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Q12906 (ILF3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 160. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Interleukin enhancer-binding factor 3
Alternative name(s):
Double-stranded RNA-binding protein 76
Short name=DRBP76
M-phase phosphoprotein 4
Short name=MPP4
Nuclear factor associated with dsRNA
Short name=NFAR
Nuclear factor of activated T-cells 90 kDa
Short name=NF-AT-90
Translational control protein 80
Short name=TCP80
Gene names
Name:ILF3
Synonyms:DRBF, MPHOSPH4, NF90
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length894 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May facilitate double-stranded RNA-regulated gene expression at the level of post-transcription. Can act as a translation inhibitory protein which binds to coding sequences of acid beta-glucosidase (GCase) and other mRNAs and functions at the initiation phase of GCase mRNA translation, probably by inhibiting its binding to polysomes. Can regulate protein arginine N-methyltransferase 1 activity. May regulate transcription of the IL2 gene during T-cell activation. Can promote the formation of stable DNA-dependent protein kinase holoenzyme complexes on DNA. The phosphorylated form at Thr-188 and Thr-315, in concert with EIF2AK2/PKR can inhibit vesicular stomatitis virus (VSV) replication By similarity. Ref.1 Ref.12

Subunit structure

Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with FUS and SMN proteins and with PRMT1. Forms a complex with ILF2. Can also bind to PRKDC/XRCC7: this may stabilize the interaction of PRKDC/XRCC7 and the heterodimeric complex of XRCC6/KU70 and XRCC5/KU80. Forms a heteromeric complex with ZNF346 and ILF3. Found in a nuclear export complex with XPO5, ILF3, Ran and double-stranded RNA or double-stranded minihelix VA1 RNA. Found in a nuclear export complex with XPO5, RAN, ILF3, ZNF346 and double-stranded RNA. Interacts with XPO5 and ZNF346. Forms a complex with ILF2, YLPM1, KHDRBS1, RBMX, NCOA5 and PPP1CA. Interacts with AGO1 and AGO2. Ref.12 Ref.15 Ref.16 Ref.17 Ref.19 Ref.20 Ref.21 Ref.24 Ref.25 Ref.26 Ref.29

Subcellular location

Nucleusnucleolus. Cytoplasm. Nucleus. Note: Localizes in the cytoplasm in response to viral dsRNA. The unphosphorylated form is retained in the nucleus by ILF2. Phosphorylation at Thr-188 and Thr-315 causes the dissociation of ILF2 from the ILF2-ILF3 complex resulting in a cytoplasmic sequestration of ILF3. Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Ref.18 Ref.26 Ref.32

Tissue specificity

Ubiquitous.

Post-translational modification

Phosphorylated at Thr-188 and Thr-315 by PKR in response to certain RNA viruses. This phosphorylation results in the dissociation of ILF2 from the ILF2-ILF3 complex resulting in a cytoplasmic sequestration of ILF3 where it can bind to viral RNAs and impede viral replication. Ref.32

Methylated by protein arginine N-methyltransferase 1.

Arg-609 is dimethylated, probably to asymmetric dimethylarginine.

Sequence similarities

Contains 2 DRBM (double-stranded RNA-binding) domains.

Contains 1 DZF domain.

Sequence caution

The sequence AAA20994.1 differs from that shown. Reason: Sequencing errors.

The sequence AAH48314.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Ontologies

Keywords
   Biological processAntiviral defense
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   LigandDNA-binding
RNA-binding
   PTMAcetylation
Methylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processM phase

Non-traceable author statement Ref.11. Source: UniProtKB

defense response to virus

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of transcription, DNA-templated

Inferred from direct assay Ref.19. Source: UniProtKB

negative regulation of translation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of viral genome replication

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay Ref.19. Source: UniProtKB

protein phosphorylation

Inferred from direct assay Ref.32. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from direct assay Ref.32. Source: UniProtKB

mitochondrion

Inferred from direct assay. Source: HPA

nucleolus

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay Ref.19Ref.32. Source: UniProtKB

ribonucleoprotein complex

Inferred from direct assay Ref.26. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from direct assay Ref.15Ref.1. Source: UniProtKB

RNA binding

Non-traceable author statement Ref.2. Source: UniProtKB

double-stranded RNA binding

Inferred from direct assay Ref.15. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.15Ref.19Ref.25Ref.12. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PRMT1Q998732EBI-78756,EBI-78738

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q12906-1)

Also known as: NFAR-2; ILF3-E;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q12906-2)

Also known as: NFAR-1; DRBP76;

The sequence of this isoform differs from the canonical sequence as follows:
     688-702: QFYSNGGHSGNASGG → DFFTDCYGYHDFGSS
     703-894: Missing.
Isoform 3 (identifier: Q12906-3)

The sequence of this isoform differs from the canonical sequence as follows:
     690-764: YSNGGHSGNA...QQQSYNQSPY → SRPPPPSRPR...LRVSGNSVCL
     765-894: Missing.
Note: Dubious isoform produced through aberrant splice sites.
Isoform 4 (identifier: Q12906-4)

Also known as: DRBP76 Alpha; ILF3-A;

The sequence of this isoform differs from the canonical sequence as follows:
     516-516: E → ENVKQ
     688-694: QFYSNGG → KCAFLSV
     695-894: Missing.
Note: Contains a phosphoserine at position 482.
Isoform 5 (identifier: Q12906-5)

Also known as: DRBP76 Delta; Gamma; ILF3-C;

The sequence of this isoform differs from the canonical sequence as follows:
     687-690: SQFY → TGFV
     691-894: Missing.
Isoform 6 (identifier: Q12906-6)

The sequence of this isoform differs from the canonical sequence as follows:
     516-516: E → ENVKQ
     688-702: QFYSNGGHSGNASGG → DFFTDCYGYHDFGSS
     703-894: Missing.
Note: Contains a phosphoserine at position 482.
Isoform 7 (identifier: Q12906-7)

The sequence of this isoform differs from the canonical sequence as follows:
     516-516: E → ENVKQ
Note: Gene prediction based on EST data. Contains a phosphoserine at position 482.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 894894Interleukin enhancer-binding factor 3
PRO_0000126070

Regions

Domain5 – 378374DZF
Domain398 – 46770DRBM 1
Domain524 – 59067DRBM 2
Region609 – 894286Interaction with PRMT1
Motif371 – 38919Bipartite nuclear localization signal Potential
Compositional bias385 – 3895Poly-Lys
Compositional bias634 – 6374Poly-Pro
Compositional bias640 – 65920Arg/Gly-rich
Compositional bias701 – 7099Poly-Gly
Compositional bias794 – 7985Poly-Gly

Amino acid modifications

Modified residue621Phosphoserine Ref.33 Ref.35
Modified residue1001N6-acetyllysine Ref.31
Modified residue1881Phosphothreonine; by PKR Ref.32
Modified residue1901Phosphoserine Ref.27 Ref.33 Ref.35
Modified residue3151Phosphothreonine; by PKR Ref.32
Modified residue3821Phosphoserine Ref.33 Ref.35
Modified residue3841Phosphoserine Ref.33
Modified residue4601N6-acetyllysine Ref.31
Modified residue4761Phosphoserine Ref.35
Modified residue4821Phosphoserine Ref.22 Ref.27 Ref.30 Ref.33 Ref.35
Modified residue5921Phosphothreonine Ref.22 Ref.23 Ref.30 Ref.33 Ref.35
Modified residue7921Phosphoserine Ref.27 Ref.30 Ref.35
Modified residue8121Phosphoserine Ref.27 Ref.33 Ref.35

Natural variations

Alternative sequence5161E → ENVKQ in isoform 4, isoform 6 and isoform 7.
VSP_003883
Alternative sequence687 – 6904SQFY → TGFV in isoform 5.
VSP_003886
Alternative sequence688 – 70215QFYSN…NASGG → DFFTDCYGYHDFGSS in isoform 2 and isoform 6.
VSP_003888
Alternative sequence688 – 6947QFYSNGG → KCAFLSV in isoform 4.
VSP_003884
Alternative sequence690 – 76475YSNGG…NQSPY → SRPPPPSRPRCCVVRCSGSP CGPSCDPYLAVFGTPCLQWF VSCHYNFVWVEFLSFCSSVS LCLFTLRVSGNSVCL in isoform 3.
VSP_003890
Alternative sequence691 – 894204Missing in isoform 5.
VSP_003887
Alternative sequence695 – 894200Missing in isoform 4.
VSP_003885
Alternative sequence703 – 894192Missing in isoform 2 and isoform 6.
VSP_003889
Alternative sequence765 – 894130Missing in isoform 3.
VSP_003891
Natural variant501D → H. Ref.6
Corresponds to variant rs1064493 [ dbSNP | Ensembl ].
VAR_022159
Natural variant5011A → S.
Corresponds to variant rs34520379 [ dbSNP | Ensembl ].
VAR_048906

Experimental info

Sequence conflict1011G → C in AAD51098. Ref.5
Sequence conflict1011G → C in AAD51099. Ref.5
Sequence conflict1011G → C in AAK07424. Ref.6
Sequence conflict1011G → C in AAK07425. Ref.6
Sequence conflict2601G → V in AAD33966. Ref.2
Sequence conflict2601G → V in CAA66918. Ref.11
Sequence conflict6471S → T in AAD33966. Ref.2
Sequence conflict6471S → T in AAK07424. Ref.6
Sequence conflict6471S → T in AAK07425. Ref.6
Sequence conflict688 – 6892QF → N in AAF82687. Ref.13
Sequence conflict7631P → L in CAC01407. Ref.4
Sequence conflict7971G → R in CAC01124. Ref.4
Sequence conflict7971G → R in AAK07425. Ref.6
Sequence conflict7991S → SGS in AAF82685. Ref.13
Sequence conflict8131G → E in AAK07425. Ref.6

Secondary structure

.......... 894
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (NFAR-2) (ILF3-E) [UniParc].

Last modified April 12, 2005. Version 3.
Checksum: 20903ABD0331F370

FASTA89495,338
        10         20         30         40         50         60 
MRPMRIFVND DRHVMAKHSS VYPTQEELEA VQNMVSHTER ALKAVSDWID EQEKGSSEQA 

        70         80         90        100        110        120 
ESDNMDVPPE DDSKEGAGEQ KTEHMTRTLR GVMRVGLVAK GLLLKGDLDL ELVLLCKEKP 

       130        140        150        160        170        180 
TTALLDKVAD NLAIQLAAVT EDKYEILQSV DDAAIVIKNT KEPPLSLTIH LTSPVVREEM 

       190        200        210        220        230        240 
EKVLAGETLS VNDPPDVLDR QKCLAALASL RHAKWFQARA NGLKSCVIVI RVLRDLCTRV 

       250        260        270        280        290        300 
PTWGPLRGWP LELLCEKSIG TANRPMGAGE ALRRVLECLA SGIVMPDGSG IYDPCEKEAT 

       310        320        330        340        350        360 
DAIGHLDRQQ REDITQSAQH ALRLAAFGQL HKVLGMDPLP SKMPKKPKNE NPVDYTVQIP 

       370        380        390        400        410        420 
PSTTYAITPM KRPMEEDGEE KSPSKKKKKI QKKEEKAEPP QAMNALMRLN QLKPGLQYKL 

       430        440        450        460        470        480 
VSQTGPVHAP IFTMSVEVDG NSFEASGPSK KTAKLHVAVK VLQDMGLPTG AEGRDSSKGE 

       490        500        510        520        530        540 
DSAEETEAKP AVVAPAPVVE AVSTPSAAFP SDATAEQGPI LTKHGKNPVM ELNEKRRGLK 

       550        560        570        580        590        600 
YELISETGGS HDKRFVMEVE VDGQKFQGAG SNKKVAKAYA ALAALEKLFP DTPLALDANK 

       610        620        630        640        650        660 
KKRAPVPVRG GPKFAAKPHN PGFGMGGPMH NEVPPPPNLR GRGRGGSIRG RGRGRGFGGA 

       670        680        690        700        710        720 
NHGGYMNAGA GYGSYGYGGN SATAGYSQFY SNGGHSGNAS GGGGGGGGGS SGYGSYYQGD 

       730        740        750        760        770        780 
NYNSPVPPKH AGKKQPHGGQ QKPSYGSGYQ SHQGQQQSYN QSPYSNYGPP QGKQKGYNHG 

       790        800        810        820        830        840 
QGSYSYSNSY NSPGGGGGSD YNYESKFNYS GSGGRSGGNS YGSGGASYNP GSHGGYGGGS 

       850        860        870        880        890 
GGGSSYQGKQ GGYSQSNYNS PGSGQNYSGP PSSYQSSQGG YGRNADHSMN YQYR 

« Hide

Isoform 2 (NFAR-1) (DRBP76) [UniParc].

Checksum: 3DDE63929988DED4
Show »

FASTA70276,033
Isoform 3 [UniParc].

Checksum: 3C7C7565F5980B1E
Show »

FASTA76482,802
Isoform 4 (DRBP76 Alpha) (ILF3-A) [UniParc].

Checksum: F4ECBD8A7C428905
Show »

FASTA69875,508
Isoform 5 (DRBP76 Delta) (Gamma) (ILF3-C) [UniParc].

Checksum: 8DEC4DC15E80A8C5
Show »

FASTA69074,607
Isoform 6 [UniParc].

Checksum: BC0B5D61BC51129C
Show »

FASTA70676,502
Isoform 7 [UniParc].

Checksum: 83A1755F05408949
Show »

FASTA89895,808

References

« Hide 'large scale' references
[1]"Cloning and expression of cyclosporin A- and FK506-sensitive nuclear factor of activated T-cells: NF45 and NF90."
Kao P.N., Chen L., Brock G., Ng J., Kenny J., Smith A.J., Corthesy B.
J. Biol. Chem. 269:20691-20699(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-41; 491-510 AND 555-565, FUNCTION.
Tissue: T-cell lymphoma.
[2]"DRBP76, a double-stranded RNA-binding nuclear protein, is phosphorylated by the interferon-induced protein kinase, PKR."
Patel R.C., Vestal D.J., Xu Z., Bandyopadhyay S., Guo W., Erme S.M., Williams B.R., Sen G.C.
J. Biol. Chem. 274:20432-20437(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF N-TERMINUS.
Tissue: Cervix carcinoma.
[3]"Molecular cloning and characterization of a translational inhibitory protein that binds to coding sequences of human acid beta-glucosidase and other mRNAs."
Xu Y.-H., Grabowski G.A.
Mol. Genet. Metab. 68:441-454(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), CHARACTERIZATION.
Tissue: Liver.
[4]"Alternative splicing in the human interleukin enhancer binding factor 3 (ILF3) gene."
Duchange N., Pidoux J., Camus E., Sauvaget D.
Gene 261:345-353(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2; 4 AND 5), ALTERNATIVE SPLICING.
Tissue: Melanoma.
[5]"Characterization of two evolutionarily conserved, alternatively spliced nuclear phosphoproteins, NFAR-1 and -2, that function in mRNA processing and interact with the double-stranded RNA-dependent protein kinase, PKR."
Saunders L.R., Perkins D.J., Balachandran S., Michaels R., Ford R., Mayeda A., Barber G.N.
J. Biol. Chem. 276:32300-32312(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), CHARACTERIZATION.
[6]"The 90- and 110-kDa human NFAR proteins are translated from two differentially spliced mRNAs encoded on chromosome 19p13."
Saunders L.R., Jurecic V., Barber G.N.
Genomics 71:256-259(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), VARIANT HIS-50.
Tissue: T-cell.
[7]"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] (ISOFORM 6).
Tissue: Placenta.
[8]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]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].
[10]"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] (ISOFORM 6).
Tissue: Duodenum and Uterus.
[11]"Identification of novel M phase phosphoproteins by expression cloning."
Matsumoto-Taniura N., Pirollet F., Monroe R., Gerace L., Westendorf J.M.
Mol. Biol. Cell 7:1455-1469(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-611.
Tissue: Blood and Cervix.
[12]"DNA-dependent protein kinase interacts with antigen receptor response element binding proteins NF90 and NF45."
Ting N.S.Y., Kao P.N., Chan D.W., Lintott L.G., Lees-Miller S.P.
J. Biol. Chem. 273:2136-2145(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-10, FUNCTION, INTERACTION WITH XRCC6; PRKDC AND XRCC5.
[13]"Structure and functional characterization of hDRBF gene."
MacArdle J., Cantarella G.M., Veyrune J.-L., Krasnoselskaya I., Kumar A.
Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 188-894 (ISOFORMS 1; 2 AND 3).
[14]Yu W., Sarginson J., Gibbs R.A.
Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 587-894 (ISOFORM 1).
Tissue: Brain.
[15]"Autoantibodies define a family of proteins with conserved double-stranded RNA-binding domains as well as DNA binding activity."
Satoh M., Shaheen V.M., Kao P.N., Okano T., Shaw M., Yoshida H., Richards H.B., Reeves W.H.
J. Biol. Chem. 274:34598-34604(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ILF2.
[16]"Protein-arginine methyltransferase I, the predominant protein-arginine methyltransferase in cells, interacts with and is regulated by interleukin enhancer-binding factor 3."
Tang J., Kao P.N., Herschman H.R.
J. Biol. Chem. 275:19866-19876(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PRMT1.
[17]"Exportin-5, a novel karyopherin, mediates nuclear export of double-stranded RNA binding proteins."
Brownawell A.M., Macara I.G.
J. Cell Biol. 156:53-64(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH XPO5; RAN AND DOUBLE-STRANDED RNA, INTERACTION WITH XPO5.
[18]"Functional proteomic analysis of human nucleolus."
Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., Greco A., Hochstrasser D.F., Diaz J.-J.
Mol. Biol. Cell 13:4100-4109(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"The RNA binding protein nuclear factor 90 functions as both a positive and negative regulator of gene expression in mammalian cells."
Reichman T.W., Muniz L.C., Mathews M.B.
Mol. Cell. Biol. 22:343-356(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ILF2.
[20]"Minihelix-containing RNAs mediate exportin-5-dependent nuclear export of the double-stranded RNA-binding protein ILF3."
Gwizdek C., Ossareh-Nazari B., Brownawell A.M., Evers S., Macara I.G., Dargemont C.
J. Biol. Chem. 279:884-891(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH XPO5; RAN AND VA1 RNA.
[21]"Nucleocytoplasmic shuttling of JAZ, a new cargo protein for exportin-5."
Chen T., Brownawell A.M., Macara I.G.
Mol. Cell. Biol. 24:6608-6619(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH XPO5; RAN; ZNF346 AND DOUBLE-STRANDED RNA, INTERACTION WITH XPO5 AND ZNF346.
[22]"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-482 AND THR-592, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[23]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-592, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[24]"The nuclear PP1 interacting protein ZAP3 (ZAP) is a putative nucleoside kinase that complexes with SAM68, CIA, NF110/45, and HNRNP-G."
Ulke-Lemee A., Trinkle-Mulcahy L., Chaulk S., Bernstein N.K., Morrice N., Glover M., Lamond A.I., Moorhead G.B.G.
Biochim. Biophys. Acta 1774:1339-1350(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH ILF2; YLPM1; KHDRBS1; RBMX; NCOA5 AND PPP1CA.
[25]"Proteomic and functional analysis of Argonaute-containing mRNA-protein complexes in human cells."
Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M., Urlaub H., Meister G.
EMBO Rep. 8:1052-1060(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AGO1 AND AGO2.
[26]"Molecular composition of IMP1 ribonucleoprotein granules."
Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R., Johnsen A.H., Christiansen J., Nielsen F.C.
Mol. Cell. Proteomics 6:798-811(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
[27]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190; SER-792 AND SER-812, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-482 (ISOFORMS 4; 6 AND 7), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[28]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[29]"Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic RNPs."
Weidensdorfer D., Stoehr N., Baude A., Lederer M., Koehn M., Schierhorn A., Buchmeier S., Wahle E., Huettelmaiery S.
RNA 15:104-115(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A MRNP COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[30]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-592 AND SER-792, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-482 (ISOFORMS 4; 6 AND 7), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[31]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-100 AND LYS-460, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[32]"Phosphorylation of the NFAR proteins by the dsRNA-dependent protein kinase PKR constitutes a novel mechanism of translational regulation and cellular defense."
Harashima A., Guettouche T., Barber G.N.
Genes Dev. 24:2640-2653(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-188 AND THR-315.
[33]"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-62; SER-190; SER-382; SER-384; SER-482; THR-592 AND SER-812, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[34]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[35]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62; SER-190; SER-382; SER-476; SER-482; THR-592; SER-792 AND SER-812, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[36]"Crystal structure of DRBM 2 domain of interleukin enhancer-binding factor 3 from Homo sapiens, Northeast structural genomics consortium target HR4527E."
Northeast structural genomics consortium (NESG)
Submitted (DEC-2010) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 520-594.
[37]"Northeast structural genomics consortium target HR4527E."
Northeast structural genomics consortium (NESG)
Submitted (SEP-2010) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 521-600.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U10324 mRNA. Translation: AAA20994.1. Sequence problems.
AF147209 mRNA. Translation: AAD33966.1.
AF141870 mRNA. Translation: AAD37575.1.
AJ271741 Genomic DNA. Translation: CAC01121.1.
AJ271741 Genomic DNA. Translation: CAC01122.1.
AJ271741 Genomic DNA. Translation: CAC01123.1.
AJ271741 Genomic DNA. Translation: CAC01124.1.
AJ271744 mRNA. Translation: CAC01404.1.
AJ271745 mRNA. Translation: CAC01405.1.
AJ271746 mRNA. Translation: CAC01406.1.
AJ271747 mRNA. Translation: CAC01407.1.
AF167569 mRNA. Translation: AAD51098.1.
AF167570 mRNA. Translation: AAD51099.1.
AF320244 expand/collapse EMBL AC list , AF320228, AF320229, AF320230, AF320231, AF320232, AF320233, AF320234, AF320235, AF320236, AF320237, AF320238, AF320239, AF320240, AF320241, AF320242, AF320243 Genomic DNA. Translation: AAK07424.1.
AF320247 expand/collapse EMBL AC list , AF320228, AF320229, AF320230, AF320231, AF320232, AF320233, AF320234, AF320235, AF320236, AF320237, AF320238, AF320239, AF320240, AF320241, AF320242, AF320243, AF320245, AF320246 Genomic DNA. Translation: AAK07425.1.
AK291617 mRNA. Translation: BAF84306.1.
AC011475 Genomic DNA. No translation available.
CH471106 Genomic DNA. Translation: EAW84132.1.
BC048314 mRNA. Translation: AAH48314.1. Sequence problems.
BC064836 mRNA. Translation: AAH64836.1.
X98264 mRNA. Translation: CAA66917.1.
X98265 mRNA. Translation: CAA66918.1.
AF202445 Genomic DNA. Translation: AAF82685.1.
AF202445 Genomic DNA. Translation: AAF82686.1.
AF202445 Genomic DNA. Translation: AAF82687.1.
AF007140 mRNA. Translation: AAC19152.1.
CCDSCCDS12246.1. [Q12906-1]
CCDS12247.1. [Q12906-2]
CCDS45965.1. [Q12906-7]
CCDS45966.1. [Q12906-5]
CCDS45967.1. [Q12906-6]
PIRB54857.
RefSeqNP_001131145.1. NM_001137673.1. [Q12906-6]
NP_004507.2. NM_004516.3. [Q12906-2]
NP_036350.2. NM_012218.3. [Q12906-1]
NP_060090.2. NM_017620.2. [Q12906-7]
NP_703194.1. NM_153464.2. [Q12906-5]
UniGeneHs.465885.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2L33NMR-A521-600[»]
3P1XX-ray1.90A/B520-594[»]
ProteinModelPortalQ12906.
SMRQ12906. Positions 6-374, 399-594.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109822. 313 interactions.
DIPDIP-29853N.
IntActQ12906. 55 interactions.
MINTMINT-4999319.

PTM databases

PhosphoSiteQ12906.

Polymorphism databases

DMDM62512150.

2D gel databases

SWISS-2DPAGEQ12906.

Proteomic databases

MaxQBQ12906.
PaxDbQ12906.
PRIDEQ12906.

Protocols and materials databases

DNASU3609.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000250241; ENSP00000250241; ENSG00000129351. [Q12906-5]
ENST00000318511; ENSP00000315205; ENSG00000129351. [Q12906-1]
ENST00000407004; ENSP00000384660; ENSG00000129351. [Q12906-6]
ENST00000420083; ENSP00000405436; ENSG00000129351. [Q12906-5]
ENST00000449870; ENSP00000404121; ENSG00000129351. [Q12906-7]
ENST00000588657; ENSP00000468181; ENSG00000129351. [Q12906-7]
ENST00000589998; ENSP00000465219; ENSG00000129351. [Q12906-2]
ENST00000590261; ENSP00000468156; ENSG00000129351. [Q12906-1]
ENST00000592763; ENSP00000465515; ENSG00000129351. [Q12906-4]
GeneID3609.
KEGGhsa:3609.
UCSCuc002mpk.2. human. [Q12906-5]
uc002mpl.2. human. [Q12906-2]
uc002mpm.2. human. [Q12906-6]
uc002mpn.3. human. [Q12906-1]
uc002mpo.3. human.
uc002mpp.3. human. [Q12906-4]

Organism-specific databases

CTD3609.
GeneCardsGC19P010764.
H-InvDBHIX0014753.
HGNCHGNC:6038. ILF3.
HPAHPA001897.
MIM603182. gene.
neXtProtNX_Q12906.
PharmGKBPA29853.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG307678.
HOVERGENHBG069915.
InParanoidQ12906.
KOK13090.
OMAPPKHAGK.
OrthoDBEOG72ZCDC.
PhylomeDBQ12906.
TreeFamTF320194.

Gene expression databases

ArrayExpressQ12906.
BgeeQ12906.
GenevestigatorQ12906.

Family and domain databases

Gene3D3.30.160.20. 2 hits.
InterProIPR014720. dsRNA-bd_dom.
IPR006561. DZF.
[Graphical view]
PfamPF00035. dsrm. 2 hits.
PF07528. DZF. 1 hit.
[Graphical view]
SMARTSM00358. DSRM. 2 hits.
SM00572. DZF. 1 hit.
[Graphical view]
PROSITEPS50137. DS_RBD. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSILF3. human.
EvolutionaryTraceQ12906.
GeneWikiILF3.
GenomeRNAi3609.
NextBio14109.
PMAP-CutDBQ12906.
PROQ12906.
SOURCESearch...

Entry information

Entry nameILF3_HUMAN
AccessionPrimary (citable) accession number: Q12906
Secondary accession number(s): A8K6F2 expand/collapse secondary AC list , G5E9M5, O43409, Q6P1X1, Q86XY7, Q99544, Q99545, Q9BZH4, Q9BZH5, Q9NQ95, Q9NQ96, Q9NQ97, Q9NQ98, Q9NQ99, Q9NQA0, Q9NQA1, Q9NQA2, Q9NRN2, Q9NRN3, Q9NRN4, Q9UMZ9, Q9UN00, Q9UN84, Q9UNA2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: April 12, 2005
Last modified: July 9, 2014
This is version 160 of the entry and version 3 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM