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Protein

Nuclear factor interleukin-3-regulated protein

Gene

Nfil3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 (By similarity). Represses promoter activity in osteoblasts. Represses transcriptional activity of PER1. Represses transcriptional activity of PER2 via the B-site on the promoter. Activates transcription from the interleukin-3 promoter in T-cells (By similarity). Competes for the same consensus-binding site with PAR DNA-binding factors (DBP, HLF and TEF). Component of the circadian clock that acts as a negative regulator for the circadian expression of PER2 oscillation in the cell-autonomous core clock. Protects pro-B cells from programmed cell death.By similarity4 Publications

GO - Molecular functioni

  1. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription Source: MGI
  2. RNA polymerase II core promoter sequence-specific DNA binding Source: MGI
  3. RNA polymerase II regulatory region sequence-specific DNA binding Source: MGI

GO - Biological processi

  1. cellular response to interleukin-4 Source: MGI
  2. circadian rhythm Source: InterPro
  3. negative regulation of transcription from RNA polymerase II promoter Source: MGI
  4. positive regulation of gene expression Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Biological rhythms, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear factor interleukin-3-regulated protein
Alternative name(s):
E4 promoter-binding protein 4
Embryo implantation-related NFIL3/E4BP4-like transcription factor
Gene namesi
Name:Nfil3
Synonyms:E4bp4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 13

Organism-specific databases

MGIiMGI:109495. Nfil3.

Subcellular locationi

Nucleus 1 PublicationPROSITE-ProRule annotation

GO - Cellular componenti

  1. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 462462Nuclear factor interleukin-3-regulated proteinPRO_0000292668Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei301 – 3011PhosphoserineBy similarity
Modified residuei353 – 3531PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiO08750.

PTM databases

PhosphoSiteiO08750.

Expressioni

Tissue specificityi

Expressed in suprachiasmatic nucleus and liver (at protein level). Expressed in suprachiasmatic nucleus, hippocampus, gyrus dentatus, piriform cortex, internal granular layer of olfactory bulb, dorsomedial hypothalamic nucleus, pontine nuclei, granular layer of cerebellum, liver and calvariae osteoblasts.2 Publications

Inductioni

Expression is regulated by circadian rhythms. Up-regulated by parathyroid hormone (PTH) (at protein level). Up-regulated by IL-3, forskolin, 8-bromo-cAMP, phorbol myristate acetate and PTH in primary osteoblasts and calvariae.3 Publications

Gene expression databases

BgeeiO08750.
CleanExiMM_NFIL3.
GenevestigatoriO08750.

Interactioni

Subunit structurei

Homodimer (By similarity). Binds DNA as a dimer (By similarity). Interacts with DR1 (By similarity). Interacts with PER2 and CRY2.By similarity1 Publication

Structurei

3D structure databases

ProteinModelPortaliO08750.
SMRiO08750. Positions 41-124.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini73 – 13664bZIPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni79 – 9517Basic motifPROSITE-ProRule annotationAdd
BLAST
Regioni99 – 1068Leucine-zipperPROSITE-ProRule annotation
Regioni281 – 420140Necessary for transcriptional repression and sufficient for interaction with PER2Add
BLAST

Sequence similaritiesi

Belongs to the bZIP family. NFIL3 subfamily.Curated
Contains 1 bZIP (basic-leucine zipper) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG260819.
GeneTreeiENSGT00530000064087.
HOGENOMiHOG000059596.
HOVERGENiHBG105717.
InParanoidiO08750.
KOiK09059.
OMAiWHQKELN.
OrthoDBiEOG7GQXWM.
PhylomeDBiO08750.
TreeFamiTF328374.

Family and domain databases

InterProiIPR004827. bZIP.
IPR016743. NFIL3/E4BP4.
IPR010533. Vert_IL3-reg_TF.
[Graphical view]
PANTHERiPTHR15284:SF1. PTHR15284:SF1. 1 hit.
PfamiPF07716. bZIP_2. 1 hit.
PF06529. Vert_IL3-reg_TF. 1 hit.
[Graphical view]
PIRSFiPIRSF019029. bZIP_E4BP4. 1 hit.
SMARTiSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEiPS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O08750-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQLRKMQTIK KEPAPLDPTS SSDKMLLLNS ALAEVAEDLA SGEDLLLNEG
60 70 80 90 100
SMGKNKSSAC RRKREFIPDE KKDAMYWEKR RKNNEAAKRS REKRRLNDLV
110 120 130 140 150
LENKLIALGE ENATLKAELL SLKLKFGLIS STAYAQEIQK LSNSTAVYFQ
160 170 180 190 200
DYQTSKAAVS SFVDEHEPAM VAGSCISVIK HSPQSSLSDV SEVSSVEHTQ
210 220 230 240 250
ESPAQGGCRS PENKFPVIKQ EPVELESFAR EAREERGTYS TSIYQSYMGS
260 270 280 290 300
SFSTYSHSPP LLQVHGSTSN SPRTSEADEG VVGKSSDGED EQQVPKGPIH
310 320 330 340 350
SPVELQRVHA TVVKVPEVNP SALPHKLRIK AKAMQVKVEA LDSEFEGMQK
360 370 380 390 400
LSSPADAIAK RHFDLEKHGT SGMAHSSLPP FSVQVTNIQD WSLKSEHWHH
410 420 430 440 450
KELSSKTQSS FKTGVVEVKD GGYKVSEAEN LYLKQGIANL SAEVVSLKRF
460
IATQPISASD SR
Length:462
Mass (Da):50,943
Last modified:July 1, 1997 - v1
Checksum:iDC711EB4CAC0112E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti101 – 1011L → F in BAE26446. (PubMed:16141072)Curated
Sequence conflicti141 – 1411L → F in AAI00385. (PubMed:15489334)Curated
Sequence conflicti189 – 1891D → G in AAI00385. (PubMed:15489334)Curated
Sequence conflicti450 – 4501F → V in BAE26446. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U83148 Genomic DNA. Translation: AAB53973.1.
AY061760 mRNA. Translation: AAL29942.1.
AK145451 mRNA. Translation: BAE26446.1.
BC031377 mRNA. Translation: AAH31377.1.
BC100384 mRNA. Translation: AAI00385.1.
CCDSiCCDS26519.1.
RefSeqiNP_059069.1. NM_017373.3.
XP_006516938.1. XM_006516875.1.
XP_006516939.1. XM_006516876.1.
XP_006516940.1. XM_006516877.1.
XP_006516941.1. XM_006516878.1.
XP_006516942.1. XM_006516879.1.
UniGeneiMm.136604.

Genome annotation databases

EnsembliENSMUST00000071065; ENSMUSP00000065363; ENSMUSG00000056749.
GeneIDi18030.
KEGGimmu:18030.
UCSCiuc007qnh.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U83148 Genomic DNA. Translation: AAB53973.1.
AY061760 mRNA. Translation: AAL29942.1.
AK145451 mRNA. Translation: BAE26446.1.
BC031377 mRNA. Translation: AAH31377.1.
BC100384 mRNA. Translation: AAI00385.1.
CCDSiCCDS26519.1.
RefSeqiNP_059069.1. NM_017373.3.
XP_006516938.1. XM_006516875.1.
XP_006516939.1. XM_006516876.1.
XP_006516940.1. XM_006516877.1.
XP_006516941.1. XM_006516878.1.
XP_006516942.1. XM_006516879.1.
UniGeneiMm.136604.

3D structure databases

ProteinModelPortaliO08750.
SMRiO08750. Positions 41-124.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

PhosphoSiteiO08750.

Proteomic databases

PRIDEiO08750.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000071065; ENSMUSP00000065363; ENSMUSG00000056749.
GeneIDi18030.
KEGGimmu:18030.
UCSCiuc007qnh.1. mouse.

Organism-specific databases

CTDi4783.
MGIiMGI:109495. Nfil3.

Phylogenomic databases

eggNOGiNOG260819.
GeneTreeiENSGT00530000064087.
HOGENOMiHOG000059596.
HOVERGENiHBG105717.
InParanoidiO08750.
KOiK09059.
OMAiWHQKELN.
OrthoDBiEOG7GQXWM.
PhylomeDBiO08750.
TreeFamiTF328374.

Miscellaneous databases

NextBioi293109.
PROiO08750.
SOURCEiSearch...

Gene expression databases

BgeeiO08750.
CleanExiMM_NFIL3.
GenevestigatoriO08750.

Family and domain databases

InterProiIPR004827. bZIP.
IPR016743. NFIL3/E4BP4.
IPR010533. Vert_IL3-reg_TF.
[Graphical view]
PANTHERiPTHR15284:SF1. PTHR15284:SF1. 1 hit.
PfamiPF07716. bZIP_2. 1 hit.
PF06529. Vert_IL3-reg_TF. 1 hit.
[Graphical view]
PIRSFiPIRSF019029. bZIP_E4BP4. 1 hit.
SMARTiSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEiPS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Pivotal role for the NFIL3/E4BP4 transcription factor in interleukin 3-mediated survival of pro-B lymphocytes."
    Ikushima S., Inukai T., Inaba T., Nimer S.D., Cleveland J.L., Look A.T.
    Proc. Natl. Acad. Sci. U.S.A. 94:2609-2614(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION, DNA-BINDING.
  2. "Identification of novel endometrial factors involved in the mouse embryo implantation."
    Shen Q.-X., Wang J., Huang Z.-P.
    Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
    Tissue: Embryo and Uterus.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and FVB/N.
    Tissue: Egg and Mammary tumor.
  5. "Antagonistic role of E4BP4 and PAR proteins in the circadian oscillatory mechanism."
    Mitsui S., Yamaguchi S., Matsuo T., Ishida Y., Okamura H.
    Genes Dev. 15:995-1006(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DNA-BINDING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  6. "Parathyroid hormone-induced E4BP4/NFIL3 down-regulates transcription in osteoblasts."
    Ozkurt I.C., Tetradis S.
    J. Biol. Chem. 278:26803-26809(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION, TISSUE SPECIFICITY.
  7. "Parathyroid hormone induces E4bp4 messenger ribonucleic acid expression primarily through cyclic adenosine 3',5'-monophosphate signaling in osteoblasts."
    Ozkurt I.C., Pirih F.Q., Tetradis S.
    Endocrinology 145:3696-3703(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION, DNA-BINDING.
  8. "The negative transcription factor E4BP4 is associated with circadian clock protein PERIOD2."
    Ohno T., Onishi Y., Ishida N.
    Biochem. Biophys. Res. Commun. 354:1010-1015(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PER2 AND CRY2.
  9. "A novel E4BP4 element drives circadian expression of mPeriod2."
    Ohno T., Onishi Y., Ishida N.
    Nucleic Acids Res. 35:648-655(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DNA-BINDING.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiNFIL3_MOUSE
AccessioniPrimary (citable) accession number: O08750
Secondary accession number(s): Q3ULK2, Q497U0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: July 1, 1997
Last modified: February 4, 2015
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.