Q12982 (BNIP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	314 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Cytoplasm › perinuclear region. Note: Localizes to the nuclear envelope region and to other cytoplasmic structures.
Sequence similarities	Contains 1 CRAL-TRIO domain.

Ontologies

Keywords
Biological process	Apoptosis
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from physical interaction Ref.1. Source: MGI muscle cell differentiation Traceable author statement. Source: Reactome negative regulation of apoptotic process Traceable author statement Ref.1. Source: UniProtKB positive regulation of muscle cell differentiation Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome nuclear envelope Inferred from direct assay Ref.1. Source: UniProtKB perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	GTPase activator activity Traceable author statement PubMed 10799524. Source: ProtInc calcium ion binding Traceable author statement Ref.1. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q12982-1)

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.

Isoform 2 (identifier: Q12982-2)

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

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	1	Phosphoserine Ref.8 Ref.9 Ref.11
Natural variations
	Alternative sequence	1	1	M → MEPCPSSAPPPFYPGVGEVA GLRWFSIYDQRPSWYRTKKL GLLDIGSLDYQEFVVDIESR LRM in isoform 2.		VSP_038964
	Natural variant	24	1	S → T. Ref.3 Corresponds to variant rs6151509 [ dbSNP | Ensembl ].		VAR_018837
Experimental info
	Sequence conflict	175	1	M → T in BAG61556. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 0A3CEC636569DD2F	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
	Isoform 2 [UniParc]. Checksum: 993DE21B8DF0D556	FASTA	376	43,135
	10 20 30 40 50 60 MEPCPSSAPP PFYPGVGEVA GLRWFSIYDQ RPSWYRTKKL GLLDIGSLDY QEFVVDIESR 70 80 90 100 110 120 LRMEGVELKE EWQDEDFPIP LPEDDSIEAD ILAITGPEDQ PGSLEVNGNK VRKKLMAPDI 130 140 150 160 170 180 SLTLDPSDGS VLSDDLDESG EIDLDGLDTP SENSNEFEWE DDLPKPKTTE VIRKGSITEY 190 200 210 220 230 240 TAAEEKEDGR RWRMFRIGEQ DHRVDMKAIE PYKKVISHGG YYGDGLNAIV VFAVCFMPES 250 260 270 280 290 300 SQPNYRYLMD NLFKYVIGTL ELLVAENYMI VYLNGATTRR KMPSLGWLRK CYQQIDRRLR 310 320 330 340 350 360 KNLKSLIIVH PSWFIRTLLA VTRPFISSKF SQKIRYVFNL AELAELVPME YVGIPECIKQ 370 VDQELNGKQD EPKNEQ

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] [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]	"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] [Europe PMC] [Abstract] 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]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[10]	"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.
[11]	"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, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00030399. IPI00943060.
PIR	I38864.
RefSeq	NP_004321.2. NM_004330.2.
UniGene	Hs.646490.
3D structure databases
ProteinModelPortal	Q12982.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q12982. 6 interactions.
MINT	MINT-1446815.
STRING	9606.ENSP00000267859.
PTM databases
PhosphoSite	Q12982.
Polymorphism databases
DMDM	6093506.
Proteomic databases
PaxDb	Q12982.
PRIDE	Q12982.
Protocols and materials databases
DNASU	663.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000415213; ENSP00000412767; ENSG00000140299.
GeneID	663.
KEGG	hsa:663.
UCSC	uc010uhb.2. human.
Organism-specific databases
CTD	663.
GeneCards	GC15M059951.
H-InvDB	HIX0012296.
HGNC	HGNC:1083. BNIP2.
HPA	HPA026843.
MIM	603292. gene.
neXtProt	NX_Q12982.
PharmGKB	PA25393.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG146204.
HOGENOM	HOG000230952.
HOVERGEN	HBG054692.
InParanoid	Q12982.
OMA	LNGKQEQ.
OrthoDB	EOG4TF0K8.
PhylomeDB	Q12982.
Enzyme and pathway databases
Reactome	REACT_111045. Developmental Biology.
Gene expression databases
ArrayExpress	Q12982.
Bgee	Q12982.
CleanEx	HS_BNIP2.
Genevestigator	Q12982.
GermOnline	ENSG00000140299. Homo sapiens.
Family and domain databases
Gene3D	3.40.525.10. 1 hit.
InterPro	IPR022181. Bcl2-/adenovirus-E1B. IPR001251. CRAL-TRIO_dom. [Graphical view]
Pfam	PF12496. BNIP2. 1 hit. [Graphical view]
SMART	SM00516. SEC14. 1 hit. [Graphical view]
SUPFAM	SSF52087. CRAL_TRIO_C. 1 hit.
PROSITE	PS50191. CRAL_TRIO. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	663.
NextBio	2704.
SOURCE	Search...

Entry information

Entry name

BNIP2_HUMAN

Accession

Primary (citable) accession number: Q12982
Secondary accession number(s): B4DS94

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	November 1, 1996
Last modified:	April 3, 2013
This is version 112 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.