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Q07817

- B2CL1_HUMAN

UniProt

Q07817 - B2CL1_HUMAN

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Protein

Bcl-2-like protein 1

Gene

BCL2L1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.
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.
Isoform Bcl-X(S) promotes apoptosis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei61 – 622Cleavage; by caspase-1

GO - Molecular functioni

  1. BH3 domain binding Source: UniProt
  2. identical protein binding Source: IntAct
  3. protein heterodimerization activity Source: RefGenome
  4. protein homodimerization activity Source: RefGenome
  5. protein kinase binding Source: UniProtKB

GO - Biological processi

  1. apoptotic mitochondrial changes Source: ProtInc
  2. apoptotic process Source: Reactome
  3. apoptotic process in bone marrow Source: Ensembl
  4. cell proliferation Source: Ensembl
  5. cellular process regulating host cell cycle in response to virus Source: Ensembl
  6. cellular response to alkaloid Source: Ensembl
  7. cellular response to amino acid stimulus Source: Ensembl
  8. cellular response to gamma radiation Source: Ensembl
  9. cytokinesis Source: UniProtKB
  10. endocytosis Source: UniProtKB-KW
  11. extrinsic apoptotic signaling pathway in absence of ligand Source: RefGenome
  12. fertilization Source: Ensembl
  13. germ cell development Source: Ensembl
  14. growth Source: Ensembl
  15. hepatocyte apoptotic process Source: Ensembl
  16. innate immune response Source: Reactome
  17. intrinsic apoptotic signaling pathway Source: Reactome
  18. intrinsic apoptotic signaling pathway in response to DNA damage Source: Ensembl
  19. in utero embryonic development Source: Ensembl
  20. male gonad development Source: Ensembl
  21. mitochondrion morphogenesis Source: Ensembl
  22. mitotic cell cycle checkpoint Source: UniProtKB
  23. negative regulation of anoikis Source: UniProtKB
  24. negative regulation of apoptotic process Source: UniProtKB
  25. negative regulation of autophagy Source: UniProtKB
  26. negative regulation of establishment of protein localization to plasma membrane Source: BHF-UCL
  27. negative regulation of execution phase of apoptosis Source: UniProtKB
  28. negative regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: BHF-UCL
  29. negative regulation of intrinsic apoptotic signaling pathway Source: BHF-UCL
  30. negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage Source: BHF-UCL
  31. negative regulation of neuron apoptotic process Source: Ensembl
  32. negative regulation of release of cytochrome c from mitochondria Source: BHF-UCL
  33. neuron apoptotic process Source: Ensembl
  34. nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway Source: Reactome
  35. ovarian follicle development Source: Ensembl
  36. positive regulation of apoptotic process Source: Ensembl
  37. positive regulation of cell proliferation Source: Ensembl
  38. positive regulation of intrinsic apoptotic signaling pathway Source: Reactome
  39. regulation of mitochondrial membrane permeability Source: HGNC
  40. regulation of mitochondrial membrane potential Source: HGNC
  41. release of cytochrome c from mitochondria Source: HGNC
  42. response to cycloheximide Source: Ensembl
  43. response to cytokine Source: MGI
  44. spermatogenesis Source: Ensembl
  45. suppression by virus of host apoptotic process Source: MGI
Complete GO annotation...

Keywords - Biological processi

Apoptosis, Endocytosis

Enzyme and pathway databases

ReactomeiREACT_330. BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members.
REACT_75927. The NLRP1 inflammasome.

Protein family/group databases

TCDBi1.A.21.1.1. the bcl-2 (bcl-2) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Bcl-2-like protein 1
Short name:
Bcl2-L-1
Alternative name(s):
Apoptosis regulator Bcl-X
Gene namesi
Name:BCL2L1
Synonyms:BCL2L, BCLX
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:992. BCL2L1.

Subcellular locationi

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 By similarity; Single-pass membrane protein By similarity; 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.By similarity

GO - Cellular componenti

  1. Bcl-2 family protein complex Source: UniProtKB
  2. cell junction Source: UniProtKB-KW
  3. centrosome Source: UniProtKB
  4. cytoplasm Source: UniProtKB
  5. cytoplasmic vesicle Source: UniProtKB-KW
  6. cytosol Source: Ensembl
  7. integral component of membrane Source: UniProtKB-KW
  8. mitochondrial inner membrane Source: UniProtKB-KW
  9. mitochondrial outer membrane Source: UniProtKB
  10. mitochondrion Source: HGNC
  11. nucleolus Source: HPA
  12. nucleus Source: HPA
  13. synapse Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Membrane, Mitochondrion, Mitochondrion inner membrane, Mitochondrion outer membrane, Nucleus, Synapse

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi49 – 491S → A: Less stable at G2 checkpoint after DNA damage. 1 Publication
Mutagenesisi61 – 611D → A: No cleavage by caspase-1 nor by caspase-3. 1 Publication
Mutagenesisi131 – 1333FRD → VRA: No heterodimerization with BAX. 1 Publication
Mutagenesisi135 – 1373VNW → AIL: Loss of anti-apoptotic activity. 1 Publication
Mutagenesisi138 – 1403GRI → ELN: Loss of anti-apoptotic activity. 1 Publication
Mutagenesisi138 – 1381G → A: No heterodimerization with BAX. 1 Publication
Mutagenesisi145 – 1473SFG → YCC: Decreases interaction with DNM1L, no effect on endocytosis enhancement. 1 Publication
Mutagenesisi148 – 1481G → E: No heterodimerization with BAX. 1 Publication
Mutagenesisi156 – 1561D → A: No effect on caspase-1 cleavage. 1 Publication
Mutagenesisi176 – 1761D → A: No effect on caspase-1 cleavage. 1 Publication
Mutagenesisi188 – 1914WDTF → SVTC: Abolishes interaction with DNM1L and endocytosis enhancement. 1 Publication
Mutagenesisi188 – 1892WD → GA: Reduces anti-apoptotic activity by about half. 1 Publication
Mutagenesisi189 – 1891D → A: No effect on caspase-1 cleavage. 1 Publication

Organism-specific databases

PharmGKBiPA76.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 233233Bcl-2-like protein 1PRO_0000143062Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei49 – 491Phosphoserine; by PLK31 Publication
Modified residuei62 – 621Phosphoserine; by CDK11 Publication

Post-translational modificationi

Proteolytically cleaved by caspases during apoptosis. The cleaved protein, lacking the BH4 motif, has pro-apoptotic activity.1 Publication
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.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ07817.
PaxDbiQ07817.
PRIDEiQ07817.

PTM databases

PhosphoSiteiQ07817.

Miscellaneous databases

PMAP-CutDBQ07817.

Expressioni

Tissue specificityi

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.

Gene expression databases

BgeeiQ07817.
CleanExiHS_BCL2L1.
ExpressionAtlasiQ07817. baseline and differential.
GenevestigatoriQ07817.

Organism-specific databases

HPAiCAB000105.
HPA035734.

Interactioni

Subunit structurei

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.11 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-78035,EBI-78035
BADQ929346EBI-287195,EBI-700771
BadQ613372EBI-287195,EBI-400328From a different organism.
BAK1Q1661110EBI-287195,EBI-519866
BAXQ0781213EBI-287195,EBI-516580
BBC3Q9BXH17EBI-287195,EBI-519884
Bbc3Q99ML13EBI-287195,EBI-727801From a different organism.
BCL2L11O4352110EBI-287195,EBI-526406
BCL2L11O43521-12EBI-287195,EBI-526416
BECN1Q144574EBI-287195,EBI-949378
BIDP559576EBI-287195,EBI-519672
BIKQ133233EBI-287195,EBI-700794
ced-4P304293EBI-78035,EBI-494118From a different organism.
CLUP10909-46EBI-287195,EBI-4322678
CYCSP999992EBI-78035,EBI-446479
HRKO001983EBI-287195,EBI-701322
NLRP1Q9C0009EBI-78035,EBI-1220518
SIVA1O153042EBI-78035,EBI-520756
SIVA1O15304-15EBI-287195,EBI-520766
SPNS1Q9H2V73EBI-78035,EBI-1386527
TP53P0463718EBI-287195,EBI-366083
Tp53P023403EBI-287195,EBI-474016From a different organism.
TP53BP2Q136254EBI-287195,EBI-77642
VRK2Q86Y07-12EBI-287195,EBI-1207633

Protein-protein interaction databases

BioGridi107070. 77 interactions.
DIPiDIP-30916N.
IntActiQ07817. 58 interactions.
MINTiMINT-89538.
STRINGi9606.ENSP00000302564.

Structurei

Secondary structure

1
233
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1816
Turni19 – 213
Helixi24 – 263
Beta strandi29 – 368
Beta strandi38 – 414
Turni42 – 443
Beta strandi50 – 534
Beta strandi56 – 594
Turni65 – 684
Turni70 – 734
Beta strandi82 – 843
Helixi85 – 10117
Helixi102 – 1043
Helixi108 – 1114
Turni112 – 1143
Turni116 – 1183
Helixi120 – 13011
Turni131 – 1333
Helixi137 – 15620
Helixi162 – 17716
Helixi179 – 1846
Turni185 – 1873
Helixi188 – 19811
Helixi199 – 2057
Beta strandi206 – 2083

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
2ME8NMR-A1-209[»]
2ME9NMR-A1-209[»]
2MEJNMR-A1-198[»]
2O1YNMR-A1-209[»]
2O2MNMR-A2-20[»]
A83-196[»]
2O2NNMR-A2-20[»]
A83-196[»]
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/D1-197[»]
3SP7X-ray1.40A1-209[»]
3SPFX-ray1.70A1-209[»]
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/F29-44[»]
4BPKX-ray1.76A/B1-209[»]
4C52X-ray2.05A/B1-209[»]
4C5DX-ray2.30A/B1-209[»]
4EHRX-ray2.09A1-209[»]
4HNJX-ray2.90A/B1-209[»]
4IEHX-ray2.10A29-44[»]
DisProtiDP00298.
ProteinModelPortaliQ07817.
SMRiQ07817. Positions 1-209.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ07817.

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei210 – 22617HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi4 – 2421BH4Add
BLAST
Motifi86 – 10015BH3Add
BLAST
Motifi129 – 14820BH1Add
BLAST
Motifi180 – 19516BH2Add
BLAST

Domaini

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.

Sequence similaritiesi

Belongs to the Bcl-2 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG300479.
GeneTreeiENSGT00530000062935.
HOGENOMiHOG000056452.
InParanoidiQ07817.
KOiK04570.
OMAiNGSPSWH.
OrthoDBiEOG70GMGD.
PhylomeDBiQ07817.
TreeFamiTF315834.

Family and domain databases

InterProiIPR013279. 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]
PANTHERiPTHR11256. PTHR11256. 1 hit.
PTHR11256:SF12. PTHR11256:SF12. 1 hit.
PfamiPF00452. Bcl-2. 1 hit.
PF02180. BH4. 1 hit.
[Graphical view]
PRINTSiPR01864. APOPREGBCLX.
PR01862. BCL2FAMILY.
SMARTiSM00265. BH4. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00865. bcl-2. 1 hit.
PROSITEiPS50062. 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]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform Bcl-X(L) (identifier: Q07817) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MSQSNRELVV DFLSYKLSQK GYSWSQFSDV EENRTEAPEG TESEMETPSA
60 70 80 90 100
INGNPSWHLA DSPAVNGATG HSSSLDAREV IPMAAVKQAL REAGDEFELR
110 120 130 140 150
YRRAFSDLTS QLHITPGTAY QSFEQVVNEL FRDGVNWGRI VAFFSFGGAL
160 170 180 190 200
CVESVDKEMQ VLVSRIAAWM ATYLNDHLEP WIQENGGWDT FVELYGNNAA
210 220 230
AESRKGQERF NRWFLTGMTV AGVVLLGSLF SRK
Length:233
Mass (Da):26,049
Last modified:February 1, 1995 - v1
Checksum:iE09D3CDD851AE9BE
GO
Isoform Bcl-X(S) (identifier: Q07817-2) [UniParc]FASTAAdd to Basket

Also known as: Bcl-xS

The sequence of this isoform differs from the canonical sequence as follows:
     126-188: Missing.

Show »
Length:170
Mass (Da):18,894
Checksum:i75D1FC01EC06AD47
GO
Isoform Bcl-X(beta) (identifier: Q07817-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     189-233: DTFVELYGNN...VLLGSLFSRK → VRTKPLVCPF...CWVIVGDVDS

Show »
Length:227
Mass (Da):25,290
Checksum:i1EF621E5D0744E4E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti70 – 701G → A in CAA80661. (PubMed:8358789)Curated
Sequence conflicti168 – 1681A → V in CAI56777. (PubMed:17974005)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei126 – 18863Missing in isoform Bcl-X(S). CuratedVSP_000515Add
BLAST
Alternative sequencei189 – 23345DTFVE…LFSRK → VRTKPLVCPFSLASGQRSPT ALLLYLFLLCWVIVGDVDS in isoform Bcl-X(beta). CuratedVSP_000516Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS13188.1. [Q07817-2]
CCDS13189.1. [Q07817-1]
PIRiB47537.
JE0203.
RefSeqiNP_001182.1. NM_001191.2. [Q07817-2]
NP_612815.1. NM_138578.1. [Q07817-1]
XP_005260543.1. XM_005260486.2. [Q07817-1]
XP_005260544.1. XM_005260487.2. [Q07817-1]
UniGeneiHs.516966.

Genome annotation databases

EnsembliENST00000307677; ENSP00000302564; ENSG00000171552. [Q07817-1]
ENST00000376055; ENSP00000365223; ENSG00000171552. [Q07817-2]
ENST00000376062; ENSP00000365230; ENSG00000171552. [Q07817-1]
GeneIDi598.
KEGGihsa:598.
UCSCiuc002wwl.3. human. [Q07817-1]

Polymorphism databases

DMDMi728955.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS13188.1. [Q07817-2 ]
CCDS13189.1. [Q07817-1 ]
PIRi B47537.
JE0203.
RefSeqi NP_001182.1. NM_001191.2. [Q07817-2 ]
NP_612815.1. NM_138578.1. [Q07817-1 ]
XP_005260543.1. XM_005260486.2. [Q07817-1 ]
XP_005260544.1. XM_005260487.2. [Q07817-1 ]
UniGenei Hs.516966.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
2ME8 NMR - A 1-209 [» ]
2ME9 NMR - A 1-209 [» ]
2MEJ NMR - A 1-198 [» ]
2O1Y NMR - A 1-209 [» ]
2O2M NMR - A 2-20 [» ]
A 83-196 [» ]
2O2N NMR - A 2-20 [» ]
A 83-196 [» ]
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 1-197 [» ]
3SP7 X-ray 1.40 A 1-209 [» ]
3SPF X-ray 1.70 A 1-209 [» ]
3WIZ X-ray 2.45 A/B 1-209 [» ]
3ZK6 X-ray 2.48 A/B 1-209 [» ]
3ZLN X-ray 2.29 A 1-209 [» ]
3ZLO X-ray 2.60 A 1-209 [» ]
3ZLR X-ray 2.03 A/B 1-209 [» ]
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 29-44 [» ]
4BPK X-ray 1.76 A/B 1-209 [» ]
4C52 X-ray 2.05 A/B 1-209 [» ]
4C5D X-ray 2.30 A/B 1-209 [» ]
4EHR X-ray 2.09 A 1-209 [» ]
4HNJ X-ray 2.90 A/B 1-209 [» ]
4IEH X-ray 2.10 A 29-44 [» ]
DisProti DP00298.
ProteinModelPortali Q07817.
SMRi Q07817. Positions 1-209.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107070. 77 interactions.
DIPi DIP-30916N.
IntActi Q07817. 58 interactions.
MINTi MINT-89538.
STRINGi 9606.ENSP00000302564.

