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O43521 (B2L11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length198 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Induces apoptosis and anoikis. Isoform BimL is more potent than isoform BimEL. Isoform Bim-alpha1, isoform Bim-alpha2 and isoform Bim-alpha3 induce apoptosis, although less potent than isoform BimEL, isoform BimL and isoform BimS. Isoform Bim-gamma induces apoptosis. Isoform Bim-alpha3 induces apoptosis possibly through a caspase-mediated pathway. Isoform BimAC and isoform BimABC lack the ability to induce apoptosis. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.11

Subunit structure

Forms heterodimers with a number of antiapoptotic Bcl-2 proteins including MCL1, BCL2, BCL2L1 isoform Bcl-X(L) BCL2A1/BFL-1, BHRF1, and BCLW. Isoform BimS and isoform Bim-alpha3 interact with BAX; this interaction induces the conformationally active form of BAX. Does not heterodimerize with proapoptotic proteins such as BAD, BOK or BAK. Interacts with DYNLL1 and YWHAZ. When phosphorylated, interacts with TRIM2; this interaction is associated with ubiquitination and degradation. Interacts with MCL1; may sequester BCL2L11 to prevent its pro-apoptotic activity. Ref.4 Ref.14

Subcellular location

Endomembrane system; Peripheral membrane protein By similarity. Note: Associated with intracytoplasmic membranes By similarity. Ref.2 Ref.3 Ref.11

Isoform BimEL: Mitochondrion Ref.2 Ref.3 Ref.11. Note: Translocates from microtubules to motochondria on loss of cell adherence. Ref.2 Ref.3 Ref.11

Isoform BimL: Mitochondrion Ref.2 Ref.3 Ref.11.

Isoform BimS: Mitochondrion Ref.2 Ref.3 Ref.11.

Isoform Bim-alpha1: Mitochondrion Ref.2 Ref.3 Ref.11.

Tissue specificity

Isoform BimEL, isoform BimL and isoform BimS are the predominant isoforms and are ubiquitously expressed with a tissue-specific variation. Isoform Bim-gamma is most abundantly expressed in small intestine and colon, and in lower levels in spleen, prostate, testis, heart, liver and kidney. Ref.3

Induction

By ER stress in a DDIT3/CHOP-dependent manner. Ref.15

Domain

The BH3 motif is required for Bcl-2 binding and cytotoxicity.

Post-translational modification

Phosphorylation at Ser-69 by MAPK1/MAPK3 induces interaction with TRIM2, followed by polyubiquitination.

Ubiquitinated by TRIM2 following phosphorylation by MAPK1/MAPK3, leading to degradation by the proteasome By similarity. Ref.11

Sequence similarities

Belongs to the Bcl-2 family.

Ontologies

Keywords
   Biological processApoptosis
   Cellular componentMembrane
Mitochondrion
   Coding sequence diversityAlternative splicing
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processB cell apoptotic process

Inferred from electronic annotation. Source: Ensembl

B cell homeostasis

Inferred from electronic annotation. Source: Ensembl

T cell homeostasis

Inferred from electronic annotation. Source: Ensembl

activation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from direct assay PubMed 21671007. Source: UniProtKB

apoptotic process

Traceable author statement PubMed 10381623. Source: UniProtKB

apoptotic process involved in embryonic digit morphogenesis

Inferred from electronic annotation. Source: Ensembl

apoptotic signaling pathway

Traceable author statement. Source: Reactome

brain development

Inferred from electronic annotation. Source: Ensembl

cell-matrix adhesion

Inferred from electronic annotation. Source: Ensembl

cellular process regulating host cell cycle in response to virus

Inferred from electronic annotation. Source: Ensembl

developmental pigmentation

Inferred from electronic annotation. Source: Ensembl

ear development

Inferred from electronic annotation. Source: Ensembl

extrinsic apoptotic signaling pathway in absence of ligand

Inferred from electronic annotation. Source: Ensembl

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

intrinsic apoptotic signaling pathway

Traceable author statement. Source: Reactome

intrinsic apoptotic signaling pathway in response to DNA damage

Inferred from direct assay PubMed 11546872. Source: MGI

kidney development

Inferred from electronic annotation. Source: Ensembl

male gonad development

Inferred from electronic annotation. Source: Ensembl

mammary gland development

Inferred from electronic annotation. Source: Ensembl

myeloid cell homeostasis

Inferred from electronic annotation. Source: Ensembl

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

odontogenesis of dentin-containing tooth

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic process

Inferred from mutant phenotype Ref.12PubMed 21671007. Source: UniProtKB

positive regulation of apoptotic process by virus

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell cycle

Inferred from electronic annotation. Source: Ensembl

positive regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of fibroblast apoptotic process

Inferred from direct assay Ref.4. Source: UniProtKB

positive regulation of intrinsic apoptotic signaling pathway

Inferred from mutant phenotype PubMed 21671007. Source: UniProtKB

positive regulation of mitochondrial membrane permeability involved in apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein homooligomerization

Inferred from direct assay PubMed 21041309. Source: BHF-UCL

positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway

Traceable author statement. Source: Reactome

positive regulation of release of cytochrome c from mitochondria

Inferred from mutant phenotype Ref.12. Source: UniProtKB

post-embryonic organ morphogenesis

Inferred from electronic annotation. Source: Ensembl

regulation of developmental pigmentation

Inferred from electronic annotation. Source: Ensembl

regulation of organ growth

Inferred from electronic annotation. Source: Ensembl

response to endoplasmic reticulum stress

Inferred from direct assay Ref.15. Source: UniProtKB

spermatogenesis

Inferred from electronic annotation. Source: Ensembl

spleen development

Inferred from electronic annotation. Source: Ensembl

thymocyte apoptotic process

Inferred from electronic annotation. Source: Ensembl

thymus development

Inferred from electronic annotation. Source: Ensembl

tube formation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentBIM-BCL-2 complex

Inferred from direct assay PubMed 21671007. Source: UniProtKB

BIM-BCL-xl complex

Inferred from direct assay PubMed 21671007. Source: UniProtKB

cytosol

Inferred from direct assay PubMed 21671007. Source: UniProtKB

endomembrane system

Inferred from electronic annotation. Source: UniProtKB-SubCell

extrinsic component of membrane

Inferred from electronic annotation. Source: Ensembl

mitochondrial outer membrane

Traceable author statement. Source: Reactome

Complete GO annotation...

Alternative products

This entry describes 20 isoforms produced by alternative splicing. [Align] [Select]
Isoform BimEL (identifier: O43521-1)

Also known as: Bim(EL);

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: O43521-2)

Also known as: Bim(L);

The sequence of this isoform differs from the canonical sequence as follows:
     42-101: Missing.
Isoform BimS (identifier: O43521-3)

Also known as: BCL2-like 11 transcript variant 9; Bim(S);

The sequence of this isoform differs from the canonical sequence as follows:
     42-131: Missing.
Isoform Bim-alpha1 (identifier: O43521-4)

Also known as: BimABCD; Bim-ABCD;

The sequence of this isoform differs from the canonical sequence as follows:
     167-198: VFLNNYQAAEDHPRMVILRLLRYIVRLVWRMH → LEK
Isoform Bim-alpha2 (identifier: O43521-5)

Also known as: BimACD; Bim-ACD;

The sequence of this isoform differs from the canonical sequence as follows:
     42-101: Missing.
     167-198: VFLNNYQAAEDHPRMVILRLLRYIVRLVWRMH → LEK
Isoform Bim-alpha3 (identifier: O43521-6)

Also known as: BCL2-like 11 transcript variant 10; BimAD; Bim-AD;

The sequence of this isoform differs from the canonical sequence as follows:
     42-131: Missing.
     167-198: VFLNNYQAAEDHPRMVILRLLRYIVRLVWRMH → LEK
Isoform Bim-alpha4 (identifier: O43521-7)

The sequence of this isoform differs from the canonical sequence as follows:
     42-131: Missing.
     167-198: VFLNNYQAAEDHPRMVILRLLRYIVRLVWRMH → LAKLLASST
Isoform Bim-alpha5 (identifier: O43521-8)

The sequence of this isoform differs from the canonical sequence as follows:
     167-198: VFLNNYQAAEDHPRMVILRLLRYIVRLVWRMH → MPLPPD
Isoform Bim-alpha6 (identifier: O43521-9)

The sequence of this isoform differs from the canonical sequence as follows:
     42-131: Missing.
     167-198: VFLNNYQAAEDHPRMVILRLLRYIVRLVWRMH → MPLPPD
Isoform Bim-beta1 (identifier: O43521-10)

The sequence of this isoform differs from the canonical sequence as follows:
     133-135: SMR → NWD
     136-198: Missing.
Isoform Bim-beta2 (identifier: O43521-11)

The sequence of this isoform differs from the canonical sequence as follows:
     132-135: ASMR → GIFE
     136-198: Missing.
Isoform Bim-beta3 (identifier: O43521-12)

The sequence of this isoform differs from the canonical sequence as follows:
     42-75: GNPEGNHGGEGDSCPHGSPQGPLAPPASPGPFAT → VSLCHPGWSALVRSWLTATSNSQVQAVLLPQPPK
Isoform Bim-beta4 (identifier: O43521-13)

The sequence of this isoform differs from the canonical sequence as follows:
     43-44: NP → IF
     45-198: Missing.
Isoform Bim-beta5 (identifier: O43521-14)

The sequence of this isoform differs from the canonical sequence as follows:
     132-140: ASMRQAEPA → VREIEEVVV
     141-198: Missing.
Isoform Bim-beta6 (identifier: O43521-15)

The sequence of this isoform differs from the canonical sequence as follows:
     42-101: Missing.
     132-135: ASMR → GIFE
     136-198: Missing.
Isoform Bim-beta7 (identifier: O43521-16)

The sequence of this isoform differs from the canonical sequence as follows:
     42-101: Missing.
     132-140: ASMRQAEPA → VREIEEVVV
     141-198: Missing.
Isoform Bim-gamma (identifier: O43521-17)

The sequence of this isoform differs from the canonical sequence as follows:
     42-101: Missing.
     132-198: ASMRQAEPAD...YIVRLVWRMH → VVILEDIGDL...TEQLNHKDFS
Isoform BimABC (identifier: O43521-18)

Also known as: Bim-ABC;

The sequence of this isoform differs from the canonical sequence as follows:
     42-101: Missing.
     132-166: Missing.
Isoform BimAC (identifier: O43521-19)

Also known as: Bim-AC;

The sequence of this isoform differs from the canonical sequence as follows:
     132-166: Missing.
Isoform BimA (identifier: O43521-20)

Also known as: Bim-A;

The sequence of this isoform differs from the canonical sequence as follows:
     42-166: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 198198Bcl-2-like protein 11
PRO_0000143109

Regions

Motif148 – 16215BH3

Amino acid modifications

Modified residue691Phosphoserine; by MAPK Ref.11

Natural variations

Alternative sequence42 – 166125Missing in isoform BimA.
VSP_042865
Alternative sequence42 – 13190Missing in isoform BimS, isoform Bim-alpha3, isoform Bim-alpha6 and isoform Bim-alpha4.
VSP_035608
Alternative sequence42 – 10160Missing in isoform BimABC, isoform BimL, isoform Bim-alpha2, isoform Bim-gamma, isoform Bim-beta6 and isoform Bim-beta7.
VSP_000535
Alternative sequence42 – 7534GNPEG…GPFAT → VSLCHPGWSALVRSWLTATS NSQVQAVLLPQPPK in isoform Bim-beta3.
VSP_035609
Alternative sequence43 – 442NP → IF in isoform Bim-beta4.
VSP_035610
Alternative sequence45 – 198154Missing in isoform Bim-beta4.
VSP_035611
Alternative sequence132 – 19867ASMRQ…VWRMH → VVILEDIGDLSLCFGFIFTG LDLYGHHHSQDTEQLNHKDF S in isoform Bim-gamma.
VSP_035612
Alternative sequence132 – 16635Missing in isoform BimAC and isoform BimABC.
VSP_042866
Alternative sequence132 – 1409ASMRQAEPA → VREIEEVVV in isoform Bim-beta5 and isoform Bim-beta7.
VSP_035613
Alternative sequence132 – 1354ASMR → GIFE in isoform Bim-beta2 and isoform Bim-beta6.
VSP_035614
Alternative sequence133 – 1353SMR → NWD in isoform Bim-beta1.
VSP_035615
Alternative sequence136 – 19863Missing in isoform Bim-beta1, isoform Bim-beta2 and isoform Bim-beta6.
VSP_035616
Alternative sequence141 – 19858Missing in isoform Bim-beta5 and isoform Bim-beta7.
VSP_035617
Alternative sequence167 – 19832VFLNN…VWRMH → LEK in isoform Bim-alpha1, isoform Bim-alpha2 and isoform Bim-alpha3.
VSP_035620
Alternative sequence167 – 19832VFLNN…VWRMH → LAKLLASST in isoform Bim-alpha4.
VSP_035618
Alternative sequence167 – 19832VFLNN…VWRMH → MPLPPD in isoform Bim-alpha5 and isoform Bim-alpha6.
VSP_035619

Experimental info

Mutagenesis1561G → A: Retains the ability to induce apoptosis. Abolishes interaction with BAX; in isoform Bim-alpha3 and isoform BimS. No effect on interaction with BCL2. Ref.4 Ref.12
Mutagenesis1561G → 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. Ref.4 Ref.12
Mutagenesis1601N → A: Retains the ability to induce apoptosis. Abolishes interaction with BCL2; in isoform Bim-alpha3 and isoform BimS. No effect on interaction with BAX. Ref.4
Sequence conflict331P → L in BAF83066. Ref.7

Secondary structure

... 198
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform BimEL (Bim(EL)) [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: D75735E469CA6997

FASTA19822,171
        10         20         30         40         50         60 
MAKQPSDVSS ECDREGRQLQ PAERPPQLRP GAPTSLQTEP QGNPEGNHGG EGDSCPHGSP 

        70         80         90        100        110        120 
QGPLAPPASP GPFATRSPLF IFMRRSSLLS RSSSGYFSFD TDRSPAPMSC DKSTQTPSPP 

       130        140        150        160        170        180 
CQAFNHYLSA MASMRQAEPA DMRPEIWIAQ ELRRIGDEFN AYYARRVFLN NYQAAEDHPR 

       190 
MVILRLLRYI VRLVWRMH 

« Hide

Isoform BimL (Bim(L)) [UniParc].

Checksum: 8BB4AAE06CB080FA
Show »

FASTA13815,967
Isoform BimS (BCL2-like 11 transcript variant 9) (Bim(S)) [UniParc].

Checksum: 60067208524D5BEA
Show »

FASTA10812,717
Isoform Bim-alpha1 (BimABCD) (Bim-ABCD) [UniParc].

Checksum: E2E24D5697C955BA
Show »

FASTA16918,536
Isoform Bim-alpha2 (BimACD) (Bim-ACD) [UniParc].

Checksum: 4335FA21C13B49AD
Show »

FASTA10912,332
Isoform Bim-alpha3 (BCL2-like 11 transcript variant 10) (BimAD) (Bim-AD) [UniParc].

Checksum: 3E03CCF2154A242C
Show »

FASTA799,081
Isoform Bim-alpha4 [UniParc].

Checksum: 7A6FD9AF07DA3E05
Show »

FASTA859,596
Isoform Bim-alpha5 [UniParc].

Checksum: D2F7FC06EE3CE697
Show »

FASTA17218,816
Isoform Bim-alpha6 [UniParc].

Checksum: 08678A7A0FBD4215
Show »

FASTA829,362
Isoform Bim-beta1 [UniParc].

Checksum: D208F1CB6D324539
Show »

FASTA13514,458
Isoform Bim-beta2 [UniParc].

Checksum: D3A245DECD324539
Show »

FASTA13514,418
Isoform Bim-beta3 [UniParc].

Checksum: A8FA866EBD5CF16E
Show »

FASTA19822,649
Isoform Bim-beta4 [UniParc].

Checksum: FA9541901CA32FD1
Show »

FASTA444,834
Isoform Bim-beta5 [UniParc].

Checksum: B7590CC04A98E081
Show »

FASTA14015,025
Isoform Bim-beta6 [UniParc].

Checksum: 7CFE6B5A5ED671F3
Show »

FASTA758,214
Isoform Bim-beta7 [UniParc].

Checksum: 6958582B30D7BCAF
Show »

FASTA808,821
Isoform Bim-gamma [UniParc].

