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Q12983

- BNIP3_HUMAN

UniProt

Q12983 - BNIP3_HUMAN

Protein

BCL2/adenovirus E1B 19 kDa protein-interacting protein 3

Gene

BNIP3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 2 (10 May 2002)
      Previous versions | rss
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    Functioni

    Apoptosis-inducing protein that can overcome BCL2 suppression. May play a role in repartitioning calcium between the two major intracellular calcium stores in association with BCL2. Involved in mitochondrial quality control via its interaction with SPATA18/MIEAP: in response to mitochondrial damage, participates to 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. Plays an important role in the calprotectin (S100A8/A9)-induced cell death pathway.2 Publications

    GO - Molecular functioni

    1. GTPase binding Source: BHF-UCL
    2. identical protein binding Source: IntAct
    3. protein binding Source: UniProtKB
    4. protein heterodimerization activity Source: UniProtKB
    5. protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    1. apoptotic process Source: MGI
    2. autophagic cell death Source: Ensembl
    3. brown fat cell differentiation Source: Ensembl
    4. cell death Source: UniProtKB
    5. cellular response to cobalt ion Source: BHF-UCL
    6. cellular response to hydrogen peroxide Source: Ensembl
    7. cellular response to hypoxia Source: BHF-UCL
    8. cellular response to mechanical stimulus Source: UniProtKB
    9. defense response to virus Source: UniProtKB
    10. granzyme-mediated apoptotic signaling pathway Source: UniProtKB
    11. intrinsic apoptotic signaling pathway in response to hypoxia Source: BHF-UCL
    12. mitochondrial fragmentation involved in apoptotic process Source: BHF-UCL
    13. mitochondrial outer membrane permeabilization Source: UniProtKB
    14. mitochondrial protein catabolic process Source: UniProtKB
    15. negative regulation of apoptotic process Source: UniProtKB
    16. negative regulation of membrane potential Source: UniProtKB
    17. negative regulation of mitochondrial fusion Source: BHF-UCL
    18. neuron apoptotic process Source: UniProtKB
    19. positive regulation of apoptotic process Source: UniProtKB
    20. positive regulation of autophagy Source: UniProtKB
    21. positive regulation of mitochondrial fission Source: BHF-UCL
    22. positive regulation of programmed cell death Source: UniProtKB
    23. positive regulation of protein complex disassembly Source: BHF-UCL
    24. positive regulation of release of cytochrome c from mitochondria Source: BHF-UCL
    25. reactive oxygen species metabolic process Source: UniProtKB
    26. regulation of mitochondrial membrane permeability Source: UniProtKB
    27. response to hyperoxia Source: Ensembl
    28. response to hypoxia Source: UniProtKB
    29. viral process Source: UniProtKB-KW

    Keywords - Biological processi

    Apoptosis, Host-virus interaction

    Protein family/group databases

    TCDBi1.A.20.1.1. the bcl2/adenovirus e1b-interacting protein 3 (bnip3) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    BCL2/adenovirus E1B 19 kDa protein-interacting protein 3
    Gene namesi
    Name:BNIP3
    Synonyms:NIP3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:1084. BNIP3.

    Subcellular locationi

    Mitochondrion. Mitochondrion outer membrane; Single-pass membrane protein
    Note: Coexpression with the EIB 19-kDa protein results in a shift in NIP3 localization pattern to the nuclear envelope. Colocalizes with ACAA2 in the mitochondria. Colocalizes with SPATA18 at the mitochondrion outer membrane.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. dendrite Source: UniProtKB
    3. endoplasmic reticulum Source: RefGenome
    4. integral component of mitochondrial outer membrane Source: UniProtKB
    5. mitochondrial membrane Source: UniProtKB
    6. mitochondrial outer membrane Source: UniProtKB
    7. mitochondrion Source: UniProtKB
    8. nuclear envelope Source: UniProtKB
    9. nucleoplasm Source: UniProtKB
    10. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion outer membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25394.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 194194BCL2/adenovirus E1B 19 kDa protein-interacting protein 3PRO_0000064964Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei86 – 861Phosphoserine1 Publication
    Modified residuei92 – 921PhosphoserineBy similarity
    Modified residuei95 – 951PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ12983.
    PaxDbiQ12983.
    PRIDEiQ12983.

    PTM databases

    PhosphoSiteiQ12983.

    Expressioni

    Gene expression databases

    ArrayExpressiQ12983.
    BgeeiQ12983.
    CleanExiHS_BNIP3.
    GenevestigatoriQ12983.

    Organism-specific databases

    HPAiCAB011676.
    HPA003015.

    Interactioni

    Subunit structurei

    Homodimer. Binds to BCL2. Interacts with BNIP3L and ACAA2. Also can interact with adenovirus E1B 19 kDa protein or Epstein-Barr virus BHRF1. Interacts (via BH3 domain) with SPATA18 (via coiled-coil domains).4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-749464,EBI-749464
    BNIP3LO602389EBI-749464,EBI-849893
    OPA1O6031310EBI-749464,EBI-1054131
    TMEM11P171522EBI-749464,EBI-723946

    Protein-protein interaction databases

    BioGridi107132. 15 interactions.
    DIPiDIP-34429N.
    IntActiQ12983. 8 interactions.
    MINTiMINT-1475327.
    STRINGi9606.ENSP00000357625.

    Structurei

    Secondary structure

    1
    194
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi159 – 18830

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2J5DNMR-A/B146-190[»]
    2KA1NMR-A/B154-188[»]
    2KA2NMR-A/B154-188[»]
    ProteinModelPortaliQ12983.
    SMRiQ12983. Positions 146-190.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ12983.

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei164 – 18421HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi100 – 12526BH3Add
    BLAST

    Sequence similaritiesi

    Belongs to the NIP3 family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG68335.
    HOVERGENiHBG050707.
    InParanoidiQ12983.
    KOiK15464.
    OMAiMKKNADW.
    OrthoDBiEOG74N5J4.
    PhylomeDBiQ12983.
    TreeFamiTF315424.

    Family and domain databases

    InterProiIPR010548. BNIP3.
    [Graphical view]
    PfamiPF06553. BNIP3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q12983-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSQNGAPGMQ EESLQGSWVE LHFSNNGNGG SVPASVSIYN GDMEKILLDA    50
    QHESGRSSSK SSHCDSPPRS QTPQDTNRAS ETDTHSIGEK NSSQSEEDDI 100
    ERRKEVESIL KKNSDWIWDW SSRPENIPPK EFLFKHPKRT ATLSMRNTSV 150
    MKKGGIFSAE FLKVFLPSLL LSHLLAIGLG IYIGRRLTTS TSTF 194
    Length:194
    Mass (Da):21,541
    Last modified:May 10, 2002 - v2
    Checksum:i6D79E68F146D25EB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti3 – 31Q → E in AAC00022. (PubMed:7954800)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U15174 mRNA. Translation: AAC00022.1.
    AF002697 mRNA. Translation: AAC16738.1.
    AY886764 Genomic DNA. Translation: AAW62256.1.
    AL162274 Genomic DNA. Translation: CAD13201.1.
    BC009342 mRNA. No translation available.
    BC021989 mRNA. Translation: AAH21989.1.
    CCDSiCCDS7663.1.
    PIRiI38865.
    RefSeqiNP_004043.2. NM_004052.2.
    UniGeneiHs.144873.

    Genome annotation databases

    EnsembliENST00000368636; ENSP00000357625; ENSG00000176171.
    GeneIDi664.
    KEGGihsa:664.
    UCSCiuc001lkv.1. human.

    Polymorphism databases

    DMDMi20532402.

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology
    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U15174 mRNA. Translation: AAC00022.1 .
    AF002697 mRNA. Translation: AAC16738.1 .
    AY886764 Genomic DNA. Translation: AAW62256.1 .
    AL162274 Genomic DNA. Translation: CAD13201.1 .
    BC009342 mRNA. No translation available.
    BC021989 mRNA. Translation: AAH21989.1 .
    CCDSi CCDS7663.1.
    PIRi I38865.
    RefSeqi NP_004043.2. NM_004052.2.
    UniGenei Hs.144873.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2J5D NMR - A/B 146-190 [» ]
    2KA1 NMR - A/B 154-188 [» ]
    2KA2 NMR - A/B 154-188 [» ]
    ProteinModelPortali Q12983.
    SMRi Q12983. Positions 146-190.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107132. 15 interactions.
    DIPi DIP-34429N.
    IntActi Q12983. 8 interactions.
    MINTi MINT-1475327.
    STRINGi 9606.ENSP00000357625.

    Protein family/group databases

    TCDBi 1.A.20.1.1. the bcl2/adenovirus e1b-interacting protein 3 (bnip3) family.

    PTM databases

    PhosphoSitei Q12983.

    Polymorphism databases

    DMDMi 20532402.

    Proteomic databases

    MaxQBi Q12983.
    PaxDbi Q12983.
    PRIDEi Q12983.

    Protocols and materials databases

    DNASUi 664.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000368636 ; ENSP00000357625 ; ENSG00000176171 .
    GeneIDi 664.
    KEGGi hsa:664.
    UCSCi uc001lkv.1. human.

    Organism-specific databases

    CTDi 664.
    GeneCardsi GC10M133781.
    H-InvDB HIX0037770.
    HGNCi HGNC:1084. BNIP3.
    HPAi CAB011676.
    HPA003015.
    MIMi 603293. gene.
    neXtProti NX_Q12983.
    PharmGKBi PA25394.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG68335.
    HOVERGENi HBG050707.
    InParanoidi Q12983.
    KOi K15464.
    OMAi MKKNADW.
    OrthoDBi EOG74N5J4.
    PhylomeDBi Q12983.
    TreeFami TF315424.

    Miscellaneous databases

    EvolutionaryTracei Q12983.
    GeneWikii BNIP3.
    GenomeRNAii 664.
    NextBioi 2708.
    PROi Q12983.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q12983.
    Bgeei Q12983.
    CleanExi HS_BNIP3.
    Genevestigatori Q12983.

    Family and domain databases

    InterProi IPR010548. BNIP3.
    [Graphical view ]
    Pfami PF06553. BNIP3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Adenovirus E1B 19 kDa and Bcl-2 proteins interact with a common set of cellular proteins."
      Boyd J.M., Malstrom S., Subramanian T., Venkatesh L.K., Schaeper U., Elangovan B., D'Sa-Eipper C., Chinnadurai G.
      Cell 79:341-351(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH BCL2.
      Tissue: B-cell.
    2. "The E1B 19K/Bcl-2-binding protein Nip3 is a dimeric mitochondrial protein that activates apoptosis."
      Chen G., Ray R., Dubik D., Shi L., Cizeau J., Bleackley R.C., Saxena S., Gietz R.D., Greenberg A.H.
      J. Exp. Med. 186:1975-1983(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: B-cell.
    3. NIEHS SNPs program
      Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    6. "A novel adenovirus E1B19K-binding protein B5 inhibits apoptosis induced by Nip3 by forming a heterodimer through the C-terminal hydrophobic region."
      Ohi N., Tokunaga A., Tsunoda H., Nakano K., Haraguchi K., Oda K., Motoyama N., Nakajima T.
      Cell Death Differ. 6:314-325(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BNIP3L.
    7. "Acetyl-Coenzyme A acyltransferase 2 attenuates the apoptotic effects of BNIP3 in two human cell lines."
      Cao W., Liu N., Tang S., Bao L., Shen L., Yuan H., Zhao X., Lu H.
      Biochim. Biophys. Acta 1780:873-880(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH ACAA2.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "S100A8/A9 induces autophagy and apoptosis via ROS-mediated cross-talk between mitochondria and lysosomes that involves BNIP3."
      Ghavami S., Eshragi M., Ande S.R., Chazin W.J., Klonisch T., Halayko A.J., McNeill K.D., Hashemi M., Kerkhoff C., Los M.
      Cell Res. 20:314-331(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      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.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "BNIP3 and NIX mediate Mieap-induced accumulation of lysosomal proteins within mitochondria."
      Nakamura Y., Kitamura N., Shinogi D., Yoshida M., Goda O., Murai R., Kamino H., Arakawa H.
      PLoS ONE 7:E30767-E30767(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SPATA18, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiBNIP3_HUMAN
    AccessioniPrimary (citable) accession number: Q12983
    Secondary accession number(s): O14620, Q96GP0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: May 10, 2002
    Last modified: October 1, 2014
    This is version 140 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3