BCL2L1
entrez
598
canonical
uniprot
Q07817
canonical
ensembl
ENSG00000171552
resolver
ensp
ENSP00000302564
resolver
ensp
ENSP00000365223
resolver
ensp
ENSP00000389688
resolver
ensp
ENSP00000390760
resolver
ensp
ENSP00000395545
resolver
ensp
ENSP00000401173
resolver
ensp
ENSP00000503725
resolver
ensp
ENSP00000504237
resolver
ensp
ENSP00000540678
resolver
ensp
ENSP00000540679
resolver
genesymbol
BCL2L1
resolver
genesymbol_syn
BCL2L
resolver
genesymbol_syn
BCLX
resolver
hgnc
HGNC:992
resolver
uniprot
A0A0S2Z3C5
resolver
uniprot
E1P5L6
resolver
uniprot
Q5CZ89
resolver
uniprot
Q5TE63
resolver
uniprot
Q5TE65
resolver
uniprot
Q92976
resolver
uniprot_entry
A0A0S2Z3C5_HUMAN
resolver
uniprot_entry
B2CL1_HUMAN
resolver
uniprot_entry
Q5TE63_HUMAN
resolver
uniprot_sec
E1P5L6
resolver
uniprot_sec
Q5CZ89
resolver
uniprot_sec
Q5TE65
resolver
uniprot_sec
Q92976
resolver
amino_acid_sequence
MSQSNRELVVDFLSYKLSQKGYSWSQFSDVEENRTEAPEGTESEMETPSAINGNPSWHLADSPAVNGATGHSSSLDAREVIPMAAVKQALREAGDEFELRYRRAFSDLTSQLHITPGTAYQSFEQVVNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQVLVSRIAAWMATYLNDHLEPWIQENGGWDTFVELYGNNAAAESRKGQERFNRWFLTGMTVAGVVLLGSLFSRK
uniprot
proteins
function
FUNCTION: Potent inhibitor of cell death. Inhibits activation of caspases. Appears to regulate cell death by blocking the voltage-dependent anion channel (VDAC) by binding to it and preventing the release of the caspase activator, CYC1, from the mitochondrial membrane. Also acts as a regulator of G2 checkpoint and progression to cytokinesis during mitosis.; FUNCTION: Isoform Bcl-X(L) also regulates presynaptic plasticity, including neurotransmitter release and recovery, number of axonal mitochondria as well as size and number of synaptic vesicle clusters. During synaptic stimulation, increases ATP availability from mitochondria through regulation of mitochondrial membrane ATP synthase F(1)F(0) activity and regulates endocytic vesicle retrieval in hippocampal neurons through association with DMN1L and stimulation of its GTPase activity in synaptic vesicles. May attenuate inflammation impairing NLRP1-inflammasome activation, hence CASP1 activation and IL1B release (PubMed:17418785). {ECO:0000269|PubMed:17418785}.; FUNCTION: Isoform Bcl-X(S) promotes apoptosis.
uniprot
proteins
mass_dalton
26049
uniprot
proteins
mutagenesis
MUTAGEN 49; /note="S->A: Less stable at G2 checkpoint after DNA damage."; /evidence="ECO:0000269|PubMed:21840391"; MUTAGEN 61; /note="D->A: No cleavage by caspase-1 nor by caspase-3."; /evidence="ECO:0000269|PubMed:9435230"; MUTAGEN 131..133; /note="FRD->VRA: No heterodimerization with BAX."; /evidence="ECO:0000269|PubMed:8596636"; MUTAGEN 135..137; /note="VNW->AIL: Loss of anti-apoptotic activity."; /evidence="ECO:0000269|PubMed:8596636"; MUTAGEN 138..140; /note="GRI->ELN: Loss of anti-apoptotic activity."; /evidence="ECO:0000269|PubMed:8596636"; MUTAGEN 138; /note="G->A: No heterodimerization with BAX."; /evidence="ECO:0000269|PubMed:7644501"; MUTAGEN 145..147; /note="SFG->YCC: Decreases interaction with DNM1L, no effect on endocytosis enhancement."; /evidence="ECO:0000269|PubMed:23792689"; MUTAGEN 148; /note="G->E: No heterodimerization with BAX."; /evidence="ECO:0000269|PubMed:8596636"; MUTAGEN 156; /note="D->A: No effect on caspase-1 cleavage."; /evidence="ECO:0000269|PubMed:8596636"; MUTAGEN 176; /note="D->A: No effect on caspase-1 cleavage."; /evidence="ECO:0000269|PubMed:8596636"; MUTAGEN 188..191; /note="WDTF->SVTC: Abolishes interaction with DNM1L and endocytosis enhancement."; /evidence="ECO:0000269|PubMed:23792689"; MUTAGEN 188..189; /note="WD->GA: Reduces anti-apoptotic activity by about half."; /evidence="ECO:0000269|PubMed:8596636"; MUTAGEN 189; /note="D->A: No effect on caspase-1 cleavage."; /evidence="ECO:0000269|PubMed:8596636
uniprot
proteins
post_translational_modification
PTM: Proteolytically cleaved by caspases during apoptosis. The cleaved protein, lacking the BH4 motif, has pro-apoptotic activity. {ECO:0000269|PubMed:9435230}.; PTM: Phosphorylated on Ser-62 by CDK1. This phosphorylation is partial in normal mitotic cells, but complete in G2-arrested cells upon DNA-damage, thus promoting subsequent apoptosis probably by triggering caspases-mediated proteolysis. Phosphorylated by PLK3, leading to regulate the G2 checkpoint and progression to cytokinesis during mitosis. Phosphorylation at Ser-49 appears during the S phase and G2, disappears rapidly in early mitosis during prometaphase, metaphase and early anaphase, and re-appears during telophase and cytokinesis. {ECO:0000269|PubMed:19917720, ECO:0000269|PubMed:21840391}.; PTM: Ubiquitinated by RNF183 during prolonged ER stress, leading to degradation by the proteosome. {ECO:0000269|PubMed:29507230}.
uniprot
proteins
protein_family
Bcl-2 family
uniprot
proteins
pubmed
10772918
uniprot
proteins
pubmed
11206074
uniprot
proteins
pubmed
11463391
uniprot
proteins
pubmed
11714801
uniprot
proteins
pubmed
11780052
uniprot
proteins
pubmed
12011449
uniprot
proteins
pubmed
14534311
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15902208
uniprot
proteins
pubmed
16368107
uniprot
proteins
pubmed
16509771
uniprot
proteins
pubmed
17046835
uniprot
proteins
pubmed
17256834
uniprot
proteins
pubmed
17337444
uniprot
proteins
pubmed
17418785
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
19917720
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21567405
uniprot
proteins
pubmed
21639858
uniprot
proteins
pubmed
21840391
uniprot
proteins
pubmed
22498477
uniprot
proteins
pubmed
23055042
uniprot
proteins
pubmed
23340338
uniprot
proteins
pubmed
23792689
uniprot
proteins
pubmed
25296756
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
27013495
uniprot
proteins
pubmed
29507230
uniprot
proteins
pubmed
7644501
uniprot
proteins
pubmed
8358789
uniprot
proteins
pubmed
8596636
uniprot
proteins
pubmed
8692274
uniprot
proteins
pubmed
9020082
uniprot
proteins
pubmed
9435230
uniprot
proteins
pubmed
9675101
uniprot
proteins
sequence_length
233
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Isoform Bcl-X(L)]: Mitochondrion inner membrane {ECO:0000250}. Mitochondrion outer membrane {ECO:0000250}. Mitochondrion matrix {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=After neuronal stimulation, translocates from cytosol to synaptic vesicle and mitochondrion membrane in a calmodulin-dependent manner (By similarity). Localizes to the centrosome when phosphorylated at Ser-49. {ECO:0000250}.
uniprot
proteins
transmembrane_region
TRANSMEM 210..226; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins