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Interleukin enhancer-binding factor 3 (Double-stranded RNA-binding protein 76) (DRBP76) (M-phase phosphoprotein 4) (MPP4) (Nuclear factor associated with dsRNA) (NFAR) (Nuclear factor of activated T-cells 90 kDa) (NF-AT-90) (Translational control protein 80) (TCP80)

 ILF3_HUMAN              Reviewed;         894 AA.
Q12906; A8K6F2; G5E9M5; O43409; Q6P1X1; Q86XY7; Q99544; Q99545; Q9BZH4;
Q9BZH5; Q9NQ95; Q9NQ96; Q9NQ97; Q9NQ98; Q9NQ99; Q9NQA0; Q9NQA1; Q9NQA2;
Q9NRN2; Q9NRN3; Q9NRN4; Q9UMZ9; Q9UN00; Q9UN84; Q9UNA2;
31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
12-APR-2005, sequence version 3.
02-JUN-2021, entry version 225.
RecName: Full=Interleukin enhancer-binding factor 3;
AltName: Full=Double-stranded RNA-binding protein 76;
Short=DRBP76;
AltName: Full=M-phase phosphoprotein 4;
Short=MPP4;
AltName: Full=Nuclear factor associated with dsRNA;
Short=NFAR;
AltName: Full=Nuclear factor of activated T-cells 90 kDa;
Short=NF-AT-90;
AltName: Full=Translational control protein 80;
Short=TCP80;
Name=ILF3; Synonyms=DRBF, MPHOSPH4, NF90;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 19-41;
491-510 AND 555-565.
TISSUE=T-cell lymphoma;
PubMed=7519613;
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;
PubMed=10400669; DOI=10.1074/jbc.274.29.20432;
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;
PubMed=10607473; DOI=10.1006/mgme.1999.2934;
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;
PubMed=11167023; DOI=10.1016/s0378-1119(00)00495-9;
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.
PubMed=11438536; DOI=10.1074/jbc.m104207200;
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;
PubMed=11161820; DOI=10.1006/geno.2000.6423;
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=Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
TISSUE=Duodenum, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-611.
TISSUE=Blood, and Cervix;
PubMed=8885239; DOI=10.1091/mbc.7.9.1455;
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).
[12]
PROTEIN SEQUENCE OF 1-10, FUNCTION, AND INTERACTION WITH XRCC6; PRKDC AND
XRCC5.
PubMed=9442054; DOI=10.1074/jbc.273.4.2136;
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).
[13]
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.
[14]
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.
[15]
INTERACTION WITH ILF2.
PubMed=10574923; DOI=10.1074/jbc.274.49.34598;
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).
[16]
INTERACTION WITH PRMT1, SUBCELLULAR LOCATION, AND METHYLATION.
PubMed=10749851; DOI=10.1074/jbc.m000023200;
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).
[17]
IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH XPO5; RAN AND
DOUBLE-STRANDED RNA, AND INTERACTION WITH XPO5.
PubMed=11777942; DOI=10.1083/jcb.200110082;
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).
[18]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=12429849; DOI=10.1091/mbc.e02-05-0271;
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).
[19]
INTERACTION WITH ILF2.
PubMed=11739746; DOI=10.1128/mcb.22.1.343-356.2002;
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).
[20]
IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH XPO5; RAN AND VA1
RNA.
PubMed=14570900; DOI=10.1074/jbc.m306808200;
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).
[21]
FUNCTION, INTERACTION WITH DHX36 AND ELAVL1, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=14731398; DOI=10.1016/s1097-2765(03)00481-7;
Tran H., Schilling M., Wirbelauer C., Hess D., Nagamine Y.;
"Facilitation of mRNA deadenylation and decay by the exosome-bound, DExH
protein RHAU.";
Mol. Cell 13:101-111(2004).
[22]
IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH XPO5; RAN; ZNF346
AND DOUBLE-STRANDED RNA, AND INTERACTION WITH XPO5 AND ZNF346.
PubMed=15254228; DOI=10.1128/mcb.24.15.6608-6619.2004;
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).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-482 AND THR-592, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
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).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-592, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
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).
[25]
IDENTIFICATION IN A COMPLEX WITH ILF2; YLPM1; KHDRBS1; RBMX; NCOA5 AND
PPP1CA.
PubMed=17890166; DOI=10.1016/j.bbapap.2007.07.015;
Ulke-Lemee A., Trinkle-Mulcahy L., Chaulk S., Bernstein N.K., Morrice N.,
Glover M., Lamond A.I., Moorhead G.B.G.;
"The nuclear PP1 interacting protein ZAP3 (ZAP) is a putative nucleoside
kinase that complexes with SAM68, CIA, NF110/45, and HNRNP-G.";
Biochim. Biophys. Acta 1774:1339-1350(2007).
[26]
INTERACTION WITH AGO1 AND AGO2.
PubMed=17932509; DOI=10.1038/sj.embor.7401088;
Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M.,
Urlaub H., Meister G.;
"Proteomic and functional analysis of Argonaute-containing mRNA-protein
complexes in human cells.";
EMBO Rep. 8:1052-1060(2007).
[27]
IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS
SPECTROMETRY, AND SUBCELLULAR LOCATION.
PubMed=17289661; DOI=10.1074/mcp.m600346-mcp200;
Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R.,
Johnsen A.H., Christiansen J., Nielsen F.C.;
"Molecular composition of IMP1 ribonucleoprotein granules.";
Mol. Cell. Proteomics 6:798-811(2007).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190; SER-792 AND SER-812,
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-482 (ISOFORMS 4; 6 AND 7),
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
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).
[29]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in a
refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[30]
IDENTIFICATION IN A MRNP COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=19029303; DOI=10.1261/rna.1175909;
Weidensdorfer D., Stoehr N., Baude A., Lederer M., Koehn M., Schierhorn A.,
Buchmeier S., Wahle E., Huettelmaiery S.;
"Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic RNPs.";
RNA 15:104-115(2009).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-592 AND SER-792,
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-482 (ISOFORMS 4; 6 AND 7),
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[32]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-100 AND LYS-460, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[33]
FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT THR-188 AND THR-315.
PubMed=21123651; DOI=10.1101/gad.1965010;
Harashima A., Guettouche T., Barber G.N.;
"Phosphorylation of the NFAR proteins by the dsRNA-dependent protein kinase
PKR constitutes a novel mechanism of translational regulation and cellular
defense.";
Genes Dev. 24:2640-2653(2010).
[34]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62; SER-190; SER-382;
SER-384; SER-482; THR-592 AND SER-812, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
"Quantitative phosphoproteomics reveals widespread full phosphorylation
site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[35]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[36]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62; SER-190; SER-382;
SER-476; SER-482; THR-592; SER-792 AND SER-812, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
"System-wide temporal characterization of the proteome and phosphoproteome
of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[37]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62; SER-382; THR-592; SER-792
AND SER-816, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[38]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62; SER-476; SER-477; SER-482
AND SER-810, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
phosphoproteome.";
J. Proteomics 96:253-262(2014).
[39]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-348, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[40]
SUBCELLULAR LOCATION, AND INTERACTION WITH ILF2.
PubMed=26240280; DOI=10.1128/mcb.00306-15;
Wandrey F., Montellese C., Koos K., Badertscher L., Bammert L., Cook A.G.,
Zemp I., Horvath P., Kutay U.;
"The NF45/NF90 Heterodimer Contributes to the Biogenesis of 60S Ribosomal
Subunits and Influences Nucleolar Morphology.";
Mol. Cell. Biol. 35:3491-3503(2015).
[41]
FUNCTION, INTERACTION WITH ILF2, AND SUBCELLULAR LOCATION.
PubMed=28625552; DOI=10.1016/j.molcel.2017.05.023;
Li X., Liu C.X., Xue W., Zhang Y., Jiang S., Yin Q.F., Wei J., Yao R.W.,
Yang L., Chen L.L.;
"Coordinated circRNA Biogenesis and Function with NF90/NF110 in Viral
Infection.";
Mol. Cell 0:0-0(2017).
[42]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-396 AND LYS-489, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-modification
with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[43]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 520-594.
Northeast structural genomics consortium (NESG);
"Crystal structure of DRBM 2 domain of interleukin enhancer-binding factor
3 from Homo sapiens, Northeast structural genomics consortium target
HR4527E.";
Submitted (DEC-2010) to the PDB data bank.
[44]
STRUCTURE BY NMR OF 521-600.
Northeast structural genomics consortium (NESG);
"Northeast structural genomics consortium target HR4527E.";
Submitted (SEP-2010) to the PDB data bank.
-!- FUNCTION: RNA-binding protein that plays an essential role in the
biogenesis of circular RNAs (circRNAs) which are produced by back-
splicing circularization of pre-mRNAs. Within the nucleus, promotes
circRNAs processing by stabilizing the regulatory elements residing in
the flanking introns of the circularized exons. Plays thereby a role in
the back-splicing of a subset of circRNAs (PubMed:28625552). As a
consequence, participates in a wide range of transcriptional and post-
transcriptional processes. Binds to poly-U elements and AU-rich
elements (AREs) in the 3'-UTR of target mRNAs (PubMed:14731398). Upon
viral infection, ILF3 accumulates in the cytoplasm and participates in
the innate antiviral response (PubMed:21123651). Mechanistically, ILF3
becomes phosphorylated and activated by the double-stranded RNA-
activated protein kinase/PKR which releases ILF3 from cellular mature
circRNAs. In turn, unbound ILF3 molecules are able to interact with and
thus inhibit viral mRNAs (PubMed:21123651, PubMed:28625552).
{ECO:0000269|PubMed:14731398, ECO:0000269|PubMed:21123651,
ECO:0000269|PubMed:28625552, ECO:0000269|PubMed:9442054}.
-!- SUBUNIT: Identified in a IGF2BP1-dependent mRNP granule complex
containing untranslated mRNAs. Interacts with FUS and SMN. Interacts
(via C-terminus) 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 XRCC6/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.
Forms a complex with ILF2, YLPM1, KHDRBS1, RBMX, NCOA5 and PPP1CA.
Interacts with AGO1 and AGO2. Interacts with DHX36; this interaction
occurs in a RNA-dependent manner (PubMed:14731398). Interacts with
ELAVL1; this interaction occurs in a RNA-dependent manner
(PubMed:14731398). {ECO:0000269|PubMed:10574923,
ECO:0000269|PubMed:10749851, ECO:0000269|PubMed:11739746,
ECO:0000269|PubMed:11777942, ECO:0000269|PubMed:14570900,
ECO:0000269|PubMed:14731398, ECO:0000269|PubMed:15254228,
ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:17890166,
ECO:0000269|PubMed:17932509, ECO:0000269|PubMed:19029303,
ECO:0000269|PubMed:26240280, ECO:0000269|PubMed:28625552,
ECO:0000269|PubMed:9442054}.
-!- INTERACTION:
Q12906; P14866-1: HNRNPL; NbExp=2; IntAct=EBI-78756, EBI-16071645;
Q12906; Q99873: PRMT1; NbExp=2; IntAct=EBI-78756, EBI-78738;
Q12906; P08325: M; Xeno; NbExp=2; IntAct=EBI-78756, EBI-15693250;
Q12906; P03496: NS; Xeno; NbExp=3; IntAct=EBI-78756, EBI-2547442;
Q12906; Q05127: VP35; Xeno; NbExp=6; IntAct=EBI-78756, EBI-6148294;
Q12906-6; Q13148: TARDBP; NbExp=6; IntAct=EBI-12904528, EBI-372899;
Q12906-6; A5D8V6: VPS37C; NbExp=3; IntAct=EBI-12904528, EBI-2559305;
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:26240280}.
Cytoplasm {ECO:0000269|PubMed:28625552}. Nucleus
{ECO:0000269|PubMed:10749851, ECO:0000269|PubMed:26240280,
ECO:0000269|PubMed:28625552}. Note=Localizes in the cytoplasm in
response to viral infection. The unphosphorylated form is retained in
the nucleus by ILF2. Phosphorylation at Thr-188 and Thr-315 causes the
dissociation of ILF2 from the ILF2-ILF3 complex resulting in a
cytoplasmic sequestration of ILF3. Localized in cytoplasmic mRNP
granules containing untranslated mRNAs. {ECO:0000269|PubMed:21123651}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=7;
Name=1; Synonyms=NFAR-2, ILF3-E;
IsoId=Q12906-1; Sequence=Displayed;
Name=2; Synonyms=NFAR-1, DRBP76;
IsoId=Q12906-2; Sequence=VSP_003888, VSP_003889;
Name=3;
IsoId=Q12906-3; Sequence=VSP_003890, VSP_003891;
Name=4; Synonyms=DRBP76 Alpha, ILF3-A;
IsoId=Q12906-4; Sequence=VSP_003883, VSP_003884, VSP_003885;
Name=5; Synonyms=DRBP76 Delta, Gamma, ILF3-C;
IsoId=Q12906-5; Sequence=VSP_003886, VSP_003887;
Name=6;
IsoId=Q12906-6; Sequence=VSP_003883, VSP_003888, VSP_003889;
Name=7;
IsoId=Q12906-7; Sequence=VSP_003883;
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- PTM: Phosphorylated at Thr-188 and Thr-315 by PKR in response to
certain RNA viruses. This phosphorylation results in the dissociation
of ILF2 from the ILF2-ILF3 complex resulting in a cytoplasmic
sequestration of ILF3 where it can bind to viral RNAs and impede viral
replication. {ECO:0000269|PubMed:21123651}.
-!- PTM: Methylated by protein arginine N-methyltransferase 1.
{ECO:0000269|PubMed:10749851}.
-!- MISCELLANEOUS: [Isoform 3]: Dubious isoform produced through aberrant
splice sites. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA20994.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
Sequence=AAH48314.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
---------------------------------------------------------------------------
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EMBL; U10324; AAA20994.1; ALT_SEQ; mRNA.
EMBL; AF147209; AAD33966.1; -; mRNA.
EMBL; AF141870; AAD37575.1; -; mRNA.
EMBL; AJ271741; CAC01121.1; -; Genomic_DNA.
EMBL; AJ271741; CAC01122.1; -; Genomic_DNA.
EMBL; AJ271741; CAC01123.1; -; Genomic_DNA.
EMBL; AJ271741; CAC01124.1; -; Genomic_DNA.
EMBL; AJ271744; CAC01404.1; -; mRNA.
EMBL; AJ271745; CAC01405.1; -; mRNA.
EMBL; AJ271746; CAC01406.1; -; mRNA.
EMBL; AJ271747; CAC01407.1; -; mRNA.
EMBL; AF167569; AAD51098.1; -; mRNA.
EMBL; AF167570; AAD51099.1; -; mRNA.
EMBL; AF320244; AAK07424.1; -; Genomic_DNA.
EMBL; AF320228; AAK07424.1; JOINED; Genomic_DNA.
EMBL; AF320229; AAK07424.1; JOINED; Genomic_DNA.
EMBL; AF320230; AAK07424.1; JOINED; Genomic_DNA.
EMBL; AF320231; AAK07424.1; JOINED; Genomic_DNA.
EMBL; AF320232; AAK07424.1; JOINED; Genomic_DNA.
EMBL; AF320233; AAK07424.1; JOINED; Genomic_DNA.
EMBL; AF320234; AAK07424.1; JOINED; Genomic_DNA.
EMBL; AF320235; AAK07424.1; JOINED; Genomic_DNA.
EMBL; AF320236; AAK07424.1; JOINED; Genomic_DNA.
EMBL; AF320237; AAK07424.1; JOINED; Genomic_DNA.
EMBL; AF320238; AAK07424.1; JOINED; Genomic_DNA.
EMBL; AF320239; AAK07424.1; JOINED; Genomic_DNA.
EMBL; AF320240; AAK07424.1; JOINED; Genomic_DNA.
EMBL; AF320241; AAK07424.1; JOINED; Genomic_DNA.
EMBL; AF320242; AAK07424.1; JOINED; Genomic_DNA.
EMBL; AF320243; AAK07424.1; JOINED; Genomic_DNA.
EMBL; AF320247; AAK07425.1; -; Genomic_DNA.
EMBL; AF320228; AAK07425.1; JOINED; Genomic_DNA.
EMBL; AF320229; AAK07425.1; JOINED; Genomic_DNA.
EMBL; AF320230; AAK07425.1; JOINED; Genomic_DNA.
EMBL; AF320231; AAK07425.1; JOINED; Genomic_DNA.
EMBL; AF320232; AAK07425.1; JOINED; Genomic_DNA.
EMBL; AF320233; AAK07425.1; JOINED; Genomic_DNA.
EMBL; AF320234; AAK07425.1; JOINED; Genomic_DNA.
EMBL; AF320235; AAK07425.1; JOINED; Genomic_DNA.
EMBL; AF320236; AAK07425.1; JOINED; Genomic_DNA.
EMBL; AF320237; AAK07425.1; JOINED; Genomic_DNA.
EMBL; AF320238; AAK07425.1; JOINED; Genomic_DNA.
EMBL; AF320239; AAK07425.1; JOINED; Genomic_DNA.
EMBL; AF320240; AAK07425.1; JOINED; Genomic_DNA.
EMBL; AF320241; AAK07425.1; JOINED; Genomic_DNA.
EMBL; AF320242; AAK07425.1; JOINED; Genomic_DNA.
EMBL; AF320243; AAK07425.1; JOINED; Genomic_DNA.
EMBL; AF320245; AAK07425.1; JOINED; Genomic_DNA.
EMBL; AF320246; AAK07425.1; JOINED; Genomic_DNA.
EMBL; AK291617; BAF84306.1; -; mRNA.
EMBL; AC011475; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471106; EAW84132.1; -; Genomic_DNA.
EMBL; BC048314; AAH48314.1; ALT_SEQ; mRNA.
EMBL; BC064836; AAH64836.1; -; mRNA.
EMBL; X98264; CAA66917.1; -; mRNA.
EMBL; X98265; CAA66918.1; -; mRNA.
EMBL; AF202445; AAF82685.1; -; Genomic_DNA.
EMBL; AF202445; AAF82686.1; -; Genomic_DNA.
EMBL; AF202445; AAF82687.1; -; Genomic_DNA.
EMBL; AF007140; AAC19152.1; -; mRNA.
CCDS; CCDS12246.1; -. [Q12906-1]
CCDS; CCDS12247.1; -. [Q12906-2]
CCDS; CCDS45965.1; -. [Q12906-7]
CCDS; CCDS45966.1; -. [Q12906-5]
CCDS; CCDS45967.1; -. [Q12906-6]
PIR; B54857; B54857.
RefSeq; NP_001131145.1; NM_001137673.1. [Q12906-6]
RefSeq; NP_004507.2; NM_004516.3. [Q12906-2]
RefSeq; NP_036350.2; NM_012218.3. [Q12906-1]
RefSeq; NP_060090.2; NM_017620.2. [Q12906-7]
RefSeq; NP_703194.1; NM_153464.2. [Q12906-5]
RefSeq; XP_011526286.2; XM_011527984.2. [Q12906-7]
RefSeq; XP_016882252.1; XM_017026763.1. [Q12906-7]
PDB; 2L33; NMR; -; A=521-600.
PDB; 3P1X; X-ray; 1.90 A; A/B=520-594.
PDBsum; 2L33; -.
PDBsum; 3P1X; -.
SMR; Q12906; -.
BioGRID; 109822; 512.
CORUM; Q12906; -.
DIP; DIP-29853N; -.
IntAct; Q12906; 128.
MINT; Q12906; -.
STRING; 9606.ENSP00000404121; -.
iPTMnet; Q12906; -.
MetOSite; Q12906; -.
PhosphoSitePlus; Q12906; -.
SwissPalm; Q12906; -.
BioMuta; ILF3; -.
DMDM; 62512150; -.
SWISS-2DPAGE; Q12906; -.
CPTAC; CPTAC-395; -.
CPTAC; CPTAC-396; -.
EPD; Q12906; -.
jPOST; Q12906; -.
MassIVE; Q12906; -.
MaxQB; Q12906; -.
PaxDb; Q12906; -.
PeptideAtlas; Q12906; -.
PRIDE; Q12906; -.
ProteomicsDB; 33984; -.
ProteomicsDB; 59014; -. [Q12906-1]
ProteomicsDB; 59015; -. [Q12906-2]
ProteomicsDB; 59016; -. [Q12906-3]
ProteomicsDB; 59017; -. [Q12906-4]
ProteomicsDB; 59018; -. [Q12906-5]
ProteomicsDB; 59019; -. [Q12906-6]
TopDownProteomics; Q12906-1; -. [Q12906-1]
Antibodypedia; 1051; 340 antibodies.
DNASU; 3609; -.
Ensembl; ENST00000250241; ENSP00000250241; ENSG00000129351. [Q12906-5]
Ensembl; ENST00000407004; ENSP00000384660; ENSG00000129351. [Q12906-6]
Ensembl; ENST00000449870; ENSP00000404121; ENSG00000129351. [Q12906-7]
Ensembl; ENST00000588657; ENSP00000468181; ENSG00000129351. [Q12906-7]
Ensembl; ENST00000589998; ENSP00000465219; ENSG00000129351. [Q12906-2]
Ensembl; ENST00000590261; ENSP00000468156; ENSG00000129351. [Q12906-1]
Ensembl; ENST00000592763; ENSP00000465515; ENSG00000129351. [Q12906-4]
GeneID; 3609; -.
KEGG; hsa:3609; -.
UCSC; uc002mpl.3; human. [Q12906-1]
CTD; 3609; -.
DisGeNET; 3609; -.
GeneCards; ILF3; -.
HGNC; HGNC:6038; ILF3.
HPA; ENSG00000129351; Low tissue specificity.
MIM; 603182; gene.
neXtProt; NX_Q12906; -.
OpenTargets; ENSG00000129351; -.
PharmGKB; PA29853; -.
VEuPathDB; HostDB:ENSG00000129351.17; -.
eggNOG; KOG3792; Eukaryota.
GeneTree; ENSGT00940000156719; -.
HOGENOM; CLU_015490_0_0_1; -.
InParanoid; Q12906; -.
OMA; YSHGQGN; -.
OrthoDB; 612611at2759; -.
PhylomeDB; Q12906; -.
TreeFam; TF320194; -.
PathwayCommons; Q12906; -.
SIGNOR; Q12906; -.
BioGRID-ORCS; 3609; 632 hits in 1000 CRISPR screens.
ChiTaRS; ILF3; human.
EvolutionaryTrace; Q12906; -.
GeneWiki; ILF3; -.
GenomeRNAi; 3609; -.
Pharos; Q12906; Tbio.
PRO; PR:Q12906; -.
Proteomes; UP000005640; Chromosome 19.
RNAct; Q12906; protein.
Bgee; ENSG00000129351; Expressed in subventricular zone (outer) (primate) and 245 other tissues.
ExpressionAtlas; Q12906; baseline and differential.
Genevisible; Q12906; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0003725; F:double-stranded RNA binding; IDA:UniProtKB.
GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; IDA:GO_Central.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0003727; F:single-stranded RNA binding; IBA:GO_Central.
GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0017148; P:negative regulation of translation; ISS:UniProtKB.
GO; GO:0045071; P:negative regulation of viral genome replication; ISS:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
Gene3D; 3.30.460.10; -; 1.
InterPro; IPR014720; dsRBD_dom.
InterPro; IPR006561; DZF_dom.
InterPro; IPR033099; ILF3/NF90.
InterPro; IPR043519; NT_sf.
PANTHER; PTHR45762:SF4; PTHR45762:SF4; 3.
Pfam; PF00035; dsrm; 2.
Pfam; PF07528; DZF; 1.
SMART; SM00358; DSRM; 2.
SMART; SM00572; DZF; 1.
PROSITE; PS50137; DS_RBD; 2.
PROSITE; PS51703; DZF; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Antiviral defense;
Cytoplasm; Direct protein sequencing; DNA-binding; Isopeptide bond;
Methylation; Nucleus; Phosphoprotein; Reference proteome; Repeat;
RNA-binding; Transcription; Transcription regulation; Ubl conjugation.
CHAIN 1..894
/note="Interleukin enhancer-binding factor 3"
/id="PRO_0000126070"
DOMAIN 5..378
/note="DZF"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01040"
DOMAIN 398..467
/note="DRBM 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
DOMAIN 524..590
/note="DRBM 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
REGION 50..86
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 363..401
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 466..524
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 609..894
/note="Interaction with PRMT1"
/evidence="ECO:0000269|PubMed:10749851"
REGION 625..660
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 718..894
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
MOTIF 371..389
/note="Bipartite nuclear localization signal"
/evidence="ECO:0000255"
COMPBIAS 67..86
/note="Basic and acidic residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 372..399
/note="Basic and acidic residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 740..827
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 843..894
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
MOD_RES 62
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:20068231,
ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
ECO:0007744|PubMed:24275569"
MOD_RES 100
/note="N6-acetyllysine"
/evidence="ECO:0007744|PubMed:19608861"
MOD_RES 188
/note="Phosphothreonine; by PKR"
/evidence="ECO:0000269|PubMed:21123651"
MOD_RES 190
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
MOD_RES 315
/note="Phosphothreonine; by PKR"
/evidence="ECO:0000269|PubMed:21123651"
MOD_RES 382
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:20068231,
ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
MOD_RES 384
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:20068231"
MOD_RES 460
/note="N6-acetyllysine"
/evidence="ECO:0007744|PubMed:19608861"
MOD_RES 476
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:21406692,
ECO:0007744|PubMed:24275569"
MOD_RES 477
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:24275569"
MOD_RES 482
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:17081983,
ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
ECO:0007744|PubMed:24275569"
MOD_RES 592
/note="Phosphothreonine"
/evidence="ECO:0007744|PubMed:16964243,
ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:19690332,
ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
ECO:0007744|PubMed:23186163"
MOD_RES 792
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
ECO:0007744|PubMed:23186163"
MOD_RES 810
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:24275569"
MOD_RES 812
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
MOD_RES 816
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:23186163"
CROSSLNK 348
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO1)"
/evidence="ECO:0007744|PubMed:25114211"
CROSSLNK 396
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0007744|PubMed:28112733"
CROSSLNK 489
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0007744|PubMed:28112733"
VAR_SEQ 516
/note="E -> ENVKQ (in isoform 4, isoform 6 and isoform 7)"
/evidence="ECO:0000303|PubMed:11167023,
ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
/id="VSP_003883"
VAR_SEQ 687..690
/note="SQFY -> TGFV (in isoform 5)"
/evidence="ECO:0000303|PubMed:11167023"
/id="VSP_003886"
VAR_SEQ 688..702
/note="QFYSNGGHSGNASGG -> DFFTDCYGYHDFGSS (in isoform 2 and
isoform 6)"
/evidence="ECO:0000303|PubMed:10400669,
ECO:0000303|PubMed:11161820, ECO:0000303|PubMed:11167023,
ECO:0000303|PubMed:11438536, ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334, ECO:0000303|Ref.13"
/id="VSP_003888"
VAR_SEQ 688..694
/note="QFYSNGG -> KCAFLSV (in isoform 4)"
/evidence="ECO:0000303|PubMed:11167023"
/id="VSP_003884"
VAR_SEQ 690..764
/note="YSNGGHSGNASGGGGGGGGGSSGYGSYYQGDNYNSPVPPKHAGKKQPHGGQQ
KPSYGSGYQSHQGQQQSYNQSPY -> SRPPPPSRPRCCVVRCSGSPCGPSCDPYLAVF
GTPCLQWFVSCHYNFVWVEFLSFCSSVSLCLFTLRVSGNSVCL (in isoform 3)"
/evidence="ECO:0000303|PubMed:10607473, ECO:0000303|Ref.13"
/id="VSP_003890"
VAR_SEQ 691..894
/note="Missing (in isoform 5)"
/evidence="ECO:0000303|PubMed:11167023"
/id="VSP_003887"
VAR_SEQ 695..894
/note="Missing (in isoform 4)"
/evidence="ECO:0000303|PubMed:11167023"
/id="VSP_003885"
VAR_SEQ 703..894
/note="Missing (in isoform 2 and isoform 6)"
/evidence="ECO:0000303|PubMed:10400669,
ECO:0000303|PubMed:11161820, ECO:0000303|PubMed:11167023,
ECO:0000303|PubMed:11438536, ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334, ECO:0000303|Ref.13"
/id="VSP_003889"
VAR_SEQ 765..894
/note="Missing (in isoform 3)"
/evidence="ECO:0000303|PubMed:10607473, ECO:0000303|Ref.13"
/id="VSP_003891"
VARIANT 50
/note="D -> H (in dbSNP:rs1064493)"
/evidence="ECO:0000269|PubMed:11161820"
/id="VAR_022159"
VARIANT 501
/note="A -> S (in dbSNP:rs34520379)"
/id="VAR_048906"
CONFLICT 101
/note="G -> C (in Ref. 5; AAD51098/AAD51099 and 6;
AAK07424/AAK07425)"
/evidence="ECO:0000305"
CONFLICT 260
/note="G -> V (in Ref. 2; AAD33966 and 11; CAA66918)"
/evidence="ECO:0000305"
CONFLICT 647
/note="S -> T (in Ref. 2; AAD33966 and 6; AAK07424/
AAK07425)"
/evidence="ECO:0000305"
CONFLICT 688..689
/note="QF -> N (in Ref. 13; AAF82687)"
/evidence="ECO:0000305"
CONFLICT 763
/note="P -> L (in Ref. 4; CAC01407)"
/evidence="ECO:0000305"
CONFLICT 797
/note="G -> R (in Ref. 4; CAC01124 and 6; AAK07425)"
/evidence="ECO:0000305"
CONFLICT 799
/note="S -> SGS (in Ref. 13; AAF82685)"
/evidence="ECO:0000305"
CONFLICT 813
/note="G -> E (in Ref. 6; AAK07425)"
/evidence="ECO:0000305"
HELIX 528..535
/evidence="ECO:0007829|PDB:3P1X"
STRAND 541..548
/evidence="ECO:0007829|PDB:3P1X"
STRAND 554..561
/evidence="ECO:0007829|PDB:3P1X"
STRAND 564..572
/evidence="ECO:0007829|PDB:3P1X"
HELIX 573..588
/evidence="ECO:0007829|PDB:3P1X"
MOD_RES Q12906-4:482
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:19690332"
MOD_RES Q12906-6:482
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:19690332"
MOD_RES Q12906-7:482
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:19690332"
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


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EIAAB27058 CCAAT-box-binding transcription factor,CTF,Homo sapiens,Human,NF1-B,NF-I_B,NFIB,NFI-B,Nuclear factor 1 B-type,Nuclear factor 1_B,Nuclear factor I_B,TGGCA-binding protein
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EIAAB27052 CCAAT-box-binding transcription factor,CTF,Mouse,Mus musculus,NF1-A,NF-I_A,Nfia,NFI-A,Nuclear factor 1 A-type,Nuclear factor 1_A,Nuclear factor I_A,TGGCA-binding protein
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Pathways :
WP1789: Binding of RNA by Insulin-like Growth Factor-2 mRNA Binding Proteins (IGF2BPs/IMPs/VICKZs)
WP1899: Regulation of Insulin-like Growth Factor (IGF) Activity by Insulin-like Growth Factor Binding Proteins (IGFBPs)
WP731: Sterol regulatory element binding protein related
WP1531: Vitamin D synthesis
WP1502: Mitochondrial biogenesis
WP2292: Chemokine signaling pathway
WP1616: ABC transporters
WP2148: Brain derived neurotrophic factor
WP1983: Splicing factor NOVA regulated synpatic proteins
WP810: Signaling of Hepatocyte Growth Factor Receptor
WP313: Signaling of Hepatocyte Growth Factor Receptor
WP1888: Post-translational protein modification
WP444: Signaling of Hepatocyte Growth Factor Receptor
WP927: Signaling of Hepatocyte Growth Factor Receptor
WP1206: Signaling of Hepatocyte Growth Factor Receptor
WP1046: Signaling of Hepatocyte Growth Factor Receptor
WP94: Signaling of Hepatocyte Growth Factor Receptor
WP1162: Signaling of Hepatocyte Growth Factor Receptor
WP193: Signaling of Hepatocyte Growth Factor Receptor
WP272: Blood Clotting Cascade
WP1235: Signaling of Hepatocyte Growth Factor Receptor
WP1692: Protein export
WP813: G Protein Signaling Pathways
WP1644: DNA replication
WP346: Protein Modifications

Related Genes :
[ILF3 DRBF MPHOSPH4 NF90] Interleukin enhancer-binding factor 3 (Double-stranded RNA-binding protein 76) (DRBP76) (M-phase phosphoprotein 4) (MPP4) (Nuclear factor associated with dsRNA) (NFAR) (Nuclear factor of activated T-cells 90 kDa) (NF-AT-90) (Translational control protein 80) (TCP80)
[ilf3-a ilf3 ubp3] Interleukin enhancer-binding factor 3-A (CCAAT box transcription factor subunit) (Double-stranded RNA-binding protein 4F.1) (DsRNA-binding protein 4F.1)
[NFKB2 LYT10] Nuclear factor NF-kappa-B p100 subunit (DNA-binding factor KBF2) (H2TF1) (Lymphocyte translocation chromosome 10 protein) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells 2) (Oncogene Lyt-10) (Lyt10) [Cleaved into: Nuclear factor NF-kappa-B p52 subunit]
[Nfkb1] Nuclear factor NF-kappa-B p105 subunit (DNA-binding factor KBF1) (EBP-1) (NF-kappa-B1 p84/NF-kappa-B1 p98) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1) [Cleaved into: Nuclear factor NF-kappa-B p50 subunit]
[NFKB1] Nuclear factor NF-kappa-B p105 subunit (DNA-binding factor KBF1) (EBP-1) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1) [Cleaved into: Nuclear factor NF-kappa-B p50 subunit]
[NFATC4 NFAT3] Nuclear factor of activated T-cells, cytoplasmic 4 (NF-ATc4) (NFATc4) (T-cell transcription factor NFAT3) (NF-AT3)