Checksum: 15E21254C12C239B
Show »

FASTA11212,412
Isoform BimABC (Bim-ABC) [UniParc].

Checksum: FD4F4A9292591961
Show »

FASTA10311,773
Isoform BimAC (Bim-AC) [UniParc].

Checksum: 215890B3975C25A5
Show »

FASTA16317,977
Isoform BimA (Bim-A) [UniParc].

Checksum: D0CE170469B8570D
Show »

FASTA738,523

References

« Hide '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] (ISOFORMS BIMEL AND BIML), FUNCTION.
Tissue: Peripheral blood and Spleen.
[2]"Molecular cloning and characterization of six novel isoforms of human Bim, a member of the proapoptotic Bcl-2 family."
Mami U., Miyashita T., Shikama Y., Tadokoro K., Yamada M.
FEBS Lett. 509:135-141(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BIM-ALPHA1; BIM-ALPHA2; BIM-BETA1; BIM-BETA2; BIM-BETA3 AND BIM-BETA4), FUNCTION (ISOFORMS BIM-ALPHA1 AND BIM-ALPHA2), SUBCELLULAR LOCATION.
[3]"Identification and characterization of Bimgamma, a novel proapoptotic BH3-only splice variant of Bim."
Liu J.-W., Chandra D., Tang S.H., Chopra D., Tang D.G.
Cancer Res. 62:2976-2981(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BIM-GAMMA), FUNCTION (ISOFORM BIM-GAMMA), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[4]"Identification of novel isoforms of the BH3 domain protein Bim which directly activate Bax to trigger apoptosis."
Marani M., Tenev T., Hancock D., Downward J., Lemoine N.R.
Mol. Cell. Biol. 22:3577-3589(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BIMEL; BIML; BIMS; BIM-ALPHA1; BIM-ALPHA2; BIM-ALPHA3; BIMA; BIMABC AND BIMAC), ALTERNATIVE SPLICING, FUNCTION, SUBUNIT, MUTAGENESIS OF GLY-156 AND ASN-160.
Tissue: Embryonic kidney and Ovarian cancer.
[5]"Over-expression of Bim alpha3, a novel isoform of human Bim, result in cell apoptosis."
Chen J.Z., Ji C.N., Gu S.H., Li J.X., Zhao E.P., Huang Y., Huang L., Ying K., Xie Y., Mao Y.M.
Int. J. Biochem. Cell Biol. 36:1554-1561(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BIMS AND BIM-ALPHA3), FUNCTION (ISOFORM BIM-ALPHA3).
[6]"Identification and characterization of BH3 domain protein Bim and its isoforms in human hepatocellular carcinomas."
Miao J., Chen G.G., Yun J.P., Chun S.Y., Zheng Z.Z., Ho R.L.K., Chak E.C., Xia N.S., Lai P.B.
Apoptosis 12:1691-1701(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BIM-ALPHA3; BIM-ALPHA4; BIM-ALPHA5; BIM-ALPHA6; BIM-BETA5; BIM-BETA6; BIM-BETA7).
[7]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS BIMEL AND BIML).
Tissue: Teratocarcinoma and Tongue.
[8]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]"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).
Tissue: Blood.
[11]"BimEL is an important determinant for induction of anoikis sensitivity by mitogen-activated protein/extracellular signal-regulated kinase kinase inhibitors."
Fukazawa H., Noguchi K., Masumi A., Murakami Y., Uehara Y.
Mol. Cancer Ther. 3:1281-1288(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-69, UBIQUITINATION.
[12]"Apoptosis initiated when BH3 ligands engage multiple Bcl-2 homologs, not Bax or Bak."
Willis S.N., Fletcher J.I., Kaufmann T., van Delft M.F., Chen L., Czabotar P.E., Ierino H., Lee E.F., Fairlie W.D., Bouillet P., Strasser A., Kluck R.M., Adams J.M., Huang D.C.
Science 315:856-859(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF GLY-156.
[13]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[14]"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 TRIM2.
