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Bcl-2-like protein 1 (Bcl2-L-1) (Apoptosis regulator Bcl-X)

 B2CL1_MOUSE             Reviewed;         233 AA.
Q64373; O35844; Q60657; Q60658; Q61338;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
12-SEP-2018, entry version 180.
RecName: Full=Bcl-2-like protein 1;
Short=Bcl2-L-1;
AltName: Full=Apoptosis regulator Bcl-X;
Name=Bcl2l1; Synonyms=Bcl2l, Bclx;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BCL-X(L)).
STRAIN=2A4B; TISSUE=B-cell;
Kamesaki H., Michaud G.Y., Takatsu K., Okuma M.;
"IL-5 inhibits anti-IgM-induced apoptosis in an immature B cell line
through inductin of bcl-Xl.";
Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BCL-X(L) AND BCL-X(BETA)),
DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=7607090;
Gonzalez-Garcia M., Perez-Ballestero R., Ding L., Duan L., Boise L.H.,
Thompson C.B., Nunez G.;
"bcl-XL is the major bcl-x mRNA form expressed during murine
development and its product localizes to mitochondria.";
Development 120:3033-3042(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BCL-X(L); BCL-X(S) AND
BCL-X(DELTA-TM)).
TISSUE=Pre-B cell;
PubMed=7963517;
Fang W., Rivard J.J., Mueller D.L., Behrens T.W.;
"Cloning and molecular characterization of mouse bcl-x in B and T
lymphocytes.";
J. Immunol. 153:4388-4398(1994).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BCL-X(L) AND BCL-X(BETA)), AND
FUNCTION.
STRAIN=C57BL/6 X CBA; TISSUE=Thymus;
PubMed=9390687; DOI=10.1016/S1074-7613(00)80384-2;
Yang X.-F., Weber G.F., Cantor H.;
"A novel Bcl-x isoform connected to the T cell receptor regulates
apoptosis in T cells.";
Immunity 7:629-639(1997).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9144489;
Grillot D.A., Gonzalez-Garcia M., Ekhterae D., Duan L., Inohara N.,
Ohta S., Seldin M.F., Nunez G.;
"Genomic organization, promoter region analysis, and chromosome
localization of the mouse bcl-x gene.";
J. Immunol. 158:4750-4757(1997).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[7]
INTERACTION WITH BCL2L11.
PubMed=27013495; DOI=10.15252/embr.201541392;
Weber A., Heinlein M., Dengjel J., Alber C., Singh P.K., Haecker G.;
"The deubiquitinase Usp27x stabilizes the BH3-only protein Bim and
enhances apoptosis.";
EMBO Rep. 17:724-738(2016).
[8]
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 1-196 IN COMPLEX WITH
BCL2L11.
PubMed=14499110; DOI=10.1016/S1074-7613(03)00234-6;
Liu X., Dai S., Zhu Y., Marrack P., Kappler J.W.;
"The structure of a Bcl-xL/Bim fragment complex: implications for Bim
function.";
Immunity 19:341-352(2003).
-!- 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.
{ECO:0000269|PubMed:9390687}.
-!- FUNCTION: 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 F(1)F(0) activity and regulates endocytic vesicle
retrieval in hippocampal neurons through association with DMN1L
and stimulation of its GTPase activity in synaptic vesicles (By
similarity). May attenuate inflammation impairing NLRP1-
inflammasome activation, hence CASP1 activation and IL1B release
(By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q07817}.
-!- FUNCTION: Isoform Bcl-X(S) promotes apoptosis. {ECO:0000250}.
-!- SUBUNIT: 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 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. 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
ATP5F1A and ATP5F1B; the interactions mediate the association of
isoform Bcl-X(L) with the mitochondrial membrane ATP synthase
F(1)F(0) ATP synthase (By similarity). Interacts with VDAC1 (By
similarity). Isoform Bcl-X(L) interacts (via the loop between
motifs BH4 and BH3) with NLRP1 (via LRR repeats), but not with
NLRP2, NLRP3, NLRP4, PYCARD, nor MEFV. Interacts with BCL2L11 (via
BH3) (PubMed:27013495, PubMed:14499110). {ECO:0000250,
ECO:0000250|UniProtKB:Q07817, ECO:0000269|PubMed:14499110,
ECO:0000269|PubMed:27013495}.
