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UniProtKB/Swiss-Prot entry Q12906


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ILF3_HUMAN
Primary accession number Q12906
Secondary accession numbers O43409 Q6P1X1 Q86XY7 Q99544 Q99545 Q9BZH4 Q9BZH5 Q9NQ95 Q9NQ96 Q9NQ97 Q9NQ98 Q9NQ99 Q9NQA0 Q9NQA1 Q9NQA2 Q9NRN2 Q9NRN3 Q9NRN4 Q9UMZ9 Q9UN00 Q9UN84 Q9UNA2
Integrated into Swiss-Prot on January 31, 2002
Sequence was last modified on April 12, 2005 (Sequence version 3)
Annotations were last modified on    December 16, 2008 (Entry version 95)
Name and origin of the protein
Protein name Interleukin enhancer-binding factor 3
Synonyms Nuclear factor of activated T-cells 90 kDa
NF-AT-90
Double-stranded RNA-binding protein 76
DRBP76
Translational control protein 80
TCP80
Nuclear factor associated with dsRNA
NFAR
M-phase phosphoprotein 4
MPP4
Gene name
Name: ILF3
Synonyms: DRBF, MPHOSPH4, NF90
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-41; 491-510 AND 555-565, AND FUNCTION.
TISSUE=T-cell lymphoma;
PubMed=7519613 [NCBI, ExPASy, EBI, Israel, Japan]
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]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND PROTEIN SEQUENCE OF N-TERMINUS.
TISSUE=Cervix carcinoma;
DOI=10.1074/jbc.274.29.20432; PubMed=10400669 [NCBI, ExPASy, EBI, Israel, Japan]
Patel R.C., Vestal D.J., Xu Z., Bandyopadhyay S., Guo W., Erme S.M., Williams B.R., 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).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND CHARACTERIZATION.
TISSUE=Liver;
DOI=10.1006/mgme.1999.2934; PubMed=10607473 [NCBI, ExPASy, EBI, Israel, Japan]
Xu Y.-H., Grabowski G.A.;
"Molecular cloning and characterization of a translational inhibitory protein that binds to coding sequences of human acid beta-glucosidase and other mRNAs.";
Mol. Genet. Metab. 68:441-454(1999).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2; 4 AND 5), AND ALTERNATIVE SPLICING.
TISSUE=Melanoma;
DOI=10.1016/S0378-1119(00)00495-9; PubMed=11167023 [NCBI, ExPASy, EBI, Israel, Japan]
Duchange N., Pidoux J., Camus E., Sauvaget D.;
"Alternative splicing in the human interleukin enhancer binding factor 3 (ILF3) gene.";
Gene 261:345-353(2000).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), AND CHARACTERIZATION.
DOI=10.1074/jbc.M104207200; PubMed=11438536 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), AND VARIANT HIS-50.
TISSUE=T-cell;
DOI=10.1006/geno.2000.6423; PubMed=11161820 [NCBI, ExPASy, EBI, Israel, Japan]
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]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
TISSUE=Duodenum, and Uterus;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-611.
TISSUE=Blood, and Cervix;
PubMed=8885239 [NCBI, ExPASy, EBI, Israel, Japan]
Matsumoto-Taniura N., Pirollet F., Monroe R., Gerace L., Westendorf J.M.;
"Identification of novel M phase phosphoproteins by expression cloning.";
Mol. Biol. Cell 7:1455-1469(1996).
[9]
PROTEIN SEQUENCE OF 1-10, FUNCTION, AND INTERACTION WITH G22P1; PRKDC AND XRCC5.
DOI=10.1074/jbc.273.4.2136; PubMed=9442054 [NCBI, ExPASy, EBI, Israel, Japan]
Ting N.S.Y., Kao P.N., Chan D.W., Lintott L.G., Lees-Miller S.P.;
"DNA-dependent protein kinase interacts with antigen receptor response element binding proteins NF90 and NF45.";
J. Biol. Chem. 273:2136-2145(1998).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 188-894 (ISOFORMS 1; 2 AND 3).
MacArdle J., Cantarella G.M., Veyrune J.-L., Krasnoselskaya I., Kumar A.;
"Structure and functional characterization of hDRBF gene.";
Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 587-894 (ISOFORM 1).
TISSUE=Brain;
Yu W., Sarginson J., Gibbs R.A.;
Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
[12]
INTERACTION WITH ILF2.
DOI=10.1074/jbc.274.49.34598; PubMed=10574923 [NCBI, ExPASy, EBI, Israel, Japan]
Satoh M., Shaheen V.M., Kao P.N., Okano T., Shaw M., Yoshida H., Richards H.B., Reeves W.H.;
"Autoantibodies define a family of proteins with conserved double-stranded RNA-binding domains as well as DNA binding activity.";
J. Biol. Chem. 274:34598-34604(1999).
[13]
INTERACTION WITH PRMT1.
DOI=10.1074/jbc.M000023200; PubMed=10749851 [NCBI, ExPASy, EBI, Israel, Japan]
Tang J., Kao P.N., Herschman H.R.;
"Protein-arginine methyltransferase I, the predominant protein-arginine methyltransferase in cells, interacts with and is regulated by interleukin enhancer-binding factor 3.";
J. Biol. Chem. 275:19866-19876(2000).
[14]
IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH XPO5; RAN AND DOUBLE-STRANDED RNA, AND INTERACTION WITH XPO5.
DOI=10.1083/jcb.200110082; PubMed=11777942 [NCBI, ExPASy, EBI, Israel, Japan]
Brownawell A.M., Macara I.G.;
"Exportin-5, a novel karyopherin, mediates nuclear export of double-stranded RNA binding proteins.";
J. Cell Biol. 156:53-64(2002).
[15]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
DOI=10.1091/mbc.E02-05-0271; PubMed=12429849 [NCBI, ExPASy, EBI, Israel, Japan]
Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., Greco A., Hochstrasser D.F., Diaz J.-J.;
"Functional proteomic analysis of human nucleolus.";
Mol. Biol. Cell 13:4100-4109(2002).
[16]
INTERACTION WITH ILF2.
DOI=10.1128/MCB.22.1.343-356.2002; PubMed=11739746 [NCBI, ExPASy, EBI, Israel, Japan]
Reichman T.W., Muniz L.C., Mathews M.B.;
"The RNA binding protein nuclear factor 90 functions as both a positive and negative regulator of gene expression in mammalian cells.";
Mol. Cell. Biol. 22:343-356(2002).
[17]
IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH XPO5; RAN AND VA1 RNA.
DOI=10.1074/jbc.M306808200; PubMed=14570900 [NCBI, ExPASy, EBI, Israel, Japan]
Gwizdek C., Ossareh-Nazari B., Brownawell A.M., Evers S., Macara I.G., Dargemont C.;
"Minihelix-containing RNAs mediate exportin-5-dependent nuclear export of the double-stranded RNA-binding protein ILF3.";
J. Biol. Chem. 279:884-891(2004).
[18]
IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH XPO5; RAN; ZNF346 AND DOUBLE-STRANDED RNA, AND INTERACTION WITH XPO5 AND ZNF346.
DOI=10.1128/MCB.24.15.6608-6619.2004; PubMed=15254228 [NCBI, ExPASy, EBI, Israel, Japan]
Chen T., Brownawell A.M., Macara I.G.;
"Nucleocytoplasmic shuttling of JAZ, a new cargo protein for exportin-5.";
Mol. Cell. Biol. 24:6608-6619(2004).
[19]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-609, AND MASS SPECTROMETRY.
DOI=10.1038/nmeth715; PubMed=15782174 [NCBI, ExPASy, EBI, Israel, Japan]
Ong S.E., Mittler G., Mann M.;
"Identifying and quantifying in vivo methylation sites by heavy methyl SILAC.";
Nat. Methods 1:119-126(2004).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62 AND THR-592, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1073/pnas.0404720101; PubMed=15302935 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-382, AND MASS SPECTROMETRY.
TISSUE=T-cell;
DOI=10.1038/nmeth776; PubMed=16094384 [NCBI, ExPASy, EBI, Israel, Japan]
Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J., Bodenmiller B., Watts J.D., Hood L., Aebersold R.;
"Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry.";
Nat. Methods 2:591-598(2005).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190; SER-382; SER-482 AND THR-592, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-592, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1038/nbt1240; PubMed=16964243 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-592 AND SER-812, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1021/pr070152u; PubMed=17924679 [NCBI, ExPASy, EBI, Israel, Japan]
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-382 AND SER-384, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0611217104; PubMed=17287340 [NCBI, ExPASy, EBI, Israel, Japan]
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-486, AND MASS SPECTROMETRY.
DOI=10.1021/pr0705441; PubMed=18220336 [NCBI, ExPASy, EBI, Israel, Japan]
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190; SER-482; TYR-579; THR-592; SER-792; SER-810 AND SER-812, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Comments
  • FUNCTION: May facilitate double-stranded RNA-regulated gene expression at the level of post-transcription. Can act as a translation inhibitory protein which binds to coding sequences of acid beta-glucosidase (GCase) and other mRNAs and functions at the initiation phase of GCase mRNA translation, probably by inhibiting its binding to polysomes. Can regulate protein arginine N-methyltransferase 1 activity. May regulate transcription of the IL2 gene during T-cell activation. Can promote the formation of stable DNA-dependent protein kinase holoenzyme complexes on DNA.
  • SUBUNIT: Interacts with FUS and SMN proteins and with PRMT1. Forms a complex with ILF2. Can also bind to PRKDC/XRCC7: this may stabilize the interaction of PRKDC/XRCC7 and the heterodimeric complex of G22P1/KU70 and XRCC5/KU80. Forms a heteromeric complex with ZNF346 and ILF3. Found in a nuclear export complex with XPO5, ILF3, Ran and double-stranded RNA or double-stranded minihelix VA1 RNA. Found in a nuclear export complex with XPO5, RAN, ILF3, ZNF346 and double-stranded RNA. Interacts with XPO5 and ZNF346.
  • INTERACTION:
    Q92597:NDRG1; NbExp=1; IntAct=EBI-288405, EBI-716486;
    Q99873:PRMT1; NbExp=2; IntAct=EBI-78756, EBI-78738;
  • SUBCELLULAR LOCATION: Nucleus, nucleolus.
  • ALTERNATIVE PRODUCTS: 6 named isoforms [FASTA] produced by alternative splicing.
    Name1
    SynonymsNFAR-2, ILF3-E
    Isoform IDQ12906-1
    This is the isoform sequence displayed in this entry.
    Name2
    SynonymsNFAR-1, DRBP76
    Isoform IDQ12906-2
    Features which should be applied to build the isoform sequence: VSP_003888, VSP_003889.
    Name3
    Isoform IDQ12906-3
    Features which should be applied to build the isoform sequence: VSP_003890, VSP_003891.
    Name4
    SynonymsDRBP76 Alpha, ILF3-A
    Isoform IDQ12906-4
    Features which should be applied to build the isoform sequence: VSP_003883, VSP_003884, VSP_003885.
    Name5
    SynonymsDRBP76 Delta, Gamma, ILF3-C
    Isoform IDQ12906-5
    Features which should be applied to build the isoform sequence: VSP_003886, VSP_003887.
    Name6
    Isoform IDQ12906-6
    Features which should be applied to build the isoform sequence: VSP_003883, VSP_003888, VSP_003889.
  • TISSUE SPECIFICITY: Ubiquitous.
  • PTM: Phosphorylated by RNA-dependent protein kinase (EIF2AK2).
  • PTM: Methylated by protein arginine N-methyltransferase 1.
  • PTM: Arg-609 is dimethylated, probably to asymmetric dimethylarginine.
  • SIMILARITY: Contains 2 DRBM (double-stranded RNA-binding) domains.
  • SIMILARITY: Contains 1 DZF domain.
  • SEQUENCE CAUTION:
    • Sequence=AAA20994.1; Type=Miscellaneous discrepancy; Note=Sequencing errors
    • Sequence=AAH48314.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U10324; AAA20994.1; ALT_SEQ; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF147209; AAD33966.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF141870; AAD37575.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ271741; CAC01121.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ271741; CAC01122.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ271741; CAC01123.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ271741; CAC01124.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ271744; CAC01404.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ271745; CAC01405.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ271746; CAC01406.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ271747; CAC01407.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF167569; AAD51098.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF167570; AAD51099.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF320244; AAK07424.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF320228; AAK07424.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF320229; AAK07424.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF320230; AAK07424.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF320231; AAK07424.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF320232; AAK07424.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF320233; AAK07424.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF320234; AAK07424.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF320235; AAK07424.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF320236; AAK07424.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF320237; AAK07424.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF320238; AAK07424.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF320239; AAK07424.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF320240; AAK07424.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF320241; AAK07424.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF320242; AAK07424.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF320243; AAK07424.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF320247; AAK07425.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF320228; AAK07425.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF320229; AAK07425.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF320230; AAK07425.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF320231; AAK07425.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF320232; AAK07425.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF320233; AAK07425.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF320234; AAK07425.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF320235; AAK07425.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF320236; AAK07425.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF320237; AAK07425.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF320238; AAK07425.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF320239; AAK07425.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF320240; AAK07425.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF320241; AAK07425.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF320242; AAK07425.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF320243; AAK07425.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF320245; AAK07425.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF320246; AAK07425.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC048314; AAH48314.1; ALT_SEQ; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC064836; AAH64836.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X98264; CAA66917.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X98265; CAA66918.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF202445; AAF82685.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF202445; AAF82686.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF202445; AAF82687.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF007140; AAC19152.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR B54857; B54857.
RefSeq NP_004507.2; -.
NP_036350.2; -.
NP_703194.1; -.
UniGene Hs.465885
3D structure databases
SMR Q12906; 403-470.
ModBase Q12906.
Protein-protein interaction databases
IntAct Q12906; 4.
PTM databases
PhosphoSite Q12906; -.
2D gel databases
SWISS-2DPAGE Q12906; -.
Organism-specific databases
GeneCards GC19P010625; -.
H-InvDB HIX0014753; -.
HGNC HGNC:6038; ILF3.
GenAtlas ILF3.
HPA HPA001897; -.
MIM 603182; gene. [NCBI / EBI]
PharmGKB PA29853; -.
GeneCards Q12906.
Gene expression databases
ArrayExpress Q12906; -.
GermOnline ENSG00000129351; Homo sapiens.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (inferred from direct assay from HPA).
GO:0005634; Cellular component: nucleus (inferred from direct assay from UniProtKB).
GO:0003677; Molecular function: DNA binding (inferred from direct assay from UniProtKB).
GO:0003725; Molecular function: double-stranded RNA binding (inferred from direct assay from UniProtKB).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0016563; Molecular function: transcription activator activity (inferred from direct assay from UniProtKB).
GO:0016564; Molecular function: transcription repressor activity (inferred from direct assay from UniProtKB).
GO:0000279; Biological process: M phase (non-traceable author statement from UniProtKB).
GO:0045892; Biological process: negative regulation of transcription, DNA-dependent (inferred from direct assay from UniProtKB).
GO:0045893; Biological process: positive regulation of transcription, DNA-dependent (inferred from direct assay from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR001159; Ds_RNA_bd.
IPR006561; DZF.
Graphical view of domain structure.
Pfam PF00035; dsrm; 2.
PF07528; DZF; 1.
Pfam graphical view of domain structure.
SMART SM00358; DSRM; 2.
SM00572; DZF; 1.
SMART graphical view of domain structure.
PROSITE PS50137; DS_RBD; 2.
PROSITE graphical view of domain structure (profiles).
Proteomics databases
PRIDE Q12906; -.
Genome annotation databases
Ensembl ENSG00000129351; Homo sapiens. [Contig view]
GeneID 3609; -.
KEGG hsa:3609; -.
Phylogenomic databases
HOVERGEN Q12906; -.
Other
NextBio 14109; -.
SOURCE ILF3; Homo sapiens.
ProtoNet Q12906.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Direct protein sequencing; DNA-binding; Methylation; Nucleus; Phosphoprotein; Polymorphism; Repeat; RNA-binding; Transcription; Transcription regulation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   894  894     Interleukin enhancer-binding factor 3. PRO_0000126070
DOMAIN   94   342  249     DZF. 
DOMAIN   398   467  70     DRBM 1. 
DOMAIN   524   590  67     DRBM 2. 
REGION   609   894  286     Interaction with PRMT1. 
MOTIF   371   389  19     Bipartite nuclear localization signal (Potential). 
COMPBIAS   385   389  5     Poly-Lys. 
COMPBIAS   634   637  4     Poly-Pro. 
COMPBIAS   640   659  20     Arg/Gly-rich. 
COMPBIAS   701   709  9     Poly-Gly. 
COMPBIAS   794   798  5     Poly-Gly. 
MOD_RES   62    62        Phosphoserine. 
MOD_RES   190   190        Phosphoserine. 
MOD_RES   382   382        Phosphoserine. 
MOD_RES   384   384        Phosphoserine. 
MOD_RES   482   482        Phosphoserine. 
MOD_RES   486   486        Phosphothreonine. 
MOD_RES   579   579        Phosphotyrosine. 
MOD_RES   592   592        Phosphothreonine. 
MOD_RES   609   609        Omega-N-methylated arginine. 
MOD_RES   792   792        Phosphoserine. 
MOD_RES   810   810        Phosphoserine. 
MOD_RES   812   812        Phosphoserine. 
VAR_SEQ   516   516        E -> ENVKQ (in isoform 4 and isoform 6). VSP_003883
VAR_SEQ   687   690        SQFY -> TGFV (in isoform 5). VSP_003886
VAR_SEQ   688   702        QFYSNGGHSGNASGG -> DFFTDCYGYHDFGSS (in isoform 2 and isoform 6). VSP_003888
VAR_SEQ   688   694        QFYSNGG -> KCAFLSV (in isoform 4). VSP_003884
VAR_SEQ   690   764        YSNGGHSGNASGGGGGGGGGSSGYGSYYQGDNYNSPVPPK HAGKKQPHGGQQKPSYGSGYQSHQGQQQSYNQSPY -> SRPPPPSRPRCCVVRCSGSPCGPSCDPYLAVFGTPCLQWF VSCHYNFVWVEFLSFCSSVSLCLFTLRVSGNSVCL (in isoform 3). VSP_003890
VAR_SEQ