BNI3L_HUMAN
ID BNI3L_HUMAN Reviewed; 219 AA.
AC O60238; B0AZS9; Q5JW63; Q8NF87;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=BCL2/adenovirus E1B 19 kDa protein-interacting protein 3-like;
DE AltName: Full=Adenovirus E1B19K-binding protein B5;
DE AltName: Full=BCL2/adenovirus E1B 19 kDa protein-interacting protein 3A;
DE AltName: Full=NIP3-like protein X;
DE Short=NIP3L;
GN Name=BNIP3L; Synonyms=BNIP3A, BNIP3H, NIX;
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] (ISOFORM 1).
RX PubMed=9523198;
RX DOI=10.1002/(sici)1098-2264(199803)21:3<230::aid-gcc7>3.0.co;2-0;
RA Matsushima M., Fujiwara T., Takahashi E., Minaguchi T., Eguchi Y.,
RA Tsujimoto Y., Suzumori K., Nakamura Y.;
RT "Isolation, mapping, and functional analysis of a novel human cDNA (BNIP3L)
RT encoding a protein homologous to human NIP3.";
RL Genes Chromosomes Cancer 21:230-235(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Yasuda M., Han J.-W., Dionne C.A., Boyd J.M., Chinnadurai G.;
RT "BNIP3a, a human homolog of pro-apoptotic protein BNIP3, promotes apoptosis
RT and interacts with viral and cellular anti-apoptosis proteins.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Fetal liver;
RX PubMed=9867803; DOI=10.1074/jbc.274.1.7;
RA Chen G., Cizeau J., Vande Velde C., Park J.H., Bozek G., Bolton J., Shi L.,
RA Dubik D., Greenberg A.;
RT "Nix and Nip3 form a subfamily of pro-apoptotic mitochondrial proteins.";
RL J. Biol. Chem. 274:7-10(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP SELF-ASSOCIATION, AND INTERACTION WITH BNIP3 AND HUMAN ADENOVIRUS-2 E1B 19
RP KDA PROTEIN (MICROBIAL INFECTION).
RX PubMed=10381623; DOI=10.1038/sj.cdd.4400493;
RA Ohi N., Tokunaga A., Tsunoda H., Nakano K., Haraguchi K., Oda K.,
RA Motoyama N., Nakajima T.;
RT "A novel adenovirus E1B19K-binding protein B5 inhibits apoptosis induced by
RT Nip3 by forming a heterodimer through the C-terminal hydrophobic region.";
RL Cell Death Differ. 6:314-325(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=12663450; DOI=10.1182/blood-2002-11-3324;
RA Aerbajinai W., Giattina M., Lee Y.T., Raffeld M., Miller J.L.;
RT "The proapoptotic factor Nix is coexpressed with Bcl-xL during terminal
RT erythroid differentiation.";
RL Blood 102:712-717(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Hair follicle dermal papilla;
RA Farooq M., Kim M.K., Kim Y.H., Seo J.M., Lee H.M., Sohn M.Y., Hwang S.Y.,
RA Chung H.J., Im S.U., Jung E.J., Kim J.C.;
RT "A catalog of genes in the human dermal papilla cells as identified by
RT expressed sequence tags.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow, and Cervix;
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 [12]
RP INTERACTION WITH STEAP3.
RX PubMed=12606722; DOI=10.1073/pnas.0530298100;
RA Passer B.J., Nancy-Portebois V., Amzallag N., Prieur S., Cans C.,
RA Roborel de Climens A., Fiucci G., Bouvard V., Tuynder M., Susini L.,
RA Morchoisne S., Crible V., Lespagnol A., Dausset J., Oren M., Amson R.,
RA Telerman A.;
RT "The p53-inducible TSAP6 gene product regulates apoptosis and the cell
RT cycle and interacts with Nix and the Myt1 kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:2284-2289(2003).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP FUNCTION, INTERACTION WITH SPATA18, AND SUBCELLULAR LOCATION.
RX PubMed=21264228; DOI=10.1371/journal.pone.0016060;
RA Kitamura N., Nakamura Y., Miyamoto Y., Miyamoto T., Kabu K., Yoshida M.,
RA Futamura M., Ichinose S., Arakawa H.;
RT "Mieap, a p53-inducible protein, controls mitochondrial quality by
RT repairing or eliminating unhealthy mitochondria.";
RL PLoS ONE 6:E16060-E16060(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62; SER-118 AND SER-120, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Induces apoptosis. Interacts with viral and cellular anti-
CC apoptosis proteins. Can overcome the suppressors BCL-2 and BCL-XL,
CC although high levels of BCL-XL expression will inhibit apoptosis.
CC Inhibits apoptosis induced by BNIP3. Involved in mitochondrial quality
CC control via its interaction with SPATA18/MIEAP: in response to
CC mitochondrial damage, participates in mitochondrial protein catabolic
CC process (also named MALM) leading to the degradation of damaged
CC proteins inside mitochondria. The physical interaction of
CC SPATA18/MIEAP, BNIP3 and BNIP3L/NIX at the mitochondrial outer membrane
CC regulates the opening of a pore in the mitochondrial double membrane in
CC order to mediate the translocation of lysosomal proteins from the
CC cytoplasm to the mitochondrial matrix. May function as a tumor
CC suppressor. {ECO:0000269|PubMed:10381623, ECO:0000269|PubMed:21264228}.
CC -!- SUBUNIT: Self-associates. Interacts with BNIP3 and STEAP3. Interacts
CC (via BH3 domain) with SPATA18 (via coiled-coil domains).
CC {ECO:0000269|PubMed:10381623, ECO:0000269|PubMed:12606722,
CC ECO:0000269|PubMed:21264228}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human adenovirus-2 E1B 19
CC kDa protein. {ECO:0000269|PubMed:10381623}.
CC -!- INTERACTION:
CC O60238; Q15848: ADIPOQ; NbExp=3; IntAct=EBI-849893, EBI-10827839;
CC O60238; Q9NQ11: ATP13A2; NbExp=2; IntAct=EBI-849893, EBI-6308763;
CC O60238; Q92934: BAD; NbExp=2; IntAct=EBI-849893, EBI-700771;
CC O60238; P10415: BCL2; NbExp=2; IntAct=EBI-849893, EBI-77694;
CC O60238; Q12983: BNIP3; NbExp=22; IntAct=EBI-849893, EBI-749464;
CC O60238; O60238: BNIP3L; NbExp=11; IntAct=EBI-849893, EBI-849893;
CC O60238; Q9BXN2: CLEC7A; NbExp=6; IntAct=EBI-849893, EBI-3939278;
CC O60238; Q9BXN2-6: CLEC7A; NbExp=3; IntAct=EBI-849893, EBI-11989440;
CC O60238; O43169: CYB5B; NbExp=3; IntAct=EBI-849893, EBI-1058710;
CC O60238; Q969F0: FATE1; NbExp=3; IntAct=EBI-849893, EBI-743099;
CC O60238; Q9H0R8: GABARAPL1; NbExp=3; IntAct=EBI-849893, EBI-746969;
CC O60238; P60520: GABARAPL2; NbExp=3; IntAct=EBI-849893, EBI-720116;
CC O60238; Q5T700: LDLRAD1; NbExp=4; IntAct=EBI-849893, EBI-10173166;
CC O60238; Q13021: MALL; NbExp=3; IntAct=EBI-849893, EBI-750078;
CC O60238; Q9H492: MAP1LC3A; NbExp=2; IntAct=EBI-849893, EBI-720768;
CC O60238; P22736-1: NR4A1; NbExp=4; IntAct=EBI-849893, EBI-16085263;
CC O60238; Q9NRQ5: SMCO4; NbExp=7; IntAct=EBI-849893, EBI-8640191;
CC O60238; P17152: TMEM11; NbExp=9; IntAct=EBI-849893, EBI-723946;
CC O60238; A0PK00: TMEM120B; NbExp=3; IntAct=EBI-849893, EBI-10171534;
CC O60238; Q9NRS4: TMPRSS4; NbExp=3; IntAct=EBI-849893, EBI-10313040;
CC O60238; Q9H2S6-2: TNMD; NbExp=3; IntAct=EBI-849893, EBI-12003398;
CC O60238; P03247: E1B; Xeno; NbExp=7; IntAct=EBI-849893, EBI-849856;
CC O60238; A0A663DJA2: ORF10; Xeno; NbExp=4; IntAct=EBI-849893, EBI-25475906;
CC -!- SUBCELLULAR LOCATION: Nucleus envelope. Endoplasmic reticulum.
CC Mitochondrion outer membrane. Membrane {ECO:0000305}; Single-pass
CC membrane protein {ECO:0000305}. Note=Colocalizes with SPATA18 at the
CC mitochondrion outer membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O60238-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O60238-2; Sequence=VSP_056248;
CC -!- PTM: Undergoes progressive proteolysis to an 11 kDa C-terminal
CC fragment, which is blocked by the proteasome inhibitor lactacystin.
CC -!- SIMILARITY: Belongs to the NIP3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI46217.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/BNIP3LID823ch8p21.html";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB004788; BAA28692.1; -; mRNA.
DR EMBL; AF079221; AAC27723.1; -; mRNA.
DR EMBL; AF067396; AAD03589.1; -; mRNA.
DR EMBL; AF536326; AAN04051.1; -; mRNA.
DR EMBL; AF452712; AAL50978.1; -; mRNA.
DR EMBL; AF255051; AAF70290.1; -; Genomic_DNA.
DR EMBL; AK315870; BAF98761.1; -; mRNA.
DR EMBL; AK316315; BAH14686.1; -; mRNA.
DR EMBL; BT019501; AAV38308.1; -; mRNA.
DR EMBL; AL132665; CAI46217.1; ALT_SEQ; mRNA.
DR EMBL; AC011726; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC015743; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC022911; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001559; AAH01559.1; -; mRNA.
DR EMBL; BC009603; AAH09603.1; -; mRNA.
DR CCDS; CCDS6050.1; -. [O60238-1]
DR CCDS; CCDS83267.1; -. [O60238-2]
DR PIR; T34523; T34523.
