Q12983 (BNIP3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
BCL2/adenovirus E1B 19 kDa protein-interacting protein 3

Gene names

Name:	BNIP3
Synonyms:	NIP3

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	194 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Apoptosis-inducing protein that, which can overcome BCL2 suppression. May play a role in repartitioning calcium between the two major intracellular calcium stores in association with BCL2.
Subunit structure	Homodimer. Binds to BCL2. Interacts with BNIP3L and ACAA2. Also can interact with adenovirus E1B 19 kDa protein or Epstein-Barr virus BHRF1. Ref.6 Ref.8
Subcellular location	Mitochondrion. Mitochondrion 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. Ref.8
Sequence similarities	Belongs to the NIP3 family.

Ontologies

Keywords
Biological process	Apoptosis Host-virus interaction
Cellular component	Membrane Mitochondrion
Domain	Transmembrane Transmembrane helix
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	DNA fragmentation involved in apoptotic nuclear change Inferred from direct assay. Source: UniProtKB cellular response to cobalt ion Inferred from mutant phenotype. Source: BHF-UCL cellular response to hypoxia Inferred from mutant phenotype. Source: BHF-UCL cellular response to mechanical stimulus Inferred from expression pattern. Source: UniProtKB chromatin remodeling Inferred from direct assay. Source: UniProtKB defense response to virus Inferred from direct assay. Source: UniProtKB interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial fragmentation involved in apoptosis Inferred from direct assay. Source: BHF-UCL negative regulation of membrane potential Inferred from direct assay. Source: UniProtKB negative regulation of mitochondrial fusion Inferred from direct assay. Source: BHF-UCL negative regulation of survival gene product expression Inferred from direct assay. Source: UniProtKB neuron apoptosis Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of mitochondrial fission Inferred from direct assay. Source: BHF-UCL positive regulation of protein complex disassembly Inferred from direct assay. Source: BHF-UCL positive regulation of release of cytochrome c from mitochondria Inferred from direct assay. Source: BHF-UCL reactive oxygen species metabolic process Inferred from direct assay. Source: UniProtKB regulation of mitochondrial membrane permeability Inferred from direct assay. Source: UniProtKB
Cellular component	dendrite Inferred from sequence or structural similarity. Source: UniProtKB integral to mitochondrial outer membrane Inferred from direct assay. Source: UniProtKB nuclear envelope Inferred from direct assay Ref.1. Source: UniProtKB nucleoplasm Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	GTPase binding Inferred from physical interaction. Source: BHF-UCL protein heterodimerization activity Inferred from direct assay Ref.6. Source: UniProtKB protein homodimerization activity Inferred from direct assay Ref.6Ref.2. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-749464,EBI-749464
BNIP3L	O60238	8	EBI-749464,EBI-849893
TMEM11	P17152	2	EBI-749464,EBI-723946

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 194

194

BCL2/adenovirus E1B 19 kDa protein-interacting protein 3

PRO_0000064964

Regions

Transmembrane

164 – 184

21

Helical; Potential

Amino acid modifications

Modified residue

86

1

Phosphoserine By similarity

Modified residue

92

1

Phosphoserine By similarity

Modified residue

93

1

Phosphoserine Ref.7

Modified residue

95

1

Phosphoserine By similarity

Experimental info

Sequence conflict

3

1

Q → E in AAC00022. Ref.1

Secondary structure

1

.

.

.

194

Helix Strand Turn

Details...

Helix

159 – 188

30

Sequences

	Sequence		Length	Mass (Da)
	Q12983 [UniParc]. Last modified May 10, 2002. Version 2. Checksum: 6D79E68F146D25EB	FASTA	194	21,541
	10 20 30 40 50 60 MSQNGAPGMQ EESLQGSWVE LHFSNNGNGG SVPASVSIYN GDMEKILLDA QHESGRSSSK 70 80 90 100 110 120 SSHCDSPPRS QTPQDTNRAS ETDTHSIGEK NSSQSEEDDI ERRKEVESIL KKNSDWIWDW 130 140 150 160 170 180 SSRPENIPPK EFLFKHPKRT ATLSMRNTSV MKKGGIFSAE FLKVFLPSLL LSHLLAIGLG 190 IYIGRRLTTS TSTF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 7954800] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. 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: 9396766] [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: 15164054] [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: 15489334] [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: 10381623] [Abstract] Cited for: INTERACTION WITH BNIP3L.
[7]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"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: 18371312] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH ACAA2.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00290409.

PIR

I38865.

RefSeq

NP_004043.2. NM_004052.2.

UniGene

Hs.144873.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q12983.

SMR

Q12983. Positions 146-190.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q12983. 8 interactions.

MINT

MINT-1475327.

STRING

Q12983.

Protein family/group databases

TCDB

1.A.20.1.1. BCL2/adenovirus E1B-interacting protein 3 (BNip3) family.

PTM databases

PhosphoSite

Q12983.

Polymorphism databases

DMDM

20532402.

Proteomic databases

PRIDE

Q12983.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000368636; ENSP00000357625; ENSG00000176171.

GeneID

664.

KEGG

hsa:664.

UCSC

uc001lkv.1. human.

Organism-specific databases

CTD

664.

GeneCards

GC10M133781.

H-InvDB

HIX0020971.
HIX0037770.

HGNC

HGNC:1084. BNIP3.

HPA

CAB011676.
HPA003015.

MIM

603293. gene.

neXtProt

NX_Q12983.

PharmGKB

PA25394.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG14892.

HOVERGEN

HBG050707.

InParanoid

Q12983.

OMA

QTPQDIN.

OrthoDB

EOG4T784H.

PhylomeDB

Q12983.

Enzyme and pathway databases

Pathway_Interaction_DB

hif1_tfpathway. HIF-1-alpha transcription factor network.

Gene expression databases

ArrayExpress

Q12983.

Bgee

Q12983.

CleanEx

HS_BNIP3.

Genevestigator

Q12983.

GermOnline

ENSG00000176171. Homo sapiens.

Family and domain databases

InterPro

IPR010548. BNIP3.
[Graphical view]

KO

K15464.

Pfam

PF06553. BNIP3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

2708.

SOURCE

Search...

Entry information

Entry name

BNIP3_HUMAN

Accession

Primary (citable) accession number: Q12983
Secondary accession number(s): O14620, Q96GP0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	May 10, 2002
Last modified:	January 25, 2012
This is version 114 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.