Reviewed, UniProtKB/Swiss-Prot Q12983 (BNIP3_HUMAN)

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.
Sequence processing	The displayed sequence is not processed.
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. Also can interact with adenovirus E1B 19 kDa protein or Epstein-Barr virus BHRF1.
Subcellular location	Mitochondrion membrane; Single-pass membrane proteinPotential. Note= Coexpression with the EIB 19-kDa protein results in a shift in NIP3 localization pattern to the nuclear envelope.
Sequence similarities	Belongs to the NIP3 family.

Ontologies

Keywords
Biological process	Apoptosis Host-virus interaction
Cellular component	Membrane Mitochondrion
Domain	Transmembrane
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	DNA fragmentation during apoptosis Inferred from direct assay. Source: UniProtKB chromatin remodeling Inferred from direct assay. Source: UniProtKB defense response to virus Inferred from direct assay. Source: UniProtKB induction of apoptosis Ref.2 Ref.6 Inferred from direct assay. Source: UniProtKB interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of membrane potential Inferred from direct assay. Source: UniProtKB negative regulation of survival gene product expression Inferred from direct assay. Source: UniProtKB neuron apoptosis Inferred from sequence or structural similarity. Source: UniProtKB oxygen and reactive oxygen species metabolic process Inferred from direct assay. Source: UniProtKB regulation of mitochondrial membrane permeability Inferred from direct assay. Source: UniProtKB response to hypoxia Inferred from sequence or structural similarity. 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 Ref.1 Inferred from direct assay. Source: UniProtKB nucleoplasm Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	protein heterodimerization activity Ref.6 Inferred from direct assay. Source: UniProtKB protein homodimerization activity Ref.2 Ref.6 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		1	EBI-749464,EBI-749464
BNIP3L	O60238	1	EBI-749464,EBI-849893
TMEM11	P17152	1	EBI-749464,EBI-749474

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

Potential

Amino acid modifications

Modified residue

86

1

Phosphoserine By similarity

Modified residue

92

1

Phosphoserine By similarity

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)
	Q12983-1 [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, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu)." Livingston R.J., Rieder M.J., Rajkumar N., Downing T.K., Olson A.N., Nguyen C.P., Gildersleeve H., Cassidy C.M., Johnson E.J., Swanson J.E., McFarland I., Yool B., Park C., Nickerson D.A. 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.

PIR

I38865.

RefSeq

NP_004043.2.

UniGene

Hs.144873

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2J5D	NMR	-	A/B	146-190	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q12983.

PTM databases

PhosphoSite

Q12983.

Polymorphism databases

NIEHS-SNPs

Search...

Genome annotation databases

Ensembl

ENSG00000176171. Homo sapiens. [Contig view]

GeneID

664.

KEGG

hsa:664.

Organism-specific databases

H-InvDB

HIX0020971.
HIX0037770.

HGNC

HGNC:1084. BNIP3.

HPA

CAB011676.
HPA003015.

MIM

603293. gene.

PharmGKB

PA25394.

GenAtlas

Search...

GeneCards

Search...

Phylogenomic databases

HOVERGEN

Q12983.

Gene expression databases

CleanEx

HS_BNIP3.

GermOnline

ENSG00000176171. Homo sapiens.

Family and domain databases

InterPro

IPR010548. BNIP3.
[Graphical view]

Pfam

PF06553. BNIP3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

LinkHub

Q12983.

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:	November 25, 2008
This is version 82 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)