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Q07817 (B2CL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 173. 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 1

Short name=Bcl2-L-1
Alternative name(s):
Apoptosis regulator Bcl-X
Gene names
Name:BCL2L1
Synonyms:BCL2L, BCLX
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length233 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Potent inhibitor of cell death. Inhibits activation of caspases. 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 Ref.20

Isoform Bcl-X(L) also regulates presynaptic plasticity, including neurotransmitter release and recovery, number of axonal mitochondria as well as size and number of synaptic vesicle clusters. During synaptic stimulation, increases ATP availability from mitochondria through regulation of mitochondrial membrane ATP synthase F1F0 activity and regulates endocytic vesicle retrieval in hippocampal neurons through association with DMN1L and stimulation of its GTPase activity in synaptic vesicles. Ref.17 Ref.19 Ref.20

Isoform Bcl-X(S) promotes apoptosis. Ref.17 Ref.19 Ref.20

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 BAD. Interacts (isoform Bcl-X(L))with SIVA1 (isoform 1);the interaction inhibits the anti-apoptotic activity. Interacts with BECN1 and PGAM5. 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. Isoform Bcl-X(L) interacts with DNM1L and CLTA; DNM1L and BCL2L1 isoform BCL-X(L)may form a complex in synaptic vesicles that also contains clathrin and MFF. Interacts with ATP5A and ATP5B; the interactions mediate the association of isoform Bcl-X(L) with the mitochondrial membrane ATP synthase F1F0 ATP synthase. Ref.2 Ref.9 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.20 Ref.26 Ref.29 Ref.30

Subcellular location

Isoform Bcl-X(L): Mitochondrion inner membrane By similarity. Mitochondrion outer membrane By similarity. Mitochondrion matrix By similarity. Cytoplasmic vesiclesecretory vesiclesynaptic vesicle membrane By similarity. Cytoplasmcytosol By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Nucleus membrane; Single-pass membrane protein; Cytoplasmic side By similarity. Note: After neuronal stimulation, translocates from cytosol to synaptic vesicle and mitochondrion membrane in a calmodulin-dependent manner 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 processApoptosis
Endocytosis
   Cellular componentCell junction
Cytoplasm
Cytoplasmic vesicle
Cytoskeleton
Membrane
Mitochondrion
Mitochondrion inner membrane
Mitochondrion outer membrane
Nucleus
Synapse
   Coding sequence diversityAlternative splicing
   DomainTransmembrane
Transmembrane helix
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic mitochondrial changes

Traceable author statement PubMed 9393856. Source: ProtInc

apoptotic process

Traceable author statement. Source: Reactome

apoptotic process in bone marrow

Inferred from electronic annotation. Source: Ensembl

cell proliferation

Inferred from electronic annotation. Source: Ensembl

cellular process regulating host cell cycle in response to virus

Inferred from electronic annotation. Source: Ensembl

cellular response to alkaloid

Inferred from electronic annotation. Source: Ensembl

cellular response to amino acid stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to gamma radiation

Inferred from electronic annotation. Source: Ensembl

cytokinesis

Inferred from mutant phenotype Ref.19. Source: UniProtKB

endocytosis

Inferred from electronic annotation. Source: UniProtKB-KW

extrinsic apoptotic signaling pathway in absence of ligand

Inferred from Biological aspect of Ancestor. Source: RefGenome

fertilization

Inferred from electronic annotation. Source: Ensembl

germ cell development

Inferred from electronic annotation. Source: Ensembl

growth

Inferred from electronic annotation. Source: Ensembl

hepatocyte apoptotic process

Inferred from electronic annotation. Source: Ensembl

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

innate immune response

Traceable author statement. Source: Reactome

intrinsic apoptotic signaling pathway

Traceable author statement. Source: Reactome

intrinsic apoptotic signaling pathway in response to DNA damage

Inferred from electronic annotation. Source: Ensembl

male gonad development

Inferred from electronic annotation. Source: Ensembl

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 9388232PubMed 21567405. 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 execution phase of apoptosis

Inferred from direct assay PubMed 20673843. Source: UniProtKB

negative regulation of extrinsic apoptotic signaling pathway in absence of ligand

Traceable author statement Ref.1. Source: BHF-UCL

negative regulation of intrinsic apoptotic signaling pathway

Inferred from direct assay Ref.15. Source: BHF-UCL

negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage

Inferred from direct assay PubMed 16608847. Source: BHF-UCL

negative regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of release of cytochrome c from mitochondria

Inferred by curator PubMed 21041309. Source: BHF-UCL

neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway

Traceable author statement. Source: Reactome

ovarian follicle development

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

response to cytokine

Inferred from direct assay PubMed 9184696. Source: MGI

spermatogenesis

Inferred from electronic annotation. Source: Ensembl

suppression by virus of host apoptotic process

Inferred from direct assay PubMed 15231831. Source: MGI

   Cellular_componentBcl-2 family protein complex

Inferred from direct assay PubMed 21199865. Source: UniProtKB

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

centrosome

Inferred from direct assay Ref.19. Source: UniProtKB

cytoplasm

Inferred from direct assay PubMed 20673843. Source: UniProtKB

cytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

mitochondrial inner membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrial outer membrane

Inferred from direct assay PubMed 19767770. Source: UniProtKB

mitochondrion

Inferred from direct assay Ref.15. Source: HGNC

nuclear membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleolus

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay. Source: HPA

synaptic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionBH3 domain binding

Inferred from physical interaction PubMed 15901672. Source: UniProtKB

identical protein binding

Inferred from physical interaction PubMed 21856303PubMed 15131699. Source: IntAct

protein heterodimerization activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein homodimerization activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein kinase binding

Inferred from physical interaction Ref.19. Source: UniProtKB

Complete GO annotation...

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 233233Bcl-2-like protein 1
PRO_0000143062

Regions

Transmembrane210 – 22617Helical; Potential
Motif4 – 2421BH4
Motif86 – 10015BH3
Motif129 – 14820BH1
Motif180 – 19516BH2

Sites

Site61 – 622Cleavage; by caspase-1

Amino acid modifications

Modified residue491Phosphoserine; by PLK3 Ref.19
Modified residue621Phosphoserine; by CDK1 Ref.17

Natural variations

Alternative sequence126 – 18863Missing in isoform Bcl-X(S).
VSP_000515
Alternative sequence189 – 23345DTFVE…LFSRK → VRTKPLVCPFSLASGQRSPT ALLLYLFLLCWVIVGDVDS in isoform Bcl-X(beta).
VSP_000516

Experimental info

Mutagenesis491S → A: Less stable at G2 checkpoint after DNA damage. Ref.10 Ref.19
Mutagenesis611D → A: No cleavage by caspase-1 nor by caspase-3. Ref.10 Ref.11
Mutagenesis131 – 1333FRD → VRA: No heterodimerization with BAX. Ref.10
Mutagenesis135 – 1373VNW → AIL: Loss of anti-apoptotic activity. Ref.10
Mutagenesis138 – 1403GRI → ELN: Loss of anti-apoptotic activity. Ref.9 Ref.10
Mutagenesis1381G → A: No heterodimerization with BAX. Ref.9 Ref.10
Mutagenesis145 – 1473SFG → YCC: Decreases interaction with DNM1L, no effect on endocytosis enhancement. Ref.10 Ref.20
Mutagenesis1481G → E: No heterodimerization with BAX. Ref.10
Mutagenesis1561D → A: No effect on caspase-1 cleavage. Ref.10
Mutagenesis1761D → A: No effect on caspase-1 cleavage. Ref.10
Mutagenesis188 – 1914WDTF → SVTC: Abolishes interaction with DNM1L and endocytosis enhancement. Ref.10 Ref.20
Mutagenesis188 – 1892WD → GA: Reduces anti-apoptotic activity by about half. Ref.10
Mutagenesis1891D → A: No effect on caspase-1 cleavage. Ref.10
Sequence conflict701G → A in CAA80661. Ref.1
Sequence conflict1681A → V in CAI56777. Ref.4

Secondary structure

................................... 233
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Bcl-X(L) (Bcl-xL) [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: E09D3CDD851AE9BE

FASTA23326,049
        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 »

FASTA17018,894
Isoform Bcl-X(beta) [UniParc].

Checksum: 1EF621E5D0744E4E
Show »

FASTA22725,290

References

« Hide '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. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., 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. 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 (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]"A Bcl-xL-Drp1 complex regulates synaptic vesicle membrane dynamics during endocytosis."
Li H., Alavian K.N., Lazrove E., Mehta N., Jones A., Zhang P., Licznerski P., Graham M., Uo T., Guo J., Rahner C., Duman R.S., Morrison R.S., Jonas E.A.
Nat. Cell Biol. 15:773-785(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DNM1L, FUNCTION, MUTAGENESIS OF 145-SER--GLY-147 AND 188-TRP--PHE-191.
[21]"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.
[22]"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.
[23]"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.
[24]"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.
[25]"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. expand/collapse author list , Ng S.-C., Nimmer P.M., O'Connor J.M., Oleksijew A., Petros A.M., Reed J.C., Shen W., Tahir S.K., Thompson C.B., Tomaselli K.J., Wang B., Wendt M.D., Zhang H., Fesik S.W., Rosenberg S.H.
Nature 435:677-681(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-209.
[26]"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.
[27]"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.
[28]"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. expand/collapse author list , Zhang H., Fesik S.W., Rosenberg S.H., Elmore S.W.
J. Med. Chem. 50:641-662(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-209.
[29]"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.
[30]"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.

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.
PIRB47537.
JE0203.
RefSeqNP_001182.1. NM_001191.2.
NP_612815.1. NM_138578.1.
XP_005260543.1. XM_005260486.2.
XP_005260544.1. XM_005260487.2.
UniGeneHs.516966.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BXLNMR-A1-209[»]
1G5JNMR-A1-209[»]
1LXLNMR-A1-209[»]
1MAZX-ray2.20A1-209[»]
1R2DX-ray1.95A1-211[»]
1R2EX-ray2.10A1-211[»]
1R2GX-ray2.70A1-211[»]
1R2HX-ray2.20A1-211[»]
1R2IX-ray2.00A1-211[»]
1YSGNMR-A1-209[»]
1YSINMR-A1-209[»]
1YSNNMR-A1-209[»]
2B48X-ray3.45A1-211[»]
2LP8NMR-A1-209[»]
2LPCNMR-A1-209[»]
2M03NMR-A1-209[»]
2M04NMR-A1-209[»]
2O1YNMR-A1-209[»]
2O2MNMR-A2-196[»]
2O2NNMR-A2-196[»]
2P1LX-ray2.50A/C/E/G1-209[»]
2PONNMR-B1-196[»]
2YJ1X-ray2.24A/C1-209[»]
2YQ6X-ray1.80A1-209[»]
2YQ7X-ray1.90A1-209[»]
2YXJX-ray2.20A/B1-209[»]
3CVAX-ray2.70X1-211[»]
3FDLX-ray1.78A1-209[»]
3FDMX-ray2.26A/B/C1-209[»]
3INQX-ray2.00A/B1-209[»]
3IO8X-ray2.30A/C1-209[»]
3PL7X-ray2.61A/B1-209[»]
3QKDX-ray2.02A/B1-209[»]
3R85X-ray1.95A/B/C/D1-209[»]
3SP7X-ray1.40A1-209[»]
3SPFX-ray1.70A1-200[»]
3WIZX-ray2.45A/B1-209[»]
3ZK6X-ray2.48A/B1-209[»]
3ZLNX-ray2.29A1-209[»]
3ZLOX-ray2.60A1-209[»]
3ZLRX-ray2.03A/B1-209[»]
4A1UX-ray1.54A1-209[»]
4A1WX-ray2.50A/B/C/D1-209[»]
4AQ3X-ray2.40A/B/C/D/E/F15-44[»]
4C52X-ray2.05A/B1-209[»]
4C5DX-ray2.30A/B1-209[»]
4EHRX-ray2.09A1-209[»]
4HNJX-ray2.90A/B1-209[»]
4IEHX-ray2.10A15-44[»]
DisProtDP00298.
ProteinModelPortalQ07817.
SMRQ07817. Positions 1-210.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107070. 74 interactions.
DIPDIP-30916N.
IntActQ07817. 54 interactions.
MINTMINT-89538.
STRING9606.ENSP00000302564.

Chemistry

BindingDBQ07817.
ChEMBLCHEMBL4625.

Protein family/group databases

TCDB1.A.21.1.1. the bcl-2 (bcl-2) family.

PTM databases

PhosphoSiteQ07817.

Polymorphism databases

DMDM728955.

Proteomic databases

PaxDbQ07817.
PRIDEQ07817.

Protocols and materials databases

DNASU598.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000307677; ENSP00000302564; ENSG00000171552. [Q07817-1]
ENST00000376055; ENSP00000365223; ENSG00000171552. [Q07817-2]
ENST00000376062; ENSP00000365230; ENSG00000171552. [Q07817-1]
ENST00000420653; ENSP00000405563; ENSG00000171552. [Q07817-1]
GeneID598.
KEGGhsa:598.
UCSCuc002wwl.3. human. [Q07817-1]

Organism-specific databases

CTD598.
GeneCardsGC20M030252.
HGNCHGNC:992. BCL2L1.
HPACAB000105.
HPA035734.
MIM600039. gene.
neXtProtNX_Q07817.
PharmGKBPA76.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG300479.
HOGENOMHOG000056452.
InParanoidQ07817.
KOK04570.
OMANGSPSWH.
OrthoDBEOG70GMGD.
PhylomeDBQ07817.
TreeFamTF315834.

Enzyme and pathway databases

ReactomeREACT_578. Apoptosis.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressQ07817.
BgeeQ07817.
CleanExHS_BCL2L1.
GenevestigatorQ07817.

Family and domain databases

InterProIPR013279. 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]
PANTHERPTHR11256. PTHR11256. 1 hit.
PTHR11256:SF12. PTHR11256:SF12. 1 hit.
PfamPF00452. Bcl-2. 1 hit.
PF02180. BH4. 1 hit.
[Graphical view]
PRINTSPR01864. APOPREGBCLX.
PR01862. BCL2FAMILY.
SMARTSM00265. BH4. 1 hit.
[Graphical view]
TIGRFAMsTIGR00865. bcl-2. 1 hit.
PROSITEPS50062. 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]
ProtoNetSearch...

Other

ChiTaRSBCL2L1. human.
EvolutionaryTraceQ07817.
GeneWikiBCL2-like_1_(gene).
GenomeRNAi598.
NextBio2433.
PMAP-CutDBQ07817.
PROQ07817.
SOURCESearch...

Entry information

Entry nameB2CL1_HUMAN
AccessionPrimary (citable) accession number: Q07817
Secondary accession number(s): E1P5L6 expand/collapse secondary AC list , Q5CZ89, Q5TE65, Q92976
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: April 16, 2014
This is version 173 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 20

Human chromosome 20: entries, gene names and cross-references to MIM