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Reviewed, UniProtKB/Swiss-Prot Q12982 (BNIP2_HUMAN)

Last modified July 22, 2008. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    BCL2/adenovirus E1B 19 kDa protein-interacting protein 2
Gene names
Name: BNIP2
Synonyms: NIP2
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length314 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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. Cytoplasmperinuclear region. Note= Localizes to the nuclear envelope region and to other cytoplasmic structures.

Sequence similarities

Contains 1 CRAL-TRIO domain.

Ontologies

Keywords

   Biological processApoptosis
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   PTMPhosphoprotein

Gene Ontology (GO)

   Biological processanti-apoptosis Ref.1

Traceable author statement. Source: UniProtKB

   Cellular componentcytoplasm Ref.1

Inferred from direct assay. Source: MGI

nuclear envelope Ref.1

Inferred from direct assay. Source: UniProtKB

   Molecular functionGTPase 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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Chain1 – 314314BCL2/adenovirus E1B 19 kDa protein-interacting protein 2

Regions

Domain147 – 304158CRAL-TRIO

Amino acid modifications

Modified residue1141Phosphoserine
Modified residue1161Phosphothreonine

Natural variations

Natural variant241S → T: dbSNP rs6151509.

Sequences

Sequence LengthMass (Da)Tools
Q12982-1 [UniParc].

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

FASTA31436,018
        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

References

« Hide '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, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu)."
Rieder M.J., Livingston R.J., Daniels M.R., Chung M.-W., Miyamoto K.E., Nguyen C.P., Nguyen D.A., Poel C.L., Robertson P.D., Schackwitz W.S., Sherwood J.K., Witrak L.A., Nickerson D.A.
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]"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.

Cross-references

Sequence databases

U15173 mRNA. Translation: AAC00021.1.
AY268590 Genomic DNA. Translation: AAP03429.1.
BC002461 mRNA. Translation: AAH02461.1.
PIRI38864.
RefSeqNP_004321.2.
UniGeneHs.646490

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActQ12982.

PTM databases

PhosphoSiteQ12982.

Polymorphism databases

NIEHS-SNPsSearch...

Genome annotation databases

EnsemblENSG00000140299. Homo sapiens. [Contig view]
GeneID663.
KEGGhsa:663.

Organism-specific databases

H-InvDBHIX0012297.
HGNCHGNC:1083. BNIP2.
MIM603292. gene.
PharmGKBPA25393.
GenAtlasSearch...
GeneCardsSearch...
GeneLynxSearch...

Phylogenomic databases

HOGENOMQ12982.
HOVERGENQ12982.

Gene expression databases

ArrayExpressQ12982.
CleanExHS_BNIP2.
GermOnlineENSG00000140299. Homo sapiens.

Family and domain databases

InterProIPR001251. CRAL_bd_TRIO_C.
[Graphical view]
Gene3DG3DSA:3.40.525.10. CRAL_bd_TRIO_C. 1 hit.
SMARTSM00516. SEC14. 1 hit.
[Graphical view]
PROSITEPS50191. CRAL_TRIO. 1 hit.
[Graphical view]
ProDomQ12982.
[Graphical view] [Entries sharing at least one domain]
BLOCKSSearch...

Other Resources

SOURCESearch...
ProtoNetSearch...

Entry information

Entry nameBNIP2_HUMAN
AccessionPrimary (citable) accession number: Q12982
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1996
Last modified: July 22, 2008
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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) · Sequences · References · Cross-references · Entry information · Relevant documents