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Apoptosis regulator Bcl-2

 BCL2_MOUSE              Reviewed;         236 AA.
P10417; P10418; Q4VBF6;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
03-OCT-2012, sequence version 3.
30-AUG-2017, entry version 184.
RecName: Full=Apoptosis regulator Bcl-2;
Name=Bcl2; Synonyms=Bcl-2;
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 [GENOMIC DNA] (ISOFORMS ALPHA AND BETA).
STRAIN=BALB/cJ; TISSUE=Liver;
PubMed=3032455; DOI=10.1016/0092-8674(87)90448-X;
Negrini M., Silini E., Kozak C., Tsujimoto Y., Croce C.M.;
"Molecular analysis of mbcl-2: structure and expression of the murine
gene homologous to the human gene involved in follicular lymphoma.";
Cell 49:455-463(1987).
[2]
SEQUENCE REVISION TO 221-222.
PubMed=1508712; DOI=10.1093/nar/20.16.4187;
Eguchi Y., Ewert D.L., Tsujimoto Y.;
"Isolation and characterization of the chicken bcl-2 gene: expression
in a variety of tissues including lymphoid and neuronal organs in
adult and embryo.";
Nucleic Acids Res. 20:4187-4192(1992).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Olfactory epithelium;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PHOSPHORYLATION AT SER-70 BY PKC, AND MUTAGENESIS OF SER-70.
PubMed=9115213; DOI=10.1074/jbc.272.18.11671;
Ito T., Deng X., Carr B., May W.S. Jr.;
"Bcl-2 phosphorylation required for anti-apoptosis function.";
J. Biol. Chem. 272:11671-11673(1997).
[7]
DEPHOSPHORYLATION BY PP2A.
PubMed=9852076; DOI=10.1074/jbc.273.51.34157;
Deng X., Ito T., Carr B., Mumby M., May W.S. Jr.;
"Reversible phosphorylation of Bcl2 following interleukin 3 or
bryostatin 1 is mediated by direct interaction with protein
phosphatase 2A.";
J. Biol. Chem. 273:34157-34163(1998).
[8]
INTERACTION WITH EI24.
PubMed=15781622; DOI=10.1158/0008-5472.CAN-04-3377;
Zhao X., Ayer R.E., Davis S.L., Ames S.J., Florence B., Torchinsky C.,
Liou J.S., Shen L., Spanjaard R.A.;
"Apoptosis factor EI24/PIG8 is a novel endoplasmic reticulum-localized
Bcl-2-binding protein which is associated with suppression of breast
cancer invasiveness.";
Cancer Res. 65:2125-2129(2005).
[9]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=17418785; DOI=10.1016/j.cell.2007.01.045;
Bruey J.M., Bruey-Sedano N., Luciano F., Zhai D., Balpai R., Xu C.,
Kress C.L., Bailly-Maitre B., Li X., Osterman A., Matsuzawa S.,
Terskikh A.V., Faustin B., Reed J.C.;
"Bcl-2 and Bcl-XL regulate proinflammatory caspase-1 activation by
interaction with NALP1.";
Cell 129:45-56(2007).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Lung, and Spleen;
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).
-!- FUNCTION: Suppresses apoptosis in a variety of cell systems
including factor-dependent lymphohematopoietic and neural cells.
Regulates cell death by controlling the mitochondrial membrane
permeability. Appears to function in a feedback loop system with
caspases. Inhibits caspase activity either by preventing the
release of cytochrome c from the mitochondria and/or by binding to
the apoptosis-activating factor (APAF-1). May attenuate
inflammation by impairing NLRP1-inflammasome activation, hence
CASP1 activation and IL1B release (PubMed:17418785).
{ECO:0000269|PubMed:17418785}.
-!- SUBUNIT: Forms homodimers, and heterodimers with BAX, BAD, BAK and
Bcl-X(L). Heterodimerization with BAX requires intact BH1 and BH2
motifs, and is necessary for anti-apoptotic activity (By
similarity). Also interacts with APAF1, BBC3, BCL2L1, BNIPL,
MRPL41 and TP53BP2. Binding to FKBP8 seems to target BCL2 to the
mitochondria and probably interferes with the binding of BCL2 to
its targets. Interacts with BAG1 in an ATP-dependent manner.
Interacts with RAF1 (the 'Ser-338' and 'Ser-339' phosphorylated
form). Interacts (via the BH4 domain) with EGLN3; the interaction
prevents the formation of the BAX-BCL2 complex and inhibits the
anti-apoptotic activity of BCL2 (By similarity). Interacts with
EI24. Interacts with G0S2; this interaction also prevents the
formation of the anti-apoptotic BAX-BCL2 complex. Interacts with
PPIF; the interaction is impaired by CsA (By similarity).
Interacts with BOP (By similarity). Interacts with the SCF(FBXO10)
complex (By similarity). Interacts (via the loop between motifs
BH4 and BH3) with NLRP1 (via LRR repeats) (By similarity).
{ECO:0000250, ECO:0000250|UniProtKB:P10415}.
-!- INTERACTION:
Q07813:Bax; NbExp=2; IntAct=EBI-526314, EBI-700711;
O54918-1:Bcl2l11; NbExp=2; IntAct=EBI-526314, EBI-526076;
O88597:Becn1; NbExp=4; IntAct=EBI-526314, EBI-643716;
-!- SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass
membrane protein. Nucleus membrane; Single-pass membrane protein.
Endoplasmic reticulum membrane; Single-pass membrane protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Alpha;
IsoId=P10417-1; Sequence=Displayed;
Name=Beta;
IsoId=P10417-2; Sequence=VSP_000513;
-!- TISSUE SPECIFICITY: Expressed in a variety of tissues.
-!- DOMAIN: The BH4 motif is required for anti-apoptotic activity and
for interaction with RAF1 and EGLN3.
-!- DOMAIN: BH1 and BH2 domains are required for the interaction with
BAX and for anti-apoptotic activity.
{ECO:0000250|UniProtKB:P10415}.
-!- DOMAIN: The loop between motifs BH4 and BH3 is required for the
interaction with NLRP1. {ECO:0000250|UniProtKB:P10415}.
-!- PTM: Phosphorylation/dephosphorylation on Ser-70 regulates anti-
apoptotic activity. Growth factor-stimulated phosphorylation on
Ser-70 by PKC is required for the anti-apoptosis activity and
occurs during the G2/M phase of the cell cycle. In the absence of
growth factors, BCL2 appears to be phosphorylated by other protein
kinases such as ERKs and stress-activated kinases. Phosphorylated
by MAPK8/JNK1 at Thr-69, Ser-70 and Ser-84, wich stimulates
starvation-induced autophagy (By similarity). Dephosphorylated by
protein phosphatase 2A (PP2A). {ECO:0000250,
ECO:0000269|PubMed:9115213}.
-!- PTM: Proteolytically cleaved by caspases during apoptosis. The
cleaved protein, lacking the BH4 motif, has pro-apoptotic
activity, causes the release of cytochrome c into the cytosol
promoting further caspase activity.
-!- PTM: Monoubiquitinated by PRKN, leading to increase its stability.
Ubiquitinated by SCF(FBXO10), leading to its degradation by the
proteasome. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: In response to intraperitoneal injection of
muramyl dipeptide (MDP), knockout animals show lower serum IL1B
levels than wild type. Mutant macrophages release 30% less IL1B
than the wild-type cells. {ECO:0000269|PubMed:17418785}.
-!- SIMILARITY: Belongs to the Bcl-2 family. {ECO:0000305}.
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EMBL; L31532; AAA37282.1; -; Genomic_DNA.
EMBL; M16506; AAA37282.1; JOINED; Genomic_DNA.
EMBL; M16506; AAA37281.1; -; Genomic_DNA.
EMBL; AC122842; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC162916; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH466520; EDL39862.1; -; Genomic_DNA.
EMBL; BC095964; AAH95964.1; -; mRNA.
CCDS; CCDS15209.1; -. [P10417-1]
CCDS; CCDS78667.1; -. [P10417-2]
PIR; A25960; TVMSA1.
PIR; B25960; TVMSB1.
RefSeq; NP_033871.2; NM_009741.5. [P10417-1]
UniGene; Mm.257460; -.
ProteinModelPortal; P10417; -.
BioGrid; 198318; 32.
DIP; DIP-1065N; -.
IntAct; P10417; 8.
MINT; MINT-209615; -.
STRING; 10090.ENSMUSP00000108371; -.
BindingDB; P10417; -.
iPTMnet; P10417; -.
PhosphoSitePlus; P10417; -.
PaxDb; P10417; -.
PeptideAtlas; P10417; -.
PRIDE; P10417; -.
Ensembl; ENSMUST00000112751; ENSMUSP00000108371; ENSMUSG00000057329. [P10417-1]
Ensembl; ENSMUST00000189999; ENSMUSP00000139856; ENSMUSG00000057329. [P10417-2]
GeneID; 12043; -.
KEGG; mmu:12043; -.
UCSC; uc007cgw.2; mouse. [P10417-1]
CTD; 596; -.
MGI; MGI:88138; Bcl2.
eggNOG; KOG4728; Eukaryota.
eggNOG; ENOG41123S0; LUCA.
GeneTree; ENSGT00530000062935; -.
HOGENOM; HOG000056452; -.
HOVERGEN; HBG004472; -.
InParanoid; P10417; -.
KO; K02161; -.
OMA; EWDAGDA; -.
OrthoDB; EOG091G0OCU; -.
TreeFam; TF315834; -.
Reactome; R-MMU-111447; Activation of BAD and translocation to mitochondria.
Reactome; R-MMU-111453; BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members.
Reactome; R-MMU-844455; The NLRP1 inflammasome.
ChiTaRS; Bcl2; mouse.
PRO; PR:P10417; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000057329; -.
CleanEx; MM_BCL2; -.
ExpressionAtlas; P10417; baseline and differential.
Genevisible; P10417; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:MGI.
GO; GO:0005622; C:intracellular; IDA:MGI.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0031966; C:mitochondrial membrane; IDA:MGI.
GO; GO:0005741; C:mitochondrial outer membrane; ISO:MGI.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0043209; C:myelin sheath; IDA:MGI.
GO; GO:0031965; C:nuclear membrane; IDA:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0046930; C:pore complex; ISO:MGI.
GO; GO:0043234; C:protein complex; ISO:MGI.
GO; GO:0051434; F:BH3 domain binding; ISO:MGI.
GO; GO:0015267; F:channel activity; ISO:MGI.
GO; GO:0016248; F:channel inhibitor activity; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0002020; F:protease binding; ISO:MGI.
GO; GO:0046982; F:protein heterodimerization activity; IPI:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0051721; F:protein phosphatase 2A binding; IDA:MGI.
GO; GO:0019903; F:protein phosphatase binding; IDA:MGI.
GO; GO:0043565; F:sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0008134; F:transcription factor binding; IPI:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0007015; P:actin filament organization; IMP:MGI.
GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI.
GO; GO:0008637; P:apoptotic mitochondrial changes; IDA:MGI.
GO; GO:0006915; P:apoptotic process; IMP:MGI.
GO; GO:0031103; P:axon regeneration; IDA:MGI.
GO; GO:0007409; P:axonogenesis; IMP:MGI.
GO; GO:0030183; P:B cell differentiation; IMP:MGI.
GO; GO:0001782; P:B cell homeostasis; IMP:MGI.
GO; GO:0002326; P:B cell lineage commitment; IMP:MGI.
GO; GO:0042100; P:B cell proliferation; ISO:MGI.
GO; GO:0050853; P:B cell receptor signaling pathway; ISO:MGI.
GO; GO:0001662; P:behavioral fear response; IMP:MGI.
GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IDA:MGI.
GO; GO:0043375; P:CD8-positive, alpha-beta T cell lineage commitment; IMP:MGI.
GO; GO:0007569; P:cell aging; IMP:MGI.
GO; GO:0016049; P:cell growth; IMP:MGI.
GO; GO:0000902; P:cell morphogenesis; IMP:MGI.
GO; GO:0008283; P:cell proliferation; IGI:MGI.
GO; GO:0006874; P:cellular calcium ion homeostasis; IDA:MGI.
GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:MGI.
GO; GO:0042149; P:cellular response to glucose starvation; IDA:MGI.
GO; GO:0071456; P:cellular response to hypoxia; IDA:MGI.
GO; GO:0071310; P:cellular response to organic substance; IDA:MGI.
GO; GO:0021747; P:cochlear nucleus development; IMP:MGI.
GO; GO:0051607; P:defense response to virus; ISO:MGI.
GO; GO:0048589; P:developmental growth; IMP:MGI.
GO; GO:0048066; P:developmental pigmentation; IMP:MGI.
GO; GO:0048546; P:digestive tract morphogenesis; IMP:MGI.
GO; GO:0043583; P:ear development; IMP:MGI.
GO; GO:0032469; P:endoplasmic reticulum calcium ion homeostasis; IGI:MGI.
GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IGI:MGI.
GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; ISO:MGI.
GO; GO:0048041; P:focal adhesion assembly; IMP:MGI.
GO; GO:0022612; P:gland morphogenesis; IMP:MGI.
GO; GO:0032835; P:glomerulus development; IMP:MGI.
GO; GO:0040007; P:growth; IMP:MGI.
GO; GO:0031069; P:hair follicle morphogenesis; IMP:UniProtKB.
GO; GO:0030097; P:hemopoiesis; IMP:MGI.
GO; GO:0048873; P:homeostasis of number of cells within a tissue; IMP:MGI.
GO; GO:0002520; P:immune system development; IMP:MGI.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IBA:GO_Central.
GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; ISS:MGI.
GO; GO:0008631; P:intrinsic apoptotic signaling pathway in response to oxidative stress; IMP:MGI.
GO; GO:0001822; P:kidney development; IMP:MGI.
GO; GO:0001776; P:leukocyte homeostasis; IMP:MGI.
GO; GO:0002260; P:lymphocyte homeostasis; IMP:MGI.
GO; GO:0002320; P:lymphoid progenitor cell differentiation; IMP:MGI.
GO; GO:0008584; P:male gonad development; IGI:MGI.
GO; GO:0006582; P:melanin metabolic process; IMP:MGI.
GO; GO:0030318; P:melanocyte differentiation; IMP:MGI.
GO; GO:0014031; P:mesenchymal cell development; IMP:MGI.
GO; GO:0001656; P:metanephros development; IMP:MGI.
GO; GO:2000811; P:negative regulation of anoikis; ISO:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:MGI.
GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IDA:MGI.
GO; GO:0010507; P:negative regulation of autophagy; IMP:ParkinsonsUK-UCL.
GO; GO:0010523; P:negative regulation of calcium ion transport into cytosol; IGI:MGI.
GO; GO:0030308; P:negative regulation of cell growth; IMP:MGI.
GO; GO:0030336; P:negative regulation of cell migration; IMP:MGI.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:MGI.
GO; GO:0032848; P:negative regulation of cellular pH reduction; ISO:MGI.
GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; ISO:MGI.
GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IDA:MGI.
GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; ISO:MGI.
GO; GO:0045930; P:negative regulation of mitotic cell cycle; IDA:MGI.
GO; GO:0033033; P:negative regulation of myeloid cell apoptotic process; IDA:MGI.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IDA:MGI.
GO; GO:0030279; P:negative regulation of ossification; IMP:MGI.
GO; GO:0033689; P:negative regulation of osteoblast proliferation; IMP:MGI.
GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; IMP:ParkinsonsUK-UCL.
GO; GO:0046671; P:negative regulation of retinal cell programmed cell death; IMP:MGI.
GO; GO:0051402; P:neuron apoptotic process; IMP:MGI.
GO; GO:0048599; P:oocyte development; IMP:MGI.
GO; GO:0035265; P:organ growth; IMP:MGI.
GO; GO:0001503; P:ossification; IMP:MGI.
GO; GO:0001541; P:ovarian follicle development; IMP:MGI.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:MGI.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:MGI.
GO; GO:0048753; P:pigment granule organization; IMP:MGI.
GO; GO:0043473; P:pigmentation; IMP:UniProtKB.
GO; GO:0030890; P:positive regulation of B cell proliferation; ISO:MGI.
GO; GO:0043085; P:positive regulation of catalytic activity; IMP:MGI.
GO; GO:0030307; P:positive regulation of cell growth; ISO:MGI.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:UniProtKB.
GO; GO:0048087; P:positive regulation of developmental pigmentation; IMP:MGI.
GO; GO:0045636; P:positive regulation of melanocyte differentiation; IMP:MGI.
GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:MGI.
GO; GO:0014042; P:positive regulation of neuron maturation; IMP:MGI.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IGI:MGI.
GO; GO:0048743; P:positive regulation of skeletal muscle fiber development; IMP:MGI.
GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IMP:MGI.
GO; GO:0009791; P:post-embryonic development; IMP:MGI.
GO; GO:0006470; P:protein dephosphorylation; IDA:MGI.
GO; GO:0000209; P:protein polyubiquitination; ISO:MGI.
GO; GO:0072593; P:reactive oxygen species metabolic process; IMP:MGI.
GO; GO:0042981; P:regulation of apoptotic process; IGI:MGI.
GO; GO:0010506; P:regulation of autophagy; IMP:CACAO.
GO; GO:0051924; P:regulation of calcium ion transport; ISO:MGI.
GO; GO:0050790; P:regulation of catalytic activity; IMP:MGI.
GO; GO:0051726; P:regulation of cell cycle; IMP:MGI.
GO; GO:0001952; P:regulation of cell-matrix adhesion; IMP:MGI.
GO; GO:0048070; P:regulation of developmental pigmentation; IGI:MGI.
GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
GO; GO:0010559; P:regulation of glycoprotein biosynthetic process; IMP:MGI.
GO; GO:0046902; P:regulation of mitochondrial membrane permeability; IDA:HGNC.
GO; GO:0051881; P:regulation of mitochondrial membrane potential; IDA:HGNC.
GO; GO:0006808; P:regulation of nitrogen utilization; IGI:MGI.
GO; GO:0043067; P:regulation of programmed cell death; IGI:MGI.
GO; GO:0043497; P:regulation of protein heterodimerization activity; ISO:MGI.
GO; GO:0043496; P:regulation of protein homodimerization activity; ISO:MGI.
GO; GO:0032880; P:regulation of protein localization; IMP:MGI.
GO; GO:0031647; P:regulation of protein stability; IMP:MGI.
GO; GO:0022898; P:regulation of transmembrane transporter activity; ISO:MGI.
GO; GO:0045069; P:regulation of viral genome replication; IDA:UniProtKB.
GO; GO:0001836; P:release of cytochrome c from mitochondria; IDA:HGNC.
GO; GO:0003014; P:renal system process; IMP:MGI.
GO; GO:0034097; P:response to cytokine; IMP:MGI.
GO; GO:0042493; P:response to drug; IDA:MGI.
GO; GO:0010332; P:response to gamma radiation; IMP:MGI.
GO; GO:0051384; P:response to glucocorticoid; IDA:MGI.
GO; GO:0042542; P:response to hydrogen peroxide; IMP:MGI.
GO; GO:0010039; P:response to iron ion; ISO:MGI.
GO; GO:0002931; P:response to ischemia; IMP:MGI.
GO; GO:0035094; P:response to nicotine; ISO:MGI.
GO; GO:0006979; P:response to oxidative stress; IMP:MGI.
GO; GO:0048545; P:response to steroid hormone; IMP:MGI.
GO; GO:0009636; P:response to toxic substance; IMP:MGI.
GO; GO:0010224; P:response to UV-B; IMP:MGI.
GO; GO:0016337; P:single organismal cell-cell adhesion; IMP:MGI.
GO; GO:0048536; P:spleen development; IMP:MGI.
GO; GO:0030217; P:T cell differentiation; IMP:MGI.
GO; GO:0033077; P:T cell differentiation in thymus; IMP:MGI.
GO; GO:0043029; P:T cell homeostasis; IMP:MGI.
GO; GO:0002360; P:T cell lineage commitment; IMP:MGI.
GO; GO:0048538; P:thymus development; IMP:MGI.
GO; GO:0001657; P:ureteric bud development; IMP:MGI.
InterPro; IPR013278; Apop_reg_Bcl2.
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; IPR026298; Blc2_fam.
PANTHER; PTHR11256; PTHR11256; 1.
PANTHER; PTHR11256:SF55; PTHR11256:SF55; 1.
Pfam; PF00452; Bcl-2; 1.
Pfam; PF02180; BH4; 1.
PRINTS; PR01863; APOPREGBCL2.
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;
Alternative splicing; Apoptosis; Complete proteome;
Endoplasmic reticulum; Membrane; Mitochondrion;
Mitochondrion outer membrane; Nucleus; Phosphoprotein;
Reference proteome; Transmembrane; Transmembrane helix;
Ubl conjugation.
CHAIN 1 236 Apoptosis regulator Bcl-2.
/FTId=PRO_0000143049.
TRANSMEM 209 230 Helical. {ECO:0000255}.
MOTIF 10 30 BH4.
MOTIF 90 104 BH3.
MOTIF 133 152 BH1.
MOTIF 184 199 BH2.
SITE 34 35 Cleavage; by caspases. {ECO:0000250}.
MOD_RES 69 69 Phosphothreonine; by MAPK8.
{ECO:0000250|UniProtKB:P10415}.
MOD_RES 70 70 Phosphoserine; by MAPK8 and PKC.
{ECO:0000269|PubMed:9115213}.
MOD_RES 84 84 Phosphoserine; by MAPK8.
{ECO:0000250|UniProtKB:P10415}.
VAR_SEQ 193 236 DAFVELYGPSMRPLFDFSWLSLKTLLSLALVGACITLGAYL
GHK -> VGACLVE (in isoform Beta).
{ECO:0000305}.
/FTId=VSP_000513.
MUTAGEN 70 70 S->A: Loss of phosphorylation. Unable to
suppress apoptosis.
{ECO:0000269|PubMed:9115213}.
CONFLICT 64 64 D -> E (in Ref. 1; AAA37281/AAA37282).
{ECO:0000305}.
CONFLICT 89 89 V -> C (in Ref. 1; AAA37281/AAA37282).
{ECO:0000305}.
SEQUENCE 236 AA; 26407 MW; 80FDCFE78C735092 CRC64;
MAQAGRTGYD NREIVMKYIH YKLSQRGYEW DAGDADAAPL GAAPTPGIFS FQPESNPMPA
VHRDMAARTS PLRPLVATAG PALSPVPPVV HLTLRRAGDD FSRRYRRDFA EMSSQLHLTP
FTARGRFATV VEELFRDGVN WGRIVAFFEF GGVMCVESVN REMSPLVDNI ALWMTEYLNR
HLHTWIQDNG GWDAFVELYG PSMRPLFDFS WLSLKTLLSL ALVGACITLG AYLGHK


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