BAX
entrez
581
canonical
uniprot
Q07812
canonical
ensembl
ENSG00000087088
resolver
ensp
ENSP00000263262
resolver
ensp
ENSP00000293288
resolver
ensp
ENSP00000346461
resolver
ensp
ENSP00000389971
resolver
ensp
ENSP00000426184
resolver
ensp
ENSP00000441413
resolver
ensp
ENSP00000765885
resolver
enst
ENST00000539787
resolver
genesymbol
BAX
resolver
genesymbol_syn
BCL2L4
resolver
hgnc
HGNC:959
resolver
uniprot
A0A0A0MTJ3
resolver
uniprot
A8K4W1
resolver
uniprot
I6LPK7
resolver
uniprot
P55269
resolver
uniprot
Q07814
resolver
uniprot
Q07815
resolver
uniprot
Q5ZPJ0
resolver
uniprot
Q5ZPJ1
resolver
uniprot
Q8WZ49
resolver
uniprot
Q9NR76
resolver
uniprot
Q9NYG7
resolver
uniprot
Q9UCZ6
resolver
uniprot
Q9UCZ7
resolver
uniprot
Q9UQD6
resolver
uniprot_entry
A0A0A0MTJ3_HUMAN
resolver
uniprot_entry
BAX_HUMAN
resolver
uniprot_entry
I6LPK7_HUMAN
resolver
uniprot_entry
Q5ZPJ0_HUMAN
resolver
uniprot_entry
Q5ZPJ1_HUMAN
resolver
uniprot_sec
A8K4W1
resolver
uniprot_sec
P55269
resolver
uniprot_sec
Q07814
resolver
uniprot_sec
Q07815
resolver
uniprot_sec
Q8WZ49
resolver
uniprot_sec
Q9NR76
resolver
uniprot_sec
Q9NYG7
resolver
uniprot_sec
Q9UCZ6
resolver
uniprot_sec
Q9UCZ7
resolver
uniprot_sec
Q9UQD6
resolver
amino_acid_sequence
MDGSGEQPRGGGPTSSEQIMKTGALLLQGFIQDRAGRMGGEAPELALDPVPQDASTKKLSECLKRIGDELDSNMELQRMIAAVDTDSPREVFFRVAADMFSDGNFNWGRVVALFYFASKLVLKALCTKVPELIRTIMGWTLDFLRERLLGWIQDQGGWDGLLSYFGTPTWQTVTIFVAGVLTASLTIWKKMG
uniprot
proteins
function
FUNCTION: Plays a role in the mitochondrial apoptotic process (PubMed:10772918, PubMed:11060313, PubMed:16113678, PubMed:16199525, PubMed:18948948, PubMed:21199865, PubMed:21458670, PubMed:25609812, PubMed:36361894, PubMed:8358790, PubMed:8521816). Under normal conditions, BAX is largely cytosolic via constant retrotranslocation from mitochondria to the cytosol mediated by BCL2L1/Bcl-xL, which avoids accumulation of toxic BAX levels at the mitochondrial outer membrane (MOM) (PubMed:21458670). Under stress conditions, undergoes a conformation change that causes translocation to the mitochondrion membrane, leading to the release of cytochrome c that then triggers apoptosis (PubMed:10772918, PubMed:11060313, PubMed:16113678, PubMed:16199525, PubMed:18948948, PubMed:21199865, PubMed:21458670, PubMed:25609812, PubMed:8358790, PubMed:8521816). Promotes activation of CASP3, and thereby apoptosis (PubMed:10772918, PubMed:11060313, PubMed:16113678, PubMed:16199525, PubMed:18948948, PubMed:21199865, PubMed:21458670, PubMed:25609812, PubMed:8358790, PubMed:8521816). {ECO:0000269|PubMed:10772918, ECO:0000269|PubMed:11060313, ECO:0000269|PubMed:16113678, ECO:0000269|PubMed:16199525, ECO:0000269|PubMed:18948948, ECO:0000269|PubMed:21199865, ECO:0000269|PubMed:21458670, ECO:0000269|PubMed:25609812, ECO:0000269|PubMed:36361894, ECO:0000269|PubMed:8358790, ECO:0000269|PubMed:8521816}.
uniprot
proteins
mass_dalton
21184
uniprot
proteins
mutagenesis
MUTAGEN 21; /note="K->E: Reduces interaction with BCL2L11, homooligomerization and triggering of apoptosis."; /evidence="ECO:0000269|PubMed:18948948"; MUTAGEN 74; /note="M->D,E: Strongly reduced interaction with MCL1, BCL2, BCL2L1 and BCL2L2. No effect on cytochrome c release and subsequent apoptosis triggered by etoposide."; /evidence="ECO:0000269|PubMed:21199865"; MUTAGEN 128; /note="K->R: Partial loss of polyubiquitination."; /evidence="ECO:0000269|PubMed:36361894"; MUTAGEN 172..192; /note="Missing: Enhanced fiber formation with humanin."; /evidence="ECO:0000269|PubMed:31690630"; MUTAGEN 184; /note="S->D,E,H,K: Constitutive cytoplasmic location."; /evidence="ECO:0000269|PubMed:10228148"; MUTAGEN 184; /note="S->V: Constitutive mitochondrial location. Enhanced fiber formation with humanin."; /evidence="ECO:0000269|PubMed:10228148, ECO:0000269|PubMed:31690630"; MUTAGEN 189; /note="K->R: No loss of polyubiquitination."; /evidence="ECO:0000269|PubMed:36361894"; MUTAGEN 190; /note="K->R: Partial loss of polyubiquitination."; /evidence="ECO:0000269|PubMed:36361894
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated in the absence of XRCC6/Ku70 (PubMed:18362350). Ubiquitination promotes protein degradation (PubMed:18362350). Ubiquitinated on Lys-128 and Lys-190. 'Lys-63'-linked polyubiquitin chains on Lys-128 are removed by USP12. {ECO:0000269|PubMed:18362350, ECO:0000269|PubMed:36361894}.
uniprot
proteins
protein_family
Bcl-2 family
uniprot
proteins
pubmed
10228148
uniprot
proteins
pubmed
10772918
uniprot
proteins
pubmed
11060313
uniprot
proteins
pubmed
11106734
uniprot
proteins
pubmed
11259440
uniprot
proteins
pubmed
11462023
uniprot
proteins
pubmed
11912183
uniprot
proteins
pubmed
12732850
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15004026
uniprot
proteins
pubmed
15004034
uniprot
proteins
pubmed
15023334
uniprot
proteins
pubmed
15071501
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16113678
uniprot
proteins
pubmed
16199525
uniprot
proteins
pubmed
16509771
uniprot
proteins
pubmed
16946732
uniprot
proteins
pubmed
16964429
uniprot
proteins
pubmed
18362350
uniprot
proteins
pubmed
18948948
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
20300062
uniprot
proteins
pubmed
21199865
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21458670
uniprot
proteins
pubmed
23055042
uniprot
proteins
pubmed
23235460
uniprot
proteins
pubmed
25609812
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
27558414
uniprot
proteins
pubmed
29531808
uniprot
proteins
pubmed
31690630
uniprot
proteins
pubmed
36361894
uniprot
proteins
pubmed
7475270
uniprot
proteins
pubmed
7607685
uniprot
proteins
pubmed
8358790
uniprot
proteins
pubmed
8521816
uniprot
proteins
pubmed
9531611
uniprot
proteins
pubmed
9920818
uniprot
proteins
sequence_length
192
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Isoform Alpha]: Mitochondrion outer membrane {ECO:0000269|PubMed:25609812, ECO:0000269|PubMed:29531808}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:27558414, ECO:0000269|PubMed:29531808}. Nucleus {ECO:0000269|PubMed:36361894}. Note=Colocalizes with 14-3-3 proteins in the cytoplasm. Under stress conditions, undergoes a conformation change that causes release from JNK-phosphorylated 14-3-3 proteins and translocation to the mitochondrion membrane. Upon Sendai virus infection, recruited to the mitochondrion through interaction with IRF3 (PubMed:25609812). {ECO:0000269|PubMed:25609812}.; SUBCELLULAR LOCATION: [Isoform Beta]: Cytoplasm.; SUBCELLULAR LOCATION: [Isoform Gamma]: Cytoplasm.; SUBCELLULAR LOCATION: [Isoform Delta]: Cytoplasm {ECO:0000305}.
uniprot
proteins
transmembrane_region
TRANSMEM 172..192; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins