Bcl2l11
entrez
12125
canonical
uniprot
O54918
canonical
ensembl
ENSMUSG00000027381
resolver
ensp
ENSMUSP00000087062
resolver
ensp
ENSMUSP00000099499
resolver
ensp
ENSMUSP00000099500
resolver
ensp
ENSMUSP00000105970
resolver
enst
ENSMUST00000089634
resolver
genesymbol
Bcl2l11
resolver
genesymbol_syn
Bim
resolver
uniprot
A2ALQ6
resolver
uniprot
F6SZ41
resolver
uniprot
O54919
resolver
uniprot
O54920
resolver
uniprot
Q3TR86
resolver
uniprot
Q3U7X3
resolver
uniprot
Q542N5
resolver
uniprot
Q6PEB3
resolver
uniprot_entry
B2L11_MOUSE
resolver
uniprot_entry
F6SZ41_MOUSE
resolver
uniprot_entry
Q3TR86_MOUSE
resolver
uniprot_entry
Q3U7X3_MOUSE
resolver
uniprot_entry
Q542N5_MOUSE
resolver
uniprot_entry
Q6PEB3_MOUSE
resolver
uniprot_sec
A2ALQ6
resolver
uniprot_sec
O54919
resolver
uniprot_sec
O54920
resolver
amino_acid_sequence
MAKQPSDVSSECDREGGQLQPAERPPQLRPGAPTSLQTEPQGNPDGEGDRCPHGSPQGPLAPPASPGPFATRSPLFIFVRRSSLLSRSSSGYFSFDTDRSPAPMSCDKSTQTPSPPCQAFNHYLSAMASIRQSQEEPEDLRPEIRIAQELRRIGDEFNETYTRRVFANDYREAEDHPQMVILQLLRFIFRLVWRRH
uniprot
proteins
function
FUNCTION: Induces apoptosis and anoikis. The isoforms vary in cytotoxicity with isoform BimS being the most potent and isoform BimEL being the least potent. {ECO:0000269|PubMed:9430630}.
uniprot
proteins
mass_dalton
22067
uniprot
proteins
mutagenesis
MUTAGEN 55; /note="S->A: Loss of TRIM2-binding; when associated with A-65 and A-73."; /evidence="ECO:0000269|PubMed:21478148"; MUTAGEN 65; /note="S->A: Loss of TRIM2-binding; when associated with A-55 and A-73."; /evidence="ECO:0000269|PubMed:21478148"; MUTAGEN 73; /note="S->A: Loss of TRIM2-binding; when associated with A-55 and A-65."; /evidence="ECO:0000269|PubMed:21478148"; MUTAGEN 150; /note="Missing: Loss of MCL1-binding, strong decrease in BCL2L1-binding, no effect on USP27X-binding; when associated with I-153 del."; /evidence="ECO:0000269|PubMed:27013495"; MUTAGEN 153; /note="Missing: Loss of MCL1-binding, strong decrease in BCL2L1-binding, no effect on USP27X-binding; when associated with L-150 del."; /evidence="ECO:0000269|PubMed:27013495
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Ser-65 by MAPK1/MAPK3 leads interaction with TRIM2 and ubiquitination, followed by proteasomal degradation (PubMed:21478148). Deubiquitination catalyzed by USP27X stabilizes the protein (PubMed:27013495). {ECO:0000269|PubMed:21478148, ECO:0000269|PubMed:27013495}.; PTM: Ubiquitination by TRIM2 following phosphorylation by MAPK1/MAPK3 leads to proteasomal degradation. Conversely, deubiquitination catalyzed by USP27X stabilizes the protein. {ECO:0000269|PubMed:21478148, ECO:0000269|PubMed:27013495}.
uniprot
proteins
protein_family
Bcl-2 family
uniprot
proteins
pubmed
14499110
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16509771
uniprot
proteins
pubmed
16543145
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21159964
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21478148
uniprot
proteins
pubmed
27013495
uniprot
proteins
pubmed
9430630
uniprot
proteins
sequence_length
196
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:9430630}; Peripheral membrane protein {ECO:0000269|PubMed:9430630}. Mitochondrion {ECO:0000250}. Note=Associated with intracytoplasmic membranes.
uniprot
proteins