UniProtKB - O43521 (B2L11_HUMAN)
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Bcl-2-like protein 11
BCL2L11
Functioni
GO - Molecular functioni
- dynein complex binding Source: Ensembl
- microtubule binding Source: GO_Central
- protein heterodimerization activity Source: Ensembl
GO - Biological processi
- activation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
- apoptotic process Source: UniProtKB
- apoptotic process involved in embryonic digit morphogenesis Source: Ensembl
- B cell apoptotic process Source: Ensembl
- B cell homeostasis Source: Ensembl
- brain development Source: Ensembl
- cell-matrix adhesion Source: Ensembl
- cellular process regulating host cell cycle in response to virus Source: Ensembl
- developmental pigmentation Source: Ensembl
- ear development Source: Ensembl
- extrinsic apoptotic signaling pathway in absence of ligand Source: Ensembl
- intrinsic apoptotic signaling pathway in response to DNA damage Source: MGI
- in utero embryonic development Source: Ensembl
- kidney development Source: Ensembl
- male gonad development Source: Ensembl
- mammary gland development Source: Ensembl
- myeloid cell homeostasis Source: Ensembl
- odontogenesis of dentin-containing tooth Source: Ensembl
- positive regulation of apoptotic process Source: UniProtKB
- positive regulation of apoptotic process by virus Source: Ensembl
- positive regulation of cell cycle Source: Ensembl
- positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
- positive regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway Source: ParkinsonsUK-UCL
- positive regulation of fibroblast apoptotic process Source: UniProtKB
- positive regulation of intrinsic apoptotic signaling pathway Source: UniProtKB
- positive regulation of IRE1-mediated unfolded protein response Source: ParkinsonsUK-UCL
- positive regulation of neuron apoptotic process Source: Ensembl
- positive regulation of protein homooligomerization Source: BHF-UCL
- positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway Source: Reactome
- positive regulation of release of cytochrome c from mitochondria Source: UniProtKB
- post-embryonic animal organ morphogenesis Source: Ensembl
- protein insertion into mitochondrial membrane involved in apoptotic signaling pathway Source: Reactome
- regulation of developmental pigmentation Source: Ensembl
- regulation of organ growth Source: Ensembl
- response to endoplasmic reticulum stress Source: UniProtKB
- spermatogenesis Source: Ensembl
- spleen development Source: Ensembl
- T cell homeostasis Source: Ensembl
- thymocyte apoptotic process Source: Ensembl
- thymus development Source: Ensembl
- tube formation Source: Ensembl
Keywordsi
| Biological process | Apoptosis |
Enzyme and pathway databases
| Reactomei | R-HSA-111446. Activation of BIM and translocation to mitochondria. R-HSA-111453. BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members. R-HSA-193648. NRAGE signals death through JNK. R-HSA-6802952. Signaling by BRAF and RAF fusions. R-HSA-8862803. Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease models. R-HSA-8952158. RUNX3 regulates BCL2L11 (BIM) transcription. |
| SIGNORi | O43521. |
Protein family/group databases
| TCDBi | 8.A.69.1.1. the pro-apoptotic bcl-2-family protein bim (bim) family. |
Names & Taxonomyi
| Protein namesi | Recommended name: Bcl-2-like protein 11Short name: Bcl2-L-11 Alternative name(s): Bcl2-interacting mediator of cell death |
| Gene namesi | Name:BCL2L11 Synonyms:BIM |
| Organismi | Homo sapiens (Human) |
| Taxonomic identifieri | 9606 [NCBI] |
| Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
| Proteomesi |
|
Organism-specific databases
| HGNCi | HGNC:994. BCL2L11. |
Subcellular locationi
- Endomembrane system By similarity; Peripheral membrane protein By similarity
Note: Associated with intracytoplasmic membranes.By similarity
- Mitochondrion
Note: Translocates from microtubules to motochondria on loss of cell adherence.