Chemistry

BindingDBi Q07817.
ChEMBLi CHEMBL3137283.

Protein family/group databases

TCDBi 1.A.21.1.1. the bcl-2 (bcl-2) family.

PTM databases

PhosphoSitei Q07817.

Polymorphism databases

DMDMi 728955.

Proteomic databases

MaxQBi Q07817.
PaxDbi Q07817.
PRIDEi Q07817.

Protocols and materials databases

DNASUi 598.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000307677 ; ENSP00000302564 ; ENSG00000171552 . [Q07817-1 ]
ENST00000376055 ; ENSP00000365223 ; ENSG00000171552 . [Q07817-2 ]
ENST00000376062 ; ENSP00000365230 ; ENSG00000171552 . [Q07817-1 ]
GeneIDi 598.
KEGGi hsa:598.
UCSCi uc002wwl.3. human. [Q07817-1 ]

Organism-specific databases

CTDi 598.
GeneCardsi GC20M030252.
HGNCi HGNC:992. BCL2L1.
HPAi CAB000105.
HPA035734.
MIMi 600039. gene.
neXtProti NX_Q07817.
PharmGKBi PA76.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG300479.
GeneTreei ENSGT00530000062935.
HOGENOMi HOG000056452.
InParanoidi Q07817.
KOi K04570.
OMAi NGSPSWH.
OrthoDBi EOG70GMGD.
PhylomeDBi Q07817.
TreeFami TF315834.

Enzyme and pathway databases

Reactomei REACT_330. BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members.
REACT_75927. The NLRP1 inflammasome.

Miscellaneous databases

ChiTaRSi BCL2L1. human.
EvolutionaryTracei Q07817.
GeneWikii BCL2-like_1_(gene).
GenomeRNAii 598.
NextBioi 2433.
PMAP-CutDB Q07817.
PROi Q07817.
SOURCEi Search...

Gene expression databases

Bgeei Q07817.
CleanExi HS_BCL2L1.
ExpressionAtlasi Q07817. baseline and differential.
Genevestigatori Q07817.

Family and domain databases

InterProi 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 ]
PANTHERi PTHR11256. PTHR11256. 1 hit.
PTHR11256:SF12. PTHR11256:SF12. 1 hit.
Pfami PF00452. Bcl-2. 1 hit.
PF02180. BH4. 1 hit.
[Graphical view ]
PRINTSi PR01864. APOPREGBCLX.
PR01862. BCL2FAMILY.
SMARTi SM00265. BH4. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00865. bcl-2. 1 hit.
PROSITEi 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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.
    , 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. 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. Cited for: MUTAGENESIS OF BH1 AND BH2 MOTIFS.
  11. Cited for: CLEAVAGE BY CASPASES, MUTAGENESIS OF ASP-61.
  12. 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. 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. 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. Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1-211.
  25. 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. 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.

Entry informationi

Entry nameiB2CL1_HUMAN
AccessioniPrimary (citable) accession number: Q07817
Secondary accession number(s): E1P5L6
, Q5CZ89, Q5TE65, Q92976
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: October 29, 2014
This is version 179 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3