DR RefSeq; NP_001317420.1; NM_001330491.1. [O60238-2]
DR RefSeq; NP_004322.1; NM_004331.2. [O60238-1]
DR AlphaFoldDB; O60238; -.
DR SMR; O60238; -.
DR BioGRID; 107133; 64.
DR DIP; DIP-35187N; -.
DR IntAct; O60238; 49.
DR MINT; O60238; -.
DR STRING; 9606.ENSP00000370003; -.
DR TCDB; 1.A.20.1.2; the bcl2/adenovirus e1b-interacting protein 3 (bnip3) family.
DR GlyGen; O60238; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O60238; -.
DR PhosphoSitePlus; O60238; -.
DR BioMuta; BNIP3L; -.
DR EPD; O60238; -.
DR jPOST; O60238; -.
DR MassIVE; O60238; -.
DR MaxQB; O60238; -.
DR PaxDb; O60238; -.
DR PeptideAtlas; O60238; -.
DR PRIDE; O60238; -.
DR ProteomicsDB; 2536; -.
DR ProteomicsDB; 49267; -. [O60238-1]
DR Antibodypedia; 2292; 472 antibodies from 43 providers.
DR DNASU; 665; -.
DR Ensembl; ENST00000380629.7; ENSP00000370003.2; ENSG00000104765.16. [O60238-1]
DR Ensembl; ENST00000518611.5; ENSP00000429851.1; ENSG00000104765.16. [O60238-2]
DR Ensembl; ENST00000520409.5; ENSP00000428597.1; ENSG00000104765.16. [O60238-2]
DR Ensembl; ENST00000523515.5; ENSP00000429698.1; ENSG00000104765.16. [O60238-2]
DR GeneID; 665; -.
DR KEGG; hsa:665; -.
DR MANE-Select; ENST00000380629.7; ENSP00000370003.2; NM_004331.3; NP_004322.1.
DR UCSC; uc003xey.3; human. [O60238-1]
DR CTD; 665; -.
DR DisGeNET; 665; -.
DR GeneCards; BNIP3L; -.
DR HGNC; HGNC:1085; BNIP3L.
DR HPA; ENSG00000104765; Low tissue specificity.
DR MIM; 605368; gene.
DR neXtProt; NX_O60238; -.
DR OpenTargets; ENSG00000104765; -.
DR PharmGKB; PA25395; -.
DR VEuPathDB; HostDB:ENSG00000104765; -.
DR eggNOG; ENOG502R8Q5; Eukaryota.
DR GeneTree; ENSGT00390000013415; -.
DR HOGENOM; CLU_091463_1_1_1; -.
DR InParanoid; O60238; -.
DR OMA; LEMNRTH; -.
DR PhylomeDB; O60238; -.
DR TreeFam; TF315424; -.
DR PathwayCommons; O60238; -.
DR Reactome; R-HSA-6803204; TP53 Regulates Transcription of Genes Involved in Cytochrome C Release.
DR SignaLink; O60238; -.
DR SIGNOR; O60238; -.
DR BioGRID-ORCS; 665; 13 hits in 1086 CRISPR screens.
DR ChiTaRS; BNIP3L; human.
DR GeneWiki; BNIP3L; -.
DR GenomeRNAi; 665; -.
DR Pharos; O60238; Tbio.
DR PRO; PR:O60238; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; O60238; protein.
DR Bgee; ENSG00000104765; Expressed in trabecular bone tissue and 208 other tissues.
DR ExpressionAtlas; O60238; baseline and differential.
DR Genevisible; O60238; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031224; C:intrinsic component of membrane; TAS:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; IMP:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005521; F:lamin binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0071456; P:cellular response to hypoxia; IGI:MGI.
DR GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
DR GO; GO:0097345; P:mitochondrial outer membrane permeabilization; IBA:GO_Central.
DR GO; GO:0035694; P:mitochondrial protein catabolic process; IMP:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0060548; P:negative regulation of cell death; IGI:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0016239; P:positive regulation of macroautophagy; IGI:MGI.
DR GO; GO:1903146; P:regulation of autophagy of mitochondrion; IEA:Ensembl.
DR GO; GO:0043067; P:regulation of programmed cell death; IBA:GO_Central.
DR GO; GO:1903214; P:regulation of protein targeting to mitochondrion; IEA:Ensembl.
DR InterPro; IPR010548; BNIP3.
DR PANTHER; PTHR15186; PTHR15186; 1.
DR Pfam; PF06553; BNIP3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; Endoplasmic reticulum;
KW Host-virus interaction; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Nucleus; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..219
FT /note="BCL2/adenovirus E1B 19 kDa protein-interacting
FT protein 3-like"
FT /id="PRO_0000064957"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 126..148
FT /note="BH3"
FT COMPBIAS 9..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2F7"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..40
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056248"
FT CONFLICT 107
FT /note="D -> E (in Ref. 4; AAN04051)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="N -> S (in Ref. 9; CAI46217)"
FT /evidence="ECO:0000305"
SQ 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
