BCL2L11 (original) (raw)

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Protein-coding gene in the species Homo sapiens

BCL2L11
Available structuresPDBOrtholog search: PDBe RCSB List of PDB id codes1F95, 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 OMIM: 603827; MGI: 1197519; HomoloGene: 7643; GeneCards: BCL2L11; OMA:BCL2L11 - orthologs
Gene location (Human)Chromosome 2 (human)Chr.Chromosome 2 (human)[1]Chromosome 2 (human)Genomic location for BCL2L11Genomic location for BCL2L11Band2q13Start111,119,378 bp[1]End111,168,445 bp[1]
Gene location (Mouse)Chromosome 2 (mouse)Chr.Chromosome 2 (mouse)[2]Chromosome 2 (mouse)Genomic location for BCL2L11Genomic location for BCL2L11Band2|2 F1Start127,967,958 bp[2]End128,004,467 bp[2]
RNA expression patternBgeeHuman Mouse (ortholog)Top expressed inspermpalpebral conjunctivaepithelium of nasopharynxmucosa of paranasal sinussuperficial temporal arterygingival epitheliummonocytemucosa of colonmucosa of sigmoid colonjejunal mucosaTop expressed intransitional epithelium of urinary bladdervestibular membrane of cochlear ductciliary bodyinternal carotid arteryretinal pigment epitheliumutricleRostral migratory streamexternal carotid arterybloodendothelial cell of lymphatic vesselMore reference expression dataBioGPSMore reference expression data
Gene ontologyMolecular function protein binding microtubule binding dynein complex binding protein heterodimerization activity protein kinase binding 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 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 positive regulation of autophagy in response to ER overload cellular response to glucocorticoid stimulus cellular response to estradiol stimulus cellular response to amyloid-beta Sources:Amigo / QuickGO
OrthologsSpeciesHuman MouseEntrez1001812125EnsemblENSG00000153094ENSMUSG00000027381UniProtO43521O54918RefSeq (mRNA)NM_001204106NM_001204107NM_001204108NM_001204109NM_001204110NM_001204111NM_001204112NM_001204113NM_006538NM_138621NM_138622NM_138623NM_138624NM_138625NM_138626NM_138627NM_207002NM_207003NM_001284410NM_001291016NM_009754NM_207680NM_207681RefSeq (protein)NP_001191035NP_001191036NP_001191037NP_001191038NP_001191039NP_001191040NP_001191041NP_001191042NP_006529NP_619527NP_619528NP_619529NP_619530NP_619531NP_619532NP_619533NP_996885NP_996886NP_001271339NP_001277945NP_033884NP_997563NP_997564NP_001392986NP_001392987NP_001392988NP_001392989NP_001392990Location (UCSC)Chr 2: 111.12 – 111.17 MbChr 2: 127.97 – 128 MbPubMed search[3][4]
Wikidata
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Bcl-2-like protein 11, commonly called BIM (Bcl-2 Interacting Mediator of cell death), is a protein that in humans is encoded by the BCL2L11 gene.[5][6]

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]

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]

BCL2L11 has been shown to interact with:

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000153094 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000027381 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ a b c d e 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.
  6. ^ a b c d 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)".
  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.
  9. ^ a b c 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.
  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.
  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.
  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.
  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.
  14. ^ Heckmeier PJ, Ruf J, Buhrke D, Janković BG, Hamm P (September 2022). "Signal Propagation Within the MCL-1/BIM Protein Complex". Journal of Molecular Biology. 434 (17): 167499. doi:10.1016/j.jmb.2022.167499. PMID 35189130.