[15]"CHOP potentially co-operates with FOXO3a in neuronal cells to regulate PUMA and BIM expression in response to ER stress."
Ghosh A.P., Klocke B.J., Ballestas M.E., Roth K.A.
PLoS ONE 7:E39586-E39586(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY ER STRESS.
[16]"Structural insights into the degradation of Mcl-1 induced by BH3 domains."
Czabotar P.E., Lee E.F., van Delft M.F., Day C.L., Smith B.J., Huang D.C.S., Fairlie W.D., Hinds M.G., Colman P.M.
Proc. Natl. Acad. Sci. U.S.A. 104:6217-6222(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 141-166 IN COMPLEX WITH MCL1.
[17]"Completing the family portrait of the anti-apoptotic Bcl-2 proteins: crystal structure of human Bfl-1 in complex with Bim."
Herman M.D., Nyman T., Welin M., Lehtio L., Flodin S., Tresaugues L., Kotenyova T., Flores A., Nordlund P.
FEBS Lett. 582:3590-3594(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 141-165 IN COMPLEX WITH BCL2A1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF032457 mRNA. Translation: AAC39593.1.
AF032458 mRNA. Translation: AAC39594.1.
AB071195 mRNA. Translation: BAB78589.1.
AB071196 mRNA. Translation: BAB78590.1.
AB071197 mRNA. Translation: BAB78591.1.
AB071198 mRNA. Translation: BAB78592.1.
AB071199 mRNA. Translation: BAB78593.1.
AB071200 mRNA. Translation: BAB78594.1.
AY352518 mRNA. Translation: AAQ62569.1.
AY305714 mRNA. Translation: AAQ82546.1.
AY305715 mRNA. Translation: AAQ82547.1.
AY423441 mRNA. Translation: AAQ99148.1.
AY423442 mRNA. Translation: AAQ99149.1.
AY423443 mRNA. Translation: AAQ99150.1.
AY428962 mRNA. Translation: AAR06908.1.
DQ849200 mRNA. Translation: ABI13589.1.
DQ849201 mRNA. Translation: ABI13590.1.
DQ849202 mRNA. Translation: ABI13591.1.
AK290377 mRNA. Translation: BAF83066.1.
AK291269 mRNA. Translation: BAF83958.1.
AC096670 Genomic DNA. Translation: AAY14797.1.
CH471237 Genomic DNA. Translation: EAW50365.1.
CH471237 Genomic DNA. Translation: EAW50367.1.
CH471237 Genomic DNA. Translation: EAW50369.1.
CH471237 Genomic DNA. Translation: EAW50370.1.
CH471237 Genomic DNA. Translation: EAW50371.1.
CH471237 Genomic DNA. Translation: EAW50372.1.
CH471237 Genomic DNA. Translation: EAW50373.1.
CH471237 Genomic DNA. Translation: EAW50374.1.
BC033694 mRNA. Translation: AAH33694.1.
RefSeqNP_001191035.1. NM_001204106.1.
NP_001191036.1. NM_001204107.1.
NP_001191037.1. NM_001204108.1.
NP_001191038.1. NM_001204109.1.
NP_001191039.1. NM_001204110.1.
NP_001191040.1. NM_001204111.1.
NP_001191041.1. NM_001204112.1.
NP_001191042.1. NM_001204113.1.
NP_006529.1. NM_006538.4.
NP_619527.1. NM_138621.4.
NP_619528.1. NM_138622.3.
NP_619529.1. NM_138623.3.
NP_619530.1. NM_138624.3.
NP_619531.1. NM_138625.3.
NP_619532.1. NM_138626.3.
NP_619533.1. NM_138627.3.
NP_996885.1. NM_207002.3.
NP_996886.1. NM_207003.2.
UniGeneHs.469658.
Hs.737004.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1F95NMR-C/D108-116[»]
2K7WNMR-B145-164[»]
2NL9X-ray1.55B141-166[»]
2V6QX-ray2.70B141-166[»]
2VM6X-ray2.20B141-165[»]
2WH6X-ray1.50B141-166[»]
2YQ6X-ray1.80B147-164[»]
3D7VX-ray2.03B141-166[»]
3FDLX-ray1.78B141-166[»]
3IO8X-ray2.30B/D141-166[»]
3IO9X-ray2.40B141-166[»]
3KJ0X-ray1.70B143-165[»]
3KJ1X-ray1.94B143-163[»]
3KJ2X-ray2.35B143-163[»]
4B4SX-ray1.90B141-166[»]
DisProtDP00643.
ProteinModelPortalO43521.
SMRO43521. Positions 141-173.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115335. 38 interactions.
DIPDIP-29185N.
IntActO43521. 28 interactions.
MINTMINT-1664421.

Chemistry

BindingDBO43521.
ChEMBLCHEMBL5777.

PTM databases

PhosphoSiteO43521.

Proteomic databases

PaxDbO43521.
PRIDEO43521.

Protocols and materials databases

DNASU10018.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000308659; ENSP00000309226; ENSG00000153094. [O43521-2]
ENST00000337565; ENSP00000338374; ENSG00000153094. [O43521-17]
ENST00000357757; ENSP00000350398; ENSG00000153094. [O43521-8]
ENST00000361493; ENSP00000354879; ENSG00000153094.
ENST00000393253; ENSP00000376942; ENSG00000153094. [O43521-7]
ENST00000393256; ENSP00000376943; ENSG00000153094. [O43521-1]
ENST00000405953; ENSP00000384641; ENSG00000153094. [O43521-17]
ENST00000415458; ENSP00000393781; ENSG00000153094. [O43521-16]
ENST00000431217; ENSP00000394640; ENSG00000153094. [O43521-10]
ENST00000433098; ENSP00000401662; ENSG00000153094. [O43521-5]
ENST00000436733; ENSP00000403727; ENSG00000153094. [O43521-14]
ENST00000437029; ENSP00000412892; ENSG00000153094. [O43521-8]
ENST00000439718; ENSP00000411137; ENSG00000153094. [O43521-7]
ENST00000452231; ENSP00000391292; ENSG00000153094. [O43521-9]
GeneID10018.
KEGGhsa:10018.
UCSCuc002tgt.1. human. [O43521-17]
uc002tgu.1. human. [O43521-2]
uc002tgv.1. human. [O43521-1]
uc002tgw.2. human. [O43521-6]
uc002tgx.2. human. [O43521-9]
uc002tgy.2. human. [O43521-16]
uc002tgz.2. human. [O43521-3]
uc002tha.2. human. [O43521-11]
uc002thb.2. human. [O43521-5]
uc002thc.2. human. [O43521-7]
uc002thd.2. human. [O43521-15]
uc010fkd.2. human. [O43521-13]
uc021vmp.1. human. [O43521-14]
uc021vmq.1. human. [O43521-4]
uc021vmr.1. human. [O43521-10]
uc021vms.1. human. [O43521-8]

Organism-specific databases

CTD10018.
GeneCardsGC02P111876.
HGNCHGNC:994. BCL2L11.
HPACAB026332.
MIM603827. gene.
neXtProtNX_O43521.
PharmGKBPA25305.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG40262.
InParanoidO43521.
KOK16341.
OMAIRLVWRM.
PhylomeDBO43521.
TreeFamTF335898.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_578. Apoptosis.

Gene expression databases

ArrayExpressO43521.
BgeeO43521.
GenevestigatorO43521.

Family and domain databases

InterProIPR014771. Apoptosis_Bim_N.
IPR017288. Bcl-2-like_11.
IPR015040. Bcl-x_interacting_BH3_dom.
[Graphical view]
PfamPF08945. Bclx_interact. 1 hit.
PF06773. Bim_N. 1 hit.
[Graphical view]
PIRSFPIRSF037827. Bcl-2-like_p11. 1 hit.
ProtoNetSearch...

Other

ChiTaRSBCL2L11. human.
EvolutionaryTraceO43521.
GeneWikiBCL2L11.
GenomeRNAi10018.
NextBio37849.
PMAP-CutDBO43521.
PROO43521.
SOURCESearch...

Entry information

Entry nameB2L11_HUMAN
AccessionPrimary (citable) accession number: O43521
Secondary accession number(s): A8K2W2 expand/collapse secondary AC list , O43522, Q0MSE7, Q0MSE8, Q0MSE9, Q53R28, Q6JTU6, Q6T851, Q6TE14, Q6TE15, Q6TE16, Q6V402, Q8WYL6, Q8WYL7, Q8WYL8, Q8WYL9, Q8WYM0, Q8WYM1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: June 1, 1998
Last modified: April 16, 2014
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM