Full text data of ILF3
ILF3
(DRBF, MPHOSPH4, NF90)
[Confidence: low (only semi-automatic identification from reviews)]
Interleukin enhancer-binding factor 3 (Double-stranded RNA-binding protein 76; DRBP76; M-phase phosphoprotein 4; MPP4; Nuclear factor associated with dsRNA; NFAR; Nuclear factor of activated T-cells 90 kDa; NF-AT-90; Translational control protein 80; TCP80)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Interleukin enhancer-binding factor 3 (Double-stranded RNA-binding protein 76; DRBP76; M-phase phosphoprotein 4; MPP4; Nuclear factor associated with dsRNA; NFAR; Nuclear factor of activated T-cells 90 kDa; NF-AT-90; Translational control protein 80; TCP80)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q12906
ID ILF3_HUMAN Reviewed; 894 AA.
AC Q12906; A8K6F2; G5E9M5; O43409; Q6P1X1; Q86XY7; Q99544; Q99545;
read moreAC Q9BZH4; Q9BZH5; Q9NQ95; Q9NQ96; Q9NQ97; Q9NQ98; Q9NQ99; Q9NQA0;
AC Q9NQA1; Q9NQA2; Q9NRN2; Q9NRN3; Q9NRN4; Q9UMZ9; Q9UN00; Q9UN84;
AC Q9UNA2;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 3.
DT 22-JAN-2014, entry version 154.
DE RecName: Full=Interleukin enhancer-binding factor 3;
DE AltName: Full=Double-stranded RNA-binding protein 76;
DE Short=DRBP76;
DE AltName: Full=M-phase phosphoprotein 4;
DE Short=MPP4;
DE AltName: Full=Nuclear factor associated with dsRNA;
DE Short=NFAR;
DE AltName: Full=Nuclear factor of activated T-cells 90 kDa;
DE Short=NF-AT-90;
DE AltName: Full=Translational control protein 80;
DE Short=TCP80;
GN Name=ILF3; Synonyms=DRBF, MPHOSPH4, NF90;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-41;
RP 491-510 AND 555-565, AND FUNCTION.
RC TISSUE=T-cell lymphoma;
RX PubMed=7519613;
RA Kao P.N., Chen L., Brock G., Ng J., Kenny J., Smith A.J., Corthesy B.;
RT "Cloning and expression of cyclosporin A- and FK506-sensitive nuclear
RT factor of activated T-cells: NF45 and NF90.";
RL J. Biol. Chem. 269:20691-20699(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND PROTEIN SEQUENCE OF
RP N-TERMINUS.
RC TISSUE=Cervix carcinoma;
RX PubMed=10400669; DOI=10.1074/jbc.274.29.20432;
RA Patel R.C., Vestal D.J., Xu Z., Bandyopadhyay S., Guo W., Erme S.M.,
RA Williams B.R., Sen G.C.;
RT "DRBP76, a double-stranded RNA-binding nuclear protein, is
RT phosphorylated by the interferon-induced protein kinase, PKR.";
RL J. Biol. Chem. 274:20432-20437(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND CHARACTERIZATION.
RC TISSUE=Liver;
RX PubMed=10607473; DOI=10.1006/mgme.1999.2934;
RA Xu Y.-H., Grabowski G.A.;
RT "Molecular cloning and characterization of a translational inhibitory
RT protein that binds to coding sequences of human acid beta-glucosidase
RT and other mRNAs.";
RL Mol. Genet. Metab. 68:441-454(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2; 4 AND 5), AND
RP ALTERNATIVE SPLICING.
RC TISSUE=Melanoma;
RX PubMed=11167023; DOI=10.1016/S0378-1119(00)00495-9;
RA Duchange N., Pidoux J., Camus E., Sauvaget D.;
RT "Alternative splicing in the human interleukin enhancer binding factor
RT 3 (ILF3) gene.";
RL Gene 261:345-353(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), AND
RP CHARACTERIZATION.
RX PubMed=11438536; DOI=10.1074/jbc.M104207200;
RA Saunders L.R., Perkins D.J., Balachandran S., Michaels R., Ford R.,
RA Mayeda A., Barber G.N.;
RT "Characterization of two evolutionarily conserved, alternatively
RT spliced nuclear phosphoproteins, NFAR-1 and -2, that function in mRNA
RT processing and interact with the double-stranded RNA-dependent protein
RT kinase, PKR.";
RL J. Biol. Chem. 276:32300-32312(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), AND
RP VARIANT HIS-50.
RC TISSUE=T-cell;
RX PubMed=11161820; DOI=10.1006/geno.2000.6423;
RA Saunders L.R., Jurecic V., Barber G.N.;
RT "The 90- and 110-kDa human NFAR proteins are translated from two
RT differentially spliced mRNAs encoded on chromosome 19p13.";
RL Genomics 71:256-259(2001).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RC TISSUE=Duodenum, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-611.
RC TISSUE=Blood, and Cervix;
RX PubMed=8885239; DOI=10.1091/mbc.7.9.1455;
RA Matsumoto-Taniura N., Pirollet F., Monroe R., Gerace L.,
RA Westendorf J.M.;
RT "Identification of novel M phase phosphoproteins by expression
RT cloning.";
RL Mol. Biol. Cell 7:1455-1469(1996).
RN [12]
RP PROTEIN SEQUENCE OF 1-10, FUNCTION, AND INTERACTION WITH XRCC6; PRKDC
RP AND XRCC5.
RX PubMed=9442054; DOI=10.1074/jbc.273.4.2136;
RA Ting N.S.Y., Kao P.N., Chan D.W., Lintott L.G., Lees-Miller S.P.;
RT "DNA-dependent protein kinase interacts with antigen receptor response
RT element binding proteins NF90 and NF45.";
RL J. Biol. Chem. 273:2136-2145(1998).
RN [13]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 188-894 (ISOFORMS 1; 2 AND 3).
RA MacArdle J., Cantarella G.M., Veyrune J.-L., Krasnoselskaya I.,
RA Kumar A.;
RT "Structure and functional characterization of hDRBF gene.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [14]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 587-894 (ISOFORM 1).
RC TISSUE=Brain;
RA Yu W., Sarginson J., Gibbs R.A.;
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [15]
RP INTERACTION WITH ILF2.
RX PubMed=10574923; DOI=10.1074/jbc.274.49.34598;
RA Satoh M., Shaheen V.M., Kao P.N., Okano T., Shaw M., Yoshida H.,
RA Richards H.B., Reeves W.H.;
RT "Autoantibodies define a family of proteins with conserved double-
RT stranded RNA-binding domains as well as DNA binding activity.";
RL J. Biol. Chem. 274:34598-34604(1999).
RN [16]
RP INTERACTION WITH PRMT1.
RX PubMed=10749851; DOI=10.1074/jbc.M000023200;
RA Tang J., Kao P.N., Herschman H.R.;
RT "Protein-arginine methyltransferase I, the predominant protein-
RT arginine methyltransferase in cells, interacts with and is regulated
RT by interleukin enhancer-binding factor 3.";
RL J. Biol. Chem. 275:19866-19876(2000).
RN [17]
RP IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH XPO5; RAN AND
RP DOUBLE-STRANDED RNA, AND INTERACTION WITH XPO5.
RX PubMed=11777942; DOI=10.1083/jcb.200110082;
RA Brownawell A.M., Macara I.G.;
RT "Exportin-5, a novel karyopherin, mediates nuclear export of double-
RT stranded RNA binding proteins.";
RL J. Cell Biol. 156:53-64(2002).
RN [18]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=12429849; DOI=10.1091/mbc.E02-05-0271;
RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA Greco A., Hochstrasser D.F., Diaz J.-J.;
RT "Functional proteomic analysis of human nucleolus.";
RL Mol. Biol. Cell 13:4100-4109(2002).
RN [19]
RP INTERACTION WITH ILF2.
RX PubMed=11739746; DOI=10.1128/MCB.22.1.343-356.2002;
RA Reichman T.W., Muniz L.C., Mathews M.B.;
RT "The RNA binding protein nuclear factor 90 functions as both a
RT positive and negative regulator of gene expression in mammalian
RT cells.";
RL Mol. Cell. Biol. 22:343-356(2002).
RN [20]
RP IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH XPO5; RAN AND
RP VA1 RNA.
RX PubMed=14570900; DOI=10.1074/jbc.M306808200;
RA Gwizdek C., Ossareh-Nazari B., Brownawell A.M., Evers S., Macara I.G.,
RA Dargemont C.;
RT "Minihelix-containing RNAs mediate exportin-5-dependent nuclear export
RT of the double-stranded RNA-binding protein ILF3.";
RL J. Biol. Chem. 279:884-891(2004).
RN [21]
RP IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH XPO5; RAN;
RP ZNF346 AND DOUBLE-STRANDED RNA, AND INTERACTION WITH XPO5 AND ZNF346.
RX PubMed=15254228; DOI=10.1128/MCB.24.15.6608-6619.2004;
RA Chen T., Brownawell A.M., Macara I.G.;
RT "Nucleocytoplasmic shuttling of JAZ, a new cargo protein for exportin-
RT 5.";
RL Mol. Cell. Biol. 24:6608-6619(2004).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-482 AND THR-592, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-592, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [24]
RP IDENTIFICATION IN A COMPLEX WITH ILF2; YLPM1; KHDRBS1; RBMX; NCOA5 AND
RP PPP1CA.
RX PubMed=17890166; DOI=10.1016/j.bbapap.2007.07.015;
RA Ulke-Lemee A., Trinkle-Mulcahy L., Chaulk S., Bernstein N.K.,
RA Morrice N., Glover M., Lamond A.I., Moorhead G.B.G.;
RT "The nuclear PP1 interacting protein ZAP3 (ZAP) is a putative
RT nucleoside kinase that complexes with SAM68, CIA, NF110/45, and HNRNP-
RT G.";
RL Biochim. Biophys. Acta 1774:1339-1350(2007).
RN [25]
RP INTERACTION WITH AGO1 AND AGO2.
RX PubMed=17932509; DOI=10.1038/sj.embor.7401088;
RA Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M.,
RA Urlaub H., Meister G.;
RT "Proteomic and functional analysis of Argonaute-containing mRNA-
RT protein complexes in human cells.";
RL EMBO Rep. 8:1052-1060(2007).
RN [26]
RP IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=17289661; DOI=10.1074/mcp.M600346-MCP200;
RA Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R.,
RA Johnsen A.H., Christiansen J., Nielsen F.C.;
RT "Molecular composition of IMP1 ribonucleoprotein granules.";
RL Mol. Cell. Proteomics 6:798-811(2007).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190; SER-792 AND
RP SER-812, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-482 (ISOFORMS
RP 4; 6 AND 7), AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [28]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [29]
RP IDENTIFICATION IN A MRNP COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=19029303; DOI=10.1261/rna.1175909;
RA Weidensdorfer D., Stoehr N., Baude A., Lederer M., Koehn M.,
RA Schierhorn A., Buchmeier S., Wahle E., Huettelmaiery S.;
RT "Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic
RT RNPs.";
RL RNA 15:104-115(2009).
RN [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-592 AND SER-792,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-482 (ISOFORMS 4; 6 AND
RP 7), AND MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [31]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-100 AND LYS-460, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [32]
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT THR-188 AND THR-315.
RX PubMed=21123651; DOI=10.1101/gad.1965010;
RA Harashima A., Guettouche T., Barber G.N.;
RT "Phosphorylation of the NFAR proteins by the dsRNA-dependent protein
RT kinase PKR constitutes a novel mechanism of translational regulation
RT and cellular defense.";
RL Genes Dev. 24:2640-2653(2010).
RN [33]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62; SER-190; SER-382;
RP SER-384; SER-482; THR-592 AND SER-812, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [34]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [35]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62; SER-190; SER-382;
RP SER-476; SER-482; THR-592; SER-792 AND SER-812, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [36]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 520-594.
RG Northeast structural genomics consortium (NESG);
RT "Crystal structure of DRBM 2 domain of interleukin enhancer-binding
RT factor 3 from Homo sapiens, Northeast structural genomics consortium
RT target HR4527E.";
RL Submitted (DEC-2010) to the PDB data bank.
RN [37]
RP STRUCTURE BY NMR OF 521-600.
RG Northeast structural genomics consortium (NESG);
RT "Northeast structural genomics consortium target HR4527E.";
RL Submitted (SEP-2010) to the PDB data bank.
CC -!- FUNCTION: May facilitate double-stranded RNA-regulated gene
CC expression at the level of post-transcription. Can act as a
CC translation inhibitory protein which binds to coding sequences of
CC acid beta-glucosidase (GCase) and other mRNAs and functions at the
CC initiation phase of GCase mRNA translation, probably by inhibiting
CC its binding to polysomes. Can regulate protein arginine N-
CC methyltransferase 1 activity. May regulate transcription of the
CC IL2 gene during T-cell activation. Can promote the formation of
CC stable DNA-dependent protein kinase holoenzyme complexes on DNA.
CC The phosphorylated form at Thr-188 and Thr-315, in concert with
CC EIF2AK2/PKR can inhibit vesicular stomatitis virus (VSV)
CC replication (By similarity).
CC -!- SUBUNIT: Identified in a IGF2BP1-dependent mRNP granule complex
CC containing untranslated mRNAs. Interacts with FUS and SMN proteins
CC and with PRMT1. Forms a complex with ILF2. Can also bind to
CC PRKDC/XRCC7: this may stabilize the interaction of PRKDC/XRCC7 and
CC the heterodimeric complex of XRCC6/KU70 and XRCC5/KU80. Forms a
CC heteromeric complex with ZNF346 and ILF3. Found in a nuclear
CC export complex with XPO5, ILF3, Ran and double-stranded RNA or
CC double-stranded minihelix VA1 RNA. Found in a nuclear export
CC complex with XPO5, RAN, ILF3, ZNF346 and double-stranded RNA.
CC Interacts with XPO5 and ZNF346. Forms a complex with ILF2, YLPM1,
CC KHDRBS1, RBMX, NCOA5 and PPP1CA. Interacts with AGO1 and AGO2.
CC -!- INTERACTION:
CC Q99873:PRMT1; NbExp=2; IntAct=EBI-78756, EBI-78738;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Cytoplasm. Nucleus.
CC Note=Localizes in the cytoplasm in response to viral dsRNA. The
CC unphosphorylated form is retained in the nucleus by ILF2.
CC Phosphorylation at Thr-188 and Thr-315 causes the dissociation of
CC ILF2 from the ILF2-ILF3 complex resulting in a cytoplasmic
CC sequestration of ILF3. Localized in cytoplasmic mRNP granules
CC containing untranslated mRNAs.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1; Synonyms=NFAR-2, ILF3-E;
CC IsoId=Q12906-1; Sequence=Displayed;
CC Name=2; Synonyms=NFAR-1, DRBP76;
CC IsoId=Q12906-2; Sequence=VSP_003888, VSP_003889;
CC Name=3;
CC IsoId=Q12906-3; Sequence=VSP_003890, VSP_003891;
CC Name=4; Synonyms=DRBP76 Alpha, ILF3-A;
CC IsoId=Q12906-4; Sequence=VSP_003883, VSP_003884, VSP_003885;
CC Note=Contains a phosphoserine at position 482;
CC Name=5; Synonyms=DRBP76 Delta, Gamma, ILF3-C;
CC IsoId=Q12906-5; Sequence=VSP_003886, VSP_003887;
CC Name=6;
CC IsoId=Q12906-6; Sequence=VSP_003883, VSP_003888, VSP_003889;
CC Note=Contains a phosphoserine at position 482;
CC Name=7;
CC IsoId=Q12906-7; Sequence=VSP_003883;
CC Note=Gene prediction based on EST data. Contains a phosphoserine
CC at position 482;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- PTM: Phosphorylated at Thr-188 and Thr-315 by PKR in response to
CC certain RNA viruses. This phosphorylation results in the
CC dissociation of ILF2 from the ILF2-ILF3 complex resulting in a
CC cytoplasmic sequestration of ILF3 where it can bind to viral RNAs
CC and impede viral replication.
CC -!- PTM: Methylated by protein arginine N-methyltransferase 1.
CC -!- PTM: Arg-609 is dimethylated, probably to asymmetric
CC dimethylarginine.
CC -!- SIMILARITY: Contains 2 DRBM (double-stranded RNA-binding) domains.
CC -!- SIMILARITY: Contains 1 DZF domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA20994.1; Type=Miscellaneous discrepancy; Note=Sequencing errors;
CC Sequence=AAH48314.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
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DR EMBL; U10324; AAA20994.1; ALT_SEQ; mRNA.
DR EMBL; AF147209; AAD33966.1; -; mRNA.
DR EMBL; AF141870; AAD37575.1; -; mRNA.
DR EMBL; AJ271741; CAC01121.1; -; Genomic_DNA.
DR EMBL; AJ271741; CAC01122.1; -; Genomic_DNA.
DR EMBL; AJ271741; CAC01123.1; -; Genomic_DNA.
DR EMBL; AJ271741; CAC01124.1; -; Genomic_DNA.
DR EMBL; AJ271744; CAC01404.1; -; mRNA.
DR EMBL; AJ271745; CAC01405.1; -; mRNA.
DR EMBL; AJ271746; CAC01406.1; -; mRNA.
DR EMBL; AJ271747; CAC01407.1; -; mRNA.
DR EMBL; AF167569; AAD51098.1; -; mRNA.
DR EMBL; AF167570; AAD51099.1; -; mRNA.
DR EMBL; AF320244; AAK07424.1; -; Genomic_DNA.
DR EMBL; AF320228; AAK07424.1; JOINED; Genomic_DNA.
DR EMBL; AF320229; AAK07424.1; JOINED; Genomic_DNA.
DR EMBL; AF320230; AAK07424.1; JOINED; Genomic_DNA.
DR EMBL; AF320231; AAK07424.1; JOINED; Genomic_DNA.
DR EMBL; AF320232; AAK07424.1; JOINED; Genomic_DNA.
DR EMBL; AF320233; AAK07424.1; JOINED; Genomic_DNA.
DR EMBL; AF320234; AAK07424.1; JOINED; Genomic_DNA.
DR EMBL; AF320235; AAK07424.1; JOINED; Genomic_DNA.
DR EMBL; AF320236; AAK07424.1; JOINED; Genomic_DNA.
DR EMBL; AF320237; AAK07424.1; JOINED; Genomic_DNA.
DR EMBL; AF320238; AAK07424.1; JOINED; Genomic_DNA.
DR EMBL; AF320239; AAK07424.1; JOINED; Genomic_DNA.
DR EMBL; AF320240; AAK07424.1; JOINED; Genomic_DNA.
DR EMBL; AF320241; AAK07424.1; JOINED; Genomic_DNA.
DR EMBL; AF320242; AAK07424.1; JOINED; Genomic_DNA.
DR EMBL; AF320243; AAK07424.1; JOINED; Genomic_DNA.
DR EMBL; AF320247; AAK07425.1; -; Genomic_DNA.
DR EMBL; AF320228; AAK07425.1; JOINED; Genomic_DNA.
DR EMBL; AF320229; AAK07425.1; JOINED; Genomic_DNA.
DR EMBL; AF320230; AAK07425.1; JOINED; Genomic_DNA.
DR EMBL; AF320231; AAK07425.1; JOINED; Genomic_DNA.
DR EMBL; AF320232; AAK07425.1; JOINED; Genomic_DNA.
DR EMBL; AF320233; AAK07425.1; JOINED; Genomic_DNA.
DR EMBL; AF320234; AAK07425.1; JOINED; Genomic_DNA.
DR EMBL; AF320235; AAK07425.1; JOINED; Genomic_DNA.
DR EMBL; AF320236; AAK07425.1; JOINED; Genomic_DNA.
DR EMBL; AF320237; AAK07425.1; JOINED; Genomic_DNA.
DR EMBL; AF320238; AAK07425.1; JOINED; Genomic_DNA.
DR EMBL; AF320239; AAK07425.1; JOINED; Genomic_DNA.
DR EMBL; AF320240; AAK07425.1; JOINED; Genomic_DNA.
DR EMBL; AF320241; AAK07425.1; JOINED; Genomic_DNA.
DR EMBL; AF320242; AAK07425.1; JOINED; Genomic_DNA.
DR EMBL; AF320243; AAK07425.1; JOINED; Genomic_DNA.
DR EMBL; AF320245; AAK07425.1; JOINED; Genomic_DNA.
DR EMBL; AF320246; AAK07425.1; JOINED; Genomic_DNA.
DR EMBL; AK291617; BAF84306.1; -; mRNA.
DR EMBL; AC011475; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471106; EAW84132.1; -; Genomic_DNA.
DR EMBL; BC048314; AAH48314.1; ALT_SEQ; mRNA.
DR EMBL; BC064836; AAH64836.1; -; mRNA.
DR EMBL; X98264; CAA66917.1; -; mRNA.
DR EMBL; X98265; CAA66918.1; -; mRNA.
DR EMBL; AF202445; AAF82685.1; -; Genomic_DNA.
DR EMBL; AF202445; AAF82686.1; -; Genomic_DNA.
DR EMBL; AF202445; AAF82687.1; -; Genomic_DNA.
DR EMBL; AF007140; AAC19152.1; -; mRNA.
DR PIR; B54857; B54857.
DR RefSeq; NP_001131145.1; NM_001137673.1.
DR RefSeq; NP_004507.2; NM_004516.3.
DR RefSeq; NP_036350.2; NM_012218.3.
DR RefSeq; NP_060090.2; NM_017620.2.
DR RefSeq; NP_703194.1; NM_153464.2.
DR RefSeq; XP_005259951.1; XM_005259894.1.
DR UniGene; Hs.465885; -.
DR PDB; 2L33; NMR; -; A=521-600.
DR PDB; 3P1X; X-ray; 1.90 A; A/B=520-594.
DR PDBsum; 2L33; -.
DR PDBsum; 3P1X; -.
DR ProteinModelPortal; Q12906; -.
DR SMR; Q12906; 6-374, 399-594.
DR DIP; DIP-29853N; -.
DR IntAct; Q12906; 48.
DR MINT; MINT-4999319; -.
DR PhosphoSite; Q12906; -.
DR DMDM; 62512150; -.
DR SWISS-2DPAGE; Q12906; -.
DR PaxDb; Q12906; -.
DR PRIDE; Q12906; -.
DR DNASU; 3609; -.
DR Ensembl; ENST00000250241; ENSP00000250241; ENSG00000129351.
DR Ensembl; ENST00000318511; ENSP00000315205; ENSG00000129351.
DR Ensembl; ENST00000407004; ENSP00000384660; ENSG00000129351.
DR Ensembl; ENST00000420083; ENSP00000405436; ENSG00000129351.
DR Ensembl; ENST00000449870; ENSP00000404121; ENSG00000129351.
DR Ensembl; ENST00000588657; ENSP00000468181; ENSG00000129351.
DR Ensembl; ENST00000589998; ENSP00000465219; ENSG00000129351.
DR Ensembl; ENST00000590261; ENSP00000468156; ENSG00000129351.
DR Ensembl; ENST00000592763; ENSP00000465515; ENSG00000129351.
DR GeneID; 3609; -.
DR KEGG; hsa:3609; -.
DR UCSC; uc002mpo.3; human.
DR CTD; 3609; -.
DR GeneCards; GC19P010764; -.
DR H-InvDB; HIX0014753; -.
DR HGNC; HGNC:6038; ILF3.
DR HPA; HPA001897; -.
DR MIM; 603182; gene.
DR neXtProt; NX_Q12906; -.
DR PharmGKB; PA29853; -.
DR eggNOG; NOG307678; -.
DR HOVERGEN; HBG069915; -.
DR InParanoid; Q12906; -.
DR KO; K13090; -.
DR OMA; PPKHAGK; -.
DR OrthoDB; EOG72ZCDC; -.
DR PhylomeDB; Q12906; -.
DR ChiTaRS; ILF3; human.
DR EvolutionaryTrace; Q12906; -.
DR GeneWiki; ILF3; -.
DR GenomeRNAi; 3609; -.
DR NextBio; 14109; -.
DR PMAP-CutDB; Q12906; -.
DR PRO; PR:Q12906; -.
DR ArrayExpress; Q12906; -.
DR Bgee; Q12906; -.
DR Genevestigator; Q12906; -.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0030529; C:ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0000279; P:M phase; NAS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-dependent; IDA:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; ISS:UniProtKB.
DR GO; GO:0045071; P:negative regulation of viral genome replication; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-dependent; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR Gene3D; 3.30.160.20; -; 2.
DR InterPro; IPR014720; dsRNA-bd_dom.
DR InterPro; IPR006561; DZF.
DR Pfam; PF00035; dsrm; 2.
DR Pfam; PF07528; DZF; 1.
DR SMART; SM00358; DSRM; 2.
DR SMART; SM00572; DZF; 1.
DR PROSITE; PS50137; DS_RBD; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Antiviral defense;
KW Complete proteome; Cytoplasm; Direct protein sequencing; DNA-binding;
KW Methylation; Nucleus; Phosphoprotein; Polymorphism;
KW Reference proteome; Repeat; RNA-binding; Transcription;
KW Transcription regulation.
FT CHAIN 1 894 Interleukin enhancer-binding factor 3.
FT /FTId=PRO_0000126070.
FT DOMAIN 94 342 DZF.
FT DOMAIN 398 467 DRBM 1.
FT DOMAIN 524 590 DRBM 2.
FT REGION 609 894 Interaction with PRMT1.
FT MOTIF 371 389 Bipartite nuclear localization signal
FT (Potential).
FT COMPBIAS 385 389 Poly-Lys.
FT COMPBIAS 634 637 Poly-Pro.
FT COMPBIAS 640 659 Arg/Gly-rich.
FT COMPBIAS 701 709 Poly-Gly.
FT COMPBIAS 794 798 Poly-Gly.
FT MOD_RES 62 62 Phosphoserine.
FT MOD_RES 100 100 N6-acetyllysine.
FT MOD_RES 188 188 Phosphothreonine; by PKR.
FT MOD_RES 190 190 Phosphoserine.
FT MOD_RES 315 315 Phosphothreonine; by PKR.
FT MOD_RES 382 382 Phosphoserine.
FT MOD_RES 384 384 Phosphoserine.
FT MOD_RES 460 460 N6-acetyllysine.
FT MOD_RES 476 476 Phosphoserine.
FT MOD_RES 482 482 Phosphoserine.
FT MOD_RES 592 592 Phosphothreonine.
FT MOD_RES 792 792 Phosphoserine.
FT MOD_RES 812 812 Phosphoserine.
FT VAR_SEQ 516 516 E -> ENVKQ (in isoform 4, isoform 6 and
FT isoform 7).
FT /FTId=VSP_003883.
FT VAR_SEQ 687 690 SQFY -> TGFV (in isoform 5).
FT /FTId=VSP_003886.
FT VAR_SEQ 688 702 QFYSNGGHSGNASGG -> DFFTDCYGYHDFGSS (in
FT isoform 2 and isoform 6).
FT /FTId=VSP_003888.
FT VAR_SEQ 688 694 QFYSNGG -> KCAFLSV (in isoform 4).
FT /FTId=VSP_003884.
FT VAR_SEQ 690 764 YSNGGHSGNASGGGGGGGGGSSGYGSYYQGDNYNSPVPPKH
FT AGKKQPHGGQQKPSYGSGYQSHQGQQQSYNQSPY -> SRP
FT PPPSRPRCCVVRCSGSPCGPSCDPYLAVFGTPCLQWFVSCH
FT YNFVWVEFLSFCSSVSLCLFTLRVSGNSVCL (in
FT isoform 3).
FT /FTId=VSP_003890.
FT VAR_SEQ 691 894 Missing (in isoform 5).
FT /FTId=VSP_003887.
FT VAR_SEQ 695 894 Missing (in isoform 4).
FT /FTId=VSP_003885.
FT VAR_SEQ 703 894 Missing (in isoform 2 and isoform 6).
FT /FTId=VSP_003889.
FT VAR_SEQ 765 894 Missing (in isoform 3).
FT /FTId=VSP_003891.
FT VARIANT 50 50 D -> H (in dbSNP:rs1064493).
FT /FTId=VAR_022159.
FT VARIANT 501 501 A -> S (in dbSNP:rs34520379).
FT /FTId=VAR_048906.
FT CONFLICT 101 101 G -> C (in Ref. 5; AAD51098/AAD51099 and
FT 6; AAK07424/AAK07425).
FT CONFLICT 260 260 G -> V (in Ref. 2; AAD33966 and 11;
FT CAA66918).
FT CONFLICT 647 647 S -> T (in Ref. 2; AAD33966 and 6;
FT AAK07424/AAK07425).
FT CONFLICT 688 689 QF -> N (in Ref. 13; AAF82687).
FT CONFLICT 763 763 P -> L (in Ref. 4; CAC01407).
FT CONFLICT 797 797 G -> R (in Ref. 4; CAC01124 and 6;
FT AAK07425).
FT CONFLICT 799 799 S -> SGS (in Ref. 13; AAF82685).
FT CONFLICT 813 813 G -> E (in Ref. 6; AAK07425).
FT HELIX 528 535
FT STRAND 541 548
FT STRAND 554 561
FT STRAND 564 572
FT HELIX 573 588
SQ SEQUENCE 894 AA; 95338 MW; 20903ABD0331F370 CRC64;
MRPMRIFVND DRHVMAKHSS VYPTQEELEA VQNMVSHTER ALKAVSDWID EQEKGSSEQA
ESDNMDVPPE DDSKEGAGEQ KTEHMTRTLR GVMRVGLVAK GLLLKGDLDL ELVLLCKEKP
TTALLDKVAD NLAIQLAAVT EDKYEILQSV DDAAIVIKNT KEPPLSLTIH LTSPVVREEM
EKVLAGETLS VNDPPDVLDR QKCLAALASL RHAKWFQARA NGLKSCVIVI RVLRDLCTRV
PTWGPLRGWP LELLCEKSIG TANRPMGAGE ALRRVLECLA SGIVMPDGSG IYDPCEKEAT
DAIGHLDRQQ REDITQSAQH ALRLAAFGQL HKVLGMDPLP SKMPKKPKNE NPVDYTVQIP
PSTTYAITPM KRPMEEDGEE KSPSKKKKKI QKKEEKAEPP QAMNALMRLN QLKPGLQYKL
VSQTGPVHAP IFTMSVEVDG NSFEASGPSK KTAKLHVAVK VLQDMGLPTG AEGRDSSKGE
DSAEETEAKP AVVAPAPVVE AVSTPSAAFP SDATAEQGPI LTKHGKNPVM ELNEKRRGLK
YELISETGGS HDKRFVMEVE VDGQKFQGAG SNKKVAKAYA ALAALEKLFP DTPLALDANK
KKRAPVPVRG GPKFAAKPHN PGFGMGGPMH NEVPPPPNLR GRGRGGSIRG RGRGRGFGGA
NHGGYMNAGA GYGSYGYGGN SATAGYSQFY SNGGHSGNAS GGGGGGGGGS SGYGSYYQGD
NYNSPVPPKH AGKKQPHGGQ QKPSYGSGYQ SHQGQQQSYN QSPYSNYGPP QGKQKGYNHG
QGSYSYSNSY NSPGGGGGSD YNYESKFNYS GSGGRSGGNS YGSGGASYNP GSHGGYGGGS
GGGSSYQGKQ GGYSQSNYNS PGSGQNYSGP PSSYQSSQGG YGRNADHSMN YQYR
//
ID ILF3_HUMAN Reviewed; 894 AA.
AC Q12906; A8K6F2; G5E9M5; O43409; Q6P1X1; Q86XY7; Q99544; Q99545;
read moreAC Q9BZH4; Q9BZH5; Q9NQ95; Q9NQ96; Q9NQ97; Q9NQ98; Q9NQ99; Q9NQA0;
AC Q9NQA1; Q9NQA2; Q9NRN2; Q9NRN3; Q9NRN4; Q9UMZ9; Q9UN00; Q9UN84;
AC Q9UNA2;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 3.
DT 22-JAN-2014, entry version 154.
DE RecName: Full=Interleukin enhancer-binding factor 3;
DE AltName: Full=Double-stranded RNA-binding protein 76;
DE Short=DRBP76;
DE AltName: Full=M-phase phosphoprotein 4;
DE Short=MPP4;
DE AltName: Full=Nuclear factor associated with dsRNA;
DE Short=NFAR;
DE AltName: Full=Nuclear factor of activated T-cells 90 kDa;
DE Short=NF-AT-90;
DE AltName: Full=Translational control protein 80;
DE Short=TCP80;
GN Name=ILF3; Synonyms=DRBF, MPHOSPH4, NF90;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-41;
RP 491-510 AND 555-565, AND FUNCTION.
RC TISSUE=T-cell lymphoma;
RX PubMed=7519613;
RA Kao P.N., Chen L., Brock G., Ng J., Kenny J., Smith A.J., Corthesy B.;
RT "Cloning and expression of cyclosporin A- and FK506-sensitive nuclear
RT factor of activated T-cells: NF45 and NF90.";
RL J. Biol. Chem. 269:20691-20699(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND PROTEIN SEQUENCE OF
RP N-TERMINUS.
RC TISSUE=Cervix carcinoma;
RX PubMed=10400669; DOI=10.1074/jbc.274.29.20432;
RA Patel R.C., Vestal D.J., Xu Z., Bandyopadhyay S., Guo W., Erme S.M.,
RA Williams B.R., Sen G.C.;
RT "DRBP76, a double-stranded RNA-binding nuclear protein, is
RT phosphorylated by the interferon-induced protein kinase, PKR.";
RL J. Biol. Chem. 274:20432-20437(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND CHARACTERIZATION.
RC TISSUE=Liver;
RX PubMed=10607473; DOI=10.1006/mgme.1999.2934;
RA Xu Y.-H., Grabowski G.A.;
RT "Molecular cloning and characterization of a translational inhibitory
RT protein that binds to coding sequences of human acid beta-glucosidase
RT and other mRNAs.";
RL Mol. Genet. Metab. 68:441-454(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2; 4 AND 5), AND
RP ALTERNATIVE SPLICING.
RC TISSUE=Melanoma;
RX PubMed=11167023; DOI=10.1016/S0378-1119(00)00495-9;
RA Duchange N., Pidoux J., Camus E., Sauvaget D.;
RT "Alternative splicing in the human interleukin enhancer binding factor
RT 3 (ILF3) gene.";
RL Gene 261:345-353(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), AND
RP CHARACTERIZATION.
RX PubMed=11438536; DOI=10.1074/jbc.M104207200;
RA Saunders L.R., Perkins D.J., Balachandran S., Michaels R., Ford R.,
RA Mayeda A., Barber G.N.;
RT "Characterization of two evolutionarily conserved, alternatively
RT spliced nuclear phosphoproteins, NFAR-1 and -2, that function in mRNA
RT processing and interact with the double-stranded RNA-dependent protein
RT kinase, PKR.";
RL J. Biol. Chem. 276:32300-32312(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), AND
RP VARIANT HIS-50.
RC TISSUE=T-cell;
RX PubMed=11161820; DOI=10.1006/geno.2000.6423;
RA Saunders L.R., Jurecic V., Barber G.N.;
RT "The 90- and 110-kDa human NFAR proteins are translated from two
RT differentially spliced mRNAs encoded on chromosome 19p13.";
RL Genomics 71:256-259(2001).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RC TISSUE=Duodenum, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-611.
RC TISSUE=Blood, and Cervix;
RX PubMed=8885239; DOI=10.1091/mbc.7.9.1455;
RA Matsumoto-Taniura N., Pirollet F., Monroe R., Gerace L.,
RA Westendorf J.M.;
RT "Identification of novel M phase phosphoproteins by expression
RT cloning.";
RL Mol. Biol. Cell 7:1455-1469(1996).
RN [12]
RP PROTEIN SEQUENCE OF 1-10, FUNCTION, AND INTERACTION WITH XRCC6; PRKDC
RP AND XRCC5.
RX PubMed=9442054; DOI=10.1074/jbc.273.4.2136;
RA Ting N.S.Y., Kao P.N., Chan D.W., Lintott L.G., Lees-Miller S.P.;
RT "DNA-dependent protein kinase interacts with antigen receptor response
RT element binding proteins NF90 and NF45.";
RL J. Biol. Chem. 273:2136-2145(1998).
RN [13]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 188-894 (ISOFORMS 1; 2 AND 3).
RA MacArdle J., Cantarella G.M., Veyrune J.-L., Krasnoselskaya I.,
RA Kumar A.;
RT "Structure and functional characterization of hDRBF gene.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [14]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 587-894 (ISOFORM 1).
RC TISSUE=Brain;
RA Yu W., Sarginson J., Gibbs R.A.;
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [15]
RP INTERACTION WITH ILF2.
RX PubMed=10574923; DOI=10.1074/jbc.274.49.34598;
RA Satoh M., Shaheen V.M., Kao P.N., Okano T., Shaw M., Yoshida H.,
RA Richards H.B., Reeves W.H.;
RT "Autoantibodies define a family of proteins with conserved double-
RT stranded RNA-binding domains as well as DNA binding activity.";
RL J. Biol. Chem. 274:34598-34604(1999).
RN [16]
RP INTERACTION WITH PRMT1.
RX PubMed=10749851; DOI=10.1074/jbc.M000023200;
RA Tang J., Kao P.N., Herschman H.R.;
RT "Protein-arginine methyltransferase I, the predominant protein-
RT arginine methyltransferase in cells, interacts with and is regulated
RT by interleukin enhancer-binding factor 3.";
RL J. Biol. Chem. 275:19866-19876(2000).
RN [17]
RP IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH XPO5; RAN AND
RP DOUBLE-STRANDED RNA, AND INTERACTION WITH XPO5.
RX PubMed=11777942; DOI=10.1083/jcb.200110082;
RA Brownawell A.M., Macara I.G.;
RT "Exportin-5, a novel karyopherin, mediates nuclear export of double-
RT stranded RNA binding proteins.";
RL J. Cell Biol. 156:53-64(2002).
RN [18]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=12429849; DOI=10.1091/mbc.E02-05-0271;
RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA Greco A., Hochstrasser D.F., Diaz J.-J.;
RT "Functional proteomic analysis of human nucleolus.";
RL Mol. Biol. Cell 13:4100-4109(2002).
RN [19]
RP INTERACTION WITH ILF2.
RX PubMed=11739746; DOI=10.1128/MCB.22.1.343-356.2002;
RA Reichman T.W., Muniz L.C., Mathews M.B.;
RT "The RNA binding protein nuclear factor 90 functions as both a
RT positive and negative regulator of gene expression in mammalian
RT cells.";
RL Mol. Cell. Biol. 22:343-356(2002).
RN [20]
RP IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH XPO5; RAN AND
RP VA1 RNA.
RX PubMed=14570900; DOI=10.1074/jbc.M306808200;
RA Gwizdek C., Ossareh-Nazari B., Brownawell A.M., Evers S., Macara I.G.,
RA Dargemont C.;
RT "Minihelix-containing RNAs mediate exportin-5-dependent nuclear export
RT of the double-stranded RNA-binding protein ILF3.";
RL J. Biol. Chem. 279:884-891(2004).
RN [21]
RP IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH XPO5; RAN;
RP ZNF346 AND DOUBLE-STRANDED RNA, AND INTERACTION WITH XPO5 AND ZNF346.
RX PubMed=15254228; DOI=10.1128/MCB.24.15.6608-6619.2004;
RA Chen T., Brownawell A.M., Macara I.G.;
RT "Nucleocytoplasmic shuttling of JAZ, a new cargo protein for exportin-
RT 5.";
RL Mol. Cell. Biol. 24:6608-6619(2004).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-482 AND THR-592, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-592, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [24]
RP IDENTIFICATION IN A COMPLEX WITH ILF2; YLPM1; KHDRBS1; RBMX; NCOA5 AND
RP PPP1CA.
RX PubMed=17890166; DOI=10.1016/j.bbapap.2007.07.015;
RA Ulke-Lemee A., Trinkle-Mulcahy L., Chaulk S., Bernstein N.K.,
RA Morrice N., Glover M., Lamond A.I., Moorhead G.B.G.;
RT "The nuclear PP1 interacting protein ZAP3 (ZAP) is a putative
RT nucleoside kinase that complexes with SAM68, CIA, NF110/45, and HNRNP-
RT G.";
RL Biochim. Biophys. Acta 1774:1339-1350(2007).
RN [25]
RP INTERACTION WITH AGO1 AND AGO2.
RX PubMed=17932509; DOI=10.1038/sj.embor.7401088;
RA Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M.,
RA Urlaub H., Meister G.;
RT "Proteomic and functional analysis of Argonaute-containing mRNA-
RT protein complexes in human cells.";
RL EMBO Rep. 8:1052-1060(2007).
RN [26]
RP IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=17289661; DOI=10.1074/mcp.M600346-MCP200;
RA Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R.,
RA Johnsen A.H., Christiansen J., Nielsen F.C.;
RT "Molecular composition of IMP1 ribonucleoprotein granules.";
RL Mol. Cell. Proteomics 6:798-811(2007).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190; SER-792 AND
RP SER-812, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-482 (ISOFORMS
RP 4; 6 AND 7), AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [28]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [29]
RP IDENTIFICATION IN A MRNP COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=19029303; DOI=10.1261/rna.1175909;
RA Weidensdorfer D., Stoehr N., Baude A., Lederer M., Koehn M.,
RA Schierhorn A., Buchmeier S., Wahle E., Huettelmaiery S.;
RT "Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic
RT RNPs.";
RL RNA 15:104-115(2009).
RN [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-592 AND SER-792,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-482 (ISOFORMS 4; 6 AND
RP 7), AND MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [31]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-100 AND LYS-460, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [32]
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT THR-188 AND THR-315.
RX PubMed=21123651; DOI=10.1101/gad.1965010;
RA Harashima A., Guettouche T., Barber G.N.;
RT "Phosphorylation of the NFAR proteins by the dsRNA-dependent protein
RT kinase PKR constitutes a novel mechanism of translational regulation
RT and cellular defense.";
RL Genes Dev. 24:2640-2653(2010).
RN [33]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62; SER-190; SER-382;
RP SER-384; SER-482; THR-592 AND SER-812, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [34]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [35]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62; SER-190; SER-382;
RP SER-476; SER-482; THR-592; SER-792 AND SER-812, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [36]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 520-594.
RG Northeast structural genomics consortium (NESG);
RT "Crystal structure of DRBM 2 domain of interleukin enhancer-binding
RT factor 3 from Homo sapiens, Northeast structural genomics consortium
RT target HR4527E.";
RL Submitted (DEC-2010) to the PDB data bank.
RN [37]
RP STRUCTURE BY NMR OF 521-600.
RG Northeast structural genomics consortium (NESG);
RT "Northeast structural genomics consortium target HR4527E.";
RL Submitted (SEP-2010) to the PDB data bank.
CC -!- FUNCTION: May facilitate double-stranded RNA-regulated gene
CC expression at the level of post-transcription. Can act as a
CC translation inhibitory protein which binds to coding sequences of
CC acid beta-glucosidase (GCase) and other mRNAs and functions at the
CC initiation phase of GCase mRNA translation, probably by inhibiting
CC its binding to polysomes. Can regulate protein arginine N-
CC methyltransferase 1 activity. May regulate transcription of the
CC IL2 gene during T-cell activation. Can promote the formation of
CC stable DNA-dependent protein kinase holoenzyme complexes on DNA.
CC The phosphorylated form at Thr-188 and Thr-315, in concert with
CC EIF2AK2/PKR can inhibit vesicular stomatitis virus (VSV)
CC replication (By similarity).
CC -!- SUBUNIT: Identified in a IGF2BP1-dependent mRNP granule complex
CC containing untranslated mRNAs. Interacts with FUS and SMN proteins
CC and with PRMT1. Forms a complex with ILF2. Can also bind to
CC PRKDC/XRCC7: this may stabilize the interaction of PRKDC/XRCC7 and
CC the heterodimeric complex of XRCC6/KU70 and XRCC5/KU80. Forms a
CC heteromeric complex with ZNF346 and ILF3. Found in a nuclear
CC export complex with XPO5, ILF3, Ran and double-stranded RNA or
CC double-stranded minihelix VA1 RNA. Found in a nuclear export
CC complex with XPO5, RAN, ILF3, ZNF346 and double-stranded RNA.
CC Interacts with XPO5 and ZNF346. Forms a complex with ILF2, YLPM1,
CC KHDRBS1, RBMX, NCOA5 and PPP1CA. Interacts with AGO1 and AGO2.
CC -!- INTERACTION:
CC Q99873:PRMT1; NbExp=2; IntAct=EBI-78756, EBI-78738;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Cytoplasm. Nucleus.
CC Note=Localizes in the cytoplasm in response to viral dsRNA. The
CC unphosphorylated form is retained in the nucleus by ILF2.
CC Phosphorylation at Thr-188 and Thr-315 causes the dissociation of
CC ILF2 from the ILF2-ILF3 complex resulting in a cytoplasmic
CC sequestration of ILF3. Localized in cytoplasmic mRNP granules
CC containing untranslated mRNAs.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1; Synonyms=NFAR-2, ILF3-E;
CC IsoId=Q12906-1; Sequence=Displayed;
CC Name=2; Synonyms=NFAR-1, DRBP76;
CC IsoId=Q12906-2; Sequence=VSP_003888, VSP_003889;
CC Name=3;
CC IsoId=Q12906-3; Sequence=VSP_003890, VSP_003891;
CC Name=4; Synonyms=DRBP76 Alpha, ILF3-A;
CC IsoId=Q12906-4; Sequence=VSP_003883, VSP_003884, VSP_003885;
CC Note=Contains a phosphoserine at position 482;
CC Name=5; Synonyms=DRBP76 Delta, Gamma, ILF3-C;
CC IsoId=Q12906-5; Sequence=VSP_003886, VSP_003887;
CC Name=6;
CC IsoId=Q12906-6; Sequence=VSP_003883, VSP_003888, VSP_003889;
CC Note=Contains a phosphoserine at position 482;
CC Name=7;
CC IsoId=Q12906-7; Sequence=VSP_003883;
CC Note=Gene prediction based on EST data. Contains a phosphoserine
CC at position 482;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- PTM: Phosphorylated at Thr-188 and Thr-315 by PKR in response to
CC certain RNA viruses. This phosphorylation results in the
CC dissociation of ILF2 from the ILF2-ILF3 complex resulting in a
CC cytoplasmic sequestration of ILF3 where it can bind to viral RNAs
CC and impede viral replication.
CC -!- PTM: Methylated by protein arginine N-methyltransferase 1.
CC -!- PTM: Arg-609 is dimethylated, probably to asymmetric
CC dimethylarginine.
CC -!- SIMILARITY: Contains 2 DRBM (double-stranded RNA-binding) domains.
CC -!- SIMILARITY: Contains 1 DZF domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA20994.1; Type=Miscellaneous discrepancy; Note=Sequencing errors;
CC Sequence=AAH48314.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
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DR EMBL; U10324; AAA20994.1; ALT_SEQ; mRNA.
DR EMBL; AF147209; AAD33966.1; -; mRNA.
DR EMBL; AF141870; AAD37575.1; -; mRNA.
DR EMBL; AJ271741; CAC01121.1; -; Genomic_DNA.
DR EMBL; AJ271741; CAC01122.1; -; Genomic_DNA.
DR EMBL; AJ271741; CAC01123.1; -; Genomic_DNA.
DR EMBL; AJ271741; CAC01124.1; -; Genomic_DNA.
DR EMBL; AJ271744; CAC01404.1; -; mRNA.
DR EMBL; AJ271745; CAC01405.1; -; mRNA.
DR EMBL; AJ271746; CAC01406.1; -; mRNA.
DR EMBL; AJ271747; CAC01407.1; -; mRNA.
DR EMBL; AF167569; AAD51098.1; -; mRNA.
DR EMBL; AF167570; AAD51099.1; -; mRNA.
DR EMBL; AF320244; AAK07424.1; -; Genomic_DNA.
DR EMBL; AF320228; AAK07424.1; JOINED; Genomic_DNA.
DR EMBL; AF320229; AAK07424.1; JOINED; Genomic_DNA.
DR EMBL; AF320230; AAK07424.1; JOINED; Genomic_DNA.
DR EMBL; AF320231; AAK07424.1; JOINED; Genomic_DNA.
DR EMBL; AF320232; AAK07424.1; JOINED; Genomic_DNA.
DR EMBL; AF320233; AAK07424.1; JOINED; Genomic_DNA.
DR EMBL; AF320234; AAK07424.1; JOINED; Genomic_DNA.
DR EMBL; AF320235; AAK07424.1; JOINED; Genomic_DNA.
DR EMBL; AF320236; AAK07424.1; JOINED; Genomic_DNA.
DR EMBL; AF320237; AAK07424.1; JOINED; Genomic_DNA.
DR EMBL; AF320238; AAK07424.1; JOINED; Genomic_DNA.
DR EMBL; AF320239; AAK07424.1; JOINED; Genomic_DNA.
DR EMBL; AF320240; AAK07424.1; JOINED; Genomic_DNA.
DR EMBL; AF320241; AAK07424.1; JOINED; Genomic_DNA.
DR EMBL; AF320242; AAK07424.1; JOINED; Genomic_DNA.
DR EMBL; AF320243; AAK07424.1; JOINED; Genomic_DNA.
DR EMBL; AF320247; AAK07425.1; -; Genomic_DNA.
DR EMBL; AF320228; AAK07425.1; JOINED; Genomic_DNA.
DR EMBL; AF320229; AAK07425.1; JOINED; Genomic_DNA.
DR EMBL; AF320230; AAK07425.1; JOINED; Genomic_DNA.
DR EMBL; AF320231; AAK07425.1; JOINED; Genomic_DNA.
DR EMBL; AF320232; AAK07425.1; JOINED; Genomic_DNA.
DR EMBL; AF320233; AAK07425.1; JOINED; Genomic_DNA.
DR EMBL; AF320234; AAK07425.1; JOINED; Genomic_DNA.
DR EMBL; AF320235; AAK07425.1; JOINED; Genomic_DNA.
DR EMBL; AF320236; AAK07425.1; JOINED; Genomic_DNA.
DR EMBL; AF320237; AAK07425.1; JOINED; Genomic_DNA.
DR EMBL; AF320238; AAK07425.1; JOINED; Genomic_DNA.
DR EMBL; AF320239; AAK07425.1; JOINED; Genomic_DNA.
DR EMBL; AF320240; AAK07425.1; JOINED; Genomic_DNA.
DR EMBL; AF320241; AAK07425.1; JOINED; Genomic_DNA.
DR EMBL; AF320242; AAK07425.1; JOINED; Genomic_DNA.
DR EMBL; AF320243; AAK07425.1; JOINED; Genomic_DNA.
DR EMBL; AF320245; AAK07425.1; JOINED; Genomic_DNA.
DR EMBL; AF320246; AAK07425.1; JOINED; Genomic_DNA.
DR EMBL; AK291617; BAF84306.1; -; mRNA.
DR EMBL; AC011475; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471106; EAW84132.1; -; Genomic_DNA.
DR EMBL; BC048314; AAH48314.1; ALT_SEQ; mRNA.
DR EMBL; BC064836; AAH64836.1; -; mRNA.
DR EMBL; X98264; CAA66917.1; -; mRNA.
DR EMBL; X98265; CAA66918.1; -; mRNA.
DR EMBL; AF202445; AAF82685.1; -; Genomic_DNA.
DR EMBL; AF202445; AAF82686.1; -; Genomic_DNA.
DR EMBL; AF202445; AAF82687.1; -; Genomic_DNA.
DR EMBL; AF007140; AAC19152.1; -; mRNA.
DR PIR; B54857; B54857.
DR RefSeq; NP_001131145.1; NM_001137673.1.
DR RefSeq; NP_004507.2; NM_004516.3.
DR RefSeq; NP_036350.2; NM_012218.3.
DR RefSeq; NP_060090.2; NM_017620.2.
DR RefSeq; NP_703194.1; NM_153464.2.
DR RefSeq; XP_005259951.1; XM_005259894.1.
DR UniGene; Hs.465885; -.
DR PDB; 2L33; NMR; -; A=521-600.
DR PDB; 3P1X; X-ray; 1.90 A; A/B=520-594.
DR PDBsum; 2L33; -.
DR PDBsum; 3P1X; -.
DR ProteinModelPortal; Q12906; -.
DR SMR; Q12906; 6-374, 399-594.
DR DIP; DIP-29853N; -.
DR IntAct; Q12906; 48.
DR MINT; MINT-4999319; -.
DR PhosphoSite; Q12906; -.
DR DMDM; 62512150; -.
DR SWISS-2DPAGE; Q12906; -.
DR PaxDb; Q12906; -.
DR PRIDE; Q12906; -.
DR DNASU; 3609; -.
DR Ensembl; ENST00000250241; ENSP00000250241; ENSG00000129351.
DR Ensembl; ENST00000318511; ENSP00000315205; ENSG00000129351.
DR Ensembl; ENST00000407004; ENSP00000384660; ENSG00000129351.
DR Ensembl; ENST00000420083; ENSP00000405436; ENSG00000129351.
DR Ensembl; ENST00000449870; ENSP00000404121; ENSG00000129351.
DR Ensembl; ENST00000588657; ENSP00000468181; ENSG00000129351.
DR Ensembl; ENST00000589998; ENSP00000465219; ENSG00000129351.
DR Ensembl; ENST00000590261; ENSP00000468156; ENSG00000129351.
DR Ensembl; ENST00000592763; ENSP00000465515; ENSG00000129351.
DR GeneID; 3609; -.
DR KEGG; hsa:3609; -.
DR UCSC; uc002mpo.3; human.
DR CTD; 3609; -.
DR GeneCards; GC19P010764; -.
DR H-InvDB; HIX0014753; -.
DR HGNC; HGNC:6038; ILF3.
DR HPA; HPA001897; -.
DR MIM; 603182; gene.
DR neXtProt; NX_Q12906; -.
DR PharmGKB; PA29853; -.
DR eggNOG; NOG307678; -.
DR HOVERGEN; HBG069915; -.
DR InParanoid; Q12906; -.
DR KO; K13090; -.
DR OMA; PPKHAGK; -.
DR OrthoDB; EOG72ZCDC; -.
DR PhylomeDB; Q12906; -.
DR ChiTaRS; ILF3; human.
DR EvolutionaryTrace; Q12906; -.
DR GeneWiki; ILF3; -.
DR GenomeRNAi; 3609; -.
DR NextBio; 14109; -.
DR PMAP-CutDB; Q12906; -.
DR PRO; PR:Q12906; -.
DR ArrayExpress; Q12906; -.
DR Bgee; Q12906; -.
DR Genevestigator; Q12906; -.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0030529; C:ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0000279; P:M phase; NAS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-dependent; IDA:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; ISS:UniProtKB.
DR GO; GO:0045071; P:negative regulation of viral genome replication; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-dependent; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR Gene3D; 3.30.160.20; -; 2.
DR InterPro; IPR014720; dsRNA-bd_dom.
DR InterPro; IPR006561; DZF.
DR Pfam; PF00035; dsrm; 2.
DR Pfam; PF07528; DZF; 1.
DR SMART; SM00358; DSRM; 2.
DR SMART; SM00572; DZF; 1.
DR PROSITE; PS50137; DS_RBD; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Antiviral defense;
KW Complete proteome; Cytoplasm; Direct protein sequencing; DNA-binding;
KW Methylation; Nucleus; Phosphoprotein; Polymorphism;
KW Reference proteome; Repeat; RNA-binding; Transcription;
KW Transcription regulation.
FT CHAIN 1 894 Interleukin enhancer-binding factor 3.
FT /FTId=PRO_0000126070.
FT DOMAIN 94 342 DZF.
FT DOMAIN 398 467 DRBM 1.
FT DOMAIN 524 590 DRBM 2.
FT REGION 609 894 Interaction with PRMT1.
FT MOTIF 371 389 Bipartite nuclear localization signal
FT (Potential).
FT COMPBIAS 385 389 Poly-Lys.
FT COMPBIAS 634 637 Poly-Pro.
FT COMPBIAS 640 659 Arg/Gly-rich.
FT COMPBIAS 701 709 Poly-Gly.
FT COMPBIAS 794 798 Poly-Gly.
FT MOD_RES 62 62 Phosphoserine.
FT MOD_RES 100 100 N6-acetyllysine.
FT MOD_RES 188 188 Phosphothreonine; by PKR.
FT MOD_RES 190 190 Phosphoserine.
FT MOD_RES 315 315 Phosphothreonine; by PKR.
FT MOD_RES 382 382 Phosphoserine.
FT MOD_RES 384 384 Phosphoserine.
FT MOD_RES 460 460 N6-acetyllysine.
FT MOD_RES 476 476 Phosphoserine.
FT MOD_RES 482 482 Phosphoserine.
FT MOD_RES 592 592 Phosphothreonine.
FT MOD_RES 792 792 Phosphoserine.
FT MOD_RES 812 812 Phosphoserine.
FT VAR_SEQ 516 516 E -> ENVKQ (in isoform 4, isoform 6 and
FT isoform 7).
FT /FTId=VSP_003883.
FT VAR_SEQ 687 690 SQFY -> TGFV (in isoform 5).
FT /FTId=VSP_003886.
FT VAR_SEQ 688 702 QFYSNGGHSGNASGG -> DFFTDCYGYHDFGSS (in
FT isoform 2 and isoform 6).
FT /FTId=VSP_003888.
FT VAR_SEQ 688 694 QFYSNGG -> KCAFLSV (in isoform 4).
FT /FTId=VSP_003884.
FT VAR_SEQ 690 764 YSNGGHSGNASGGGGGGGGGSSGYGSYYQGDNYNSPVPPKH
FT AGKKQPHGGQQKPSYGSGYQSHQGQQQSYNQSPY -> SRP
FT PPPSRPRCCVVRCSGSPCGPSCDPYLAVFGTPCLQWFVSCH
FT YNFVWVEFLSFCSSVSLCLFTLRVSGNSVCL (in
FT isoform 3).
FT /FTId=VSP_003890.
FT VAR_SEQ 691 894 Missing (in isoform 5).
FT /FTId=VSP_003887.
FT VAR_SEQ 695 894 Missing (in isoform 4).
FT /FTId=VSP_003885.
FT VAR_SEQ 703 894 Missing (in isoform 2 and isoform 6).
FT /FTId=VSP_003889.
FT VAR_SEQ 765 894 Missing (in isoform 3).
FT /FTId=VSP_003891.
FT VARIANT 50 50 D -> H (in dbSNP:rs1064493).
FT /FTId=VAR_022159.
FT VARIANT 501 501 A -> S (in dbSNP:rs34520379).
FT /FTId=VAR_048906.
FT CONFLICT 101 101 G -> C (in Ref. 5; AAD51098/AAD51099 and
FT 6; AAK07424/AAK07425).
FT CONFLICT 260 260 G -> V (in Ref. 2; AAD33966 and 11;
FT CAA66918).
FT CONFLICT 647 647 S -> T (in Ref. 2; AAD33966 and 6;
FT AAK07424/AAK07425).
FT CONFLICT 688 689 QF -> N (in Ref. 13; AAF82687).
FT CONFLICT 763 763 P -> L (in Ref. 4; CAC01407).
FT CONFLICT 797 797 G -> R (in Ref. 4; CAC01124 and 6;
FT AAK07425).
FT CONFLICT 799 799 S -> SGS (in Ref. 13; AAF82685).
FT CONFLICT 813 813 G -> E (in Ref. 6; AAK07425).
FT HELIX 528 535
FT STRAND 541 548
FT STRAND 554 561
FT STRAND 564 572
FT HELIX 573 588
SQ SEQUENCE 894 AA; 95338 MW; 20903ABD0331F370 CRC64;
MRPMRIFVND DRHVMAKHSS VYPTQEELEA VQNMVSHTER ALKAVSDWID EQEKGSSEQA
ESDNMDVPPE DDSKEGAGEQ KTEHMTRTLR GVMRVGLVAK GLLLKGDLDL ELVLLCKEKP
TTALLDKVAD NLAIQLAAVT EDKYEILQSV DDAAIVIKNT KEPPLSLTIH LTSPVVREEM
EKVLAGETLS VNDPPDVLDR QKCLAALASL RHAKWFQARA NGLKSCVIVI RVLRDLCTRV
PTWGPLRGWP LELLCEKSIG TANRPMGAGE ALRRVLECLA SGIVMPDGSG IYDPCEKEAT
DAIGHLDRQQ REDITQSAQH ALRLAAFGQL HKVLGMDPLP SKMPKKPKNE NPVDYTVQIP
PSTTYAITPM KRPMEEDGEE KSPSKKKKKI QKKEEKAEPP QAMNALMRLN QLKPGLQYKL
VSQTGPVHAP IFTMSVEVDG NSFEASGPSK KTAKLHVAVK VLQDMGLPTG AEGRDSSKGE
DSAEETEAKP AVVAPAPVVE AVSTPSAAFP SDATAEQGPI LTKHGKNPVM ELNEKRRGLK
YELISETGGS HDKRFVMEVE VDGQKFQGAG SNKKVAKAYA ALAALEKLFP DTPLALDANK
KKRAPVPVRG GPKFAAKPHN PGFGMGGPMH NEVPPPPNLR GRGRGGSIRG RGRGRGFGGA
NHGGYMNAGA GYGSYGYGGN SATAGYSQFY SNGGHSGNAS GGGGGGGGGS SGYGSYYQGD
NYNSPVPPKH AGKKQPHGGQ QKPSYGSGYQ SHQGQQQSYN QSPYSNYGPP QGKQKGYNHG
QGSYSYSNSY NSPGGGGGSD YNYESKFNYS GSGGRSGGNS YGSGGASYNP GSHGGYGGGS
GGGSSYQGKQ GGYSQSNYNS PGSGQNYSGP PSSYQSSQGG YGRNADHSMN YQYR
//
MIM
603182
*RECORD*
*FIELD* NO
603182
*FIELD* TI
*603182 INTERLEUKIN ENHANCER-BINDING FACTOR 3; ILF3
;;NUCLEAR FACTOR OF ACTIVATED T CELLS, 90-KD; NF90;;
read moreDOUBLE-STRANDED RNA-BINDING PROTEIN, 76-KD; DRBP76;;
M-PHASE PHOSPHOPROTEIN 4; MPP4; MPHOSPH4;;
NUCLEAR FACTOR ASSOCIATED WITH DOUBLE-STRANDED RNA; NFAR
*FIELD* TX
For background information, see NF45 (ILF2; 603181).
CLONING
Kao et al. (1994) cloned cDNAs encoding NF45 and NF90. The NF90 gene
encodes a 671-amino acid polypeptide with limited similarity to several
RNA-binding proteins. The NF90 gene also appears to encode an
alternatively spliced 404-amino acid polypeptide, of which the first 394
amino acids are identical to the longer clone. Northern and Western blot
analysis demonstrated NF45 and NF90 expression in several cell types,
including both unstimulated and stimulated Jurkat T cells.
By immunoscreening a HeLa cell cDNA library for phosphoproteins,
Matsumoto-Taniura et al. (1996) isolated a partial cDNA encoding ILF3,
which they termed MPP4. Immunoprecipitation analysis indicated that MPP4
encodes 90- and 110-kD proteins. Immunofluorescence microscopy
demonstrated cytoplasmic expression during M phase and nuclear/nucleolar
expression during interphase.
Patel et al. (1999) purified double-stranded RNA (dsRNA)-binding
proteins from HeLa cell extracts and microsequenced a 90-kD protein with
identity to MPP4 in its N terminus. Using a yeast 2-hybrid screen with a
mutant RNA-activated protein kinase (PRKR; 176871) as bait, followed by
RT-PCR, they isolated a full-length cDNA encoding ILF3, which they
called DRBP76. Sequence analysis predicted that the 702-amino acid
protein has a bipartite nuclear localization signal, 2 dsRNA-binding
domains, an RG2 domain, and multiple potential phosphorylation sites.
SDS-PAGE analysis showed expression of a 90-kD protein, larger than the
calculated 76 kD. EMSA analysis confirmed the dsRNA binding activity of
DRBP76. Autoradiographic analysis indicated that DRBP76 is
phosphorylated by PRKR.
Langland et al. (1999) noted that NF90 is primarily localized to
ribosomes.
Saunders et al. (2001) obtained a cDNA encoding DRBP76, which they
termed NFAR1, as well as a variant cDNA encoding a 110-kD, 894-amino
acid protein they designated NFAR2. Sequence analysis showed that the
NFAR proteins share homology with a known PRKR substrate, the
translation initiation factor EIF2S1 (603907). Northern blot analysis
revealed ubiquitous expression of multiple transcripts ranging from 4.0
to 8.0 kb. Immunoblot analysis indicated variable expression with lower
amounts particularly notable in liver and spleen, suggesting
differential regulation at the translational or posttranslational level.
Immunoblot analysis and confocal microscopy demonstrated that PRKR and
both NFAR variants reciprocally coimmunoprecipitate and colocalize in
the nucleus. Immunoprecipitation analysis indicated an association with
spliceosomes.
Viranaicken et al. (2006) identified splice variants of human and mouse
ILF3 that encode long and short isoforms of the ILF3 and NF90 proteins
via inclusion or exclusion of 13 N-terminal residues, respectively.
GENE FUNCTION
Kao et al. (1994) showed that the NF45 and NF90 proteins form an NFAT
DNA-binding activity that is enhanced by T-cell stimulation and
inhibited by cyclosporin A and FK506.
Functional analysis by Saunders et al. (2001) indicated that both NFAR
proteins regulate gene transcription, probably at the level of mRNA
elongation. NFAR2 exhibited potent, constitutive regulatory activity
through its unique C-terminal region, which specifically interacted with
FUS (137070) and SMN1 (600354). Saunders et al. (2001) concluded that
NFARs facilitate dsRNA-regulated gene expression at the level of
posttranscription.
Shim et al. (2002) showed that NF90 binds to a subregion of the 3-prime
untranslated region that contains several AU-rich elements (AREs) and
slows down the degradation of IL2 (147680) mRNA. In nonstimulated cells,
NF90 was mostly nuclear, but T-cell activation resulted in its
accumulation in the cytoplasm. The authors concluded that nuclear export
of NF90 is required for IL2 mRNA stabilization.
Pfeifer et al. (2008) found that NFAR1 and NFAR2 were involved in
retaining cellular transcripts in intranuclear foci and could regulate
mRNA export to the cytoplasm. They also remained associated with
exported ribonucleoprotein complexes. Treatment of HeLa cells with small
interfering RNA to NFAR1 and/or NFAR2 resulted in an increase in protein
synthesis rates, particularly in the presence the mRNA export factors
TAP (NXF1; 602647), p15 (NXT1; 605811), or RAE1 (603343). Depletion of
NFAR in mouse fibroblasts or HeLa cells dramatically increased their
susceptibility to vesicular stomatitis virus or influenza virus,
respectively. Pfeifer et al. (2008) concluded that NFAR1 and NFAR2 are
retained on polyribosomes and act to govern translation rates, and that
they also play a role in innate immune defense to virus infection.
GENE STRUCTURE
By genomic sequence analysis, Saunders et al. (2001) determined that the
NFAR gene contains 21 exons and spans 16.2 kb. The 90-kD NFAR1 variant
expresses exon 18, which contains several stop codons that lead to
termination at amino acid 702. The 110-kD NFAR2 variant lacks exon 18
but contains exons 19, 20, and 21.
Viranaicken et al. (2006) identified an additional alternatively spliced
exon within intron 2 of the mouse and human ILF3 genes, increasing the
total number of exons to 22.
MAPPING
Saunders et al. (2001) mapped the NFAR gene to chromosome 19p13 by FISH.
ANIMAL MODEL
Pfeifer et al. (2008) found that mice lacking Nfar died in utero.
*FIELD* RF
1. Kao, P. N.; Chen, L.; Brock, G.; Ng, J.; Kenny, J.; Smith, A. J.;
Corthesy, B.: Cloning and expression of cyclosporin A- and FK506-sensitive
nuclear factor of activated T-cells: NF45 and NF90. J. Biol. Chem. 269:
20691-20699, 1994.
2. Langland, J. O.; Kao, P. N.; Jacobs, B. L.: Nuclear factor-90
of activated T-cells: a double-stranded RNA-binding protein and substrate
for the double-stranded RNA-dependent protein kinase, PKR. Biochemistry 38:
6361-6368, 1999.
3. Matsumoto-Taniura, N.; Pirollet, F.; Monroe, R.; Gerace, L.; Westendorf,
J. M.: Identification of novel M phase phosphoproteins by expression
cloning. Molec. Biol. Cell 7: 1455-1469, 1996.
4. Patel, R. C.; Vestal, D. J.; Xu, Z.; Bandyopadhyay, S.; Guo, W.;
Erme, S. M.; Williams, B. R. G.; Sen, G. C.: DRBP76, a double-stranded
RNA-binding nuclear protein, is phosphorylated by the interferon-induced
protein kinase, PKR. J. Biol. Chem. 274: 20432-20437, 1999.
5. Pfeifer, I.; Elsby, R.; Fernandez, M.; Faria, P. A.; Nussenzveig,
D. R.; Lossos, I. S.; Fontoura, B. M. A.; Martin, W. D.; Barber, G.
N.: NFAR-1 and -2 modulate translation and are required for efficient
host defense. Proc. Nat. Acad. Sci. 105: 4173-4178, 2008.
6. Saunders, L. R.; Jurecic, V.; Barber, G. N.: The 90- and 110-kDa
human NFAR proteins are translated from two differentially spliced
mRNAs encoded on chromosome 19p13. Genomics 71: 256-259, 2001.
7. Saunders, L. R.; Perkins, D. J.; Balachandran, S.; Michaels, R.;
Ford, R.; Mayeda, A.; Barber, G. N.: Characterization of two evolutionarily
conserved, alternatively spliced nuclear phosphoproteins, NFAR-1 and
-2, that function in mRNA processing and interact with the double-stranded
RNA-dependent protein kinase, PKR. J. Biol. Chem. 276: 32300-32312,
2001.
8. Shim, J.; Lim, H.; Yates, J. R., III; Karin, M.: Nuclear export
of NF90 is required for interleukin-2 mRNA stabilization. Molec.
Cell 10: 1331-1344, 2002.
9. Viranaicken, W.; Gasmi, L.; Chauvin, C.; Denoulet, P.; Larcher,
J.-C.: Identification of a newly spliced exon in the mouse Ilf3 gene
generating two long and short isoforms of Ilf3 and NF90. Genomics 88:
622-632, 2006.
*FIELD* CN
Paul J. Converse - updated: 7/2/2008
Patricia A. Hartz - updated: 11/8/2006
Stylianos E. Antonarakis - updated: 4/28/2003
Paul J. Converse - updated: 3/4/2002
*FIELD* CD
Jennifer P. Macke: 10/22/1998
*FIELD* ED
mgross: 07/11/2008
mgross: 7/11/2008
terry: 7/2/2008
mgross: 11/28/2006
terry: 11/8/2006
mgross: 4/28/2003
mgross: 3/4/2002
alopez: 10/22/1998
*RECORD*
*FIELD* NO
603182
*FIELD* TI
*603182 INTERLEUKIN ENHANCER-BINDING FACTOR 3; ILF3
;;NUCLEAR FACTOR OF ACTIVATED T CELLS, 90-KD; NF90;;
read moreDOUBLE-STRANDED RNA-BINDING PROTEIN, 76-KD; DRBP76;;
M-PHASE PHOSPHOPROTEIN 4; MPP4; MPHOSPH4;;
NUCLEAR FACTOR ASSOCIATED WITH DOUBLE-STRANDED RNA; NFAR
*FIELD* TX
For background information, see NF45 (ILF2; 603181).
CLONING
Kao et al. (1994) cloned cDNAs encoding NF45 and NF90. The NF90 gene
encodes a 671-amino acid polypeptide with limited similarity to several
RNA-binding proteins. The NF90 gene also appears to encode an
alternatively spliced 404-amino acid polypeptide, of which the first 394
amino acids are identical to the longer clone. Northern and Western blot
analysis demonstrated NF45 and NF90 expression in several cell types,
including both unstimulated and stimulated Jurkat T cells.
By immunoscreening a HeLa cell cDNA library for phosphoproteins,
Matsumoto-Taniura et al. (1996) isolated a partial cDNA encoding ILF3,
which they termed MPP4. Immunoprecipitation analysis indicated that MPP4
encodes 90- and 110-kD proteins. Immunofluorescence microscopy
demonstrated cytoplasmic expression during M phase and nuclear/nucleolar
expression during interphase.
Patel et al. (1999) purified double-stranded RNA (dsRNA)-binding
proteins from HeLa cell extracts and microsequenced a 90-kD protein with
identity to MPP4 in its N terminus. Using a yeast 2-hybrid screen with a
mutant RNA-activated protein kinase (PRKR; 176871) as bait, followed by
RT-PCR, they isolated a full-length cDNA encoding ILF3, which they
called DRBP76. Sequence analysis predicted that the 702-amino acid
protein has a bipartite nuclear localization signal, 2 dsRNA-binding
domains, an RG2 domain, and multiple potential phosphorylation sites.
SDS-PAGE analysis showed expression of a 90-kD protein, larger than the
calculated 76 kD. EMSA analysis confirmed the dsRNA binding activity of
DRBP76. Autoradiographic analysis indicated that DRBP76 is
phosphorylated by PRKR.
Langland et al. (1999) noted that NF90 is primarily localized to
ribosomes.
Saunders et al. (2001) obtained a cDNA encoding DRBP76, which they
termed NFAR1, as well as a variant cDNA encoding a 110-kD, 894-amino
acid protein they designated NFAR2. Sequence analysis showed that the
NFAR proteins share homology with a known PRKR substrate, the
translation initiation factor EIF2S1 (603907). Northern blot analysis
revealed ubiquitous expression of multiple transcripts ranging from 4.0
to 8.0 kb. Immunoblot analysis indicated variable expression with lower
amounts particularly notable in liver and spleen, suggesting
differential regulation at the translational or posttranslational level.
Immunoblot analysis and confocal microscopy demonstrated that PRKR and
both NFAR variants reciprocally coimmunoprecipitate and colocalize in
the nucleus. Immunoprecipitation analysis indicated an association with
spliceosomes.
Viranaicken et al. (2006) identified splice variants of human and mouse
ILF3 that encode long and short isoforms of the ILF3 and NF90 proteins
via inclusion or exclusion of 13 N-terminal residues, respectively.
GENE FUNCTION
Kao et al. (1994) showed that the NF45 and NF90 proteins form an NFAT
DNA-binding activity that is enhanced by T-cell stimulation and
inhibited by cyclosporin A and FK506.
Functional analysis by Saunders et al. (2001) indicated that both NFAR
proteins regulate gene transcription, probably at the level of mRNA
elongation. NFAR2 exhibited potent, constitutive regulatory activity
through its unique C-terminal region, which specifically interacted with
FUS (137070) and SMN1 (600354). Saunders et al. (2001) concluded that
NFARs facilitate dsRNA-regulated gene expression at the level of
posttranscription.
Shim et al. (2002) showed that NF90 binds to a subregion of the 3-prime
untranslated region that contains several AU-rich elements (AREs) and
slows down the degradation of IL2 (147680) mRNA. In nonstimulated cells,
NF90 was mostly nuclear, but T-cell activation resulted in its
accumulation in the cytoplasm. The authors concluded that nuclear export
of NF90 is required for IL2 mRNA stabilization.
Pfeifer et al. (2008) found that NFAR1 and NFAR2 were involved in
retaining cellular transcripts in intranuclear foci and could regulate
mRNA export to the cytoplasm. They also remained associated with
exported ribonucleoprotein complexes. Treatment of HeLa cells with small
interfering RNA to NFAR1 and/or NFAR2 resulted in an increase in protein
synthesis rates, particularly in the presence the mRNA export factors
TAP (NXF1; 602647), p15 (NXT1; 605811), or RAE1 (603343). Depletion of
NFAR in mouse fibroblasts or HeLa cells dramatically increased their
susceptibility to vesicular stomatitis virus or influenza virus,
respectively. Pfeifer et al. (2008) concluded that NFAR1 and NFAR2 are
retained on polyribosomes and act to govern translation rates, and that
they also play a role in innate immune defense to virus infection.
GENE STRUCTURE
By genomic sequence analysis, Saunders et al. (2001) determined that the
NFAR gene contains 21 exons and spans 16.2 kb. The 90-kD NFAR1 variant
expresses exon 18, which contains several stop codons that lead to
termination at amino acid 702. The 110-kD NFAR2 variant lacks exon 18
but contains exons 19, 20, and 21.
Viranaicken et al. (2006) identified an additional alternatively spliced
exon within intron 2 of the mouse and human ILF3 genes, increasing the
total number of exons to 22.
MAPPING
Saunders et al. (2001) mapped the NFAR gene to chromosome 19p13 by FISH.
ANIMAL MODEL
Pfeifer et al. (2008) found that mice lacking Nfar died in utero.
*FIELD* RF
1. Kao, P. N.; Chen, L.; Brock, G.; Ng, J.; Kenny, J.; Smith, A. J.;
Corthesy, B.: Cloning and expression of cyclosporin A- and FK506-sensitive
nuclear factor of activated T-cells: NF45 and NF90. J. Biol. Chem. 269:
20691-20699, 1994.
2. Langland, J. O.; Kao, P. N.; Jacobs, B. L.: Nuclear factor-90
of activated T-cells: a double-stranded RNA-binding protein and substrate
for the double-stranded RNA-dependent protein kinase, PKR. Biochemistry 38:
6361-6368, 1999.
3. Matsumoto-Taniura, N.; Pirollet, F.; Monroe, R.; Gerace, L.; Westendorf,
J. M.: Identification of novel M phase phosphoproteins by expression
cloning. Molec. Biol. Cell 7: 1455-1469, 1996.
4. Patel, R. C.; Vestal, D. J.; Xu, Z.; Bandyopadhyay, S.; Guo, W.;
Erme, S. M.; Williams, B. R. G.; Sen, G. C.: DRBP76, a double-stranded
RNA-binding nuclear protein, is phosphorylated by the interferon-induced
protein kinase, PKR. J. Biol. Chem. 274: 20432-20437, 1999.
5. Pfeifer, I.; Elsby, R.; Fernandez, M.; Faria, P. A.; Nussenzveig,
D. R.; Lossos, I. S.; Fontoura, B. M. A.; Martin, W. D.; Barber, G.
N.: NFAR-1 and -2 modulate translation and are required for efficient
host defense. Proc. Nat. Acad. Sci. 105: 4173-4178, 2008.
6. Saunders, L. R.; Jurecic, V.; Barber, G. N.: The 90- and 110-kDa
human NFAR proteins are translated from two differentially spliced
mRNAs encoded on chromosome 19p13. Genomics 71: 256-259, 2001.
7. Saunders, L. R.; Perkins, D. J.; Balachandran, S.; Michaels, R.;
Ford, R.; Mayeda, A.; Barber, G. N.: Characterization of two evolutionarily
conserved, alternatively spliced nuclear phosphoproteins, NFAR-1 and
-2, that function in mRNA processing and interact with the double-stranded
RNA-dependent protein kinase, PKR. J. Biol. Chem. 276: 32300-32312,
2001.
8. Shim, J.; Lim, H.; Yates, J. R., III; Karin, M.: Nuclear export
of NF90 is required for interleukin-2 mRNA stabilization. Molec.
Cell 10: 1331-1344, 2002.
9. Viranaicken, W.; Gasmi, L.; Chauvin, C.; Denoulet, P.; Larcher,
J.-C.: Identification of a newly spliced exon in the mouse Ilf3 gene
generating two long and short isoforms of Ilf3 and NF90. Genomics 88:
622-632, 2006.
*FIELD* CN
Paul J. Converse - updated: 7/2/2008
Patricia A. Hartz - updated: 11/8/2006
Stylianos E. Antonarakis - updated: 4/28/2003
Paul J. Converse - updated: 3/4/2002
*FIELD* CD
Jennifer P. Macke: 10/22/1998
*FIELD* ED
mgross: 07/11/2008
mgross: 7/11/2008
terry: 7/2/2008
mgross: 11/28/2006
terry: 11/8/2006
mgross: 4/28/2003
mgross: 3/4/2002
alopez: 10/22/1998