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 27-MAR-2024, entry version 179. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; 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; 33. DR ComplexPortal; CPX-6404; bZIP transcription factor complex, ATF1-NFIL3. DR ComplexPortal; CPX-7017; bZIP transcription factor complex, BATF-NFIL3. DR IntAct; Q16649; 26. 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; 9606-ENSP00000297689; -. DR PeptideAtlas; Q16649; -. DR ProteomicsDB; 61000; -. DR Pumba; Q16649; -. DR Antibodypedia; 926; 418 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 AGR; HGNC:7787; -. 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; PVDMTSK; -. DR OrthoDB; 4467729at2759; -. 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 1178 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 202 other cell types or tissues. DR ExpressionAtlas; Q16649; baseline and differential. 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:0045892; P:negative regulation of DNA-templated transcription; IDA:GO_Central. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:BHF-UCL. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:UniProtKB. DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; NAS:ComplexPortal. DR GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc. DR CDD; cd14694; bZIP_NFIL3; 1. DR Gene3D; 1.20.5.170; -; 1. DR InterPro; IPR004827; bZIP. DR InterPro; IPR046347; bZIP_sf. DR InterPro; IPR047229; NFIL3-like. DR InterPro; IPR047106; NFIL3-like_bZIP. DR InterPro; IPR016743; NFIL3/E4BP4. DR InterPro; IPR010533; Vert_IL3-reg_TF. DR PANTHER; PTHR15284; NUCLEAR FACTOR INTERLEUKIN-3-REGULATED PROTEIN; 1. DR PANTHER; PTHR15284:SF1; NUCLEAR FACTOR INTERLEUKIN-3-REGULATED PROTEIN; 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; Leucine zipper domain; 1. DR PROSITE; PS50217; BZIP; 1. DR PROSITE; PS00036; BZIP_BASIC; 1. DR Genevisible; Q16649; HS. 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 FT E-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 FT E-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 //