O43521 (B2L11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	198 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.1 Ref.2 Ref.3 Ref.4
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, BAX or BAK By similarity. Interacts with DYNLL1 and YWHAZ By similarity. When phosphorylated, interacts with TRIM2; this interaction is associated with ubiquitination and degradation By similarity. Ref.12
Subcellular location	Endomembrane system; Peripheral membrane protein By similarity. Note: Associated with intracytoplasmic membranes By similarity. Ref.2 Ref.3 Isoform BimEL: Mitochondrion Ref.2 Ref.3. Isoform BimL: Mitochondrion Ref.2 Ref.3. Isoform BimS: Mitochondrion Ref.2 Ref.3. Isoform Bim-alpha1: Mitochondrion Ref.2 Ref.3.
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
Domain	The BH3 motif is required for Bcl-2 binding and cytotoxicity.
Post-translational modification	Phosphorylation by MAPK1/MAPK3 induces interaction with TRIM2, followed by ubiquitination By similarity. Ubiquitinated by TRIM2 following phosphorylation by MAPK1/MAPK3, leading to degradation by the proteasome By similarity.
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	activation of cysteine-type endopeptidase activity involved in apoptotic process Inferred from direct assay. Source: UniProtKB activation of pro-apoptotic gene products Traceable author statement. Source: Reactome induction of apoptosis by extracellular signals Traceable author statement. Source: Reactome induction of apoptosis by intracellular signals Traceable author statement. Source: Reactome nerve growth factor receptor signaling pathway Traceable author statement. Source: Reactome positive regulation of apoptotic process Inferred from mutant phenotype. Source: UniProtKB positive regulation of protein homooligomerization Inferred from direct assay. Source: BHF-UCL positive regulation of release of cytochrome c from mitochondria Inferred from genetic interaction. Source: BHF-UCL
Cellular component	BIM-BCL-2 complex Inferred from direct assay. Source: UniProtKB BIM-BCL-xl complex Inferred from direct assay. Source: UniProtKB cytosol Traceable author statement. Source: Reactome endomembrane system Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrial outer membrane Traceable author statement. Source: Reactome plasma membrane Traceable author statement. Source: Reactome
Molecular function	protein binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BCL2	P10415	3	EBI-526406,EBI-77694
BCL2L1	Q07817-1	6	EBI-526406,EBI-287195
BCL2L2	Q92843	3	EBI-526406,EBI-707714
GNB2L1	P63244	2	EBI-526406,EBI-296739
MCL1	Q07820	4	EBI-526406,EBI-1003422
Mcl1	P97287	4	EBI-526406,EBI-707292	From a different organism.
MIF	P14174	5	EBI-526420,EBI-372712

Alternative products

This entry describes 17 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)

The sequence of this isoform differs from the canonical sequence as follows:
     167-198: VFLNNYQAAEDHPRMVILRLLRYIVRLVWRMH → LEK

Isoform Bim-alpha2 (identifier: O43521-5)

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;

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 198

198

Bcl-2-like protein 11

PRO_0000143109

Regions

Motif

148 – 162

15

BH3

Amino acid modifications

Modified residue

69

1

Phosphoserine By similarity

Modified residue

77

1

Phosphoserine Ref.10 Ref.11

Modified residue

87

1

Phosphoserine By similarity

Natural variations

Alternative sequence

42 – 131

90

Missing in isoform BimS, isoform Bim-alpha3, isoform Bim-alpha6 and isoform Bim-alpha4.

VSP_035608

Alternative sequence

42 – 101

60

Missing in isoform BimL, isoform Bim-alpha2, isoform Bim-gamma, isoform Bim-beta6 and isoform Bim-beta7.

VSP_000535

Alternative sequence

42 – 75

34

GNPEG…GPFAT → VSLCHPGWSALVRSWLTATS NSQVQAVLLPQPPK in isoform Bim-beta3.

VSP_035609

Alternative sequence

43 – 44

2

NP → IF in isoform Bim-beta4.

VSP_035610

Alternative sequence

45 – 198

154

Missing in isoform Bim-beta4.

VSP_035611

Alternative sequence

132 – 198

67

ASMRQ…VWRMH → VVILEDIGDLSLCFGFIFTG LDLYGHHHSQDTEQLNHKDF S in isoform Bim-gamma.

VSP_035612

Alternative sequence

132 – 140

9

ASMRQAEPA → VREIEEVVV in isoform Bim-beta5 and isoform Bim-beta7.

VSP_035613

Alternative sequence

132 – 135

4

ASMR → GIFE in isoform Bim-beta2 and isoform Bim-beta6.

VSP_035614

Alternative sequence

133 – 135

3

SMR → NWD in isoform Bim-beta1.

VSP_035615

Alternative sequence

136 – 198

63

Missing in isoform Bim-beta1, isoform Bim-beta2 and isoform Bim-beta6.

VSP_035616

Alternative sequence

141 – 198

58

Missing in isoform Bim-beta5 and isoform Bim-beta7.

VSP_035617

Alternative sequence

167 – 198

32

VFLNN…VWRMH → LEK in isoform Bim-alpha1, isoform Bim-alpha2 and isoform Bim-alpha3.

VSP_035620

Alternative sequence

167 – 198

32

VFLNN…VWRMH → LAKLLASST in isoform Bim-alpha4.

VSP_035618

Alternative sequence

167 – 198

32

VFLNN…VWRMH → MPLPPD in isoform Bim-alpha5 and isoform Bim-alpha6.

VSP_035619

Experimental info

Sequence conflict

33

1

P → L in BAF83066. Ref.6

Secondary structure

1

.

.

.

198

Helix Strand Turn

Details...

Helix

144 – 164

21

Sequences

	Sequence		Length	Mass (Da)
	Isoform BimEL (Bim(EL)) [UniParc]. Last modified June 1, 1998. Version 1. Checksum: D75735E469CA6997	FASTA	198	22,171
	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
	Isoform BimL (Bim(L)) [UniParc]. Checksum: 8BB4AAE06CB080FA	FASTA	138	15,967
	10 20 30 40 50 60 MAKQPSDVSS ECDREGRQLQ PAERPPQLRP GAPTSLQTEP QDRSPAPMSC DKSTQTPSPP 70 80 90 100 110 120 CQAFNHYLSA MASMRQAEPA DMRPEIWIAQ ELRRIGDEFN AYYARRVFLN NYQAAEDHPR 130 MVILRLLRYI VRLVWRMH
	Isoform BimS (BCL2-like 11 transcript variant 9) (Bim(S)) [UniParc]. Checksum: 60067208524D5BEA	FASTA	108	12,717
	10 20 30 40 50 60 MAKQPSDVSS ECDREGRQLQ PAERPPQLRP GAPTSLQTEP QASMRQAEPA DMRPEIWIAQ 70 80 90 100 ELRRIGDEFN AYYARRVFLN NYQAAEDHPR MVILRLLRYI VRLVWRMH
	Isoform Bim-alpha1 [UniParc]. Checksum: E2E24D5697C955BA	FASTA	169	18,536
	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 CQAFNHYLSA MASMRQAEPA DMRPEIWIAQ ELRRIGDEFN AYYARRLEK
	Isoform Bim-alpha2 [UniParc]. Checksum: 4335FA21C13B49AD	FASTA	109	12,332
	10 20 30 40 50 60 MAKQPSDVSS ECDREGRQLQ PAERPPQLRP GAPTSLQTEP QDRSPAPMSC DKSTQTPSPP 70 80 90 100 CQAFNHYLSA MASMRQAEPA DMRPEIWIAQ ELRRIGDEFN AYYARRLEK
	Isoform Bim-alpha3 (BCL2-like 11 transcript variant 10) [UniParc]. Checksum: 3E03CCF2154A242C	FASTA	79	9,081
	10 20 30 40 50 60 MAKQPSDVSS ECDREGRQLQ PAERPPQLRP GAPTSLQTEP QASMRQAEPA DMRPEIWIAQ 70 ELRRIGDEFN AYYARRLEK
	Isoform Bim-alpha4 [UniParc]. Checksum: 7A6FD9AF07DA3E05	FASTA	85	9,596
	10 20 30 40 50 60 MAKQPSDVSS ECDREGRQLQ PAERPPQLRP GAPTSLQTEP QASMRQAEPA DMRPEIWIAQ 70 80 ELRRIGDEFN AYYARRLAKL LASST
	Isoform Bim-alpha5 [UniParc]. Checksum: D2F7FC06EE3CE697	FASTA	172	18,816
	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 CQAFNHYLSA MASMRQAEPA DMRPEIWIAQ ELRRIGDEFN AYYARRMPLP PD
	Isoform Bim-alpha6 [UniParc]. Checksum: 08678A7A0FBD4215	FASTA	82	9,362
	10 20 30 40 50 60 MAKQPSDVSS ECDREGRQLQ PAERPPQLRP GAPTSLQTEP QASMRQAEPA DMRPEIWIAQ 70 80 ELRRIGDEFN AYYARRMPLP PD
	Isoform Bim-beta1 [UniParc]. Checksum: D208F1CB6D324539	FASTA	135	14,458
	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 CQAFNHYLSA MANWD
	Isoform Bim-beta2 [UniParc]. Checksum: D3A245DECD324539	FASTA	135	14,418
	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 CQAFNHYLSA MGIFE
	Isoform Bim-beta3 [UniParc]. Checksum: A8FA866EBD5CF16E	FASTA	198	22,649
	10 20 30 40 50 60 MAKQPSDVSS ECDREGRQLQ PAERPPQLRP GAPTSLQTEP QVSLCHPGWS ALVRSWLTAT 70 80 90 100 110 120 SNSQVQAVLL PQPPKRSPLF IFMRRSSLLS RSSSGYFSFD TDRSPAPMSC DKSTQTPSPP 130 140 150 160 170 180 CQAFNHYLSA MASMRQAEPA DMRPEIWIAQ ELRRIGDEFN AYYARRVFLN NYQAAEDHPR 190 MVILRLLRYI VRLVWRMH
	Isoform Bim-beta4 [UniParc]. Checksum: FA9541901CA32FD1	FASTA	44	4,834
	10 20 30 40 MAKQPSDVSS ECDREGRQLQ PAERPPQLRP GAPTSLQTEP QGIF
	Isoform Bim-beta5 [UniParc]. Checksum: B7590CC04A98E081	FASTA	140	15,025
	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 CQAFNHYLSA MVREIEEVVV
	Isoform Bim-beta6 [UniParc]. Checksum: 7CFE6B5A5ED671F3	FASTA	75	8,214
	10 20 30 40 50 60 MAKQPSDVSS ECDREGRQLQ PAERPPQLRP GAPTSLQTEP QDRSPAPMSC DKSTQTPSPP 70 CQAFNHYLSA MGIFE
	Isoform Bim-beta7 [UniParc]. Checksum: 6958582B30D7BCAF	FASTA	80	8,821
	10 20 30 40 50 60 MAKQPSDVSS ECDREGRQLQ PAERPPQLRP GAPTSLQTEP QDRSPAPMSC DKSTQTPSPP 70 80 CQAFNHYLSA MVREIEEVVV
	Isoform Bim-gamma [UniParc]. Checksum: 15E21254C12C239B	FASTA	112	12,412
	10 20 30 40 50 60 MAKQPSDVSS ECDREGRQLQ PAERPPQLRP GAPTSLQTEP QDRSPAPMSC DKSTQTPSPP 70 80 90 100 110 CQAFNHYLSA MVVILEDIGD LSLCFGFIFT GLDLYGHHHS QDTEQLNHKD FS

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: 9430630] [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: 11734221] [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: 12019181] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BIM-GAMMA), FUNCTION (ISOFORM BIM-GAMMA), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[4]	"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: 15147734] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BIMS AND BIM-ALPHA3), FUNCTION (ISOFORM BIM-ALPHA3).
[5]	"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: 17503221] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BIM-ALPHA3; BIM-ALPHA4; BIM-ALPHA5; BIM-ALPHA6; BIM-BETA5; BIM-BETA6; BIM-BETA7).
[6]	"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. , 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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS BIMEL AND BIML). Tissue: Teratocarcinoma and Tongue.
[7]	"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. , 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: 15815621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	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. , 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].
[9]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BIMEL). Tissue: Blood.
[10]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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: 21478148] [Abstract] Cited for: INTERACTION WITH TRIM2.
[13]	"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: 17389404] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 141-166 IN COMPLEX WITH MCL1.
[14]	"Human BCL-2A1 in complex with BIM." Structural genomics consortium (SGC) Submitted (FEB-2008) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 141-165 IN COMPLEX WITH BCL2A1.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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.

IPI

IPI00012853.
IPI00103743.
IPI00216585.
IPI00410159.
IPI00428840.
IPI00451139.
IPI00514401.
IPI00873921.
IPI00878323.
IPI00914559.
IPI00914560.
IPI00914563.
IPI00914586.
IPI00914592.
IPI00914600.
IPI00914670.
IPI00914677.

RefSeq

NP_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.

UniGene

Hs.469658.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
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	[»]
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	[»]

ProteinModelPortal

O43521.

SMR

O43521. Positions 141-173.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29185N.

IntAct

O43521. 29 interactions.

MINT

MINT-1664421.

STRING

O43521.

PTM databases

PhosphoSite

O43521.

Proteomic databases

PRIDE

O43521.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000357682; ENSP00000350311; ENSG00000153094.
ENST00000393256; ENSP00000376943; ENSG00000153094.

GeneID

10018.

KEGG

hsa:10018.

UCSC

uc002tgu.1. human.
uc002tgv.1. human.

Organism-specific databases

CTD

10018.

GeneCards

GC02P111876.

H-InvDB

HIX0002369.

HGNC

HGNC:994. BCL2L11.

HPA

CAB026332.

MIM

603827. gene.

neXtProt

NX_O43521.

PharmGKB

PA25305.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG19086.

GeneTree

ENSGT00390000003178.

InParanoid

O43521.

OMA

IRLVWRM.

OrthoDB

EOG4C87TR.

PhylomeDB

O43521.

Enzyme and pathway databases

Pathway_Interaction_DB

foxopathway. FoxO family signaling.
p75ntrpathway. p75(NTR)-mediated signaling.

Reactome

REACT_111102. Signal Transduction.
REACT_578. Apoptosis.

Gene expression databases

ArrayExpress

O43521.

Bgee

O43521.

Genevestigator

O43521.

GermOnline

ENSG00000153094. Homo sapiens.

Family and domain databases

InterPro

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

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

NextBio

37849.

PMAP-CutDB

O43521.

SOURCE

Search...

Entry information

Entry name

B2L11_HUMAN

Accession

Primary (citable) accession number: O43521
Secondary accession number(s): A8K2W2 , 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:	January 25, 2012
This is version 110 of the entry and version 1 of the sequence. [Complete history]

Entry status

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.