| General information | | DisProt: | DP00643_A002 | | Name: | Bcl-2-like protein 11 [Isoform BimL] | | Synonym(s): | B2L11_HUMAN
Bcl2-interacting mediator of cell death
Bcl-2-like protein 11 [Isoform Bim(L)]
| | First appeared in release: | Release 5.1 (05/28/2010) | | UniProt: | O43521-2 | | UniGene: | Hs.469658 | | SwissProt: | B2L11_HUMAN | | TrEMBL: | | | NCBI (GI): | 5729740 | | Source organism: | Homo sapiens (Human) | | Sequence length: | 138 | | Percent disordered: | 80% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MAKQPSDVSS ECDREGRQLQ PAERPPQLRP GAPTSLQTEP QDRSPAPMSC DKSTQTPSPP - 60
CQAFNHYLSA MASMRQAEPA DMRPEIWIAQ ELRRIGDEFN AYYARRVFLN NYQAAEDHPR - 120
MVILRLLRYI VRLVWRMH
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| Functional narrative |
Induces apoptosis. Isoform BimL is more potent than isoform BimEL. Isoform Bim-alpha1, isoform Bim-alpha2 and isoform Bim-alpha3 induce apoptosis, although less potent than the isoforms BimEL, BimL and BimS. Isoform Bim-gamma induces apoptosis.
Forms heterodimers with a number of antiapoptotic Bcl-2 proteins including MCL1, BCL2, BCL2L1 isoform Bcl-X(L), BCL2A1/BFL-1, and BHRF1. Does not heterodimerize with proapoptotic proteins such as BAD, BOK, BAX or BAK
Belongs to the Bcl-2 family. (UniProt). Isoform Bim(L) is missing aa 42-101 of UniProt's canonical sequence, Isoform Bim(EL)
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered | | Name: | BimL-C27 | | Location: | 1 - 111 | | Length: | 111 | | Region sequence: |
MAKQPSDVSSECDREGRQLQPAERPPQLRPGAPTSLQTEPQDRSPAPMSCDKSTQTPSPP
CQAFNHYLSAMASMRQAEPADMRPEIWIAQELRRIGDEFNAYYARRVFLNN | | Modification type: | Fragment
| | PDB: | | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | | | Functional subclasses: | Apoptosis Regulation
Protein-protein binding
| Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV (pH: 6.7; Olis (spectro- polarimeter ); protein concentration range (10-50 uM); sodium phosphate (buffer) 5 mM; resolution 1 nm; integration time 3 s; pathlength cuvettes (1-2 mm))
- Analytical ultracentrifugation (293 K; pH: 7.4; Optima XL-A (analytical ultracentrifuge); phosphate-buffered saline (buffer) 400 uM; protein (sample) 0.8 mg/mL; speed 50000 rpm)
- Size exclusion/gel filtration chromatography (pH: 7.4; fraction 500 uL; PBS; Superdex S200 column 20 mL)
- Nuclear magnetic resonance (NMR) (298 K; pH: 6.7; Bruker DRX-600 (spectrometer); NaCl 70 mM; protein (sample) 0.5 mM; sodium azide (in H2O:2H2O (95:5)) 0.04 %; sodium phosphate (buffer) 50 mM; TCEP 20 mM)
| References:
- Hinds MG, Smits C, Fredericks-Short R, Risk JM, Bailey M, Huang DC, Day CL. "Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets." Cell Death Differ. 2006. PubMed: 16645638
| Comments:
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| References |
- Hinds MG, Smits C, Fredericks-Short R, Risk JM, Bailey M, Huang DC, Day CL. "Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets." Cell Death Differ. 2006. PubMed: 16645638
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