(data stored in ACNUC9552 zone)

HOGENOM: MOUSE1_PE1415

ID   MOUSE1_PE1415                        STANDARD;      PRT;   236 AA.
AC   MOUSE1_PE1415; P10417; P10418;
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=Apoptosis regulator Bcl-2; (MOUSE1.PE1415).
GN   Name=Bcl2; Synonyms=Bcl-2;
OS   MUS MUSCULUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae;
OC   Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS MOUSE1.PE1415.
CC       Mus musculus chromosome 1 NCBIM37  sequence 1..197195432 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:BCL2_MOUSE
CC   -!- FUNCTION: Suppresses apoptosis in a variety of cell systems
CC       including factor-dependent lymphohematopoietic and neural cells.
CC       Regulates cell death by controlling the mitochondrial membrane
CC       permeability. Appears to function in a feedback loop system with
CC       caspases. Inhibits caspase activity either by preventing the
CC       release of cytochrome c from the mitochondria and/or by binding to
CC       the apoptosis-activating factor (APAF-1).
CC   -!- SUBUNIT: Forms homodimers, and heterodimers with BAX, BAD, BAK and
CC       Bcl-X(L). Heterodimerization with BAX requires intact BH1 and BH2
CC       motifs, and is necessary for anti-apoptotic activity. Also
CC       interacts with APAF1, BBC3, BCL2L1, BNIPL, EI24, MRPL41, RAF-1 and
CC       TP53BP2. Binding to FKBP8 seems to target BCL2 to the mitochondria
CC       and probably interferes with the binding of BCL2 to its targets.
CC       Interacts with BAG1 in an ATP-dependent manner (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass
CC       membrane protein. Nucleus membrane; Single-pass membrane protein.
CC       Endoplasmic reticulum membrane; Single-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Alpha;
CC         IsoId=P10417-1; Sequence=Displayed;
CC       Name=Beta;
CC         IsoId=P10417-2; Sequence=VSP_000513;
CC   -!- TISSUE SPECIFICITY: Expressed in a variety of tissues.
CC   -!- DOMAIN: The BH4 motif is required for anti-apoptotic activity and
CC       for interaction with RAF-1.
CC   -!- PTM: Phosphorylation/dephosphorylation on Ser-70 regulates anti-
CC       apoptotic activity. Growth factor-stimulated phosphorylation on
CC       Ser-70 by PKC is required for the anti-apoptosis activity and
CC       occurs during the G2/M phase of the cell cycle. In the absence of
CC       growth factors, BCL2 appears to be phosphorylated by other protein
CC       kinases such as ERKs and stress-activated kinases.
CC       Dephosphorylated by protein phosphatase 2A (PP2A).
CC   -!- PTM: Proteolytically cleaved by caspases during apoptosis. The
CC       cleaved protein, lacking the BH4 motif, has pro-apoptotic
CC       activity, causes the release of cytochrome c into the cytosol
CC       promoting further caspase activity.
CC   -!- PTM: Monoubiquitinated by PARK2, leading to increase its stability
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the Bcl-2 family.
CC   -!- GENE_FAMILY: HOG000056452 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Mus_musculus;ENSMUSG00000057329;ENSMUST00000112751;ENSMUSP00000108371.
DR   EMBL; AK049473; - ;
DR   EMBL; BC068988; - ;
DR   EMBL; BC095964; - ;
DR   EMBL; CH466520; - ;
DR   EMBL; L31532; - ;
DR   EMBL; M16506; - ;
DR   UniProtKB/Swiss-Prot; P10417; P10418; -.
DR   EMBL; L31532; AAA37282.1; -; Genomic_DNA.
DR   EMBL; M16506; AAA37282.1; JOINED; Genomic_DNA.
DR   EMBL; M16506; AAA37281.1; -; Genomic_DNA.
DR   IPI; IPI00111518; -.
DR   IPI; IPI00227012; -.
DR   PIR; A25960; TVMSA1.
DR   PIR; B25960; TVMSB1.
DR   UniGene; Mm.257460; -.
DR   ProteinModelPortal; P10417; -.
DR   SMR; P10417; 3-204.
DR   DIP; DIP-1065N; -.
DR   IntAct; P10417; 6.
DR   MINT; MINT-209615; -.
DR   STRING; P10417; -.
DR   PhosphoSite; P10417; -.
DR   PRIDE; P10417; -.
DR   MGI; MGI:88138; Bcl2.
DR   eggNOG; roNOG04876; -.
DR   InParanoid; P10417; -.
DR   OrthoDB; EOG4X97J4; -.
DR   ArrayExpress; P10417; -.
DR   Bgee; P10417; -.
DR   CleanEx; MM_BCL2; -.
DR   Genevestigator; P10417; -.
DR   GermOnline; ENSMUSG00000057329; Mus musculus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031069; P:hair follicle morphogenesis; IMP:UniProtKB.
DR   GO; GO:0043473; P:pigmentation; IMP:UniProtKB.
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:0045069; P:regulation of viral genome replication; IDA:UniProtKB.
DR   GO; GO:0001836; P:release of cytochrome c from mitochondria; IDA:HGNC.
DR   InterPro; IPR013278; Apop_reg_Bcl2.
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; PR01863; APOPREGBCL2.
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; MOUSE1.PE1415; -.
KW   ENSMUSG000000573295old_1320000031; ENSMUSP000001083711old_1320000031;
KW   Q4VBF6_MOUSE; Q6NTH7_MOUSE; Q8BQK4_MOUSE; AK049473; BC068988; BC095964;
KW   L31532; M16506;
KW   Alternative splicing; Apoptosis; Complete proteome;
KW   Endoplasmic reticulum; Membrane; Mitochondrion;
KW   Mitochondrion outer membrane; Nucleus; Phosphoprotein;
KW   Reference proteome; Transmembrane; Transmembrane helix;
KW   Ubl conjugation.
SQ   SEQUENCE   236 AA;  UNKNOWN MW;  UNKNOWN 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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