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Bcl-2-related ovarian killer protein (hBOK) (Bcl-2-like protein 9) (Bcl2-L-9)

 BOK_HUMAN               Reviewed;         212 AA.
Q9UMX3;
04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
29-SEP-2021, entry version 157.
RecName: Full=Bcl-2-related ovarian killer protein {ECO:0000303|PubMed:11034351};
Short=hBOK {ECO:0000303|PubMed:15868100};
AltName: Full=Bcl-2-like protein 9;
Short=Bcl2-L-9;
Name=BOK {ECO:0000312|HGNC:HGNC:1087}; Synonyms=BCL2L9;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=11034351; DOI=10.1016/s0014-5793(00)01921-9;
Zhang H., Holzgreve W., De Geyter C.;
"Evolutionarily conserved Bok proteins in the Bcl-2 family.";
FEBS Lett. 480:311-313(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), DEVELOPMENTAL STAGE, AND FUNCTION
(ISOFORM 2).
PubMed=15775999; DOI=10.1038/sj.cdd.4401593;
Soleymanlou N., Wu Y., Wang J.X., Todros T., Ietta F., Jurisicova A.,
Post M., Caniggia I.;
"A novel Mtd splice isoform is responsible for trophoblast cell death in
pre-eclampsia.";
Cell Death Differ. 12:441-452(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
TISSUE SPECIFICITY.
PubMed=9535847; DOI=10.1074/jbc.273.15.8705;
Inohara N., Ekhterae D., Garcia I., Carrio R., Merino J., Merry A.,
Chen S., Nunez G.;
"Mtd, a novel Bcl-2 family member activates apoptosis in the absence of
heterodimerization with Bcl-2 and Bcl-XL.";
J. Biol. Chem. 273:8705-8710(1998).
[6]
SUBCELLULAR LOCATION, FUNCTION, AND INDUCTION.
PubMed=15102863; DOI=10.1074/jbc.m313526200;
Yakovlev A.G., Di Giovanni S., Wang G., Liu W., Stoica B., Faden A.I.;
"BOK and NOXA are essential mediators of p53-dependent apoptosis.";
J. Biol. Chem. 279:28367-28374(2004).
[7]
SUBCELLULAR LOCATION, AND INTERACTION WITH BNIP3.
PubMed=15868100; DOI=10.1007/s00018-005-4543-3;
Gao S., Fu W., Duerrenberger M., De Geyter C., Zhang H.;
"Membrane translocation and oligomerization of hBok are triggered in
response to apoptotic stimuli and Bnip3.";
Cell. Mol. Life Sci. 62:1015-1024(2005).
[8]
SUBCELLULAR LOCATION, MUTAGENESIS OF 71-LEU--LEU-73, REGION, AND
INTERACTION WITH XPO1.
PubMed=16302269; DOI=10.1002/mc.20156;
Bartholomeusz G., Wu Y., Ali Seyed M., Xia W., Kwong K.Y., Hortobagyi G.,
Hung M.C.;
"Nuclear translocation of the pro-apoptotic Bcl-2 family member Bok induces
apoptosis.";
Mol. Carcinog. 45:73-83(2006).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[10]
DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=19942931; DOI=10.1038/cdd.2009.167;
Ray J.E., Garcia J., Jurisicova A., Caniggia I.;
"Mtd/Bok takes a swing: proapoptotic Mtd/Bok regulates trophoblast cell
proliferation during human placental development and in preeclampsia.";
Cell Death Differ. 17:846-859(2010).
[11]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=20673843; DOI=10.1016/j.mce.2010.07.020;
Jaeaeskelaeinen M., Nieminen A., Poekkylae R.M., Kauppinen M., Liakka A.,
Heikinheimo M., Vaskivuo T.E., Klefstroem J., Tapanainen J.S.;
"Regulation of cell death in human fetal and adult ovaries--role of Bok and
Bcl-X(L).";
Mol. Cell. Endocrinol. 330:17-24(2010).
[12]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=24113155; DOI=10.4161/auto.26452;
Kalkat M., Garcia J., Ebrahimi J., Melland-Smith M., Todros T., Post M.,
Caniggia I.;
"Placental autophagy regulation by the BOK-MCL1 rheostat.";
Autophagy 9:2140-2153(2013).
[13]
INTERACTION WITH ITPR1.
PubMed=23884412; DOI=10.1074/jbc.m113.496570;
Schulman J.J., Wright F.A., Kaufmann T., Wojcikiewicz R.J.;
"The Bcl-2 protein family member Bok binds to the coupling domain of
inositol 1,4,5-trisphosphate receptors and protects them from proteolytic
cleavage.";
J. Biol. Chem. 288:25340-25349(2013).
[14]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=27076518; DOI=10.1242/jcs.181727;
Einsele-Scholz S., Malmsheimer S., Bertram K., Stehle D., Johaenning J.,
Manz M., Daniel P.T., Gillissen B.F., Schulze-Osthoff K., Essmann F.;
"Bok is a genuine multi-BH-domain protein that triggers apoptosis in the
absence of Bax and Bak.";
J. Cell Sci. 129:2213-2223(2016).
-!- FUNCTION: [Isoform 1]: Apoptosis regulator that functions through
different apoptotic signaling pathways (PubMed:27076518,
PubMed:15102863, PubMed:20673843). 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:27076518, PubMed:15102863). 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}.
-!- SUBUNIT: Monomer; positively regulates apoptotic process. Homodimer (By
similarity). Heterodimer (By similarity). Oligomer; promoted by
apoptotic stimuli and BH3-only proteins; mediates constitutive
activation (PubMed:15868100). Interacts (via BH4 domain) with ITPR1;
enhances BOK expression and stabilization; limits apoptosis and
prevents ubiquitination and then degradation; protects ITPR1 from
proteolysis by CASP3 during apoptosis (PubMed:23884412). Interacts with
ITPR2 AND ITPR3; binds most strongly to ITPR2, and barely to ITPR3;
regulates their expression (By similarity). Interacts with XPO1;
translocates to the cytoplasm (PubMed:16302269). Interacts with BNIP3;
promotes oligomerization (PubMed:15868100).
{ECO:0000250|UniProtKB:O35425, ECO:0000250|UniProtKB:Q792S6,
ECO:0000269|PubMed:15868100, ECO:0000269|PubMed:16302269,
ECO:0000269|PubMed:23884412}.
-!- INTERACTION:
Q9UMX3; Q86V38: ATN1; NbExp=3; IntAct=EBI-7105206, EBI-11954292;
Q9UMX3; P13637: ATP1A3; NbExp=3; IntAct=EBI-7105206, EBI-948169;
Q9UMX3; P50570-2: DNM2; NbExp=3; IntAct=EBI-7105206, EBI-10968534;
Q9UMX3; Q8TB36: GDAP1; NbExp=3; IntAct=EBI-7105206, EBI-11110431;
Q9UMX3; P10809: HSPD1; NbExp=3; IntAct=EBI-7105206, EBI-352528;
Q9UMX3; P16284: PECAM1; NbExp=3; IntAct=EBI-7105206, EBI-716404;
-!- 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}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Mtd-L {ECO:0000303|PubMed:15775999};
IsoId=Q9UMX3-1; Sequence=Displayed;
Name=2; Synonyms=Mtd-P {ECO:0000303|PubMed:15775999};
IsoId=Q9UMX3-2; Sequence=VSP_058599;
-!- TISSUE SPECIFICITY: Expressed mainly in oocytes; weak expression in
granulosa cells of the developing follicles. In adult human ovaries,
expressed in granulosa cells at all follicular stages, but expression
in primordial/primary follicles granulosa cell is stronger than in
secondary and antral follicles. {ECO:0000269|PubMed:20673843}.
-!- DEVELOPMENTAL STAGE: Isoform 1: at 5-7 weeks of gestation, detected
primarily in the cytotrophoblast layer. By 10-13 weeks, expression
becomes restricted primarily to the apical border of the
syncytiotrophoblast (PubMed:19942931). Isoform 2: expression
significantly increased around 6-8 weeks (PubMed:15775999).
{ECO:0000269|PubMed:15775999, ECO:0000269|PubMed:19942931}.
-!- INDUCTION: Up-regulated by DNA damage. {ECO:0000269|PubMed:15102863}.
-!- DOMAIN: BH4 domain mediates interaction with ITPR1.
{ECO:0000250|UniProtKB:O35425}.
-!- 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}.
-!- SIMILARITY: Belongs to the Bcl-2 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
Haematology;
URL="http://atlasgeneticsoncology.org/Genes/BOKID824ch2q37.html";
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EMBL; AF174487; AAD51719.1; -; mRNA.
EMBL; BT007272; AAP35936.1; -; mRNA.
EMBL; BC006203; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS2550.1; -. [Q9UMX3-1]
RefSeq; NP_115904.1; NM_032515.4. [Q9UMX3-1]
RefSeq; XP_011509998.1; XM_011511696.2. [Q9UMX3-1]
PDB; 6CKV; NMR; -; A=21-177.
PDBsum; 6CKV; -.
BMRB; Q9UMX3; -.
SMR; Q9UMX3; -.
BioGRID; 107134; 7.
IntAct; Q9UMX3; 8.
STRING; 9606.ENSP00000314132; -.
TCDB; 1.A.21.1.7; the bcl-2 (bcl-2) family.
iPTMnet; Q9UMX3; -.
PhosphoSitePlus; Q9UMX3; -.
BioMuta; BOK; -.
DMDM; 57012554; -.
EPD; Q9UMX3; -.
jPOST; Q9UMX3; -.
MassIVE; Q9UMX3; -.
PaxDb; Q9UMX3; -.
PeptideAtlas; Q9UMX3; -.
PRIDE; Q9UMX3; -.
ProteomicsDB; 85221; -.
Antibodypedia; 20324; 278 antibodies.
DNASU; 666; -.
Ensembl; ENST00000318407; ENSP00000314132; ENSG00000176720. [Q9UMX3-1]
GeneID; 666; -.
KEGG; hsa:666; -.
UCSC; uc002wbq.4; human. [Q9UMX3-1]
CTD; 666; -.
DisGeNET; 666; -.
GeneCards; BOK; -.
HGNC; HGNC:1087; BOK.
HPA; ENSG00000176720; Tissue enhanced (adipose tissue, brain).
MIM; 605404; gene.
neXtProt; NX_Q9UMX3; -.
OpenTargets; ENSG00000176720; -.
PharmGKB; PA25396; -.
VEuPathDB; HostDB:ENSG00000176720; -.
eggNOG; KOG4728; Eukaryota.
GeneTree; ENSGT01020000230347; -.
HOGENOM; CLU_114994_0_0_1; -.
InParanoid; Q9UMX3; -.
OMA; MVHAIVD; -.
PhylomeDB; Q9UMX3; -.
TreeFam; TF315834; -.
PathwayCommons; Q9UMX3; -.
BioGRID-ORCS; 666; 4 hits in 1012 CRISPR screens.
ChiTaRS; BOK; human.
GeneWiki; BOK_(gene); -.
GenomeRNAi; 666; -.
Pharos; Q9UMX3; Tbio.
PRO; PR:Q9UMX3; -.
Proteomes; UP000005640; Chromosome 2.
RNAct; Q9UMX3; protein.
Bgee; ENSG00000176720; Expressed in C1 segment of cervical spinal cord and 208 other tissues.
ExpressionAtlas; Q9UMX3; baseline and differential.
Genevisible; Q9UMX3; HS.
GO; GO:0033106; C:cis-Golgi network membrane; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
GO; GO:0031966; C:mitochondrial membrane; IDA:UniProtKB.
GO; GO:0005741; C:mitochondrial outer membrane; IBA:GO_Central.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0005640; C:nuclear outer membrane; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB.
GO; GO:0032588; C:trans-Golgi network membrane; ISS:UniProtKB.
GO; GO:0051400; F:BH domain binding; IEA:Ensembl.
GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB.
GO; GO:0008635; P:activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c; ISS:UniProtKB.
GO; GO:0006915; P:apoptotic process; IDA:UniProtKB.
GO; GO:0007420; P:brain development; IEA:Ensembl.
GO; GO:0006921; P:cellular component disassembly involved in execution phase of apoptosis; ISS:UniProtKB.
GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IBA:GO_Central.
GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; IMP:UniProtKB.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IBA:GO_Central.
GO; GO:0008584; P:male gonad development; IEA:Ensembl.
GO; GO:0051902; P:negative regulation of mitochondrial depolarization; IEA:Ensembl.
GO; GO:1901029; P:negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0060546; P:negative regulation of necroptotic process; IEA:Ensembl.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
GO; GO:0048709; P:oligodendrocyte differentiation; IEA:Ensembl.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
GO; GO:1902237; P:positive regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; ISS:UniProtKB.
GO; GO:1900119; P:positive regulation of execution phase of apoptosis; IMP:UniProtKB.
GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; ISS:UniProtKB.
GO; GO:1901030; P:positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; ISS:UniProtKB.
GO; GO:1903899; P:positive regulation of PERK-mediated unfolded protein response; ISS:UniProtKB.
GO; GO:0051259; P:protein complex oligomerization; ISS:UniProtKB.
GO; GO:0010506; P:regulation of autophagy; IMP:UniProtKB.
GO; GO:1901382; P:regulation of chorionic trophoblast cell proliferation; IDA:UniProtKB.
GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IEA:Ensembl.
GO; GO:1904708; P:regulation of granulosa cell apoptotic process; IMP:UniProtKB.
GO; GO:0001836; P:release of cytochrome c from mitochondria; IDA:UniProtKB.
CDD; cd06845; Bcl-2_like; 1.
Gene3D; 1.10.437.10; -; 1.
InterPro; IPR036834; Bcl-2-like_sf.
InterPro; IPR026298; Bcl-2_fam.
InterPro; IPR002475; Bcl2-like.
InterPro; IPR026309; BOK.
PANTHER; PTHR11256; PTHR11256; 1.
PANTHER; PTHR11256:SF48; PTHR11256:SF48; 1.
Pfam; PF00452; Bcl-2; 1.
PRINTS; PR01862; BCL2FAMILY.
SMART; SM00337; BCL; 1.
SUPFAM; SSF56854; SSF56854; 1.
PROSITE; PS50062; BCL2_FAMILY; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Apoptosis; Cytoplasm;
Endoplasmic reticulum; Endosome; Golgi apparatus; Isopeptide bond;
Membrane; Mitochondrion; Mitochondrion inner membrane;
Mitochondrion outer membrane; Nucleus; Phosphoprotein; Reference proteome;
Transmembrane; Transmembrane helix; Ubl conjugation.
CHAIN 1..212
/note="Bcl-2-related ovarian killer protein"
/id="PRO_0000143086"
TRANSMEM 189..209
/note="Helical"
/evidence="ECO:0000255"
REGION 15..45
/note="Interactions with ITPR1"
/evidence="ECO:0000250|UniProtKB:O35425"
REGION 70..78
/note="Nuclear export signal"
/evidence="ECO:0000269|PubMed:16302269"
MOTIF 32..44
/note="BH4"
MOTIF 66..82
/note="BH3"
MOTIF 112..131
/note="BH1"
MOTIF 164..178
/note="BH2"
MOD_RES 7
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:O35425"
CROSSLNK 25
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000250|UniProtKB:O35425"
CROSSLNK 32
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000250|UniProtKB:O35425"
CROSSLNK 159
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000250|UniProtKB:O35425"
CROSSLNK 176
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000250|UniProtKB:O35425"
VAR_SEQ 1..78
/note="Missing (in isoform 2)"
/id="VSP_058599"
MUTAGEN 71..73
/note="LRL->AAA: Significantly accumulates in the nucleus.
Increases apoptotic activity. Does not interact with XPO1."
/evidence="ECO:0000269|PubMed:16302269"
HELIX 24..46
/evidence="ECO:0007829|PDB:6CKV"
HELIX 61..80
/evidence="ECO:0007829|PDB:6CKV"
TURN 85..87
/evidence="ECO:0007829|PDB:6CKV"
HELIX 88..91
/evidence="ECO:0007829|PDB:6CKV"
HELIX 100..115
/evidence="ECO:0007829|PDB:6CKV"
HELIX 120..139
/evidence="ECO:0007829|PDB:6CKV"
HELIX 144..159
/evidence="ECO:0007829|PDB:6CKV"
HELIX 162..168
/evidence="ECO:0007829|PDB:6CKV"
HELIX 171..176
/evidence="ECO:0007829|PDB:6CKV"
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


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BOLA2 BOK Gene BCL2-related ovarian killer
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Pathways :
WP1438: Influenza A virus infection
WP2199: Seed Development
WP2272: Pathogenic Escherichia coli infection
WP731: Sterol regulatory element binding protein related
WP1700: Selenoamino acid metabolism
WP1657: Glycerolipid metabolism
WP210: Cytoplasmic Ribosomal Proteins
WP1663: Homologous recombination
WP1673: Naphthalene and anthracene degradation
WP73: G Protein Signaling Pathways
WP1531: Vitamin D synthesis
WP232: G Protein Signaling Pathways
WP1613: 1,4-Dichlorobenzene degradation
WP1909: Signal regulatory protein (SIRP) family interactions
WP1678: Nucleotide excision repair
WP1690: Propanoate metabolism
WP1625: Base excision repair
WP813: G Protein Signaling Pathways
WP1654: gamma-Hexachlorocyclohexane degradation
WP525: Mitochondrial Unfolded-Protein Response
WP1694: Pyrimidine metabolism
WP1493: Carbon assimilation C4 pathway
WP1714: Tyrosine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1672: Mismatch repair

Related Genes :
[BOK BCL2L9] Bcl-2-related ovarian killer protein (hBOK) (Bcl-2-like protein 9) (Bcl2-L-9)
[Bok Mtd] Bcl-2-related ovarian killer protein (Apoptosis activator Mtd) (Protein matador)
[Bcl2l11 Bim Bod] Bcl-2-like protein 11 (Bcl2-L-11) (Bcl-2-related ovarian death protein) (Bcl2-interacting mediator of cell death)
[Bok] Bcl-2-related ovarian killer protein
[BAK1 BAK BCL2L7 CDN1] Bcl-2 homologous antagonist/killer (Apoptosis regulator BAK) (Bcl-2-like protein 7) (Bcl2-L-7)
[Bcl2l1 Bcl2l Bclx] Bcl-2-like protein 1 (Bcl2-L-1) (Apoptosis regulator Bcl-X)
[MCL1 BCL2L3] Induced myeloid leukemia cell differentiation protein Mcl-1 (Bcl-2-like protein 3) (Bcl2-L-3) (Bcl-2-related protein EAT/mcl1) (mcl1/EAT)
[BCL2A1 BCL2L5 BFL1 GRS HBPA1] Bcl-2-related protein A1 (Bcl-2-like protein 5) (Bcl2-L-5) (Hemopoietic-specific early response protein) (Protein BFL-1) (Protein GRS)
[BCL2L1 BCL2L BCLX] Bcl-2-like protein 1 (Bcl2-L-1) (Apoptosis regulator Bcl-X)
[BCL2L11 BIM] Bcl-2-like protein 11 (Bcl2-L-11) (Bcl2-interacting mediator of cell death)
[BAD BBC6 BCL2L8] Bcl2-associated agonist of cell death (BAD) (Bcl-2-binding component 6) (Bcl-2-like protein 8) (Bcl2-L-8) (Bcl-xL/Bcl-2-associated death promoter) (Bcl2 antagonist of cell death)
[BAX BCL2L4] Apoptosis regulator BAX (Bcl-2-like protein 4) (Bcl2-L-4)
[Bcl2l1 Bclx Blc2l] Bcl-2-like protein 1 (Bcl2-L-1) (Apoptosis regulator Bcl-X)
[BCL2] Apoptosis regulator Bcl-2
[Mcl1] Induced myeloid leukemia cell differentiation protein Mcl-1 homolog (Bcl-2-related protein EAT/mcl1)
[BCL2L2 BCLW KIAA0271] Bcl-2-like protein 2 (Bcl2-L-2) (Apoptosis regulator Bcl-W)
[Bak1 Bak] Bcl-2 homologous antagonist/killer (Apoptosis regulator BAK)
[BCL2] Apoptosis regulator Bcl-2
[Bcl2l11 Bim] Bcl-2-like protein 11 (Bcl2-L-11) (Bcl2-interacting mediator of cell death)
[Bcl2 Bcl-2] Apoptosis regulator Bcl-2
[Bcl2 Bcl-2] Apoptosis regulator Bcl-2
[BCL2L10 BCLB] Bcl-2-like protein 10 (Bcl2-L-10) (Anti-apoptotic protein NrH) (Apoptosis regulator Bcl-B)
[BCL2 BCL-2] Apoptosis regulator Bcl-2
[BCL2L13 MIL1 CD003] Bcl-2-like protein 13 (Bcl2-L-13) (Bcl-rambo) (Protein Mil1)
[BIK NBK] Bcl-2-interacting killer (Apoptosis inducer NBK) (BIP1) (BP4)
[BNIP3L BNIP3A BNIP3H NIX] BCL2/adenovirus E1B 19 kDa protein-interacting protein 3-like (Adenovirus E1B19K-binding protein B5) (BCL2/adenovirus E1B 19 kDa protein-interacting protein 3A) (NIP3-like protein X) (NIP3L)
[BAG3 BIS] BAG family molecular chaperone regulator 3 (BAG-3) (Bcl-2-associated athanogene 3) (Bcl-2-binding protein Bis) (Docking protein CAIR-1)
[Bak1 Bak rCG_60911] BAK protein (BCL2-antagonist/killer 1) (BCL2-antagonist/killer 1, isoform CRA_b) (Bak1 protein)
[Bad Bbc6] Bcl2-associated agonist of cell death (BAD) (Bcl-2-binding component 6) (Bcl-xL/Bcl-2-associated death promoter) (Bcl2 antagonist of cell death)
[Bad] Bcl2-associated agonist of cell death (BAD) (Bcl-2-binding component 6) (Bcl-xL/Bcl-2-associated death promoter) (Bcl2 antagonist of cell death)

Bibliography :