-!- INTERACTION:
Q61337:Bad; NbExp=2; IntAct=EBI-526380, EBI-400328;
-!- SUBCELLULAR LOCATION: Mitochondrion membrane
{ECO:0000269|PubMed:7607090}; Single-pass membrane protein
{ECO:0000269|PubMed:7607090}. Nucleus membrane {ECO:0000250};
Single-pass membrane protein {ECO:0000250}; Cytoplasmic side
{ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing
center, centrosome {ECO:0000269|PubMed:7607090}. Note=Localizes to
the centrosome when phosphorylated at Ser-49.
-!- SUBCELLULAR LOCATION: Isoform Bcl-X(L): Mitochondrion inner
membrane. Mitochondrion outer membrane. Mitochondrion matrix
{ECO:0000250}. Cytoplasmic vesicle, secretory vesicle, synaptic
vesicle membrane {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}.
Note=After neuronal stimulation, translocates from cytosol to
synaptic vesicle and mitochondrion membrane in a calmodulin-
dependent manner. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform Bcl-X(delta-TM): Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=Bcl-X(L); Synonyms=Bcl-xL;
IsoId=Q64373-1; Sequence=Displayed;
Name=Bcl-X(S); Synonyms=Bcl-xS;
IsoId=Q64373-2; Sequence=VSP_000517;
Name=Bcl-X(beta);
IsoId=Q64373-3; Sequence=VSP_000518;
Name=Bcl-X(delta-TM);
IsoId=Q64373-4; Sequence=VSP_000519;
-!- TISSUE SPECIFICITY: Widely expressed, with highest levels in the
brain, thymus, bone marrow, and kidney. Bcl-X(L) and Bcl-X(delta-
TM) expression is enhanced in B- and T-lymphocytes that have been
activated. {ECO:0000269|PubMed:7607090}.
-!- DEVELOPMENTAL STAGE: Bcl-X(beta) is expressed in both embryonal
and postnatal tissues, whereas Bcl-X(L) is predominantly found in
postnatal tissues. {ECO:0000269|PubMed:7607090}.
-!- 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.
-!- DOMAIN: The loop between motifs BH4 and BH3 is required for the
interaction with NLRP1. {ECO:0000250|UniProtKB:Q07817}.
-!- PTM: Proteolytically cleaved by caspases during apoptosis. The
cleaved protein, lacking the BH4 motif, has pro-apoptotic
activity. {ECO:0000250}.
-!- PTM: 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 (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the Bcl-2 family. {ECO:0000305}.
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EMBL; X83574; CAA58557.1; -; mRNA.
EMBL; L35049; AAA51039.1; -; mRNA.
EMBL; L35048; AAA51040.1; -; mRNA.
EMBL; U10102; AAA82174.1; -; mRNA.
EMBL; U10101; AAA82173.1; -; mRNA.
EMBL; U10100; AAA82172.1; -; mRNA.
EMBL; U51278; AAC53459.1; -; mRNA.
EMBL; U51279; AAC53460.1; -; mRNA.
EMBL; U78031; AAB96881.1; -; Genomic_DNA.
EMBL; U78030; AAB96881.1; JOINED; Genomic_DNA.
CCDS; CCDS16899.1; -. [Q64373-1]
PIR; I49055; I49055.
PIR; I49056; I49056.
PIR; I49057; I49057.
RefSeq; NP_001276645.1; NM_001289716.1. [Q64373-1]
RefSeq; NP_001276646.1; NM_001289717.1. [Q64373-1]
RefSeq; NP_033873.3; NM_009743.5. [Q64373-1]
RefSeq; XP_006498672.1; XM_006498609.3.
RefSeq; XP_006498674.1; XM_006498611.3. [Q64373-1]
RefSeq; XP_006498675.1; XM_006498612.2. [Q64373-1]
RefSeq; XP_011237562.1; XM_011239260.2. [Q64373-1]
UniGene; Mm.238213; -.
PDB; 1PQ0; X-ray; 2.20 A; A=1-196.
PDB; 1PQ1; X-ray; 1.65 A; A=1-196.
PDB; 2BZW; X-ray; 2.30 A; A=1-211.
PDB; 3IHC; X-ray; 1.85 A; A=1-196.
PDB; 3IHD; X-ray; 1.88 A; A=1-196.
PDB; 3IHE; X-ray; 3.00 A; A=1-196.
PDB; 3IHF; X-ray; 2.28 A; A/B/C/D=1-196.
PDB; 3IIG; X-ray; 2.30 A; A=1-196.
PDB; 3IIH; X-ray; 2.75 A; A=1-196.
PDB; 3ILB; X-ray; 2.38 A; A/N=1-196.
PDB; 3ILC; X-ray; 1.64 A; A=1-196.
PDB; 4YJ4; X-ray; 2.10 A; A=1-196.
PDB; 4YK9; X-ray; 1.70 A; A/F=2-196.
PDB; 5C3G; X-ray; 2.45 A; A=1-26.
PDBsum; 1PQ0; -.
PDBsum; 1PQ1; -.
PDBsum; 2BZW; -.
PDBsum; 3IHC; -.
PDBsum; 3IHD; -.
PDBsum; 3IHE; -.
PDBsum; 3IHF; -.
PDBsum; 3IIG; -.
PDBsum; 3IIH; -.
PDBsum; 3ILB; -.
PDBsum; 3ILC; -.
PDBsum; 4YJ4; -.
PDBsum; 4YK9; -.
PDBsum; 5C3G; -.
ProteinModelPortal; Q64373; -.
SMR; Q64373; -.
BioGrid; 198323; 9.
ComplexPortal; CPX-2021; BAD:BCL-XL complex. [Q64373-1]
ComplexPortal; CPX-2025; BIM:BCL-XL complex. [Q64373-1]
ComplexPortal; CPX-2029; PUMA:BCL-XL complex. [Q64373-1]
ComplexPortal; CPX-2037; BID:BCL-XL complex. [Q64373-1]
ComplexPortal; CPX-299; BCL-XL complex. [Q64373-1]
CORUM; Q64373; -.
ELM; Q64373; -.
IntAct; Q64373; 8.
STRING; 10090.ENSMUSP00000007803; -.
BindingDB; Q64373; -.
ChEMBL; CHEMBL3309112; -.
iPTMnet; Q64373; -.
PhosphoSitePlus; Q64373; -.
PaxDb; Q64373; -.
PRIDE; Q64373; -.
Ensembl; ENSMUST00000007803; ENSMUSP00000007803; ENSMUSG00000007659. [Q64373-1]
Ensembl; ENSMUST00000109820; ENSMUSP00000105445; ENSMUSG00000007659. [Q64373-1]
Ensembl; ENSMUST00000134902; ENSMUSP00000134614; ENSMUSG00000007659. [Q64373-3]
Ensembl; ENSMUST00000140436; ENSMUSP00000134596; ENSMUSG00000007659. [Q64373-3]
GeneID; 12048; -.
KEGG; mmu:12048; -.
UCSC; uc008ngi.2; mouse. [Q64373-2]
UCSC; uc008ngj.2; mouse. [Q64373-1]
UCSC; uc008ngn.2; mouse. [Q64373-3]
CTD; 598; -.
MGI; MGI:88139; Bcl2l1.
eggNOG; KOG4728; Eukaryota.
eggNOG; ENOG41123S0; LUCA.
GeneTree; ENSGT00530000062935; -.
HOGENOM; HOG000056452; -.
InParanoid; Q64373; -.
KO; K04570; -.
OMA; NGSPSWH; -.
OrthoDB; EOG091G0OCU; -.
TreeFam; TF315834; -.
Reactome; R-MMU-111453; BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members.
Reactome; R-MMU-844455; The NLRP1 inflammasome.
EvolutionaryTrace; Q64373; -.
PMAP-CutDB; Q64373; -.
PRO; PR:Q64373; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000007659; Expressed in 289 organ(s), highest expression level in blood.
CleanEx; MM_BCL2L1; -.
ExpressionAtlas; Q64373; baseline and differential.
Genevisible; Q64373; MM.
GO; GO:0097136; C:Bcl-2 family protein complex; ISO:MGI.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005813; C:centrosome; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005622; C:intracellular; IDA:MGI.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0005740; C:mitochondrial envelope; ISO:MGI.
GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
GO; GO:0031966; C:mitochondrial membrane; IDA:MGI.
GO; GO:0005741; C:mitochondrial outer membrane; IDA:MGI.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
GO; GO:0098794; C:postsynapse; IEA:GOC.
GO; GO:0098793; C:presynapse; ISO:MGI.
GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0051400; F:BH domain binding; ISO:MGI.
GO; GO:0051434; F:BH3 domain binding; ISO:MGI.
GO; GO:0030276; F:clathrin binding; ISO:MGI.
GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; ISO:MGI.
GO; GO:0051020; F:GTPase binding; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0097371; F:MDM2/MDM4 family protein binding; ISO:MGI.
GO; GO:0046982; F:protein heterodimerization activity; IPI:MGI.
GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
GO; GO:0008134; F:transcription factor binding; ISO:MGI.
GO; GO:0071839; P:apoptotic process in bone marrow; IMP:MGI.
GO; GO:0008283; P:cell proliferation; IDA:MGI.
GO; GO:0060154; P:cellular process regulating host cell cycle in response to virus; IMP:MGI.
GO; GO:0071312; P:cellular response to alkaloid; IDA:MGI.
GO; GO:0071230; P:cellular response to amino acid stimulus; IMP:MGI.
GO; GO:0071480; P:cellular response to gamma radiation; IMP:MGI.
GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IMP:MGI.
GO; GO:0009566; P:fertilization; IGI:MGI.
GO; GO:0007281; P:germ cell development; IMP:MGI.
GO; GO:0097284; P:hepatocyte apoptotic process; IMP:MGI.
GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IMP:MGI.
GO; GO:0008584; P:male gonad development; IMP:MGI.
GO; GO:0070584; P:mitochondrion morphogenesis; IGI:MGI.
GO; GO:0007093; P:mitotic cell cycle checkpoint; ISS:UniProtKB.
GO; GO:2000811; P:negative regulation of anoikis; ISO:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:MGI.
GO; GO:1900118; P:negative regulation of execution phase of apoptosis; ISS:UniProtKB.
GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; ISO:MGI.
GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; ISO:MGI.
GO; GO:1902230; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage; ISO:MGI.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IDA:MGI.
GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; ISO:MGI.
GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; ISO:MGI.
GO; GO:0051402; P:neuron apoptotic process; IMP:MGI.
GO; GO:0001541; P:ovarian follicle development; IMP:MGI.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:MGI.
GO; GO:2001171; P:positive regulation of ATP biosynthetic process; ISO:MGI.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:MGI.
GO; GO:2000809; P:positive regulation of synaptic vesicle clustering; ISO:MGI.
GO; GO:1900244; P:positive regulation of synaptic vesicle endocytosis; ISO:MGI.
GO; GO:2000302; P:positive regulation of synaptic vesicle exocytosis; ISO:MGI.
GO; GO:0042981; P:regulation of apoptotic process; ISO:MGI.
GO; GO:0032465; P:regulation of cytokinesis; ISS:UniProtKB.
GO; GO:0040008; P:regulation of growth; IMP:MGI.
GO; GO:1900452; P:regulation of long term synaptic depression; ISO:MGI.
GO; GO:0046902; P:regulation of mitochondrial membrane permeability; ISO:MGI.
GO; GO:0051881; P:regulation of mitochondrial membrane potential; ISO:MGI.
GO; GO:0001836; P:release of cytochrome c from mitochondria; IGI:MGI.
GO; GO:0046898; P:response to cycloheximide; IDA:MGI.
GO; GO:0034097; P:response to cytokine; ISO:MGI.
GO; GO:0002931; P:response to ischemia; ISO:MGI.
GO; GO:0009314; P:response to radiation; IMP:MGI.
GO; GO:0009615; P:response to virus; IDA:MGI.
GO; GO:0007283; P:spermatogenesis; IGI:MGI.
GO; GO:0019050; P:suppression by virus of host apoptotic process; ISO:MGI.
GO; GO:0036466; P:synaptic vesicle recycling via endosome; ISO:MGI.
Gene3D; 1.10.437.10; -; 1.
InterPro; IPR013279; Apop_reg_BclX.
InterPro; IPR002475; Bcl2-like.
InterPro; IPR004725; Bcl2/BclX.
InterPro; IPR020717; Bcl2_BH1_motif_CS.
InterPro; IPR020726; Bcl2_BH2_motif_CS.
InterPro; IPR020728; Bcl2_BH3_motif_CS.
InterPro; IPR003093; Bcl2_BH4.
InterPro; IPR020731; Bcl2_BH4_motif_CS.
InterPro; IPR036834; Blc2-like_sf.
InterPro; IPR026298; Blc2_fam.
PANTHER; PTHR11256; PTHR11256; 1.
PANTHER; PTHR11256:SF12; PTHR11256:SF12; 1.
Pfam; PF00452; Bcl-2; 1.
Pfam; PF02180; BH4; 1.
PRINTS; PR01864; APOPREGBCLX.
PRINTS; PR01862; BCL2FAMILY.
SMART; SM00265; BH4; 1.
SUPFAM; SSF56854; SSF56854; 1.
TIGRFAMs; TIGR00865; bcl-2; 1.
PROSITE; PS50062; BCL2_FAMILY; 1.
PROSITE; PS01080; BH1; 1.
PROSITE; PS01258; BH2; 1.
PROSITE; PS01259; BH3; 1.
PROSITE; PS01260; BH4_1; 1.
PROSITE; PS50063; BH4_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Apoptosis; Cell junction;
Complete proteome; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
Membrane; Mitochondrion; Mitochondrion inner membrane;
Mitochondrion outer membrane; Nucleus; Phosphoprotein;
Reference proteome; Synapse; Transmembrane; Transmembrane helix.
CHAIN 1 233 Bcl-2-like protein 1.
/FTId=PRO_0000143063.
TRANSMEM 210 226 Helical. {ECO:0000255}.
MOTIF 4 24 BH4.
MOTIF 86 100 BH3.
MOTIF 129 148 BH1.
MOTIF 180 195 BH2.
MOD_RES 49 49 Phosphoserine; by PLK3.
{ECO:0000250|UniProtKB:Q07817}.
MOD_RES 62 62 Phosphoserine; by CDK1.
{ECO:0000250|UniProtKB:Q07817}.
VAR_SEQ 126 188 Missing (in isoform Bcl-X(S)).
{ECO:0000305}.
/FTId=VSP_000517.
VAR_SEQ 189 233 DTFVDLYGNNAAAESRKGQERFNRWFLTGMTVAGVVLLGSL
FSRK -> VRTTPLVCPPLACVSLLCEHP (in isoform
Bcl-X(beta)). {ECO:0000305}.
/FTId=VSP_000518.
VAR_SEQ 194 233 LYGNNAAAESRKGQERFNRWFLTGMTVAGVVLLGSLFSRK
-> GHDCGWCGSAGLTLQSEVTRH (in isoform Bcl-
X(delta-TM)). {ECO:0000305}.
/FTId=VSP_000519.
CONFLICT 207 209 QER -> KEG (in Ref. 4; AAC53459).
{ECO:0000305}.
HELIX 1 20 {ECO:0000244|PDB:3ILC}.
HELIX 24 27 {ECO:0000244|PDB:4YK9}.
HELIX 83 101 {ECO:0000244|PDB:3ILC}.
HELIX 102 105 {ECO:0000244|PDB:1PQ1}.
HELIX 106 112 {ECO:0000244|PDB:3ILC}.
TURN 116 118 {ECO:0000244|PDB:1PQ1}.
HELIX 120 127 {ECO:0000244|PDB:3ILC}.
HELIX 128 131 {ECO:0000244|PDB:3ILC}.
HELIX 137 156 {ECO:0000244|PDB:3ILC}.
HELIX 162 177 {ECO:0000244|PDB:3ILC}.
HELIX 179 184 {ECO:0000244|PDB:3ILC}.
HELIX 187 195 {ECO:0000244|PDB:3ILC}.
SEQUENCE 233 AA; 26132 MW; 24D2AC79887E072E CRC64;
MSQSNRELVV DFLSYKLSQK GYSWSQFSDV EENRTEAPEE TEAERETPSA INGNPSWHLA
DSPAVNGATG HSSSLDAREV IPMAAVKQAL REAGDEFELR YRRAFSDLTS QLHITPGTAY
QSFEQVVNEL FRDGVNWGRI VAFFSFGGAL CVESVDKEMQ VLVSRIASWM ATYLNDHLEP
WIQENGGWDT FVDLYGNNAA AESRKGQERF NRWFLTGMTV AGVVLLGSLF SRK


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