B2L11_HUMAN
ID B2L11_HUMAN Reviewed; 198 AA.
AC O43521; A8K2W2; O43522; Q0MSE7; Q0MSE8; Q0MSE9; Q53R28; Q6JTU6; Q6T851;
AC Q6TE14; Q6TE15; Q6TE16; Q6V402; Q8WYL6; Q8WYL7; Q8WYL8; Q8WYL9; Q8WYM0;
AC Q8WYM1;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Bcl-2-like protein 11;
DE Short=Bcl2-L-11;
DE AltName: Full=Bcl2-interacting mediator of cell death;
GN Name=BCL2L11; Synonyms=BIM;
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 BIMEL AND BIML), AND FUNCTION.
RC TISSUE=Peripheral blood, and Spleen;
RX PubMed=9430630; DOI=10.1093/emboj/17.2.384;
RA O'Connor L., Strasser A., O'Reilly L.A., Hausmann G., Adams J.M., Cory S.,
RA Huang D.C.S.;
RT "Bim: a novel member of the Bcl-2 family that promotes apoptosis.";
RL EMBO J. 17:384-395(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BIM-ALPHA1; BIM-ALPHA2; BIM-BETA1;
RP BIM-BETA2; BIM-BETA3 AND BIM-BETA4), FUNCTION (ISOFORMS BIM-ALPHA1 AND
RP BIM-ALPHA2), AND SUBCELLULAR LOCATION.
RX PubMed=11734221; DOI=10.1016/s0014-5793(01)03145-3;
RA Mami U., Miyashita T., Shikama Y., Tadokoro K., Yamada M.;
RT "Molecular cloning and characterization of six novel isoforms of human Bim,
RT a member of the proapoptotic Bcl-2 family.";
RL FEBS Lett. 509:135-141(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BIM-GAMMA), FUNCTION (ISOFORM
RP BIM-GAMMA), SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12019181;
RA Liu J.-W., Chandra D., Tang S.H., Chopra D., Tang D.G.;
RT "Identification and characterization of Bimgamma, a novel proapoptotic BH3-
RT only splice variant of Bim.";
RL Cancer Res. 62:2976-2981(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BIMEL; BIML; BIMS; BIM-ALPHA1;
RP BIM-ALPHA2; BIM-ALPHA3; BIMA; BIMABC AND BIMAC), ALTERNATIVE SPLICING,
RP FUNCTION, INTERACTION WITH BCL2; BCL2L1 ISOFORM BCL-XL AND BAX, AND
RP MUTAGENESIS OF GLY-156 AND ASN-160.
RC TISSUE=Embryonic kidney, and Ovarian cancer;
RX PubMed=11997495; DOI=10.1128/mcb.22.11.3577-3589.2002;
RA Marani M., Tenev T., Hancock D., Downward J., Lemoine N.R.;
RT "Identification of novel isoforms of the BH3 domain protein Bim which
RT directly activate Bax to trigger apoptosis.";
RL Mol. Cell. Biol. 22:3577-3589(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BIMS AND BIM-ALPHA3), AND FUNCTION
RP (ISOFORM BIM-ALPHA3).
RX PubMed=15147734; DOI=10.1016/j.biocel.2003.12.015;
RA Chen J.Z., Ji C.N., Gu S.H., Li J.X., Zhao E.P., Huang Y., Huang L.,
RA Ying K., Xie Y., Mao Y.M.;
RT "Over-expression of Bim alpha3, a novel isoform of human Bim, result in
RT cell apoptosis.";
RL Int. J. Biochem. Cell Biol. 36:1554-1561(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BIM-ALPHA3; BIM-ALPHA4; BIM-ALPHA5;
RP BIM-ALPHA6; BIM-BETA5; BIM-BETA6; BIM-BETA7).
RX PubMed=17503221; DOI=10.1007/s10495-007-0093-5;
RA Miao J., Chen G.G., Yun J.P., Chun S.Y., Zheng Z.Z., Ho R.L.K., Chak E.C.,
RA Xia N.S., Lai P.B.;
RT "Identification and characterization of BH3 domain protein Bim and its
RT isoforms in human hepatocellular carcinomas.";
RL Apoptosis 12:1691-1701(2007).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS BIMEL AND BIML).
RC TISSUE=Teratocarcinoma, and Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BIMEL).
RC TISSUE=Blood;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-69, AND
RP UBIQUITINATION.
RX PubMed=15486195;
RA Fukazawa H., Noguchi K., Masumi A., Murakami Y., Uehara Y.;
RT "BimEL is an important determinant for induction of anoikis sensitivity by
RT mitogen-activated protein/extracellular signal-regulated kinase kinase
RT inhibitors.";
RL Mol. Cancer Ther. 3:1281-1288(2004).
RN [12]
RP FUNCTION, AND INTERACTION WITH HUMANIN.
RX PubMed=15661735; DOI=10.1074/jbc.m413062200;
RA Luciano F., Zhai D., Zhu X., Bailly-Maitre B., Ricci J.E.,
RA Satterthwait A.C., Reed J.C.;
RT "Cytoprotective peptide humanin binds and inhibits proapoptotic Bcl-2/Bax
RT family protein BimEL.";
RL J. Biol. Chem. 280:15825-15835(2005).
RN [13]
RP INTERACTION WITH 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 [14]
RP MUTAGENESIS OF GLY-156.
RX PubMed=17289999; DOI=10.1126/science.1133289;
RA Willis S.N., Fletcher J.I., Kaufmann T., van Delft M.F., Chen L.,
RA Czabotar P.E., Ierino H., Lee E.F., Fairlie W.D., Bouillet P., Strasser A.,
RA Kluck R.M., Adams J.M., Huang D.C.;
RT "Apoptosis initiated when BH3 ligands engage multiple Bcl-2 homologs, not
RT Bax or Bak.";
RL Science 315:856-859(2007).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [16]
RP INTERACTION WITH TRIM2.
RX PubMed=21478148; DOI=10.1074/jbc.m110.197707;
RA Thompson S., Pearson A.N., Ashley M.D., Jessick V., Murphy B.M., Gafken P.,
RA Henshall D.C., Morris K.T., Simon R.P., Meller R.;
RT "Identification of a novel Bcl-2-interacting mediator of cell death (Bim)
RT E3 ligase, tripartite motif-containing protein 2 (TRIM2), and its role in
RT rapid ischemic tolerance-induced neuroprotection.";
RL J. Biol. Chem. 286:19331-19339(2011).
RN [17]
RP INTERACTION WITH BCL2L10.
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 [18]
RP INDUCTION BY ER STRESS.
RX PubMed=22761832; DOI=10.1371/journal.pone.0039586;
RA Ghosh A.P., Klocke B.J., Ballestas M.E., Roth K.A.;
RT "CHOP potentially co-operates with FOXO3a in neuronal cells to regulate
RT PUMA and BIM expression in response to ER stress.";
RL PLoS ONE 7:E39586-E39586(2012).
RN [19]
RP INTERACTION WITH BCL2L10.
RX PubMed=23563182; DOI=10.1038/onc.2013.99;
RA van de Kooij B., Rooswinkel R.W., Kok F., Herrebout M., de Vries E.,
RA Paauwe M., Janssen G.M., van Veelen P.A., Borst J.;
RT "Polyubiquitination and proteasomal turnover controls the anti-apoptotic
RT activity of Bcl-B.";
RL Oncogene 32:5439-5448(2013).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [21]
RP INTERACTION WITH BCL2L1; MCL1 AND USP27X.
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 [22]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 141-166 IN COMPLEX WITH MCL1.
RX PubMed=17389404; DOI=10.1073/pnas.0701297104;
RA Czabotar P.E., Lee E.F., van Delft M.F., Day C.L., Smith B.J.,
RA Huang D.C.S., Fairlie W.D., Hinds M.G., Colman P.M.;
RT "Structural insights into the degradation of Mcl-1 induced by BH3
RT domains.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:6217-6222(2007).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 141-165 IN COMPLEX WITH BCL2A1.
RX PubMed=18812174; DOI=10.1016/j.febslet.2008.09.028;
RA Herman M.D., Nyman T., Welin M., Lehtio L., Flodin S., Tresaugues L.,
RA Kotenyova T., Flores A., Nordlund P.;
RT "Completing the family portrait of the anti-apoptotic Bcl-2 proteins:
RT crystal structure of human Bfl-1 in complex with Bim.";
RL FEBS Lett. 582:3590-3594(2008).
RN [24] {ECO:0007744|PDB:4B4S}
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 51-76 IN COMPLEX WITH BCL2L10, AND
RP INTERACTION WITH BCL2L10.
RX PubMed=23235460; DOI=10.1038/cddis.2012.178;
RA Rautureau G.J., Yabal M., Yang H., Huang D.C., Kvansakul M., Hinds M.G.;
RT "The restricted binding repertoire of Bcl-B leaves Bim as the universal
RT BH3-only prosurvival Bcl-2 protein antagonist.";
RL Cell Death Dis. 3:e443-e443(2012).
CC -!- FUNCTION: Induces apoptosis and anoikis. Isoform BimL is more potent
CC than isoform BimEL. Isoform Bim-alpha1, isoform Bim-alpha2 and isoform
CC Bim-alpha3 induce apoptosis, although less potent than isoform BimEL,
CC isoform BimL and isoform BimS. Isoform Bim-gamma induces apoptosis.
CC Isoform Bim-alpha3 induces apoptosis possibly through a caspase-
CC mediated pathway. Isoform BimAC and isoform BimABC lack the ability to
CC induce apoptosis. {ECO:0000269|PubMed:11997495,
CC ECO:0000269|PubMed:15486195, ECO:0000269|PubMed:15661735,
CC ECO:0000269|PubMed:9430630}.
CC -!- SUBUNIT: Forms heterodimers with a number of antiapoptotic Bcl-2
CC proteins, including MCL1, BCL2, BCL2L1 isoform Bcl-X(L), BCL2A1/BFL-1,
CC BHRF1, and BCL2L2/BCLW (PubMed:11997495, PubMed:27013495,
CC PubMed:18812174). Does not heterodimerize with proapoptotic proteins
CC such as BAD, BOK or BAK. Identified in a complex containing BCL2L11,
CC DYNLL1 and BCL2L1 isoform Bcl-X(L); BH3 integrity is required for
CC BCL2L1-binding. Interacts with YWHAZ. When phosphorylated, interacts
CC with TRIM2; this interaction is associated with ubiquitination and
CC degradation (PubMed:21478148). Interacts with MCL1; may sequester
CC BCL2L11 to prevent its pro-apoptotic activity (PubMed:27013495,
CC PubMed:17389404). Interacts with GIMAP5 (PubMed:16509771). Interacts
CC with BCL2L10/BCL-B (PubMed:23235460, PubMed:23563182, PubMed:22498477).
CC {ECO:0000269|PubMed:11997495, ECO:0000269|PubMed:16509771,
CC ECO:0000269|PubMed:17389404, ECO:0000269|PubMed:18812174,
CC ECO:0000269|PubMed:21478148, ECO:0000269|PubMed:22498477,
CC ECO:0000269|PubMed:23235460, ECO:0000269|PubMed:23563182,
CC ECO:0000269|PubMed:27013495}.
CC -!- SUBUNIT: [Isoform BimEL]: Interacts (when phosphorylated) with USP27X;
CC the interaction leads to BCL2L11 deubiquitination and stabilization
CC (PubMed:27013495). Interacts with humanin; the interaction prevents
CC BIM-induced apoptosis. {ECO:0000269|PubMed:15661735}.
CC -!- SUBUNIT: [Isoform BimL]: Does not interact with humanin.
CC {ECO:0000269|PubMed:15661735}.
CC -!- SUBUNIT: [Isoform BimS]: Interacts with BAX; the interaction may lead
CC to BAX activation through conformational change (PubMed:11997495). Does
CC not interact with humanin (PubMed:15661735).
CC {ECO:0000269|PubMed:11997495, ECO:0000269|PubMed:15661735}.
CC -!- SUBUNIT: [Isoform Bim-alpha3]: Interacts with BAX; the interaction may
CC lead to BAX activation through conformational change.
CC {ECO:0000269|PubMed:11997495}.
CC -!- INTERACTION:
CC O43521; Q92934: BAD; NbExp=2; IntAct=EBI-526406, EBI-700771;
CC O43521; Q07812: BAX; NbExp=22; IntAct=EBI-526406, EBI-516580;
CC O43521; P10415: BCL2; NbExp=8; IntAct=EBI-526406, EBI-77694;
CC O43521; Q16548: BCL2A1; NbExp=4; IntAct=EBI-526406, EBI-1003550;
CC O43521; Q07817: BCL2L1; NbExp=8; IntAct=EBI-526406, EBI-78035;
CC O43521; Q07817-1: BCL2L1; NbExp=10; IntAct=EBI-526406, EBI-287195;
CC O43521; Q9HD36: BCL2L10; NbExp=10; IntAct=EBI-526406, EBI-2126349;
CC O43521; Q92843: BCL2L2; NbExp=9; IntAct=EBI-526406, EBI-707714;
CC O43521; Q86UW9: DTX2; NbExp=3; IntAct=EBI-526406, EBI-740376;
CC O43521; P43364-2: MAGEA11; NbExp=3; IntAct=EBI-526406, EBI-10178634;
CC O43521; Q07820: MCL1; NbExp=15; IntAct=EBI-526406, EBI-1003422;
CC O43521; Q13064: MKRN3; NbExp=3; IntAct=EBI-526406, EBI-2340269;
CC O43521; P07237: P4HB; NbExp=3; IntAct=EBI-526406, EBI-395883;
CC O43521; P40855: PEX19; NbExp=3; IntAct=EBI-526406, EBI-594747;
CC O43521; P63244: RACK1; NbExp=2; IntAct=EBI-526406, EBI-296739;
CC O43521; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-526406, EBI-947187;
CC O43521; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-526406, EBI-739895;
CC O43521; Q07813-1: Bax; Xeno; NbExp=7; IntAct=EBI-526406, EBI-15666406;
CC O43521; Q07440: Bcl2a1; Xeno; NbExp=2; IntAct=EBI-526406, EBI-707754;
CC O43521; P68451: F1L; Xeno; NbExp=4; IntAct=EBI-526406, EBI-7066119;
CC O43521; P97287: Mcl1; Xeno; NbExp=7; IntAct=EBI-526406, EBI-707292;
CC O43521; P03495: NS; Xeno; NbExp=2; IntAct=EBI-526406, EBI-2548993;
CC O43521-1; P10415: BCL2; NbExp=3; IntAct=EBI-526416, EBI-77694;
CC O43521-1; Q07817-1: BCL2L1; NbExp=2; IntAct=EBI-526416, EBI-287195;
CC O43521-1; Q9HD36: BCL2L10; NbExp=2; IntAct=EBI-526416, EBI-2126349;
CC O43521-2; P10415: BCL2; NbExp=4; IntAct=EBI-526420, EBI-77694;
CC O43521-2; P14174: MIF; NbExp=5; IntAct=EBI-526420, EBI-372712;
CC -!- SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}. Note=Associated with intracytoplasmic
CC membranes. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform BimEL]: Mitochondrion. Note=Translocates
CC from microtubules to mitochondria on loss of cell adherence.
CC -!- SUBCELLULAR LOCATION: [Isoform BimL]: Mitochondrion.
CC -!- SUBCELLULAR LOCATION: [Isoform BimS]: Mitochondrion.
CC -!- SUBCELLULAR LOCATION: [Isoform Bim-alpha1]: Mitochondrion.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=20;
CC Name=BimEL; Synonyms=Bim(EL);
CC IsoId=O43521-1; Sequence=Displayed;
CC Name=BimL; Synonyms=Bim(L);
CC IsoId=O43521-2; Sequence=VSP_000535;
CC Name=BimS; Synonyms=BCL2-like 11 transcript variant 9, Bim(S);
CC IsoId=O43521-3; Sequence=VSP_035608;
CC Name=Bim-alpha1; Synonyms=BimABCD, Bim-ABCD;
CC IsoId=O43521-4; Sequence=VSP_035620;
CC Name=Bim-alpha2; Synonyms=BimACD, Bim-ACD;
CC IsoId=O43521-5; Sequence=VSP_000535, VSP_035620;
CC Name=Bim-alpha3; Synonyms=BCL2-like 11 transcript variant 10, BimAD,
CC Bim-AD;
CC IsoId=O43521-6; Sequence=VSP_035608, VSP_035620;
CC Name=Bim-alpha4;
CC IsoId=O43521-7; Sequence=VSP_035608, VSP_035618;
CC Name=Bim-alpha5;
CC IsoId=O43521-8; Sequence=VSP_035619;
CC Name=Bim-alpha6;
CC IsoId=O43521-9; Sequence=VSP_035608, VSP_035619;
CC Name=Bim-beta1;
CC IsoId=O43521-10; Sequence=VSP_035615, VSP_035616;
CC Name=Bim-beta2;
CC IsoId=O43521-11; Sequence=VSP_035614, VSP_035616;
CC Name=Bim-beta3;
CC IsoId=O43521-12; Sequence=VSP_035609;
CC Name=Bim-beta4;
CC IsoId=O43521-13; Sequence=VSP_035610, VSP_035611;
CC Name=Bim-beta5;
CC IsoId=O43521-14; Sequence=VSP_035613, VSP_035617;
CC Name=Bim-beta6;
CC IsoId=O43521-15; Sequence=VSP_000535, VSP_035614, VSP_035616;
CC Name=Bim-beta7;
CC IsoId=O43521-16; Sequence=VSP_000535, VSP_035613, VSP_035617;
CC Name=Bim-gamma;
CC IsoId=O43521-17; Sequence=VSP_000535, VSP_035612;
CC Name=BimABC; Synonyms=Bim-ABC;
CC IsoId=O43521-18; Sequence=VSP_000535, VSP_042866;
CC Name=BimAC; Synonyms=Bim-AC;
CC IsoId=O43521-19; Sequence=VSP_042866;
CC Name=BimA; Synonyms=Bim-A;
CC IsoId=O43521-20; Sequence=VSP_042865;
CC -!- TISSUE SPECIFICITY: Isoform BimEL, isoform BimL and isoform BimS are
CC the predominant isoforms and are widely expressed with tissue-specific
CC variation. Isoform Bim-gamma is most abundantly expressed in small
CC intestine and colon, and in lower levels in spleen, prostate, testis,
CC heart, liver and kidney. {ECO:0000269|PubMed:12019181}.
CC -!- INDUCTION: By ER stress in a DDIT3/CHOP-dependent manner.
CC {ECO:0000269|PubMed:22761832}.
CC -!- DOMAIN: The BH3 motif is required for interaction with Bcl-2 proteins
CC and cytotoxicity. {ECO:0000250|UniProtKB:O54918}.
CC -!- PTM: Phosphorylation at Ser-69 by MAPK1/MAPK3 leads to interaction with
CC TRIM2 and polyubiquitination, followed by proteasomal degradation
CC (PubMed:15486195, PubMed:21478148). Deubiquitination catalyzed by
CC USP27X stabilizes the protein (By similarity).
CC {ECO:0000250|UniProtKB:O54918, ECO:0000269|PubMed:15486195,
CC ECO:0000269|PubMed:21478148}.
CC -!- PTM: Ubiquitination by TRIM2 following phosphorylation by MAPK1/MAPK3
CC leads to proteasomal degradation. Conversely, deubiquitination
CC catalyzed by USP27X stabilizes the protein.
CC {ECO:0000250|UniProtKB:O54918}.
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/BCL2L11ID772ch2q13.html";
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DR EMBL; AF032457; AAC39593.1; -; mRNA.
DR EMBL; AF032458; AAC39594.1; -; mRNA.
DR EMBL; AB071195; BAB78589.1; -; mRNA.
DR EMBL; AB071196; BAB78590.1; -; mRNA.
DR EMBL; AB071197; BAB78591.1; -; mRNA.
DR EMBL; AB071198; BAB78592.1; -; mRNA.
DR EMBL; AB071199; BAB78593.1; -; mRNA.
DR EMBL; AB071200; BAB78594.1; -; mRNA.
DR EMBL; AY352518; AAQ62569.1; -; mRNA.
DR EMBL; AY305714; AAQ82546.1; -; mRNA.
DR EMBL; AY305715; AAQ82547.1; -; mRNA.
DR EMBL; AY423441; AAQ99148.1; -; mRNA.
DR EMBL; AY423442; AAQ99149.1; -; mRNA.
DR EMBL; AY423443; AAQ99150.1; -; mRNA.
DR EMBL; AY428962; AAR06908.1; -; mRNA.
DR EMBL; DQ849200; ABI13589.1; -; mRNA.
DR EMBL; DQ849201; ABI13590.1; -; mRNA.
DR EMBL; DQ849202; ABI13591.1; -; mRNA.
DR EMBL; AK290377; BAF83066.1; -; mRNA.
DR EMBL; AK291269; BAF83958.1; -; mRNA.
DR EMBL; AC096670; AAY14797.1; -; Genomic_DNA.
DR EMBL; CH471237; EAW50365.1; -; Genomic_DNA.
DR EMBL; CH471237; EAW50367.1; -; Genomic_DNA.
DR EMBL; CH471237; EAW50369.1; -; Genomic_DNA.
DR EMBL; CH471237; EAW50370.1; -; Genomic_DNA.
DR EMBL; CH471237; EAW50371.1; -; Genomic_DNA.
DR EMBL; CH471237; EAW50372.1; -; Genomic_DNA.
DR EMBL; CH471237; EAW50373.1; -; Genomic_DNA.
DR EMBL; CH471237; EAW50374.1; -; Genomic_DNA.
DR EMBL; BC033694; AAH33694.1; -; mRNA.
DR CCDS; CCDS2089.1; -. [O43521-1]
DR CCDS; CCDS2092.1; -. [O43521-17]
DR CCDS; CCDS42731.1; -. [O43521-2]
DR CCDS; CCDS56131.1; -. [O43521-16]
DR CCDS; CCDS56132.1; -. [O43521-7]
DR CCDS; CCDS56133.1; -. [O43521-9]
DR CCDS; CCDS56134.1; -. [O43521-10]
DR CCDS; CCDS56135.1; -. [O43521-8]
DR CCDS; CCDS56136.1; -. [O43521-14]
DR CCDS; CCDS74560.1; -. [O43521-4]
DR CCDS; CCDS74561.1; -. [O43521-11]
DR RefSeq; NP_001191035.1; NM_001204106.1. [O43521-3]
DR RefSeq; NP_001191036.1; NM_001204107.1. [O43521-7]
DR RefSeq; NP_001191037.1; NM_001204108.1. [O43521-8]
DR RefSeq; NP_001191038.1; NM_001204109.1. [O43521-14]
DR RefSeq; NP_001191039.1; NM_001204110.1. [O43521-9]
DR RefSeq; NP_001191040.1; NM_001204111.1. [O43521-15]
DR RefSeq; NP_001191041.1; NM_001204112.1. [O43521-16]
DR RefSeq; NP_001191042.1; NM_001204113.1.
DR RefSeq; NP_006529.1; NM_006538.4. [O43521-2]
DR RefSeq; NP_619527.1; NM_138621.4. [O43521-1]
DR RefSeq; NP_619528.1; NM_138622.3. [O43521-4]
DR RefSeq; NP_619529.1; NM_138623.3. [O43521-5]
DR RefSeq; NP_619530.1; NM_138624.3. [O43521-10]
DR RefSeq; NP_619531.1; NM_138625.3.
DR RefSeq; NP_619532.1; NM_138626.3. [O43521-11]
DR RefSeq; NP_619533.1; NM_138627.3.
DR RefSeq; NP_996885.1; NM_207002.3. [O43521-17]
DR RefSeq; NP_996886.1; NM_207003.2. [O43521-6]
DR PDB; 1F95; NMR; -; C/D=108-116.
DR PDB; 2K7W; NMR; -; B=145-164.
DR PDB; 2NL9; X-ray; 1.55 A; B=141-166.
DR PDB; 2V6Q; X-ray; 2.70 A; B=141-166.
DR PDB; 2VM6; X-ray; 2.20 A; B=141-165.
DR PDB; 2WH6; X-ray; 1.50 A; B=141-166.
DR PDB; 2YQ6; X-ray; 1.80 A; B=147-164.
DR PDB; 2YQ7; X-ray; 1.90 A; B=147-164.
DR PDB; 3D7V; X-ray; 2.03 A; B=141-166.
DR PDB; 3FDL; X-ray; 1.78 A; B=141-166.
DR PDB; 3IO8; X-ray; 2.30 A; B/D=141-166.
DR PDB; 3IO9; X-ray; 2.40 A; B=141-166.
DR PDB; 3KJ0; X-ray; 1.70 A; B=143-165.
DR PDB; 3KJ1; X-ray; 1.94 A; B=143-163.
DR PDB; 3KJ2; X-ray; 2.35 A; B=143-163.
DR PDB; 4A1U; X-ray; 1.54 A; B=146-163.
DR PDB; 4A1W; X-ray; 2.50 A; P/Q/R/S=146-163.
DR PDB; 4B4S; X-ray; 1.90 A; B=141-166.
DR PDB; 4D2M; X-ray; 2.10 A; B/D=141-166.
DR PDB; 4QVF; X-ray; 1.53 A; B=141-166.
DR PDB; 4UF3; X-ray; 2.70 A; B=141-166.
DR PDB; 4YJ4; X-ray; 2.10 A; B=146-165.
DR PDB; 4ZIE; X-ray; 1.80 A; C=141-166.
DR PDB; 4ZIF; X-ray; 2.40 A; B=141-160.
DR PDB; 4ZIH; X-ray; 2.50 A; B=141-160.
DR PDB; 5AGW; X-ray; 2.69 A; C/D=146-166.
DR PDB; 5AGX; X-ray; 2.24 A; C/D=146-166.
DR PDB; 5C3G; X-ray; 2.45 A; B=146-166.
DR PDB; 5VWV; X-ray; 1.90 A; B=141-165.
DR PDB; 5VWW; X-ray; 2.80 A; C/D=141-166.
DR PDB; 5VWX; X-ray; 2.49 A; B/D=142-164.
DR PDB; 5VWY; X-ray; 1.55 A; B=141-166.
DR PDB; 5VWZ; X-ray; 1.62 A; B/D=141-166.
DR PDB; 5VX0; X-ray; 1.60 A; B/D=141-166.
DR PDB; 5VX2; X-ray; 1.85 A; B/D=141-166.
DR PDB; 5VX3; X-ray; 1.95 A; B/D/F/H=141-166.
DR PDB; 5WOS; X-ray; 2.45 A; B=141-166.
DR PDB; 6QFI; X-ray; 2.40 A; B=141-166.
DR PDB; 6RJP; X-ray; 2.57 A; C/D=147-163.
DR PDB; 6TQQ; X-ray; 3.00 A; B=141-166.
DR PDB; 6UA3; X-ray; 1.55 A; B=146-166.
DR PDB; 6UAB; X-ray; 2.10 A; B=146-166.
DR PDB; 6VBX; X-ray; 1.95 A; B=148-159.
DR PDB; 6X8O; X-ray; 1.31 A; A/B/C/D=141-166.
DR PDBsum; 1F95; -.
DR PDBsum; 2K7W; -.
DR PDBsum; 2NL9; -.
DR PDBsum; 2V6Q; -.
DR PDBsum; 2VM6; -.
DR PDBsum; 2WH6; -.
DR PDBsum; 2YQ6; -.
DR PDBsum; 2YQ7; -.
DR PDBsum; 3D7V; -.
DR PDBsum; 3FDL; -.
DR PDBsum; 3IO8; -.
DR PDBsum; 3IO9; -.
DR PDBsum; 3KJ0; -.
DR PDBsum; 3KJ1; -.
DR PDBsum; 3KJ2; -.
DR PDBsum; 4A1U; -.
DR PDBsum; 4A1W; -.
DR PDBsum; 4B4S; -.
DR PDBsum; 4D2M; -.
DR PDBsum; 4QVF; -.
DR PDBsum; 4UF3; -.
DR PDBsum; 4YJ4; -.
DR PDBsum; 4ZIE; -.
DR PDBsum; 4ZIF; -.
DR PDBsum; 4ZIH; -.
DR PDBsum; 5AGW; -.
DR PDBsum; 5AGX; -.
DR PDBsum; 5C3G; -.
DR PDBsum; 5VWV; -.
DR PDBsum; 5VWW; -.
DR PDBsum; 5VWX; -.
DR PDBsum; 5VWY; -.
DR PDBsum; 5VWZ; -.
DR PDBsum; 5VX0; -.
DR PDBsum; 5VX2; -.
DR PDBsum; 5VX3; -.
DR PDBsum; 5WOS; -.
DR PDBsum; 6QFI; -.
DR PDBsum; 6RJP; -.
DR PDBsum; 6TQQ; -.
DR PDBsum; 6UA3; -.
DR PDBsum; 6UAB; -.
DR PDBsum; 6VBX; -.
DR PDBsum; 6X8O; -.
DR AlphaFoldDB; O43521; -.
DR SMR; O43521; -.
DR BioGRID; 115335; 69.
DR ComplexPortal; CPX-1985; BIM:BCL-XL complex.
DR ComplexPortal; CPX-1990; BIM:BCL-2 complex.
DR ComplexPortal; CPX-481; MCL-1-BIM complex.
DR DIP; DIP-29185N; -.
DR ELM; O43521; -.
DR IntAct; O43521; 56.
DR MINT; O43521; -.
DR STRING; 9606.ENSP00000376943; -.
DR BindingDB; O43521; -.
DR ChEMBL; CHEMBL5777; -.
DR TCDB; 8.A.69.1.1; the pro-apoptotic bcl-2-family protein bim (bim) family.
DR iPTMnet; O43521; -.
DR PhosphoSitePlus; O43521; -.
DR BioMuta; BCL2L11; -.
DR EPD; O43521; -.
DR MassIVE; O43521; -.
DR MaxQB; O43521; -.
DR PaxDb; O43521; -.
DR PeptideAtlas; O43521; -.
DR PRIDE; O43521; -.
DR ProteomicsDB; 49009; -. [O43521-1]
DR ProteomicsDB; 49010; -. [O43521-10]
DR ProteomicsDB; 49011; -. [O43521-11]
DR ProteomicsDB; 49012; -. [O43521-12]
DR ProteomicsDB; 49013; -. [O43521-13]
DR ProteomicsDB; 49014; -. [O43521-14]
DR ProteomicsDB; 49015; -. [O43521-15]
DR ProteomicsDB; 49016; -. [O43521-16]
DR ProteomicsDB; 49017; -. [O43521-17]
DR ProteomicsDB; 49018; -. [O43521-18]
DR ProteomicsDB; 49019; -. [O43521-19]
DR ProteomicsDB; 49020; -. [O43521-2]
DR ProteomicsDB; 49021; -. [O43521-20]
DR ProteomicsDB; 49022; -. [O43521-3]
DR ProteomicsDB; 49023; -. [O43521-4]
DR ProteomicsDB; 49024; -. [O43521-5]
DR ProteomicsDB; 49025; -. [O43521-6]
DR ProteomicsDB; 49026; -. [O43521-7]
DR ProteomicsDB; 49027; -. [O43521-8]
DR ProteomicsDB; 49028; -. [O43521-9]
DR Antibodypedia; 3621; 1286 antibodies from 45 providers.
DR DNASU; 10018; -.
DR Ensembl; ENST00000308659.12; ENSP00000309226.8; ENSG00000153094.24. [O43521-2]
DR Ensembl; ENST00000337565.9; ENSP00000338374.5; ENSG00000153094.24. [O43521-17]
DR Ensembl; ENST00000393256.8; ENSP00000376943.2; ENSG00000153094.24. [O43521-1]
DR Ensembl; ENST00000405953.5; ENSP00000384641.1; ENSG00000153094.24. [O43521-17]
DR Ensembl; ENST00000415458.5; ENSP00000393781.1; ENSG00000153094.24. [O43521-16]
DR Ensembl; ENST00000431217.1; ENSP00000394640.1; ENSG00000153094.24. [O43521-10]
DR Ensembl; ENST00000433098.5; ENSP00000401662.1; ENSG00000153094.24. [O43521-5]
DR Ensembl; ENST00000436733.5; ENSP00000403727.1; ENSG00000153094.24. [O43521-14]
DR Ensembl; ENST00000437029.5; ENSP00000412892.1; ENSG00000153094.24. [O43521-8]
DR Ensembl; ENST00000439718.1; ENSP00000411137.1; ENSG00000153094.24. [O43521-7]
DR Ensembl; ENST00000452231.5; ENSP00000391292.1; ENSG00000153094.24. [O43521-9]
DR Ensembl; ENST00000610735.4; ENSP00000481030.1; ENSG00000153094.24. [O43521-14]
DR Ensembl; ENST00000615946.4; ENSP00000481423.1; ENSG00000153094.24. [O43521-7]
DR Ensembl; ENST00000619294.4; ENSP00000479714.1; ENSG00000153094.24. [O43521-10]
DR Ensembl; ENST00000620862.4; ENSP00000478133.1; ENSG00000153094.24. [O43521-5]
DR Ensembl; ENST00000621302.4; ENSP00000481652.1; ENSG00000153094.24. [O43521-4]
DR Ensembl; ENST00000622509.4; ENSP00000482175.1; ENSG00000153094.24. [O43521-8]
DR Ensembl; ENST00000622612.4; ENSP00000484360.1; ENSG00000153094.24. [O43521-11]
DR GeneID; 10018; -.
DR KEGG; hsa:10018; -.
DR MANE-Select; ENST00000393256.8; ENSP00000376943.2; NM_138621.5; NP_619527.1.
DR UCSC; uc002tgt.2; human. [O43521-1]
DR CTD; 10018; -.
DR DisGeNET; 10018; -.
DR GeneCards; BCL2L11; -.
DR HGNC; HGNC:994; BCL2L11.
DR HPA; ENSG00000153094; Low tissue specificity.
DR MIM; 603827; gene.
DR neXtProt; NX_O43521; -.
DR OpenTargets; ENSG00000153094; -.
DR PharmGKB; PA25305; -.
DR VEuPathDB; HostDB:ENSG00000153094; -.
DR eggNOG; ENOG502S0DF; Eukaryota.
DR GeneTree; ENSGT00390000003178; -.
DR HOGENOM; CLU_171932_0_0_1; -.
DR InParanoid; O43521; -.
DR OMA; EIWIARE; -.
DR OrthoDB; 1460067at2759; -.
DR PhylomeDB; O43521; -.
DR TreeFam; TF335898; -.
DR PathwayCommons; O43521; -.
DR Reactome; R-HSA-111446; Activation of BIM and translocation to mitochondria.
DR Reactome; R-HSA-111453; BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members.
DR Reactome; R-HSA-193648; NRAGE signals death through JNK.
DR Reactome; R-HSA-6802952; Signaling by BRAF and RAF1 fusions.
DR Reactome; R-HSA-8862803; Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease models.
DR Reactome; R-HSA-8952158; RUNX3 regulates BCL2L11 (BIM) transcription.
DR Reactome; R-HSA-9607240; FLT3 Signaling.
DR Reactome; R-HSA-9614657; FOXO-mediated transcription of cell death genes.
DR SignaLink; O43521; -.
DR SIGNOR; O43521; -.
DR BioGRID-ORCS; 10018; 21 hits in 1086 CRISPR screens.
DR ChiTaRS; BCL2L11; human.
DR EvolutionaryTrace; O43521; -.
DR GeneWiki; BCL2L11; -.
DR GenomeRNAi; 10018; -.
DR Pharos; O43521; Tchem.
DR PRO; PR:O43521; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; O43521; protein.
DR Bgee; ENSG00000153094; Expressed in sperm and 166 other tissues.
DR ExpressionAtlas; O43521; baseline and differential.
DR Genevisible; O43521; HS.
DR GO; GO:0097136; C:Bcl-2 family protein complex; IPI:ComplexPortal.
DR GO; GO:0097141; C:BIM-BCL-2 complex; IDA:UniProtKB.
DR GO; GO:0097140; C:BIM-BCL-xl complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0019898; C:extrinsic component of membrane; IEA:Ensembl.
DR GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; TAS:UniProtKB.
DR GO; GO:1902263; P:apoptotic process involved in embryonic digit morphogenesis; IEA:Ensembl.
DR GO; GO:0001782; P:B cell homeostasis; IEA:Ensembl.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0007160; P:cell-matrix adhesion; IEA:Ensembl.
DR GO; GO:1904646; P:cellular response to amyloid-beta; IEA:Ensembl.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; IEA:Ensembl.
DR GO; GO:0071385; P:cellular response to glucocorticoid stimulus; TAS:ARUK-UCL.
DR GO; GO:0048066; P:developmental pigmentation; IEA:Ensembl.
DR GO; GO:0043583; P:ear development; IEA:Ensembl.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; 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; IDA:MGI.
DR GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR GO; GO:0030879; P:mammary gland development; IEA:Ensembl.
DR GO; GO:0007127; P:meiosis I; IBA:GO_Central.
DR GO; GO:0002262; P:myeloid cell homeostasis; IEA:Ensembl.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0034263; P:positive regulation of autophagy in response to ER overload; IEA:Ensembl.
DR GO; GO:0045787; P:positive regulation of cell cycle; IEA:Ensembl.
DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
DR GO; GO:1902237; P:positive regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; TAS:ParkinsonsUK-UCL.
DR GO; GO:2000271; P:positive regulation of fibroblast apoptotic process; IDA:UniProtKB.
DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IMP:UniProtKB.
DR GO; GO:1903896; P:positive regulation of IRE1-mediated unfolded protein response; TAS:ParkinsonsUK-UCL.
DR GO; GO:1902110; P:positive regulation of mitochondrial membrane permeability involved in apoptotic process; IEA:Ensembl.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; IDA:BHF-UCL.
DR GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; IMP:UniProtKB.
DR GO; GO:0070234; P:positive regulation of T cell apoptotic process; IEA:Ensembl.
DR GO; GO:0048563; P:post-embryonic animal organ morphogenesis; IEA:Ensembl.
DR GO; GO:0042981; P:regulation of apoptotic process; IDA:ComplexPortal.
DR GO; GO:0048070; P:regulation of developmental pigmentation; IEA:Ensembl.
DR GO; GO:0046620; P:regulation of organ growth; IEA:Ensembl.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IDA:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR GO; GO:0048536; P:spleen development; IEA:Ensembl.
DR GO; GO:0043029; P:T cell homeostasis; IEA:Ensembl.
DR GO; GO:0070242; P:thymocyte apoptotic process; IEA:Ensembl.
DR GO; GO:0048538; P:thymus development; IEA:Ensembl.
DR GO; GO:0035148; P:tube formation; IEA:Ensembl.
DR InterPro; IPR014771; Apoptosis_Bim_N.
DR InterPro; IPR017288; Bcl-2-like_11.
DR InterPro; IPR015040; Bcl-x_interacting_BH3_dom.
DR Pfam; PF08945; Bclx_interact; 1.
DR Pfam; PF06773; Bim_N; 1.
