ID BIM_HUMAN Reviewed; 198 AA. AC O43521; O43522; DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 22-JUL-2008, entry version 69. DE RecName: Full=Bcl-2-like protein 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 [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 [3] 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). CC -!- FUNCTION: Induces apoptosis. Isoform BimL is more potent than CC isoform BimEL. CC -!- SUBUNIT: Forms heterodimers with a number of antiapoptotic Bcl-2 CC proteins including Mcl-1, Bcl-2, Bcl-X(L), BFL-1, and BHRF1. Does CC not heterodimerize with proapoptotic proteins such as BAD, BOK, CC BAX or BAK (By similarity). CC -!- INTERACTION: CC P31749:AKT1; NbExp=1; IntAct=EBI-526416, EBI-296087; CC P10415:BCL2; NbExp=1; IntAct=EBI-526406, EBI-77694; CC P10415:BCL2; NbExp=2; IntAct=EBI-526420, EBI-77694; CC P10415:BCL2; NbExp=1; IntAct=EBI-526416, EBI-77694; CC Q07440:Bcl2a1 (xeno); NbExp=1; IntAct=EBI-526406, EBI-707754; 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=1; IntAct=EBI-526406, EBI-707714; CC Q9NP97:DYNLRB1; NbExp=1; IntAct=EBI-526406, EBI-372128; CC P63085:Mapk1 (xeno); NbExp=1; IntAct=EBI-526416, EBI-397697; CC P97287:Mcl1 (xeno); NbExp=3; IntAct=EBI-526406, EBI-707292; CC P31946:YWHAB; NbExp=1; IntAct=EBI-526406, EBI-359815; CC -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein. CC Note=Associated with intracytoplasmic membranes (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=BimEL; CC IsoId=O43521-1; Sequence=Displayed; CC Name=BimL; CC IsoId=O43521-2; Sequence=VSP_000535; CC -!- DOMAIN: The BH3 motif is required for Bcl-2 binding and CC cytotoxicity. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF032457; AAC39593.1; -; mRNA. DR EMBL; AF032458; AAC39594.1; -; mRNA. DR EMBL; BC033694; AAH33694.1; -; mRNA. DR RefSeq; NP_006529.1; -. DR RefSeq; NP_619527.1; -. DR UniGene; Hs.469658; -. DR PDB; 2NL9; X-ray; 1.55 A; B=141-166. DR PDB; 2VM6; X-ray; 2.20 A; B=141-165. DR PDBsum; 2NL9; -. DR PDBsum; 2VM6; -. DR DIP; DIP:29185N; -. DR IntAct; O43521; -. DR PhosphoSite; O43521; -. DR Ensembl; ENSG00000153094; Homo sapiens. DR GeneID; 10018; -. DR KEGG; hsa:10018; -. DR HGNC; HGNC:994; BCL2L11. DR HPA; CAB002616; -. DR MIM; 603827; gene. DR PharmGKB; PA25305; -. DR HOGENOM; O43521; -. DR HOVERGEN; O43521; -. DR Reactome; REACT_578; Apoptosis. DR LinkHub; O43521; -. DR ArrayExpress; O43521; -. DR CleanEx; HS_BCL2L11; -. DR GermOnline; ENSG00000153094; Homo sapiens. DR GO; GO:0005829; C:cytosol; EXP:Reactome. DR GO; GO:0005624; C:membrane fraction; TAS:ProtInc. 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:IntAct. DR GO; GO:0008633; P:activation of pro-apoptotic gene products; EXP:Reactome. DR GO; GO:0006917; P:induction of apoptosis; TAS:UniProtKB. DR InterPro; IPR017288; Apoptosis_Bcl-2-like_11. DR InterPro; IPR014771; Apoptosis_Bim_N. DR InterPro; IPR000712; Bcl2_BH. DR InterPro; IPR015040; Bclx_interact. 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; Membrane; KW 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 VAR_SEQ 42 101 Missing (in isoform BimL). FT /FTId=VSP_000535. 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 //