Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

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)

 BNI3L_HUMAN             Reviewed;         219 AA.
O60238; B0AZS9; Q5JW63; Q8NF87;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
01-AUG-1998, sequence version 1.
25-OCT-2017, entry version 164.
RecName: Full=BCL2/adenovirus E1B 19 kDa protein-interacting protein 3-like;
AltName: Full=Adenovirus E1B19K-binding protein B5;
AltName: Full=BCL2/adenovirus E1B 19 kDa protein-interacting protein 3A;
AltName: Full=NIP3-like protein X;
Short=NIP3L;
Name=BNIP3L; Synonyms=BNIP3A, BNIP3H, NIX;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9523198;
DOI=10.1002/(SICI)1098-2264(199803)21:3<230::AID-GCC7>3.3.CO;2-G;
Matsushima M., Fujiwara T., Takahashi E., Minaguchi T., Eguchi Y.,
Tsujimoto Y., Suzumori K., Nakamura Y.;
"Isolation, mapping, and functional analysis of a novel human cDNA
(BNIP3L) encoding a protein homologous to human NIP3.";
Genes Chromosomes Cancer 21:230-235(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Yasuda M., Han J.-W., Dionne C.A., Boyd J.M., Chinnadurai G.;
"BNIP3a, a human homolog of pro-apoptotic protein BNIP3, promotes
apoptosis and interacts with viral and cellular anti-apoptosis
proteins.";
Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Fetal liver;
PubMed=9867803; DOI=10.1074/jbc.274.1.7;
Chen G., Cizeau J., Vande Velde C., Park J.H., Bozek G., Bolton J.,
Shi L., Dubik D., Greenberg A.;
"Nix and Nip3 form a subfamily of pro-apoptotic mitochondrial
proteins.";
J. Biol. Chem. 274:7-10(1999).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
LOCATION, SELF-ASSOCIATION, AND INTERACTION WITH BNIP3 AND HUMAN
ADENOVIRUS-2 E1B 19 KDA PROTEIN.
PubMed=10381623; DOI=10.1038/sj.cdd.4400493;
Ohi N., Tokunaga A., Tsunoda H., Nakano K., Haraguchi K., Oda K.,
Motoyama N., Nakajima T.;
"A novel adenovirus E1B19K-binding protein B5 inhibits apoptosis
induced by Nip3 by forming a heterodimer through the C-terminal
hydrophobic region.";
Cell Death Differ. 6:314-325(1999).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=12663450; DOI=10.1182/blood-2002-11-3324;
Aerbajinai W., Giattina M., Lee Y.T., Raffeld M., Miller J.L.;
"The proapoptotic factor Nix is coexpressed with Bcl-xL during
terminal erythroid differentiation.";
Blood 102:712-717(2003).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Hair follicle dermal papilla;
Farooq M., Kim M.K., Kim Y.H., Seo J.M., Lee H.M., Sohn M.Y.,
Hwang S.Y., Chung H.J., Im S.U., Jung E.J., Kim J.C.;
"A catalog of genes in the human dermal papilla cells as identified by
expressed sequence tags.";
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Kidney;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16421571; DOI=10.1038/nature04406;
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
Lander E.S.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(2006).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Bone marrow, and Cervix;
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).
[12]
INTERACTION WITH STEAP3.
PubMed=12606722; DOI=10.1073/pnas.0530298100;
Passer B.J., Nancy-Portebois V., Amzallag N., Prieur S., Cans C.,
Roborel de Climens A., Fiucci G., Bouvard V., Tuynder M., Susini L.,
Morchoisne S., Crible V., Lespagnol A., Dausset J., Oren M., Amson R.,
Telerman A.;
"The p53-inducible TSAP6 gene product regulates apoptosis and the cell
cycle and interacts with Nix and the Myt1 kinase.";
Proc. Natl. Acad. Sci. U.S.A. 100:2284-2289(2003).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[15]
FUNCTION, INTERACTION WITH SPATA18, AND SUBCELLULAR LOCATION.
PubMed=21264228; DOI=10.1371/journal.pone.0016060;
Kitamura N., Nakamura Y., Miyamoto Y., Miyamoto T., Kabu K.,
Yoshida M., Futamura M., Ichinose S., Arakawa H.;
"Mieap, a p53-inducible protein, controls mitochondrial quality by
repairing or eliminating unhealthy mitochondria.";
PLoS ONE 6:E16060-E16060(2011).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62; SER-118 AND SER-120,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- FUNCTION: Induces apoptosis. Interacts with viral and cellular
anti-apoptosis proteins. Can overcome the suppressors BCL-2 and
BCL-XL, although high levels of BCL-XL expression will inhibit
apoptosis. Inhibits apoptosis induced by BNIP3. Involved in
mitochondrial quality control via its interaction with
SPATA18/MIEAP: in response to mitochondrial damage, participates
in mitochondrial protein catabolic process (also named MALM)
leading to the degradation of damaged proteins inside
mitochondria. The physical interaction of SPATA18/MIEAP, BNIP3 and
BNIP3L/NIX at the mitochondrial outer membrane regulates the
opening of a pore in the mitochondrial double membrane in order to
mediate the translocation of lysosomal proteins from the cytoplasm
to the mitochondrial matrix. May function as a tumor suppressor.
{ECO:0000269|PubMed:10381623, ECO:0000269|PubMed:21264228}.
-!- SUBUNIT: Self-associates. Interacts with BNIP3 and STEAP3.
Interacts with human adenovirus-2 E1B 19 kDa protein. Interacts
(via BH3 domain) with SPATA18 (via coiled-coil domains).
{ECO:0000269|PubMed:10381623, ECO:0000269|PubMed:12606722,
ECO:0000269|PubMed:21264228}.
-!- INTERACTION:
Self; NbExp=11; IntAct=EBI-849893, EBI-849893;
Q15848:ADIPOQ; NbExp=3; IntAct=EBI-849893, EBI-10827839;
Q9NQ11:ATP13A2; NbExp=2; IntAct=EBI-849893, EBI-6308763;
Q92934:BAD; NbExp=2; IntAct=EBI-849893, EBI-700771;
P10415:BCL2; NbExp=2; IntAct=EBI-849893, EBI-77694;
Q12983:BNIP3; NbExp=21; IntAct=EBI-849893, EBI-749464;
Q9BXN2:CLEC7A; NbExp=6; IntAct=EBI-849893, EBI-3939278;
Q9BXN2-6:CLEC7A; NbExp=4; IntAct=EBI-849893, EBI-11989440;
P03247:E1B (xeno); NbExp=7; IntAct=EBI-849893, EBI-849856;
Q969F0:FATE1; NbExp=3; IntAct=EBI-849893, EBI-743099;
P60520:GABARAPL2; NbExp=4; IntAct=EBI-849893, EBI-720116;
Q5T700:LDLRAD1; NbExp=3; IntAct=EBI-849893, EBI-10173166;
P22736-1:NR4A1; NbExp=4; IntAct=EBI-849893, EBI-16085263;
Q9NRQ5:SMCO4; NbExp=6; IntAct=EBI-849893, EBI-8640191;
P17152:TMEM11; NbExp=10; IntAct=EBI-849893, EBI-723946;
-!- SUBCELLULAR LOCATION: Nucleus envelope. Endoplasmic reticulum.
Mitochondrion outer membrane. Membrane {ECO:0000305}; Single-pass
membrane protein {ECO:0000305}. Note=Colocalizes with SPATA18 at
the mitochondrion outer membrane.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O60238-1; Sequence=Displayed;
Name=2;
IsoId=O60238-2; Sequence=VSP_056248;
Note=No experimental confirmation available.;
-!- PTM: Undergoes progressive proteolysis to an 11 kDa C-terminal
fragment, which is blocked by the proteasome inhibitor
lactacystin.
-!- SIMILARITY: Belongs to the NIP3 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAI46217.1; Type=Erroneous termination; Positions=122; Note=Translated as Glu.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/BNIP3LID823ch8p21.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AB004788; BAA28692.1; -; mRNA.
EMBL; AF079221; AAC27723.1; -; mRNA.
EMBL; AF067396; AAD03589.1; -; mRNA.
EMBL; AF536326; AAN04051.1; -; mRNA.
EMBL; AF452712; AAL50978.1; -; mRNA.
EMBL; AF255051; AAF70290.1; -; Genomic_DNA.
EMBL; AK315870; BAF98761.1; -; mRNA.
EMBL; AK316315; BAH14686.1; -; mRNA.
EMBL; BT019501; AAV38308.1; -; mRNA.
EMBL; AL132665; CAI46217.1; ALT_SEQ; mRNA.
EMBL; AC011726; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC015743; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC022911; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC001559; AAH01559.1; -; mRNA.
EMBL; BC009603; AAH09603.1; -; mRNA.
CCDS; CCDS6050.1; -. [O60238-1]
CCDS; CCDS83267.1; -. [O60238-2]
PIR; T34523; T34523.
RefSeq; NP_001317420.1; NM_001330491.1. [O60238-2]
RefSeq; NP_004322.1; NM_004331.2. [O60238-1]
UniGene; Hs.131226; -.
ProteinModelPortal; O60238; -.
SMR; O60238; -.
BioGrid; 107133; 33.
DIP; DIP-35187N; -.
IntAct; O60238; 39.
MINT; MINT-1429960; -.
STRING; 9606.ENSP00000370003; -.
TCDB; 1.A.20.1.2; the bcl2/adenovirus e1b-interacting protein 3 (bnip3) family.
iPTMnet; O60238; -.
PhosphoSitePlus; O60238; -.
BioMuta; BNIP3L; -.
EPD; O60238; -.
PaxDb; O60238; -.
PeptideAtlas; O60238; -.
PRIDE; O60238; -.
DNASU; 665; -.
Ensembl; ENST00000380629; ENSP00000370003; ENSG00000104765. [O60238-1]
Ensembl; ENST00000518611; ENSP00000429851; ENSG00000104765. [O60238-2]
Ensembl; ENST00000520409; ENSP00000428597; ENSG00000104765. [O60238-2]
Ensembl; ENST00000523515; ENSP00000429698; ENSG00000104765. [O60238-2]
GeneID; 665; -.
KEGG; hsa:665; -.
UCSC; uc003xey.3; human. [O60238-1]
CTD; 665; -.
DisGeNET; 665; -.
EuPathDB; HostDB:ENSG00000104765.14; -.
GeneCards; BNIP3L; -.
HGNC; HGNC:1085; BNIP3L.
HPA; CAB025371; -.
HPA; HPA015652; -.
MIM; 605368; gene.
neXtProt; NX_O60238; -.
OpenTargets; ENSG00000104765; -.
PharmGKB; PA25395; -.
eggNOG; ENOG410IK24; Eukaryota.
eggNOG; ENOG4111HIM; LUCA.
GeneTree; ENSGT00390000013415; -.
HOGENOM; HOG000232139; -.
HOVERGEN; HBG050707; -.
InParanoid; O60238; -.
KO; K15465; -.
OMA; PQDDGQI; -.
PhylomeDB; O60238; -.
TreeFam; TF315424; -.
Reactome; R-HSA-6803204; TP53 Regulates Transcription of Genes Involved in Cytochrome C Release.
ChiTaRS; BNIP3L; human.
GeneWiki; BNIP3L; -.
GenomeRNAi; 665; -.
PRO; PR:O60238; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000104765; -.
CleanEx; HS_BNIP3L; -.
ExpressionAtlas; O60238; baseline and differential.
Genevisible; O60238; HS.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0031224; C:intrinsic component of membrane; TAS:UniProtKB.
GO; GO:0005741; C:mitochondrial outer membrane; IMP:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
GO; GO:0016607; C:nuclear speck; IDA:HPA.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0005521; F:lamin binding; IDA:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0071456; P:cellular response to hypoxia; IGI:MGI.
GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
GO; GO:0097345; P:mitochondrial outer membrane permeabilization; IBA:GO_Central.
GO; GO:0035694; P:mitochondrial protein catabolic process; IMP:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0060548; P:negative regulation of cell death; IGI:MGI.
GO; GO:0010917; P:negative regulation of mitochondrial membrane potential; IEA:Ensembl.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0016239; P:positive regulation of macroautophagy; IGI:MGI.
GO; GO:0042981; P:regulation of apoptotic process; TAS:Reactome.
GO; GO:1903146; P:regulation of autophagy of mitochondrion; IEA:Ensembl.
GO; GO:1903214; P:regulation of protein targeting to mitochondrion; IEA:Ensembl.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
InterPro; IPR010548; BNIP3.
PANTHER; PTHR15186; PTHR15186; 1.
Pfam; PF06553; BNIP3; 1.
1: Evidence at protein level;
Alternative splicing; Apoptosis; Complete proteome;
Endoplasmic reticulum; Host-virus interaction; Membrane;
Mitochondrion; Mitochondrion outer membrane; Nucleus; Phosphoprotein;
Reference proteome; Transmembrane; Transmembrane helix.
CHAIN 1 219 BCL2/adenovirus E1B 19 kDa protein-
interacting protein 3-like.
/FTId=PRO_0000064957.
TRANSMEM 188 208 Helical. {ECO:0000255}.
MOTIF 126 148 BH3.
MOD_RES 62 62 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 117 117 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Z2F7}.
MOD_RES 118 118 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 120 120 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 166 166 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
VAR_SEQ 1 40 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056248.
CONFLICT 107 107 D -> E (in Ref. 4; AAN04051).
{ECO:0000305}.
CONFLICT 150 150 N -> S (in Ref. 9; CAI46217).
{ECO:0000305}.
SEQUENCE 219 AA; 23930 MW; 19372E897BC63609 CRC64;
MSSHLVEPPP PLHNNNNNCE ENEQSLPPPA GLNSSWVELP MNSSNGNDNG NGKNGGLEHV
PSSSSIHNGD MEKILLDAQH ESGQSSSRGS SHCDSPSPQE DGQIMFDVEM HTSRDHSSQS
EEEVVEGEKE VEALKKSADW VSDWSSRPEN IPPKEFHFRH PKRSVSLSMR KSGAMKKGGI
FSAEFLKVFI PSLFLSHVLA LGLGIYIGKR LSTPSASTY


Related products :

Catalog number Product name Quantity
CSB-EL002767HU Human BCL2 per adenovirus E1B 19 kDa protein-interacting protein 3-like(BNIP3L) ELISA kit 96T
E1419m Mouse ELISA Kit FOR BCL2 per adenovirus E1B 19 kDa protein-interacting protein 3 96T
CD43 Human BCL2 Adenovirus E1B 19 kDa Protein-Interacting Protein 3 BNIP3 50
CF87 Human BCL2 Adenovirus E1B 19 kDa Protein-Interacting Protein 3 BNIP3 l0
BNI3L_BOVIN ELISA Kit FOR BCL2 per adenovirus E1B 19 kDa protein-interacting protein 3-like; organism: Bovine; gene name: BNIP3L 96T
BNIP3_HUMAN ELISA Kit FOR BCL2 per adenovirus E1B 19 kDa protein-interacting protein 3; organism: Human; gene name: BNIP3 96T
BNI3L_HUMAN ELISA Kit FOR BCL2 per adenovirus E1B 19 kDa protein-interacting protein 3-like; organism: Human; gene name: BNIP3L 96T
BNIP2_HUMAN ELISA Kit FOR BCL2 per adenovirus E1B 19 kDa protein-interacting protein 2; organism: Human; gene name: BNIP2 96T
BNIP3_BOVIN ELISA Kit FOR BCL2 per adenovirus E1B 19 kDa protein-interacting protein 3; organism: Bovine; gene name: BNIP3 96T
CF87 BCL2 Adenovirus E1B 19 kDa Protein-Interacting Protein 3 BNIP3 500
CF87 BCL2 Adenovirus E1B 19 kDa Protein-Interacting Protein 3 BNIP3 lmg
E0826Ra Rat Bcl2 per Adenovirus E1B 19kDa Interacting Protein 3 (BNIP3)ELISA Kit 48T
E0826Ra Rat Bcl2-Adenovirus E1B 19kDa Interacting Protein 3 (BNIP3)ELISA Kit 96T
E0826Ra Rat Bcl2 per Adenovirus E1B 19kDa Interacting Protein 3 (BNIP3)ELISA Kit 96T
UB-E10806 Rat Bcl2 per Adenovirus E1B 19kDa Interacting Protein 3(BNIP3)ELISA Kit 96T
YHB0150Ra Rat Bcl2-Adenovirus E1B 19kDa Interacting Protein 3 (BNIP3)ELISA Kit 48T
YHB0150Ra Rat Bcl2-Adenovirus E1B 19kDa Interacting Protein 3 (BNIP3)ELISA Kit 96T
UT-E05118 Human Bcl2 Adenovirus E1B 19k Da Interacting Protein 3 (BNIP3) ELISA Kit 96T
E12410419 Rat BCL2 per Adenovirus E1B 19kDa Interacting Protein 3 (BNIP3) ELISA Kit 1
E0825Ra Rat Bcl2-Adenovirus E1B 19kDa Interacting Protein 3 (BNIP3)ELISA Kit 48T
E1063Mo Mouse Bcl2-Adenovirus E1B 19kDa Interacting Protein 3 (BNIP3)ELISA Kit 48T
E2458Hu Human Bcl2-Adenovirus E1B 19kDa Interacting Protein 3 (BNIP3)ELISA Kit 96T
UB-E20189 Mouse Bcl2 per Adenovirus E1B 19kDa Interacting Protein 3(BNIP3)ELISA Kit 96T
E1064Mo Mouse Bcl2 per Adenovirus E1B 19kDa Interacting Protein 3 (BNIP3)ELISA Kit 48T
E13750307 Rabbit BCL2 per Adenovirus E1B 19kDa Interacting Protein 3 (BNIP3) ELISA Kit 1


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur