BCL2L11 (Mus musculus)
Description [+]
- Synonyms: BCL2L11, BCL2L11, BCL2-LIKE 11 (APOPTOSIS FACILITATOR), 1500006F24RIK, BIM, BOD
- Species: Metazoa;Bilateria;Deuterostoma;Chordata;Vertebrata;Mammalia;Rodentia; Mus musculus
- Short gene description: BCL2-like 11 (apoptosis facilitator) Gene [Source:MGI (curated);Acc:Bcl2l11-001]
- Family: Bcl-2 family : BH3-only
- Process: apoptosis,
- Pathways: intrinsic pathway, pre-mitochondrial signaling events,
- Criteria: manually curated
- Curator comment:
- Human ortholog(s): BCL2L11
- WIKI: BCL2L11-M_musculus
References [+]
- Bim: a novel member of the Bcl-2 family that promotes apoptosis.
- O'Connor L, Strasser A, O'Reilly LA, Hausmann G, Adams JM, Cory S, Huang DC
- Certain members of the Bcl-2 family inhibit apoptosis while others facilitate this physiological process of cell death. An expression screen for proteins that bind to Bcl-2 yielded a small novel protein, denoted Bim, whose only similarity to any known protein is the short (nine amino acid) BH3 motif shared by most Bcl-2 homologues. Bim provokes apoptosis, and the BH3 region is required for Bcl-2 binding and for most of its cytotoxicity. Like Bcl-2, Bim possesses a hydrophobic C-terminus and localizes to intracytoplasmic membranes. Three Bim isoforms, probably generated by alternative splicing, all induce apoptosis, the shortest being the most potent. Wild-type Bcl-2 associates with Bim in vivo and modulates its death function, whereas Bcl-2 mutants that lack survival function do neither. Significantly, Bcl-xL and Bcl-w, the two closest homologues of Bcl-2, also bind to Bim and inhibit its activity, but more distant viral homologues, adenovirus E1B19K and Epstein-Barr virus BHRF-1, can do neither. Hence, Bim appears to act as a 'death ligand' which can only neutralize certain members of the pro-survival Bcl-2 sub-family. EMBO J. 1998 Jan 15;17(2):384-95.
- Bim and Bmf in tissue homeostasis and malignant disease.
- Pinon JD, Labi V, Egle A, Villunger A
- Among all BH3-only proteins known to date, most information is available on the biological role and function of Bim (Bcl-2 interacting mediator of cell death)/BOD (Bcl-2 related ovarian death agonist), whereas little is still known about its closest relative, Bcl-2 modifying factor (Bmf). Although Bim has been implicated in the regulation of cell death induction in multiple cell types and tissues in response to a large number of stimuli, including growth factor or cytokine deprivation, calcium flux, ligation of antigen receptors on T and B cells, glucocorticoid or loss of adhesion, Bmf seems to play a more restricted role by supporting Bim in some of these cell death processes. This review aims to highlight similarities between Bim and Bmf function in apoptosis signaling and their role in normal development and disease. Oncogene. 2008 Dec;27 Suppl 1:S41-52.
- References from Human ortholog(s):
- Bim: a novel member of the Bcl-2 family that promotes apoptosis.
- O'Connor L, Strasser A, O'Reilly LA, Hausmann G, Adams JM, Cory S, Huang DC
- Certain members of the Bcl-2 family inhibit apoptosis while others facilitate this physiological process of cell death. An expression screen for proteins that bind to Bcl-2 yielded a small novel protein, denoted Bim, whose only similarity to any known protein is the short (nine amino acid) BH3 motif shared by most Bcl-2 homologues. Bim provokes apoptosis, and the BH3 region is required for Bcl-2 binding and for most of its cytotoxicity. Like Bcl-2, Bim possesses a hydrophobic C-terminus and localizes to intracytoplasmic membranes. Three Bim isoforms, probably generated by alternative splicing, all induce apoptosis, the shortest being the most potent. Wild-type Bcl-2 associates with Bim in vivo and modulates its death function, whereas Bcl-2 mutants that lack survival function do neither. Significantly, Bcl-xL and Bcl-w, the two closest homologues of Bcl-2, also bind to Bim and inhibit its activity, but more distant viral homologues, adenovirus E1B19K and Epstein-Barr virus BHRF-1, can do neither. Hence, Bim appears to act as a 'death ligand' which can only neutralize certain members of the pro-survival Bcl-2 sub-family. EMBO J. 1998 Jan 15;17(2):384-95.
- Bim and Bmf in tissue homeostasis and malignant disease.
- Pinon JD, Labi V, Egle A, Villunger A
- Among all BH3-only proteins known to date, most information is available on the biological role and function of Bim (Bcl-2 interacting mediator of cell death)/BOD (Bcl-2 related ovarian death agonist), whereas little is still known about its closest relative, Bcl-2 modifying factor (Bmf). Although Bim has been implicated in the regulation of cell death induction in multiple cell types and tissues in response to a large number of stimuli, including growth factor or cytokine deprivation, calcium flux, ligation of antigen receptors on T and B cells, glucocorticoid or loss of adhesion, Bmf seems to play a more restricted role by supporting Bim in some of these cell death processes. This review aims to highlight similarities between Bim and Bmf function in apoptosis signaling and their role in normal development and disease. Oncogene. 2008 Dec;27 Suppl 1:S41-52.
- Bim and Bmf in tissue homeostasis and malignant disease.
- Pinon JD, Labi V, Egle A, Villunger A
- Among all BH3-only proteins known to date, most information is available on the biological role and function of Bim (Bcl-2 interacting mediator of cell death)/BOD (Bcl-2 related ovarian death agonist), whereas little is still known about its closest relative, Bcl-2 modifying factor (Bmf). Although Bim has been implicated in the regulation of cell death induction in multiple cell types and tissues in response to a large number of stimuli, including growth factor or cytokine deprivation, calcium flux, ligation of antigen receptors on T and B cells, glucocorticoid or loss of adhesion, Bmf seems to play a more restricted role by supporting Bim in some of these cell death processes. This review aims to highlight similarities between Bim and Bmf function in apoptosis signaling and their role in normal development and disease. Oncogene. 2008 Dec;27 Suppl 1:S41-52.
Structure & Sequence [+]
Pfam domains:
(Pfam is a large collection of protein families.)
Source | Domain Name | Start | End |
---|---|---|---|
PFAM A | Bim_N | 4 | 40 |
PFAM A | Bclx_interact | 127 | 165 |
Protein sequence [+]
Bcl2l11 | Mus musculus | 10090 | length:196
MAKQPSDVSSECDREGGQLQPAERPPQLRPGAPTSLQTEPQGNPDGEGDRCPHGSPQGPL
APPASPGPFATRSPLFIFVRRSSLLSRSSSGYFSFDTDRSPAPMSCDKSTQTPSPPCQAF
NHYLSAMASIRQSQEEPEDLRPEIRIAQELRRIGDEFNETYTRRVFANDYREAEDHPQMV
ILQLLRFIFRLVWRRH
APPASPGPFATRSPLFIFVRRSSLLSRSSSGYFSFDTDRSPAPMSCDKSTQTPSPPCQAF
NHYLSAMASIRQSQEEPEDLRPEIRIAQELRRIGDEFNETYTRRVFANDYREAEDHPQMV
ILQLLRFIFRLVWRRH
Evolution [+]
View protein alignment and tree with Jalview:  
Explore tree at phylomeDB:   Click here.
Homologs list [+]
Name | Relationship | Species |
---|---|---|
BCL2L11 | orthology | Chimpanzee |
NP_001068778.1 | orthology | Cow |
BCL2L11 | orthology | Dog |
BCL2L11 | orthology | Gorilla |
BCL2L11 | orthology | Horse |
BCL2L11 | orthology | Human |
BCL2L11 | orthology | Macaca |
BCL2L11 | orthology | Monodelphis |
BCL2L11 | orthology | Orangutan |
BCL2L11 | orthology | Ornithorhynchus |
BCL2L11 | orthology | Rabbit |
BIM_RAT | orthology | Rat |
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Gene Ontology [+]
GO id | Name | Ontology type | Evidence |
---|---|---|---|
GO:0001701 | in utero embryonic development | biological_proccess | IGI |
GO:0001782 | B cell homeostasis | biological_proccess | IMP |
GO:0001783 | B cell apoptosis | biological_proccess | IGI |
GO:0001822 | kidney development | biological_proccess | IGI |
GO:0002262 | myeloid cell homeostasis | biological_proccess | IGI |
GO:0007160 | cell-matrix adhesion | biological_proccess | IMP |
GO:0007283 | spermatogenesis | biological_proccess | IGI |
GO:0008584 | male gonad development | biological_proccess | IGI |
GO:0009791 | post-embryonic development | biological_proccess | IGI |
GO:0030879 | mammary gland development | biological_proccess | IMP |
GO:0035148 | lumen formation | biological_proccess | IMP |
GO:0042475 | odontogenesis of dentine-containing tooth | biological_proccess | IGI |
GO:0043029 | T cell homeostasis | biological_proccess | IMP |
GO:0043065 | positive regulation of apoptosis | biological_proccess | IMP |
GO:0043583 | ear development | biological_proccess | IGI |
GO:0046620 | regulation of organ growth | biological_proccess | IMP |
GO:0048070 | regulation of pigmentation during development | biological_proccess | IGI |
GO:0048536 | spleen development | biological_proccess | IGI |
GO:0048538 | thymus development | biological_proccess | IGI |
GO:0048563 | post-embryonic organ morphogenesis | biological_proccess | IMP |
GO:0002260 | lymphocyte homeostasis | biological_proccess | IMP |
GO:0001776 | leukocyte homeostasis | biological_proccess | IMP |
GO:0006915 | apoptosis | biological_proccess | IGI |
GO:0048066 | pigmentation during development | biological_proccess | IGI |
GO:0042981 | regulation of apoptosis | biological_proccess | RCA |
GO:0005515 | protein binding | mollecular_function | IPI |
GO:0008017 | microtubule binding | mollecular_function | IDA |
GO:0005515 | protein binding | mollecular_function | IEA |
GO:0000300 | peripheral to membrane of membrane fraction | cell_component | IDA |
GO:0005737 | cytoplasm | cell_component | IDA |
GO:0005739 | mitochondrion | cell_component | IDA |
GO:0016020 | membrane | cell_component | IEA |
GO:0043231 | intracellular membrane-bounded organelle | cell_component | IDA |
Check GO Evidence Codes here
Curated Isoforms [+]
Info from The Vertebrate Genome Annotation (VEGA) database.
(*) Canonical transcript and translation forms.
Information from other databases [+]
- Gene info from MGI [?] MGI:1197519
- Ensembl genome browser [?] : ENSMUSG00000027381
- Expression info from Arrayexpress [?] : ENSMUSG00000027381
- Protein expression from Protein Atlas: [?] ENSMUSG00000027381
- Community gene edition from Wikigenes: [?] 12125
Click on [?] for more information.