Bcl-2-like protein 11 - Mus musculus (Mouse)

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O54918 (B2L11_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 123. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Bcl-2-like protein 11
Short name=Bcl2-L-11

Alternative name(s):
Bcl2-interacting mediator of cell death

Gene names

Name:	Bcl2l11
Synonyms:	Bim

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	196 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Induces apoptosis and anoikis. The isoforms vary in cytotoxicity with isoform BimS being the most potent and isoform BimEL being the least potent. Ref.1
Subunit structure	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 or BAK By similarity. Interacts with Bax (in vitro). Identified in a complex containing BCL2L11, DYNLL1 and BCL2L1 isoform Bcl-X(L). Interacts with YWHAZ. When phosphorylated, interacts with TRIM2; this interaction is associated with ubiquitination and degradation. Ref.6 Ref.7
Subcellular location	Membrane; Peripheral membrane protein. Mitochondrion By similarity. Note: Associated with intracytoplasmic membranes. Ref.1
Tissue specificity	Expressed in a number of B- and T-lymphoid cell lines. Ref.1
Induction	By ER stress. Ref.5
Domain	The BH3 motif is required for Bcl-2 binding and cytotoxicity.
Post-translational modification	Phosphorylation at Ser-65 by MAPK1/MAPK3 induces interaction with TRIM2, followed by ubiquitination. Ubiquitinated by TRIM2 following phosphorylation by MAPK1/MAPK3, leading to degradation by the proteasome. Ref.6
Sequence similarities	Belongs to the Bcl-2 family.

Ontologies

Keywords
Biological process	Apoptosis
Cellular component	Membrane Mitochondrion
Coding sequence diversity	Alternative splicing
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	B cell apoptotic process Inferred from genetic interaction PubMed 16055554. Source: MGI B cell homeostasis Inferred from mutant phenotype PubMed 16055554 PubMed 16270031. Source: MGI T cell homeostasis Inferred from mutant phenotype PubMed 16270031. Source: MGI activation of cysteine-type endopeptidase activity involved in apoptotic process Inferred from electronic annotation. Source: Compara brain development Inferred from electronic annotation. Source: Compara cell-matrix adhesion Inferred from mutant phenotype PubMed 17276340. Source: MGI cellular process regulating host cell cycle in response to virus Inferred from direct assay PubMed 15231831. Source: MGI developmental pigmentation Inferred from genetic interaction PubMed 11709185. Source: MGI ear development Inferred from genetic interaction PubMed 11709185. Source: MGI in utero embryonic development Inferred from genetic interaction PubMed 16282979. Source: MGI induction of apoptosis Inferred from direct assay PubMed 15231831. Source: MGI kidney development Inferred from genetic interaction PubMed 11709185. Source: MGI male gonad development Inferred from genetic interaction PubMed 16270031. Source: MGI mammary gland development Inferred from mutant phenotype PubMed 17276340. Source: MGI myeloid cell homeostasis Inferred from genetic interaction PubMed 15967824. Source: MGI odontogenesis of dentin-containing tooth Inferred from genetic interaction PubMed 15967824. Source: MGI positive regulation of cell cycle Inferred from mutant phenotype PubMed 17705137. Source: MGI positive regulation of intrinsic apoptotic signaling pathway Inferred from electronic annotation. Source: Compara positive regulation of neuron apoptotic process Inferred from direct assay PubMed 15231831. Source: MGI positive regulation of protein homooligomerization Inferred from electronic annotation. Source: Compara positive regulation of release of cytochrome c from mitochondria Inferred from electronic annotation. Source: Compara post-embryonic organ morphogenesis Inferred from mutant phenotype PubMed 17276340. Source: MGI regulation of developmental pigmentation Inferred from genetic interaction PubMed 15818405. Source: MGI regulation of organ growth Inferred from mutant phenotype PubMed 17276340. Source: MGI response to endoplasmic reticulum stress Inferred from direct assay Ref.5. Source: UniProtKB spermatogenesis Inferred from genetic interaction PubMed 16270031. Source: MGI spleen development Inferred from genetic interaction PubMed 15818405. Source: MGI thymus development Inferred from genetic interaction PubMed 15818405. Source: MGI tube formation Inferred from mutant phenotype PubMed 17276340. Source: MGI
Cellular_component	BIM-BCL-2 complex Inferred from electronic annotation. Source: Compara BIM-BCL-xl complex Inferred from electronic annotation. Source: Compara extrinsic to membrane Inferred from direct assay PubMed 15136728. Source: MGI microtubule Inferred from electronic annotation. Source: Compara mitochondrion Inferred from direct assay PubMed 15136728. Source: MGI
Molecular_function	microtubule binding Inferred from direct assay PubMed 16832056. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DYNLRB1	Q9NP97	3	EBI-526080,EBI-372128	From a different organism.
GNB2L1	P63244	2	EBI-526076,EBI-296739	From a different organism.
Mcl1	P97287	3	EBI-526067,EBI-707292

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform BimEL (identifier: O54918-1) 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.

Isoform BimL (identifier: O54918-2) The sequence of this isoform differs from the canonical sequence as follows: 42-97: Missing.

Isoform BimS (identifier: O54918-3) The sequence of this isoform differs from the canonical sequence as follows: 42-127: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 196

196

Bcl-2-like protein 11

PRO_0000143110

Regions

Motif

146 – 160

BH3

Amino acid modifications

Modified residue

Phosphoserine; by MAPK Ref.6

Modified residue

Phosphoserine Ref.4

Natural variations

Alternative sequence

42 – 127

Missing in isoform BimS.

VSP_000537

Alternative sequence

42 – 97

Missing in isoform BimL.

VSP_000536

Experimental info

Mutagenesis

S → A: Loss of TRIM2-binding; when associated with A-65 and A-73. Ref.6

Mutagenesis

S → A: Loss of TRIM2-binding; when associated with A-55 and A-73. Ref.6

Mutagenesis

S → A: Loss of TRIM2-binding; when associated with A-55 and A-65. Ref.6

Secondary structure

196

Helix Strand Turn

Details...

Sequences

Sequence		Length	Mass (Da)
Isoform BimEL [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 531C176E5F1AC9AA Show »	FASTA	196	22,067
10 20 30 40 50 60 MAKQPSDVSS ECDREGGQLQ PAERPPQLRP GAPTSLQTEP QGNPDGEGDR CPHGSPQGPL 70 80 90 100 110 120 APPASPGPFA TRSPLFIFVR RSSLLSRSSS GYFSFDTDRS PAPMSCDKST QTPSPPCQAF 130 140 150 160 170 180 NHYLSAMASI RQSQEEPEDL RPEIRIAQEL RRIGDEFNET YTRRVFANDY REAEDHPQMV 190 ILQLLRFIFR LVWRRH « Hide
Isoform BimL [UniParc]. Checksum: B127B40A190DA923 Show »	FASTA	140	16,205
10 20 30 40 50 60 MAKQPSDVSS ECDREGGQLQ PAERPPQLRP GAPTSLQTEP QDRSPAPMSC DKSTQTPSPP 70 80 90 100 110 120 CQAFNHYLSA MASIRQSQEE PEDLRPEIRI AQELRRIGDE FNETYTRRVF ANDYREAEDH 130 140 PQMVILQLLR FIFRLVWRRH « Hide
Isoform BimS [UniParc]. Checksum: 67AB421AC1E4D2CA Show »	FASTA	110	12,954
10 20 30 40 50 60 MAKQPSDVSS ECDREGGQLQ PAERPPQLRP GAPTSLQTEP QASIRQSQEE PEDLRPEIRI 70 80 90 100 110 AQELRRIGDE FNETYTRRVF ANDYREAEDH PQMVILQLLR FIFRLVWRRH « Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Bim: a novel member of the Bcl-2 family that promotes apoptosis." O'Connor L., Strasser A., O'Reilly L.A., Hausmann G., Adams J.M., Cory S., Huang D.C.S. EMBO J. 17:384-395(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, ALTERNATIVE SPLICING.
[2]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BIMEL). Strain: FVB/N. Tissue: Mammary tumor.
[4]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, MASS SPECTROMETRY. Tissue: Melanoma.
[5]	"Neuronal apoptosis induced by endoplasmic reticulum stress is regulated by ATF4-CHOP-mediated induction of the Bcl-2 homology 3-only member PUMA." Galehdar Z., Swan P., Fuerth B., Callaghan S.M., Park D.S., Cregan S.P. J. Neurosci. 30:16938-16948(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION.
[6]	"Identification of a novel Bcl-2-interacting mediator of cell death (Bim) E3 ligase, tripartite motif-containing protein 2 (TRIM2), and its role in rapid ischemic tolerance-induced neuroprotection." Thompson S., Pearson A.N., Ashley M.D., Jessick V., Murphy B.M., Gafken P., Henshall D.C., Morris K.T., Simon R.P., Meller R. J. Biol. Chem. 286:19331-19339(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DYNLL1; TRIM2 AND YWHAZ, UBIQUITINATION, PHOSPHORYLATION AT SER-65, MUTAGENESIS OF SER-55; SER-65 AND SER-73.
[7]	"The structure of a Bcl-xL/Bim fragment complex: implications for Bim function." Liu X., Dai S., Zhu Y., Marrack P., Kappler J.W. Immunity 19:341-352(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 139-171 IN COMPLEX WITH BCL2L1 ISOFORM BCL-XL, IDENTIFICATION IN A COMPLEX WITH DYNLL1 AND BCL-XL, INTERACTION WITH BAX.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF032459 mRNA. Translation: AAC40029.1.
AF032460 mRNA. Translation: AAC40030.1.
AF032461 mRNA. Translation: AAC40031.1.
AL805950 Genomic DNA. Translation: CAM14745.1.
BC019556 mRNA. Translation: AAH19556.1.

IPI

IPI00119799.
IPI00225688.
IPI00225689.

RefSeq

NP_033884.1. NM_009754.3.
NP_997563.1. NM_207680.2.
NP_997564.1. NM_207681.2.

UniGene

Mm.141083.
Mm.453214.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1PQ1	X-ray	1.65	B	139-171	[»]

DisProt

DP00518.

ProteinModelPortal

O54918.

SMR

O54918. Positions 139-171.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29214N.

IntAct

O54918. 13 interactions.

MINT

MINT-89451.

PTM databases

PhosphoSite

O54918.

Proteomic databases

PaxDb

O54918.

PRIDE

O54918.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000019281; ENSMUSP00000019281; ENSMUSG00000027381.
ENSMUST00000103210; ENSMUSP00000099499; ENSMUSG00000027381.
ENSMUST00000103211; ENSMUSP00000099500; ENSMUSG00000027381.
ENSMUST00000110341; ENSMUSP00000105970; ENSMUSG00000027381.

GeneID

12125.

KEGG

mmu:12125.

UCSC

uc008mgk.1. mouse.

Organism-specific databases

CTD

10018.

MGI

MGI:1197519. Bcl2l11.

Phylogenomic databases

eggNOG

NOG40262.

GeneTree

ENSGT00390000003178.

HOGENOM

HOG000231637.

InParanoid

O54918.

K16341.

OMA

IRLVWRM.

OrthoDB

EOG4C87TR.

Gene expression databases

ArrayExpress

O54918.

Bgee

O54918.

CleanEx

MM_BCL2L11.

Genevestigator

O54918.

GermOnline

ENSMUSG00000027381. Mus musculus.

Family and domain databases

InterPro

IPR014771. Apoptosis_Bim_N.
IPR017288. Bcl-2-like_11.
IPR015040. Bcl-x_interacting.
[Graphical view]

PANTHER

PTHR12044:SF1. PTHR12044:SF1. 1 hit.

Pfam

PF08945. Bclx_interact. 1 hit.
PF06773. Bim_N. 1 hit.
[Graphical view]

PIRSF

PIRSF037827. Bcl-2-like_p11. 1 hit.

PROSITE

PS01259. BH3. False negative.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

O54918.

NextBio

280451.

SOURCE

Search...

Entry information

Entry name

B2L11_MOUSE

Accession

Primary (citable) accession number: O54918
Secondary accession number(s): A2ALQ6, O54919, O54920

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 18, 2001
Last sequence update:	June 1, 1998
Last modified:	May 1, 2013
This is version 123 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) 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

Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Alternative products

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents