BCL2
entrez
596
canonical
uniprot
P10415
canonical
ensembl
ENSG00000171791
resolver
ensp
ENSP00000329623
resolver
ensp
ENSP00000381185
resolver
ensp
ENSP00000466417
resolver
ensp
ENSP00000503628
resolver
enst
ENST00000678134
resolver
genesymbol
BCL2
resolver
hgnc
HGNC:990
resolver
uniprot
A0A7I2V3S7
resolver
uniprot
C9JHD5
resolver
uniprot
P10416
resolver
uniprot
Q13842
resolver
uniprot
Q16197
resolver
uniprot_entry
A0A7I2V3S7_HUMAN
resolver
uniprot_entry
BCL2_HUMAN
resolver
uniprot_sec
C9JHD5
resolver
uniprot_sec
P10416
resolver
uniprot_sec
Q13842
resolver
uniprot_sec
Q16197
resolver
amino_acid_sequence
MAHAGRTGYDNREIVMKYIHYKLSQRGYEWDAGDVGAAPPGAAPAPGIFSSQPGHTPHPAASRDPVARTSPLQTPAAPGAAAGPALSPVPPVVHLTLRQAGDDFSRRYRRDFAEMSSQLHLTPFTARGRFATVVEELFRDGVNWGRIVAFFEFGGVMCVESVNREMSPLVDNIALWMTEYLNRHLHTWIQDNGGWDAFVELYGPSMRPLFDFSWLSLKTLLSLALVGACITLGAYLGHK
uniprot
proteins
disease_involvement
DISEASE: Note=A chromosomal aberration involving BCL2 has been found in chronic lymphatic leukemia. Translocation t(14;18)(q32;q21) with immunoglobulin gene regions. BCL2 mutations found in non-Hodgkin lymphomas carrying the chromosomal translocation could be attributed to the Ig somatic hypermutation mechanism resulting in nucleotide transitions. {ECO:0000269|PubMed:2875799, ECO:0000269|PubMed:3285301}.
uniprot
proteins
function
FUNCTION: Suppresses apoptosis in a variety of cell systems including factor-dependent lymphohematopoietic and neural cells (PubMed:1508712, PubMed:8183370). Regulates cell death by controlling the mitochondrial membrane permeability (PubMed:11368354). Appears to function in a feedback loop system with caspases (PubMed:11368354). 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) (PubMed:11368354). Also acts as an inhibitor of autophagy: interacts with BECN1 and AMBRA1 during non-starvation conditions and inhibits their autophagy function (PubMed:18570871, PubMed:20889974, PubMed:21358617). May attenuate inflammation by impairing NLRP1-inflammasome activation, hence CASP1 activation and IL1B release (PubMed:17418785). {ECO:0000269|PubMed:1508712, ECO:0000269|PubMed:17418785, ECO:0000269|PubMed:18570871, ECO:0000269|PubMed:20889974, ECO:0000269|PubMed:21358617, ECO:0000269|PubMed:8183370, ECO:0000303|PubMed:11368354}.
uniprot
proteins
mass_dalton
26266
uniprot
proteins
mutagenesis
MUTAGEN 34; /note="D->A: Abolishes cleavage by caspase-3."; /evidence="ECO:0000269|PubMed:9395403"; MUTAGEN 64; /note="D->A: No effect on cleavage by caspase-3."; /evidence="ECO:0000269|PubMed:9395403"; MUTAGEN 138..141; /note="FRDG->AAAA: Loss of BAX-binding and of anti-apoptotic activity."; /evidence="ECO:0000269|PubMed:8183370"; MUTAGEN 144; /note="W->A: Loss of BAX-binding and of anti-apoptotic activity; when associated with A-145 and A146."; /evidence="ECO:0000269|PubMed:8183370"; MUTAGEN 145; /note="G->A: Loss of BAX-binding and of anti-apoptotic activity. No effect on NLRP1-induced IL1B release, nor on homodimerization. Loss of BAX-binding and of anti-apoptotic activity; when associated with A-145 and A146."; /evidence="ECO:0000269|PubMed:17418785, ECO:0000269|PubMed:8183370"; MUTAGEN 145; /note="G->E: Loss of BAX-binding and of anti-apoptotic activity. No effect on homodimerization."; /evidence="ECO:0000269|PubMed:17418785, ECO:0000269|PubMed:8183370"; MUTAGEN 146; /note="R->A: Loss of BAX-binding and of anti-apoptotic activity; when associated with A-144 and A145."; /evidence="ECO:0000269|PubMed:8183370"; MUTAGEN 188; /note="W->A: Loss of BAX-binding and of anti-apoptotic activity. No effect on homodimerization."; /evidence="ECO:0000269|PubMed:8183370"; MUTAGEN 190; /note="Q->L: Partial loss of BAX-binding and 50% decrease in anti-apoptotic activity; when associated with A-191 and A-192. No effect on homodimerization; when associated with L-190 and A-191."; /evidence="ECO:0000269|PubMed:8183370"; MUTAGEN 191; /note="D->A: No effect on BAX-binding, nor on anti-apoptotic activity. Partial loss of BAX-binding and 50% decrease in anti-apoptotic activity; when associated with L-190 and A-192. No effect on homodimerization; when associated with L-190 and A-191."; /evidence="ECO:0000269|PubMed:8183370"; MUTAGEN 192; /note="N->A: Partial loss of BAX-binding and 50% decrease in anti-apoptotic activity; when associated with L-190 and A-191. No effect on homodimerization; when associated with L-190 and A-191."; /evidence="ECO:0000269|PubMed:8183370"; MUTAGEN 194..197; /note="Missing: Loss of BAX-binding and of anti-apoptotic activity. May also affect protein stability."; /evidence="ECO:0000269|PubMed:8183370"; MUTAGEN 200; /note="E->A: Partial loss of BAX-binding and 50% decrease in anti-apoptotic activity."; /evidence="ECO:0000269|PubMed:8183370
uniprot
proteins
post_translational_modification
PTM: Phosphorylation/dephosphorylation on Ser-70 regulates anti-apoptotic activity (PubMed:11368354). 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:11368354). In the absence of growth factors, BCL2 appears to be phosphorylated by other protein kinases such as ERKs and stress-activated kinases (PubMed:11368354). Phosphorylated by MAPK8/JNK1 at Thr-69, Ser-70 and Ser-87, which stimulates starvation-induced autophagy (PubMed:10567572, PubMed:18570871). Dephosphorylated by protein phosphatase 2A (PP2A) (By similarity). {ECO:0000250|UniProtKB:P10417, ECO:0000269|PubMed:10567572, ECO:0000269|PubMed:18570871, ECO:0000303|PubMed:11368354}.; 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:0000269|PubMed:9395403}.; PTM: Monoubiquitinated by PRKN, leading to an increase in its stability (PubMed:20889974). Ubiquitinated by SCF(FBXO10), leading to its degradation by the proteasome (PubMed:23431138). Ubiquitinated by XIAP, leading to its degradation by the proteasome (PubMed:29020630). {ECO:0000269|PubMed:20889974, ECO:0000269|PubMed:23431138, ECO:0000269|PubMed:29020630}.
uniprot
proteins
protein_family
Bcl-2 family
uniprot
proteins
pubmed
10567572
uniprot
proteins
pubmed
11248023
uniprot
proteins
pubmed
11368354
uniprot
proteins
pubmed
11463391
uniprot
proteins
pubmed
12901880
uniprot
proteins
pubmed
1339299
uniprot
proteins
pubmed
1508712
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15547950
uniprot
proteins
pubmed
15733859
uniprot
proteins
pubmed
15849194
uniprot
proteins
pubmed
15902208
uniprot
proteins
pubmed
16177791
uniprot
proteins
pubmed
17090549
uniprot
proteins
pubmed
17256834
uniprot
proteins
pubmed
17418785
uniprot
proteins
pubmed
18570871
uniprot
proteins
pubmed
19228691
uniprot
proteins
pubmed
19706769
uniprot
proteins
pubmed
20849813
uniprot
proteins
pubmed
20889974
uniprot
proteins
pubmed
21358617
uniprot
proteins
pubmed
2250705
uniprot
proteins
pubmed
23055042
uniprot
proteins
pubmed
23431138
uniprot
proteins
pubmed
23822101
uniprot
proteins
pubmed
25609812
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
2834197
uniprot
proteins
pubmed
2875799
uniprot
proteins
pubmed
29020630
uniprot
proteins
pubmed
31206022
uniprot
proteins
pubmed
3285301
uniprot
proteins
pubmed
34180401
uniprot
proteins
pubmed
3523487
uniprot
proteins
pubmed
8183370
uniprot
proteins
pubmed
8668206
uniprot
proteins
pubmed
9305631
uniprot
proteins
pubmed
9395403
uniprot
proteins
sequence_length
239
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:21358617, ECO:0000269|PubMed:2250705}; Single-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000269|PubMed:2250705}; Single-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:21358617, ECO:0000269|PubMed:2250705}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:P10417}.
uniprot
proteins
transmembrane_region
TRANSMEM 212..233; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins