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 27-MAR-2024, entry version 238. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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. DR RefSeq; XP_016882252.1; XM_017026763.1. DR PDB; 2L33; NMR; -; A=521-600. DR PDB; 3P1X; X-ray; 1.90 A; A/B=520-594. DR PDB; 7RJM; X-ray; 2.10 A; C=99-106. DR PDB; 7RJQ; X-ray; 1.72 A; B=99-106. DR PDBsum; 2L33; -. DR PDBsum; 3P1X; -. DR PDBsum; 7RJM; -. DR PDBsum; 7RJQ; -. DR AlphaFoldDB; Q12906; -. DR SMR; Q12906; -. DR BioGRID; 109822; 856. DR CORUM; Q12906; -. DR DIP; DIP-29853N; -. DR IntAct; Q12906; 146. DR MINT; Q12906; -. DR STRING; 9606.ENSP00000404121; -. DR GlyGen; Q12906; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; Q12906; -. DR MetOSite; Q12906; -. DR PhosphoSitePlus; Q12906; -. DR SwissPalm; Q12906; -. DR BioMuta; ILF3; -. DR DMDM; 62512150; -. DR CPTAC; CPTAC-395; -. DR CPTAC; CPTAC-396; -. DR EPD; Q12906; -. DR jPOST; Q12906; -. DR MassIVE; Q12906; -. DR MaxQB; Q12906; -. DR PaxDb; 9606-ENSP00000404121; -. DR PeptideAtlas; 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 Pumba; Q12906; -. DR TopDownProteomics; Q12906-1; -. [Q12906-1] DR Antibodypedia; 1051; 426 antibodies from 37 providers. DR DNASU; 3609; -. DR Ensembl; ENST00000250241.12; ENSP00000250241.8; ENSG00000129351.18. [Q12906-5] DR Ensembl; ENST00000407004.8; ENSP00000384660.2; ENSG00000129351.18. [Q12906-6] DR Ensembl; ENST00000588657.6; ENSP00000468181.1; ENSG00000129351.18. [Q12906-7] DR Ensembl; ENST00000589998.6; ENSP00000465219.1; ENSG00000129351.18. [Q12906-2] DR Ensembl; ENST00000590261.5; ENSP00000468156.1; ENSG00000129351.18. [Q12906-1] DR Ensembl; ENST00000592763.5; ENSP00000465515.1; ENSG00000129351.18. [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 AGR; HGNC:6038; -. 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; PANHTQY; -. DR OrthoDB; 4565640at2759; -. DR PhylomeDB; Q12906; -. DR TreeFam; TF320194; -. DR PathwayCommons; Q12906; -. DR Reactome; R-HSA-9762293; Regulation of CDH11 gene transcription. DR Reactome; R-HSA-9833482; PKR-mediated signaling. DR SignaLink; Q12906; -. DR SIGNOR; Q12906; -. DR BioGRID-ORCS; 3609; 672 hits in 1165 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 207 other cell types or tissues. DR ExpressionAtlas; Q12906; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. 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:0001618; F:virus receptor activity; IDA:UniProt. DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; 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 DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB. DR CDD; cd19910; DSRM_ILF3_rpt1; 1. DR CDD; cd19912; DSRM_ILF3_rpt2; 1. DR Gene3D; 1.10.1410.40; -; 1. DR Gene3D; 3.30.160.20; -; 2. DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 2. DR InterPro; IPR014720; dsRBD_dom. DR InterPro; IPR033099; DSRM1_ILF3. DR InterPro; IPR006561; DZF_dom. DR InterPro; IPR049402; DZF_dom_C. DR InterPro; IPR049401; DZF_dom_N. DR InterPro; IPR043519; NT_sf. DR PANTHER; PTHR45762:SF4; INTERLEUKIN ENHANCER-BINDING FACTOR 3; 1. DR PANTHER; PTHR45762; ZINC FINGER RNA-BINDING PROTEIN; 1. DR Pfam; PF00035; dsrm; 2. DR Pfam; PF20965; DZF_C; 1. DR Pfam; PF07528; DZF_N; 1. DR SMART; SM00358; DSRM; 2. DR SMART; SM00572; DZF; 1. DR SUPFAM; SSF54768; dsRNA-binding domain-like; 2. DR PROSITE; PS50137; DS_RBD; 2. DR PROSITE; PS51703; DZF; 1. DR SWISS-2DPAGE; Q12906; -. DR Genevisible; Q12906; HS. 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; FT AAK07424/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 102..104 FT /evidence="ECO:0007829|PDB:7RJQ" 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 //