BCL2L11

BCL2L11
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1F95, 2K7W, 2NL9, 2V6Q, 2VM6, 2WH6, 2YQ6, 2YQ7, 3D7V, 3FDL, 3IO8, 3IO9, 3KJ0, 3KJ1, 3KJ2, 4A1U, 4A1W, 4B4S, 4D2M, 4QVF, 4UF3, 4YJ4, 4ZIF, 4ZIH, 5AGW, 5AGX, 5C3G
Identifiers
Aliases	BCL2L11, BAM, BIM, BOD, BCL2 like 11
External IDs	MGI: 1197519 HomoloGene: 7643 GeneCards: BCL2L11
Gene location (Human)
Chr.	Chromosome 2 (human)[1]
End	111,168,447 bp[1]
Gene location (Mouse)
Chr.	Chromosome 2 (mouse)[2]
End	128,162,547 bp[2]
RNA expression pattern
	; ;
	More reference expression data
Gene ontology
Molecular function	• protein binding; • microtubule binding; • dynein complex binding; • protein heterodimerization activity;
Cellular component	• cytoplasm; • cytosol; • membrane; • intracellular membrane-bounded organelle; • BIM-BCL-2 complex; • mitochondrial outer membrane; • BIM-BCL-xl complex; • cytoplasmic dynein complex; • mitochondrion; • microtubule; • endomembrane system; • extrinsic component of membrane; • Bcl-2 family protein complex;
Biological process	• leukocyte homeostasis; • regulation of apoptotic process; • positive regulation of protein homooligomerization; • cellular process regulating host cell cycle in response to virus; • male gonad development; • positive regulation of cell death; • positive regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; • B cell apoptotic process; • kidney development; • thymus development; • lymphocyte homeostasis; • positive regulation of apoptotic process by virus; • myeloid cell homeostasis; • post-embryonic animal organ morphogenesis; • ear development; • in utero embryonic development; • B cell homeostasis; • spleen development; • thymocyte apoptotic process; • post-embryonic development; • response to endoplasmic reticulum stress; • mammary gland development; • T cell homeostasis; • odontogenesis of dentin-containing tooth; • positive regulation of IRE1-mediated unfolded protein response; • positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; • tube formation; • brain development; • positive regulation of neuron apoptotic process; • positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; • positive regulation of cell cycle; • positive regulation of mitochondrial membrane permeability involved in apoptotic process; • meiosis I; • spermatogenesis; • intrinsic apoptotic signaling pathway in response to DNA damage; • extrinsic apoptotic signaling pathway in absence of ligand; • positive regulation of apoptotic process; • positive regulation of fibroblast apoptotic process; • developmental pigmentation; • positive regulation of release of cytochrome c from mitochondria; • regulation of developmental pigmentation; • cell-matrix adhesion; • regulation of organ growth; • activation of cysteine-type endopeptidase activity involved in apoptotic process; • positive regulation of intrinsic apoptotic signaling pathway; • apoptotic process involved in embryonic digit morphogenesis; • apoptotic process; • protein insertion into mitochondrial membrane involved in apoptotic signaling pathway;
	Sources:Amigo / QuickGO
Orthologs
	10018
	12125
	ENSG00000153094
	ENSMUSG00000027381
	O43521
	O54918
NM_001204106; NM_001204107; NM_001204108; NM_001204109; NM_001204110;
	NM_001204111; NM_001204112; NM_001204113; NM_006538; NM_138621; NM_138622; NM_138623; NM_138624; NM_138625; NM_138626; NM_138627; NM_207002; NM_207003
	NM_001284410; NM_001291016; NM_009754; NM_207680; NM_207681
NP_001191035; NP_001191036; NP_001191037; NP_001191038; NP_001191039;
	NP_001191040; NP_001191041; NP_001191042; NP_006529; NP_619527; NP_619528; NP_619529; NP_619530; NP_619531; NP_619532; NP_619533; NP_996885; NP_996886
	NP_001271339; NP_001277945; NP_033884; NP_997563; NP_997564
	Wikidata
View/Edit Human	View/Edit Mouse

Bcl-2-like protein 11, commonly called BIM, is a protein that in humans is encoded by the BCL2L11 gene.^[5]^[6]

Function

The protein encoded by this gene belongs to the BCL-2 protein family. BCL-2 family members form hetero- or homodimers and act as anti- or pro-apoptotic regulators that are involved in a wide variety of cellular activities. The protein encoded by this gene contains a Bcl-2 homology domain 3 (BH3). It has been shown to interact with other members of the BCL-2 protein family, including BCL2, BCL2L1/BCL-X(L), and MCL1, and to act as an apoptotic activator. The expression of this gene can be induced by nerve growth factor (NGF), as well as by the forkhead transcription factor FKHR-L1 (FoxO3a), which suggests a role of this gene in neuronal and lymphocyte apoptosis. Transgenic studies of the mouse counterpart suggested that this gene functions as an essential initiator of apoptosis in thymocyte-negative selection. Several alternatively spliced transcript variants of this gene have been identified.^[7]

Regulation of Bim

Bim expression and activity are regulated at the transcriptional, translational and post-translational levels; coordinated expression and activity of Bim shape immune responses, and ensure tissue integrity. Cancer cells develop mechanisms that suppress Bim expression, which allows for tumor progression and metastasis.^[8]

Interactions

BCL2L11 has been shown to interact with:

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000153094 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000027381 - Ensembl, May 2017
↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
1 2 3 4 5 Hsu SY, Lin P, Hsueh AJ (November 1998). "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 (9): 1432–40. doi:10.1210/mend.12.9.0166. PMID 9731710.
1 2 3 4 O'Connor L, Strasser A, O'Reilly LA, Hausmann G, Adams JM, Cory S, Huang DC (February 1998). "Bim: a novel member of the Bcl-2 family that promotes apoptosis". EMBO J. 17 (2): 384–95. doi:10.1093/emboj/17.2.384. PMC 1170389. PMID 9430630.
↑ "Entrez Gene: BCL2L11 BCL2-like 11 (apoptosis facilitator)".
↑ Sionov RV, Vlahopoulos SA, Granot Z (2015). "Regulation of Bim in Health and Disease". Oncotarget. 6 (27): 23058–134. doi:10.18632/oncotarget.5492. PMC 4695108. PMID 26405162.
1 2 3 Chen L, Willis SN, Wei A, Smith BJ, Fletcher JI, Hinds MG, Colman PM, Day CL, Adams JM, Huang DC (February 2005). "Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function". Mol. Cell. 17 (3): 393–403. doi:10.1016/j.molcel.2004.12.030. PMID 15694340.
↑ Whitfield J, Harada K, Bardelle C, Staddon JM (November 2003). "High-throughput methods to detect dimerization of Bcl-2 family proteins". Anal. Biochem. 322 (2): 170–8. doi:10.1016/j.ab.2003.07.014. PMID 14596824.
↑ Day CL, Puthalakath H, Skea G, Strasser A, Barsukov I, Lian LY, Huang DC, Hinds MG (February 2004). "Localization of dynein light chains 1 and 2 and their pro-apoptotic ligands". Biochem. J. 377 (Pt 3): 597–605. doi:10.1042/BJ20031251. PMC 1223895. PMID 14561217.
↑ Vadlamudi RK, Bagheri-Yarmand R, Yang Z, Balasenthil S, Nguyen D, Sahin AA, den Hollander P, Kumar R (June 2004). "Dynein light chain 1, a p21-activated kinase 1-interacting substrate, promotes cancerous phenotypes". Cancer Cell. 5 (6): 575–85. doi:10.1016/j.ccr.2004.05.022. PMID 15193260.
↑ Bae J, Leo CP, Hsu SY, Hsueh AJ (August 2000). "MCL-1S, a splicing variant of the antiapoptotic BCL-2 family member MCL-1, encodes a proapoptotic protein possessing only the BH3 domain". J. Biol. Chem. 275 (33): 25255–61. doi:10.1074/jbc.M909826199. PMID 10837489.

External links

BCL2L11 human gene location in the UCSC Genome Browser.
BCL2L11 human gene details in the UCSC Genome Browser.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000153094 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000027381 - Ensembl, May 2017

[3] "Human PubMed Reference:".

[4] "Mouse PubMed Reference:".

[pmid9731710-5] 1 2 3 4 5 Hsu SY, Lin P, Hsueh AJ (November 1998). "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 (9): 1432–40. doi:10.1210/mend.12.9.0166. PMID 9731710.

[pmid9430630-6] 1 2 3 4 O'Connor L, Strasser A, O'Reilly LA, Hausmann G, Adams JM, Cory S, Huang DC (February 1998). "Bim: a novel member of the Bcl-2 family that promotes apoptosis". EMBO J. 17 (2): 384–95. doi:10.1093/emboj/17.2.384. PMC 1170389. PMID 9430630.

[7] "Entrez Gene: BCL2L11 BCL2-like 11 (apoptosis facilitator)".

[pmid26405162-8] Sionov RV, Vlahopoulos SA, Granot Z (2015). "Regulation of Bim in Health and Disease". Oncotarget. 6 (27): 23058–134. doi:10.18632/oncotarget.5492. PMC 4695108. PMID 26405162.

[pmid15694340-9] 1 2 3 Chen L, Willis SN, Wei A, Smith BJ, Fletcher JI, Hinds MG, Colman PM, Day CL, Adams JM, Huang DC (February 2005). "Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function". Mol. Cell. 17 (3): 393–403. doi:10.1016/j.molcel.2004.12.030. PMID 15694340.

[pmid14596824-10] Whitfield J, Harada K, Bardelle C, Staddon JM (November 2003). "High-throughput methods to detect dimerization of Bcl-2 family proteins". Anal. Biochem. 322 (2): 170–8. doi:10.1016/j.ab.2003.07.014. PMID 14596824.

[pmid14561217-11] Day CL, Puthalakath H, Skea G, Strasser A, Barsukov I, Lian LY, Huang DC, Hinds MG (February 2004). "Localization of dynein light chains 1 and 2 and their pro-apoptotic ligands". Biochem. J. 377 (Pt 3): 597–605. doi:10.1042/BJ20031251. PMC 1223895. PMID 14561217.

[pmid15193260-12] Vadlamudi RK, Bagheri-Yarmand R, Yang Z, Balasenthil S, Nguyen D, Sahin AA, den Hollander P, Kumar R (June 2004). "Dynein light chain 1, a p21-activated kinase 1-interacting substrate, promotes cancerous phenotypes". Cancer Cell. 5 (6): 575–85. doi:10.1016/j.ccr.2004.05.022. PMID 15193260.

[pmid10837489-13] Bae J, Leo CP, Hsu SY, Hsueh AJ (August 2000). "MCL-1S, a splicing variant of the antiapoptotic BCL-2 family member MCL-1, encodes a proapoptotic protein possessing only the BH3 domain". J. Biol. Chem. 275 (33): 25255–61. doi:10.1074/jbc.M909826199. PMID 10837489.