Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Bcl-2-like protein 1 (Bcl2-L-1) (Apoptosis regulator Bcl-X)

 B2CL1_HUMAN             Reviewed;         233 AA.
Q07817; E1P5L6; Q5CZ89; Q5TE65; Q92976;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
22-NOV-2017, entry version 211.
RecName: Full=Bcl-2-like protein 1;
Short=Bcl2-L-1;
AltName: Full=Apoptosis regulator Bcl-X;
Name=BCL2L1; Synonyms=BCL2L, BCLX;
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 BCL-X(L) AND BCL-X(S)).
PubMed=8358789; DOI=10.1016/0092-8674(93)90508-N;
Boise L.H., Gonzalez-Garcia M., Postema C.E., Ding L., Lindsten T.,
Turka L.A., Mao X., Nunez G., Thompson C.B.;
"bcl-x, a bcl-2-related gene that functions as a dominant regulator of
apoptotic cell death.";
Cell 74:597-608(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BCL-X(BETA)), AND INTERACTION WITH
BAX.
PubMed=9675101; DOI=10.1006/bbrc.1998.8907;
Ban J., Eckhart L., Weninger W., Mildner M., Tschachler E.;
"Identification of a human cDNA encoding a novel Bcl-x isoform.";
Biochem. Biophys. Res. Commun. 248:147-152(1998).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM BCL-X(BETA)).
Inohara N., Ohta S.;
Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BCL-X(L)).
TISSUE=Colon carcinoma;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BCL-X(L)).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BCL-X(L)).
TISSUE=Lung;
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).
[9]
MUTAGENESIS OF GLY-138, AND HETERODIMERIZATION.
PubMed=7644501; DOI=10.1073/pnas.92.17.7834;
Sedlak T.W., Oltvai Z.N., Yang E., Wang K., Boise L.H., Thompson C.B.,
Korsmeyer S.J.;
"Multiple Bcl-2 family members demonstrate selective dimerizations
with Bax.";
Proc. Natl. Acad. Sci. U.S.A. 92:7834-7838(1995).
[10]
MUTAGENESIS OF BH1 AND BH2 MOTIFS.
PubMed=8596636; DOI=10.1038/379554a0;
Cheng E.H.-Y., Levine B., Boise L.H., Thompson C.B., Hardwick J.M.,
Korsmeyer S.J.;
"Bax-independent inhibition of apoptosis by Bcl-XL.";
Nature 379:554-556(1996).
[11]
CLEAVAGE BY CASPASES, AND MUTAGENESIS OF ASP-61.
PubMed=9435230; DOI=10.1073/pnas.95.2.554;
Clem R.J., Cheng E.H.-Y., Karp C.L., Kirsch D.G., Ueno K.,
Takahashi A., Kastan M.B., Griffin D.E., Earnshaw W.C., Veliuona M.A.,
Hardwick J.M.;
"Modulation of cell death by Bcl-xL through caspase interaction.";
Proc. Natl. Acad. Sci. U.S.A. 95:554-559(1998).
[12]
INTERACTION WITH BAX.
PubMed=10772918; DOI=10.1006/bbrc.2000.2537;
Schmitt E., Paquet C., Beauchemin M., Dever-Bertrand J., Bertrand R.;
"Characterization of Bax-sigma, a cell death-inducing isoform of
Bax.";
Biochem. Biophys. Res. Commun. 270:868-879(2000).
[13]
INTERACTION WITH IKZF3.
PubMed=11714801; DOI=10.4049/jimmunol.167.11.6366;
Rebollo A., Ayllon V., Fleischer A., Martinez C.A., Zaballos A.;
"The association of Aiolos transcription factor and Bcl-xL is involved
in the control of apoptosis.";
J. Immunol. 167:6366-6373(2001).
[14]
INTERACTION WITH BCL2 AND BBC3.
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).
[15]
INTERACTION WITH SIVA1.
PubMed=12011449; DOI=10.1073/pnas.102182299;
Xue L., Chu F., Cheng Y., Sun X., Borthakur A., Ramarao M., Pandey P.,
Wu M., Schlossman S.F., Prasad K.V.S.;
"Siva-1 binds to and inhibits BCL-X(L)-mediated protection against UV
radiation-induced apoptosis.";
Proc. Natl. Acad. Sci. U.S.A. 99:6925-6930(2002).
[16]
INTERACTION WITH PGAM5.
PubMed=17046835; DOI=10.1074/jbc.M606539200;
Lo S.-C., Hannink M.;
"PGAM5, a Bcl-XL-interacting protein, is a novel substrate for the
redox-regulated Keap1-dependent ubiquitin ligase complex.";
J. Biol. Chem. 281:37893-37903(2006).
[17]
FUNCTION, AND INTERACTION WITH NLRP1.
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).
[18]
FUNCTION IN APOPTOSIS, PHOSPHORYLATION AT SER-62 BY CDK1, AND
SUBCELLULAR LOCATION.
PubMed=19917720; DOI=10.1128/MCB.00882-09;
Terrano D.T., Upreti M., Chambers T.C.;
"Cyclin-dependent kinase 1-mediated Bcl-xL/Bcl-2 phosphorylation acts
as a functional link coupling mitotic arrest and apoptosis.";
Mol. Cell. Biol. 30:640-656(2010).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[20]
FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-49, AND
MUTAGENESIS OF SER-49.
PubMed=21840391; DOI=10.1016/j.cellsig.2011.07.017;
Wang J., Beauchemin M., Bertrand R.;
"Bcl-xL phosphorylation at Ser49 by polo kinase 3 during cell cycle
progression and checkpoints.";
Cell. Signal. 23:2030-2038(2011).
[21]
INTERACTION WITH DNM1L, FUNCTION, AND MUTAGENESIS OF 145-SER--GLY-147
AND 188-TRP--PHE-191.
PubMed=23792689; DOI=10.1038/ncb2791;
Li H., Alavian K.N., Lazrove E., Mehta N., Jones A., Zhang P.,
Licznerski P., Graham M., Uo T., Guo J., Rahner C., Duman R.S.,
Morrison R.S., Jonas E.A.;
"A Bcl-xL-Drp1 complex regulates synaptic vesicle membrane dynamics
during endocytosis.";
Nat. Cell Biol. 15:773-785(2013).
[22]
INTERACTION WITH VDAC1.
PubMed=25296756; DOI=10.1074/jbc.M114.567792;
Li L., Yao Y.C., Gu X.Q., Che D., Ma C.Q., Dai Z.Y., Li C., Zhou T.,
Cai W.B., Yang Z.H., Yang X., Gao G.Q.;
"Plasminogen kringle 5 induces endothelial cell apoptosis by
triggering a voltage-dependent anion channel 1 (VDAC1) positive
feedback loop.";
J. Biol. Chem. 289:32628-32638(2014).
[23]
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).
[24]
INTERACTION WITH BCL2L11.
PubMed=27013495; DOI=10.15252/embr.201541392;
Weber A., Heinlein M., Dengjel J., Alber C., Singh P.K., Haecker G.;
"The deubiquitinase Usp27x stabilizes the BH3-only protein Bim and
enhances apoptosis.";
EMBO Rep. 17:724-738(2016).
[25]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), AND STRUCTURE BY NMR OF 1-209.
PubMed=8692274; DOI=10.1038/381335a0;
Muchmore S.W., Sattler M., Liang H., Meadows R.P., Harlan J.E.,
Yoon H.S., Nettesheim D., Chang B.S., Thompson C.B., Wong S.L.,
Ng S.L., Fesik S.W.;
"X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed
cell death.";
Nature 381:335-341(1996).
[26]
STRUCTURE BY NMR OF 1-209.
PubMed=9020082; DOI=10.1126/science.275.5302.983;
Sattler M., Liang H., Nettesheim D., Meadows R.P., Harlan J.E.,
Eberstadt M., Yoon H.S., Shuker S.B., Chang B.S., Minn A.J.,
Thompson C.B., Fesik S.W.;
"Structure of Bcl-xL-Bak peptide complex: recognition between
regulators of apoptosis.";
Science 275:983-986(1997).
[27]
STRUCTURE BY NMR OF 1-209 IN COMPLEX WITH BAD.
PubMed=11206074; DOI=10.1110/ps.9.12.2528;
Petros A.M., Nettesheim D.G., Wang Y., Olejniczak E.T., Meadows R.P.,
Mack J., Swift K., Matayoshi E.D., Zhang H., Thompson C.B.,
Fesik S.W.;
"Rationale for Bcl-xL/Bad peptide complex formation from structure,
mutagenesis, and biophysical studies.";
Protein Sci. 9:2528-2534(2000).
[28]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1-211.
PubMed=14534311; DOI=10.1074/jbc.M306021200;
Manion M.K., O'Neill J.W., Giedt C.D., Kim K.M., Zhang K.Y.Z.,
Hockenbery D.M.;
"Bcl-XL mutations suppress cellular sensitivity to antimycin A.";
J. Biol. Chem. 279:2159-2165(2004).
[29]
STRUCTURE BY NMR OF 1-209.
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).
[30]
X-RAY CRYSTALLOGRAPHY (3.45 ANGSTROMS) OF 1-211, AND HOMODIMERIZATION.
PubMed=16368107; DOI=10.1016/j.jmb.2005.11.032;
O'Neill J.W., Manion M.K., Maguire B., Hockenbery D.M.;
"BCL-XL dimerization by three-dimensional domain swapping.";
J. Mol. Biol. 356:367-381(2006).
[31]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 83-209 IN COMPLEX WITH BECN1.
PubMed=17337444; DOI=10.1074/jbc.M700492200;
Oberstein A., Jeffrey P.D., Shi Y.;
"Crystal structure of the Bcl-XL-Beclin 1 peptide complex: Beclin 1 is
a novel BH3-only protein.";
J. Biol. Chem. 282:13123-13132(2007).
[32]
STRUCTURE BY NMR OF 1-209.
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).
[33]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1-209 IN COMPLEX WITH HEBP2,
AND INTERACTION WITH HEBP2.
PubMed=21639858; DOI=10.1042/BJ20110257;
Ambrosi E., Capaldi S., Bovi M., Saccomani G., Perduca M.,
Monaco H.L.;
"Structural changes in the BH3 domain of SOUL protein upon interaction
with the anti-apoptotic protein Bcl-xL.";
Biochem. J. 438:291-301(2011).
[34]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-209 IN COMPLEX WITH BBC3,
STRUCTURE BY NMR OF 1-209 IN COMPLEX WITH BBC3, AND INTERACTION WITH
BBC3 AND TP53.
PubMed=23340338; DOI=10.1038/nchembio.1166;
Follis A.V., Chipuk J.E., Fisher J.C., Yun M.K., Grace C.R.,
Nourse A., Baran K., Ou L., Min L., White S.W., Green D.R.,
Kriwacki R.W.;
"PUMA binding induces partial unfolding within BCL-xL to disrupt p53
binding and promote apoptosis.";
Nat. Chem. Biol. 9:163-168(2013).
-!- FUNCTION: Potent inhibitor of cell death. Inhibits activation of
caspases. Appears to regulate cell death by blocking the voltage-
dependent anion channel (VDAC) by binding to it and preventing the
release of the caspase activator, CYC1, from the mitochondrial
membrane. Also acts as a regulator of G2 checkpoint and
progression to cytokinesis during mitosis.
-!- FUNCTION: Isoform Bcl-X(L) also regulates presynaptic plasticity,
including neurotransmitter release and recovery, number of axonal
mitochondria as well as size and number of synaptic vesicle
clusters. During synaptic stimulation, increases ATP availability
from mitochondria through regulation of mitochondrial membrane ATP
synthase F(1)F(0) activity and regulates endocytic vesicle
retrieval in hippocampal neurons through association with DMN1L
and stimulation of its GTPase activity in synaptic vesicles. May
attenuate inflammation impairing NLRP1-inflammasome activation,
hence CASP1 activation and IL1B release (PubMed:17418785).
{ECO:0000269|PubMed:17418785}.
-!- FUNCTION: Isoform Bcl-X(S) promotes apoptosis.
-!- SUBUNIT: Homodimer. Isoform Bcl-X(L) forms heterodimers with BAX,
BAK or BCL2. Heterodimerization with BAX does not seem to be
required for anti-apoptotic activity. Interacts with BCL2L11.
Interacts with BAD. Interacts (isoform Bcl-X(L)) with SIVA1
(isoform 1); the interaction inhibits the anti-apoptotic activity.
Interacts with BECN1 and PGAM5. Isoform Bcl-X(L) interacts with
IKZF3. Interacts with HEBP2. Isoform Bcl-X(L) interacts with
RTL10/BOP. Interacts with p53/TP53 and BBC3; interaction with BBC3
disrupts the interaction with p53/TP53. Isoform Bcl-X(L) interacts
with DNM1L and CLTA; DNM1L and BCL2L1 isoform BCL-X(L) may form a
complex in synaptic vesicles that also contains clathrin and MFF.
Interacts with ATP5A and ATP5B; the interactions mediate the
association of isoform Bcl-X(L) with the mitochondrial membrane
ATP synthase F(1)F(0) ATP synthase. Interacts with VDAC1
(PubMed:25296756). Isoform Bcl-X(L) 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).
Interacts with BCL2L11 (via BH3) (PubMed:27013495).
{ECO:0000269|PubMed:10772918, ECO:0000269|PubMed:11206074,
ECO:0000269|PubMed:11463391, ECO:0000269|PubMed:11714801,
ECO:0000269|PubMed:12011449, ECO:0000269|PubMed:17046835,
ECO:0000269|PubMed:17337444, ECO:0000269|PubMed:17418785,
ECO:0000269|PubMed:21639858, ECO:0000269|PubMed:23340338,
ECO:0000269|PubMed:23792689, ECO:0000269|PubMed:25296756,
ECO:0000269|PubMed:27013495, ECO:0000269|PubMed:9675101}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-78035, EBI-78035;
Q92934:BAD; NbExp=9; IntAct=EBI-78035, EBI-700771;
Q61337:Bad (xeno); NbExp=3; IntAct=EBI-287195, EBI-400328;
Q16611:BAK1; NbExp=13; IntAct=EBI-287195, EBI-519866;
Q07812:BAX; NbExp=20; IntAct=EBI-287195, EBI-516580;
Q9BXH1:BBC3; NbExp=9; IntAct=EBI-287195, EBI-519884;
Q99ML1:Bbc3 (xeno); NbExp=3; IntAct=EBI-287195, EBI-727801;
O43521:BCL2L11; NbExp=10; IntAct=EBI-287195, EBI-526406;
O43521-1:BCL2L11; NbExp=2; IntAct=EBI-287195, EBI-526416;
O54918-3:Bcl2l11 (xeno); NbExp=3; IntAct=EBI-287195, EBI-526084;
Q14457:BECN1; NbExp=5; IntAct=EBI-287195, EBI-949378;
P55957:BID; NbExp=7; IntAct=EBI-287195, EBI-519672;
Q13323:BIK; NbExp=9; IntAct=EBI-78035, EBI-700794;
Q96LC9:BMF; NbExp=7; IntAct=EBI-78035, EBI-3919268;
P30429-2:ced-4 (xeno); NbExp=2; IntAct=EBI-287195, EBI-536271;
P10909-4:CLU; NbExp=6; IntAct=EBI-287195, EBI-4322678;
P99999:CYCS; NbExp=2; IntAct=EBI-78035, EBI-446479;
Q99MI6:Gimap3 (xeno); NbExp=3; IntAct=EBI-287195, EBI-15572304;
Q8BWF2:Gimap5 (xeno); NbExp=3; IntAct=EBI-287195, EBI-15572348;
O00198:HRK; NbExp=3; IntAct=EBI-287195, EBI-701322;
P42345:MTOR; NbExp=3; IntAct=EBI-287195, EBI-359260;
Q9C000:NLRP1; NbExp=9; IntAct=EBI-78035, EBI-1220518;
Q7L3V2:RTL10; NbExp=3; IntAct=EBI-287195, EBI-10697720;
O15304:SIVA1; NbExp=2; IntAct=EBI-78035, EBI-520756;
O15304-1:SIVA1; NbExp=5; IntAct=EBI-287195, EBI-520766;
Q9H2V7:SPNS1; NbExp=3; IntAct=EBI-78035, EBI-1386527;
P04637:TP53; NbExp=26; IntAct=EBI-287195, EBI-366083;
P02340:Tp53 (xeno); NbExp=3; IntAct=EBI-287195, EBI-474016;
Q13625:TP53BP2; NbExp=3; IntAct=EBI-287195, EBI-77642;
Q86Y07-1:VRK2; NbExp=2; IntAct=EBI-287195, EBI-1207633;
-!- SUBCELLULAR LOCATION: Isoform Bcl-X(L): Mitochondrion inner
membrane {ECO:0000250}. Mitochondrion outer membrane
{ECO:0000250}. Mitochondrion matrix {ECO:0000250}. Cytoplasmic
vesicle, secretory vesicle, synaptic vesicle membrane
{ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Cytoplasm,
cytoskeleton, microtubule organizing center, centrosome. Nucleus
membrane {ECO:0000250}; Single-pass membrane protein
{ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=After neuronal
stimulation, translocates from cytosol to synaptic vesicle and
mitochondrion membrane in a calmodulin-dependent manner (By
similarity). Localizes to the centrosome when phosphorylated at
Ser-49. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=Bcl-X(L); Synonyms=Bcl-xL;
IsoId=Q07817-1; Sequence=Displayed;
Name=Bcl-X(S); Synonyms=Bcl-xS;
IsoId=Q07817-2; Sequence=VSP_000515;
Name=Bcl-X(beta);
IsoId=Q07817-3; Sequence=VSP_000516;
-!- TISSUE SPECIFICITY: Bcl-X(S) is expressed at high levels in cells
that undergo a high rate of turnover, such as developing
lymphocytes. In contrast, Bcl-X(L) is found in tissues containing
long-lived postmitotic cells, such as adult brain.
-!- DOMAIN: The BH4 motif is required for anti-apoptotic activity. The
BH1 and BH2 motifs are required for both heterodimerization with
other Bcl-2 family members and for repression of cell death.
-!- DOMAIN: The loop between motifs BH4 and BH3 is required for the
interaction with NLRP1. {ECO:0000269|PubMed:17418785}.
-!- PTM: Proteolytically cleaved by caspases during apoptosis. The
cleaved protein, lacking the BH4 motif, has pro-apoptotic
activity. {ECO:0000269|PubMed:9435230}.
-!- PTM: Phosphorylated on Ser-62 by CDK1. This phosphorylation is
partial in normal mitotic cells, but complete in G2-arrested cells
upon DNA-damage, thus promoting subsequent apoptosis probably by
triggering caspases-mediated proteolysis. Phosphorylated by PLK3,
leading to regulate the G2 checkpoint and progression to
cytokinesis during mitosis. Phosphorylation at Ser-49 appears
during the S phase and G2, disappears rapidly in early mitosis
during prometaphase, metaphase and early anaphase, and re-appears
during telophase and cytokinesis. {ECO:0000269|PubMed:19917720,
ECO:0000269|PubMed:21840391}.
-!- 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/BCL2L1ID129ch20q11.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; Z23115; CAA80661.1; -; mRNA.
EMBL; Z23116; CAA80662.1; -; mRNA.
EMBL; U72398; AAB17354.1; -; Genomic_DNA.
EMBL; CR936637; CAI56777.1; -; mRNA.
EMBL; BT007208; AAP35872.1; -; mRNA.
EMBL; AL160175; CAI12811.1; -; Genomic_DNA.
EMBL; AL117381; CAI12811.1; JOINED; Genomic_DNA.
EMBL; AL117381; CAI23025.1; -; Genomic_DNA.
EMBL; AL160175; CAI23025.1; JOINED; Genomic_DNA.
EMBL; CH471077; EAW76424.1; -; Genomic_DNA.
EMBL; CH471077; EAW76425.1; -; Genomic_DNA.
EMBL; CH471077; EAW76429.1; -; Genomic_DNA.
EMBL; BC019307; AAH19307.1; -; mRNA.
CCDS; CCDS13188.1; -. [Q07817-2]
CCDS; CCDS13189.1; -. [Q07817-1]
PIR; B47537; B47537.
PIR; JE0203; JE0203.
RefSeq; NP_001182.1; NM_001191.3. [Q07817-2]
RefSeq; NP_001304848.1; NM_001317919.1. [Q07817-1]
RefSeq; NP_001304849.1; NM_001317920.1. [Q07817-1]
RefSeq; NP_001304850.1; NM_001317921.1. [Q07817-1]
RefSeq; NP_001309168.1; NM_001322239.1. [Q07817-1]
RefSeq; NP_001309169.1; NM_001322240.1. [Q07817-1]
RefSeq; NP_001309171.1; NM_001322242.1. [Q07817-1]
RefSeq; NP_612815.1; NM_138578.2. [Q07817-1]
RefSeq; XP_011527266.1; XM_011528964.2. [Q07817-1]
RefSeq; XP_016883482.1; XM_017027993.1. [Q07817-1]
UniGene; Hs.516966; -.
UniGene; Hs.732176; -.
PDB; 1BXL; NMR; -; A=1-209.
PDB; 1G5J; NMR; -; A=1-209.
PDB; 1LXL; NMR; -; A=1-209.
PDB; 1MAZ; X-ray; 2.20 A; A=1-209.
PDB; 1R2D; X-ray; 1.95 A; A=1-211.
PDB; 1R2E; X-ray; 2.10 A; A=1-211.
PDB; 1R2G; X-ray; 2.70 A; A=1-211.
PDB; 1R2H; X-ray; 2.20 A; A=1-211.
PDB; 1R2I; X-ray; 2.00 A; A=1-211.
PDB; 1YSG; NMR; -; A=1-209.
PDB; 1YSI; NMR; -; A=1-209.
PDB; 1YSN; NMR; -; A=1-209.
PDB; 2B48; X-ray; 3.45 A; A=1-211.
PDB; 2LP8; NMR; -; A=1-209.
PDB; 2LPC; NMR; -; A=1-209.
PDB; 2M03; NMR; -; A=1-209.
PDB; 2M04; NMR; -; A=1-209.
PDB; 2ME8; NMR; -; A=1-209.
PDB; 2ME9; NMR; -; A=1-209.
PDB; 2MEJ; NMR; -; A=1-209.
PDB; 2O1Y; NMR; -; A=1-209.
PDB; 2O2M; NMR; -; A=2-20, A=83-196.
PDB; 2O2N; NMR; -; A=2-20, A=83-196.
PDB; 2P1L; X-ray; 2.50 A; A/C/E/G=1-209.
PDB; 2PON; NMR; -; B=1-196.
PDB; 2YJ1; X-ray; 2.24 A; A/C=1-209.
PDB; 2YQ6; X-ray; 1.80 A; A=1-209.
PDB; 2YQ7; X-ray; 1.90 A; A=1-209.
PDB; 2YXJ; X-ray; 2.20 A; A/B=1-209.
PDB; 3CVA; X-ray; 2.70 A; X=1-211.
PDB; 3FDL; X-ray; 1.78 A; A=1-209.
PDB; 3FDM; X-ray; 2.26 A; A/B/C=1-209.
PDB; 3INQ; X-ray; 2.00 A; A/B=1-209.
PDB; 3IO8; X-ray; 2.30 A; A/C=1-209.
PDB; 3PL7; X-ray; 2.61 A; A/B=1-209.
PDB; 3QKD; X-ray; 2.02 A; A/B=1-209.
PDB; 3R85; X-ray; 1.95 A; A/B/C/D=1-197.
PDB; 3SP7; X-ray; 1.40 A; A=1-209.
PDB; 3SPF; X-ray; 1.70 A; A=1-209.
PDB; 3WIZ; X-ray; 2.45 A; A/B=1-209.
PDB; 3ZK6; X-ray; 2.48 A; A/B=1-209.
PDB; 3ZLN; X-ray; 2.29 A; A=1-209.
PDB; 3ZLO; X-ray; 2.60 A; A=1-209.
PDB; 3ZLR; X-ray; 2.03 A; A/B=1-209.
PDB; 4A1U; X-ray; 1.54 A; A=1-209.
PDB; 4A1W; X-ray; 2.50 A; A/B/C/D=1-209.
PDB; 4AQ3; X-ray; 2.40 A; A/B/C/D/E/F=29-44.
PDB; 4BPK; X-ray; 1.76 A; A/B=1-209.
PDB; 4C52; X-ray; 2.05 A; A/B=1-209.
PDB; 4C5D; X-ray; 2.30 A; A/B=1-209.
PDB; 4CIN; X-ray; 2.69 A; A/B=1-209, C/D=79-102.
PDB; 4EHR; X-ray; 2.09 A; A=1-209.
PDB; 4HNJ; X-ray; 2.90 A; A/B=1-209.
PDB; 4IEH; X-ray; 2.10 A; A=29-44.
PDB; 4PPI; X-ray; 2.85 A; A=1-209.
PDB; 4QVE; X-ray; 2.05 A; A=1-209.
PDB; 4QVF; X-ray; 1.53 A; A=1-209.
PDB; 4QVX; X-ray; 2.10 A; A/B=1-23, A/B=83-209.
PDB; 4TUH; X-ray; 1.80 A; A/B/C/D/E/F/G/H=1-209.
PDB; 4Z9V; X-ray; 2.10 A; A/B=1-208.
PDB; 5AGW; X-ray; 2.69 A; A/B=29-44.
PDB; 5AGX; X-ray; 2.24 A; A/B=29-44.
PDB; 5B1Z; X-ray; 2.15 A; A/B=1-209.
PDB; 5C3G; X-ray; 2.45 A; A=83-209.
PDB; 5FMJ; X-ray; 2.43 A; A=1-209.
PDB; 5FMK; X-ray; 1.73 A; A=1-209.
PDB; 5L1Y; NMR; -; A=1-209.
PDBsum; 1BXL; -.
PDBsum; 1G5J; -.
PDBsum; 1LXL; -.
PDBsum; 1MAZ; -.
PDBsum; 1R2D; -.
PDBsum; 1R2E; -.
PDBsum; 1R2G; -.
PDBsum; 1R2H; -.
PDBsum; 1R2I; -.
PDBsum; 1YSG; -.
PDBsum; 1YSI; -.
PDBsum; 1YSN; -.
PDBsum; 2B48; -.
PDBsum; 2LP8; -.
PDBsum; 2LPC; -.
PDBsum; 2M03; -.
PDBsum; 2M04; -.
PDBsum; 2ME8; -.
PDBsum; 2ME9; -.
PDBsum; 2MEJ; -.
PDBsum; 2O1Y; -.
PDBsum; 2O2M; -.
PDBsum; 2O2N; -.
PDBsum; 2P1L; -.
PDBsum; 2PON; -.
PDBsum; 2YJ1; -.
PDBsum; 2YQ6; -.
PDBsum; 2YQ7; -.
PDBsum; 2YXJ; -.
PDBsum; 3CVA; -.
PDBsum; 3FDL; -.
PDBsum; 3FDM; -.
PDBsum; 3INQ; -.
PDBsum; 3IO8; -.
PDBsum; 3PL7; -.
PDBsum; 3QKD; -.
PDBsum; 3R85; -.
PDBsum; 3SP7; -.
PDBsum; 3SPF; -.
PDBsum; 3WIZ; -.
PDBsum; 3ZK6; -.
PDBsum; 3ZLN; -.
PDBsum; 3ZLO; -.
PDBsum; 3ZLR; -.
PDBsum; 4A1U; -.
PDBsum; 4A1W; -.
PDBsum; 4AQ3; -.
PDBsum; 4BPK; -.
PDBsum; 4C52; -.
PDBsum; 4C5D; -.
PDBsum; 4CIN; -.
PDBsum; 4EHR; -.
PDBsum; 4HNJ; -.
PDBsum; 4IEH; -.
PDBsum; 4PPI; -.
PDBsum; 4QVE; -.
PDBsum; 4QVF; -.
PDBsum; 4QVX; -.
PDBsum; 4TUH; -.
PDBsum; 4Z9V; -.
PDBsum; 5AGW; -.
PDBsum; 5AGX; -.
PDBsum; 5B1Z; -.
PDBsum; 5C3G; -.
PDBsum; 5FMJ; -.
PDBsum; 5FMK; -.
PDBsum; 5L1Y; -.
DisProt; DP00298; -.
ProteinModelPortal; Q07817; -.
SMR; Q07817; -.
BioGrid; 107070; 94.
CORUM; Q07817; -.
DIP; DIP-30916N; -.
ELM; Q07817; -.
IntAct; Q07817; 86.
MINT; MINT-89538; -.
STRING; 9606.ENSP00000302564; -.
BindingDB; Q07817; -.
ChEMBL; CHEMBL4625; -.
GuidetoPHARMACOLOGY; 2845; -.
TCDB; 1.A.21.1.1; the bcl-2 (bcl-2) family.
iPTMnet; Q07817; -.
PhosphoSitePlus; Q07817; -.
BioMuta; BCL2L1; -.
DMDM; 728955; -.
EPD; Q07817; -.
MaxQB; Q07817; -.
PaxDb; Q07817; -.
PeptideAtlas; Q07817; -.
PRIDE; Q07817; -.
TopDownProteomics; Q07817-1; -. [Q07817-1]
TopDownProteomics; Q07817-2; -. [Q07817-2]
DNASU; 598; -.
Ensembl; ENST00000307677; ENSP00000302564; ENSG00000171552. [Q07817-1]
Ensembl; ENST00000376055; ENSP00000365223; ENSG00000171552. [Q07817-2]
Ensembl; ENST00000376062; ENSP00000365230; ENSG00000171552. [Q07817-1]
GeneID; 598; -.
KEGG; hsa:598; -.
UCSC; uc002wwl.4; human. [Q07817-1]
CTD; 598; -.
DisGeNET; 598; -.
EuPathDB; HostDB:ENSG00000171552.12; -.
GeneCards; BCL2L1; -.
HGNC; HGNC:992; BCL2L1.
HPA; CAB072801; -.
HPA; HPA035734; -.
MIM; 600039; gene.
neXtProt; NX_Q07817; -.
OpenTargets; ENSG00000171552; -.
PharmGKB; PA76; -.
eggNOG; KOG4728; Eukaryota.
eggNOG; ENOG41123S0; LUCA.
GeneTree; ENSGT00530000062935; -.
HOGENOM; HOG000056452; -.
InParanoid; Q07817; -.
KO; K04570; -.
OMA; NGSPSWH; -.
OrthoDB; EOG091G0OCU; -.
PhylomeDB; Q07817; -.
TreeFam; TF315834; -.
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; Q07817; -.
ChiTaRS; BCL2L1; human.
EvolutionaryTrace; Q07817; -.
GeneWiki; BCL2-like_1_(gene); -.
GenomeRNAi; 598; -.
PMAP-CutDB; Q07817; -.
PRO; PR:Q07817; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000171552; -.
CleanEx; HS_BCL2L1; -.
ExpressionAtlas; Q07817; baseline and differential.
Genevisible; Q07817; HS.
GO; GO:0097136; C:Bcl-2 family protein complex; IDA:UniProtKB.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:HGNC.
GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0051434; F:BH3 domain binding; IPI:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046982; F:protein heterodimerization activity; IBA:GO_Central.
GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0008637; P:apoptotic mitochondrial changes; TAS:ProtInc.
GO; GO:0071839; P:apoptotic process in bone marrow; IEA:Ensembl.
GO; GO:0008283; P:cell proliferation; IEA:Ensembl.
GO; GO:0060154; P:cellular process regulating host cell cycle in response to virus; IEA:Ensembl.
GO; GO:0071312; P:cellular response to alkaloid; IEA:Ensembl.
GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
GO; GO:0071480; P:cellular response to gamma radiation; IEA:Ensembl.
GO; GO:0000910; P:cytokinesis; IMP:UniProtKB.
GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
GO; GO:0009566; P:fertilization; IEA:Ensembl.
GO; GO:0007281; P:germ cell development; IEA:Ensembl.
GO; GO:0040007; P:growth; IEA:Ensembl.
GO; GO:0097284; P:hepatocyte apoptotic process; IEA:Ensembl.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IEA:Ensembl.
GO; GO:0008584; P:male gonad development; IEA:Ensembl.
GO; GO:0070584; P:mitochondrion morphogenesis; IEA:Ensembl.
GO; GO:0007093; P:mitotic cell cycle checkpoint; IMP:UniProtKB.
GO; GO:2000811; P:negative regulation of anoikis; IMP:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0010507; P:negative regulation of autophagy; TAS:UniProtKB.
GO; GO:1900118; P:negative regulation of execution phase of apoptosis; IDA:UniProtKB.
GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; TAS:BHF-UCL.
GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; IDA:MGI.
GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IDA:BHF-UCL.
GO; GO:1902230; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage; IDA:BHF-UCL.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; IDA:BHF-UCL.
GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; IDA:UniProtKB.
GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
GO; GO:0001541; P:ovarian follicle development; IEA:Ensembl.
GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl.
GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; TAS:Reactome.
GO; GO:0046902; P:regulation of mitochondrial membrane permeability; IDA:HGNC.
GO; GO:0051881; P:regulation of mitochondrial membrane potential; IDA:HGNC.
GO; GO:0001836; P:release of cytochrome c from mitochondria; IDA:HGNC.
GO; GO:0046898; P:response to cycloheximide; IEA:Ensembl.
GO; GO:0034097; P:response to cytokine; IDA:MGI.
GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
GO; GO:0019050; P:suppression by virus of host apoptotic process; IDA:MGI.
Gene3D; 1.10.437.10; -; 1.
InterPro; IPR013279; Apop_reg_BclX.
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; IPR036834; Blc2-like_sf.
InterPro; IPR026298; Blc2_fam.
PANTHER; PTHR11256; PTHR11256; 1.
PANTHER; PTHR11256:SF12; PTHR11256:SF12; 1.
Pfam; PF00452; Bcl-2; 1.
Pfam; PF02180; BH4; 1.
PRINTS; PR01864; APOPREGBCLX.
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; Cell junction;
Complete proteome; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
Endocytosis; Membrane; Mitochondrion; Mitochondrion inner membrane;
Mitochondrion outer membrane; Nucleus; Phosphoprotein;
Reference proteome; Synapse; Transmembrane; Transmembrane helix.
CHAIN 1 233 Bcl-2-like protein 1.
/FTId=PRO_0000143062.
TRANSMEM 210 226 Helical. {ECO:0000255}.
MOTIF 4 24 BH4.
MOTIF 86 100 BH3.
MOTIF 129 148 BH1.
MOTIF 180 195 BH2.
SITE 61 62 Cleavage; by caspase-1.
MOD_RES 49 49 Phosphoserine; by PLK3.
{ECO:0000269|PubMed:21840391}.
MOD_RES 62 62 Phosphoserine; by CDK1.
{ECO:0000269|PubMed:19917720}.
VAR_SEQ 126 188 Missing (in isoform Bcl-X(S)).
{ECO:0000305}.
/FTId=VSP_000515.
VAR_SEQ 189 233 DTFVELYGNNAAAESRKGQERFNRWFLTGMTVAGVVLLGSL
FSRK -> VRTKPLVCPFSLASGQRSPTALLLYLFLLCWVI
VGDVDS (in isoform Bcl-X(beta)).
{ECO:0000305}.
/FTId=VSP_000516.
MUTAGEN 49 49 S->A: Less stable at G2 checkpoint after
DNA damage.
{ECO:0000269|PubMed:21840391}.
MUTAGEN 61 61 D->A: No cleavage by caspase-1 nor by
caspase-3. {ECO:0000269|PubMed:9435230}.
MUTAGEN 131 133 FRD->VRA: No heterodimerization with BAX.
{ECO:0000269|PubMed:8596636}.
MUTAGEN 135 137 VNW->AIL: Loss of anti-apoptotic
activity. {ECO:0000269|PubMed:8596636}.
MUTAGEN 138 140 GRI->ELN: Loss of anti-apoptotic
activity. {ECO:0000269|PubMed:8596636}.
MUTAGEN 138 138 G->A: No heterodimerization with BAX.
{ECO:0000269|PubMed:7644501}.
MUTAGEN 145 147 SFG->YCC: Decreases interaction with
DNM1L, no effect on endocytosis
enhancement.
{ECO:0000269|PubMed:23792689}.
MUTAGEN 148 148 G->E: No heterodimerization with BAX.
{ECO:0000269|PubMed:8596636}.
MUTAGEN 156 156 D->A: No effect on caspase-1 cleavage.
{ECO:0000269|PubMed:8596636}.
MUTAGEN 176 176 D->A: No effect on caspase-1 cleavage.
{ECO:0000269|PubMed:8596636}.
MUTAGEN 188 191 WDTF->SVTC: Abolishes interaction with
DNM1L and endocytosis enhancement.
{ECO:0000269|PubMed:23792689}.
MUTAGEN 188 189 WD->GA: Reduces anti-apoptotic activity
by about half.
{ECO:0000269|PubMed:8596636}.
MUTAGEN 189 189 D->A: No effect on caspase-1 cleavage.
{ECO:0000269|PubMed:8596636}.
CONFLICT 70 70 G -> A (in Ref. 1; CAA80661).
{ECO:0000305}.
CONFLICT 168 168 A -> V (in Ref. 4; CAI56777).
{ECO:0000305}.
STRAND 1 3 {ECO:0000244|PDB:1YSG}.
HELIX 5 18 {ECO:0000244|PDB:4QVF}.
TURN 19 21 {ECO:0000244|PDB:4QVF}.
HELIX 24 26 {ECO:0000244|PDB:4QVF}.
STRAND 29 36 {ECO:0000244|PDB:1LXL}.
STRAND 38 41 {ECO:0000244|PDB:1G5J}.
TURN 42 44 {ECO:0000244|PDB:1BXL}.
STRAND 50 53 {ECO:0000244|PDB:2ME9}.
STRAND 56 59 {ECO:0000244|PDB:2ME8}.
STRAND 62 64 {ECO:0000244|PDB:5L1Y}.
TURN 65 68 {ECO:0000244|PDB:1LXL}.
TURN 70 73 {ECO:0000244|PDB:1LXL}.
HELIX 77 79 {ECO:0000244|PDB:5L1Y}.
STRAND 82 84 {ECO:0000244|PDB:2ME8}.
HELIX 86 104 {ECO:0000244|PDB:4QVF}.
HELIX 108 111 {ECO:0000244|PDB:4QVF}.
TURN 112 114 {ECO:0000244|PDB:2ME8}.
TURN 116 118 {ECO:0000244|PDB:4QVF}.
HELIX 119 130 {ECO:0000244|PDB:4QVF}.
TURN 131 133 {ECO:0000244|PDB:4QVF}.
HELIX 137 156 {ECO:0000244|PDB:4QVF}.
HELIX 162 177 {ECO:0000244|PDB:4QVF}.
HELIX 179 184 {ECO:0000244|PDB:4QVF}.
TURN 185 187 {ECO:0000244|PDB:1R2D}.
HELIX 188 195 {ECO:0000244|PDB:4QVF}.
TURN 196 198 {ECO:0000244|PDB:4A1U}.
HELIX 199 205 {ECO:0000244|PDB:4A1U}.
STRAND 206 208 {ECO:0000244|PDB:2M03}.
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


Related products :

Catalog number Product name Quantity
U1343h CLIA Apoptosis regulator BAX,BAX,BCL2L4,Bcl2-L-4,Bcl-2-like protein 4,Homo sapiens,Human 96T
E1343h ELISA kit Apoptosis regulator BAX,BAX,BCL2L4,Bcl2-L-4,Bcl-2-like protein 4,Homo sapiens,Human 96T
E1343h ELISA Apoptosis regulator BAX,BAX,BCL2L4,Bcl2-L-4,Bcl-2-like protein 4,Homo sapiens,Human 96T
CSB-EL002611BO Bovine Apoptosis regulator Bcl-2(BCL2) ELISA kit 96T
CSB-EL002611CH Chicken Apoptosis regulator Bcl-2(BCL2) ELISA kit 96T
U0778b CLIA Apoptosis regulator Bcl-2,BCL2,Bos taurus,Bovine 96T
CSB-EL002611BO Bovine Apoptosis regulator Bcl-2(BCL2) ELISA kit SpeciesBovine 96T
CSB-EL002611CH Chicken Apoptosis regulator Bcl-2(BCL2) ELISA kit SpeciesChicken 96T
E0778b ELISA kit Apoptosis regulator Bcl-2,BCL2,Bos taurus,Bovine 96T
U0778m CLIA Apoptosis regulator Bcl-2,Bcl2,Bcl-2,Mouse,Mus musculus 96T
E0778m ELISA Apoptosis regulator Bcl-2,Bcl2,Bcl-2,Mouse,Mus musculus 96T
E0778r ELISA Apoptosis regulator Bcl-2,Bcl2,Bcl-2,Rat,Rattus norvegicus 96T
E0778m ELISA kit Apoptosis regulator Bcl-2,Bcl2,Bcl-2,Mouse,Mus musculus 96T
U0778r CLIA Apoptosis regulator Bcl-2,Bcl2,Bcl-2,Rat,Rattus norvegicus 96T
E0778r ELISA kit Apoptosis regulator Bcl-2,Bcl2,Bcl-2,Rat,Rattus norvegicus 96T
E0778b ELISA Apoptosis regulator Bcl-2,BCL2,Bos taurus,Bovine 96T
E0778b ELISA Kit FOR Apoptosis regulator Bcl-2; organism: Bovine; gene name: BCL2 96T
E0778h ELISA kit Apoptosis regulator Bcl-2,BCL2,Homo sapiens,Human 96T
U0778h CLIA Apoptosis regulator Bcl-2,BCL2,Homo sapiens,Human 96T
E0778h ELISA Apoptosis regulator Bcl-2,BCL2,Homo sapiens,Human 96T
GWB-E2C8B2 Apoptosis Regulator Bcl-2 (BCL2) Rabbit anti-Human Polyclonal (Thr56) Antibody
GWB-47C732 Apoptosis Regulator Bcl-2 (BCL2) Rabbit anti-Human Polyclonal (Ser70) Antibody
E0778c ELISA kit Apoptosis regulator Bcl-2,BCL2,BCL-2,Chicken,Gallus gallus 96T
E0778c ELISA Apoptosis regulator Bcl-2,BCL2,BCL-2,Chicken,Gallus gallus 96T
U0778c CLIA Apoptosis regulator Bcl-2,BCL2,BCL-2,Chicken,Gallus gallus 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur