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Bcl-2-like protein 11 (Bcl2-L-11) (Bcl2-interacting mediator of cell death)

 B2L11_MOUSE             Reviewed;         196 AA.
O54918; A2ALQ6; O54919; O54920;
18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
28-MAR-2018, entry version 167.
RecName: Full=Bcl-2-like protein 11;
Short=Bcl2-L-11;
AltName: Full=Bcl2-interacting mediator of cell death;
Name=Bcl2l11; Synonyms=Bim;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND ALTERNATIVE SPLICING.
PubMed=9430630; DOI=10.1093/emboj/17.2.384;
O'Connor L., Strasser A., O'Reilly L.A., Hausmann G., Adams J.M.,
Cory S., Huang D.C.S.;
"Bim: a novel member of the Bcl-2 family that promotes apoptosis.";
EMBO J. 17:384-395(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BIMEL).
STRAIN=FVB/N; TISSUE=Mammary tumor;
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).
[4]
INTERACTION WITH MCL1.
PubMed=16543145; DOI=10.1016/j.molcel.2006.02.009;
Maurer U., Charvet C., Wagman A.S., Dejardin E., Green D.R.;
"Glycogen synthase kinase-3 regulates mitochondrial outer membrane
permeabilization and apoptosis by destabilization of MCL-1.";
Mol. Cell 21:749-760(2006).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Lung, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[6]
INDUCTION.
PubMed=21159964; DOI=10.1523/JNEUROSCI.1598-10.2010;
Galehdar Z., Swan P., Fuerth B., Callaghan S.M., Park D.S.,
Cregan S.P.;
"Neuronal apoptosis induced by endoplasmic reticulum stress is
regulated by ATF4-CHOP-mediated induction of the Bcl-2 homology 3-only
member PUMA.";
J. Neurosci. 30:16938-16948(2010).
[7]
INTERACTION WITH DYNLL1; TRIM2 AND YWHAZ, UBIQUITINATION,
PHOSPHORYLATION AT SER-65, AND MUTAGENESIS OF SER-55; SER-65 AND
SER-73.
PubMed=21478148; DOI=10.1074/jbc.M110.197707;
Thompson S., Pearson A.N., Ashley M.D., Jessick V., Murphy B.M.,
Gafken P., Henshall D.C., Morris K.T., Simon R.P., Meller R.;
"Identification of a novel Bcl-2-interacting mediator of cell death
(Bim) E3 ligase, tripartite motif-containing protein 2 (TRIM2), and
its role in rapid ischemic tolerance-induced neuroprotection.";
J. Biol. Chem. 286:19331-19339(2011).
[8]
INTERACTION WITH BCL2L1; MCL1 AND USP27X, PHOSPHORYLATION AT SER-65,
UBIQUITINATION, DEUBIQUITINATION BY USP27X, AND MUTAGENESIS OF LEU-150
AND ILE-153.
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).
[9]
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 139-171 IN COMPLEX WITH
BCL2L1 ISOFORM BCL-XL, IDENTIFICATION IN A COMPLEX WITH DYNLL1 AND
BCL-XL, AND INTERACTION WITH BAX.
PubMed=14499110; DOI=10.1016/S1074-7613(03)00234-6;
Liu X., Dai S., Zhu Y., Marrack P., Kappler J.W.;
"The structure of a Bcl-xL/Bim fragment complex: implications for Bim
function.";
Immunity 19:341-352(2003).
-!- FUNCTION: Induces apoptosis and anoikis. The isoforms vary in
cytotoxicity with isoform BimS being the most potent and isoform
BimEL being the least potent. {ECO:0000269|PubMed:9430630}.
-!- SUBUNIT: Forms heterodimers with a number of antiapoptotic Bcl-2
proteins, including MCL1, BCL2, BCL2L1 isoform Bcl-X(L),
BCL2A1/BFL-1, and BCL2L2/BCLW (PubMed:16543145, PubMed:27013495,
PubMed:14499110). Interacts with BAX (in vitro); this interaction
may induce the conformationally active form of BAX
(PubMed:14499110). Does not heterodimerize with proapoptotic
proteins such as BAD, BOK or BAK. Identified in a complex
containing BCL2L11, DYNLL1 and BCL2L1 isoform Bcl-X(L); BH3
integrity is required for BCL2L1-binding (PubMed:21478148,
PubMed:27013495, PubMed:14499110). Interacts with YWHAZ. When
phosphorylated, interacts with TRIM2; this interaction is
associated with ubiquitination and degradation (PubMed:21478148).
Interacts (via BH3) with MCL1; this interaction may sequester
BCL2L11 and prevent its pro-apoptotic activity (PubMed:16543145,
PubMed:27013495). When phosphorylated, isoform BimEL interacts
with USP27X; this interaction leads to BCL2L11 deubiquitination
and stabilization (PubMed:27013495). {ECO:0000269|PubMed:14499110,
ECO:0000269|PubMed:16543145, ECO:0000269|PubMed:21478148,
ECO:0000269|PubMed:27013495}.
-!- INTERACTION:
P10417:Bcl2; NbExp=2; IntAct=EBI-526076, EBI-526314;
Q07817-1:BCL2L1 (xeno); NbExp=3; IntAct=EBI-526084, EBI-287195;
Q92843:BCL2L2 (xeno); NbExp=2; IntAct=EBI-526067, EBI-707714;
P03182:BHRF1 (xeno); NbExp=3; IntAct=EBI-526067, EBI-1207659;
Q9NP97:DYNLRB1 (xeno); NbExp=3; IntAct=EBI-526080, EBI-372128;
P97287:Mcl1; NbExp=4; IntAct=EBI-526067, EBI-707292;
Q9DBC7:Prkar1a; NbExp=2; IntAct=EBI-526076, EBI-645677;
P63244:RACK1 (xeno); NbExp=2; IntAct=EBI-526076, EBI-296739;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:9430630};
Peripheral membrane protein {ECO:0000269|PubMed:9430630}.
Mitochondrion {ECO:0000250}. Note=Associated with intracytoplasmic
membranes.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=BimEL;
IsoId=O54918-1; Sequence=Displayed;
Name=BimL;
IsoId=O54918-2; Sequence=VSP_000536;
Name=BimS;
IsoId=O54918-3; Sequence=VSP_000537;
-!- TISSUE SPECIFICITY: Expressed in a number of B- and T-lymphoid
cell lines. {ECO:0000269|PubMed:9430630}.
-!- INDUCTION: By ER stress. {ECO:0000269|PubMed:21159964}.
-!- DOMAIN: The BH3 motif is required for the interaction with Bcl-2
proteins and cytotoxicity. {ECO:0000269|PubMed:14499110,
ECO:0000269|PubMed:27013495}.
-!- PTM: Phosphorylation at Ser-65 by MAPK1/MAPK3 leads interaction
with TRIM2 and ubiquitination, followed by proteasomal degradation
(PubMed:21478148). Deubiquitination catalyzed by USP27X stabilizes
the protein (PubMed:27013495). {ECO:0000269|PubMed:21478148,
ECO:0000269|PubMed:27013495}.
-!- PTM: Ubiquitination by TRIM2 following phosphorylation by
MAPK1/MAPK3 leads to proteasomal degradation. Conversely,
deubiquitination catalyzed by USP27X stabilizes the protein.
{ECO:0000269|PubMed:21478148, ECO:0000269|PubMed:27013495}.
-!- SIMILARITY: Belongs to the Bcl-2 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF032459; AAC40029.1; -; mRNA.
EMBL; AF032460; AAC40030.1; -; mRNA.
EMBL; AF032461; AAC40031.1; -; mRNA.
EMBL; AL805950; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC019556; AAH19556.1; -; mRNA.
CCDS; CCDS16712.1; -. [O54918-3]
CCDS; CCDS16713.1; -. [O54918-1]
CCDS; CCDS16714.1; -. [O54918-2]
RefSeq; NP_033884.1; NM_009754.3. [O54918-3]
RefSeq; NP_997563.1; NM_207680.2. [O54918-1]
RefSeq; NP_997564.1; NM_207681.2. [O54918-2]
UniGene; Mm.141083; -.
UniGene; Mm.453214; -.
PDB; 1PQ1; X-ray; 1.65 A; B=139-171.
PDBsum; 1PQ1; -.
DisProt; DP00518; -.
ProteinModelPortal; O54918; -.
SMR; O54918; -.
BioGrid; 198352; 14.
DIP; DIP-29214N; -.
ELM; O54918; -.
IntAct; O54918; 18.
MINT; O54918; -.
STRING; 10090.ENSMUSP00000105970; -.
iPTMnet; O54918; -.
PhosphoSitePlus; O54918; -.
PaxDb; O54918; -.
PeptideAtlas; O54918; -.
PRIDE; O54918; -.
Ensembl; ENSMUST00000019281; ENSMUSP00000019281; ENSMUSG00000027381. [O54918-3]
Ensembl; ENSMUST00000103210; ENSMUSP00000099499; ENSMUSG00000027381. [O54918-2]
Ensembl; ENSMUST00000103211; ENSMUSP00000099500; ENSMUSG00000027381. [O54918-3]
Ensembl; ENSMUST00000110341; ENSMUSP00000105970; ENSMUSG00000027381. [O54918-1]
GeneID; 12125; -.
KEGG; mmu:12125; -.
UCSC; uc008mgh.1; mouse. [O54918-1]
UCSC; uc008mgk.1; mouse. [O54918-2]
CTD; 10018; -.
MGI; MGI:1197519; Bcl2l11.
eggNOG; ENOG410IZKS; Eukaryota.
eggNOG; ENOG410Y8GB; LUCA.
GeneTree; ENSGT00390000003178; -.
HOGENOM; HOG000231637; -.
InParanoid; O54918; -.
KO; K16341; -.
OMA; AEDHPQM; -.
OrthoDB; EOG091G0XD3; -.
PhylomeDB; O54918; -.
TreeFam; TF335898; -.
Reactome; R-MMU-111446; Activation of BIM and translocation to mitochondria.
Reactome; R-MMU-111453; BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members.
Reactome; R-MMU-193648; NRAGE signals death through JNK.
ChiTaRS; Bcl2l11; mouse.
EvolutionaryTrace; O54918; -.
PRO; PR:O54918; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000027381; -.
CleanEx; MM_BCL2L11; -.
ExpressionAtlas; O54918; baseline and differential.
Genevisible; O54918; MM.
GO; GO:0097136; C:Bcl-2 family protein complex; IMP:CAFA.
GO; GO:0097141; C:BIM-BCL-2 complex; ISO:MGI.
GO; GO:0097140; C:BIM-BCL-xl complex; ISO:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0019898; C:extrinsic component of membrane; IDA:MGI.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:MGI.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0070840; F:dynein complex binding; IDA:MGI.
GO; GO:0008017; F:microtubule binding; IDA:MGI.
GO; GO:0046982; F:protein heterodimerization activity; IMP:CAFA.
GO; GO:0019901; F:protein kinase binding; IPI:ARUK-UCL.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
GO; GO:1902263; P:apoptotic process involved in embryonic digit morphogenesis; IGI:MGI.
GO; GO:0001783; P:B cell apoptotic process; IGI:MGI.
GO; GO:0001782; P:B cell homeostasis; IMP:MGI.
GO; GO:0007420; P:brain development; IEA:Ensembl.
GO; GO:0007160; P:cell-matrix adhesion; IMP:MGI.
GO; GO:0060154; P:cellular process regulating host cell cycle in response to virus; IDA:MGI.
GO; GO:0048066; P:developmental pigmentation; IGI:MGI.
GO; GO:0043583; P:ear development; IGI:MGI.
GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IMP:MGI.
GO; GO:0001701; P:in utero embryonic development; IGI:MGI.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IGI:MGI.
GO; GO:0001822; P:kidney development; IGI:MGI.
GO; GO:0001776; P:leukocyte homeostasis; IMP:MGI.
GO; GO:0002260; P:lymphocyte homeostasis; IMP:MGI.
GO; GO:0008584; P:male gonad development; IGI:MGI.
GO; GO:0030879; P:mammary gland development; IMP:MGI.
GO; GO:0002262; P:myeloid cell homeostasis; IGI:MGI.
GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IGI:MGI.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:MGI.
GO; GO:0060139; P:positive regulation of apoptotic process by virus; IDA:MGI.
GO; GO:0045787; P:positive regulation of cell cycle; IMP:MGI.
GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:MGI.
GO; GO:2000271; P:positive regulation of fibroblast apoptotic process; ISO:MGI.
GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; ISO:MGI.
GO; GO:1902110; P:positive regulation of mitochondrial membrane permeability involved in apoptotic process; IGI:MGI.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IDA:MGI.
GO; GO:0032464; P:positive regulation of protein homooligomerization; ISO:MGI.
GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; ISO:MGI.
GO; GO:0048563; P:post-embryonic animal organ morphogenesis; IMP:MGI.
GO; GO:0009791; P:post-embryonic development; IGI:MGI.
GO; GO:0042981; P:regulation of apoptotic process; IGI:MGI.
GO; GO:0048070; P:regulation of developmental pigmentation; IGI:MGI.
GO; GO:0046620; P:regulation of organ growth; IMP:MGI.
GO; GO:0034976; P:response to endoplasmic reticulum stress; IDA:UniProtKB.
GO; GO:0007283; P:spermatogenesis; IGI:MGI.
GO; GO:0048536; P:spleen development; IGI:MGI.
GO; GO:0043029; P:T cell homeostasis; IMP:MGI.
GO; GO:0070242; P:thymocyte apoptotic process; IGI:MGI.
GO; GO:0048538; P:thymus development; IGI:MGI.
GO; GO:0035148; P:tube formation; IMP:MGI.
InterPro; IPR014771; Apoptosis_Bim_N.
InterPro; IPR017288; Bcl-2-like_11.
InterPro; IPR015040; Bcl-x_interacting_BH3_dom.
Pfam; PF08945; Bclx_interact; 1.
Pfam; PF06773; Bim_N; 1.
PIRSF; PIRSF037827; Bcl-2-like_p11; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Apoptosis; Complete proteome;
Membrane; Mitochondrion; Phosphoprotein; Reference proteome;
Ubl conjugation.
CHAIN 1 196 Bcl-2-like protein 11.
/FTId=PRO_0000143110.
MOTIF 146 160 BH3.
MOD_RES 65 65 Phosphoserine; by MAPK.
{ECO:0000269|PubMed:21478148,
ECO:0000269|PubMed:27013495}.
MOD_RES 73 73 Phosphoserine.
{ECO:0000250|UniProtKB:O88498}.
MOD_RES 83 83 Phosphoserine.
{ECO:0000250|UniProtKB:O88498}.
MOD_RES 90 90 Phosphoserine.
{ECO:0000250|UniProtKB:O43521}.
VAR_SEQ 42 127 Missing (in isoform BimS). {ECO:0000305}.
/FTId=VSP_000537.
VAR_SEQ 42 97 Missing (in isoform BimL). {ECO:0000305}.
/FTId=VSP_000536.
MUTAGEN 55 55 S->A: Loss of TRIM2-binding; when
associated with A-65 and A-73.
{ECO:0000269|PubMed:21478148}.
MUTAGEN 65 65 S->A: Loss of TRIM2-binding; when
associated with A-55 and A-73.
{ECO:0000269|PubMed:21478148}.
MUTAGEN 73 73 S->A: Loss of TRIM2-binding; when
associated with A-55 and A-65.
{ECO:0000269|PubMed:21478148}.
MUTAGEN 150 150 Missing: Loss of MCL1-binding, strong
decrease in BCL2L1-binding, no effect on
USP27X-binding; when associated with I-
153 del. {ECO:0000269|PubMed:27013495}.
MUTAGEN 153 153 Missing: Loss of MCL1-binding, strong
decrease in BCL2L1-binding, no effect on
USP27X-binding; when associated with L-
150 del. {ECO:0000269|PubMed:27013495}.
HELIX 142 168 {ECO:0000244|PDB:1PQ1}.
SEQUENCE 196 AA; 22067 MW; 531C176E5F1AC9AA CRC64;
MAKQPSDVSS ECDREGGQLQ PAERPPQLRP GAPTSLQTEP QGNPDGEGDR CPHGSPQGPL
APPASPGPFA TRSPLFIFVR RSSLLSRSSS GYFSFDTDRS PAPMSCDKST QTPSPPCQAF
NHYLSAMASI RQSQEEPEDL RPEIRIAQEL RRIGDEFNET YTRRVFANDY REAEDHPQMV
ILQLLRFIFR LVWRRH


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