Bcl2
entrez
24224
canonical
uniprot
P49950
canonical
ensembl
ENSRNOG00000077679
resolver
ensp
ENSRNOP00000106668
resolver
enst
ENSRNOT00000156655
resolver
genesymbol
Bcl2
resolver
genesymbol_syn
Bcl-2
resolver
uniprot
A0ABK0LXU8
resolver
uniprot
Q62837
resolver
uniprot
Q64032
resolver
uniprot_entry
A0ABK0LXU8_RAT
resolver
uniprot_entry
BCL2_RAT
resolver
uniprot_sec
Q62837
resolver
uniprot_sec
Q64032
resolver
amino_acid_sequence
MAQAGRTGYDNREIVMKYIHYKLSQRGYEWDTGDEDSAPLRAAPTPGIFSFQPESNRTPAVHRDTAARTSPLRPLVANAGPALSPVPPVVHLTLRRAGDDFSRRYRRDFAEMSSQLHLTPFTARGRFATVVEELFRDGVNWGRIVAFFEFGGVMCVESVNREMSPLVDNIALWMTEYLNRHLHTWIQDNGGWDAFVELYGPSMRPLFDFSWLSLKTLLSLALVGACITLGAYLGHK
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. May attenuate inflammation by impairing NLRP1-inflammasome activation, hence CASP1 activation and IL1B release. {ECO:0000250|UniProtKB:P10415}.
uniprot
proteins
mass_dalton
26622
uniprot
proteins
post_translational_modification
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, which stimulates starvation-induced autophagy (By similarity). Dephosphorylated by protein phosphatase 2A (PP2A) (By similarity). {ECO:0000250|UniProtKB:P10415, ECO:0000250|UniProtKB:P10417}.; 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 (By similarity). {ECO:0000250|UniProtKB:P10415}.; PTM: Monoubiquitinated by PRKN, leading to an increase in its stability. Ubiquitinated by SCF(FBXO10), leading to its degradation by the proteasome. {ECO:0000250|UniProtKB:P10415}.
uniprot
proteins
protein_family
Bcl-2 family
uniprot
proteins
pubmed
19228691
uniprot
proteins
pubmed
30980393
uniprot
proteins
pubmed
7828536
uniprot
proteins
pubmed
7969891
uniprot
proteins
pubmed
8144041
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:0000250|UniProtKB:P10417}.
uniprot
proteins
transmembrane_region
TRANSMEM 209..230; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins