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Q12982

- BNIP2_HUMAN

UniProt

Q12982 - BNIP2_HUMAN

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Protein
BCL2/adenovirus E1B 19 kDa protein-interacting protein 2
Gene
BNIP2, NIP2
Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. GTPase activator activity Source: ProtInc
  2. calcium ion binding Source: UniProtKB
  3. identical protein binding Source: RefGenome
  4. protein binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. apoptotic process Source: MGI
  2. muscle cell differentiation Source: Reactome
  3. negative regulation of apoptotic process Source: UniProtKB
  4. positive regulation of GTPase activity Source: GOC
  5. 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: Chromosome 15

Organism-specific databases

HGNCiHGNC:1083. BNIP2.

Subcellular locationi

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

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. cytosol Source: RefGenome
  3. intracellular membrane-bounded organelle Source: UniProtKB
  4. nuclear envelope Source: UniProtKB
  5. perinuclear region of cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25393.

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei114 – 1141Phosphoserine3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ12982.
PaxDbiQ12982.
PRIDEiQ12982.

PTM databases

PhosphoSiteiQ12982.

Expressioni

Gene expression databases

ArrayExpressiQ12982.
BgeeiQ12982.
CleanExiHS_BNIP2.
GenevestigatoriQ12982.

Organism-specific databases

HPAiHPA026843.

Interactioni

Protein-protein interaction databases

BioGridi107131. 11 interactions.
IntActiQ12982. 7 interactions.
MINTiMINT-1446815.
STRINGi9606.ENSP00000267859.

Structurei

3D structure databases

ProteinModelPortaliQ12982.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini147 – 304158CRAL-TRIO
Add
BLAST

Sequence similaritiesi

Contains 1 CRAL-TRIO domain.

Phylogenomic databases

eggNOGiNOG146204.
HOGENOMiHOG000230952.
HOVERGENiHBG054692.
InParanoidiQ12982.
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. Align

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

MEGVELKEEW QDEDFPIPLP EDDSIEADIL AITGPEDQPG SLEVNGNKVR    50
KKLMAPDISL TLDPSDGSVL SDDLDESGEI DLDGLDTPSE NSNEFEWEDD 100
LPKPKTTEVI RKGSITEYTA AEEKEDGRRW RMFRIGEQDH RVDMKAIEPY 150
KKVISHGGYY GDGLNAIVVF AVCFMPESSQ PNYRYLMDNL FKYVIGTLEL 200
LVAENYMIVY LNGATTRRKM PSLGWLRKCY QQIDRRLRKN LKSLIIVHPS 250
WFIRTLLAVT RPFISSKFSQ KIRYVFNLAE LAELVPMEYV GIPECIKQVD 300
QELNGKQDEP KNEQ 314
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

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.
VSP_038964

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti175 – 1751M → T in BAG61556. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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]

Polymorphism databases

DMDMi6093506.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
PIRi I38864.
RefSeqi NP_004321.2. NM_004330.2.
UniGenei Hs.592515.
Hs.646490.

3D structure databases

ProteinModelPortali Q12982.
ModBasei Search...

Protein-protein interaction databases

BioGridi 107131. 11 interactions.
IntActi Q12982. 7 interactions.
MINTi MINT-1446815.
STRINGi 9606.ENSP00000267859.

PTM databases

PhosphoSitei Q12982.

Polymorphism databases

DMDMi 6093506.

Proteomic databases

MaxQBi Q12982.
PaxDbi Q12982.
PRIDEi Q12982.

Protocols and materials databases

DNASUi 663.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000415213 ; ENSP00000412767 ; ENSG00000140299 . [Q12982-2 ]
ENST00000607373 ; ENSP00000475320 ; ENSG00000140299 . [Q12982-1 ]
GeneIDi 663.
KEGGi hsa:663.
UCSCi uc010uhb.2. human. [Q12982-2 ]

Organism-specific databases

CTDi 663.
GeneCardsi GC15M059951.
H-InvDB HIX0012296.
HGNCi HGNC:1083. BNIP2.
HPAi HPA026843.
MIMi 603292. gene.
neXtProti NX_Q12982.
PharmGKBi PA25393.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG146204.
HOGENOMi HOG000230952.
HOVERGENi HBG054692.
InParanoidi Q12982.
OMAi LNGKQEQ.
PhylomeDBi Q12982.

Enzyme and pathway databases

Reactomei REACT_21402. CDO in myogenesis.

Miscellaneous databases

GeneWikii BNIP2.
GenomeRNAii 663.
NextBioi 2704.
PROi Q12982.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q12982.
Bgeei Q12982.
CleanExi HS_BNIP2.
Genevestigatori Q12982.

Family and domain databases

Gene3Di 3.40.525.10. 1 hit.
InterProi IPR022181. Bcl2-/adenovirus-E1B.
IPR001251. CRAL-TRIO_dom.
[Graphical view ]
Pfami PF12496. BNIP2. 1 hit.
PF13716. CRAL_TRIO_2. 1 hit.
[Graphical view ]
SMARTi SM00516. SEC14. 1 hit.
[Graphical view ]
SUPFAMi SSF52087. SSF52087. 1 hit.
PROSITEi PS50191. CRAL_TRIO. 1 hit.
[Graphical view ]
ProtoNeti Search...

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].

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: September 3, 2014
This is version 123 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

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