Bcl-2-like protein 1 - Homo sapiens (Human)

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Q07817 (B2CL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 163. History...

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

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

Names and origin

Protein names

Recommended name:
Bcl-2-like protein 1
Short name=Bcl2-L-1

Alternative name(s):
Apoptosis regulator Bcl-X

Gene names

Name:	BCL2L1
Synonyms:	BCL2L, BCLX

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	233 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Potent inhibitor of cell death. Inhibits activation of caspases By similarity. Appears to regulate cell death by blocking the voltage-dependent anion channel (VDAC) by binding to it and preventing the release of the caspase activator, CYC1, from the mitochondrial membrane. Also acts as a regulator of G2 checkpoint and progression to cytokinesis during mitosis. Ref.17 Ref.19 Isoform Bcl-X(S) promotes apoptosis. Ref.17 Ref.19
Subunit structure	Homodimer. Isoform Bcl-X(L) forms heterodimers with BAX, BAK or BCL2. Heterodimerization with BAX does not seem to be required for anti-apoptotic activity. Interacts with BCL2L11. Interacts with DMN1L; the interaction stimulates the GTPase activity of DMN1L in synapses and increases the number of axonal mitochondria and the size and number of synaptic vesicle clusters By similarity. Interacts with BAD. Interacts (isoform Bcl-X(L)) with SIVA1 (isoform 1); the interaction inhibits the anti-apoptotic activity. Interacts with BECN1 and PGAM5. Interacts (isoform Bcl-X(L)) with BAX (isoform Sigma). Isoform Bcl-X(L) interacts with IKZF3. Interacts with HEBP2. Isoform Bcl-X(L) interacts with BOP/C22orf29. Interacts with P53/TP53 and BBC3; interaction with BBC3 disrupts the interaction with P53/TP53. Ref.2 Ref.9 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.25 Ref.28 Ref.29
Subcellular location	Mitochondrion membrane; Single-pass membrane protein. Nucleus membrane; Single-pass membrane protein; Cytoplasmic side By similarity. Cytoplasm › cytoskeleton › centrosome. Note: Mitochondrial membranes and perinuclear envelope By similarity. Localizes to the centrosome when phosphorylated at Ser-49. Ref.17 Ref.19
Tissue specificity	Bcl-X(S) is expressed at high levels in cells that undergo a high rate of turnover, such as developing lymphocytes. In contrast, Bcl-X(L) is found in tissues containing long-lived postmitotic cells, such as adult brain.
Domain	The BH4 motif is required for anti-apoptotic activity. The BH1 and BH2 motifs are required for both heterodimerization with other Bcl-2 family members and for repression of cell death.
Post-translational modification	Proteolytically cleaved by caspases during apoptosis. The cleaved protein, lacking the BH4 motif, has pro-apoptotic activity. Ref.11 Phosphorylated on Ser-62 by CDK1. This phosphorylation is partial in normal mitotic cells, but complete in G2-arrested cells upon DNA-damage, thus promoting subsequent apoptosis probably by triggering caspases-mediated proteolysis. Phosphorylated by PLK3, leading to regulate the G2 checkpoint and progression to cytokinesis during mitosis. Phosphorylation at Ser-49 appears during the S phase and G2, disappears rapidly in early mitosis during prometaphase, metaphase and early anaphase, and re-appears during telophase and cytokinesis. Ref.17 Ref.19
Sequence similarities	Belongs to the Bcl-2 family.

Ontologies

Keywords
Biological process	Apoptosis
Cellular component	Cytoplasm Cytoskeleton Membrane Mitochondrion Nucleus
Coding sequence diversity	Alternative splicing
Domain	Transmembrane Transmembrane helix
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell proliferation Inferred from electronic annotation. Source: Compara cellular process regulating host cell cycle in response to virus Inferred from electronic annotation. Source: Compara cellular response to alkaloid Inferred from electronic annotation. Source: Compara cellular response to amino acid stimulus Inferred from electronic annotation. Source: Compara cellular response to gamma radiation Inferred from electronic annotation. Source: Compara cytokinesis Inferred from mutant phenotype Ref.19. Source: UniProtKB fertilization Inferred from electronic annotation. Source: Compara germ cell development Inferred from electronic annotation. Source: Compara growth Inferred from electronic annotation. Source: Compara in utero embryonic development Inferred from electronic annotation. Source: Compara innate immune response Traceable author statement. Source: Reactome intrinsic apoptotic signaling pathway Traceable author statement. Source: Reactome male gonad development Inferred from electronic annotation. Source: Compara mitotic cell cycle checkpoint Inferred from mutant phenotype Ref.19. Source: UniProtKB negative regulation of anoikis Inferred from mutant phenotype PubMed 15006356. Source: UniProtKB negative regulation of apoptotic process Inferred from direct assay PubMed 20673843 PubMed 9388232. Source: UniProtKB negative regulation of autophagy Traceable author statement PubMed 18309324. Source: UniProtKB negative regulation of establishment of protein localization to plasma membrane Inferred from direct assay PubMed 21041309. Source: BHF-UCL negative regulation of intrinsic apoptotic signaling pathway Inferred from direct assay PubMed 21567405. Source: UniProtKB negative regulation of neuron apoptotic process Inferred from electronic annotation. Source: Compara negative regulation of release of cytochrome c from mitochondria Inferred by curator PubMed 21041309. Source: BHF-UCL nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway Traceable author statement. Source: Reactome ovarian follicle development Inferred from electronic annotation. Source: Compara positive regulation of apoptotic process Inferred from electronic annotation. Source: Compara positive regulation of cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of intrinsic apoptotic signaling pathway Traceable author statement. Source: Reactome regulation of mitochondrial membrane permeability Inferred from direct assay PubMed 9843949. Source: HGNC regulation of mitochondrial membrane potential Inferred from direct assay PubMed 9843949. Source: HGNC release of cytochrome c from mitochondria Inferred from direct assay PubMed 9843949. Source: HGNC response to cycloheximide Inferred from electronic annotation. Source: Compara response to cytokine stimulus Inferred from direct assay PubMed 9184696. Source: MGI spermatogenesis Inferred from electronic annotation. Source: Compara
Cellular_component	Bcl-2 family protein complex Inferred from direct assay PubMed 21199865. Source: UniProtKB centrosome Inferred from direct assay Ref.19. Source: UniProtKB cytosol Inferred from electronic annotation. Source: Compara integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial outer membrane Non-traceable author statement PubMed 12667443. Source: UniProtKB nuclear membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BAD	Q92934	6	EBI-287195,EBI-700771
Bad	Q61337	2	EBI-287195,EBI-400328	From a different organism.
BAK1	Q16611	8	EBI-287195,EBI-519866
BAX	Q07812	13	EBI-287195,EBI-516580
BBC3	Q9BXH1	7	EBI-287195,EBI-519884
Bbc3	Q99ML1	3	EBI-287195,EBI-727801	From a different organism.
BCL2L11	O43521	10	EBI-287195,EBI-526406
BCL2L11	O43521-1	2	EBI-287195,EBI-526416
BECN1	Q14457	4	EBI-287195,EBI-949378
BID	P55957	6	EBI-287195,EBI-519672
BIK	Q13323	3	EBI-287195,EBI-700794
ced-4	P30429	3	EBI-78035,EBI-494118	From a different organism.
CLU	P10909-4	6	EBI-287195,EBI-4322678
HRK	O00198	3	EBI-287195,EBI-701322
NLRP1	Q9C000	9	EBI-78035,EBI-1220518
SIVA1	O15304	2	EBI-287195,EBI-520756
SIVA1	O15304-1	5	EBI-287195,EBI-520766
SPNS1	Q9H2V7	3	EBI-78035,EBI-1386527
TP53	P04637	18	EBI-287195,EBI-366083
Tp53	P02340	3	EBI-287195,EBI-474016	From a different organism.
VRK2	Q86Y07-1	2	EBI-287195,EBI-1207633

Alternative products

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

Isoform Bcl-X(L) (identifier: Q07817-1) Also known as: Bcl-xL; 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 Bcl-X(S) (identifier: Q07817-2) Also known as: Bcl-xS; The sequence of this isoform differs from the canonical sequence as follows: 126-188: Missing.

Isoform Bcl-X(beta) (identifier: Q07817-3) The sequence of this isoform differs from the canonical sequence as follows: 189-233: DTFVELYGNN...VLLGSLFSRK → VRTKPLVCPF...CWVIVGDVDS

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 233

233

Bcl-2-like protein 1

PRO_0000143062

Regions

Transmembrane

210 – 226

Helical; Potential

Motif

4 – 24

BH4

Motif

86 – 100

BH3

Motif

129 – 148

BH1

Motif

180 – 195

BH2

Sites

Site

61 – 62

Cleavage; by caspase-1

Amino acid modifications

Modified residue

Phosphoserine; by PLK3 Ref.19

Modified residue

Phosphoserine; by CDK1 Ref.17

Natural variations

Alternative sequence

126 – 188

Missing in isoform Bcl-X(S).

VSP_000515

Alternative sequence

189 – 233

DTFVE…LFSRK → VRTKPLVCPFSLASGQRSPT ALLLYLFLLCWVIVGDVDS in isoform Bcl-X(beta).

VSP_000516

Experimental info

Mutagenesis

S → A: Less stable at G2 checkpoint after DNA damage. Ref.10 Ref.19

Mutagenesis

D → A: No cleavage by caspase-1 nor by caspase-3. Ref.10 Ref.11

Mutagenesis

131 – 133

FRD → VRA: No heterodimerization with BAX. Ref.10

Mutagenesis

135 – 137

VNW → AIL: Loss of anti-apoptotic activity. Ref.10

Mutagenesis

138 – 140

GRI → ELN: Loss of anti-apoptotic activity. Ref.9 Ref.10

Mutagenesis

138

G → A: No heterodimerization with BAX. Ref.9 Ref.10

Mutagenesis

148

G → E: No heterodimerization with BAX. Ref.10

Mutagenesis

156

D → A: No effect on caspase-1 cleavage. Ref.10

Mutagenesis

176

D → A: No effect on caspase-1 cleavage. Ref.10

Mutagenesis

188 – 189

WD → GA: Reduces anti-apoptotic activity by about half. Ref.10

Mutagenesis

189

D → A: No effect on caspase-1 cleavage. Ref.10

Sequence conflict

G → A in CAA80661. Ref.1

Sequence conflict

168

A → V in CAI56777. Ref.4

Secondary structure

233

Helix Strand Turn

Details...

Sequences

Sequence		Length	Mass (Da)
Isoform Bcl-X(L) (Bcl-xL) [UniParc]. Last modified February 1, 1995. Version 1. Checksum: E09D3CDD851AE9BE Show »	FASTA	233	26,049
10 20 30 40 50 60 MSQSNRELVV DFLSYKLSQK GYSWSQFSDV EENRTEAPEG TESEMETPSA INGNPSWHLA 70 80 90 100 110 120 DSPAVNGATG HSSSLDAREV IPMAAVKQAL REAGDEFELR YRRAFSDLTS QLHITPGTAY 130 140 150 160 170 180 QSFEQVVNEL FRDGVNWGRI VAFFSFGGAL CVESVDKEMQ VLVSRIAAWM ATYLNDHLEP 190 200 210 220 230 WIQENGGWDT FVELYGNNAA AESRKGQERF NRWFLTGMTV AGVVLLGSLF SRK « Hide
Isoform Bcl-X(S) (Bcl-xS) [UniParc]. Checksum: 75D1FC01EC06AD47 Show »	FASTA	170	18,894
10 20 30 40 50 60 MSQSNRELVV DFLSYKLSQK GYSWSQFSDV EENRTEAPEG TESEMETPSA INGNPSWHLA 70 80 90 100 110 120 DSPAVNGATG HSSSLDAREV IPMAAVKQAL REAGDEFELR YRRAFSDLTS QLHITPGTAY 130 140 150 160 170 QSFEQDTFVE LYGNNAAAES RKGQERFNRW FLTGMTVAGV VLLGSLFSRK « Hide
Isoform Bcl-X(beta) [UniParc]. Checksum: 1EF621E5D0744E4E Show »	FASTA	227	25,290
10 20 30 40 50 60 MSQSNRELVV DFLSYKLSQK GYSWSQFSDV EENRTEAPEG TESEMETPSA INGNPSWHLA 70 80 90 100 110 120 DSPAVNGATG HSSSLDAREV IPMAAVKQAL REAGDEFELR YRRAFSDLTS QLHITPGTAY 130 140 150 160 170 180 QSFEQVVNEL FRDGVNWGRI VAFFSFGGAL CVESVDKEMQ VLVSRIAAWM ATYLNDHLEP 190 200 210 220 WIQENGGWVR TKPLVCPFSL ASGQRSPTAL LLYLFLLCWV IVGDVDS « Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"bcl-x, a bcl-2-related gene that functions as a dominant regulator of apoptotic cell death." Boise L.H., Gonzalez-Garcia M., Postema C.E., Ding L., Lindsten T., Turka L.A., Mao X., Nunez G., Thompson C.B. Cell 74:597-608(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BCL-X(L) AND BCL-X(S)).
[2]	"Identification of a human cDNA encoding a novel Bcl-x isoform." Ban J., Eckhart L., Weninger W., Mildner M., Tschachler E. Biochem. Biophys. Res. Commun. 248:147-152(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BCL-X(BETA)), INTERACTION WITH BAX.
[3]	Inohara N., Ohta S. Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM BCL-X(BETA)).
[4]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BCL-X(L)). Tissue: Colon carcinoma.
[5]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BCL-X(L)).
[6]	"The DNA sequence and comparative analysis of human chromosome 20." Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. Rogers J. Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	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. Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"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 BCL-X(L)). Tissue: Lung.
[9]	"Multiple Bcl-2 family members demonstrate selective dimerizations with Bax." Sedlak T.W., Oltvai Z.N., Yang E., Wang K., Boise L.H., Thompson C.B., Korsmeyer S.J. Proc. Natl. Acad. Sci. U.S.A. 92:7834-7838(1995) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF GLY-138, HETERODIMERIZATION.
[10]	"Bax-independent inhibition of apoptosis by Bcl-XL." Cheng E.H.-Y., Levine B., Boise L.H., Thompson C.B., Hardwick J.M., Korsmeyer S.J. Nature 379:554-556(1996) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF BH1 AND BH2 MOTIFS.
[11]	"Modulation of cell death by Bcl-xL through caspase interaction." Clem R.J., Cheng E.H.-Y., Karp C.L., Kirsch D.G., Ueno K., Takahashi A., Kastan M.B., Griffin D.E., Earnshaw W.C., Veliuona M.A., Hardwick J.M. Proc. Natl. Acad. Sci. U.S.A. 95:554-559(1998) [PubMed] [Europe PMC] [Abstract] Cited for: CLEAVAGE BY CASPASES, MUTAGENESIS OF ASP-61.
[12]	"Characterization of Bax-sigma, a cell death-inducing isoform of Bax." Schmitt E., Paquet C., Beauchemin M., Dever-Bertrand J., Bertrand R. Biochem. Biophys. Res. Commun. 270:868-879(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH BAX.
[13]	"The association of Aiolos transcription factor and Bcl-xL is involved in the control of apoptosis." Rebollo A., Ayllon V., Fleischer A., Martinez C.A., Zaballos A. J. Immunol. 167:6366-6373(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH IKZF3.
[14]	"PUMA induces the rapid apoptosis of colorectal cancer cells." Yu J., Zhang L., Hwang P.M., Kinzler K.W., Vogelstein B. Mol. Cell 7:673-682(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH BCL2 AND BBC3.
[15]	"Siva-1 binds to and inhibits BCL-X(L)-mediated protection against UV radiation-induced apoptosis." Xue L., Chu F., Cheng Y., Sun X., Borthakur A., Ramarao M., Pandey P., Wu M., Schlossman S.F., Prasad K.V.S. Proc. Natl. Acad. Sci. U.S.A. 99:6925-6930(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SIVA1.
[16]	"PGAM5, a Bcl-XL-interacting protein, is a novel substrate for the redox-regulated Keap1-dependent ubiquitin ligase complex." Lo S.-C., Hannink M. J. Biol. Chem. 281:37893-37903(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PGAM5.
[17]	"Cyclin-dependent kinase 1-mediated Bcl-xL/Bcl-2 phosphorylation acts as a functional link coupling mitotic arrest and apoptosis." Terrano D.T., Upreti M., Chambers T.C. Mol. Cell. Biol. 30:640-656(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN APOPTOSIS, PHOSPHORYLATION AT SER-62 BY CDK1, SUBCELLULAR LOCATION.
[18]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]	"Bcl-xL phosphorylation at Ser49 by polo kinase 3 during cell cycle progression and checkpoints." Wang J., Beauchemin M., Bertrand R. Cell. Signal. 23:2030-2038(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-49, MUTAGENESIS OF SER-49.
[20]	"X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell death." Muchmore S.W., Sattler M., Liang H., Meadows R.P., Harlan J.E., Yoon H.S., Nettesheim D., Chang B.S., Thompson C.B., Wong S.L., Ng S.L., Fesik S.W. Nature 381:335-341(1996) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), STRUCTURE BY NMR OF 1-209.
[21]	"Structure of Bcl-xL-Bak peptide complex: recognition between regulators of apoptosis." Sattler M., Liang H., Nettesheim D., Meadows R.P., Harlan J.E., Eberstadt M., Yoon H.S., Shuker S.B., Chang B.S., Minn A.J., Thompson C.B., Fesik S.W. Science 275:983-986(1997) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 1-209.
[22]	"Rationale for Bcl-xL/Bad peptide complex formation from structure, mutagenesis, and biophysical studies." Petros A.M., Nettesheim D.G., Wang Y., Olejniczak E.T., Meadows R.P., Mack J., Swift K., Matayoshi E.D., Zhang H., Thompson C.B., Fesik S.W. Protein Sci. 9:2528-2534(2000) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 1-209 IN COMPLEX WITH BAD.
[23]	"Bcl-XL mutations suppress cellular sensitivity to antimycin A." Manion M.K., O'Neill J.W., Giedt C.D., Kim K.M., Zhang K.Y.Z., Hockenbery D.M. J. Biol. Chem. 279:2159-2165(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1-211.
[24]	"An inhibitor of Bcl-2 family proteins induces regression of solid tumours." Oltersdorf T., Elmore S.W., Shoemaker A.R., Armstrong R.C., Augeri D.J., Belli B.A., Bruncko M., Deckwerth T.L., Dinges J., Hajduk P.J., Joseph M.K., Kitada S., Korsmeyer S.J., Kunzer A.R., Letai A., Li C., Mitten M.J., Nettesheim D.G. Rosenberg S.H. Nature 435:677-681(2005) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 1-209.
[25]	"BCL-XL dimerization by three-dimensional domain swapping." O'Neill J.W., Manion M.K., Maguire B., Hockenbery D.M. J. Mol. Biol. 356:367-381(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.45 ANGSTROMS) OF 1-211, HOMODIMERIZATION.
[26]	"Crystal structure of the Bcl-XL-Beclin 1 peptide complex: Beclin 1 is a novel BH3-only protein." Oberstein A., Jeffrey P.D., Shi Y. J. Biol. Chem. 282:13123-13132(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 83-209 IN COMPLEX WITH BECN1.
[27]	"Studies leading to potent, dual inhibitors of Bcl-2 and Bcl-xL." Bruncko M., Oost T.K., Belli B.A., Ding H., Joseph M.K., Kunzer A., Martineau D., McClellan W.J., Mitten M., Ng S.-C., Nimmer P.M., Oltersdorf T., Park C.-M., Petros A.M., Shoemaker A.R., Song X., Wang X., Wendt M.D. Elmore S.W. J. Med. Chem. 50:641-662(2007) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 1-209.
[28]	"Structural changes in the BH3 domain of SOUL protein upon interaction with the anti-apoptotic protein Bcl-xL." Ambrosi E., Capaldi S., Bovi M., Saccomani G., Perduca M., Monaco H.L. Biochem. J. 438:291-301(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1-209 IN COMPLEX WITH HEBP2, INTERACTION WITH HEBP2.
[29]	"PUMA binding induces partial unfolding within BCL-xL to disrupt p53 binding and promote apoptosis." Follis A.V., Chipuk J.E., Fisher J.C., Yun M.K., Grace C.R., Nourse A., Baran K., Ou L., Min L., White S.W., Green D.R., Kriwacki R.W. Nat. Chem. Biol. 9:163-168(2013) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-209 IN COMPLEX WITH BBC3, STRUCTURE BY NMR OF 1-209 IN COMPLEX WITH BBC3, INTERACTION WITH BBC3 AND TP53.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z23115 mRNA. Translation: CAA80661.1.
Z23116 mRNA. Translation: CAA80662.1.
U72398 Genomic DNA. Translation: AAB17354.1.
CR936637 mRNA. Translation: CAI56777.1.
BT007208 mRNA. Translation: AAP35872.1.
AL160175, AL117381 Genomic DNA. Translation: CAI12811.1.
AL117381, AL160175 Genomic DNA. Translation: CAI23025.1.
CH471077 Genomic DNA. Translation: EAW76424.1.
CH471077 Genomic DNA. Translation: EAW76425.1.
CH471077 Genomic DNA. Translation: EAW76429.1.
BC019307 mRNA. Translation: AAH19307.1.

IPI

IPI00019983.
IPI00219133.
IPI00219134.

PIR

B47537.
JE0203.

RefSeq

NP_001182.1. NM_001191.2.
NP_612815.1. NM_138578.1.

UniGene

Hs.516966.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BXL	NMR	-	A	1-209	[»]
1G5J	NMR	-	A	1-209	[»]
1LXL	NMR	-	A	1-209	[»]
1MAZ	X-ray	2.20	A	1-209	[»]
1R2D	X-ray	1.95	A	1-211	[»]
1R2E	X-ray	2.10	A	1-211	[»]
1R2G	X-ray	2.70	A	1-211	[»]
1R2H	X-ray	2.20	A	1-211	[»]
1R2I	X-ray	2.00	A	1-211	[»]
1YSG	NMR	-	A	1-209	[»]
1YSI	NMR	-	A	1-209	[»]
1YSN	NMR	-	A	1-209	[»]
2B48	X-ray	3.45	A	1-211	[»]
2LP8	NMR	-	A	1-209	[»]
2LPC	NMR	-	A	1-209	[»]
2M03	NMR	-	A	1-209	[»]
2M04	NMR	-	A	1-209	[»]
2O1Y	NMR	-	A	1-209	[»]
2O2M	NMR	-	A	2-196	[»]
2O2N	NMR	-	A	2-196	[»]
2P1L	X-ray	2.50	A/C/E/G	1-209	[»]
2PON	NMR	-	B	1-196	[»]
2YJ1	X-ray	2.24	A/C	1-209	[»]
2YQ6	X-ray	1.80	A	1-209	[»]
2YQ7	X-ray	1.90	A	1-209	[»]
2YXJ	X-ray	2.20	A/B	1-209	[»]
3CVA	X-ray	2.70	X	1-211	[»]
3FDL	X-ray	1.78	A	1-209	[»]
3FDM	X-ray	2.26	A/B/C	1-209	[»]
3INQ	X-ray	2.00	A/B	1-209	[»]
3IO8	X-ray	2.30	A/C	1-209	[»]
3PL7	X-ray	2.61	A/B	1-209	[»]
3QKD	X-ray	2.02	A/B	1-209	[»]
3R85	X-ray	1.95	A/B/C/D	1-209	[»]
3SP7	X-ray	1.40	A	1-209	[»]
3SPF	X-ray	1.70	A	1-200	[»]
4A1U	X-ray	1.54	A	1-209	[»]
4A1W	X-ray	2.50	A/B/C/D	1-209	[»]
4AQ3	X-ray	2.40	A/B/C/D/E/F	15-44	[»]
4EHR	X-ray	2.09	A	1-209	[»]
4HNJ	X-ray	2.90	A/B	1-209	[»]

DisProt

DP00298.

ProteinModelPortal

Q07817.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-30916N.

IntAct

Q07817. 33 interactions.

MINT

MINT-89538.

STRING

9606.ENSP00000302564.

Protein family/group databases

TCDB

1.A.21.1.1. bcl-2 (Bcl-2) family.

PTM databases

PhosphoSite

Q07817.

Polymorphism databases

DMDM

728955.

Proteomic databases

PaxDb

Q07817.

PRIDE

Q07817.

Protocols and materials databases

DNASU

598.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000307677; ENSP00000302564; ENSG00000171552.
ENST00000376055; ENSP00000365223; ENSG00000171552.
ENST00000376062; ENSP00000365230; ENSG00000171552.
ENST00000420653; ENSP00000405563; ENSG00000171552.

GeneID

598.

KEGG

hsa:598.

UCSC

uc002wwl.3. human.

Organism-specific databases

CTD

598.

GeneCards

GC20M030252.

HGNC

HGNC:992. BCL2L1.

HPA

CAB000105.

MIM

600039. gene.

neXtProt

NX_Q07817.

PharmGKB

PA76.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG300479.

HOGENOM

HOG000056452.

InParanoid

Q07817.

K04570.

OMA

NGSPSWH.

OrthoDB

EOG47PX6Z.

PhylomeDB

Q07817.

Enzyme and pathway databases

Pathway_Interaction_DB

pi3kciaktpathway. Class I PI3K signaling events mediated by Akt.
epopathway. EPO signaling pathway.
il2_pi3kpathway. IL2 signaling events mediated by PI3K.
il2_stat5pathway. IL2 signaling events mediated by STAT5.
il4_2pathway. IL4-mediated signaling events.
il6_7pathway. IL6-mediated signaling events.
nfat_3pathway. Role of Calcineurin-dependent NFAT signaling in lymphocytes.

Reactome

REACT_578. Apoptosis.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

Q07817.

Bgee

Q07817.

CleanEx

HS_BCL2L1.

Genevestigator

Q07817.

GermOnline

ENSG00000171552. Homo sapiens.

Family and domain databases

InterPro

IPR013279. Apop_reg_BclX.
IPR002475. Bcl2-like.
IPR004725. Bcl2/BclX.
IPR020717. Bcl2_BH1_motif_CS.
IPR020726. Bcl2_BH2_motif_CS.
IPR020728. Bcl2_BH3_motif_CS.
IPR003093. Bcl2_BH4.
IPR020731. Bcl2_BH4_motif_CS.
IPR026298. Blc2_fam.
[Graphical view]

PANTHER

PTHR11256. PTHR11256. 1 hit.
PTHR11256:SF12. PTHR11256:SF12. 1 hit.

Pfam

PF00452. Bcl-2. 1 hit.
PF02180. BH4. 1 hit.
[Graphical view]

PRINTS

PR01864. APOPREGBCLX.
PR01862. BCL2FAMILY.

SMART

SM00265. BH4. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00865. bcl-2. 1 hit.

PROSITE

PS50062. BCL2_FAMILY. 1 hit.
PS01080. BH1. 1 hit.
PS01258. BH2. 1 hit.
PS01259. BH3. 1 hit.
PS01260. BH4_1. 1 hit.
PS50063. BH4_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q07817.

ChEMBL

CHEMBL4625.

ChiTaRS

BCL2L1. human.

EvolutionaryTrace

Q07817.

GenomeRNAi

598.

NextBio

2433.

PMAP-CutDB

Q07817.

SOURCE

Search...

Entry information

Entry name

B2CL1_HUMAN

Accession

Primary (citable) accession number: Q07817
Secondary accession number(s): E1P5L6

Q92976

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	May 29, 2013
This is version 163 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.

Relevant documents

Human chromosome 20

Human chromosome 20: 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

Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·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

Sites

Amino acid modifications

Natural variations

Experimental info

Secondary structure

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents