BOK_HUMAN
ID BOK_HUMAN Reviewed; 212 AA.
AC Q9UMX3;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Bcl-2-related ovarian killer protein {ECO:0000303|PubMed:11034351};
DE Short=hBOK {ECO:0000303|PubMed:15868100};
DE AltName: Full=Bcl-2-like protein 9;
DE Short=Bcl2-L-9;
GN Name=BOK {ECO:0000312|HGNC:HGNC:1087}; Synonyms=BCL2L9;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11034351; DOI=10.1016/s0014-5793(00)01921-9;
RA Zhang H., Holzgreve W., De Geyter C.;
RT "Evolutionarily conserved Bok proteins in the Bcl-2 family.";
RL FEBS Lett. 480:311-313(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), DEVELOPMENTAL STAGE, AND FUNCTION
RP (ISOFORM 2).
RX PubMed=15775999; DOI=10.1038/sj.cdd.4401593;
RA Soleymanlou N., Wu Y., Wang J.X., Todros T., Ietta F., Jurisicova A.,
RA Post M., Caniggia I.;
RT "A novel Mtd splice isoform is responsible for trophoblast cell death in
RT pre-eclampsia.";
RL Cell Death Differ. 12:441-452(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=9535847; DOI=10.1074/jbc.273.15.8705;
RA Inohara N., Ekhterae D., Garcia I., Carrio R., Merino J., Merry A.,
RA Chen S., Nunez G.;
RT "Mtd, a novel Bcl-2 family member activates apoptosis in the absence of
RT heterodimerization with Bcl-2 and Bcl-XL.";
RL J. Biol. Chem. 273:8705-8710(1998).
RN [6]
RP SUBCELLULAR LOCATION, FUNCTION, AND INDUCTION.
RX PubMed=15102863; DOI=10.1074/jbc.m313526200;
RA Yakovlev A.G., Di Giovanni S., Wang G., Liu W., Stoica B., Faden A.I.;
RT "BOK and NOXA are essential mediators of p53-dependent apoptosis.";
RL J. Biol. Chem. 279:28367-28374(2004).
RN [7]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH BNIP3.
RX PubMed=15868100; DOI=10.1007/s00018-005-4543-3;
RA Gao S., Fu W., Duerrenberger M., De Geyter C., Zhang H.;
RT "Membrane translocation and oligomerization of hBok are triggered in
RT response to apoptotic stimuli and Bnip3.";
RL Cell. Mol. Life Sci. 62:1015-1024(2005).
RN [8]
RP SUBCELLULAR LOCATION, MUTAGENESIS OF 71-LEU--LEU-73, REGION, AND
RP INTERACTION WITH XPO1.
RX PubMed=16302269; DOI=10.1002/mc.20156;
RA Bartholomeusz G., Wu Y., Ali Seyed M., Xia W., Kwong K.Y., Hortobagyi G.,
RA Hung M.C.;
RT "Nuclear translocation of the pro-apoptotic Bcl-2 family member Bok induces
RT apoptosis.";
RL Mol. Carcinog. 45:73-83(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=19942931; DOI=10.1038/cdd.2009.167;
RA Ray J.E., Garcia J., Jurisicova A., Caniggia I.;
RT "Mtd/Bok takes a swing: proapoptotic Mtd/Bok regulates trophoblast cell
RT proliferation during human placental development and in preeclampsia.";
RL Cell Death Differ. 17:846-859(2010).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=20673843; DOI=10.1016/j.mce.2010.07.020;
RA Jaeaeskelaeinen M., Nieminen A., Poekkylae R.M., Kauppinen M., Liakka A.,
RA Heikinheimo M., Vaskivuo T.E., Klefstroem J., Tapanainen J.S.;
RT "Regulation of cell death in human fetal and adult ovaries--role of Bok and
RT Bcl-X(L).";
RL Mol. Cell. Endocrinol. 330:17-24(2010).
RN [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24113155; DOI=10.4161/auto.26452;
RA Kalkat M., Garcia J., Ebrahimi J., Melland-Smith M., Todros T., Post M.,
RA Caniggia I.;
RT "Placental autophagy regulation by the BOK-MCL1 rheostat.";
RL Autophagy 9:2140-2153(2013).
RN [13]
RP INTERACTION WITH ITPR1.
RX PubMed=23884412; DOI=10.1074/jbc.m113.496570;
RA Schulman J.J., Wright F.A., Kaufmann T., Wojcikiewicz R.J.;
RT "The Bcl-2 protein family member Bok binds to the coupling domain of
RT inositol 1,4,5-trisphosphate receptors and protects them from proteolytic
RT cleavage.";
RL J. Biol. Chem. 288:25340-25349(2013).
RN [14]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=27076518; DOI=10.1242/jcs.181727;
RA Einsele-Scholz S., Malmsheimer S., Bertram K., Stehle D., Johaenning J.,
RA Manz M., Daniel P.T., Gillissen B.F., Schulze-Osthoff K., Essmann F.;
RT "Bok is a genuine multi-BH-domain protein that triggers apoptosis in the
RT absence of Bax and Bak.";
RL J. Cell Sci. 129:2213-2223(2016).
CC -!- FUNCTION: [Isoform 1]: Apoptosis regulator that functions through
CC different apoptotic signaling pathways (PubMed:27076518,
CC PubMed:15102863, PubMed:20673843). Plays a roles as pro-apoptotic
CC protein that positively regulates intrinsic apoptotic process in a
CC BAX- and BAK1-dependent manner or in a BAX- and BAK1-independent manner
CC (PubMed:27076518, PubMed:15102863). In response to endoplasmic
CC reticulum stress promotes mitochondrial apoptosis through downstream
CC BAX/BAK1 activation and positive regulation of PERK-mediated unfolded
CC protein response (By similarity). Activates apoptosis independently of
CC heterodimerization with survival-promoting BCL2 and BCL2L1 through
CC induction of mitochondrial outer membrane permeabilization, in a
CC BAX- and BAK1-independent manner, in response to inhibition of ERAD-
CC proteasome degradation system, resulting in cytochrome c release
CC (PubMed:27076518). In response to DNA damage, mediates intrinsic
CC apoptotic process in a TP53-dependent manner (PubMed:15102863). Plays a
CC role in granulosa cell apoptosis by CASP3 activation (PubMed:20673843).
CC Plays a roles as anti-apoptotic protein during neuronal apoptotic
CC process, by negatively regulating poly ADP-ribose polymerase-dependent
CC cell death through regulation of neuronal calcium homeostasis and
CC mitochondrial bioenergetics in response to NMDA excitation (By
CC similarity). In addition to its role in apoptosis, may regulate
CC trophoblast cell proliferation during the early stages of placental
CC development, by acting on G1/S transition through regulation of CCNE1
CC expression (PubMed:19942931). May also play a role as an inducer of
CC autophagy by disrupting interaction between MCL1 and BECN1
CC (PubMed:24113155). {ECO:0000250|UniProtKB:O35425,
CC ECO:0000269|PubMed:15102863, ECO:0000269|PubMed:19942931,
CC ECO:0000269|PubMed:20673843, ECO:0000269|PubMed:24113155,
CC ECO:0000269|PubMed:27076518}.
CC -!- FUNCTION: [Isoform 2]: Pro-apoptotic molecule exerting its function
CC through the mitochondrial pathway. {ECO:0000269|PubMed:15775999}.
CC -!- SUBUNIT: Monomer; positively regulates apoptotic process. Homodimer (By
CC similarity). Heterodimer (By similarity). Oligomer; promoted by
CC apoptotic stimuli and BH3-only proteins; mediates constitutive
CC activation (PubMed:15868100). Interacts (via BH4 domain) with ITPR1;
CC enhances BOK expression and stabilization; limits apoptosis and
CC prevents ubiquitination and then degradation; protects ITPR1 from
CC proteolysis by CASP3 during apoptosis (PubMed:23884412). Interacts with
CC ITPR2 AND ITPR3; binds most strongly to ITPR2, and barely to ITPR3;
CC regulates their expression (By similarity). Interacts with XPO1;
CC translocates to the cytoplasm (PubMed:16302269). Interacts with BNIP3;
CC promotes oligomerization (PubMed:15868100).
CC {ECO:0000250|UniProtKB:O35425, ECO:0000250|UniProtKB:Q792S6,
CC ECO:0000269|PubMed:15868100, ECO:0000269|PubMed:16302269,
CC ECO:0000269|PubMed:23884412}.
CC -!- INTERACTION:
CC Q9UMX3; Q86V38: ATN1; NbExp=3; IntAct=EBI-7105206, EBI-11954292;
CC Q9UMX3; P13637: ATP1A3; NbExp=3; IntAct=EBI-7105206, EBI-948169;
CC Q9UMX3; P50570-2: DNM2; NbExp=3; IntAct=EBI-7105206, EBI-10968534;
CC Q9UMX3; Q8TB36: GDAP1; NbExp=3; IntAct=EBI-7105206, EBI-11110431;
CC Q9UMX3; P10809: HSPD1; NbExp=3; IntAct=EBI-7105206, EBI-352528;
CC Q9UMX3; P16284: PECAM1; NbExp=3; IntAct=EBI-7105206, EBI-716404;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion membrane
CC {ECO:0000250|UniProtKB:O35425}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:O35425}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:27076518}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:O35425}. Mitochondrion inner membrane
CC {ECO:0000269|PubMed:24113155}. Cytoplasm {ECO:0000269|PubMed:15868100,
CC ECO:0000269|PubMed:16302269, ECO:0000269|PubMed:19942931,
CC ECO:0000269|PubMed:20673843, ECO:0000269|PubMed:24113155}. Nucleus
CC {ECO:0000269|PubMed:16302269, ECO:0000269|PubMed:19942931,
CC ECO:0000269|PubMed:20673843}. Mitochondrion
CC {ECO:0000269|PubMed:15102863, ECO:0000269|PubMed:15868100,
CC ECO:0000269|PubMed:19942931, ECO:0000269|PubMed:27076518}. Endoplasmic
CC reticulum {ECO:0000269|PubMed:16302269}. Mitochondrion outer membrane
CC {ECO:0000269|PubMed:27076518}. Early endosome membrane
CC {ECO:0000250|UniProtKB:O35425}. Recycling endosome membrane
CC {ECO:0000250|UniProtKB:O35425}. Nucleus outer membrane
CC {ECO:0000250|UniProtKB:O35425}. Golgi apparatus, cis-Golgi network
CC membrane {ECO:0000250|UniProtKB:O35425}. Golgi apparatus, trans-Golgi
CC network membrane {ECO:0000250|UniProtKB:O35425}. Membrane
CC {ECO:0000269|PubMed:19942931}. Note=Nuclear and cytoplasmic
CC compartments in the early stages of apoptosis and during apoptosis it
CC associates with mitochondria (PubMed:19942931). In healthy cells,
CC associates loosely with the membrane in a hit-and-run mode. The
CC insertion and accumulation on membranes is enhanced through the
CC activity of death signals, resulting in the integration of the
CC membrane-bound protein into the membrane (PubMed:15868100). The
CC transmembrane domain controls subcellular localization; constitutes a
CC tail-anchor. Localizes in early and late endosome upon blocking of
CC apoptosis. Must localize to the mitochondria to induce mitochondrial
CC outer membrane permeabilization and apoptosis (By similarity).
CC {ECO:0000250|UniProtKB:O35425, ECO:0000269|PubMed:15868100,
CC ECO:0000269|PubMed:19942931}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Membrane
CC {ECO:0000269|PubMed:19942931}. Cytoplasm {ECO:0000269|PubMed:19942931}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Mtd-L {ECO:0000303|PubMed:15775999};
CC IsoId=Q9UMX3-1; Sequence=Displayed;
CC Name=2; Synonyms=Mtd-P {ECO:0000303|PubMed:15775999};
CC IsoId=Q9UMX3-2; Sequence=VSP_058599;
CC -!- TISSUE SPECIFICITY: Expressed mainly in oocytes; weak expression in
CC granulosa cells of the developing follicles. In adult human ovaries,
CC expressed in granulosa cells at all follicular stages, but expression
CC in primordial/primary follicles granulosa cell is stronger than in
CC secondary and antral follicles. {ECO:0000269|PubMed:20673843}.
CC -!- DEVELOPMENTAL STAGE: Isoform 1: at 5-7 weeks of gestation, detected
CC primarily in the cytotrophoblast layer. By 10-13 weeks, expression
CC becomes restricted primarily to the apical border of the
CC syncytiotrophoblast (PubMed:19942931). Isoform 2: expression
CC significantly increased around 6-8 weeks (PubMed:15775999).
CC {ECO:0000269|PubMed:15775999, ECO:0000269|PubMed:19942931}.
CC -!- INDUCTION: Up-regulated by DNA damage. {ECO:0000269|PubMed:15102863}.
CC -!- DOMAIN: BH4 domain mediates interaction with ITPR1.
CC {ECO:0000250|UniProtKB:O35425}.
CC -!- PTM: Ubiquitinated by AMFR/gp78 E3 ubiquitin ligase complex; mediates
CC degradation by ubiquitin-proteasome pathway in a VCP/p97-dependent
CC manner; prevents from pro-apoptotic activity; promotes degradation of
CC newly synthesized proteins that are not ITPR1 associated.
CC {ECO:0000250|UniProtKB:O35425}.
CC -!- SIMILARITY: Belongs to the Bcl-2 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/BOKID824ch2q37.html";
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DR EMBL; AF174487; AAD51719.1; -; mRNA.
DR EMBL; BT007272; AAP35936.1; -; mRNA.
DR EMBL; BC006203; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS2550.1; -. [Q9UMX3-1]
DR RefSeq; NP_115904.1; NM_032515.4. [Q9UMX3-1]
DR RefSeq; XP_011509998.1; XM_011511696.2. [Q9UMX3-1]
DR PDB; 6CKV; NMR; -; A=21-177.
DR PDBsum; 6CKV; -.
DR AlphaFoldDB; Q9UMX3; -.
DR BMRB; Q9UMX3; -.
DR SMR; Q9UMX3; -.
DR BioGRID; 107134; 9.
DR IntAct; Q9UMX3; 8.
DR MINT; Q9UMX3; -.
DR STRING; 9606.ENSP00000314132; -.
DR TCDB; 1.A.21.1.7; the bcl-2 (bcl-2) family.
DR iPTMnet; Q9UMX3; -.
DR PhosphoSitePlus; Q9UMX3; -.
DR BioMuta; BOK; -.
DR DMDM; 57012554; -.
DR EPD; Q9UMX3; -.
DR jPOST; Q9UMX3; -.
DR MassIVE; Q9UMX3; -.
DR PaxDb; Q9UMX3; -.
DR PeptideAtlas; Q9UMX3; -.
DR PRIDE; Q9UMX3; -.
DR ProteomicsDB; 85221; -.
DR Antibodypedia; 20324; 280 antibodies from 32 providers.
DR DNASU; 666; -.
DR Ensembl; ENST00000318407.5; ENSP00000314132.3; ENSG00000176720.6. [Q9UMX3-1]
DR GeneID; 666; -.
DR KEGG; hsa:666; -.
DR MANE-Select; ENST00000318407.5; ENSP00000314132.3; NM_032515.5; NP_115904.1.
DR UCSC; uc002wbq.4; human. [Q9UMX3-1]
DR CTD; 666; -.
DR DisGeNET; 666; -.
DR GeneCards; BOK; -.
DR HGNC; HGNC:1087; BOK.
DR HPA; ENSG00000176720; Tissue enhanced (brain).
DR MIM; 605404; gene.
DR neXtProt; NX_Q9UMX3; -.
DR OpenTargets; ENSG00000176720; -.
DR PharmGKB; PA25396; -.
DR VEuPathDB; HostDB:ENSG00000176720; -.
DR eggNOG; KOG4728; Eukaryota.
DR GeneTree; ENSGT01050000244872; -.
DR HOGENOM; CLU_114994_0_0_1; -.
DR InParanoid; Q9UMX3; -.
DR OMA; DMTKCVV; -.
DR PhylomeDB; Q9UMX3; -.
DR TreeFam; TF315834; -.
DR PathwayCommons; Q9UMX3; -.
DR SignaLink; Q9UMX3; -.
DR BioGRID-ORCS; 666; 8 hits in 1072 CRISPR screens.
DR ChiTaRS; BOK; human.
DR GeneWiki; BOK_(gene); -.
DR GenomeRNAi; 666; -.
DR Pharos; Q9UMX3; Tbio.
DR PRO; PR:Q9UMX3; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9UMX3; protein.
DR Bgee; ENSG00000176720; Expressed in C1 segment of cervical spinal cord and 164 other tissues.
DR ExpressionAtlas; Q9UMX3; baseline and differential.
DR Genevisible; Q9UMX3; HS.
DR GO; GO:0033106; C:cis-Golgi network membrane; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005640; C:nuclear outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB.
DR GO; GO:0032588; C:trans-Golgi network membrane; ISS:UniProtKB.
DR GO; GO:0051400; F:BH domain binding; IEA:Ensembl.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB.
DR GO; GO:0008635; P:activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IDA:UniProtKB.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0006921; P:cellular component disassembly involved in execution phase of apoptosis; ISS:UniProtKB.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IBA:GO_Central.
DR GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; IMP:UniProtKB.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IBA:GO_Central.
DR GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR GO; GO:0051902; P:negative regulation of mitochondrial depolarization; IEA:Ensembl.
DR GO; GO:1901029; P:negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0060546; P:negative regulation of necroptotic process; IEA:Ensembl.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0048709; P:oligodendrocyte differentiation; IEA:Ensembl.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:1902237; P:positive regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; ISS:UniProtKB.
DR GO; GO:1900119; P:positive regulation of execution phase of apoptosis; IMP:UniProtKB.
DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; ISS:UniProtKB.
DR GO; GO:1901030; P:positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; ISS:UniProtKB.
DR GO; GO:1903899; P:positive regulation of PERK-mediated unfolded protein response; ISS:UniProtKB.
DR GO; GO:0051259; P:protein complex oligomerization; ISS:UniProtKB.
DR GO; GO:0010506; P:regulation of autophagy; IMP:UniProtKB.
DR GO; GO:1901382; P:regulation of chorionic trophoblast cell proliferation; IDA:UniProtKB.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IEA:Ensembl.
DR GO; GO:1904708; P:regulation of granulosa cell apoptotic process; IMP:UniProtKB.
DR GO; GO:0001836; P:release of cytochrome c from mitochondria; IDA:UniProtKB.
DR CDD; cd06845; Bcl-2_like; 1.
DR Gene3D; 1.10.437.10; -; 1.
DR InterPro; IPR036834; Bcl-2-like_sf.
DR InterPro; IPR046371; Bcl-2_BH1-3.
DR InterPro; IPR026298; Bcl-2_fam.
DR InterPro; IPR002475; Bcl2-like.
DR InterPro; IPR026309; BOK.
DR PANTHER; PTHR11256; PTHR11256; 1.
DR PANTHER; PTHR11256:SF48; PTHR11256:SF48; 1.
DR Pfam; PF00452; Bcl-2; 1.
DR PRINTS; PR01862; BCL2FAMILY.
DR SMART; SM00337; BCL; 1.
DR SUPFAM; SSF56854; SSF56854; 1.
DR PROSITE; PS50062; BCL2_FAMILY; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Apoptosis; Cytoplasm;
KW Endoplasmic reticulum; Endosome; Golgi apparatus; Isopeptide bond;
KW Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Mitochondrion outer membrane; Nucleus; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix; Ubl conjugation.
FT CHAIN 1..212
FT /note="Bcl-2-related ovarian killer protein"
FT /id="PRO_0000143086"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 15..45
FT /note="Interactions with ITPR1"
FT /evidence="ECO:0000250|UniProtKB:O35425"
FT REGION 70..78
FT /note="Nuclear export signal"
FT /evidence="ECO:0000269|PubMed:16302269"
FT MOTIF 32..44
FT /note="BH4"
FT MOTIF 66..82
FT /note="BH3"
FT MOTIF 112..131
FT /note="BH1"
FT MOTIF 164..178
FT /note="BH2"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35425"
FT CROSSLNK 25
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:O35425"
FT CROSSLNK 32
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:O35425"
FT CROSSLNK 159
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:O35425"
FT CROSSLNK 176
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:O35425"
FT VAR_SEQ 1..78
FT /note="Missing (in isoform 2)"
FT /id="VSP_058599"
FT MUTAGEN 71..73
FT /note="LRL->AAA: Significantly accumulates in the nucleus.
FT Increases apoptotic activity. Does not interact with XPO1."
FT /evidence="ECO:0000269|PubMed:16302269"
FT HELIX 24..46
FT /evidence="ECO:0007829|PDB:6CKV"
FT HELIX 61..80
FT /evidence="ECO:0007829|PDB:6CKV"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:6CKV"
FT HELIX 88..91
FT /evidence="ECO:0007829|PDB:6CKV"
FT HELIX 100..115
FT /evidence="ECO:0007829|PDB:6CKV"
FT HELIX 120..139
FT /evidence="ECO:0007829|PDB:6CKV"
FT HELIX 144..159
FT /evidence="ECO:0007829|PDB:6CKV"
FT HELIX 162..168
FT /evidence="ECO:0007829|PDB:6CKV"
FT HELIX 171..176
FT /evidence="ECO:0007829|PDB:6CKV"
SQ SEQUENCE 212 AA; 23280 MW; 053ED605FF8EF5B2 CRC64;
MEVLRRSSVF AAEIMDAFDR SPTDKELVAQ AKALGREYVH ARLLRAGLSW SAPERAAPVP
GRLAEVCAVL LRLGDELEMI RPSVYRNVAR QLHISLQSEP VVTDAFLAVA GHIFSAGITW
GKVVSLYAVA AGLAVDCVRQ AQPAMVHALV DCLGEFVRKT LATWLRRRGG WTDVLKCVVS
TDPGLRSHWL VAALCSFGRF LKAAFFVLLP ER
