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Q16649 · NFIL3_HUMAN

  • Protein
    Nuclear factor interleukin-3-regulated protein
  • Gene
    NFIL3
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

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).

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentchromatin
Cellular Componentnucleus
Cellular ComponentRNA polymerase II transcription regulator complex
Molecular FunctionDNA-binding transcription factor activity
Molecular FunctionDNA-binding transcription factor activity, RNA polymerase II-specific
Molecular FunctionDNA-binding transcription repressor activity, RNA polymerase II-specific
Molecular Functionidentical protein binding
Molecular FunctionRNA polymerase II cis-regulatory region sequence-specific DNA binding
Molecular FunctionRNA polymerase II transcription regulatory region sequence-specific DNA binding
Biological Processcellular response to interleukin-4
Biological Processcircadian rhythm
Biological Processimmune response
Biological Processnatural killer cell differentiation
Biological Processnegative regulation of DNA-templated transcription
Biological Processnegative regulation of transcription by RNA polymerase II
Biological Processpositive regulation of DNA-templated transcription
Biological Processpositive regulation of gene expression
Biological Processregulation of DNA-templated transcription
Biological Processregulation of transcription by RNA polymerase II
Biological Processtranscription by RNA polymerase II

Keywords

Enzyme and pathway databases

Community curation (1)

Community annotation

The subsequence ACRRKREFIPDEKKDAMYWEKRRKNNEAAKRSREKRRLNDLVLENKLIALGEENATLKAELLSLKLKFGLISSTAYAQEI, which contains the bZIP_2 domain, shows transcriptional repressor activity in a high-throughput recruitment assay.

SourceSubmission dateContributor
PubMed:333267460000-0002-4108-0575

Names & Taxonomy

Protein names

  • Recommended name
    Nuclear factor interleukin-3-regulated protein
  • Alternative names
    • E4 promoter-binding protein 4
    • Interleukin-3 promoter transcriptional activator
    • Interleukin-3-binding protein 1
    • Transcriptional activator NF-IL3A

Gene names

    • Name
      NFIL3
    • Synonyms
      E4BP4, IL3BP1

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q16649
  • Secondary accessions
    • B2R9Y8
    • Q14211
    • Q6FGQ8
    • Q96HS0

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Disease & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis330Interacts with DR1 and partially affects transcriptional repression; when associated with E-332.
Mutagenesis330Does not interact with DR1 and drastically affects transcriptional repression; when associated with E-332.
Mutagenesis332Interacts with DR1 and partially affects transcriptional repression; when associated with E-330.
Mutagenesis332Does not interact with DR1 and drastically affects transcriptional repression; when associated with E-330.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 400 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

Showing features for chain, modified residue (large scale data), cross-link, modified residue.

Type
IDPosition(s)Source
Description
ChainPRO_00002926671-462UniProtNuclear factor interleukin-3-regulated protein
Modified residue (large scale data)19PRIDEPhosphoserine
Cross-link24UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue (large scale data)182PRIDEPhosphoserine
Modified residue (large scale data)207PRIDEPhosphoserine
Modified residue (large scale data)210PRIDEPhosphoserine
Cross-link214UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link219UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate
Cross-link219UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate
Modified residue (large scale data)285PRIDEPhosphoserine
Modified residue (large scale data)286PRIDEPhosphoserine
Modified residue301UniProtPhosphoserine
Modified residue (large scale data)301PRIDEPhosphoserine
Cross-link306UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link314UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link326UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link332UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link337UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link350UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue (large scale data)352PRIDEPhosphoserine
Modified residue353UniProtPhosphoserine
Modified residue (large scale data)353PRIDEPhosphoserine
Cross-link360UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link394UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link401UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link406UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link412UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link419UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link424UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link434UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link448UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue (large scale data)461PRIDEPhosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed in bladder stomach, thyroid, spinal cord, lymph node, trachea, adrenal gland, bone marrow and muscle.

Induction

Up-regulated by PHA or TPA.

Gene expression databases

Organism-specific databases

Interaction

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).

Binary interactions

Complex viewer

View interactors in UniProtKB
View CPX-6404 in Complex Portal

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for domain, region, compositional bias.

Type
IDPosition(s)Description
Domain73-136bZIP
Region79-95Basic motif
Region99-106Leucine-zipper
Compositional bias189-214Polar residues
Region189-237Disordered
Compositional bias258-279Polar residues
Region258-302Disordered
Compositional bias280-294Basic and acidic residues
Region299-363Necessary for transcriptional repression and sufficient for interaction with DR1

Sequence similarities

Belongs to the bZIP family. NFIL3 subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    462
  • Mass (Da)
    51,472
  • Last updated
    2007-06-26 v2
  • MD5 Checksum
    0D8193908B054B8C9FB18BD0930426B1
MQLRKMQTVKKEQASLDASSNVDKMMVLNSALTEVSEDSTTGEELLLSEGSVGKNKSSACRRKREFIPDEKKDAMYWEKRRKNNEAAKRSREKRRLNDLVLENKLIALGEENATLKAELLSLKLKFGLISSTAYAQEIQKLSNSTAVYFQDYQTSKSNVSSFVDEHEPSMVSSSCISVIKHSPQSSLSDVSEVSSVEHTQESSVQGSCRSPENKFQIIKQEPMELESYTREPRDDRGSYTASIYQNYMGNSFSGYSHSPPLLQVNRSSSNSPRTSETDDGVVGKSSDGEDEQQVPKGPIHSPVELKHVHATVVKVPEVNSSALPHKLRIKAKAMQIKVEAFDNEFEATQKLSSPIDMTSKRHFELEKHSAPSMVHSSLTPFSVQVTNIQDWSLKSEHWHQKELSGKTQNSFKTGVVEMKDSGYKVSDPENLYLKQGIANLSAEVVSLKRLIATQPISASDSG

Features

Showing features for sequence conflict, compositional bias.

Type
IDPosition(s)Description
Sequence conflict44-45in Ref. 1; AAA93067/CAA45597 and 2; AAB35410
Sequence conflict149in Ref. 4; CAG46846
Compositional bias189-214Polar residues
Compositional bias258-279Polar residues
Sequence conflict273in Ref. 1; AAA93067/CAA45597 and 2; AAB35410
Compositional bias280-294Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U26173
EMBL· GenBank· DDBJ
AAA93067.1
EMBL· GenBank· DDBJ
mRNA
X64318
EMBL· GenBank· DDBJ
CAA45597.1
EMBL· GenBank· DDBJ
mRNA
S79880
EMBL· GenBank· DDBJ
AAB35410.1
EMBL· GenBank· DDBJ
mRNA
EF028070
EMBL· GenBank· DDBJ
ABK15691.1
EMBL· GenBank· DDBJ
Genomic DNA
CR542049
EMBL· GenBank· DDBJ
CAG46846.1
EMBL· GenBank· DDBJ
mRNA
AK313970
EMBL· GenBank· DDBJ
BAG36685.1
EMBL· GenBank· DDBJ
mRNA
AL353764
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
CH471089
EMBL· GenBank· DDBJ
EAW62796.1
EMBL· GenBank· DDBJ
Genomic DNA
BC008197
EMBL· GenBank· DDBJ
AAH08197.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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