NFIL3_HUMAN
ID NFIL3_HUMAN Reviewed; 462 AA.
AC Q16649; B2R9Y8; Q14211; Q6FGQ8; Q96HS0;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Nuclear factor interleukin-3-regulated protein;
DE AltName: Full=E4 promoter-binding protein 4;
DE AltName: Full=Interleukin-3 promoter transcriptional activator;
DE AltName: Full=Interleukin-3-binding protein 1;
DE AltName: Full=Transcriptional activator NF-IL3A;
GN Name=NFIL3; Synonyms=E4BP4, IL3BP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, AND DNA-BINDING.
RC TISSUE=Placenta;
RX PubMed=1620116; DOI=10.1128/mcb.12.7.3070-3077.1992;
RA Cowell I.G., Skinner A., Hurst H.C.;
RT "Transcriptional repression by a novel member of the bZIP family of
RT transcription factors.";
RL Mol. Cell. Biol. 12:3070-3077(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, AND DNA-BINDING.
RC TISSUE=T-cell;
RX PubMed=7565758; DOI=10.1128/mcb.15.11.6055;
RA Zhang W., Zhang J., Kornuc M., Kwan K., Frank R., Nimer S.D.;
RT "Molecular cloning and characterization of NF-IL3A, a transcriptional
RT activator of the human interleukin-3 promoter.";
RL Mol. Cell. Biol. 15:6055-6063(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP FUNCTION, INTERACTION WITH DR1, AND MUTAGENESIS OF LYS-330 AND LYS-332.
RX PubMed=8836190; DOI=10.1093/nar/24.18.3607;
RA Cowell I.G., Hurst H.C.;
RT "Protein-protein interaction between the transcriptional repressor E4BP4
RT and the TBP-binding protein Dr1.";
RL Nucleic Acids Res. 24:3607-3613(1996).
RN [10]
RP TISSUE SPECIFICITY.
RX PubMed=10942106; DOI=10.1007/s004390000306;
RA Hulme D.J., Blair I.P., Dawkins J.L., Nicholson G.A.;
RT "Exclusion of NFIL3 as the gene causing hereditary sensory neuropathy type
RT I by mutation analysis.";
RL Hum. Genet. 106:594-596(2000).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301 AND SER-353, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301 AND SER-353, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [16]
RP INTERACTION WITH MYSM1.
RX PubMed=24062447; DOI=10.1073/pnas.1308888110;
RA Nandakumar V., Chou Y., Zang L., Huang X.F., Chen S.Y.;
RT "Epigenetic control of natural killer cell maturation by histone H2A
RT deubiquitinase, MYSM1.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:E3927-E3936(2013).
RN [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-219; LYS-337; LYS-394 AND
RP LYS-406, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-219, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-219; LYS-337; LYS-394; LYS-434
RP AND LYS-448, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-219 AND LYS-337, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [21]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-24; LYS-214; LYS-219; LYS-306;
RP LYS-314; LYS-326; LYS-332; LYS-337; LYS-350; LYS-360; LYS-394; LYS-401;
RP LYS-406; LYS-412; LYS-419; LYS-424; LYS-434 AND LYS-448, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Acts as a transcriptional regulator that recognizes and binds
CC to the sequence 5'-[GA]TTA[CT]GTAA[CT]-3', a sequence present in many
CC cellular and viral promoters. Represses transcription from promoters
CC with activating transcription factor (ATF) sites. Represses promoter
CC activity in osteoblasts (By similarity). Represses transcriptional
CC activity of PER1 (By similarity). Represses transcriptional activity of
CC PER2 via the B-site on the promoter (By similarity). Activates
CC transcription from the interleukin-3 promoter in T-cells. Competes for
CC the same consensus-binding site with PAR DNA-binding factors (DBP, HLF
CC and TEF) (By similarity). Component of the circadian clock that acts as
CC a negative regulator for the circadian expression of PER2 oscillation
CC in the cell-autonomous core clock (By similarity). Protects pro-B cells
CC from programmed cell death (By similarity). Represses the transcription
CC of CYP2A5 (By similarity). Positively regulates the expression and
CC activity of CES2 by antagonizing the repressive action of NR1D1 on CES2
CC (By similarity). Required for the development of natural killer cell
CC precursors (By similarity). {ECO:0000250|UniProtKB:O08750,
CC ECO:0000269|PubMed:1620116, ECO:0000269|PubMed:7565758,
CC ECO:0000269|PubMed:8836190}.
CC -!- SUBUNIT: Homodimer (PubMed:1620116). Binds DNA as a dimer
CC (PubMed:1620116). Interacts with DR1 (PubMed:8836190). Interacts with
CC PER2 and CRY2 (By similarity). Interacts with NR0B2 (By similarity).
CC Interacts with MYSM1 (PubMed:24062447). {ECO:0000250|UniProtKB:O08750,
CC ECO:0000269|PubMed:1620116, ECO:0000269|PubMed:24062447,
CC ECO:0000269|PubMed:8836190}.
CC -!- INTERACTION:
CC Q16649; Q9Y2J4: AMOTL2; NbExp=4; IntAct=EBI-3951858, EBI-746752;
CC Q16649; Q9Y2J4-4: AMOTL2; NbExp=3; IntAct=EBI-3951858, EBI-10187270;
CC Q16649; P18846: ATF1; NbExp=3; IntAct=EBI-3951858, EBI-852794;
CC Q16649; P16220: CREB1; NbExp=3; IntAct=EBI-3951858, EBI-711855;
CC Q16649; Q68CJ9: CREB3L3; NbExp=2; IntAct=EBI-3951858, EBI-852194;
CC Q16649; P35638: DDIT3; NbExp=2; IntAct=EBI-3951858, EBI-742651;
CC Q16649; Q96IK5: GMCL1; NbExp=3; IntAct=EBI-3951858, EBI-2548508;
CC Q16649; O75031: HSF2BP; NbExp=3; IntAct=EBI-3951858, EBI-7116203;
CC Q16649; Q9ULX9: MAFF; NbExp=2; IntAct=EBI-3951858, EBI-721128;
CC Q16649; O15525: MAFG; NbExp=2; IntAct=EBI-3951858, EBI-713514;
CC Q16649; Q16649: NFIL3; NbExp=2; IntAct=EBI-3951858, EBI-3951858;
CC Q16649; O76083-2: PDE9A; NbExp=3; IntAct=EBI-3951858, EBI-11524542;
CC Q16649; Q8WWB5: PIH1D2; NbExp=3; IntAct=EBI-3951858, EBI-10232538;
CC Q16649; Q6NUQ1: RINT1; NbExp=3; IntAct=EBI-3951858, EBI-726876;
CC Q16649; Q12933: TRAF2; NbExp=3; IntAct=EBI-3951858, EBI-355744;
CC Q16649; Q9DGW5: MDV005; Xeno; NbExp=3; IntAct=EBI-3951858, EBI-10889526;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
CC -!- TISSUE SPECIFICITY: Expressed in bladder stomach, thyroid, spinal cord,
CC lymph node, trachea, adrenal gland, bone marrow and muscle.
CC {ECO:0000269|PubMed:10942106}.
CC -!- INDUCTION: Up-regulated by PHA or TPA. {ECO:0000269|PubMed:7565758}.
CC -!- SIMILARITY: Belongs to the bZIP family. NFIL3 subfamily. {ECO:0000305}.
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DR EMBL; U26173; AAA93067.1; -; mRNA.
DR EMBL; X64318; CAA45597.1; -; mRNA.
DR EMBL; S79880; AAB35410.1; -; mRNA.
DR EMBL; EF028070; ABK15691.1; -; Genomic_DNA.
DR EMBL; CR542049; CAG46846.1; -; mRNA.
DR EMBL; AK313970; BAG36685.1; -; mRNA.
DR EMBL; AL353764; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471089; EAW62796.1; -; Genomic_DNA.
DR EMBL; BC008197; AAH08197.1; -; mRNA.
DR CCDS; CCDS6690.1; -.
DR PIR; G01804; G01804.
DR RefSeq; NP_001276928.1; NM_001289999.1.
DR RefSeq; NP_001276929.1; NM_001290000.1.
DR RefSeq; NP_005375.2; NM_005384.2.
DR RefSeq; XP_016870232.1; XM_017014743.1.
DR RefSeq; XP_016870233.1; XM_017014744.1.
DR AlphaFoldDB; Q16649; -.
DR SMR; Q16649; -.
DR BioGRID; 110855; 31.
DR ComplexPortal; CPX-6404; bZIP transcription factor complex, ATF1-NFIL3.
DR ComplexPortal; CPX-7017; bZIP transcription factor complex, BATF-NFIL3.
DR IntAct; Q16649; 24.
DR MINT; Q16649; -.
DR STRING; 9606.ENSP00000297689; -.
DR iPTMnet; Q16649; -.
DR PhosphoSitePlus; Q16649; -.
DR BioMuta; NFIL3; -.
DR DMDM; 150385077; -.
DR EPD; Q16649; -.
DR jPOST; Q16649; -.
DR MassIVE; Q16649; -.
DR MaxQB; Q16649; -.
DR PaxDb; Q16649; -.
DR PeptideAtlas; Q16649; -.
DR PRIDE; Q16649; -.
DR ProteomicsDB; 61000; -.
DR Antibodypedia; 926; 383 antibodies from 39 providers.
DR DNASU; 4783; -.
DR Ensembl; ENST00000297689.4; ENSP00000297689.2; ENSG00000165030.4.
DR GeneID; 4783; -.
DR KEGG; hsa:4783; -.
DR MANE-Select; ENST00000297689.4; ENSP00000297689.2; NM_005384.3; NP_005375.2.
DR UCSC; uc004arh.3; human.
DR CTD; 4783; -.
DR DisGeNET; 4783; -.
DR GeneCards; NFIL3; -.
DR HGNC; HGNC:7787; NFIL3.
DR HPA; ENSG00000165030; Low tissue specificity.
DR MIM; 605327; gene.
DR neXtProt; NX_Q16649; -.
DR OpenTargets; ENSG00000165030; -.
DR PharmGKB; PA31593; -.
DR VEuPathDB; HostDB:ENSG00000165030; -.
DR eggNOG; KOG3119; Eukaryota.
DR GeneTree; ENSGT00940000160540; -.
DR HOGENOM; CLU_052045_0_0_1; -.
DR InParanoid; Q16649; -.
DR OMA; KNVHATV; -.
DR OrthoDB; 1450431at2759; -.
DR PhylomeDB; Q16649; -.
DR TreeFam; TF328374; -.
DR PathwayCommons; Q16649; -.
DR Reactome; R-HSA-400253; Circadian Clock.
DR SignaLink; Q16649; -.
DR SIGNOR; Q16649; -.
DR BioGRID-ORCS; 4783; 17 hits in 1100 CRISPR screens.
DR ChiTaRS; NFIL3; human.
DR GeneWiki; NFIL3; -.
DR GenomeRNAi; 4783; -.
DR Pharos; Q16649; Tbio.
DR PRO; PR:Q16649; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q16649; protein.
DR Bgee; ENSG00000165030; Expressed in vena cava and 200 other tissues.
DR ExpressionAtlas; Q16649; baseline and differential.
DR Genevisible; Q16649; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IPI:ComplexPortal.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:ProtInc.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:BHF-UCL.
DR GO; GO:0071353; P:cellular response to interleukin-4; IEA:Ensembl.
DR GO; GO:0007623; P:circadian rhythm; IBA:GO_Central.
DR GO; GO:0006955; P:immune response; TAS:ProtInc.
DR GO; GO:0001779; P:natural killer cell differentiation; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:GO_Central.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR016743; NFIL3/E4BP4.
DR InterPro; IPR010533; Vert_IL3-reg_TF.
DR PANTHER; PTHR15284:SF1; PTHR15284:SF1; 1.
DR Pfam; PF07716; bZIP_2; 1.
DR Pfam; PF06529; Vert_IL3-reg_TF; 1.
DR PIRSF; PIRSF019029; bZIP_E4BP4; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 1: Evidence at protein level;
KW Activator; Biological rhythms; DNA-binding; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..462
FT /note="Nuclear factor interleukin-3-regulated protein"
FT /id="PRO_0000292667"
FT DOMAIN 73..136
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 79..95
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 99..106
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 189..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..363
FT /note="Necessary for transcriptional repression and
FT sufficient for interaction with DR1"
FT /evidence="ECO:0000269|PubMed:8836190"
FT COMPBIAS 189..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..294
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 24
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 214
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 219
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 219
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 306
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 314
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 326
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 332
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 337
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 350
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 360
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 394
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 401
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 406
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 412
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 419
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 424
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 434
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 448
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT MUTAGEN 330
FT /note="K->A: Interacts with DR1 and partially affects
FT transcriptional repression; when associated with E-332."
FT /evidence="ECO:0000269|PubMed:8836190"
FT MUTAGEN 330
FT /note="K->E: Does not interact with DR1 and drastically
FT affects transcriptional repression; when associated with E-
FT 332."
FT /evidence="ECO:0000269|PubMed:8836190"
FT MUTAGEN 332
FT /note="K->A: Interacts with DR1 and partially affects
FT transcriptional repression; when associated with E-330."
FT /evidence="ECO:0000269|PubMed:8836190"
FT MUTAGEN 332
FT /note="K->E: Does not interact with DR1 and drastically
FT affects transcriptional repression; when associated with E-
FT 330."
FT /evidence="ECO:0000269|PubMed:8836190"
FT CONFLICT 44..45
FT /note="EL -> DV (in Ref. 1; AAA93067/CAA45597 and 2;
FT AAB35410)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="F -> S (in Ref. 4; CAG46846)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="R -> G (in Ref. 1; AAA93067/CAA45597 and 2;
FT AAB35410)"
FT /evidence="ECO:0000305"
SQ 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
