BCL2/adenovirus E1B 19 kDa protein-interacting protein 3-like

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Reviewed, UniProtKB/Swiss-Prot O60238 (BNI3L_HUMAN)

Last modified November 25, 2008. Version 75. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    BCL2/adenovirus E1B 19 kDa protein-interacting protein 3-like
Alternative name(s):
    NIP3-like protein X
      Short name=NIP3L
    BCL2/adenovirus E1B 19 kDa protein-interacting protein 3A
    Adenovirus E1B19K-binding protein B5

Gene names

Name:	BNIP3L
Synonyms:	BNIP3A, BNIP3H, NIX

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

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Protein attributes

Sequence length	219 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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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. May function as a tumor suppressor. Inhibits apoptosis induced by BNIP3.
Subunit structure	Self-associates. Interacts with BNIP3 and STEAP3. Interacts with human adenovirus-2 E1B 19 kDa protein.
Subcellular location	Nucleus envelope. Endoplasmic reticulum. Mitochondrion. Membrane; Single-pass membrane proteinPotential.
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.

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Ontologies

Keywords
Biological process	Apoptosis Host-virus interaction
Cellular component	Endoplasmic reticulum Membrane Mitochondrion Nucleus
Domain	Transmembrane
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	defense response to virus Inferred from direct assay. Source: UniProtKB induction of apoptosis Inferred from direct assay. Source: UniProtKB interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of survival gene product expression Inferred from direct assay. Source: UniProtKB
Cellular component	endoplasmic reticulum Ref.4 Inferred from direct assay. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: InterPro mitochondrial envelope Inferred from electronic annotation. Source: InterPro nuclear envelope Ref.4 Inferred from direct assay. Source: UniProtKB
Molecular function	lamin binding Ref.4 Inferred from direct assay. Source: UniProtKB protein heterodimerization activity Ref.4 Inferred from direct assay. Source: UniProtKB protein homodimerization activity Ref.4 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		1	EBI-849893,EBI-849893
BAD	Q92934	1	EBI-849893,EBI-700771
BCL2	P10415	1	EBI-849893,EBI-77694
BNIP3	Q12983	1	EBI-849893,EBI-749464
E1B	P03247	3	EBI-849893,EBI-849856	From a different organism.

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 219

219

BCL2/adenovirus E1B 19 kDa protein-interacting protein 3-like

PRO_0000064957

Regions

Transmembrane

188 – 208

Potential

Amino acid modifications

Modified residue

Phosphoserine By similarity

Modified residue

Phosphoserine By similarity

Modified residue

117

Phosphoserine By similarity

Modified residue

120

Phosphoserine

Experimental info

Sequence conflict

107

D → E in AAN04051. Ref.4

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Sequences

Sequence

Length

Mass (Da)

Tools

O60238-1 [UniParc].

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

219

23,930

        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

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References

	« Hide 'large scale' referencesShow '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: 9523198] [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: 9867803] [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: 10381623] [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: 12663450] [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 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: Bone marrow and Cervix.
[9]	"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: 12606722] [Abstract] Cited for: INTERACTION WITH STEAP3.
[10]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, MASS SPECTROMETRY. Tissue: Epithelium.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	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. BC001559 mRNA. Translation: AAH01559.1. BC009603 mRNA. Translation: AAH09603.1.
PIR	T34523.
RefSeq	NP_004322.1.
UniGene	Hs.131226
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	O60238.
PTM databases
PhosphoSite	O60238.
Genome annotation databases
Ensembl	ENSG00000104765. Homo sapiens. [Contig view]
GeneID	665.
KEGG	hsa:665.
Organism-specific databases
H-InvDB	HIX0007401.
HGNC	HGNC:1085. BNIP3L.
HPA	HPA015652.
MIM	605368. gene.
PharmGKB	PA25395.
GenAtlas	Search...
GeneCards	Search...
Phylogenomic databases
HOVERGEN	O60238.
Gene expression databases
ArrayExpress	O60238.
CleanEx	HS_BNIP3L.
GermOnline	ENSG00000104765. Homo sapiens.
Family and domain databases
InterPro	IPR010548. BNIP3. [Graphical view]
Pfam	PF06553. BNIP3. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	2712.
SOURCE	Search...

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Entry information

Entry name

BNI3L_HUMAN

Accession

Primary (citable) accession number: O60238
Secondary accession number(s): Q8NF87

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	August 1, 1998
Last modified:	November 25, 2008
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 8

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

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents