BNIP2_MOUSE
ID BNIP2_MOUSE Reviewed; 326 AA.
AC O54940; Q8K4H0;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=BCL2/adenovirus E1B 19 kDa protein-interacting protein 2;
GN Name=Bnip2; Synonyms=Nip2l;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Barbosa M.D.F.S., Detter J.C., Kingsmore S.F.;
RT "The mouse Nip2l gene: cloning, sequencing, expression analysis and genetic
RT mapping.";
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=A/J; TISSUE=Heart;
RX PubMed=12089062; DOI=10.1161/01.res.0000024690.69379.5c;
RA Zhang H.M., Yanagawa B., Cheung P., Luo H., Yuan J., Chau D., Wang A.,
RA Bohunek L., Wilson J.E., McManus B.M., Yang D.;
RT "Nip21 gene expression reduces coxsackievirus B3 replication by promoting
RT apoptotic cell death via a mitochondria-dependent pathway.";
RL Circ. Res. 90:1251-1258(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zhou Y.T., Low B.C.;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Implicated in the suppression of cell death. Interacts with
CC the BCL-2 and adenovirus E1B 19 kDa proteins (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear
CC region {ECO:0000250}. Note=Localizes to the nuclear envelope region and
CC to other cytoplasmic structures. {ECO:0000250}.
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DR EMBL; AF035207; AAC04329.1; -; mRNA.
DR EMBL; AF400107; AAM76082.1; -; mRNA.
DR EMBL; AY591758; AAT92040.1; -; mRNA.
DR EMBL; AK054288; BAC35718.1; -; mRNA.
DR EMBL; CH466522; EDL26178.1; -; Genomic_DNA.
DR CCDS; CCDS23319.1; -.
DR RefSeq; NP_058067.2; NM_016787.4.
DR AlphaFoldDB; O54940; -.
DR BioGRID; 198376; 2.
DR STRING; 10090.ENSMUSP00000034754; -.
DR iPTMnet; O54940; -.
DR PhosphoSitePlus; O54940; -.
DR EPD; O54940; -.
DR jPOST; O54940; -.
DR MaxQB; O54940; -.
DR PaxDb; O54940; -.
DR PRIDE; O54940; -.
DR ProteomicsDB; 273790; -.
DR Antibodypedia; 12947; 333 antibodies from 29 providers.
DR DNASU; 12175; -.
DR Ensembl; ENSMUST00000034754; ENSMUSP00000034754; ENSMUSG00000011958.
DR GeneID; 12175; -.
DR KEGG; mmu:12175; -.
DR UCSC; uc009qno.3; mouse.
DR CTD; 663; -.
DR MGI; MGI:109327; Bnip2.
DR VEuPathDB; HostDB:ENSMUSG00000011958; -.
DR eggNOG; ENOG502QUXY; Eukaryota.
DR GeneTree; ENSGT00940000158531; -.
DR InParanoid; O54940; -.
DR OMA; REESRRW; -.
DR TreeFam; TF324164; -.
DR Reactome; R-MMU-525793; Myogenesis.
DR BioGRID-ORCS; 12175; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Bnip2; mouse.
DR PRO; PR:O54940; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; O54940; protein.
DR Bgee; ENSMUSG00000011958; Expressed in ascending aorta and 264 other tissues.
DR ExpressionAtlas; O54940; baseline and differential.
DR Genevisible; O54940; MM.
DR GO; GO:0005814; C:centriole; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISS:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0031616; C:spindle pole centrosome; IDA:MGI.
DR GO; GO:0006915; P:apoptotic process; ISO:MGI.
DR GO; GO:0001824; P:blastocyst development; IMP:MGI.
DR GO; GO:0007098; P:centrosome cycle; IMP:MGI.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:MGI.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IMP:MGI.
DR GO; GO:0051057; P:positive regulation of small GTPase mediated signal transduction; IMP:MGI.
DR GO; GO:0051146; P:striated muscle cell differentiation; IGI:MGI.
DR CDD; cd00170; SEC14; 1.
DR Gene3D; 3.40.525.10; -; 1.
DR InterPro; IPR022181; Bcl2-/adenovirus-E1B.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR Pfam; PF12496; BNIP2; 1.
DR Pfam; PF13716; CRAL_TRIO_2; 1.
DR SMART; SM00516; SEC14; 1.
DR SUPFAM; SSF52087; SSF52087; 1.
DR PROSITE; PS50191; CRAL_TRIO; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..326
FT /note="BCL2/adenovirus E1B 19 kDa protein-interacting
FT protein 2"
FT /id="PRO_0000064962"
FT DOMAIN 147..304
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..29
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12982"
FT MOD_RES 87
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q12982"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12982"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12982"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT CONFLICT 67
FT /note="D -> G (in Ref. 1; AAC04329)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 326 AA; 37769 MW; ED9CA74520E2913B CRC64;
MEGVELKEEW QDEDFPIPLP EDDSIEADTL DGTDPDRQPG SLEVNGNKVR KKLMAPDISL
TLDPGEDSLW SDDLDEAGEV DLEGLDTPSE NSDEFEWEDD LPKPKTTEVI RKGSITEYTA
TEEKGDGRRW RMFRIGEQDH RVDMKAIEPY KKVISHGGYY GDGLNAIVVF AVCFMPESGQ
PNYRYLMDNL FKYVIGTLEL LVAENYMIIY LNGATTRRKM PSLGWLRRCY QQIDRRLRKN
LKSLIIVHPS WFIRTLLAVT RPFISSKFSQ KIRYVFNLAE LAELVPMEYV GIPECIKQYE
EEKFKKRQKR VDQELNGKQE PPKSEQ
