ID B2L11_HUMAN Reviewed; 198 AA. AC O43521; A8K2W2; O43522; Q0MSE7; Q0MSE8; Q0MSE9; Q53R28; Q6JTU6; AC Q6T851; Q6TE14; Q6TE15; Q6TE16; Q6V402; Q8WYL6; Q8WYL7; Q8WYL8; AC Q8WYL9; Q8WYM0; Q8WYM1; DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 19-JAN-2010, entry version 90. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BIMEL AND BIML), AND FUNCTION. RC TISSUE=Peripheral blood, and Spleen; RX MEDLINE=98094360; PubMed=9430630; DOI=10.1093/emboj/17.2.384; RA O'Connor L., Strasser A., O'Reilly L.A., Hausmann G., Adams J.M., RA Cory S., 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; RP BIM-BETA1; BIM-BETA2; BIM-BETA3 AND BIM-BETA4), FUNCTION (ISOFORMS RP BIM-ALPHA1 AND BIM-ALPHA2), AND SUBCELLULAR LOCATION. RX MEDLINE=21592301; 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 RT Bim, 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 MEDLINE=22013778; 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 RT BH3-only splice variant of Bim."; RL Cancer Res. 62:2976-2981(2002). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BIMS AND BIM-ALPHA3), AND RP FUNCTION (ISOFORM BIM-ALPHA3). RX PubMed=15147734; 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 RT in cell apoptosis."; RL Int. J. Biochem. Cell Biol. 36:1554-1561(2004). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BIM-ALPHA3; BIM-ALPHA4; RP BIM-ALPHA5; 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., RA Chak E.C., 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 [6] 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [7] 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., RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., RA 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., RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., RA 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., RA Waterston R.H., Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 RT and 4."; RL Nature 434:724-731(2005). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [9] 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77, AND MASS RP SPECTROMETRY. RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., RA Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for RT efficient phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77, AND MASS RP SPECTROMETRY. RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of RT the kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [12] RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 141-166 IN COMPLEX WITH RP 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 [13] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 141-165 IN COMPLEX WITH RP BCL2A1. RG Structural genomics consortium (SGC); RT "Human BCL-2A1 in complex with BIM."; RL Submitted (FEB-2008) to the PDB data bank. CC -!- FUNCTION: Induces apoptosis. Isoform BimL is more potent than CC isoform BimEL. Isoform Bim-alpha1, isoform Bim-alpha2 and isoform CC Bim-alpha3 induce apoptosis, although less potent than the CC isoforms BimEL, BimL and BimS. Isoform Bim-gamma induces CC apoptosis. CC -!- SUBUNIT: Forms heterodimers with a number of antiapoptotic Bcl-2 CC proteins including MCL1, BCL2, BCL2L1 isoform Bcl-X(L), CC BCL2A1/BFL-1, and BHRF1. Does not heterodimerize with proapoptotic CC proteins such as BAD, BOK, BAX or BAK (By similarity). CC -!- INTERACTION: CC P31749:AKT1; NbExp=1; IntAct=EBI-526416, EBI-296087; CC P10415:BCL2; NbExp=2; IntAct=EBI-526406, EBI-77694; CC P10415:BCL2; NbExp=1; IntAct=EBI-526416, EBI-77694; CC P10415:BCL2; NbExp=2; IntAct=EBI-526420, EBI-77694; CC Q16548:BCL2A1; NbExp=1; IntAct=EBI-526406, EBI-1003550; CC Q07440:Bcl2a1 (xeno); NbExp=1; IntAct=EBI-526406, EBI-707754; CC Q07817:BCL2L1; NbExp=1; IntAct=EBI-526406, EBI-78035; CC Q07817-1:BCL2L1; NbExp=4; IntAct=EBI-526406, EBI-287195; CC Q07817-1:BCL2L1; NbExp=1; IntAct=EBI-526416, EBI-287195; CC Q92843:BCL2L2; NbExp=2; IntAct=EBI-526406, EBI-707714; CC Q9NP97:DYNLRB1; NbExp=1; IntAct=EBI-526406, EBI-372128; CC P63244:GNB2L1; NbExp=2; IntAct=EBI-526406, EBI-296739; CC P63085:Mapk1 (xeno); NbExp=1; IntAct=EBI-526416, EBI-397697; CC Q07820:MCL1; NbExp=1; IntAct=EBI-526406, EBI-1003422; CC P97287:Mcl1 (xeno); NbExp=3; IntAct=EBI-526406, EBI-707292; CC P14174:MIF; NbExp=1; IntAct=EBI-2123748, EBI-372712; CC P14174:MIF; NbExp=1; IntAct=EBI-526416, EBI-372712; CC P14174:MIF; NbExp=5; IntAct=EBI-526420, EBI-372712; CC P31946:YWHAB; NbExp=1; IntAct=EBI-526406, EBI-359815; CC -!- SUBCELLULAR LOCATION: Endomembrane system; Peripheral membrane CC protein (By similarity). Note=Associated with intracytoplasmic CC membranes (By similarity). CC -!- SUBCELLULAR LOCATION: Isoform BimEL: Mitochondrion. 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=17; 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; CC IsoId=O43521-4; Sequence=VSP_035620; CC Name=Bim-alpha2; CC IsoId=O43521-5; Sequence=VSP_000535, VSP_035620; CC Name=Bim-alpha3; Synonyms=BCL2-like 11 transcript variant 10; 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 -!- TISSUE SPECIFICITY: Isoform BimEL, isoform BimL and isoform BimS CC are the predominant isoforms and are ubiquitously expressed with a CC tissue-specific variation. Isoform Bim-gamma is most abundantly CC expressed in small intestine and colon, and in lower levels in CC spleen, prostate, testis, heart, liver and kidney. CC -!- DOMAIN: The BH3 motif is required for Bcl-2 binding and CC cytotoxicity. CC -!- SIMILARITY: Belongs to the Bcl-2 family. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology CC and Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/BCL2L11ID772ch2q13.html"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 IPI; IPI00012853; -. DR IPI; IPI00103743; -. DR IPI; IPI00216585; -. DR IPI; IPI00410159; -. DR IPI; IPI00428840; -. DR IPI; IPI00451139; -. DR IPI; IPI00514401; -. DR IPI; IPI00873921; -. DR IPI; IPI00878323; -. DR IPI; IPI00914559; -. DR IPI; IPI00914560; -. DR IPI; IPI00914563; -. DR IPI; IPI00914586; -. DR IPI; IPI00914592; -. DR IPI; IPI00914600; -. DR IPI; IPI00914670; -. DR IPI; IPI00914677; -. DR RefSeq; NP_006529.1; -. DR RefSeq; NP_619527.1; -. DR RefSeq; NP_996885.1; -. DR UniGene; Hs.469658; -. 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; 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 PDBsum; 2K7W; -. DR PDBsum; 2NL9; -. DR PDBsum; 2V6Q; -. DR PDBsum; 2VM6; -. DR PDBsum; 3D7V; -. DR PDBsum; 3FDL; -. DR PDBsum; 3IO8; -. DR PDBsum; 3IO9; -. DR DIP; DIP-29185N; -. DR IntAct; O43521; 24. DR STRING; O43521; -. DR PhosphoSite; O43521; -. DR PRIDE; O43521; -. DR Ensembl; ENST00000357682; ENSP00000350311; ENSG00000153094; Homo sapiens. DR Ensembl; ENST00000393256; ENSP00000376943; ENSG00000153094; Homo sapiens. DR GeneID; 10018; -. DR KEGG; hsa:10018; -. DR UCSC; uc002tgu.1; human. DR UCSC; uc002tgv.1; human. DR CTD; 10018; -. DR