(data stored in ACNUC9552 zone)

HOGENOM: HS20_PE662

ID   HS20_PE662                           STANDARD;      PRT;   233 AA.
AC   HS20_PE662; Q07817; E1P5L6; Q5CZ89; Q5TE65; Q92976;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Bcl-2-like protein 1; Short=Bcl2-L-1;AltName:
DE   Full=Apoptosis regulator Bcl-X; (HS20.PE662).
GN   Name=BCL2L1; Synonyms=BCL2L, BCLX;
OS   HOMO SAPIENS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Primates; Haplorrhini; Simiiformes; Catarrhini;
OC   Hominoidea; Hominidae; Homininae; Homo.
OX   NCBI_TaxID=9606;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS HS20.PE662.
CC       Homo sapiens chromosome 20 GRCh37  sequence 1..62965520 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:B2CL1_HUMAN
CC   -!- FUNCTION: Potent inhibitor of cell death. Inhibits activation of
CC       caspases (By similarity). Appears to regulate cell death by
CC       blocking the voltage-dependent anion channnel (VDAC) by binding to
CC       it and preventing the release of the caspase activator, CYC1, from
CC       the mitochondrial membrane.
CC   -!- FUNCTION: Isoform Bcl-X(S) promotes apoptosis.
CC   -!- SUBUNIT: Homodimer. Isoform Bcl-X(L) forms heterodimers with BAX,
CC       BAK or BCL2. Heterodimerization with BAX does not seem to be
CC       required for anti-apoptotic activity. Interacts with BCL2L11.
CC       Interacts with DMN1L; the interaction stimulates the GTPase
CC       activity of DMN1L in synapses and increases the number of axonal
CC       mitochondria and the size and number of synaptic vesicle clusters
CC       (By similarity). Interacts with BAD and BBC3. Interacts (isoform
CC       Bcl-X(L)) with SIVA1 (isoform 1); the interaction inhibits the
CC       anti-apoptotic activity. Interacts with BECN1 and PGAM5. Interacts
CC       (isoform Bcl-X(L)) with BAX (isoform Sigma). Isoform Bcl-X(L)
CC       interacts with IKZF3.
CC   -!- INTERACTION:
CC       Q92934:BAD; NbExp=6; IntAct=EBI-287195, EBI-700771;
CC       Q61337:Bad (xeno); NbExp=2; IntAct=EBI-287195, EBI-400328;
CC       Q16611:BAK1; NbExp=3; IntAct=EBI-78035, EBI-519866;
CC       Q07812:BAX; NbExp=2; IntAct=EBI-287195, EBI-516580;
CC       Q9BXH1:BBC3; NbExp=6; IntAct=EBI-287195, EBI-519884;
CC       Q99ML1:Bbc3 (xeno); NbExp=3; IntAct=EBI-287195, EBI-727801;
CC       Q07817-1:BCL2L1; NbExp=3; IntAct=EBI-287195, EBI-287195;
CC       O43521:BCL2L11; NbExp=4; IntAct=EBI-287195, EBI-526406;
CC       O43521-1:BCL2L11; NbExp=2; IntAct=EBI-287195, EBI-526416;
CC       Q13323:BIK; NbExp=2; IntAct=EBI-78035, EBI-700794;
CC       P30429:ced-4 (xeno); NbExp=3; IntAct=EBI-78035, EBI-494118;
CC       O00198:HRK; NbExp=2; IntAct=EBI-287195, EBI-701322;
CC       Q9C000:NLRP1; NbExp=9; IntAct=EBI-78035, EBI-1220518;
CC       O15304:SIVA1; NbExp=2; IntAct=EBI-78035, EBI-520756;
CC       O15304-1:SIVA1; NbExp=5; IntAct=EBI-287195, EBI-520766;
CC       Q9H2V7:SPNS1; NbExp=3; IntAct=EBI-78035, EBI-1386527;
CC       P04637:TP53; NbExp=2; IntAct=EBI-287195, EBI-366083;
CC       P02340:Tp53 (xeno); NbExp=3; IntAct=EBI-287195, EBI-474016;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane; Single-pass membrane
CC       protein (By similarity). Nucleus membrane; Single-pass membrane
CC       protein; Cytoplasmic side (By similarity). Note=Mitochondrial
CC       membranes and perinuclear envelope (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=Bcl-X(L);
CC         IsoId=Q07817-1; Sequence=Displayed;
CC       Name=Bcl-X(S);
CC         IsoId=Q07817-2; Sequence=VSP_000515;
CC       Name=Bcl-X(beta);
CC         IsoId=Q07817-3; Sequence=VSP_000516;
CC   -!- TISSUE SPECIFICITY: Bcl-X(S) is expressed at high levels in cells
CC       that undergo a high rate of turnover, such as developing
CC       lymphocytes. In contrast, Bcl-X(L) is found in tissues containing
CC       long-lived postmitotic cells, such as adult brain.
CC   -!- DOMAIN: The BH4 motif is required for anti-apoptotic activity. The
CC       BH1 and BH2 motifs are required for both heterodimerization with
CC       other Bcl-2 family members and for repression of cell death.
CC   -!- PTM: Proteolytically cleaved by caspases during apoptosis. The
CC       cleaved protein, lacking the BH4 motif, has pro-apoptotic
CC       activity.
CC   -!- SIMILARITY: Belongs to the Bcl-2 family.
CC   -!- GENE_FAMILY: HOG000056452 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Homo_sapiens;ENSG00000171552;ENST00000376062;ENSP00000365230.
DR   EMBL; AL117381; - ;
DR   EMBL; AL160175; - ;
DR   EMBL; BC019307; - ;
DR   EMBL; BT007208; - ;
DR   EMBL; CR936637; - ;
DR   EMBL; U72398; - ;
DR   EMBL; Z23115; - ;
DR   EMBL; Z23116; - ;
DR   UniProtKB/Swiss-Prot; Q07817; E1P5L6; Q5CZ89; Q5TE65; Q92976; -.
DR   EMBL; Z23115; CAA80661.1; -; mRNA.
DR   EMBL; Z23116; CAA80662.1; -; mRNA.
DR   EMBL; U72398; AAB17354.1; -; Genomic_DNA.
DR   EMBL; CR936637; CAI56777.1; -; mRNA.
DR   EMBL; BT007208; AAP35872.1; -; mRNA.
DR   EMBL; AL160175; CAI12811.1; -; Genomic_DNA.
DR   EMBL; AL117381; CAI12811.1; JOINED; Genomic_DNA.
DR   EMBL; AL117381; CAI23025.1; -; Genomic_DNA.
DR   EMBL; AL160175; CAI23025.1; JOINED; Genomic_DNA.
DR   EMBL; CH471077; EAW76424.1; -; Genomic_DNA.
DR   EMBL; CH471077; EAW76425.1; -; Genomic_DNA.
DR   EMBL; CH471077; EAW76429.1; -; Genomic_DNA.
DR   EMBL; BC019307; AAH19307.1; -; mRNA.
DR   IPI; IPI00019983; -.
DR   IPI; IPI00219133; -.
DR   IPI; IPI00219134; -.
DR   PIR; B47537; B47537.
DR   PIR; JE0203; JE0203.
DR   RefSeq; NP_001182.1; NM_001191.2.
DR   RefSeq; NP_612815.1; NM_138578.1.
DR   UniGene; Hs.516966; -.
DR   PDB; 1BXL; NMR; -; A=1-209.
DR   PDB; 1G5J; NMR; -; A=1-209.
DR   PDB; 1LXL; NMR; -; A=1-209.
DR   PDB; 1MAZ; X-ray; 2.20 A; A=1-209.
DR   PDB; 1R2D; X-ray; 1.95 A; A=1-211.
DR   PDB; 1R2E; X-ray; 2.10 A; A=1-211.
DR   PDB; 1R2G; X-ray; 2.70 A; A=1-211.
DR   PDB; 1R2H; X-ray; 2.20 A; A=1-211.
DR   PDB; 1R2I; X-ray; 2.00 A; A=1-211.
DR   PDB; 1YSG; NMR; -; A=1-209.
DR   PDB; 1YSI; NMR; -; A=1-209.
DR   PDB; 1YSN; NMR; -; A=1-209.
DR   PDB; 2B48; X-ray; 3.45 A; A=1-211.
DR   PDB; 2O1Y; NMR; -; A=1-209.
DR   PDB; 2O2M; NMR; -; A=2-196.
DR   PDB; 2O2N; NMR; -; A=2-196.
DR   PDB; 2P1L; X-ray; 2.50 A; A/C/E/G=1-209.
DR   PDB; 2PON; NMR; -; B=1-196.
DR   PDB; 2YXJ; X-ray; 2.20 A; A/B=1-209.
DR   PDB; 3CVA; X-ray; 2.70 A; X=1-211.
DR   PDB; 3FDL; X-ray; 1.78 A; A=1-209.
DR   PDB; 3FDM; X-ray; 2.26 A; A/B/C=1-209.
DR   PDB; 3INQ; X-ray; 2.00 A; A/B=1-209.
DR   PDB; 3IO8; X-ray; 2.30 A; A/C=1-209.
DR   PDB; 3PL7; X-ray; 2.61 A; A/B=1-209.
DR   PDB; 3QKD; X-ray; 2.02 A; A/B=1-209.
DR   PDB; 3R85; X-ray; 1.95 A; A/B/C/D=1-209.
DR   PDBsum; 1BXL; -.
DR   PDBsum; 1G5J; -.
DR   PDBsum; 1LXL; -.
DR   PDBsum; 1MAZ; -.
DR   PDBsum; 1R2D; -.
DR   PDBsum; 1R2E; -.
DR   PDBsum; 1R2G; -.
DR   PDBsum; 1R2H; -.
DR   PDBsum; 1R2I; -.
DR   PDBsum; 1YSG; -.
DR   PDBsum; 1YSI; -.
DR   PDBsum; 1YSN; -.
DR   PDBsum; 2B48; -.
DR   PDBsum; 2O1Y; -.
DR   PDBsum; 2O2M; -.
DR   PDBsum; 2O2N; -.
DR   PDBsum; 2P1L; -.
DR   PDBsum; 2PON; -.
DR   PDBsum; 2YXJ; -.
DR   PDBsum; 3CVA; -.
DR   PDBsum; 3FDL; -.
DR   PDBsum; 3FDM; -.
DR   PDBsum; 3INQ; -.
DR   PDBsum; 3IO8; -.
DR   PDBsum; 3PL7; -.
DR   PDBsum; 3QKD; -.
DR   PDBsum; 3R85; -.
DR   ProteinModelPortal; Q07817; -.
DR   SMR; Q07817; 1-210.
DR   DisProt; DP00298; -.
DR   DIP; DIP-30916N; -.
DR   IntAct; Q07817; 42.
DR   MINT; MINT-89538; -.
DR   STRING; Q07817; -.
DR   TCDB; 1.A.21.1.1; bcl-2 (Bcl-2) family.
DR   PhosphoSite; Q07817; -.
DR   PRIDE; Q07817; -.
DR   Ensembl; ENST00000307677; ENSP00000302564; ENSG00000171552.
DR   Ensembl; ENST00000376062; ENSP00000365230; ENSG00000171552.
DR   Ensembl; ENST00000420653; ENSP00000405563; ENSG00000171552.
DR   GeneID; 598; -.
DR   KEGG; hsa:598; -.
DR   UCSC; uc002wwl.1; human.
DR   CTD; 598; -.
DR   GeneCards; GC20M027040; -.
DR   H-InvDB; HIX0015713; -.
DR   HGNC; HGNC:992; BCL2L1.
DR   HPA; CAB000105; -.
DR   MIM; 600039; gene.
DR   neXtProt; NX_Q07817; -.
DR   PharmGKB; PA76; -.
DR   eggNOG; prNOG07177; -.
DR   InParanoid; Q07817; -.
DR   OMA; NGSPSWH; -.
DR   OrthoDB; EOG47PX6Z; -.
DR   PhylomeDB; Q07817; -.
DR   Pathway_Interaction_DB; pi3kciaktpathway; Class I PI3K signaling events mediated by Akt.
DR   Pathway_Interaction_DB; epopathway; EPO signaling pathway.
DR   Pathway_Interaction_DB; il2_pi3kpathway; IL2 signaling events mediated by PI3K.
DR   Pathway_Interaction_DB; il2_stat5pathway; IL2 signaling events mediated by STAT5.
DR   Pathway_Interaction_DB; il4_2pathway; IL4-mediated signaling events.
DR   Pathway_Interaction_DB; il6_7pathway; IL6-mediated signaling events.
DR   Pathway_Interaction_DB; nfat_3pathway; Role of Calcineurin-dependent NFAT signaling in lymphocytes.
DR   Reactome; REACT_578; Apoptosis.
DR   Reactome; REACT_6900; Immune System.
DR   NextBio; 2433; -.
DR   PMAP-CutDB; Q07817; -.
DR   ArrayExpress; Q07817; -.
DR   Bgee; Q07817; -.
DR   CleanEx; HS_BCL2L1; -.
DR   Genevestigator; Q07817; -.
DR   GermOnline; ENSG00000171552; Homo sapiens.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005741; C:mitochondrial outer membrane; NAS:UniProtKB.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051434; F:BH3 domain binding; IPI:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0008629; P:induction of apoptosis by intracellular signals; TAS:Reactome.
DR   GO; GO:0090005; P:negative regulation of establishment of protein localization in plasma membrane; IDA:BHF-UCL.
DR   GO; GO:0008634; P:negative regulation of survival gene product expression; TAS:ProtInc.
DR   GO; GO:0046902; P:regulation of mitochondrial membrane permeability; IDA:HGNC.
DR   GO; GO:0051881; P:regulation of mitochondrial membrane potential; IDA:HGNC.
DR   GO; GO:0001836; P:release of cytochrome c from mitochondria; IDA:HGNC.
DR   GO; GO:0034097; P:response to cytokine stimulus; IDA:MGI.
DR   InterPro; IPR013279; Apop_reg_BclX.
DR   InterPro; IPR002475; Bcl2-like_apoptosis.
DR   InterPro; IPR000712; Bcl2_BH.
DR   InterPro; IPR020717; Bcl2_BH1_motif_CS.
DR   InterPro; IPR020726; Bcl2_BH2_motif_CS.
DR   InterPro; IPR020728; Bcl2_BH3_motif_CS.
DR   InterPro; IPR003093; Bcl2_BH4.
DR   InterPro; IPR020731; Bcl2_BH4_motif_CS.
DR   InterPro; IPR004725; Bcl2_reg.
DR   Pfam; PF00452; Bcl-2; 1.
DR   Pfam; PF02180; BH4; 1.
DR   PRINTS; PR01864; APOPREGBCLX.
DR   PRINTS; PR01862; BCL2FAMILY.
DR   SMART; SM00337; BCL; 1.
DR   SMART; SM00265; BH4; 1.
DR   TIGRFAMs; TIGR00865; Bcl-2; 1.
DR   PROSITE; PS50062; BCL2_FAMILY; 1.
DR   PROSITE; PS01080; BH1; 1.
DR   PROSITE; PS01258; BH2; 1.
DR   PROSITE; PS01259; BH3; 1.
DR   PROSITE; PS01260; BH4_1; 1.
DR   PROSITE; PS50063; BH4_2; 1.
DR   HOGENOMDNA; HS20.PE662; -.
KW   ENSG000001715521755old_1320000031; ENSP000003652307901old_1320000031;
KW   Q5QP56_HUMAN; Q5QP59_HUMAN; Q5TE64_HUMAN; Q9H1R6_HUMAN; AL117381;
KW   BC019307; BT007208; CR936637; U72398; Z23115; Z23116;
KW   3D-structure; Alternative splicing; Apoptosis; Complete proteome;
KW   Membrane; Mitochondrion; Nucleus; Reference proteome; Transmembrane;
KW   Transmembrane helix.
SQ   SEQUENCE   233 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSQSNRELVV DFLSYKLSQK GYSWSQFSDV EENRTEAPEG TESEMETPSA INGNPSWHLA
     DSPAVNGATG HSSSLDAREV IPMAAVKQAL REAGDEFELR YRRAFSDLTS QLHITPGTAY
     QSFEQVVNEL FRDGVNWGRI VAFFSFGGAL CVESVDKEMQ VLVSRIAAWM ATYLNDHLEP
     WIQENGGWDT FVELYGNNAA AESRKGQERF NRWFLTGMTV AGVVLLGSLF SRK
//

If you have problems or comments...

PBIL Back to PBIL home page