Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q07817

- B2CL1_HUMAN

UniProt

Q07817 - B2CL1_HUMAN

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 178 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 binding Source: UniProtKB
    4. protein heterodimerization activity Source: RefGenome
    5. protein homodimerization activity Source: RefGenome
    6. 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. mitotic cell cycle checkpoint Source: UniProtKB
    22. negative regulation of anoikis Source: UniProtKB
    23. negative regulation of apoptotic process Source: UniProtKB
    24. negative regulation of autophagy Source: UniProtKB
    25. negative regulation of establishment of protein localization to plasma membrane Source: BHF-UCL
    26. negative regulation of execution phase of apoptosis Source: UniProtKB
    27. negative regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: BHF-UCL
    28. negative regulation of intrinsic apoptotic signaling pathway Source: BHF-UCL
    29. negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage Source: BHF-UCL
    30. negative regulation of neuron apoptotic process Source: Ensembl
    31. negative regulation of release of cytochrome c from mitochondria Source: BHF-UCL
    32. neuron apoptotic process Source: Ensembl
    33. nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway Source: Reactome
    34. ovarian follicle development Source: Ensembl
    35. positive regulation of apoptotic process Source: Ensembl
    36. positive regulation of cell proliferation Source: Ensembl
    37. positive regulation of intrinsic apoptotic signaling pathway Source: Reactome
    38. regulation of mitochondrial membrane permeability Source: HGNC
    39. regulation of mitochondrial membrane potential Source: HGNC
    40. release of cytochrome c from mitochondria Source: HGNC
    41. response to cycloheximide Source: Ensembl
    42. response to cytokine Source: MGI
    43. spermatogenesis Source: Ensembl
    44. suppression by virus of host apoptotic process Source: MGI

    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. cytosol Source: UniProtKB-SubCell
    6. integral component of membrane Source: UniProtKB-KW
    7. mitochondrial inner membrane Source: UniProtKB-SubCell
    8. mitochondrial matrix Source: UniProtKB-SubCell
    9. mitochondrial outer membrane Source: UniProtKB
    10. mitochondrion Source: HGNC
    11. nuclear membrane Source: UniProtKB-SubCell
    12. nucleolus Source: HPA
    13. nucleus Source: HPA
    14. synaptic vesicle membrane Source: UniProtKB-SubCell

    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.
    Mutagenesisi135 – 1373VNW → AIL: Loss of anti-apoptotic activity.
    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.
    Mutagenesisi148 – 1481G → E: No heterodimerization with BAX.
    Mutagenesisi156 – 1561D → A: No effect on caspase-1 cleavage.
    Mutagenesisi176 – 1761D → A: No effect on caspase-1 cleavage.
    Mutagenesisi188 – 1914WDTF → SVTC: Abolishes interaction with DNM1L and endocytosis enhancement.
    Mutagenesisi188 – 1892WD → GA: Reduces anti-apoptotic activity by about half.
    Mutagenesisi189 – 1891D → A: No effect on caspase-1 cleavage.

    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

    ArrayExpressiQ07817.
    BgeeiQ07817.
    CleanExiHS_BCL2L1.
    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-287195,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. 74 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 1-210.
    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.
    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: Q07817-1) [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

    MSQSNRELVV DFLSYKLSQK GYSWSQFSDV EENRTEAPEG TESEMETPSA    50
    INGNPSWHLA DSPAVNGATG HSSSLDAREV IPMAAVKQAL REAGDEFELR 100
    YRRAFSDLTS QLHITPGTAY QSFEQVVNEL FRDGVNWGRI VAFFSFGGAL 150
    CVESVDKEMQ VLVSRIAAWM ATYLNDHLEP WIQENGGWDT FVELYGNNAA 200
    AESRKGQERF NRWFLTGMTV AGVVLLGSLF SRK 233
    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 1-210.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107070. 74 interactions.
    DIPi DIP-30916N.
    IntActi Q07817. 58 interactions.
    MINTi MINT-89538.
    STRINGi 9606.ENSP00000302564.

    Chemistry

    BindingDBi Q07817.
    ChEMBLi CHEMBL4625.

    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.
    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

    ArrayExpressi Q07817.
    Bgeei Q07817.
    CleanExi HS_BCL2L1.
    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

    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 1, 2014
    This is version 178 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