GeneCards; GC02P111597; -. DR HGNC; HGNC:994; BCL2L11. DR MIM; 603827; gene. DR PharmGKB; PA25305; -. DR eggNOG; prNOG19086; -. DR HOVERGEN; O43521; -. DR InParanoid; O43521; -. DR OMA; FNAYYPR; -. DR PhylomeDB; O43521; -. DR Pathway_Interaction_DB; foxopathway; FoxO family signaling. DR Pathway_Interaction_DB; p75ntrpathway; p75(NTR)-mediated signaling. DR Reactome; REACT_11061; Signalling by NGF. DR Reactome; REACT_578; Apoptosis. DR NextBio; 37849; -. DR PMAP-CutDB; O43521; -. DR ArrayExpress; O43521; -. DR Bgee; O43521; -. DR Genevestigator; O43521; -. DR GermOnline; ENSG00000153094; Homo sapiens. DR GO; GO:0005829; C:cytosol; EXP:Reactome. DR GO; GO:0019898; C:extrinsic to membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005741; C:mitochondrial outer membrane; EXP:Reactome. DR GO; GO:0005886; C:plasma membrane; EXP:Reactome. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0008633; P:activation of pro-apoptotic gene products; EXP:Reactome. DR GO; GO:0008624; P:induction of apoptosis by extracellular sig...; EXP:Reactome. DR InterPro; IPR017288; Apoptosis_Bcl-2-like_11. DR InterPro; IPR014771; Apoptosis_Bim_N. DR InterPro; IPR015040; Bcl-x_interacting. DR Pfam; PF08945; Bclx_interact; 1. DR Pfam; PF06773; Bim_N; 1. DR PIRSF; PIRSF037827; Bcl-2-like_p11; 1. DR PROSITE; PS01259; BH3; FALSE_NEG. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Apoptosis; Complete proteome; KW Membrane; Mitochondrion; Phosphoprotein. FT CHAIN 1 198 Bcl-2-like protein 11. FT /FTId=PRO_0000143109. FT MOTIF 148 162 BH3. FT MOD_RES 77 77 Phosphoserine. FT MOD_RES 87 87 Phosphoserine (By similarity). FT VAR_SEQ 42 131 Missing (in isoform BimS, isoform Bim- FT alpha3, isoform Bim-alpha6 and isoform FT Bim-alpha4). FT /FTId=VSP_035608. FT VAR_SEQ 42 101 Missing (in isoform BimL, isoform Bim- FT alpha2, isoform Bim-gamma, isoform Bim- FT beta6 and isoform Bim-beta7). FT /FTId=VSP_000535. FT VAR_SEQ 42 75 GNPEGNHGGEGDSCPHGSPQGPLAPPASPGPFAT -> VSL FT CHPGWSALVRSWLTATSNSQVQAVLLPQPPK (in FT isoform Bim-beta3). FT /FTId=VSP_035609. FT VAR_SEQ 43 44 NP -> IF (in isoform Bim-beta4). FT /FTId=VSP_035610. FT VAR_SEQ 45 198 Missing (in isoform Bim-beta4). FT /FTId=VSP_035611. FT VAR_SEQ 132 198 ASMRQAEPADMRPEIWIAQELRRIGDEFNAYYARRVFLNNY FT QAAEDHPRMVILRLLRYIVRLVWRMH -> VVILEDIGDLS FT LCFGFIFTGLDLYGHHHSQDTEQLNHKDFS (in FT isoform Bim-gamma). FT /FTId=VSP_035612. FT VAR_SEQ 132 140 ASMRQAEPA -> VREIEEVVV (in isoform Bim- FT beta5 and isoform Bim-beta7). FT /FTId=VSP_035613. FT VAR_SEQ 132 135 ASMR -> GIFE (in isoform Bim-beta2 and FT isoform Bim-beta6). FT /FTId=VSP_035614. FT VAR_SEQ 133 135 SMR -> NWD (in isoform Bim-beta1). FT /FTId=VSP_035615. FT VAR_SEQ 136 198 Missing (in isoform Bim-beta1, isoform FT Bim-beta2 and isoform Bim-beta6). FT /FTId=VSP_035616. FT VAR_SEQ 141 198 Missing (in isoform Bim-beta5 and isoform FT Bim-beta7). FT /FTId=VSP_035617. FT VAR_SEQ 167 198 VFLNNYQAAEDHPRMVILRLLRYIVRLVWRMH -> LEK FT (in isoform Bim-alpha1, isoform Bim- FT alpha2 and isoform Bim-alpha3). FT /FTId=VSP_035620. FT VAR_SEQ 167 198 VFLNNYQAAEDHPRMVILRLLRYIVRLVWRMH -> LAKLL FT ASST (in isoform Bim-alpha4). FT /FTId=VSP_035618. FT VAR_SEQ 167 198 VFLNNYQAAEDHPRMVILRLLRYIVRLVWRMH -> MPLPP FT D (in isoform Bim-alpha5 and isoform Bim- FT alpha6). FT /FTId=VSP_035619. FT CONFLICT 33 33 P -> L (in Ref. 6; BAF83066). FT HELIX 144 164 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 //