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 28-JAN-2026, entry version 210. 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>3.3.co;2-g; 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). RN [18] RP FUNCTION, AND INTERACTION WITH KAPOSI'S SARCOMA-ASSOCIATED HERPESVIRUS RP PROTEIN VIRF-1 (MICROBIAL INFECTION). RX PubMed=31324791; DOI=10.1038/s41467-019-11164-2; RA Vo M.T., Smith B.J., Nicholas J., Choi Y.B.; RT "Activation of NIX-mediated mitophagy by an interferon regulatory factor RT homologue of human herpesvirus."; RL Nat. Commun. 10:3203-3203(2019). RN [19] RP INTERACTION WITH PPTC7. RX PubMed=38992176; DOI=10.1038/s44319-024-00181-y; RA Nguyen-Dien G.T., Townsend B., Kulkarni P.G., Kozul K.L., Ooi S.S., RA Eldershaw D.N., Weeratunga S., Liu M., Jones M.J., Millard S.S., Ng D.C., RA Pagano M., Bonfim-Melo A., Schneider T., Komander D., Lazarou M., RA Collins B.M., Pagan J.K.; RT "PPTC7 antagonizes mitophagy by promoting BNIP3 and NIX degradation via RT SCFFBXL4."; RL EMBO Rep. 25:3324-3347(2024). 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). Interacts with CC PPTC7; this interaction promotes BNIP3L degradation (PubMed:38992176). CC {ECO:0000269|PubMed:10381623, ECO:0000269|PubMed:12606722, CC ECO:0000269|PubMed:21264228, ECO:0000269|PubMed:38992176}. CC -!- SUBUNIT: (Microbial infection) Interacts with human adenovirus-2 E1B 19 CC kDa protein. {ECO:0000269|PubMed:10381623}. CC -!- SUBUNIT: (Microbial infection) Interacts with Kaposi's sarcoma- CC associated herpesvirus protein VIRF-1. {ECO:0000269|PubMed:31324791}. 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=24; 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; 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; P38182: ATG8; Xeno; NbExp=4; IntAct=EBI-849893, EBI-2684; 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="https://atlasgeneticsoncology.org/gene/823/BNIP3L"; 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_001330491.2. [O60238-2] DR RefSeq; NP_004322.1; NM_004331.3. [O60238-1] DR AlphaFoldDB; O60238; -. DR SMR; O60238; -. DR BioGRID; 107133; 82. DR DIP; DIP-35187N; -. DR FunCoup; O60238; 3163. DR IntAct; O60238; 54. 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 jPOST; O60238; -. DR MassIVE; O60238; -. DR PaxDb; 9606-ENSP00000370003; -. DR PeptideAtlas; O60238; -. DR ProteomicsDB; 2536; -. DR ProteomicsDB; 49267; -. [O60238-1] DR Pumba; O60238; -. DR Antibodypedia; 2292; 466 antibodies from 43 providers. DR DNASU; 665; -. DR Ensembl; ENST00000380629.7; ENSP00000370003.2; ENSG00000104765.17. [O60238-1] DR Ensembl; ENST00000518611.5; ENSP00000429851.1; ENSG00000104765.17. [O60238-2] DR Ensembl; ENST00000520409.5; ENSP00000428597.1; ENSG00000104765.17. [O60238-2] DR Ensembl; ENST00000523515.5; ENSP00000429698.1; ENSG00000104765.17. [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 AGR; HGNC:1085; -. DR ClinPGx; PA25395; -. 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 OpenTargets; ENSG00000104765; -. DR VEuPathDB; HostDB:ENSG00000104765; -. DR eggNOG; ENOG502R8Q5; Eukaryota. DR GeneTree; ENSGT00390000013415; -. DR HOGENOM; CLU_091463_1_1_1; -. DR InParanoid; O60238; -. DR OMA; EAVEDHY; -. DR OrthoDB; 5857140at2759; -. DR PAN-GO; O60238; 7 GO annotations based on evolutionary models. DR PhylomeDB; O60238; -. 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 Agora; ENSG00000104765; -. DR BioGRID-ORCS; 665; 14 hits in 1164 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 210 other cell types or tissues. DR ExpressionAtlas; O60238; baseline and differential. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; TAS:UniProtKB. DR GO; GO:0005741; C:mitochondrial outer membrane; IMP:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IDA:HPA. 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:0010917; P:negative regulation of mitochondrial membrane potential; IEA:Ensembl. DR GO; GO:0043069; P:negative regulation of programmed 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:1901524; P:regulation of mitophagy; 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 Gene3D; 6.10.250.1020; -; 1. DR InterPro; IPR010548; BNIP3. DR PANTHER; PTHR15186:SF3; BCL2_ADENOVIRUS E1B 19 KDA PROTEIN-INTERACTING PROTEIN 3-LIKE; 1. DR PANTHER; PTHR15186; RE48077P; 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; KW Proteomics identification; Reference proteome; Transmembrane; KW 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 42..51 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 69..80 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 82..97 FT /note="Low complexity" 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 //