Bok
entrez
51800
canonical
uniprot
O35425
canonical
ensembl
ENSMUSG00000026278
resolver
ensp
ENSMUSP00000027499
resolver
genesymbol
Bok
resolver
genesymbol_syn
Mtd
resolver
uniprot
Q3TH93
resolver
uniprot_entry
BOK_MOUSE
resolver
uniprot_entry
Q3TH93_MOUSE
resolver
amino_acid_sequence
MEVLRRSSVFAAEIMDAFDRSPTDKELVAQAKALGREYVHARLLRAGLSWSAPERASPAPGGRLAEVCTVLLRLGDELEQIRPSVYRNVARQLHIPLQSEPVVTDAFLAVAGHIFSAGITWGKVVSLYSVAAGLAVDCVRQAQPAMVHALVDCLGEFVRKTLATWLRRRGGWTDVLKCVVSTDPGFRSHWLVATLCSFGRFLKAAFFLLLPER
uniprot
proteins
function
FUNCTION: Apoptosis regulator that functions through different apoptotic signaling pathways (PubMed:23429263, PubMed:26015568, PubMed:26949185, PubMed:27098698, PubMed:9535847). Plays a roles as pro-apoptotic protein that positively regulates intrinsic apoptotic process in a BAX- and BAK1-dependent manner or in a BAX- and BAK1-independent manner (PubMed:23429263, PubMed:26015568, PubMed:26949185). In response to endoplasmic reticulum stress promotes mitochondrial apoptosis through downstream BAX/BAK1 activation and positive regulation of PERK-mediated unfolded protein response (PubMed:26015568). Activates apoptosis independently of heterodimerization with survival-promoting BCL2 and BCL2L1 through induction of mitochondrial outer membrane permeabilization, in a BAX- and BAK1-independent manner, in response to inhibition of ERAD-proteasome degradation system, resulting in cytochrome c release (PubMed:26949185, PubMed:9535847). In response to DNA damage, mediates intrinsic apoptotic process in a TP53-dependent manner. Plays a role in granulosa cell apoptosis by CASP3 activation (By similarity). Plays a roles as anti-apoptotic protein during neuronal apoptotic process, by negatively regulating poly ADP-ribose polymerase-dependent cell death through regulation of neuronal calcium homeostasis and mitochondrial bioenergetics in response to NMDA excitation (PubMed:27098698). In addition to its role in apoptosis, may regulate trophoblast cell proliferation during the early stages of placental development, by acting on G1/S transition through regulation of CCNE1 expression. May also play a role as an inducer of autophagy by disrupting interaction between MCL1 and BECN1 (By similarity). {ECO:0000250|UniProtKB:Q9UMX3, ECO:0000269|PubMed:23429263, ECO:0000269|PubMed:26015568, ECO:0000269|PubMed:26949185, ECO:0000269|PubMed:27098698, ECO:0000269|PubMed:9535847}.
uniprot
proteins
mass_dalton
23456
uniprot
proteins
mutagenesis
MUTAGEN 25; /note="K->R: Increases protein expression and stability; when associated with R-32, R-160 and R-177. Increases apoptosis; when associated with R-32, R-160 and R-177."; /evidence="ECO:0000269|PubMed:26949185"; MUTAGEN 32; /note="K->R: Increases protein expression and stability; when associated with R-25, R-160 and R-177. Increases apoptosis; when associated with R-25, R-160 and R-177."; /evidence="ECO:0000269|PubMed:26949185"; MUTAGEN 34..38; /note="LGREY->AAAAA: Does not interact with ITPR1."; /evidence="ECO:0000269|PubMed:23884412"; MUTAGEN 34; /note="L->G: Does not interact with ITPR1. Triggers apoptosis."; /evidence="ECO:0000269|PubMed:27053113"; MUTAGEN 71; /note="L->Q: No change in apoptosis induction; when associated with Q-74 and Q-78."; /evidence="ECO:0000269|PubMed:9535847"; MUTAGEN 74; /note="L->Q: No change in apoptosis induction; when associated with Q-71 and Q-78."; /evidence="ECO:0000269|PubMed:9535847"; MUTAGEN 76; /note="D->A: Disrupts homodimerization. Positively regulates intrinsic apoptotic signaling pathway."; /evidence="ECO:0000269|PubMed:23429263"; MUTAGEN 78; /note="L->Q: No change in apoptosis induction; when associated with Q-71 and Q-74."; /evidence="ECO:0000269|PubMed:9535847"; MUTAGEN 160; /note="K->R: Increases protein expression and stability; when associated with R-25, R-32 and R-177. Increases apoptosis; when associated with R-25, R-32 and R-177."; /evidence="ECO:0000269|PubMed:26949185"; MUTAGEN 177; /note="K->R: Increases protein expression and stability; when associated with R-25, R-32 and R-160. Increases apoptosis; when associated with R-25, R-32 and R-160."; /evidence="ECO:0000269|PubMed:26949185
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated by AMFR/gp78 E3 ubiquitin ligase complex; mediates degradation by ubiquitin-proteasome pathway in a VCP/p97-dependent manner; prevents from proapoptotic activity; promotes degradation of newly synthesized proteins that are not ITPR1 associated. {ECO:0000269|PubMed:23884412, ECO:0000269|PubMed:26949185, ECO:0000269|PubMed:27053113}.
uniprot
proteins
protein_family
Bcl-2 family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23429263
uniprot
proteins
pubmed
23884412
uniprot
proteins
pubmed
26015568
uniprot
proteins
pubmed
26949185
uniprot
proteins
pubmed
27053113
uniprot
proteins
pubmed
27098698
uniprot
proteins
pubmed
9535847
uniprot
proteins
sequence_length
213
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000269|PubMed:23429263, ECO:0000269|PubMed:26949185}; Single-pass membrane protein {ECO:0000269|PubMed:26949185}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:23429263, ECO:0000269|PubMed:26949185}; Single-pass membrane protein {ECO:0000269|PubMed:26949185}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9UMX3}. Cytoplasm {ECO:0000250|UniProtKB:Q9UMX3}. Nucleus {ECO:0000250|UniProtKB:Q9UMX3}. Mitochondrion {ECO:0000250|UniProtKB:Q9UMX3}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9UMX3}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q9UMX3}. Early endosome membrane {ECO:0000269|PubMed:23429263}. Recycling endosome membrane {ECO:0000269|PubMed:23429263}. Nucleus outer membrane {ECO:0000269|PubMed:23429263}. Golgi apparatus, cis-Golgi network membrane {ECO:0000269|PubMed:23429263}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:23429263}. Membrane {ECO:0000250|UniProtKB:Q9UMX3}. Note=Nuclear and cytoplasmic compartments in the early stages of apoptosis and during apoptosis associates with mitochondria. In healthy cells, associates loosely with the membrane in a hit-and-run mode. The insertion and accumulation on membranes is enhanced through the activity of death signals, resulting in the integration of the membrane-bound protein into the membrane (By similarity). The transmembrane domain controls subcellular localization; constitutes a tail-anchor (PubMed:23429263, PubMed:26949185). Localizes in early and late endosome upon blocking of apoptosis (PubMed:23429263). Must localize to the mitochondria to induce mitochondrial outer membrane permeabilization and apoptosis (PubMed:26949185). {ECO:0000250|UniProtKB:Q9UMX3, ECO:0000269|PubMed:23429263, ECO:0000269|PubMed:26949185}.
uniprot
proteins
transmembrane_region
TRANSMEM 190..210; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins