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

 B2L11_RAT               Reviewed;         196 AA.
O88498; O88497; Q9WUI8;
18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
29-SEP-2021, entry version 154.
RecName: Full=Bcl-2-like protein 11;
Short=Bcl2-L-11;
AltName: Full=Bcl-2-related ovarian death protein;
AltName: Full=Bcl2-interacting mediator of cell death;
Name=Bcl2l11; Synonyms=Bim, Bod;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH BCL-2 PROTEINS, AND
TISSUE SPECIFICITY (ISOFORMS BOD-L; BOD-M AND BOD-S).
TISSUE=Ovary;
PubMed=9731710; DOI=10.1210/mend.12.9.0166;
Hsu S.Y., Lin P., Hsueh A.J.W.;
"BOD (Bcl-2-related ovarian death gene) is an ovarian BH3 domain-containing
proapoptotic Bcl-2 protein capable of dimerization with diverse
antiapoptotic Bcl-2 members.";
Mol. Endocrinol. 12:1432-1440(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BIML).
Chen D., Simon R.P., Chen J.;
"Cloning of rat bimEL and bimL, and their differential expression in
ischemia and normal rat brain.";
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
[3]
INTERACTION WITH DYNLL1; TRIM2 AND YWHAZ, AND UBIQUITINATION.
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).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73 AND SER-83, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14 different rat
organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Induces apoptosis and anoikis. {ECO:0000269|PubMed:9731710}.
-!- 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. Does not heterodimerize with proapoptotic proteins
such as BAD, BOK or BAK (PubMed:9731710). Identified in a complex
containing BCL2L11, DYNLL1 and BCL2L1 isoform Bcl-X(L); BH3 integrity
is required for BCL2L1-binding. 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:9731710). When phosphorylated, isoform
BimEL interacts with USP27X; this interaction leads to BCL2L11
deubiquitination and stabilization (By similarity). Interacts with
GIMAP5 (By similarity). {ECO:0000250|UniProtKB:O54918,
ECO:0000269|PubMed:21478148, ECO:0000269|PubMed:9731710}.
-!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein.
Mitochondrion {ECO:0000250}. Note=Associated with intracytoplasmic
membranes. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing, Alternative initiation; Named isoforms=4;
Name=BOD-L;
IsoId=O88498-1; Sequence=Displayed;
Name=BimL;
IsoId=O88498-2; Sequence=VSP_000538;
Name=BOD-M;
IsoId=O88498-3; Sequence=VSP_000539;
Name=BOD-S;
IsoId=O88498-4; Sequence=VSP_018668;
-!- TISSUE SPECIFICITY: Widely expressed.
-!- DOMAIN: The BH3 motif is required for the interaction with Bcl-2
proteins and cytotoxicity. {ECO:0000250|UniProtKB:O54918}.
-!- PTM: Phosphorylation at Ser-65 by MAPK1/MAPK3 leads interaction with
TRIM2 and ubiquitination, followed by proteasomal degradation.
Deubiquitination catalyzed by USP27X stabilizes the protein.
{ECO:0000250|UniProtKB:O54918}.
-!- PTM: Ubiquitination by TRIM2 following phosphorylation by MAPK1/MAPK3
leads to proteasomal degradation (PubMed:21478148). Conversely,
deubiquitination catalyzed by USP27X stabilizes the protein (By
similarity). {ECO:0000250|UniProtKB:O54918,
ECO:0000269|PubMed:21478148}.
-!- MISCELLANEOUS: [Isoform BOD-S]: Produced by alternative initiation at
Met-104 of isoform BOD-L. {ECO:0000305}.
-!- SIMILARITY: Belongs to the Bcl-2 family. {ECO:0000305}.
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EMBL; AF065433; AAC23595.1; -; mRNA.
EMBL; AF065431; AAC23593.1; -; mRNA.
EMBL; AF065432; AAC23594.1; -; mRNA.
EMBL; AF136927; AAD26594.1; -; mRNA.
RefSeq; NP_072134.1; NM_022612.1.
RefSeq; NP_741985.1; NM_171988.2. [O88498-1]
RefSeq; NP_741986.1; NM_171989.1.
SMR; O88498; -.
BioGRID; 249128; 4.