[RELA NFKB3] Transcription factor p65 (Nuclear factor NF-kappa-B p65 subunit) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells 3)
[Nfkb1] Nuclear factor NF-kappa-B p105 subunit (DNA-binding factor KBF1) (EBP-1) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1) [Cleaved into: Nuclear factor NF-kappa-B p50 subunit] (Fragment)
[Nfkb2] Nuclear factor NF-kappa-B p100 subunit (DNA-binding factor KBF2) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells 2) [Cleaved into: Nuclear factor NF-kappa-B p52 subunit]
[NFATC3 NFAT4] Nuclear factor of activated T-cells, cytoplasmic 3 (NF-ATc3) (NFATc3) (NFATx) (T-cell transcription factor NFAT4) (NF-AT4) (NF-AT4c)
[Nfatc4 Nfat3] Nuclear factor of activated T-cells, cytoplasmic 4 (NF-ATc4) (NFATc4) (T-cell transcription factor NFAT3) (NF-AT3)
[NFKB1] Nuclear factor NF-kappa-B p105 subunit (Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1) [Cleaved into: Nuclear factor NF-kappa-B p50 subunit]
[Nfatc3 Nfat4] Nuclear factor of activated T-cells, cytoplasmic 3 (NF-ATc3) (NFATc3) (NFATx) (T-cell transcription factor NFAT4) (NF-AT4)
[Rela Nfkb3] Transcription factor p65 (Nuclear factor NF-kappa-B p65 subunit) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells 3)
[Ilf3] Interleukin enhancer-binding factor 3
[CEBPB TCF5 PP9092] CCAAT/enhancer-binding protein beta (C/EBP beta) (Liver activator protein) (LAP) (Liver-enriched inhibitory protein) (LIP) (Nuclear factor NF-IL6) (Transcription factor 5) (TCF-5)
[ilf3-b ubp4] Interleukin enhancer-binding factor 3-B (Double-stranded RNA-binding protein 4F.2) (DsRNA-binding protein 4F.2)
[EIF2AK2 PKR PRKR] Interferon-induced, double-stranded RNA-activated protein kinase (EC 2.7.11.1) (Eukaryotic translation initiation factor 2-alpha kinase 2) (eIF-2A protein kinase 2) (Interferon-inducible RNA-dependent protein kinase) (P1/eIF-2A protein kinase) (Protein kinase RNA-activated) (PKR) (Protein kinase R) (Tyrosine-protein kinase EIF2AK2) (EC 2.7.10.2) (p68 kinase)
[NFATC2 NFAT1 NFATP] Nuclear factor of activated T-cells, cytoplasmic 2 (NF-ATc2) (NFATc2) (NFAT pre-existing subunit) (NF-ATp) (T-cell transcription factor NFAT1)
[Nfatc4 Nfat3] Nuclear factor of activated T-cells, cytoplasmic 4 (NF-ATc4) (NFATc4) (T-cell transcription factor NFAT3) (NF-AT3)
[Nfatc2 Nfat1 Nfatp] Nuclear factor of activated T-cells, cytoplasmic 2 (NF-ATc2) (NFATc2) (NFAT pre-existing subunit) (NF-ATp) (T-cell transcription factor NFAT1)
[FOXM1 FKHL16 HFH11 MPP2 WIN] Forkhead box protein M1 (Forkhead-related protein FKHL16) (Hepatocyte nuclear factor 3 forkhead homolog 11) (HFH-11) (HNF-3/fork-head homolog 11) (M-phase phosphoprotein 2) (MPM-2 reactive phosphoprotein 2) (Transcription factor Trident) (Winged-helix factor from INS-1 cells)
[Cebpb Crp2 Nf-il6 Sfb] CCAAT/enhancer-binding protein beta (C/EBP beta) (C/EBP-related protein 2) (Interleukin-6-dependent-binding protein) (IL-6DBP) (Liver-enriched inhibitory protein) (LIP) (Liver-enriched transcriptional activator) (LAP) (Silencer factor B) (SF-B)
[NFATC1 NFAT2 NFATC] Nuclear factor of activated T-cells, cytoplasmic 1 (NF-ATc1) (NFATc1) (NFAT transcription complex cytosolic component) (NF-ATc) (NFATc)
[Nfatc1 Nfat2 Nfatc] Nuclear factor of activated T-cells, cytoplasmic 1 (NF-ATc1) (NFATc1) (NFAT transcription complex cytosolic component) (NF-ATc) (NFATc)
[Eif2ak2 Pkr Prkr Tik] Interferon-induced, double-stranded RNA-activated protein kinase (EC 2.7.11.1) (Eukaryotic translation initiation factor 2-alpha kinase 2) (eIF-2A protein kinase 2) (Interferon-inducible RNA-dependent protein kinase) (P1/eIF-2A protein kinase) (Protein kinase RNA-activated) (PKR) (Protein kinase R) (Serine/threonine-protein kinase TIK) (Tyrosine-protein kinase EIF2AK2) (EC 2.7.10.2) (p68 kinase)
[ADAR ADAR1 DSRAD G1P1 IFI4] Double-stranded RNA-specific adenosine deaminase (DRADA) (EC 3.5.4.37) (136 kDa double-stranded RNA-binding protein) (p136) (Interferon-inducible protein 4) (IFI-4) (K88DSRBP)
[Pre C,C C core E PC pre-C pre-C/C PreC preC PreC/C preC/C precore-core HBVgp4] Capsid protein (Core antigen) (Core protein) (HBcAg) (p21.5)
[IKBKG FIP3 NEMO] NF-kappa-B essential modulator (NEMO) (FIP-3) (IkB kinase-associated protein 1) (IKKAP1) (Inhibitor of nuclear factor kappa-B kinase subunit gamma) (I-kappa-B kinase subunit gamma) (IKK-gamma) (IKKG) (IkB kinase subunit gamma) (NF-kappa-B essential modifier)
[Nfatc2ip Nip45] NFATC2-interacting protein (45 kDa NF-AT-interacting protein) (45 kDa NFAT-interacting protein) (Nuclear factor of activated T-cells, cytoplasmic 2-interacting protein)

Bibliography :