GO - Cellular componenti
- Bcl-2 family protein complex Source: Ensembl
- BIM-BCL-2 complex Source: UniProtKB
- BIM-BCL-xl complex Source: UniProtKB
- cytoplasmic dynein complex Source: Ensembl
- cytosol Source: UniProtKB
- endomembrane system Source: UniProtKB-SubCell
- extrinsic component of membrane Source: Ensembl
- mitochondrial outer membrane Source: Reactome
- mitochondrion Source: GO_Central
Keywords - Cellular componenti
Membrane, MitochondrionPathology & Biotechi
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Mutagenesisi | 156 | G → A: Retains the ability to induce apoptosis. Abolishes interaction with BAX; in isoform Bim-alpha3 and isoform BimS. No effect on interaction with BCL2. 2 Publications | 1 | |
| Mutagenesisi | 156 | G → E: Abolishes induction of apoptosis. Abolishes interaction with BAX and BCL2; in isoform Bim-alpha3 and isoform BimS. Loses the ability to induce the conformationally active form of BAX. 2 Publications | 1 | |
| Mutagenesisi | 160 | N → A: Retains the ability to induce apoptosis. Abolishes interaction with BCL2; in isoform Bim-alpha3 and isoform BimS. No effect on interaction with BAX. 1 Publication | 1 |
Organism-specific databases
| DisGeNETi | 10018. |
| OpenTargetsi | ENSG00000153094. |
| PharmGKBi | PA25305. |
Chemistry databases
| ChEMBLi | CHEMBL5777. |
Polymorphism and mutation databases
| BioMutai | BCL2L11. |
PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| ChainiPRO_0000143109 | 1 – 198 | Bcl-2-like protein 11Add BLAST | 198 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Modified residuei | 69 | Phosphoserine; by MAPK1 Publication | 1 | |
| Modified residuei | 77 | PhosphoserineBy similarity | 1 | |
| Modified residuei | 87 | PhosphoserineBy similarity | 1 | |
| Modified residuei | 94 | PhosphoserineCombined sources | 1 |
Post-translational modificationi
Keywords - PTMi
Phosphoprotein, Ubl conjugationProteomic databases
| MaxQBi | O43521. |
| PaxDbi | O43521. |
| PeptideAtlasi | O43521. |
| PRIDEi | O43521. |
PTM databases
| iPTMneti | O43521. |
| PhosphoSitePlusi | O43521. |
Miscellaneous databases
| PMAP-CutDBi | O43521. |
Expressioni
Tissue specificityi
Inductioni
Gene expression databases
| Bgeei | ENSG00000153094. |
| ExpressionAtlasi | O43521. baseline and differential. |
| Genevisiblei | O43521. HS. |
Organism-specific databases
| HPAi | CAB026332. |
Interactioni
Subunit structurei
Binary interactionsi
GO - Molecular functioni
- dynein complex binding Source: Ensembl
- microtubule binding Source: GO_Central
- protein heterodimerization activity Source: Ensembl
Protein-protein interaction databases
| BioGridi | 115335. 56 interactors. |
| DIPi | DIP-29185N. |
| IntActi | O43521. 39 interactors. |
| MINTi | MINT-1664421. |
| STRINGi | 9606.ENSP00000376943. |
Chemistry databases
| BindingDBi | O43521. |
Structurei
Secondary structure
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Beta strandi | 112 – 115 | Combined sources | 4 | |
| Helixi | 143 – 159 | Combined sources | 17 | |
| Turni | 160 – 163 | Combined sources | 4 |
3D structure databases
| Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 1F95 | NMR | - | C/D | 108-116 | [»] | |
| 2K7W | NMR | - | B | 145-164 | [»] | |
| 2NL9 | X-ray | 1.55 | B | 141-166 | [»] | |
| 2V6Q | X-ray | 2.70 | B | 141-166 | [»] | |
| 2VM6 | X-ray | 2.20 | B | 141-165 | [»] | |
| 2WH6 | X-ray | 1.50 | B | 141-166 | [»] | |
| 2YQ6 | X-ray | 1.80 | B | 147-164 | [»] | |
| 2YQ7 | X-ray | 1.90 | B | 147-164 | [»] | |
| 3D7V | X-ray | 2.03 | B | 141-166 | [»] | |
| 3FDL | X-ray | 1.78 | B | 141-166 | [»] | |
| 3IO8 | X-ray | 2.30 | B/D | 141-166 | [»] | |
| 3IO9 | X-ray | 2.40 | B | 141-166 | [»] | |
| 3KJ0 | X-ray | 1.70 | B | 143-165 | [»] | |
| 3KJ1 | X-ray | 1.94 | B | 143-163 | [»] | |
| 3KJ2 | X-ray | 2.35 | B | 143-163 | [»] | |
| 4A1U | X-ray | 1.54 | B | 146-163 | [»] | |
