Bcl2
entrez
12043
canonical
uniprot
P10417
canonical
ensembl
ENSMUSG00000057329
resolver
ensp
ENSMUSP00000108371
resolver
ensp
ENSMUSP00000139856
resolver
genesymbol
Bcl2
resolver
genesymbol_syn
Bcl-2
resolver
uniprot
P10418
resolver
uniprot
Q4VBF6
resolver
uniprot
Q6NTH7
resolver
uniprot
Q8BQK4
resolver
uniprot_entry
BCL2_MOUSE
resolver
uniprot_entry
Q6NTH7_MOUSE
resolver
uniprot_entry
Q8BQK4_MOUSE
resolver
uniprot_sec
P10418
resolver
uniprot_sec
Q4VBF6
resolver
amino_acid_sequence
MAQAGRTGYDNREIVMKYIHYKLSQRGYEWDAGDADAAPLGAAPTPGIFSFQPESNPMPAVHRDMAARTSPLRPLVATAGPALSPVPPVVHLTLRRAGDDFSRRYRRDFAEMSSQLHLTPFTARGRFATVVEELFRDGVNWGRIVAFFEFGGVMCVESVNREMSPLVDNIALWMTEYLNRHLHTWIQDNGGWDAFVELYGPSMRPLFDFSWLSLKTLLSLALVGACITLGAYLGHK
uniprot
proteins
function
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). Also acts as an inhibitor of autophagy: interacts with BECN1 and AMBRA1 during non-starvation conditions and inhibits their autophagy function (By similarity). May attenuate inflammation by impairing NLRP1-inflammasome activation, hence CASP1 activation and IL1B release (PubMed:17418785). {ECO:0000250|UniProtKB:P10415, ECO:0000269|PubMed:17418785}.
uniprot
proteins
mass_dalton
26407
uniprot
proteins
mutagenesis
MUTAGEN 70; /note="S->A: Loss of phosphorylation. Unable to suppress apoptosis."; /evidence="ECO:0000269|PubMed:9115213
uniprot
proteins
post_translational_modification
PTM: Phosphorylation/dephosphorylation on Ser-70 regulates anti-apoptotic activity (PubMed:9115213). 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 (PubMed:9115213). In the absence of growth factors, BCL2 appears to be phosphorylated by other protein kinases such as ERKs and stress-activated kinases (PubMed:9115213). Phosphorylated by MAPK8/JNK1 at Thr-69, Ser-70 and Ser-84, which stimulates starvation-induced autophagy (By similarity). Dephosphorylated by protein phosphatase 2A (PP2A) (PubMed:9852076). {ECO:0000250|UniProtKB:P10415, ECO:0000269|PubMed:9115213, ECO:0000269|PubMed:9852076}.; 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. {ECO:0000250|UniProtKB:P10415}.; PTM: Monoubiquitinated by PRKN, leading to an increase in its stability (By similarity). Ubiquitinated by SCF(FBXO10), leading to its degradation by the proteasome (By similarity). {ECO:0000250|UniProtKB:P10415}.
uniprot
proteins
protein_family
Bcl-2 family
uniprot
proteins
pubmed
1508712
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15781622
uniprot
proteins
pubmed
16509771
uniprot
proteins
pubmed
17418785
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21502331
uniprot
proteins
pubmed
29020630
uniprot
proteins
pubmed
3032455
uniprot
proteins
pubmed
9115213
uniprot
proteins
pubmed
9852076
uniprot
proteins
sequence_length
236
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:P10415}; Single-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:P10415}; Single-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P10415}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:29020630}.
uniprot
proteins
transmembrane_region
TRANSMEM 209..230; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins