ILF3_HUMAN
ID ILF3_HUMAN Reviewed; 894 AA.
AC Q12906; A8K6F2; G5E9M5; O43409; Q6P1X1; Q86XY7; Q99544; Q99545; Q9BZH4;
AC Q9BZH5; Q9NQ95; Q9NQ96; Q9NQ97; Q9NQ98; Q9NQ99; Q9NQA0; Q9NQA1; Q9NQA2;
AC Q9NRN2; Q9NRN3; Q9NRN4; Q9UMZ9; Q9UN00; Q9UN84; Q9UNA2;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 3.
DT 03-AUG-2022, entry version 229.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 19-41;
RP 491-510 AND 555-565.
RC TISSUE=T-cell lymphoma;
RX PubMed=7519613; DOI=10.1016/s0021-9258(17)32048-3;
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 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 phosphorylated
RT 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 and
RT 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 3
RT (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 spliced
RT nuclear phosphoproteins, NFAR-1 and -2, that function in mRNA processing
RT and interact with the double-stranded RNA-dependent protein kinase, PKR.";
RL J. Biol. Chem. 276:32300-32312(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 project:
RT 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., Westendorf J.M.;
RT "Identification of novel M phase phosphoproteins by expression cloning.";
RL Mol. Biol. Cell 7:1455-1469(1996).
RN [12]
RP PROTEIN SEQUENCE OF 1-10, FUNCTION, AND INTERACTION WITH XRCC6; PRKDC AND
RP 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., 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-stranded
RT RNA-binding domains as well as DNA binding activity.";
RL J. Biol. Chem. 274:34598-34604(1999).
RN [16]
RP INTERACTION WITH PRMT1, SUBCELLULAR LOCATION, AND METHYLATION.
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-arginine
RT methyltransferase in cells, interacts with and is regulated by interleukin
RT 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].
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 positive and
RT negative regulator of gene expression in mammalian cells.";
RL Mol. Cell. Biol. 22:343-356(2002).
RN [20]
RP IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH XPO5; RAN AND VA1
RP 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 of
RT the double-stranded RNA-binding protein ILF3.";
RL J. Biol. Chem. 279:884-891(2004).
RN [21]
RP FUNCTION, INTERACTION WITH DHX36 AND ELAVL1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=14731398; DOI=10.1016/s1097-2765(03)00481-7;
RA Tran H., Schilling M., Wirbelauer C., Hess D., Nagamine Y.;
RT "Facilitation of mRNA deadenylation and decay by the exosome-bound, DExH
RT protein RHAU.";
RL Mol. Cell 13:101-111(2004).
RN [22]
RP IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH XPO5; RAN; ZNF346
RP 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-5.";
RL Mol. Cell. Biol. 24:6608-6619(2004).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-482 AND THR-592, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-592, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [25]
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., Morrice N.,
RA Glover M., Lamond A.I., Moorhead G.B.G.;
RT "The nuclear PP1 interacting protein ZAP3 (ZAP) is a putative nucleoside
RT kinase that complexes with SAM68, CIA, NF110/45, and HNRNP-G.";
RL Biochim. Biophys. Acta 1774:1339-1350(2007).
RN [26]
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-protein
RT complexes in human cells.";
RL EMBO Rep. 8:1052-1060(2007).
RN [27]
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 [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190; SER-792 AND SER-812,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-482 (ISOFORMS 4; 6 AND 7),
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [29]
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., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [30]
RP IDENTIFICATION IN A MRNP COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19029303; DOI=10.1261/rna.1175909;
RA Weidensdorfer D., Stoehr N., Baude A., Lederer M., Koehn M., Schierhorn A.,
RA Buchmeier S., Wahle E., Huettelmaiery S.;
RT "Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic RNPs.";
RL RNA 15:104-115(2009).
RN [31]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-592 AND SER-792,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-482 (ISOFORMS 4; 6 AND 7),
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [32]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-100 AND LYS-460, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA 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 [33]
RP FUNCTION, 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 kinase
RT PKR constitutes a novel mechanism of translational regulation and cellular
RT defense.";
RL Genes Dev. 24:2640-2653(2010).
RN [34]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62; SER-190; SER-382;
RP SER-384; SER-482; THR-592 AND SER-812, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [35]
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., Buerckstuemmer T.,
RA 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 [36]
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 IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [37]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62; SER-382; THR-592; SER-792
RP AND SER-816, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [38]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62; SER-476; SER-477; SER-482
RP AND SER-810, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [39]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-348, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [40]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH ILF2.
RX PubMed=26240280; DOI=10.1128/mcb.00306-15;
RA Wandrey F., Montellese C., Koos K., Badertscher L., Bammert L., Cook A.G.,
RA Zemp I., Horvath P., Kutay U.;
RT "The NF45/NF90 Heterodimer Contributes to the Biogenesis of 60S Ribosomal
RT Subunits and Influences Nucleolar Morphology.";
RL Mol. Cell. Biol. 35:3491-3503(2015).
RN [41]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=26891316; DOI=10.3390/v8020047;
RA Li Y., Belshan M.;
RT "NF45 and NF90 Bind HIV-1 RNA and Modulate HIV Gene Expression.";
RL Viruses 8:0-0(2016).
RN [42]
RP FUNCTION, INTERACTION WITH ILF2, AND SUBCELLULAR LOCATION.
RX PubMed=28625552; DOI=10.1016/j.molcel.2017.05.023;
RA Li X., Liu C.X., Xue W., Zhang Y., Jiang S., Yin Q.F., Wei J., Yao R.W.,
RA Yang L., Chen L.L.;
RT "Coordinated circRNA Biogenesis and Function with NF90/NF110 in Viral
RT Infection.";
RL Mol. Cell 0:0-0(2017).
RN [43]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-396 AND LYS-489, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [44]
RP FUNCTION, UBIQUITINATION AT LYS-297, MUTAGENESIS OF LYS-297, AND
RP INTERACTION WITH HAVCR2.
RX PubMed=34110282; DOI=10.7554/elife.66501;
RA Dou S., Li G., Li G., Hou C., Zheng Y., Tang L., Gao Y., Mo R., Li Y.,
RA Wang R., Shen B., Zhang J., Han G.;
RT "Ubiquitination and degradation of NF90 by Tim-3 inhibits antiviral innate
RT immunity.";
RL Elife 10:0-0(2021).
RN [45]
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 factor
RT 3 from Homo sapiens, Northeast structural genomics consortium target
RT HR4527E.";
RL Submitted (DEC-2010) to the PDB data bank.
RN [46]
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: RNA-binding protein that plays an essential role in the
CC biogenesis of circular RNAs (circRNAs) which are produced by back-
CC splicing circularization of pre-mRNAs. Within the nucleus, promotes
CC circRNAs processing by stabilizing the regulatory elements residing in
CC the flanking introns of the circularized exons. Plays thereby a role in
CC the back-splicing of a subset of circRNAs (PubMed:28625552). As a
CC consequence, participates in a wide range of transcriptional and post-
CC transcriptional processes. Binds to poly-U elements and AU-rich
CC elements (AREs) in the 3'-UTR of target mRNAs (PubMed:14731398). Upon
CC viral infection, ILF3 accumulates in the cytoplasm and participates in
CC the innate antiviral response (PubMed:21123651, PubMed:34110282).
CC Mechanistically, ILF3 becomes phosphorylated and activated by the
CC double-stranded RNA-activated protein kinase/PKR which releases ILF3
CC from cellular mature circRNAs. In turn, unbound ILF3 molecules are able
CC to interact with and thus inhibit viral mRNAs (PubMed:21123651,
CC PubMed:28625552). {ECO:0000269|PubMed:14731398,
CC ECO:0000269|PubMed:21123651, ECO:0000269|PubMed:28625552,
CC ECO:0000269|PubMed:9442054}.
CC -!- FUNCTION: (Microbial infection) Plays a positive role in HIV-1 virus
CC production by binding to and thereby stabilizing HIV-1 RNA, together
CC with ILF3. {ECO:0000269|PubMed:26891316}.
CC -!- SUBUNIT: Identified in a IGF2BP1-dependent mRNP granule complex
CC containing untranslated mRNAs. Interacts with FUS and SMN. Interacts
CC (via C-terminus) with PRMT1. Forms a complex with ILF2. Can also bind
CC to 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 export
CC complex with XPO5, ILF3, Ran and double-stranded RNA or double-stranded
CC minihelix VA1 RNA. Found in a nuclear export complex with XPO5, RAN,
CC ILF3, ZNF346 and double-stranded RNA. Interacts with XPO5 and ZNF346.
CC Forms a complex with ILF2, YLPM1, KHDRBS1, RBMX, NCOA5 and PPP1CA.
CC Interacts with AGO1 and AGO2. Interacts with DHX36; this interaction
CC occurs in a RNA-dependent manner (PubMed:14731398). Interacts with
CC ELAVL1; this interaction occurs in a RNA-dependent manner
CC (PubMed:14731398). Interacts with HAVCR2; this interaction promotes
CC ILF3 ubiquitination and subsequent degradation (PubMed:34110282).
CC {ECO:0000269|PubMed:10574923, ECO:0000269|PubMed:10749851,
CC ECO:0000269|PubMed:11739746, ECO:0000269|PubMed:11777942,
CC ECO:0000269|PubMed:14570900, ECO:0000269|PubMed:14731398,
CC ECO:0000269|PubMed:15254228, ECO:0000269|PubMed:17289661,
CC ECO:0000269|PubMed:17890166, ECO:0000269|PubMed:17932509,
CC ECO:0000269|PubMed:19029303, ECO:0000269|PubMed:26240280,
CC ECO:0000269|PubMed:28625552, ECO:0000269|PubMed:34110282,
CC ECO:0000269|PubMed:9442054}.
CC -!- INTERACTION:
CC Q12906; P14866-1: HNRNPL; NbExp=2; IntAct=EBI-78756, EBI-16071645;
CC Q12906; Q99873: PRMT1; NbExp=2; IntAct=EBI-78756, EBI-78738;
CC Q12906; P08325: M; Xeno; NbExp=2; IntAct=EBI-78756, EBI-15693250;
CC Q12906; P03496: NS; Xeno; NbExp=3; IntAct=EBI-78756, EBI-2547442;
CC Q12906; Q05127: VP35; Xeno; NbExp=6; IntAct=EBI-78756, EBI-6148294;
CC Q12906-6; Q13148: TARDBP; NbExp=6; IntAct=EBI-12904528, EBI-372899;
CC Q12906-6; A5D8V6: VPS37C; NbExp=3; IntAct=EBI-12904528, EBI-2559305;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:26240280}.
CC Cytoplasm {ECO:0000269|PubMed:28625552}. Nucleus
CC {ECO:0000269|PubMed:10749851, ECO:0000269|PubMed:26240280,
CC ECO:0000269|PubMed:28625552}. Note=Localizes in the cytoplasm in
CC response to viral infection. The unphosphorylated form is retained in
CC the nucleus by ILF2. Phosphorylation at Thr-188 and Thr-315 causes the
CC dissociation of ILF2 from the ILF2-ILF3 complex resulting in a
CC cytoplasmic sequestration of ILF3. Localized in cytoplasmic mRNP
CC granules containing untranslated mRNAs. {ECO:0000269|PubMed:21123651}.
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 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 Name=7;
CC IsoId=Q12906-7; Sequence=VSP_003883;
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 dissociation
CC of ILF2 from the ILF2-ILF3 complex resulting in a cytoplasmic
CC sequestration of ILF3 where it can bind to viral RNAs and impede viral
CC replication. {ECO:0000269|PubMed:21123651}.
CC -!- PTM: Methylated by protein arginine N-methyltransferase 1.
CC {ECO:0000269|PubMed:10749851}.
CC -!- PTM: Ubiquitinated at Lys-297 in a TRIM47-dependent manner; this 'Lys-
CC 48'-linked ubiquitination promotes ILF3 degradation.
CC {ECO:0000269|PubMed:34110282}.
CC -!- MISCELLANEOUS: [Isoform 3]: Dubious isoform produced through aberrant
CC splice sites. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA20994.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
CC Sequence=AAH48314.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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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 CCDS; CCDS12246.1; -. [Q12906-1]
DR CCDS; CCDS12247.1; -. [Q12906-2]
DR CCDS; CCDS45965.1; -. [Q12906-7]
DR CCDS; CCDS45966.1; -. [Q12906-5]
DR CCDS; CCDS45967.1; -. [Q12906-6]
DR PIR; B54857; B54857.
DR RefSeq; NP_001131145.1; NM_001137673.1. [Q12906-6]
DR RefSeq; NP_004507.2; NM_004516.3. [Q12906-2]
DR RefSeq; NP_036350.2; NM_012218.3. [Q12906-1]
DR RefSeq; NP_060090.2; NM_017620.2. [Q12906-7]
DR RefSeq; NP_703194.1; NM_153464.2. [Q12906-5]
DR RefSeq; XP_011526286.2; XM_011527984.2. [Q12906-7]
DR RefSeq; XP_016882252.1; XM_017026763.1. [Q12906-7]
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 AlphaFoldDB; Q12906; -.
DR SMR; Q12906; -.
DR BioGRID; 109822; 652.
DR CORUM; Q12906; -.
DR DIP; DIP-29853N; -.
DR IntAct; Q12906; 135.
DR MINT; Q12906; -.
DR STRING; 9606.ENSP00000404121; -.
DR GlyGen; Q12906; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q12906; -.
DR MetOSite; Q12906; -.
DR PhosphoSitePlus; Q12906; -.
DR SwissPalm; Q12906; -.
DR BioMuta; ILF3; -.
DR DMDM; 62512150; -.
DR SWISS-2DPAGE; Q12906; -.
DR CPTAC; CPTAC-395; -.
DR CPTAC; CPTAC-396; -.
DR EPD; Q12906; -.
DR jPOST; Q12906; -.
DR MassIVE; Q12906; -.
DR MaxQB; Q12906; -.
DR PaxDb; Q12906; -.
DR PeptideAtlas; Q12906; -.
DR PRIDE; Q12906; -.
DR ProteomicsDB; 33984; -.
DR ProteomicsDB; 59014; -. [Q12906-1]
DR ProteomicsDB; 59015; -. [Q12906-2]
DR ProteomicsDB; 59016; -. [Q12906-3]
DR ProteomicsDB; 59017; -. [Q12906-4]
DR ProteomicsDB; 59018; -. [Q12906-5]
DR ProteomicsDB; 59019; -. [Q12906-6]
DR TopDownProteomics; Q12906-1; -. [Q12906-1]
DR Antibodypedia; 1051; 360 antibodies from 37 providers.
DR DNASU; 3609; -.
DR Ensembl; ENST00000250241.12; ENSP00000250241.8; ENSG00000129351.17. [Q12906-5]
DR Ensembl; ENST00000407004.7; ENSP00000384660.2; ENSG00000129351.17. [Q12906-6]
DR Ensembl; ENST00000449870.5; ENSP00000404121.1; ENSG00000129351.17. [Q12906-7]
DR Ensembl; ENST00000588657.5; ENSP00000468181.1; ENSG00000129351.17. [Q12906-7]
DR Ensembl; ENST00000589998.5; ENSP00000465219.1; ENSG00000129351.17. [Q12906-2]
DR Ensembl; ENST00000590261.5; ENSP00000468156.1; ENSG00000129351.17. [Q12906-1]
DR Ensembl; ENST00000592763.5; ENSP00000465515.1; ENSG00000129351.17. [Q12906-4]
DR GeneID; 3609; -.
DR KEGG; hsa:3609; -.
DR MANE-Select; ENST00000588657.6; ENSP00000468181.1; NM_017620.3; NP_060090.2. [Q12906-7]
DR UCSC; uc002mpl.3; human. [Q12906-1]
DR CTD; 3609; -.
DR DisGeNET; 3609; -.
DR GeneCards; ILF3; -.
DR HGNC; HGNC:6038; ILF3.
DR HPA; ENSG00000129351; Low tissue specificity.
DR MIM; 603182; gene.
DR neXtProt; NX_Q12906; -.
DR OpenTargets; ENSG00000129351; -.
DR PharmGKB; PA29853; -.
DR VEuPathDB; HostDB:ENSG00000129351; -.
DR eggNOG; KOG3792; Eukaryota.
DR GeneTree; ENSGT00940000156719; -.
DR HOGENOM; CLU_015490_0_0_1; -.
DR InParanoid; Q12906; -.
DR OMA; YYQGGDN; -.
DR OrthoDB; 612611at2759; -.
DR PhylomeDB; Q12906; -.
DR TreeFam; TF320194; -.
DR PathwayCommons; Q12906; -.
DR SignaLink; Q12906; -.
DR SIGNOR; Q12906; -.
DR BioGRID-ORCS; 3609; 641 hits in 1087 CRISPR screens.
DR ChiTaRS; ILF3; human.
DR EvolutionaryTrace; Q12906; -.
DR GeneWiki; ILF3; -.
DR GenomeRNAi; 3609; -.
DR Pharos; Q12906; Tbio.
DR PRO; PR:Q12906; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q12906; protein.
DR Bgee; ENSG00000129351; Expressed in ganglionic eminence and 205 other tissues.
DR ExpressionAtlas; Q12906; baseline and differential.
DR Genevisible; Q12906; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:1990904; 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:0035925; F:mRNA 3'-UTR AU-rich region binding; IDA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003727; F:single-stranded RNA binding; IBA:GO_Central.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; 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-templated; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR Gene3D; 3.30.460.10; -; 2.
DR InterPro; IPR014720; dsRBD_dom.
DR InterPro; IPR006561; DZF_dom.
DR InterPro; IPR033099; ILF3/NF90.
DR InterPro; IPR043519; NT_sf.
DR PANTHER; PTHR45762:SF4; PTHR45762:SF4; 3.
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.
DR PROSITE; PS51703; DZF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Antiviral defense;
KW Cytoplasm; Direct protein sequencing; DNA-binding; Isopeptide bond;
KW Methylation; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding; Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..894
FT /note="Interleukin enhancer-binding factor 3"
FT /id="PRO_0000126070"
FT DOMAIN 5..378
FT /note="DZF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01040"
FT DOMAIN 398..467
FT /note="DRBM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT DOMAIN 524..590
FT /note="DRBM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT REGION 50..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..894
FT /note="Interaction with PRMT1"
FT /evidence="ECO:0000269|PubMed:10749851"
FT REGION 625..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 718..894
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 371..389
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 67..86
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..399
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..827
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 843..894
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 100
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 188
FT /note="Phosphothreonine; by PKR"
FT /evidence="ECO:0000269|PubMed:21123651"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 315
FT /note="Phosphothreonine; by PKR"
FT /evidence="ECO:0000269|PubMed:21123651"
FT MOD_RES 382
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 460
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 476
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 477
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 592
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 792
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 810
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 812
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 816
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 297
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:34110282"
FT CROSSLNK 348
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 396
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 489
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 516
FT /note="E -> ENVKQ (in isoform 4, isoform 6 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:11167023,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT /id="VSP_003883"
FT VAR_SEQ 687..690
FT /note="SQFY -> TGFV (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:11167023"
FT /id="VSP_003886"
FT VAR_SEQ 688..702
FT /note="QFYSNGGHSGNASGG -> DFFTDCYGYHDFGSS (in isoform 2 and
FT isoform 6)"
FT /evidence="ECO:0000303|PubMed:10400669,
FT ECO:0000303|PubMed:11161820, ECO:0000303|PubMed:11167023,
FT ECO:0000303|PubMed:11438536, ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.13"
FT /id="VSP_003888"
FT VAR_SEQ 688..694
FT /note="QFYSNGG -> KCAFLSV (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11167023"
FT /id="VSP_003884"
FT VAR_SEQ 690..764
FT /note="YSNGGHSGNASGGGGGGGGGSSGYGSYYQGDNYNSPVPPKHAGKKQPHGGQQ
FT KPSYGSGYQSHQGQQQSYNQSPY -> SRPPPPSRPRCCVVRCSGSPCGPSCDPYLAVF
FT GTPCLQWFVSCHYNFVWVEFLSFCSSVSLCLFTLRVSGNSVCL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10607473, ECO:0000303|Ref.13"
FT /id="VSP_003890"
FT VAR_SEQ 691..894
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:11167023"
FT /id="VSP_003887"
FT VAR_SEQ 695..894
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11167023"
FT /id="VSP_003885"
FT VAR_SEQ 703..894
FT /note="Missing (in isoform 2 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:10400669,
FT ECO:0000303|PubMed:11161820, ECO:0000303|PubMed:11167023,
FT ECO:0000303|PubMed:11438536, ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.13"
FT /id="VSP_003889"
FT VAR_SEQ 765..894
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10607473, ECO:0000303|Ref.13"
FT /id="VSP_003891"
FT VARIANT 50
FT /note="D -> H (in dbSNP:rs1064493)"
FT /evidence="ECO:0000269|PubMed:11161820"
FT /id="VAR_022159"
FT VARIANT 501
FT /note="A -> S (in dbSNP:rs34520379)"
FT /id="VAR_048906"
FT CONFLICT 101
FT /note="G -> C (in Ref. 5; AAD51098/AAD51099 and 6;
FT AAK07424/AAK07425)"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="G -> V (in Ref. 2; AAD33966 and 11; CAA66918)"
FT /evidence="ECO:0000305"
FT CONFLICT 647
FT /note="S -> T (in Ref. 2; AAD33966 and 6; AAK07424/
FT AAK07425)"
FT /evidence="ECO:0000305"
FT CONFLICT 688..689
FT /note="QF -> N (in Ref. 13; AAF82687)"
FT /evidence="ECO:0000305"
FT CONFLICT 763
FT /note="P -> L (in Ref. 4; CAC01407)"
FT /evidence="ECO:0000305"
FT CONFLICT 797
FT /note="G -> R (in Ref. 4; CAC01124 and 6; AAK07425)"
FT /evidence="ECO:0000305"
FT CONFLICT 799
FT /note="S -> SGS (in Ref. 13; AAF82685)"
FT /evidence="ECO:0000305"
FT CONFLICT 813
FT /note="G -> E (in Ref. 6; AAK07425)"
FT /evidence="ECO:0000305"
FT HELIX 528..535
FT /evidence="ECO:0007829|PDB:3P1X"
FT STRAND 541..548
FT /evidence="ECO:0007829|PDB:3P1X"
FT STRAND 554..561
FT /evidence="ECO:0007829|PDB:3P1X"
FT STRAND 564..572
FT /evidence="ECO:0007829|PDB:3P1X"
FT HELIX 573..588
FT /evidence="ECO:0007829|PDB:3P1X"
FT MOD_RES Q12906-4:482
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES Q12906-6:482
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES Q12906-7:482
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
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
