BOK
entrez
666
canonical
uniprot
Q9UMX3
canonical
ensembl
ENSG00000176720
resolver
ensp
ENSP00000314132
resolver
ensp
ENSP00000523643
resolver
ensp
ENSP00000788102
resolver
ensp
ENSP00000788103
resolver
genesymbol
BOK
resolver
genesymbol_syn
BCL2L9
resolver
genesymbol_syn
BOKL
resolver
hgnc
HGNC:1087
resolver
uniprot
A0A024R4A8
resolver
uniprot
A0A481T0E4
resolver
uniprot
A0A481T0W6
resolver
uniprot
A0A4D6NU76
resolver
uniprot_entry
A0A024R4A8_HUMAN
resolver
uniprot_entry
A0A481T0W6_HUMAN
resolver
uniprot_entry
A0A4D6NU76_HUMAN
resolver
uniprot_entry
BOK_HUMAN
resolver
uniprot_sec
A0A481T0E4
resolver
amino_acid_sequence
MEVLRRSSVFAAEIMDAFDRSPTDKELVAQAKALGREYVHARLLRAGLSWSAPERAAPVPGRLAEVCAVLLRLGDELEMIRPSVYRNVARQLHISLQSEPVVTDAFLAVAGHIFSAGITWGKVVSLYAVAAGLAVDCVRQAQPAMVHALVDCLGEFVRKTLATWLRRRGGWTDVLKCVVSTDPGLRSHWLVAALCSFGRFLKAAFFVLLPER
uniprot
proteins
function
FUNCTION: [Isoform 1]: Apoptosis regulator that functions through different apoptotic signaling pathways (PubMed:15102863, PubMed:20673843, PubMed:27076518). 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:15102863, PubMed:27076518). In response to endoplasmic reticulum stress promotes mitochondrial apoptosis through downstream BAX/BAK1 activation and positive regulation of PERK-mediated unfolded protein response (By similarity). 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:27076518). In response to DNA damage, mediates intrinsic apoptotic process in a TP53-dependent manner (PubMed:15102863). Plays a role in granulosa cell apoptosis by CASP3 activation (PubMed:20673843). 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 (By similarity). 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 (PubMed:19942931). May also play a role as an inducer of autophagy by disrupting interaction between MCL1 and BECN1 (PubMed:24113155). {ECO:0000250|UniProtKB:O35425, ECO:0000269|PubMed:15102863, ECO:0000269|PubMed:19942931, ECO:0000269|PubMed:20673843, ECO:0000269|PubMed:24113155, ECO:0000269|PubMed:27076518}.; FUNCTION: [Isoform 2]: Pro-apoptotic molecule exerting its function through the mitochondrial pathway. {ECO:0000269|PubMed:15775999}.
uniprot
proteins
mass_dalton
23280
uniprot
proteins
mutagenesis
MUTAGEN 71..73; /note="LRL->AAA: Significantly accumulates in the nucleus. Increases apoptotic activity. Does not interact with XPO1."; /evidence="ECO:0000269|PubMed:16302269
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 pro-apoptotic activity; promotes degradation of newly synthesized proteins that are not ITPR1 associated. {ECO:0000250|UniProtKB:O35425}.
uniprot
proteins
protein_family
Bcl-2 family
uniprot
proteins
pubmed
11034351
uniprot
proteins
pubmed
15102863
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15775999
uniprot
proteins
pubmed
15868100
uniprot
proteins
pubmed
16302269
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
19942931
uniprot
proteins
pubmed
20673843
uniprot
proteins
pubmed
23884412
uniprot
proteins
pubmed
24113155
uniprot
proteins
pubmed
27076518
uniprot
proteins
pubmed
9535847
uniprot
proteins
sequence_length
212
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion membrane {ECO:0000250|UniProtKB:O35425}; Single-pass membrane protein {ECO:0000250|UniProtKB:O35425}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:27076518}; Single-pass membrane protein {ECO:0000250|UniProtKB:O35425}. Mitochondrion inner membrane {ECO:0000269|PubMed:24113155}. Cytoplasm {ECO:0000269|PubMed:15868100, ECO:0000269|PubMed:16302269, ECO:0000269|PubMed:19942931, ECO:0000269|PubMed:20673843, ECO:0000269|PubMed:24113155}. Nucleus {ECO:0000269|PubMed:16302269, ECO:0000269|PubMed:19942931, ECO:0000269|PubMed:20673843}. Mitochondrion {ECO:0000269|PubMed:15102863, ECO:0000269|PubMed:15868100, ECO:0000269|PubMed:19942931, ECO:0000269|PubMed:27076518}. Endoplasmic reticulum {ECO:0000269|PubMed:16302269}. Mitochondrion outer membrane {ECO:0000269|PubMed:27076518}. Early endosome membrane {ECO:0000250|UniProtKB:O35425}. Recycling endosome membrane {ECO:0000250|UniProtKB:O35425}. Nucleus outer membrane {ECO:0000250|UniProtKB:O35425}. Golgi apparatus, cis-Golgi network membrane {ECO:0000250|UniProtKB:O35425}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:O35425}. Membrane {ECO:0000269|PubMed:19942931}. Note=Nuclear and cytoplasmic compartments in the early stages of apoptosis and during apoptosis it associates with mitochondria (PubMed:19942931). 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 (PubMed:15868100). The transmembrane domain controls subcellular localization; constitutes a tail-anchor. Localizes in early and late endosome upon blocking of apoptosis. Must localize to the mitochondria to induce mitochondrial outer membrane permeabilization and apoptosis (By similarity). {ECO:0000250|UniProtKB:O35425, ECO:0000269|PubMed:15868100, ECO:0000269|PubMed:19942931}.; SUBCELLULAR LOCATION: [Isoform 2]: Membrane {ECO:0000269|PubMed:19942931}. Cytoplasm {ECO:0000269|PubMed:19942931}.
uniprot
proteins
transmembrane_region
TRANSMEM 189..209; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins