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Nuclear factor interleukin-3-regulated protein (E4 promoter-binding protein 4) (Interleukin-3 promoter transcriptional activator) (Interleukin-3-binding protein 1) (Transcriptional activator NF-IL3A)

 NFIL3_HUMAN             Reviewed;         462 AA.
Q16649; B2R9Y8; Q14211; Q6FGQ8; Q96HS0;
26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
26-JUN-2007, sequence version 2.
02-JUN-2021, entry version 166.
RecName: Full=Nuclear factor interleukin-3-regulated protein;
AltName: Full=E4 promoter-binding protein 4;
AltName: Full=Interleukin-3 promoter transcriptional activator;
AltName: Full=Interleukin-3-binding protein 1;
AltName: Full=Transcriptional activator NF-IL3A;
Name=NFIL3; Synonyms=E4BP4, IL3BP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, AND DNA-BINDING.
TISSUE=Placenta;
PubMed=1620116; DOI=10.1128/mcb.12.7.3070;
Cowell I.G., Skinner A., Hurst H.C.;
"Transcriptional repression by a novel member of the bZIP family of
transcription factors.";
Mol. Cell. Biol. 12:3070-3077(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, AND DNA-BINDING.
TISSUE=T-cell;
PubMed=7565758; DOI=10.1128/mcb.15.11.6055;
Zhang W., Zhang J., Kornuc M., Kwan K., Frank R., Nimer S.D.;
"Molecular cloning and characterization of NF-IL3A, a transcriptional
activator of the human interleukin-3 promoter.";
Mol. Cell. Biol. 15:6055-6063(1995).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[7]
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.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
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).
[9]
FUNCTION, INTERACTION WITH DR1, AND MUTAGENESIS OF LYS-330 AND LYS-332.
PubMed=8836190; DOI=10.1093/nar/24.18.3607;
Cowell I.G., Hurst H.C.;
"Protein-protein interaction between the transcriptional repressor E4BP4
and the TBP-binding protein Dr1.";
Nucleic Acids Res. 24:3607-3613(1996).
[10]
TISSUE SPECIFICITY.
PubMed=10942106; DOI=10.1007/s004390000306;
Hulme D.J., Blair I.P., Dawkins J.L., Nicholson G.A.;
"Exclusion of NFIL3 as the gene causing hereditary sensory neuropathy type
I by mutation analysis.";
Hum. Genet. 106:594-596(2000).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301, 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).
[12]
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).
[13]
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).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301 AND SER-353, 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).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301 AND SER-353, 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).
[16]
INTERACTION WITH MYSM1.
PubMed=24062447; DOI=10.1073/pnas.1308888110;
Nandakumar V., Chou Y., Zang L., Huang X.F., Chen S.Y.;
"Epigenetic control of natural killer cell maturation by histone H2A
deubiquitinase, MYSM1.";
Proc. Natl. Acad. Sci. U.S.A. 110:E3927-E3936(2013).
[17]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-219; LYS-337; LYS-394 AND
LYS-406, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[18]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-219, 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).
[19]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-219; LYS-337; LYS-394; LYS-434
AND LYS-448, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[20]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-219 AND LYS-337, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.o114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to replication
stress reveals novel small ubiquitin-like modified target proteins and
acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[21]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-24; LYS-214; LYS-219; LYS-306;
LYS-314; LYS-326; LYS-332; LYS-337; LYS-350; LYS-360; LYS-394; LYS-401;
LYS-406; LYS-412; LYS-419; LYS-424; LYS-434 AND LYS-448, 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).
-!- FUNCTION: Acts as a transcriptional regulator that recognizes and binds
to the sequence 5'-[GA]TTA[CT]GTAA[CT]-3', a sequence present in many
cellular and viral promoters. Represses transcription from promoters
with activating transcription factor (ATF) sites. Represses promoter
activity in osteoblasts (By similarity). Represses transcriptional
activity of PER1 (By similarity). Represses transcriptional activity of
PER2 via the B-site on the promoter (By similarity). Activates
transcription from the interleukin-3 promoter in T-cells. Competes for
the same consensus-binding site with PAR DNA-binding factors (DBP, HLF
and TEF) (By similarity). Component of the circadian clock that acts as
a negative regulator for the circadian expression of PER2 oscillation
in the cell-autonomous core clock (By similarity). Protects pro-B cells
from programmed cell death (By similarity). Represses the transcription
of CYP2A5 (By similarity). Positively regulates the expression and
activity of CES2 by antagonizing the repressive action of NR1D1 on CES2
(By similarity). Required for the development of natural killer cell
precursors (By similarity). {ECO:0000250|UniProtKB:O08750,
ECO:0000269|PubMed:1620116, ECO:0000269|PubMed:7565758,
ECO:0000269|PubMed:8836190}.
-!- SUBUNIT: Homodimer (PubMed:1620116). Binds DNA as a dimer
(PubMed:1620116). Interacts with DR1 (PubMed:8836190). Interacts with
PER2 and CRY2 (By similarity). Interacts with NR0B2 (By similarity).
Interacts with MYSM1 (PubMed:24062447). {ECO:0000250|UniProtKB:O08750,
ECO:0000269|PubMed:1620116, ECO:0000269|PubMed:24062447,
ECO:0000269|PubMed:8836190}.
-!- INTERACTION:
Q16649; Q9Y2J4: AMOTL2; NbExp=4; IntAct=EBI-3951858, EBI-746752;
Q16649; Q9Y2J4-4: AMOTL2; NbExp=3; IntAct=EBI-3951858, EBI-10187270;
Q16649; P18846: ATF1; NbExp=3; IntAct=EBI-3951858, EBI-852794;
Q16649; P16220: CREB1; NbExp=3; IntAct=EBI-3951858, EBI-711855;
Q16649; Q68CJ9: CREB3L3; NbExp=2; IntAct=EBI-3951858, EBI-852194;
Q16649; P35638: DDIT3; NbExp=2; IntAct=EBI-3951858, EBI-742651;
Q16649; Q96IK5: GMCL1; NbExp=3; IntAct=EBI-3951858, EBI-2548508;
Q16649; O75031: HSF2BP; NbExp=3; IntAct=EBI-3951858, EBI-7116203;
Q16649; Q9ULX9: MAFF; NbExp=2; IntAct=EBI-3951858, EBI-721128;
Q16649; O15525: MAFG; NbExp=2; IntAct=EBI-3951858, EBI-713514;
Q16649; Q16649: NFIL3; NbExp=2; IntAct=EBI-3951858, EBI-3951858;
Q16649; O76083-2: PDE9A; NbExp=3; IntAct=EBI-3951858, EBI-11524542;
Q16649; Q8WWB5: PIH1D2; NbExp=3; IntAct=EBI-3951858, EBI-10232538;
Q16649; Q6NUQ1: RINT1; NbExp=3; IntAct=EBI-3951858, EBI-726876;
Q16649; Q12933: TRAF2; NbExp=3; IntAct=EBI-3951858, EBI-355744;
Q16649; Q9DGW5: MDV005; Xeno; NbExp=3; IntAct=EBI-3951858, EBI-10889526;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
-!- TISSUE SPECIFICITY: Expressed in bladder stomach, thyroid, spinal cord,
lymph node, trachea, adrenal gland, bone marrow and muscle.
{ECO:0000269|PubMed:10942106}.
-!- INDUCTION: Up-regulated by PHA or TPA. {ECO:0000269|PubMed:7565758}.
-!- SIMILARITY: Belongs to the bZIP family. NFIL3 subfamily. {ECO:0000305}.
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EMBL; U26173; AAA93067.1; -; mRNA.
EMBL; X64318; CAA45597.1; -; mRNA.
EMBL; S79880; AAB35410.1; -; mRNA.
EMBL; EF028070; ABK15691.1; -; Genomic_DNA.
EMBL; CR542049; CAG46846.1; -; mRNA.
EMBL; AK313970; BAG36685.1; -; mRNA.
EMBL; AL353764; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471089; EAW62796.1; -; Genomic_DNA.
EMBL; BC008197; AAH08197.1; -; mRNA.
CCDS; CCDS6690.1; -.
PIR; G01804; G01804.
RefSeq; NP_001276928.1; NM_001289999.1.
RefSeq; NP_001276929.1; NM_001290000.1.
RefSeq; NP_005375.2; NM_005384.2.
RefSeq; XP_016870232.1; XM_017014743.1.
RefSeq; XP_016870233.1; XM_017014744.1.
SMR; Q16649; -.
BioGRID; 110855; 29.
IntAct; Q16649; 23.
MINT; Q16649; -.
STRING; 9606.ENSP00000297689; -.
iPTMnet; Q16649; -.
PhosphoSitePlus; Q16649; -.
BioMuta; NFIL3; -.
DMDM; 150385077; -.
EPD; Q16649; -.
jPOST; Q16649; -.
MassIVE; Q16649; -.
MaxQB; Q16649; -.
PaxDb; Q16649; -.
PeptideAtlas; Q16649; -.
PRIDE; Q16649; -.
ProteomicsDB; 61000; -.
Antibodypedia; 926; 367 antibodies.
DNASU; 4783; -.
Ensembl; ENST00000297689; ENSP00000297689; ENSG00000165030.
GeneID; 4783; -.
KEGG; hsa:4783; -.
UCSC; uc004arh.3; human.
CTD; 4783; -.
DisGeNET; 4783; -.
GeneCards; NFIL3; -.
HGNC; HGNC:7787; NFIL3.
HPA; ENSG00000165030; Low tissue specificity.
MIM; 605327; gene.
neXtProt; NX_Q16649; -.
OpenTargets; ENSG00000165030; -.
PharmGKB; PA31593; -.
VEuPathDB; HostDB:ENSG00000165030.3; -.
eggNOG; KOG3119; Eukaryota.
GeneTree; ENSGT00940000160540; -.
HOGENOM; CLU_052045_0_0_1; -.
InParanoid; Q16649; -.
OMA; QDWSLKP; -.
OrthoDB; 1450431at2759; -.
PhylomeDB; Q16649; -.
TreeFam; TF328374; -.
PathwayCommons; Q16649; -.
Reactome; R-HSA-400253; Circadian Clock.
SignaLink; Q16649; -.
SIGNOR; Q16649; -.
BioGRID-ORCS; 4783; 6 hits in 1015 CRISPR screens.
ChiTaRS; NFIL3; human.
GeneWiki; NFIL3; -.
GenomeRNAi; 4783; -.
Pharos; Q16649; Tbio.
PRO; PR:Q16649; -.
Proteomes; UP000005640; Chromosome 9.
RNAct; Q16649; protein.
Bgee; ENSG00000165030; Expressed in ectocervix and 237 other tissues.
ExpressionAtlas; Q16649; baseline and differential.
Genevisible; Q16649; HS.
GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:ProtInc.
GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:GO_Central.
GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:GO_Central.
GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0071353; P:cellular response to interleukin-4; IEA:Ensembl.
GO; GO:0007623; P:circadian rhythm; IBA:GO_Central.
GO; GO:0006955; P:immune response; TAS:ProtInc.
GO; GO:0001779; P:natural killer cell differentiation; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:GO_Central.
GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
InterPro; IPR004827; bZIP.
InterPro; IPR016743; NFIL3/E4BP4.
InterPro; IPR010533; Vert_IL3-reg_TF.
PANTHER; PTHR15284:SF1; PTHR15284:SF1; 1.
Pfam; PF07716; bZIP_2; 1.
Pfam; PF06529; Vert_IL3-reg_TF; 1.
PIRSF; PIRSF019029; bZIP_E4BP4; 1.
SMART; SM00338; BRLZ; 1.
PROSITE; PS50217; BZIP; 1.
PROSITE; PS00036; BZIP_BASIC; 1.
1: Evidence at protein level;
Activator; Biological rhythms; DNA-binding; Isopeptide bond; Nucleus;
Phosphoprotein; Reference proteome; Repressor; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1..462
/note="Nuclear factor interleukin-3-regulated protein"
/id="PRO_0000292667"
DOMAIN 73..136
/note="bZIP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
REGION 79..95
/note="Basic motif"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
REGION 99..106
/note="Leucine-zipper"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
REGION 189..237
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 258..302
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 299..363
/note="Necessary for transcriptional repression and
sufficient for interaction with DR1"
/evidence="ECO:0000269|PubMed:8836190"
COMPBIAS 189..214
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 258..279
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 280..294
/note="Basic and acidic residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
MOD_RES 301
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:17081983,
ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
MOD_RES 353
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:20068231,
ECO:0007744|PubMed:23186163"
CROSSLNK 24
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0007744|PubMed:28112733"
CROSSLNK 214
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0007744|PubMed:28112733"
CROSSLNK 219
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO1); alternate"
/evidence="ECO:0007744|PubMed:25114211"
CROSSLNK 219
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2); alternate"
/evidence="ECO:0007744|PubMed:25114211,
ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297,
ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
CROSSLNK 306
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0007744|PubMed:28112733"
CROSSLNK 314
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0007744|PubMed:28112733"
CROSSLNK 326
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0007744|PubMed:28112733"
CROSSLNK 332
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0007744|PubMed:28112733"
CROSSLNK 337
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0007744|PubMed:25218447,
ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
ECO:0007744|PubMed:28112733"
CROSSLNK 350
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0007744|PubMed:28112733"
CROSSLNK 360
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0007744|PubMed:28112733"
CROSSLNK 394
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0007744|PubMed:25218447,
ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
CROSSLNK 401
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0007744|PubMed:28112733"
CROSSLNK 406
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0007744|PubMed:25218447,
ECO:0007744|PubMed:28112733"
CROSSLNK 412
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0007744|PubMed:28112733"
CROSSLNK 419
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0007744|PubMed:28112733"
CROSSLNK 424
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0007744|PubMed:28112733"
CROSSLNK 434
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0007744|PubMed:25772364,
ECO:0007744|PubMed:28112733"
CROSSLNK 448
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0007744|PubMed:25772364,
ECO:0007744|PubMed:28112733"
MUTAGEN 330
/note="K->A: Interacts with DR1 and partially affects
transcriptional repression; when associated with E-332."
/evidence="ECO:0000269|PubMed:8836190"
MUTAGEN 330
/note="K->E: Does not interact with DR1 and drastically
affects transcriptional repression; when associated with E-
332."
/evidence="ECO:0000269|PubMed:8836190"
MUTAGEN 332
/note="K->A: Interacts with DR1 and partially affects
transcriptional repression; when associated with E-330."
/evidence="ECO:0000269|PubMed:8836190"
MUTAGEN 332
/note="K->E: Does not interact with DR1 and drastically
affects transcriptional repression; when associated with E-
330."
/evidence="ECO:0000269|PubMed:8836190"
CONFLICT 44..45
/note="EL -> DV (in Ref. 1; AAA93067/CAA45597 and 2;
AAB35410)"
/evidence="ECO:0000305"
CONFLICT 149
/note="F -> S (in Ref. 4; CAG46846)"
/evidence="ECO:0000305"
CONFLICT 273
/note="R -> G (in Ref. 1; AAA93067/CAA45597 and 2;
AAB35410)"
/evidence="ECO:0000305"
SEQUENCE 462 AA; 51472 MW; D19946AAC774C3E7 CRC64;
MQLRKMQTVK KEQASLDASS NVDKMMVLNS ALTEVSEDST TGEELLLSEG SVGKNKSSAC
RRKREFIPDE KKDAMYWEKR RKNNEAAKRS REKRRLNDLV LENKLIALGE ENATLKAELL
SLKLKFGLIS STAYAQEIQK LSNSTAVYFQ DYQTSKSNVS SFVDEHEPSM VSSSCISVIK
HSPQSSLSDV SEVSSVEHTQ ESSVQGSCRS PENKFQIIKQ EPMELESYTR EPRDDRGSYT
ASIYQNYMGN SFSGYSHSPP LLQVNRSSSN SPRTSETDDG VVGKSSDGED EQQVPKGPIH
SPVELKHVHA TVVKVPEVNS SALPHKLRIK AKAMQIKVEA FDNEFEATQK LSSPIDMTSK
RHFELEKHSA PSMVHSSLTP FSVQVTNIQD WSLKSEHWHQ KELSGKTQNS FKTGVVEMKD
SGYKVSDPEN LYLKQGIANL SAEVVSLKRL IATQPISASD SG


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Related Genes :
[NFIL3 E4BP4 IL3BP1] Nuclear factor interleukin-3-regulated protein (E4 promoter-binding protein 4) (Interleukin-3 promoter transcriptional activator) (Interleukin-3-binding protein 1) (Transcriptional activator NF-IL3A)
[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)
[Cebpb] CCAAT/enhancer-binding protein beta (C/EBP beta) (AGP/EBP) (Interleukin-6-dependent-binding protein) (IL-6DBP) (Liver-enriched transcriptional activator) (LAP)
[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)
[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)
[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]
[IL33 C9orf26 IL1F11 NFHEV] Interleukin-33 (IL-33) (Interleukin-1 family member 11) (IL-1F11) (Nuclear factor from high endothelial venules) (NF-HEV) [Cleaved into: Interleukin-33 (95-270); Interleukin-33 (99-270); Interleukin-33 (109-270)]
[TRAF6 RNF85] TNF receptor-associated factor 6 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF6) (Interleukin-1 signal transducer) (RING finger protein 85) (RING-type E3 ubiquitin transferase TRAF6)
[Ilf3] Interleukin enhancer-binding factor 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]
[RELA NFKB3] Transcription factor p65 (Nuclear factor NF-kappa-B p65 subunit) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells 3)
[Rela Nfkb3] Transcription factor p65 (Nuclear factor NF-kappa-B p65 subunit) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells 3)
[FOXK2 ILF ILF1] Forkhead box protein K2 (G/T-mismatch specific binding protein) (nGTBP) (Interleukin enhancer-binding factor 1)
[NFATC4 NFAT3] Nuclear factor of activated T-cells, cytoplasmic 4 (NF-ATc4) (NFATc4) (T-cell transcription factor NFAT3) (NF-AT3)
[Rel CG11992] Nuclear factor NF-kappa-B p110 subunit (Rel-p110) (Relish protein) [Cleaved into: Nuclear factor NF-kappa-B p68 subunit (Rel-p68); Nuclear factor NF-kappa-B p49 subunit (Rel-p49)]
[SMARCA4 BAF190A BRG1 SNF2B SNF2L4] Transcription activator BRG1 (EC 3.6.4.-) (ATP-dependent helicase SMARCA4) (BRG1-associated factor 190A) (BAF190A) (Mitotic growth and transcription activator) (Protein BRG-1) (Protein brahma homolog 1) (SNF2-beta) (SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4)
[Pou2f2 Oct2 Otf2] POU domain, class 2, transcription factor 2 (Lymphoid-restricted immunoglobulin octamer-binding protein NF-A2) (Octamer-binding protein 2) (Oct-2) (Octamer-binding transcription factor 2) (OTF-2)
[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]
[GABPB1 E4TF1B GABPB GABPB2] GA-binding protein subunit beta-1 (GABP subunit beta-1) (GABPB-1) (GABP subunit beta-2) (GABPB-2) (Nuclear respiratory factor 2) (Transcription factor E4TF1-47) (Transcription factor E4TF1-53)
[Nfatc4 Nfat3] Nuclear factor of activated T-cells, cytoplasmic 4 (NF-ATc4) (NFATc4) (T-cell transcription factor NFAT3) (NF-AT3)
[tat] Protein Tat (Transactivating regulatory protein)
[Il1rl1 Ly84 St2 Ste2] Interleukin-1 receptor-like 1 (EC 3.2.2.6) (Interleukin-33 receptor alpha chain) (Lymphocyte antigen 84) (Protein ST2) (Protein T1)
[Ilf3] Interleukin enhancer-binding factor 3
[tat] Protein Tat (Transactivating regulatory protein)
[tat] Protein Tat (Transactivating regulatory protein)
[tat] Protein Tat (Transactivating regulatory protein)
[tat] Protein Tat (Transactivating regulatory protein)
[TICAM1 PRVTIRB TRIF] TIR domain-containing adapter molecule 1 (TICAM-1) (Proline-rich, vinculin and TIR domain-containing protein B) (Putative NF-kappa-B-activating protein 502H) (Toll-interleukin-1 receptor domain-containing adapter protein inducing interferon beta) (MyD88-3) (TIR domain-containing adapter protein inducing IFN-beta)
[TRAF3IP2 C6orf2 C6orf4 C6orf5 C6orf6] E3 ubiquitin ligase TRAF3IP2 (EC 2.3.2.27) (Adapter protein CIKS) (Connection to IKK and SAPK/JNK) (E3 ubiquitin-protein ligase CIKS) (Nuclear factor NF-kappa-B activator 1) (ACT1) (TRAF3-interacting protein 2)

Bibliography :
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