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Protein

BCL2/adenovirus E1B 19 kDa protein-interacting protein 3

Gene

BNIP3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

  • GTPase binding Source: BHF-UCL
  • identical protein binding Source: IntAct
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

  • apoptotic process Source: MGI
  • autophagic cell death Source: Ensembl
  • brown fat cell differentiation Source: Ensembl
  • cell death Source: UniProtKB
  • cellular response to cobalt ion Source: BHF-UCL
  • cellular response to hydrogen peroxide Source: Ensembl
  • cellular response to hypoxia Source: BHF-UCL
  • cellular response to mechanical stimulus Source: UniProtKB
  • defense response to virus Source: UniProtKB
  • granzyme-mediated apoptotic signaling pathway Source: UniProtKB
  • intrinsic apoptotic signaling pathway in response to hypoxia Source: BHF-UCL
  • mitochondrial fragmentation involved in apoptotic process Source: BHF-UCL
  • mitochondrial outer membrane permeabilization Source: UniProtKB
  • mitochondrial protein catabolic process Source: UniProtKB
  • mitochondrion degradation Source: ParkinsonsUK-UCL
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of membrane potential Source: UniProtKB
  • negative regulation of mitochondrial fusion Source: BHF-UCL
  • neuron apoptotic process Source: UniProtKB
  • positive regulation of apoptotic process Source: UniProtKB
  • positive regulation of autophagy Source: UniProtKB
  • positive regulation of mitochondrial fission Source: BHF-UCL
  • positive regulation of programmed cell death Source: UniProtKB
  • positive regulation of protein complex disassembly Source: BHF-UCL
  • positive regulation of release of cytochrome c from mitochondria Source: BHF-UCL
  • reactive oxygen species metabolic process Source: UniProtKB
  • regulation of mitochondrial membrane permeability Source: UniProtKB
  • response to hyperoxia Source: Ensembl
  • response to hypoxia Source: UniProtKB
  • toxin transport Source: Ensembl
  • 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 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:1084. BNIP3.

Subcellular locationi

Topology

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

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • dendrite Source: UniProtKB
  • endoplasmic reticulum Source: ParkinsonsUK-UCL
  • integral component of mitochondrial outer membrane Source: UniProtKB
  • mitochondrial membrane Source: UniProtKB
  • mitochondrial outer membrane Source: UniProtKB
  • mitochondrion Source: UniProtKB
  • nuclear envelope Source: UniProtKB
  • nucleoplasm Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25394.

Polymorphism and mutation databases

BioMutaiBNIP3.
DMDMi20532402.

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 residuei54 – 541Phosphoserine1 Publication
Modified residuei66 – 661Phosphoserine1 Publication
Modified residuei86 – 861Phosphoserine1 Publication
Modified residuei92 – 921PhosphoserineBy similarity
Modified residuei95 – 951Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ12983.
PaxDbiQ12983.
PRIDEiQ12983.

PTM databases

PhosphoSiteiQ12983.

Expressioni

Gene expression databases

BgeeiQ12983.
CleanExiHS_BNIP3.
ExpressionAtlasiQ12983. baseline and differential.
GenevisibleiQ12983. HS.

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
itself3EBI-749464,EBI-749464
BNIP3LO6023812EBI-749464,EBI-849893
CLEC7AQ9BXN23EBI-749464,EBI-3939278
FATE1Q969F03EBI-749464,EBI-743099
KTN1Q86UP23EBI-749464,EBI-359761
LDLRAD1Q5T7003EBI-749464,EBI-10173166
OPA1O6031310EBI-749464,EBI-1054131
TMEM11P171525EBI-749464,EBI-723946

Protein-protein interaction databases

BioGridi107132. 19 interactions.
DIPiDIP-34429N.
IntActiQ12983. 12 interactions.
MINTiMINT-1475327.
STRINGi9606.ENSP00000357625.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.

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:
EMBLi
GenBanki
DDBJi
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.
PIRiI38865.
RefSeqiNP_004043.3. NM_004052.3.
UniGeneiHs.144873.

Genome annotation databases

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

Cross-referencesi

Web resourcesi

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
PIRiI38865.
RefSeqiNP_004043.3. NM_004052.3.
UniGeneiHs.144873.

3D structure databases

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

Protein-protein interaction databases

BioGridi107132. 19 interactions.
DIPiDIP-34429N.
IntActiQ12983. 12 interactions.
MINTiMINT-1475327.
STRINGi9606.ENSP00000357625.

Protein family/group databases

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

PTM databases

PhosphoSiteiQ12983.

Polymorphism and mutation databases

BioMutaiBNIP3.
DMDMi20532402.

Proteomic databases

MaxQBiQ12983.
PaxDbiQ12983.
PRIDEiQ12983.

Protocols and materials databases

DNASUi664.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi664.
GeneCardsiGC10M133781.
H-InvDBHIX0037770.
HGNCiHGNC:1084. BNIP3.
HPAiCAB011676.
HPA003015.
MIMi603293. gene.
neXtProtiNX_Q12983.
PharmGKBiPA25394.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG68335.
GeneTreeiENSGT00390000013415.
HOVERGENiHBG050707.
InParanoidiQ12983.
KOiK15464.
OMAiMKKNADW.
OrthoDBiEOG74N5J4.
PhylomeDBiQ12983.
TreeFamiTF315424.

Miscellaneous databases

EvolutionaryTraceiQ12983.
GeneWikiiBNIP3.
GenomeRNAii664.
NextBioi2708.
PROiQ12983.
SOURCEiSearch...

Gene expression databases

BgeeiQ12983.
CleanExiHS_BNIP3.
ExpressionAtlasiQ12983. baseline and differential.
GenevisibleiQ12983. HS.

Family and domain databases

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

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.
  13. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; SER-66 AND SER-95, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

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: June 24, 2015
This is version 147 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.