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Protein

BCL2/adenovirus E1B 19 kDa protein-interacting protein 2

Gene

BNIP2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Implicated in the suppression of cell death. Interacts with the BCL-2 and adenovirus E1B 19 kDa proteins.

GO - Molecular functioni

  • calcium ion binding Source: UniProtKB
  • GTPase activator activity Source: ProtInc
  • identical protein binding Source: GO_Central

GO - Biological processi

  • apoptotic process Source: MGI
  • muscle cell differentiation Source: Reactome
  • negative regulation of apoptotic process Source: UniProtKB
  • positive regulation of GTPase activity Source: GOC
  • positive regulation of muscle cell differentiation Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Apoptosis

Enzyme and pathway databases

ReactomeiREACT_21402. CDO in myogenesis.

Names & Taxonomyi

Protein namesi
Recommended name:
BCL2/adenovirus E1B 19 kDa protein-interacting protein 2
Gene namesi
Name:BNIP2
Synonyms:NIP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:1083. BNIP2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • cytosol Source: GO_Central
  • intracellular membrane-bounded organelle Source: UniProtKB
  • nuclear envelope Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25393.

Polymorphism and mutation databases

BioMutaiBNIP2.
DMDMi6093506.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 314314BCL2/adenovirus E1B 19 kDa protein-interacting protein 2PRO_0000064961Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei41 – 411Phosphoserine1 Publication
Modified residuei77 – 771Phosphoserine1 Publication
Modified residuei87 – 871Phosphothreonine1 Publication
Modified residuei89 – 891Phosphoserine1 Publication
Modified residuei92 – 921Phosphoserine1 Publication
Modified residuei114 – 1141Phosphoserine4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ12982.
PaxDbiQ12982.
PRIDEiQ12982.

PTM databases

PhosphoSiteiQ12982.

Expressioni

Gene expression databases

BgeeiQ12982.
CleanExiHS_BNIP2.
ExpressionAtlasiQ12982. baseline and differential.
GenevisibleiQ12982. HS.

Organism-specific databases

HPAiHPA026843.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
B2R9H73EBI-752094,EBI-10175711
FATE1Q969F03EBI-752094,EBI-743099
FRKP426854EBI-752094,EBI-1383583
KLC1Q078663EBI-752094,EBI-721019
MYO5BQ9ULV05EBI-752094,EBI-311356

Protein-protein interaction databases

BioGridi107131. 18 interactions.
IntActiQ12982. 11 interactions.
MINTiMINT-1446815.
STRINGi9606.ENSP00000267859.

Structurei

3D structure databases

ProteinModelPortaliQ12982.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini147 – 304158CRAL-TRIOPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 CRAL-TRIO domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG146204.
GeneTreeiENSGT00420000029688.
HOGENOMiHOG000230952.
HOVERGENiHBG054692.
InParanoidiQ12982.
KOiK18448.
OMAiLNGKQEQ.
PhylomeDBiQ12982.

Family and domain databases

Gene3Di3.40.525.10. 1 hit.
InterProiIPR022181. Bcl2-/adenovirus-E1B.
IPR001251. CRAL-TRIO_dom.
[Graphical view]
PfamiPF12496. BNIP2. 1 hit.
PF13716. CRAL_TRIO_2. 1 hit.
[Graphical view]
SMARTiSM00516. SEC14. 1 hit.
[Graphical view]
SUPFAMiSSF52087. SSF52087. 1 hit.
PROSITEiPS50191. CRAL_TRIO. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q12982-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MEGVELKEEW QDEDFPIPLP EDDSIEADIL AITGPEDQPG SLEVNGNKVR
60 70 80 90 100
KKLMAPDISL TLDPSDGSVL SDDLDESGEI DLDGLDTPSE NSNEFEWEDD
110 120 130 140 150
LPKPKTTEVI RKGSITEYTA AEEKEDGRRW RMFRIGEQDH RVDMKAIEPY
160 170 180 190 200
KKVISHGGYY GDGLNAIVVF AVCFMPESSQ PNYRYLMDNL FKYVIGTLEL
210 220 230 240 250
LVAENYMIVY LNGATTRRKM PSLGWLRKCY QQIDRRLRKN LKSLIIVHPS
260 270 280 290 300
WFIRTLLAVT RPFISSKFSQ KIRYVFNLAE LAELVPMEYV GIPECIKQVD
310
QELNGKQDEP KNEQ
Length:314
Mass (Da):36,018
Last modified:November 1, 1996 - v1
Checksum:i0A3CEC636569DD2F
GO
Isoform 2 (identifier: Q12982-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MEPCPSSAPPPFYPGVGEVAGLRWFSIYDQRPSWYRTKKLGLLDIGSLDYQEFVVDIESRLRM

Show »
Length:376
Mass (Da):43,135
Checksum:i993DE21B8DF0D556
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti175 – 1751M → T in BAG61556 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti24 – 241S → T.1 Publication
Corresponds to variant rs6151509 [ dbSNP | Ensembl ].
VAR_018837

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MEPCPSSAPPPFYPGVGEVA GLRWFSIYDQRPSWYRTKKL GLLDIGSLDYQEFVVDIESR LRM in isoform 2. 1 PublicationVSP_038964

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U15173 mRNA. Translation: AAC00021.1.
AK299628 mRNA. Translation: BAG61556.1.
AY268590 Genomic DNA. Translation: AAP03429.1.
AC092755 Genomic DNA. No translation available.
BC002461 mRNA. Translation: AAH02461.1.
PIRiI38864.
RefSeqiNP_004321.2. NM_004330.2.
UniGeneiHs.592515.
Hs.646490.

Genome annotation databases

EnsembliENST00000415213; ENSP00000412767; ENSG00000140299. [Q12982-2]
ENST00000607373; ENSP00000475320; ENSG00000140299. [Q12982-1]
GeneIDi663.
KEGGihsa:663.
UCSCiuc010uhb.2. human. [Q12982-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U15173 mRNA. Translation: AAC00021.1.
AK299628 mRNA. Translation: BAG61556.1.
AY268590 Genomic DNA. Translation: AAP03429.1.
AC092755 Genomic DNA. No translation available.
BC002461 mRNA. Translation: AAH02461.1.
PIRiI38864.
RefSeqiNP_004321.2. NM_004330.2.
UniGeneiHs.592515.
Hs.646490.

3D structure databases

ProteinModelPortaliQ12982.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107131. 18 interactions.
IntActiQ12982. 11 interactions.
MINTiMINT-1446815.
STRINGi9606.ENSP00000267859.

PTM databases

PhosphoSiteiQ12982.

Polymorphism and mutation databases

BioMutaiBNIP2.
DMDMi6093506.

Proteomic databases

MaxQBiQ12982.
PaxDbiQ12982.
PRIDEiQ12982.

Protocols and materials databases

DNASUi663.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000415213; ENSP00000412767; ENSG00000140299. [Q12982-2]
ENST00000607373; ENSP00000475320; ENSG00000140299. [Q12982-1]
GeneIDi663.
KEGGihsa:663.
UCSCiuc010uhb.2. human. [Q12982-2]

Organism-specific databases

CTDi663.
GeneCardsiGC15M059951.
H-InvDBHIX0012296.
HGNCiHGNC:1083. BNIP2.
HPAiHPA026843.
MIMi603292. gene.
neXtProtiNX_Q12982.
PharmGKBiPA25393.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG146204.
GeneTreeiENSGT00420000029688.
HOGENOMiHOG000230952.
HOVERGENiHBG054692.
InParanoidiQ12982.
KOiK18448.
OMAiLNGKQEQ.
PhylomeDBiQ12982.

Enzyme and pathway databases

ReactomeiREACT_21402. CDO in myogenesis.

Miscellaneous databases

GeneWikiiBNIP2.
GenomeRNAii663.
NextBioi2704.
PROiQ12982.
SOURCEiSearch...

Gene expression databases

BgeeiQ12982.
CleanExiHS_BNIP2.
ExpressionAtlasiQ12982. baseline and differential.
GenevisibleiQ12982. HS.

Family and domain databases

Gene3Di3.40.525.10. 1 hit.
InterProiIPR022181. Bcl2-/adenovirus-E1B.
IPR001251. CRAL-TRIO_dom.
[Graphical view]
PfamiPF12496. BNIP2. 1 hit.
PF13716. CRAL_TRIO_2. 1 hit.
[Graphical view]
SMARTiSM00516. SEC14. 1 hit.
[Graphical view]
SUPFAMiSSF52087. SSF52087. 1 hit.
PROSITEiPS50191. CRAL_TRIO. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Brain.
  3. NIEHS SNPs program
    Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT THR-24.
  4. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(2006) [PubMed] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Eye.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  7. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  11. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; SER-77; THR-87; SER-89; SER-92 AND SER-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiBNIP2_HUMAN
AccessioniPrimary (citable) accession number: Q12982
Secondary accession number(s): B4DS94
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1996
Last modified: June 24, 2015
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.