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O60238 (BNI3L_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
BCL2/adenovirus E1B 19 kDa protein-interacting protein 3-like
Alternative name(s):
Adenovirus E1B19K-binding protein B5
BCL2/adenovirus E1B 19 kDa protein-interacting protein 3A
NIP3-like protein X
Short name=NIP3L
Gene names
Name:BNIP3L
Synonyms:BNIP3A, BNIP3H, NIX
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length219 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Induces apoptosis. Interacts with viral and cellular anti-apoptosis proteins. Can overcome the suppressors BCL-2 and BCL-XL, although high levels of BCL-XL expression will inhibit apoptosis. Inhibits apoptosis induced by BNIP3. 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. May function as a tumor suppressor. Ref.4 Ref.13

Subunit structure

Self-associates. Interacts with BNIP3 and STEAP3. Interacts with human adenovirus-2 E1B 19 kDa protein. Interacts (via BH3 domain) with SPATA18 (via coiled-coil domains). Ref.4 Ref.10 Ref.13

Subcellular location

Nucleus envelope. Endoplasmic reticulum. Mitochondrion outer membrane. Membrane; Single-pass membrane protein Potential. Note: Colocalizes with SPATA18 at the mitochondrion outer membrane. Ref.4 Ref.13

Post-translational modification

Undergoes progressive proteolysis to an 11 kDa C-terminal fragment, which is blocked by the proteasome inhibitor lactacystin.

Sequence similarities

Belongs to the NIP3 family.

Sequence caution

The sequence CAI46217.1 differs from that shown. Reason: Erroneous termination at position 122. Translated as Glu.

Ontologies

Keywords
   Biological processApoptosis
Host-virus interaction
   Cellular componentEndoplasmic reticulum
Membrane
Mitochondrion
Mitochondrion outer membrane
Nucleus
   DomainTransmembrane
Transmembrane helix
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processdefense response to virus

Inferred from direct assay PubMed 9973195. Source: UniProtKB

mitochondrial outer membrane permeabilization

Inferred from Biological aspect of Ancestor. Source: RefGenome

mitochondrial protein catabolic process

Inferred from mutant phenotype Ref.13. Source: UniProtKB

negative regulation of apoptotic process

Inferred from direct assay Ref.4. Source: UniProtKB

positive regulation of apoptotic process

Inferred from direct assay PubMed 9973195. Source: UniProtKB

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentendoplasmic reticulum

Inferred from direct assay Ref.4. Source: UniProtKB

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

intrinsic component of membrane

Traceable author statement Ref.4. Source: UniProtKB

mitochondrial outer membrane

Inferred from mutant phenotype Ref.13. Source: UniProtKB

mitochondrion

Inferred from direct assay Ref.4PubMed 9973195. Source: UniProtKB

nuclear envelope

Inferred from direct assay Ref.4. Source: UniProtKB

   Molecular_functionidentical protein binding

Inferred from physical interaction Ref.4PubMed 16189514PubMed 21516116. Source: IntAct

lamin binding

Inferred from direct assay Ref.4. Source: UniProtKB

protein heterodimerization activity

Inferred from direct assay Ref.4. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay Ref.4. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 219219BCL2/adenovirus E1B 19 kDa protein-interacting protein 3-like
PRO_0000064957

Regions

Transmembrane188 – 20821Helical; Potential
Motif126 – 14823BH3

Amino acid modifications

Modified residue621Phosphoserine By similarity
Modified residue1171Phosphoserine By similarity
Modified residue1181Phosphoserine By similarity
Modified residue1201Phosphoserine Ref.12

Experimental info

Sequence conflict1071D → E in AAN04051. Ref.4
Sequence conflict1501N → S in CAI46217. Ref.8

Sequences

Sequence LengthMass (Da)Tools
O60238 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 19372E897BC63609

FASTA21923,930
        10         20         30         40         50         60 
MSSHLVEPPP PLHNNNNNCE ENEQSLPPPA GLNSSWVELP MNSSNGNDNG NGKNGGLEHV 

        70         80         90        100        110        120 
PSSSSIHNGD MEKILLDAQH ESGQSSSRGS SHCDSPSPQE DGQIMFDVEM HTSRDHSSQS 

       130        140        150        160        170        180 
EEEVVEGEKE VEALKKSADW VSDWSSRPEN IPPKEFHFRH PKRSVSLSMR KSGAMKKGGI 

       190        200        210 
FSAEFLKVFI PSLFLSHVLA LGLGIYIGKR LSTPSASTY 

« Hide

References

« Hide 'large scale' references
[1]"Isolation, mapping, and functional analysis of a novel human cDNA (BNIP3L) encoding a protein homologous to human NIP3."
Matsushima M., Fujiwara T., Takahashi E., Minaguchi T., Eguchi Y., Tsujimoto Y., Suzumori K., Nakamura Y.
Genes Chromosomes Cancer 21:230-235(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"BNIP3a, a human homolog of pro-apoptotic protein BNIP3, promotes apoptosis and interacts with viral and cellular anti-apoptosis proteins."
Yasuda M., Han J.-W., Dionne C.A., Boyd J.M., Chinnadurai G.
Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Nix and Nip3 form a subfamily of pro-apoptotic mitochondrial proteins."
Chen G., Cizeau J., Vande Velde C., Park J.H., Bozek G., Bolton J., Shi L., Dubik D., Greenberg A.
J. Biol. Chem. 274:7-10(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Fetal liver.
[4]"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: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, SELF-ASSOCIATION, INTERACTION WITH BNIP3 AND HUMAN ADENOVIRUS-2 E1B 19 KDA PROTEIN.
[5]"The proapoptotic factor Nix is coexpressed with Bcl-xL during terminal erythroid differentiation."
Aerbajinai W., Giattina M., Lee Y.T., Raffeld M., Miller J.L.
Blood 102:712-717(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[6]"A catalog of genes in the human dermal papilla cells as identified by expressed sequence tags."
Farooq M., Kim M.K., Kim Y.H., Seo J.M., Lee H.M., Sohn M.Y., Hwang S.Y., Chung H.J., Im S.U., Jung E.J., Kim J.C.
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Hair follicle dermal papilla.
[7]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[8]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
[9]"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: Bone marrow and Cervix.
[10]"The p53-inducible TSAP6 gene product regulates apoptosis and the cell cycle and interacts with Nix and the Myt1 kinase."
Passer B.J., Nancy-Portebois V., Amzallag N., Prieur S., Cans C., Roborel de Climens A., Fiucci G., Bouvard V., Tuynder M., Susini L., Morchoisne S., Crible V., Lespagnol A., Dausset J., Oren M., Amson R., Telerman A.
Proc. Natl. Acad. Sci. U.S.A. 100:2284-2289(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH STEAP3.
[11]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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-120, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Mieap, a p53-inducible protein, controls mitochondrial quality by repairing or eliminating unhealthy mitochondria."
Kitamura N., Nakamura Y., Miyamoto Y., Miyamoto T., Kabu K., Yoshida M., Futamura M., Ichinose S., Arakawa H.
PLoS ONE 6:E16060-E16060(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SPATA18, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB004788 mRNA. Translation: BAA28692.1.
AF079221 mRNA. Translation: AAC27723.1.
AF067396 mRNA. Translation: AAD03589.1.
AF536326 mRNA. Translation: AAN04051.1.
AF452712 mRNA. Translation: AAL50978.1.
AF255051 Genomic DNA. Translation: AAF70290.1.
BT019501 mRNA. Translation: AAV38308.1.
AL132665 mRNA. Translation: CAI46217.1. Sequence problems.
BC001559 mRNA. Translation: AAH01559.1.
BC009603 mRNA. Translation: AAH09603.1.
PIRT34523.
RefSeqNP_004322.1. NM_004331.2.
UniGeneHs.131226.

3D structure databases

ProteinModelPortalO60238.
SMRO60238. Positions 178-212.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107133. 26 interactions.
IntActO60238. 28 interactions.
MINTMINT-1429960.
STRING9606.ENSP00000370003.

Protein family/group databases

TCDB1.A.20.1.2. the bcl2/adenovirus e1b-interacting protein 3 (bnip3) family.

PTM databases

PhosphoSiteO60238.

Proteomic databases

PaxDbO60238.
PRIDEO60238.

Protocols and materials databases

DNASU665.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000380629; ENSP00000370003; ENSG00000104765.
GeneID665.
KEGGhsa:665.
UCSCuc003xex.1. human.

Organism-specific databases

CTD665.
GeneCardsGC08P026240.
HGNCHGNC:1085. BNIP3L.
HPACAB025371.
HPA015652.
MIM605368. gene.
neXtProtNX_O60238.
PharmGKBPA25395.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG83470.
HOVERGENHBG050707.
InParanoidO60238.
KOK15465.
OMAMVGGLEH.
OrthoDBEOG74N5J4.
PhylomeDBO60238.
TreeFamTF315424.

Gene expression databases

ArrayExpressO60238.
BgeeO60238.
CleanExHS_BNIP3L.
GenevestigatorO60238.

Family and domain databases

InterProIPR010548. BNIP3.
[Graphical view]
PfamPF06553. BNIP3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSBNIP3L. human.
GeneWikiBNIP3L.
GenomeRNAi665.
NextBio2712.
PROO60238.
SOURCESearch...

Entry information

Entry nameBNI3L_HUMAN
AccessionPrimary (citable) accession number: O60238
Secondary accession number(s): Q5JW63, Q8NF87
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: August 1, 1998
Last modified: April 16, 2014
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM