Bad
entrez
12015
canonical
uniprot
Q61337
canonical
ensembl
ENSMUSG00000024959
resolver
ensp
ENSMUSP00000025910
resolver
ensp
ENSMUSP00000109050
resolver
ensp
ENSMUSP00000157664
resolver
ensp
ENSMUSP00000158059
resolver
enst
ENSMUST00000025910
resolver
enst
ENSMUST00000113423
resolver
enst
ENSMUST00000235240
resolver
enst
ENSMUST00000238184
resolver
genesymbol
Bad
resolver
genesymbol_syn
Bbc6
resolver
uniprot
F6WY57
resolver
uniprot
Q3U9H3
resolver
uniprot_entry
BAD_MOUSE
resolver
uniprot_entry
F6WY57_MOUSE
resolver
uniprot_entry
Q3U9H3_MOUSE
resolver
amino_acid_sequence
MGTPKQPSLAPAHALGLRKSDPGIRSLGSDAGGRRWRPAAQSMFQIPEFEPSEQEDASATDRGLGPSLTEDQPGPYLAPGLLGSNIHQQGRAATNSHHGGAGAMETRSRHSSYPAGTEEDEGMEEELSPFRGRSRSAPPNLWAAQRYGRELRRMSDEFEGSFKGLPRPKSAGTATQMRQSAGWTRIIQSWWDRNLGKGGSTPSQ
uniprot
proteins
function
FUNCTION: Promotes cell death. Successfully competes for the binding to Bcl-X(L), Bcl-2 and Bcl-W, thereby affecting the level of heterodimerization of these proteins with BAX. Can reverse the death repressor activity of Bcl-X(L), but not that of Bcl-2. Appears to act as a link between growth factor receptor signaling and the apoptotic pathways.
uniprot
proteins
mass_dalton
22080
uniprot
proteins
mutagenesis
MUTAGEN 112; /note="S->A: Enhances pro-apoptotic activity; no phosphorylation."; /evidence="ECO:0000269|PubMed:11717309, ECO:0000269|PubMed:9381178"; MUTAGEN 136; /note="S->A: No phosphorylation."; /evidence="ECO:0000269|PubMed:9381178"; MUTAGEN 155; /note="S->A: Enhances pro-apoptotic activity; no phosphorylation; interacts with Bcl-X(L)."; /evidence="ECO:0000269|PubMed:11717309"; MUTAGEN 155; /note="S->D: No pro-apoptotic activity, no interaction with Bcl-X(L)."; /evidence="ECO:0000269|PubMed:11717309"; MUTAGEN 170; /note="S->A: Enhances pro-apoptotic activity."; /evidence="ECO:0000269|PubMed:11717309"; MUTAGEN 170; /note="S->D: No pro-apoptotic activity; even when associated with A-112."; /evidence="ECO:0000269|PubMed:11717309
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on one or more of Ser-112, Ser-136, Ser-155 and Ser-170 in response to survival stimuli, which blocks its pro-apoptotic activity. Phosphorylation on Ser-136 or Ser-112 promotes heterodimerization with 14-3-3 proteins. This interaction then facilitates the phosphorylation at Ser-155, a site within the BH3 motif, leading to the release of Bcl-X(L) and the promotion of cell survival. Ser-136 is the major site of AKT/PKB phosphorylation, Ser-155 the major site of protein kinase A (CAPK) phosphorylation. {ECO:0000269|PubMed:10611223, ECO:0000269|PubMed:10679322, ECO:0000269|PubMed:11278362, ECO:0000269|PubMed:11342610, ECO:0000269|PubMed:11493700, ECO:0000269|PubMed:11717309, ECO:0000269|PubMed:12954615, ECO:0000269|PubMed:15849194, ECO:0000269|PubMed:9381178}.; PTM: Methylation at Arg-131 and Arg-133 by PRMT1 inhibits Akt-mediated phosphorylation at Ser-136. {ECO:0000269|PubMed:10611223, ECO:0000269|PubMed:10679322, ECO:0000269|PubMed:11342610, ECO:0000269|PubMed:11493700, ECO:0000269|PubMed:9381178}.
uniprot
proteins
protein_family
Bcl-2 family
uniprot
proteins
pubmed
10611223
uniprot
proteins
pubmed
10679322
uniprot
proteins
pubmed
10949026
uniprot
proteins
pubmed
11278362
uniprot
proteins
pubmed
11342610
uniprot
proteins
pubmed
11493700
uniprot
proteins
pubmed
11717309
uniprot
proteins
pubmed
12954615
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15849194
uniprot
proteins
pubmed
16509771
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21546903
uniprot
proteins
pubmed
7834748
uniprot
proteins
pubmed
9381178
uniprot
proteins
sequence_length
204
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion outer membrane. Cytoplasm {ECO:0000269|PubMed:21546903}. Note=Colocalizes with HIF3A isoform 2 in the cytoplasm (PubMed:21546903). Upon phosphorylation, locates to the cytoplasm. {ECO:0000269|PubMed:21546903}.
uniprot
proteins