DR PIRSF; PIRSF037827; Bcl-2-like_p11; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Apoptosis; Membrane; Mitochondrion;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..198
FT /note="Bcl-2-like protein 11"
FT /id="PRO_0000143109"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 148..162
FT /note="BH3"
FT MOD_RES 69
FT /note="Phosphoserine; by MAPK"
FT /evidence="ECO:0000269|PubMed:15486195"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88498"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88498"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 42..166
FT /note="Missing (in isoform BimA)"
FT /evidence="ECO:0000303|PubMed:11997495"
FT /id="VSP_042865"
FT VAR_SEQ 42..131
FT /note="Missing (in isoform BimS, isoform Bim-alpha3,
FT isoform Bim-alpha6 and isoform Bim-alpha4)"
FT /evidence="ECO:0000303|PubMed:11997495,
FT ECO:0000303|PubMed:15147734, ECO:0000303|PubMed:17503221"
FT /id="VSP_035608"
FT VAR_SEQ 42..101
FT /note="Missing (in isoform BimABC, isoform BimL, isoform
FT Bim-alpha2, isoform Bim-gamma, isoform Bim-beta6 and
FT isoform Bim-beta7)"
FT /evidence="ECO:0000303|PubMed:11734221,
FT ECO:0000303|PubMed:11997495, ECO:0000303|PubMed:12019181,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:17503221,
FT ECO:0000303|PubMed:9430630"
FT /id="VSP_000535"
FT VAR_SEQ 42..75
FT /note="GNPEGNHGGEGDSCPHGSPQGPLAPPASPGPFAT -> VSLCHPGWSALVRS
FT WLTATSNSQVQAVLLPQPPK (in isoform Bim-beta3)"
FT /evidence="ECO:0000303|PubMed:11734221"
FT /id="VSP_035609"
FT VAR_SEQ 43..44
FT /note="NP -> IF (in isoform Bim-beta4)"
FT /evidence="ECO:0000303|PubMed:11734221"
FT /id="VSP_035610"
FT VAR_SEQ 45..198
FT /note="Missing (in isoform Bim-beta4)"
FT /evidence="ECO:0000303|PubMed:11734221"
FT /id="VSP_035611"
FT VAR_SEQ 132..198
FT /note="ASMRQAEPADMRPEIWIAQELRRIGDEFNAYYARRVFLNNYQAAEDHPRMVI
FT LRLLRYIVRLVWRMH -> VVILEDIGDLSLCFGFIFTGLDLYGHHHSQDTEQLNHKDF
FT S (in isoform Bim-gamma)"
FT /evidence="ECO:0000303|PubMed:12019181"
FT /id="VSP_035612"
FT VAR_SEQ 132..166
FT /note="Missing (in isoform BimAC and isoform BimABC)"
FT /evidence="ECO:0000303|PubMed:11997495"
FT /id="VSP_042866"
FT VAR_SEQ 132..140
FT /note="ASMRQAEPA -> VREIEEVVV (in isoform Bim-beta5 and
FT isoform Bim-beta7)"
FT /evidence="ECO:0000303|PubMed:17503221"
FT /id="VSP_035613"
FT VAR_SEQ 132..135
FT /note="ASMR -> GIFE (in isoform Bim-beta2 and isoform Bim-
FT beta6)"
FT /evidence="ECO:0000303|PubMed:11734221,
FT ECO:0000303|PubMed:17503221"
FT /id="VSP_035614"
FT VAR_SEQ 133..135
FT /note="SMR -> NWD (in isoform Bim-beta1)"
FT /evidence="ECO:0000303|PubMed:11734221"
FT /id="VSP_035615"
FT VAR_SEQ 136..198
FT /note="Missing (in isoform Bim-beta1, isoform Bim-beta2 and
FT isoform Bim-beta6)"
FT /evidence="ECO:0000303|PubMed:11734221,
FT ECO:0000303|PubMed:17503221"
FT /id="VSP_035616"
FT VAR_SEQ 141..198
FT /note="Missing (in isoform Bim-beta5 and isoform Bim-
FT beta7)"
FT /evidence="ECO:0000303|PubMed:17503221"
FT /id="VSP_035617"
FT VAR_SEQ 167..198
FT /note="VFLNNYQAAEDHPRMVILRLLRYIVRLVWRMH -> LEK (in isoform
FT Bim-alpha1, isoform Bim-alpha2 and isoform Bim-alpha3)"
FT /evidence="ECO:0000303|PubMed:11734221,
FT ECO:0000303|PubMed:11997495, ECO:0000303|PubMed:15147734,
FT ECO:0000303|PubMed:17503221"
FT /id="VSP_035620"
FT VAR_SEQ 167..198
FT /note="VFLNNYQAAEDHPRMVILRLLRYIVRLVWRMH -> LAKLLASST (in
FT isoform Bim-alpha4)"
FT /evidence="ECO:0000303|PubMed:17503221"
FT /id="VSP_035618"
FT VAR_SEQ 167..198
FT /note="VFLNNYQAAEDHPRMVILRLLRYIVRLVWRMH -> MPLPPD (in
FT isoform Bim-alpha5 and isoform Bim-alpha6)"
FT /evidence="ECO:0000303|PubMed:17503221"
FT /id="VSP_035619"
FT MUTAGEN 156
FT /note="G->A: Retains the ability to induce apoptosis.
FT Abolishes interaction with BAX; in isoform Bim-alpha3 and
FT isoform BimS. No effect on interaction with BCL2."
FT /evidence="ECO:0000269|PubMed:11997495,
FT ECO:0000269|PubMed:17289999"
FT MUTAGEN 156
FT /note="G->E: Abolishes induction of apoptosis. Abolishes
FT interaction with BAX and BCL2; in isoform Bim-alpha3 and
FT isoform BimS. Loses the ability to induce the
FT conformationally active form of BAX."
FT /evidence="ECO:0000269|PubMed:11997495,
FT ECO:0000269|PubMed:17289999"
FT MUTAGEN 160
FT /note="N->A: Retains the ability to induce apoptosis.
FT Abolishes interaction with BCL2; in isoform Bim-alpha3 and
FT isoform BimS. No effect on interaction with BAX."
FT /evidence="ECO:0000269|PubMed:11997495"
FT CONFLICT 33
FT /note="P -> L (in Ref. 7; BAF83066)"
FT /evidence="ECO:0000305"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:1F95"
FT HELIX 144..165
FT /evidence="ECO:0007829|PDB:6X8O"
SQ SEQUENCE 198 AA; 22171 MW; D75735E469CA6997 CRC64;
MAKQPSDVSS ECDREGRQLQ PAERPPQLRP GAPTSLQTEP QGNPEGNHGG EGDSCPHGSP
QGPLAPPASP GPFATRSPLF IFMRRSSLLS RSSSGYFSFD TDRSPAPMSC DKSTQTPSPP
CQAFNHYLSA MASMRQAEPA DMRPEIWIAQ ELRRIGDEFN AYYARRVFLN NYQAAEDHPR
MVILRLLRYI VRLVWRMH
