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Q12983

- BNIP3_HUMAN

UniProt

Q12983 - BNIP3_HUMAN

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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

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 heterodimerization activity Source: UniProtKB
  4. 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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ12983.
CleanExiHS_BNIP3.
ExpressionAtlasiQ12983. baseline and differential.
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. 16 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.
GeneTreeiENSGT00390000013415.
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

        10         20         30         40         50
MSQNGAPGMQ EESLQGSWVE LHFSNNGNGG SVPASVSIYN GDMEKILLDA
60 70 80 90 100
QHESGRSSSK SSHCDSPPRS QTPQDTNRAS ETDTHSIGEK NSSQSEEDDI
110 120 130 140 150
ERRKEVESIL KKNSDWIWDW SSRPENIPPK EFLFKHPKRT ATLSMRNTSV
160 170 180 190
MKKGGIFSAE FLKVFLPSLL LSHLLAIGLG IYIGRRLTTS TSTF
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. 16 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.
GeneTreei ENSGT00390000013415.
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

Bgeei Q12983.
CleanExi HS_BNIP3.
ExpressionAtlasi Q12983. baseline and differential.
Genevestigatori Q12983.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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 29, 2014
This is version 141 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