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Q16649 (NFIL3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nuclear factor interleukin-3-regulated protein
Alternative name(s):
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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length462 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.1 Ref.2 Ref.9

Subunit structure

Homodimer. Binds DNA as a dimer. Interacts with DR1. Interacts with PER2 and CRY2 By similarity. Ref.1 Ref.9

Subcellular location

Nucleus By similarity.

Tissue specificity

Expressed in bladder stomach, thyroid, spinal cord, lymph node, trachea, adrenal gland, bone marrow and muscle. Ref.10

Induction

Up-regulated by PHA or TPA. Ref.2

Sequence similarities

Belongs to the bZIP family. NFIL3 subfamily.

Contains 1 bZIP (basic-leucine zipper) domain.

Ontologies

Keywords
   Biological processBiological rhythms
Transcription
Transcription regulation
   Cellular componentNucleus
   LigandDNA-binding
   Molecular functionActivator
Repressor
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to interleukin-4

Inferred from electronic annotation. Source: Ensembl

circadian rhythm

Inferred from electronic annotation. Source: InterPro

immune response

Traceable author statement Ref.2. Source: ProtInc

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 20093779. Source: BHF-UCL

positive regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

transcription from RNA polymerase II promoter

Traceable author statement Ref.2. Source: ProtInc

   Cellular_componentnucleus

Traceable author statement Ref.2. Source: ProtInc

   Molecular_functionDNA binding

Traceable author statement Ref.1. Source: ProtInc

RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription

Inferred from direct assay PubMed 20093779. Source: BHF-UCL

RNA polymerase II core promoter sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

RNA polymerase II regulatory region sequence-specific DNA binding

Inferred from direct assay PubMed 20093779. Source: BHF-UCL

sequence-specific DNA binding transcription factor activity

Traceable author statement Ref.2. Source: ProtInc

transcription corepressor activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 462462Nuclear factor interleukin-3-regulated protein
PRO_0000292667

Regions

Domain73 – 13664bZIP
Region79 – 9517Basic motif By similarity
Region99 – 1068Leucine-zipper By similarity
Region299 – 36365Necessary for transcriptional repression and sufficient for interaction with DR1
Compositional bias155 – 21056Ser-rich

Amino acid modifications

Modified residue3011Phosphoserine Ref.11 Ref.14
Modified residue3531Phosphoserine Ref.14

Experimental info

Mutagenesis3301K → A: Interacts with DR1 and partially affects transcriptional repression; when associated with E-332. Ref.9
Mutagenesis3301K → E: Does not interact with DR1 and drastically affects transcriptional repression; when associated with E-332. Ref.9
Mutagenesis3321K → A: Interacts with DR1 and partially affects transcriptional repression; when associated with E-330. Ref.9
Mutagenesis3321K → E: Does not interact with DR1 and drastically affects transcriptional repression; when associated with E-330. Ref.9
Sequence conflict44 – 452EL → DV in AAA93067. Ref.1
Sequence conflict44 – 452EL → DV in CAA45597. Ref.1
Sequence conflict44 – 452EL → DV in AAB35410. Ref.2
Sequence conflict1491F → S in CAG46846. Ref.4
Sequence conflict2731R → G in AAA93067. Ref.1
Sequence conflict2731R → G in CAA45597. Ref.1
Sequence conflict2731R → G in AAB35410. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q16649 [UniParc].

Last modified June 26, 2007. Version 2.
Checksum: D19946AAC774C3E7

FASTA46251,472
        10         20         30         40         50         60 
MQLRKMQTVK KEQASLDASS NVDKMMVLNS ALTEVSEDST TGEELLLSEG SVGKNKSSAC 

        70         80         90        100        110        120 
RRKREFIPDE KKDAMYWEKR RKNNEAAKRS REKRRLNDLV LENKLIALGE ENATLKAELL 

       130        140        150        160        170        180 
SLKLKFGLIS STAYAQEIQK LSNSTAVYFQ DYQTSKSNVS SFVDEHEPSM VSSSCISVIK 

       190        200        210        220        230        240 
HSPQSSLSDV SEVSSVEHTQ ESSVQGSCRS PENKFQIIKQ EPMELESYTR EPRDDRGSYT 

       250        260        270        280        290        300 
ASIYQNYMGN SFSGYSHSPP LLQVNRSSSN SPRTSETDDG VVGKSSDGED EQQVPKGPIH 

       310        320        330        340        350        360 
SPVELKHVHA TVVKVPEVNS SALPHKLRIK AKAMQIKVEA FDNEFEATQK LSSPIDMTSK 

       370        380        390        400        410        420 
RHFELEKHSA PSMVHSSLTP FSVQVTNIQD WSLKSEHWHQ KELSGKTQNS FKTGVVEMKD 

       430        440        450        460 
SGYKVSDPEN LYLKQGIANL SAEVVSLKRL IATQPISASD SG 

« Hide

References

« Hide 'large scale' references
[1]"Transcriptional repression by a novel member of the bZIP family of transcription factors."
Cowell I.G., Skinner A., Hurst H.C.
Mol. Cell. Biol. 12:3070-3077(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, DNA-BINDING.
Tissue: Placenta.
[2]"Molecular cloning and characterization of NF-IL3A, a transcriptional activator of the human interleukin-3 promoter."
Zhang W., Zhang J., Kornuc M., Kwan K., Frank R., Nimer S.D.
Mol. Cell. Biol. 15:6055-6063(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, DNA-BINDING.
Tissue: T-cell.
[3]NHLBI resequencing and genotyping service (RS&G)
Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Liver.
[6]"DNA sequence and analysis of human chromosome 9."
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. expand/collapse author list , 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.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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].
Tissue: Placenta.
[9]"Protein-protein interaction between the transcriptional repressor E4BP4 and the TBP-binding protein Dr1."
Cowell I.G., Hurst H.C.
Nucleic Acids Res. 24:3607-3613(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH DR1, MUTAGENESIS OF LYS-330 AND LYS-332.
[10]"Exclusion of NFIL3 as the gene causing hereditary sensory neuropathy type I by mutation analysis."
Hulme D.J., Blair I.P., Dawkins J.L., Nicholson G.A.
Hum. Genet. 106:594-596(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[11]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[14]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
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.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301 AND SER-353, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U26173 mRNA. Translation: AAA93067.1.
X64318 mRNA. Translation: CAA45597.1.
S79880 mRNA. Translation: AAB35410.1.
EF028070 Genomic DNA. Translation: ABK15691.1.
CR542049 mRNA. Translation: CAG46846.1.
AK313970 mRNA. Translation: BAG36685.1.
AL353764 Genomic DNA. Translation: CAH73854.1.
CH471089 Genomic DNA. Translation: EAW62796.1.
BC008197 mRNA. Translation: AAH08197.1.
PIRG01804.
RefSeqNP_005375.2. NM_005384.2.
UniGeneHs.79334.

3D structure databases

ProteinModelPortalQ16649.
SMRQ16649. Positions 79-123.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110855. 9 interactions.
IntActQ16649. 5 interactions.
MINTMINT-268122.
STRING9606.ENSP00000297689.

PTM databases

PhosphoSiteQ16649.

Polymorphism databases

DMDM150385077.

Proteomic databases

PaxDbQ16649.
PRIDEQ16649.

Protocols and materials databases

DNASU4783.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000297689; ENSP00000297689; ENSG00000165030.
GeneID4783.
KEGGhsa:4783.
UCSCuc004arh.3. human.

Organism-specific databases

CTD4783.
GeneCardsGC09M094171.
H-InvDBHIX0169355.
HGNCHGNC:7787. NFIL3.
HPAHPA003261.
MIM605327. gene.
neXtProtNX_Q16649.
PharmGKBPA31593.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG260819.
HOGENOMHOG000059596.
HOVERGENHBG105717.
InParanoidQ16649.
KOK09059.
OMAQTIKKEQ.
OrthoDBEOG7GQXWM.
PhylomeDBQ16649.
TreeFamTF328374.

Enzyme and pathway databases

SignaLinkQ16649.

Gene expression databases

BgeeQ16649.
CleanExHS_NFIL3.
GenevestigatorQ16649.

Family and domain databases

InterProIPR004827. bZIP.
IPR016743. TF_bZIP_E4BP4.
IPR010533. Vert_IL3-reg_TF.
[Graphical view]
PfamPF07716. bZIP_2. 1 hit.
PF06529. Vert_IL3-reg_TF. 1 hit.
[Graphical view]
PIRSFPIRSF019029. bZIP_E4BP4. 1 hit.
SMARTSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEPS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNFIL3. human.
GeneWikiNFIL3.
GenomeRNAi4783.
NextBio18446.
PROQ16649.
SOURCESearch...

Entry information

Entry nameNFIL3_HUMAN
AccessionPrimary (citable) accession number: Q16649
Secondary accession number(s): B2R9Y8 expand/collapse secondary AC list , Q14211, Q6FGQ8, Q96HS0
Entry history
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: June 26, 2007
Last modified: April 16, 2014
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM