BCL2/adenovirus E1B 19 kDa protein-interacting protein 2

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Reviewed, UniProtKB/Swiss-Prot Q12982 (BNIP2_HUMAN)

Last modified January 19, 2010. Version 81. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · 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 2

Gene names

Name:	BNIP2
Synonyms:	NIP2

Organism

Homo sapiens (Human) [Complete proteome]

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	314 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Implicated in the suppression of cell death. Interacts with the BCL-2 and adenovirus E1B 19 kDa proteins.
Subcellular location	Cytoplasm. Cytoplasm › perinuclear region. Note: Localizes to the nuclear envelope region and to other cytoplasmic structures.
Sequence similarities	Contains 1 CRAL-TRIO domain.

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Ontologies

Keywords
Biological process	Apoptosis
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	anti-apoptosis Ref.1 Traceable author statement. Source: UniProtKB apoptosis Ref.1 Inferred from physical interaction. Source: MGI
Cellular component	nuclear envelope Ref.1 Inferred from direct assay. Source: UniProtKB perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	GTPase activator activity Traceable author statement. Source: ProtInc calcium ion binding Ref.1 Traceable author statement. Source: UniProtKB protein binding Ref.1 Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 314

314

BCL2/adenovirus E1B 19 kDa protein-interacting protein 2

PRO_0000064961

Regions

Domain

147 – 304

158

CRAL-TRIO

Amino acid modifications

Modified residue

114

Phosphoserine Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9

Modified residue

116

Phosphothreonine Ref.5

Natural variations

Natural variant

S → T: dbSNP rs6151509. Ref.2

VAR_018837

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Sequences

Sequence

Length

Mass (Da)

Tools

Q12982-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 0A3CEC636569DD2F
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FASTA

314

36,018

        10         20         30         40         50         60 
MEGVELKEEW QDEDFPIPLP EDDSIEADIL AITGPEDQPG SLEVNGNKVR KKLMAPDISL 

        70         80         90        100        110        120 
TLDPSDGSVL SDDLDESGEI DLDGLDTPSE NSNEFEWEDD LPKPKTTEVI RKGSITEYTA 

       130        140        150        160        170        180 
AEEKEDGRRW RMFRIGEQDH RVDMKAIEPY KKVISHGGYY GDGLNAIVVF AVCFMPESSQ 

       190        200        210        220        230        240 
PNYRYLMDNL FKYVIGTLEL LVAENYMIVY LNGATTRRKM PSLGWLRKCY QQIDRRLRKN 

       250        260        270        280        290        300 
LKSLIIVHPS WFIRTLLAVT RPFISSKFSQ KIRYVFNLAE LAELVPMEYV GIPECIKQVD 

       310 
QELNGKQDEP KNEQ

« Hide

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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].
[2]	NIEHS SNPs program Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT THR-24.
[3]	"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: Eye.
[4]	"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-114, MASS SPECTROMETRY.
[5]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114 AND THR-116, MASS SPECTROMETRY. Tissue: Platelet.
[6]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, MASS SPECTROMETRY.
[7]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, MASS SPECTROMETRY.
[8]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, MASS SPECTROMETRY.
[9]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, MASS SPECTROMETRY. Tissue: T-cell.
+	Additional computationally mapped references.

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Web resources

NIEHS-SNPs

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Cross-references

Sequence databases
EMBL GenBank DDBJ	U15173 mRNA. Translation: AAC00021.1. AY268590 Genomic DNA. Translation: AAP03429.1. BC002461 mRNA. Translation: AAH02461.1.
IPI	IPI00937973.
PIR	I38864.
RefSeq	NP_004321.2.
UniGene	Hs.646490
3D structure databases
SMR	Q12982. Positions 143-308.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q12982. 4 interactions.
STRING	Q12982.
PTM databases
PhosphoSite	Q12982.
Proteomic databases
PRIDE	Q12982.
Genome annotation databases
Ensembl	ENST00000267859; ENSP00000267859; ENSG00000140299; Homo sapiens. [Genome view] ENST00000409352; ENSP00000386585; ENSG00000140299; Homo sapiens. [Genome view] ENST00000415213; ENSP00000412767; ENSG00000140299; Homo sapiens. [Genome view]
GeneID	663.
KEGG	hsa:663.
UCSC	uc010bgg.1. human.
Organism-specific databases
CTD	663.
GeneCards	GC15M057742.
H-InvDB	HIX0012297.
HGNC	HGNC:1083. BNIP2.
HPA	HPA026843.
MIM	603292. gene.
PharmGKB	PA25393.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG16288.
HOGENOM	HBG445458.
HOVERGEN	Q12982.
InParanoid	Q12982.
PhylomeDB	Q12982.
Gene expression databases
ArrayExpress	Q12982.
Bgee	Q12982.
CleanEx	HS_BNIP2.
Genevestigator	Q12982.
GermOnline	ENSG00000140299. Homo sapiens.
Family and domain databases
InterPro	IPR001251. CRAL_bd_TRIO_C. [Graphical view]
Gene3D	G3DSA:3.40.525.10. CRAL_bd_TRIO_C. 1 hit.
Pfam	PF00650. CRAL_TRIO. 1 hit. [Graphical view]
SMART	SM00516. SEC14. 1 hit. [Graphical view]
PROSITE	PS50191. CRAL_TRIO. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	2704.
SOURCE	Search...

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Entry information

Entry name

BNIP2_HUMAN

Accession

Primary (citable) accession number: Q12982

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	November 1, 1996
Last modified:	January 19, 2010
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.

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Relevant documents

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

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

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents