GA: Reduces anti-apoptotic activity by about
FT half."
FT /evidence="ECO:0000269|PubMed:8596636"
FT MUTAGEN 189
FT /note="D->A: No effect on caspase-1 cleavage."
FT /evidence="ECO:0000269|PubMed:8596636"
FT CONFLICT 70
FT /note="G -> A (in Ref. 1; CAA80661)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="A -> V (in Ref. 4; CAI56777)"
FT /evidence="ECO:0000305"
FT HELIX 1..19
FT /evidence="ECO:0007829|PDB:7JGW"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:3SP7"
FT STRAND 29..36
FT /evidence="ECO:0007829|PDB:1LXL"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:1G5J"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:1BXL"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:2ME9"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:2ME8"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:6BF2"
FT TURN 65..68
FT /evidence="ECO:0007829|PDB:1LXL"
FT TURN 70..73
FT /evidence="ECO:0007829|PDB:1LXL"
FT HELIX 83..100
FT /evidence="ECO:0007829|PDB:7JGW"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:7JGW"
FT HELIX 108..111
FT /evidence="ECO:0007829|PDB:7JGW"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:2ME8"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:4QVF"
FT HELIX 120..130
FT /evidence="ECO:0007829|PDB:7JGW"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:7JGW"
FT HELIX 137..156
FT /evidence="ECO:0007829|PDB:7JGW"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:7JGW"
FT HELIX 163..177
FT /evidence="ECO:0007829|PDB:7JGW"
FT HELIX 179..184
FT /evidence="ECO:0007829|PDB:7JGW"
FT HELIX 187..195
FT /evidence="ECO:0007829|PDB:7JGW"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:4A1U"
FT HELIX 199..204
FT /evidence="ECO:0007829|PDB:7LH7"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:2M03"
FT HELIX 213..229
FT /evidence="ECO:0007829|PDB:6F46"
SQ SEQUENCE 233 AA; 26049 MW; E09D3CDD851AE9BE CRC64;
MSQSNRELVV DFLSYKLSQK GYSWSQFSDV EENRTEAPEG TESEMETPSA INGNPSWHLA
DSPAVNGATG HSSSLDAREV IPMAAVKQAL REAGDEFELR YRRAFSDLTS QLHITPGTAY
QSFEQVVNEL FRDGVNWGRI VAFFSFGGAL CVESVDKEMQ VLVSRIAAWM ATYLNDHLEP
WIQENGGWDT FVELYGNNAA AESRKGQERF NRWFLTGMTV AGVVLLGSLF SRK