ComplexPortal; CPX-2026; BIM:BCL-XL complex.
ComplexPortal; CPX-2035; BIM:BCL-2 complex.
ELM; O88498; -.
IntAct; O88498; 5.
STRING; 10116.ENSRNOP00000039006; -.
iPTMnet; O88498; -.
PhosphoSitePlus; O88498; -.
PaxDb; O88498; -.
Ensembl; ENSRNOT00000022596; ENSRNOP00000022596; ENSRNOG00000016551. [O88498-2]
Ensembl; ENSRNOT00000051069; ENSRNOP00000039006; ENSRNOG00000016551. [O88498-1]
GeneID; 64547; -.
KEGG; rno:64547; -.
UCSC; RGD:628774; rat. [O88498-1]
CTD; 10018; -.
RGD; 628774; Bcl2l11.
eggNOG; ENOG502S0DF; Eukaryota.
GeneTree; ENSGT00390000003178; -.
HOGENOM; CLU_104244_0_0_1; -.
InParanoid; O88498; -.
OMA; PETWIAQ; -.
OrthoDB; 1460067at2759; -.
PhylomeDB; O88498; -.
Reactome; R-RNO-111446; Activation of BIM and translocation to mitochondria.
Reactome; R-RNO-111453; BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members.
Reactome; R-RNO-193648; NRAGE signals death through JNK.
PRO; PR:O88498; -.
Proteomes; UP000002494; Chromosome 3.
Bgee; ENSRNOG00000016551; Expressed in thymus and 21 other tissues.
Genevisible; O88498; RN.
GO; GO:0097136; C:Bcl-2 family protein complex; ISO:RGD.
GO; GO:0005737; C:cytoplasm; ISO:RGD.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0019898; C:extrinsic component of membrane; ISO:RGD.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:RGD.
GO; GO:0005739; C:mitochondrion; IDA:RGD.
GO; GO:0008017; F:microtubule binding; ISO:RGD.
GO; GO:0019901; F:protein kinase binding; ISO:RGD.
GO; GO:1902263; P:apoptotic process involved in embryonic digit morphogenesis; ISO:RGD.
GO; GO:0001782; P:B cell homeostasis; ISO:RGD.
GO; GO:0007420; P:brain development; IEP:RGD.
GO; GO:0007160; P:cell-matrix adhesion; ISO:RGD.
GO; GO:1904646; P:cellular response to amyloid-beta; IEP:RGD.
GO; GO:0071392; P:cellular response to estradiol stimulus; IEP:RGD.
GO; GO:0048066; P:developmental pigmentation; ISO:RGD.
GO; GO:0043583; P:ear development; ISO:RGD.
GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; ISO:RGD.
GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; ISO:RGD.
GO; GO:0001822; P:kidney development; ISO:RGD.
GO; GO:0001776; P:leukocyte homeostasis; ISO:RGD.
GO; GO:0002260; P:lymphocyte homeostasis; ISO:RGD.
GO; GO:0008584; P:male gonad development; ISO:RGD.
GO; GO:0030879; P:mammary gland development; ISO:RGD.
GO; GO:0007127; P:meiosis I; IBA:GO_Central.
GO; GO:0002262; P:myeloid cell homeostasis; ISO:RGD.
GO; GO:0042475; P:odontogenesis of dentin-containing tooth; ISO:RGD.
GO; GO:0043065; P:positive regulation of apoptotic process; ISO:RGD.
GO; GO:0060139; P:positive regulation of apoptotic process by virus; ISO:RGD.
GO; GO:0034263; P:positive regulation of autophagy in response to ER overload; IMP:RGD.
GO; GO:0045787; P:positive regulation of cell cycle; ISO:RGD.
GO; GO:0010942; P:positive regulation of cell death; IDA:RGD.
GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:RGD.
GO; GO:2000271; P:positive regulation of fibroblast apoptotic process; ISO:RGD.
GO; GO:1902110; P:positive regulation of mitochondrial membrane permeability involved in apoptotic process; ISO:RGD.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISO:RGD.
GO; GO:0031334; P:positive regulation of protein-containing complex assembly; ISO:RGD.
GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; ISO:RGD.
GO; GO:0048563; P:post-embryonic animal organ morphogenesis; ISO:RGD.
GO; GO:0009791; P:post-embryonic development; ISO:RGD.
GO; GO:0042981; P:regulation of apoptotic process; ISO:RGD.
GO; GO:0048070; P:regulation of developmental pigmentation; ISO:RGD.
GO; GO:0046620; P:regulation of organ growth; ISO:RGD.
GO; GO:0034976; P:response to endoplasmic reticulum stress; ISO:RGD.
GO; GO:0007283; P:spermatogenesis; ISO:RGD.
GO; GO:0048536; P:spleen development; ISO:RGD.
GO; GO:0043029; P:T cell homeostasis; ISO:RGD.
GO; GO:0070242; P:thymocyte apoptotic process; ISO:RGD.
GO; GO:0048538; P:thymus development; ISO:RGD.
GO; GO:0035148; P:tube formation; ISO:RGD.
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;
Alternative initiation; Alternative splicing; Apoptosis; Membrane;
Mitochondrion; Phosphoprotein; Reference proteome; Ubl conjugation.
CHAIN 1..196
/note="Bcl-2-like protein 11"
/id="PRO_0000002814"
REGION 1..68
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 90..114
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
MOTIF 146..160
/note="BH3"
MOD_RES 65
/note="Phosphoserine; by MAPK"
/evidence="ECO:0000250|UniProtKB:O43521"
MOD_RES 73
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:22673903"
MOD_RES 83
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:22673903"
MOD_RES 90
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:O43521"
VAR_SEQ 1..103
/note="Missing (in isoform BOD-S)"
/evidence="ECO:0000305"
/id="VSP_018668"
VAR_SEQ 42..127
/note="Missing (in isoform BOD-M)"
/evidence="ECO:0000305"
/id="VSP_000539"
VAR_SEQ 42..97
/note="Missing (in isoform BimL)"
/evidence="ECO:0000303|Ref.2"
/id="VSP_000538"
CONFLICT 136
/note="E -> D (in Ref. 1; AAC23594)"
/evidence="ECO:0000305"
SEQUENCE 196 AA; 22056 MW; B4D2146F9C0B37A0 CRC64;
MAKQPSDVNS ECDREGGQLQ PAERPPQLRP GAPTSLQTES QGNPDGEGDR CPHGSPQGPL
APPASPGPFA TRSPLFIFVR RSSLLSRSSS GYFSFDTDRS PAPMSCDKST QTPSPPCQAF
NHYLSAMASI RQSQEEPEDL RPEIRIAQEL RRIGDEFNET YTRRAFANDY REAEDHPQMV
ILQLLRFIFR LVWRRH


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Pathways :
WP1438: Influenza A virus infection
WP285: B Cell Receptor Signaling Pathway
WP2199: Seed Development
WP2272: Pathogenic Escherichia coli infection
WP367: Programmed Cell Death
WP1144: B Cell Receptor Signaling Pathway
WP274: B Cell Receptor Signaling Pathway
WP731: Sterol regulatory element binding protein related
WP2152: BDNF
WP908: B Cell Receptor Signaling Pathway
WP1025: B Cell Receptor Signaling Pathway
WP1354: B Cell Receptor Signaling Pathway
WP794: B Cell Receptor Signaling Pathway
WP2032: TSH signaling pathway
WP615: Senescence and Autophagy
WP1290: Apoptosis
WP89: FAS pathway and Stress induction of HSP regulation
WP1659: Glycine, serine and threonine metabolism
WP1888: Post-translational protein modification
WP373: IL-3 Signaling Pathway
WP813: G Protein Signaling Pathways
WP1137: Apoptosis
WP1491: PI3K_AKT_NFKB pathway
WP1713: Two-component system
WP232: G Protein Signaling Pathways

Related Genes :
[Bcl2l11 Bim Bod] Bcl-2-like protein 11 (Bcl2-L-11) (Bcl-2-related ovarian death protein) (Bcl2-interacting mediator of cell death)
[BCL2L11 BIM] Bcl-2-like protein 11 (Bcl2-L-11) (Bcl2-interacting mediator of cell death)
[Bcl2l11 Bim] Bcl-2-like protein 11 (Bcl2-L-11) (Bcl2-interacting mediator of cell death)
[BAD BBC6 BCL2L8] Bcl2-associated agonist of cell death (BAD) (Bcl-2-binding component 6) (Bcl-2-like protein 8) (Bcl2-L-8) (Bcl-xL/Bcl-2-associated death promoter) (Bcl2 antagonist of cell death)
[BOK BCL2L9] Bcl-2-related ovarian killer protein (hBOK) (Bcl-2-like protein 9) (Bcl2-L-9)
[Bad Bbc6] Bcl2-associated agonist of cell death (BAD) (Bcl-2-binding component 6) (Bcl-xL/Bcl-2-associated death promoter) (Bcl2 antagonist of cell death)
[Bad] Bcl2-associated agonist of cell death (BAD) (Bcl-2-binding component 6) (Bcl-xL/Bcl-2-associated death promoter) (Bcl2 antagonist of cell death)
[MCL1 BCL2L3] Induced myeloid leukemia cell differentiation protein Mcl-1 (Bcl-2-like protein 3) (Bcl2-L-3) (Bcl-2-related protein EAT/mcl1) (mcl1/EAT)
[BCL2L1 BCL2L BCLX] Bcl-2-like protein 1 (Bcl2-L-1) (Apoptosis regulator Bcl-X)
[Bok Mtd] Bcl-2-related ovarian killer protein (Apoptosis activator Mtd) (Protein matador)
[BAX BCL2L4] Apoptosis regulator BAX (Bcl-2-like protein 4) (Bcl2-L-4)
[Bcl2l1 Bcl2l Bclx] Bcl-2-like protein 1 (Bcl2-L-1) (Apoptosis regulator Bcl-X)
[BCL2A1 BCL2L5 BFL1 GRS HBPA1] Bcl-2-related protein A1 (Bcl-2-like protein 5) (Bcl2-L-5) (Hemopoietic-specific early response protein) (Protein BFL-1) (Protein GRS)
[BNIP3L BNIP3A BNIP3H NIX] BCL2/adenovirus E1B 19 kDa protein-interacting protein 3-like (Adenovirus E1B19K-binding protein B5) (BCL2/adenovirus E1B 19 kDa protein-interacting protein 3A) (NIP3-like protein X) (NIP3L)
[Bok] Bcl-2-related ovarian killer protein
[Bcl2l1 Bclx Blc2l] Bcl-2-like protein 1 (Bcl2-L-1) (Apoptosis regulator Bcl-X)
[BCL2] Apoptosis regulator Bcl-2
[BCL2L10 BCLB] Bcl-2-like protein 10 (Bcl2-L-10) (Anti-apoptotic protein NrH) (Apoptosis regulator Bcl-B)
[BAK1 BAK BCL2L7 CDN1] Bcl-2 homologous antagonist/killer (Apoptosis regulator BAK) (Bcl-2-like protein 7) (Bcl2-L-7)
[Bcl2 Bcl-2] Apoptosis regulator Bcl-2
[Bcl2 Bcl-2] Apoptosis regulator Bcl-2
[BCL2 BCL-2] Apoptosis regulator Bcl-2
[Mcl1] Induced myeloid leukemia cell differentiation protein Mcl-1 homolog (Bcl-2-related protein EAT/mcl1)
[BCL2L2 BCLW KIAA0271] Bcl-2-like protein 2 (Bcl2-L-2) (Apoptosis regulator Bcl-W)
[BCL2L13 MIL1 CD003] Bcl-2-like protein 13 (Bcl2-L-13) (Bcl-rambo) (Protein Mil1)
[BCL2] Apoptosis regulator Bcl-2
[BECN1 GT197] Beclin-1 (Coiled-coil myosin-like BCL2-interacting protein) (Protein GT197) [Cleaved into: Beclin-1-C 35 kDa; Beclin-1-C 37 kDa]
[BAG3 BIS] BAG family molecular chaperone regulator 3 (BAG-3) (Bcl-2-associated athanogene 3) (Bcl-2-binding protein Bis) (Docking protein CAIR-1)
[Becn1] Beclin-1 (Coiled-coil myosin-like BCL2-interacting protein) [Cleaved into: Beclin-1-C 35 kDa; Beclin-1-C 37 kDa]
[BIK NBK] Bcl-2-interacting killer (Apoptosis inducer NBK) (BIP1) (BP4)

Bibliography :