BNIP3_HUMAN
ID BNIP3_HUMAN Reviewed; 194 AA.
AC Q12983; O14620; Q96GP0;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 25-MAY-2022, sequence version 4.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=BCL2/adenovirus E1B 19 kDa protein-interacting protein 3 {ECO:0000305};
GN Name=BNIP3 {ECO:0000312|HGNC:HGNC:1084}; Synonyms=NIP3;
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], INTERACTION WITH BCL2, AND INTERACTION WITH
RP ADENOVIRUS E1B (MICROBIAL INFECTION).
RC TISSUE=B-cell;
RX PubMed=7954800; DOI=10.1016/0092-8674(94)90202-x;
RA Boyd J.M., Malstrom S., Subramanian T., Venkatesh L.K., Schaeper U.,
RA Elangovan B., D'Sa-Eipper C., Chinnadurai G.;
RT "Adenovirus E1B 19 kDa and Bcl-2 proteins interact with a common set of
RT cellular proteins.";
RL Cell 79:341-351(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=B-cell;
RX PubMed=9396766; DOI=10.1084/jem.186.12.1975;
RA Chen G., Ray R., Dubik D., Shi L., Cizeau J., Bleackley R.C., Saxena S.,
RA Gietz R.D., Greenberg A.H.;
RT "The E1B 19K/Bcl-2-binding protein Nip3 is a dimeric mitochondrial protein
RT that activates apoptosis.";
RL J. Exp. Med. 186:1975-1983(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [6]
RP INTERACTION WITH EPSTEIN-BARR VIRUS PROTEIN BHRF1 (MICROBIAL INFECTION).
RX PubMed=9575197; DOI=10.1074/jbc.273.20.12415;
RA Yasuda M., Theodorakis P., Subramanian T., Chinnadurai G.;
RT "Adenovirus E1B-19K/BCL-2 interacting protein BNIP3 contains a BH3 domain
RT and a mitochondrial targeting sequence.";
RL J. Biol. Chem. 273:12415-12421(1998).
RN [7]
RP INTERACTION WITH BNIP3L.
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 [8]
RP INTERACTION WITH BOK.
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 [9]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH ACAA2.
RX PubMed=18371312; DOI=10.1016/j.bbagen.2008.02.007;
RA Cao W., Liu N., Tang S., Bao L., Shen L., Yuan H., Zhao X., Lu H.;
RT "Acetyl-Coenzyme A acyltransferase 2 attenuates the apoptotic effects of
RT BNIP3 in two human cell lines.";
RL Biochim. Biophys. Acta 1780:873-880(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19935772; DOI=10.1038/cr.2009.129;
RA Ghavami S., Eshragi M., Ande S.R., Chazin W.J., Klonisch T., Halayko A.J.,
RA McNeill K.D., Hashemi M., Kerkhoff C., Los M.;
RT "S100A8/A9 induces autophagy and apoptosis via ROS-mediated cross-talk
RT between mitochondria and lysosomes that involves BNIP3.";
RL Cell Res. 20:314-331(2010).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86, 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 [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP FUNCTION, INTERACTION WITH SPATA18, AND SUBCELLULAR LOCATION.
RX PubMed=22292033; DOI=10.1371/journal.pone.0030767;
RA Nakamura Y., Kitamura N., Shinogi D., Yoshida M., Goda O., Murai R.,
RA Kamino H., Arakawa H.;
RT "BNIP3 and NIX mediate Mieap-induced accumulation of lysosomal proteins
RT within mitochondria.";
RL PLoS ONE 7:E30767-E30767(2012).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; SER-66 AND SER-95, AND
RP IDENTIFICATION BY 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: Apoptosis-inducing protein that can overcome BCL2
CC suppression. May play a role in repartitioning calcium between the two
CC major intracellular calcium stores in association with BCL2. Involved
CC in mitochondrial quality control via its interaction with
CC SPATA18/MIEAP: in response to mitochondrial damage, participates in
CC mitochondrial protein catabolic process (also named MALM) leading to
CC the degradation of damaged proteins inside mitochondria. The physical
CC interaction of SPATA18/MIEAP, BNIP3 and BNIP3L/NIX at the mitochondrial
CC outer membrane regulates the opening of a pore in the mitochondrial
CC double membrane in order to mediate the translocation of lysosomal
CC proteins from the cytoplasm to the mitochondrial matrix. Plays an
CC important role in the calprotectin (S100A8/A9)-induced cell death
CC pathway. {ECO:0000269|PubMed:19935772, ECO:0000269|PubMed:22292033}.
CC -!- SUBUNIT: Homodimer. Binds to BCL2. Interacts with BNIP3L and ACAA2.
CC Interacts (via BH3 domain) with SPATA18 (via coiled-coil domains).
CC Interacts with BOK; promotes BOK oligomerization (PubMed:15868100).
CC {ECO:0000269|PubMed:10381623, ECO:0000269|PubMed:15868100,
CC ECO:0000269|PubMed:18371312, ECO:0000269|PubMed:22292033,
CC ECO:0000269|PubMed:7954800}.
CC -!- SUBUNIT: (Microbial infection) Interacts with adenovirus E1B 19 kDa
CC protein. {ECO:0000269|PubMed:7954800}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Epstein-Barr virus BHRF1.
CC {ECO:0000269|PubMed:9575197}.
CC -!- INTERACTION:
CC Q12983; Q86WK6: AMIGO1; NbExp=3; IntAct=EBI-749464, EBI-19125216;
CC Q12983; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-749464, EBI-11343438;
CC Q12983; Q13323: BIK; NbExp=3; IntAct=EBI-749464, EBI-700794;
CC Q12983; Q12982: BNIP2; NbExp=3; IntAct=EBI-749464, EBI-752094;
CC Q12983; Q12983: BNIP3; NbExp=8; IntAct=EBI-749464, EBI-749464;
CC Q12983; O60238: BNIP3L; NbExp=22; IntAct=EBI-749464, EBI-849893;
CC Q12983; P07766: CD3E; NbExp=3; IntAct=EBI-749464, EBI-1211297;
CC Q12983; O95484: CLDN9; NbExp=3; IntAct=EBI-749464, EBI-18341636;
CC Q12983; Q9BXN2: CLEC7A; NbExp=3; IntAct=EBI-749464, EBI-3939278;
CC Q12983; Q9BXN2-6: CLEC7A; NbExp=3; IntAct=EBI-749464, EBI-11989440;
CC Q12983; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-749464, EBI-11522780;
CC Q12983; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-749464, EBI-6942903;
CC Q12983; O00559: EBAG9; NbExp=3; IntAct=EBI-749464, EBI-8787095;
CC Q12983; Q15125: EBP; NbExp=3; IntAct=EBI-749464, EBI-3915253;
CC Q12983; Q9GZR5: ELOVL4; NbExp=3; IntAct=EBI-749464, EBI-18535450;
CC Q12983; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-749464, EBI-781551;
CC Q12983; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-749464, EBI-18304435;
CC Q12983; Q96D05-2: FAM241B; NbExp=3; IntAct=EBI-749464, EBI-12118888;
CC Q12983; Q92520: FAM3C; NbExp=3; IntAct=EBI-749464, EBI-2876774;
CC Q12983; Q969F0: FATE1; NbExp=6; IntAct=EBI-749464, EBI-743099;
CC Q12983; O15552: FFAR2; NbExp=3; IntAct=EBI-749464, EBI-2833872;
CC Q12983; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-749464, EBI-13345167;
CC Q12983; O15529: GPR42; NbExp=3; IntAct=EBI-749464, EBI-18076404;
CC Q12983; P05981: HPN; NbExp=3; IntAct=EBI-749464, EBI-12816745;
CC Q12983; P38484: IFNGR2; NbExp=3; IntAct=EBI-749464, EBI-3905457;
CC Q12983; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-749464, EBI-10266796;
CC Q12983; Q86UP2: KTN1; NbExp=3; IntAct=EBI-749464, EBI-359761;
CC Q12983; Q86UP2-3: KTN1; NbExp=3; IntAct=EBI-749464, EBI-12007212;
CC Q12983; Q5T700: LDLRAD1; NbExp=6; IntAct=EBI-749464, EBI-10173166;
CC Q12983; Q13021: MALL; NbExp=3; IntAct=EBI-749464, EBI-750078;
CC Q12983; Q5SR56: MFSD14B; NbExp=3; IntAct=EBI-749464, EBI-373355;
CC Q12983; Q96HJ5: MS4A3; NbExp=3; IntAct=EBI-749464, EBI-12806656;
CC Q12983; O60313: OPA1; NbExp=10; IntAct=EBI-749464, EBI-1054131;
CC Q12983; Q04941: PLP2; NbExp=3; IntAct=EBI-749464, EBI-608347;
CC Q12983; Q8NI37: PPTC7; NbExp=8; IntAct=EBI-749464, EBI-9089276;
CC Q12983; Q9BRK0: REEP2; NbExp=3; IntAct=EBI-749464, EBI-11337973;
CC Q12983; Q6P5S7: RNASEK; NbExp=3; IntAct=EBI-749464, EBI-18397230;
CC Q12983; Q9Y225-2: RNF24; NbExp=3; IntAct=EBI-749464, EBI-13044680;
CC Q12983; Q9NS64: RPRM; NbExp=3; IntAct=EBI-749464, EBI-1052363;
CC Q12983; Q9NY72: SCN3B; NbExp=3; IntAct=EBI-749464, EBI-17247926;
CC Q12983; Q96IW7: SEC22A; NbExp=3; IntAct=EBI-749464, EBI-8652744;
CC Q12983; Q15436: SEC23A; NbExp=3; IntAct=EBI-749464, EBI-81088;
CC Q12983; O15432: SLC31A2; NbExp=3; IntAct=EBI-749464, EBI-17867220;
CC Q12983; P78383: SLC35B1; NbExp=3; IntAct=EBI-749464, EBI-12147661;
CC Q12983; Q9H1V8: SLC6A17; NbExp=3; IntAct=EBI-749464, EBI-18396863;
CC Q12983; Q9BZL3: SMIM3; NbExp=3; IntAct=EBI-749464, EBI-741850;
CC Q12983; Q9HBV2: SPACA1; NbExp=3; IntAct=EBI-749464, EBI-17498703;
CC Q12983; Q96MV1: TLCD4; NbExp=3; IntAct=EBI-749464, EBI-12947623;
CC Q12983; Q96CE8: TM4SF18; NbExp=3; IntAct=EBI-749464, EBI-13351685;
CC Q12983; Q96IK0: TMEM101; NbExp=3; IntAct=EBI-749464, EBI-3922699;
CC Q12983; Q9BVX2: TMEM106C; NbExp=3; IntAct=EBI-749464, EBI-2821497;
CC Q12983; P17152: TMEM11; NbExp=11; IntAct=EBI-749464, EBI-723946;
CC Q12983; Q6UW68: TMEM205; NbExp=3; IntAct=EBI-749464, EBI-6269551;
CC Q12983; O15393-2: TMPRSS2; NbExp=3; IntAct=EBI-749464, EBI-12345267;
CC Q12983; Q9Y320: TMX2; NbExp=3; IntAct=EBI-749464, EBI-6447886;
CC Q12983; Q9H2S6-2: TNMD; NbExp=3; IntAct=EBI-749464, EBI-12003398;
CC Q12983; Q96MV8: ZDHHC15; NbExp=3; IntAct=EBI-749464, EBI-12837904;
CC Q12983; Q5ZSD5: sidF; Xeno; NbExp=3; IntAct=EBI-749464, EBI-15625247;
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion outer membrane;
CC Single-pass membrane protein. Note=Coexpression with the EIB 19-kDa
CC protein results in a shift in NIP3 localization pattern to the nuclear
CC envelope. Colocalizes with ACAA2 in the mitochondria. Colocalizes with
CC SPATA18 at the mitochondrion outer membrane.
CC -!- SIMILARITY: Belongs to the NIP3 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/BNIP3ID822ch10q26.html";
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/bnip3/";
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DR EMBL; U15174; AAC00022.1; -; mRNA.
DR EMBL; AF002697; AAC16738.1; -; mRNA.
DR EMBL; AY886764; AAW62256.1; -; Genomic_DNA.
DR EMBL; AL162274; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC009342; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC021989; AAH21989.1; -; mRNA.
DR PIR; I38865; I38865.
DR RefSeq; NP_004043.3; NM_004052.3.
DR PDB; 2J5D; NMR; -; A/B=146-190.
DR PDB; 2KA1; NMR; -; A/B=154-188.
DR PDB; 2KA2; NMR; -; A/B=154-188.
DR PDBsum; 2J5D; -.
DR PDBsum; 2KA1; -.
DR PDBsum; 2KA2; -.
DR AlphaFoldDB; Q12983; -.
DR BMRB; Q12983; -.
DR SMR; Q12983; -.
DR BioGRID; 107132; 94.
DR DIP; DIP-34429N; -.
DR IntAct; Q12983; 70.
DR MINT; Q12983; -.
DR STRING; 9606.ENSP00000357625; -.
DR TCDB; 1.A.20.1.1; the bcl2/adenovirus e1b-interacting protein 3 (bnip3) family.
DR iPTMnet; Q12983; -.
DR PhosphoSitePlus; Q12983; -.
DR BioMuta; BNIP3; -.
DR DMDM; 20532402; -.
DR EPD; Q12983; -.
DR jPOST; Q12983; -.
DR MassIVE; Q12983; -.
DR PaxDb; Q12983; -.
DR PeptideAtlas; Q12983; -.
DR PRIDE; Q12983; -.
DR ProteomicsDB; 59081; -.
DR Antibodypedia; 31; 602 antibodies from 36 providers.
DR DNASU; 664; -.
DR Ensembl; ENST00000368636.9; ENSP00000357625.6; ENSG00000176171.12.
DR GeneID; 664; -.
DR KEGG; hsa:664; -.
DR MANE-Select; ENST00000368636.9; ENSP00000357625.6; NM_004052.4; NP_004043.4.
DR UCSC; uc001lkv.2; human.
DR CTD; 664; -.
DR DisGeNET; 664; -.
DR GeneCards; BNIP3; -.
DR HGNC; HGNC:1084; BNIP3.
DR HPA; ENSG00000176171; Tissue enhanced (pancreas, skeletal muscle).
DR MIM; 603293; gene.
DR neXtProt; NX_Q12983; -.
DR OpenTargets; ENSG00000176171; -.
DR PharmGKB; PA25394; -.
DR VEuPathDB; HostDB:ENSG00000176171; -.
DR eggNOG; ENOG502QQ4B; Eukaryota.
DR GeneTree; ENSGT00390000013415; -.
DR InParanoid; Q12983; -.
DR OMA; KDWKFKH; -.
DR OrthoDB; 1250566at2759; -.
DR PhylomeDB; Q12983; -.
DR TreeFam; TF315424; -.
DR PathwayCommons; Q12983; -.
DR SignaLink; Q12983; -.
DR SIGNOR; Q12983; -.
DR BioGRID-ORCS; 664; 128 hits in 1075 CRISPR screens.
DR ChiTaRS; BNIP3; human.
DR EvolutionaryTrace; Q12983; -.
DR GeneWiki; BNIP3; -.
DR GenomeRNAi; 664; -.
DR Pharos; Q12983; Tbio.
DR PRO; PR:Q12983; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q12983; protein.
DR Bgee; ENSG00000176171; Expressed in endothelial cell and 208 other tissues.
DR ExpressionAtlas; Q12983; baseline and differential.
DR Genevisible; Q12983; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; IDA:UniProtKB.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:0051020; F:GTPase binding; IPI:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IPI:MGI.
DR GO; GO:0048102; P:autophagic cell death; IEA:Ensembl.
DR GO; GO:0000422; P:autophagy of mitochondrion; NAS:ParkinsonsUK-UCL.
DR GO; GO:0050873; P:brown fat cell differentiation; IEA:Ensembl.
DR GO; GO:0010659; P:cardiac muscle cell apoptotic process; IEA:Ensembl.
DR GO; GO:0008219; P:cell death; ISS:UniProtKB.
DR GO; GO:0071279; P:cellular response to cobalt ion; IMP:BHF-UCL.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
DR GO; GO:0071456; P:cellular response to hypoxia; IMP:BHF-UCL.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:UniProtKB.
DR GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
DR GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
DR GO; GO:0140507; P:granzyme-mediated programmed cell death signaling pathway; IDA:GO_Central.
DR GO; GO:1990144; P:intrinsic apoptotic signaling pathway in response to hypoxia; IMP:BHF-UCL.
DR GO; GO:0043653; P:mitochondrial fragmentation involved in apoptotic process; IDA:BHF-UCL.
DR GO; GO:0097345; P:mitochondrial outer membrane permeabilization; IDA:UniProtKB.
DR GO; GO:0035694; P:mitochondrial protein catabolic process; IMP:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:UniProtKB.
DR GO; GO:0060548; P:negative regulation of cell death; IGI:MGI.
DR GO; GO:0045837; P:negative regulation of membrane potential; IDA:UniProtKB.
DR GO; GO:0010637; P:negative regulation of mitochondrial fusion; IDA:BHF-UCL.
DR GO; GO:1902109; P:negative regulation of mitochondrial membrane permeability involved in apoptotic process; IEA:Ensembl.
DR GO; GO:0010917; P:negative regulation of mitochondrial membrane potential; IEA:Ensembl.
DR GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; IEA:Ensembl.
DR GO; GO:0051402; P:neuron apoptotic process; ISS:UniProtKB.
DR GO; GO:0048709; P:oligodendrocyte differentiation; IEA:Ensembl.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0010508; P:positive regulation of autophagy; TAS:UniProtKB.
DR GO; GO:1903599; P:positive regulation of autophagy of mitochondrion; IEA:Ensembl.
DR GO; GO:0010666; P:positive regulation of cardiac muscle cell apoptotic process; IEA:Ensembl.
DR GO; GO:0016239; P:positive regulation of macroautophagy; IGI:MGI.
DR GO; GO:0051561; P:positive regulation of mitochondrial calcium ion concentration; IEA:Ensembl.
DR GO; GO:0090141; P:positive regulation of mitochondrial fission; IDA:BHF-UCL.
DR GO; GO:0010940; P:positive regulation of necrotic cell death; IEA:Ensembl.
DR GO; GO:0043068; P:positive regulation of programmed cell death; IDA:UniProtKB.
DR GO; GO:0043243; P:positive regulation of protein-containing complex disassembly; IDA:BHF-UCL.
DR GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; IDA:BHF-UCL.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; IDA:UniProtKB.
DR GO; GO:1903715; P:regulation of aerobic respiration; IEA:Ensembl.
DR GO; GO:0046902; P:regulation of mitochondrial membrane permeability; IDA:UniProtKB.
DR GO; GO:0043067; P:regulation of programmed cell death; IBA:GO_Central.
DR GO; GO:0048678; P:response to axon injury; IEA:Ensembl.
DR GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR GO; GO:0055093; P:response to hyperoxia; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; ISS:UniProtKB.
DR GO; GO:0090649; P:response to oxygen-glucose deprivation; IEA:Ensembl.
DR GO; GO:1901998; P:toxin transport; IEA:Ensembl.
DR InterPro; IPR010548; BNIP3.
DR PANTHER; PTHR15186; PTHR15186; 1.
DR Pfam; PF06553; BNIP3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Apoptosis; Host-virus interaction; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..194
FT /note="BCL2/adenovirus E1B 19 kDa protein-interacting
FT protein 3"
FT /id="PRO_0000064964"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 100..125
FT /note="BH3"
FT COMPBIAS 1..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..102
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55003"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CONFLICT 3
FT /note="Q -> E (in Ref. 1; AAC00022)"
FT /evidence="ECO:0000305"
FT HELIX 159..188
FT /evidence="ECO:0007829|PDB:2J5D"
SQ SEQUENCE 194 AA; 21541 MW; 6D79E68F146D25EB CRC64;
MSQNGAPGMQ EESLQGSWVE LHFSNNGNGG SVPASVSIYN GDMEKILLDA QHESGRSSSK
SSHCDSPPRS QTPQDTNRAS ETDTHSIGEK NSSQSEEDDI ERRKEVESIL KKNSDWIWDW
SSRPENIPPK EFLFKHPKRT ATLSMRNTSV MKKGGIFSAE FLKVFLPSLL LSHLLAIGLG
IYIGRRLTTS TSTF