| 4A1W | X-ray | 2.50 | P/Q/R/S | 146-163 | [»] | |
| 4B4S | X-ray | 1.90 | B | 141-166 | [»] | |
| 4D2M | X-ray | 2.10 | B/D | 141-166 | [»] | |
| 4QVF | X-ray | 1.53 | B | 141-166 | [»] | |
| 4UF3 | X-ray | 2.70 | B | 141-166 | [»] | |
| 4YJ4 | X-ray | 2.10 | B | 146-165 | [»] | |
| 4ZIE | X-ray | 1.80 | C | 141-166 | [»] | |
| 4ZIF | X-ray | 2.40 | B | 141-160 | [»] | |
| 4ZIH | X-ray | 2.50 | B | 141-160 | [»] | |
| 5AGW | X-ray | 2.69 | C/D | 146-166 | [»] | |
| 5AGX | X-ray | 2.24 | C/D | 146-166 | [»] | |
| 5C3G | X-ray | 2.45 | B | 146-166 | [»] | |
| ProteinModelPortali | O43521. | |||||
| SMRi | O43521. | |||||
| ModBasei | Search... | |||||
| MobiDBi | Search... | |||||
Miscellaneous databases
| EvolutionaryTracei | O43521. |
Family & Domainsi
Motif
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Motifi | 148 – 162 | BH3Add BLAST | 15 |
Domaini
Sequence similaritiesi
Phylogenomic databases
| eggNOGi | ENOG410IZKS. Eukaryota. ENOG410Y8GB. LUCA. |
| GeneTreei | ENSGT00390000003178. |
| InParanoidi | O43521. |
| KOi | K16341. |
| OMAi | AEDHPQM. |
| OrthoDBi | EOG091G0XD3. |
| PhylomeDBi | O43521. |
| TreeFami | TF335898. |
Family and domain databases
| InterProi | View protein in InterPro IPR014771. Apoptosis_Bim_N. IPR017288. Bcl-2-like_11. IPR015040. Bcl-x_interacting_BH3_dom. |
| Pfami | View protein in Pfam PF08945. Bclx_interact. 1 hit. PF06773. Bim_N. 1 hit. |
| PIRSFi | PIRSF037827. Bcl-2-like_p11. 1 hit. |
Sequences (20)i
Sequence statusi: Complete.
This entry describes 20 isoformsi produced by alternative splicing. AlignAdd to basket
This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
10 20 30 40 50
MAKQPSDVSS ECDREGRQLQ PAERPPQLRP GAPTSLQTEP QGNPEGNHGG
60 70 80 90 100
EGDSCPHGSP QGPLAPPASP GPFATRSPLF IFMRRSSLLS RSSSGYFSFD
110 120 130 140 150
TDRSPAPMSC DKSTQTPSPP CQAFNHYLSA MASMRQAEPA DMRPEIWIAQ
160 170 180 190
ELRRIGDEFN AYYARRVFLN NYQAAEDHPR MVILRLLRYI VRLVWRMH
The sequence of this isoform differs from the canonical sequence as follows:
42-101: Missing.
The sequence of this isoform differs from the canonical sequence as follows:
42-131: Missing.
The sequence of this isoform differs from the canonical sequence as follows:
167-198: VFLNNYQAAEDHPRMVILRLLRYIVRLVWRMH → LEK
The sequence of this isoform differs from the canonical sequence as follows:
42-101: Missing.
167-198: VFLNNYQAAEDHPRMVILRLLRYIVRLVWRMH → LEK
The sequence of this isoform differs from the canonical sequence as follows:
42-131: Missing.
167-198: VFLNNYQAAEDHPRMVILRLLRYIVRLVWRMH → LEK
The sequence of this isoform differs from the canonical sequence as follows:
42-131: Missing.
167-198: VFLNNYQAAEDHPRMVILRLLRYIVRLVWRMH → LAKLLASST
The sequence of this isoform differs from the canonical sequence as follows:
167-198: VFLNNYQAAEDHPRMVILRLLRYIVRLVWRMH → MPLPPD
The sequence of this isoform differs from the canonical sequence as follows:
42-131: Missing.
167-198: VFLNNYQAAEDHPRMVILRLLRYIVRLVWRMH → MPLPPD
The sequence of this isoform differs from the canonical sequence as follows:
133-135: SMR → NWD
136-198: Missing.
The sequence of this isoform differs from the canonical sequence as follows:
132-135: ASMR → GIFE
136-198: Missing.
The sequence of this isoform differs from the canonical sequence as follows:
42-75: GNPEGNHGGEGDSCPHGSPQGPLAPPASPGPFAT → VSLCHPGWSALVRSWLTATSNSQVQAVLLPQPPK
The sequence of this isoform differs from the canonical sequence as follows:
43-44: NP → IF
45-198: Missing.
The sequence of this isoform differs from the canonical sequence as follows:
132-140: ASMRQAEPA → VREIEEVVV
141-198: Missing.
The sequence of this isoform differs from the canonical sequence as follows:
42-101: Missing.
132-135: ASMR → GIFE
136-198: Missing.
The sequence of this isoform differs from the canonical sequence as follows:
42-101: Missing.
132-140: ASMRQAEPA → VREIEEVVV
141-198: Missing.
The sequence of this isoform differs from the canonical sequence as follows:
42-101: Missing.
132-198: ASMRQAEPAD...YIVRLVWRMH → VVILEDIGDL...TEQLNHKDFS
The sequence of this isoform differs from the canonical sequence as follows:
42-101: Missing.
132-166: Missing.
The sequence of this isoform differs from the canonical sequence as follows:
132-166: Missing.
The sequence of this isoform differs from the canonical sequence as follows:
42-166: Missing.
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Sequence conflicti | 33 | P → L in BAF83066 (PubMed:14702039).Curated | 1 |
Alternative sequence
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Alternative sequenceiVSP_042865 | 42 – 166 | Missing in isoform BimA. 1 PublicationAdd BLAST | 125 | |
| Alternative sequenceiVSP_035608 | 42 – 131 | Missing in isoform BimS, isoform Bim-alpha3, isoform Bim-alpha6 and isoform Bim-alpha4. 3 PublicationsAdd BLAST | 90 | |
| Alternative sequenceiVSP_000535 | 42 – 101 | Missing in isoform BimABC, isoform BimL, isoform Bim-alpha2, isoform Bim-gamma, isoform Bim-beta6 and isoform Bim-beta7. 6 PublicationsAdd BLAST | 60 | |
| Alternative sequenceiVSP_035609 | 42 – 75 | GNPEG…GPFAT → VSLCHPGWSALVRSWLTATS NSQVQAVLLPQPPK in isoform Bim-beta3. 1 PublicationAdd BLAST | 34 | |
| Alternative sequenceiVSP_035610 | 43 – 44 | NP → IF in isoform Bim-beta4. 1 Publication | 2 | |
| Alternative sequenceiVSP_035611 | 45 – 198 | Missing in isoform Bim-beta4. 1 PublicationAdd BLAST | 154 | |
| Alternative sequenceiVSP_035612 | 132 – 198 | ASMRQ…VWRMH → VVILEDIGDLSLCFGFIFTG LDLYGHHHSQDTEQLNHKDF S in isoform Bim-gamma. 1 PublicationAdd BLAST | 67 | |
| Alternative sequenceiVSP_042866 | 132 – 166 | Missing in isoform BimAC and isoform BimABC. 1 PublicationAdd BLAST | 35 | |
| Alternative sequenceiVSP_035613 | 132 – 140 | ASMRQAEPA → VREIEEVVV in isoform Bim-beta5 and isoform Bim-beta7. 1 Publication | 9 | |
| Alternative sequenceiVSP_035614 | 132 – 135 | ASMR → GIFE in isoform Bim-beta2 and isoform Bim-beta6. 2 Publications | 4 | |
| Alternative sequenceiVSP_035615 | 133 – 135 | SMR → NWD in isoform Bim-beta1. 1 Publication | 3 | |
| Alternative sequenceiVSP_035616 | 136 – 198 | Missing in isoform Bim-beta1, isoform Bim-beta2 and isoform Bim-beta6. 2 PublicationsAdd BLAST | 63 | |
| Alternative sequenceiVSP_035617 | 141 – 198 | Missing in isoform Bim-beta5 and isoform Bim-beta7. 1 PublicationAdd BLAST | 58 | |
| Alternative sequenceiVSP_035620 | 167 – 198 | VFLNN…VWRMH → LEK in isoform Bim-alpha1, isoform Bim-alpha2 and isoform Bim-alpha3. 4 PublicationsAdd BLAST | 32 | |
| Alternative sequenceiVSP_035618 | 167 – 198 | VFLNN…VWRMH → LAKLLASST in isoform Bim-alpha4. 1 PublicationAdd BLAST | 32 | |
| Alternative sequenceiVSP_035619 | 167 – 198 | VFLNN…VWRMH → MPLPPD in isoform Bim-alpha5 and isoform Bim-alpha6. 1 PublicationAdd BLAST | 32 |
Sequence databases
Genome annotation databases
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:| 100% | UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry. |
| 90% | UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence). |
| 50% | UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster. |
Entry informationi
| Entry namei | B2L11_HUMAN | |
| Accessioni | O43521Primary (citable) accession number: O43521 Secondary accession number(s): A8K2W2 Q8WYM1 | |
| Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 18, 2001 |
| Last sequence update: | June 1, 1998 | |
| Last modified: | June 7, 2017 | |
| This is version 168 of the entry and version 1 of the sequence. See complete history. | ||
| Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | |
Miscellaneousi
Keywords - Technical termi
3D-structure, Complete proteome, Reference proteomeDocuments
- Human chromosome 2
Human chromosome 2: entries, gene names and cross-references to MIM - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
