Reviewed, UniProtKB/Swiss-Prot Q12906 (ILF3_HUMAN)

Names and origin

Protein names

Recommended name:
    Interleukin enhancer-binding factor 3
Alternative name(s):
    Nuclear factor of activated T-cells 90 kDa
      Short name=NF-AT-90
    Double-stranded RNA-binding protein 76
      Short name=DRBP76
    Translational control protein 80
      Short name=TCP80
    Nuclear factor associated with dsRNA
      Short name=NFAR
    M-phase phosphoprotein 4
      Short name=MPP4

Gene names

Name:	ILF3
Synonyms:	DRBF, MPHOSPH4, NF90

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	894 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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. Ref.1 Ref.10
Subunit structure	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 G22P1/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. Ref.10 Ref.13 Ref.14 Ref.15 Ref.17 Ref.19
Subcellular location	Nucleus › nucleolus. Ref.16
Tissue specificity	Ubiquitous.
Post-translational modification	Phosphorylated by RNA-dependent protein kinase (EIF2AK2). Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Methylated by protein arginine N-methyltransferase 1. Ref.20 Arg-609 is dimethylated, probably to asymmetric dimethylarginine. Ref.20
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: Miscellaneous discrepancy. Sequencing errors. The sequence AAH48314.1 differs from that shown. Reason: Miscellaneous discrepancy. Contaminating sequence. Potential poly-A sequence.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Ligand	DNA-binding RNA-binding
PTM	Methylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	M phase Ref.9 Non-traceable author statement. Source: UniProtKB negative regulation of transcription, DNA-dependent Ref.17 Inferred from direct assay. Source: UniProtKB positive regulation of transcription, DNA-dependent Ref.17 Inferred from direct assay. Source: UniProtKB transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrion Inferred from direct assay. Source: HPA nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	DNA binding Ref.1 Ref.13 Inferred from direct assay. Source: UniProtKB double-stranded RNA binding Ref.13 Inferred from direct assay. Source: UniProtKB protein binding Ref.10 Ref.13 Ref.14 Ref.17 Inferred from physical interaction. Source: UniProtKB transcription activator activity Ref.17 Inferred from direct assay. Source: UniProtKB transcription repressor activity Ref.17 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NDRG1	Q92597	1	EBI-288405,EBI-716486
PRMT1	Q99873	2	EBI-78756,EBI-78738

Alternative products

This entry describes 6 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.

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.

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.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 894	894	Interleukin enhancer-binding factor 3		PRO_0000126070
Regions
	Domain	94 – 342	249	DZF
	Domain	398 – 467	70	DRBM 1
	Domain	524 – 590	67	DRBM 2
	Region	609 – 894	286	Interaction with PRMT1
	Motif	371 – 389	19	Bipartite nuclear localization signal Potential
	Compositional bias	385 – 389	5	Poly-Lys
	Compositional bias	634 – 637	4	Poly-Pro
	Compositional bias	640 – 659	20	Arg/Gly-rich
	Compositional bias	701 – 709	9	Poly-Gly
	Compositional bias	794 – 798	5	Poly-Gly
Amino acid modifications
	Modified residue	62	1	Phosphoserine Ref.21
	Modified residue	190	1	Phosphoserine Ref.23 Ref.28
	Modified residue	382	1	Phosphoserine Ref.22 Ref.23 Ref.26
	Modified residue	384	1	Phosphoserine Ref.26
	Modified residue	482	1	Phosphoserine Ref.23 Ref.28
	Modified residue	486	1	Phosphothreonine Ref.27
	Modified residue	579	1	Phosphotyrosine Ref.28
	Modified residue	592	1	Phosphothreonine Ref.21 Ref.23 Ref.24 Ref.25 Ref.28
	Modified residue	609	1	Omega-N-methylated arginine Ref.20
	Modified residue	792	1	Phosphoserine Ref.28
	Modified residue	810	1	Phosphoserine Ref.28
	Modified residue	812	1	Phosphoserine Ref.25 Ref.28
Natural variations
	Alternative sequence	516	1	E → ENVKQ in isoform 4 and isoform 6.		VSP_003883
	Alternative sequence	687 – 690	4	SQFY → TGFV in isoform 5.		VSP_003886
	Alternative sequence	688 – 702	15	QFYSN…NASGG → DFFTDCYGYHDFGSS in isoform 2 and isoform 6.		VSP_003888
	Alternative sequence	688 – 694	7	QFYSNGG → KCAFLSV in isoform 4.		VSP_003884
	Alternative sequence	690 – 764	75	YSNGG…NQSPY → SRPPPPSRPRCCVVRCSGSP CGPSCDPYLAVFGTPCLQWF VSCHYNFVWVEFLSFCSSVS LCLFTLRVSGNSVCL in isoform 3.		VSP_003890
	Alternative sequence	691 – 894	204	Missing in isoform 5.		VSP_003887
	Alternative sequence	695 – 894	200	Missing in isoform 4.		VSP_003885
	Alternative sequence	703 – 894	192	Missing in isoform 2 and isoform 6.		VSP_003889
	Alternative sequence	765 – 894	130	Missing in isoform 3.		VSP_003891
	Natural variant	50	1	D → H: dbSNP rs1064493. Ref.6		VAR_022159
	Natural variant	501	1	A → S: dbSNP rs34520379.		VAR_048906
Experimental info
	Sequence conflict	101	1	G → C Ref.5
	Sequence conflict	101	1	G → C Ref.6
	Sequence conflict	260	1	G → V in AAD33966. Ref.2
	Sequence conflict	260	1	G → V in CAA66918. Ref.9
	Sequence conflict	647	1	S → T Ref.2
	Sequence conflict	647	1	S → T Ref.6
	Sequence conflict	688 – 689	2	QF → N in AAF82687. Ref.11
	Sequence conflict	763	1	P → L in CAC01407. Ref.4
	Sequence conflict	797	1	G → R in CAC01124. Ref.4
	Sequence conflict	797	1	G → R in AAK07425. Ref.6
	Sequence conflict	799	1	S → SGS in AAF82685. Ref.11
	Sequence conflict	813	1	G → E in AAK07425. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (NFAR-2) (ILF3-E) [UniParc]. Last modified April 12, 2005. Version 3. Checksum: 20903ABD0331F370	FASTA	894	95,338
	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
	Isoform 2 (NFAR-1) (DRBP76). Checksum: 3DDE63929988DED4	FASTA	702	76,033
	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 NHGGYMNAGA GYGSYGYGGN SATAGYSDFF TDCYGYHDFG SS
	Isoform 3. Checksum: 3C7C7565F5980B1E	FASTA	764	82,802
	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 SATAGYSQFS RPPPPSRPRC CVVRCSGSPC GPSCDPYLAV 730 740 750 760 FGTPCLQWFV SCHYNFVWVE FLSFCSSVSL CLFTLRVSGN SVCL
	Isoform 4 (DRBP76 Alpha) (ILF3-A). Checksum: F4ECBD8A7C428905	FASTA	698	75,508
	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 SDATAENVKQ QGPILTKHGK NPVMELNEKR 550 560 570 580 590 600 RGLKYELISE TGGSHDKRFV MEVEVDGQKF QGAGSNKKVA KAYAALAALE KLFPDTPLAL 610 620 630 640 650 660 DANKKKRAPV PVRGGPKFAA KPHNPGFGMG GPMHNEVPPP PNLRGRGRGG SIRGRGRGRG 670 680 690 FGGANHGGYM NAGAGYGSYG YGGNSATAGY SKCAFLSV
	Isoform 5 (DRBP76 Delta) (Gamma) (ILF3-C). Checksum: 8DEC4DC15E80A8C5	FASTA	690	74,607
	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 NHGGYMNAGA GYGSYGYGGN SATAGYTGFV
	Isoform 6. Checksum: BC0B5D61BC51129C	FASTA	706	76,502
	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 SDATAENVKQ QGPILTKHGK NPVMELNEKR 550 560 570 580 590 600 RGLKYELISE TGGSHDKRFV MEVEVDGQKF QGAGSNKKVA KAYAALAALE KLFPDTPLAL 610 620 630 640 650 660 DANKKKRAPV PVRGGPKFAA KPHNPGFGMG GPMHNEVPPP PNLRGRGRGG SIRGRGRGRG 670 680 690 700 FGGANHGGYM NAGAGYGSYG YGGNSATAGY SDFFTDCYGY HDFGSS

References

	« Hide 'large scale' referencesShow '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: 7519613] [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: 10400669] [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: 10607473] [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: 11167023] [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: 11438536] [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: 11161820] [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. , 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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6). Tissue: Placenta.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6). Tissue: Duodenum and Uterus.
[9]	"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: 8885239] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-611. Tissue: Blood and Cervix.
[10]	"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: 9442054] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-10, FUNCTION, INTERACTION WITH G22P1; PRKDC AND XRCC5.
[11]	"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).
[12]	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.
[13]	"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: 10574923] [Abstract] Cited for: INTERACTION WITH ILF2.
[14]	"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: 10749851] [Abstract] Cited for: INTERACTION WITH PRMT1.
[15]	"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: 11777942] [Abstract] Cited for: IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH XPO5; RAN AND DOUBLE-STRANDED RNA, INTERACTION WITH XPO5.
[16]	"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: 12429849] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[17]	"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: 11739746] [Abstract] Cited for: INTERACTION WITH ILF2.
[18]	"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: 14570900] [Abstract] Cited for: IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH XPO5; RAN AND VA1 RNA.
[19]	"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: 15254228] [Abstract] Cited for: IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH XPO5; RAN; ZNF346 AND DOUBLE-STRANDED RNA, INTERACTION WITH XPO5 AND ZNF346.
[20]	"Identifying and quantifying in vivo methylation sites by heavy methyl SILAC." Ong S.E., Mittler G., Mann M. Nat. Methods 1:119-126(2004) [PubMed: 15782174] [Abstract] Cited for: METHYLATION [LARGE SCALE ANALYSIS] AT ARG-609, MASS SPECTROMETRY.
[21]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62 AND THR-592, MASS SPECTROMETRY. Tissue: Epithelium.
[22]	"Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry." Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J., Bodenmiller B., Watts J.D., Hood L., Aebersold R. Nat. Methods 2:591-598(2005) [PubMed: 16094384] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-382, MASS SPECTROMETRY. Tissue: T-cell.
[23]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190; SER-382; SER-482 AND THR-592, MASS SPECTROMETRY. Tissue: Epithelium.
[24]	"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: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-592, MASS SPECTROMETRY. Tissue: Epithelium.
[25]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-592 AND SER-812, MASS SPECTROMETRY. Tissue: Epithelium.
[26]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-382 AND SER-384, MASS SPECTROMETRY.
[27]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-486, MASS SPECTROMETRY.
[28]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190; SER-482; TYR-579; THR-592; SER-792; SER-810 AND SER-812, MASS SPECTROMETRY.
[29]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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 , AF320228, AF320229, AF320230, AF320231, AF320232, AF320233, AF320234, AF320235, AF320236, AF320237, AF320238, AF320239, AF320240, AF320241, AF320242, AF320243 Genomic DNA. Translation: AAK07424.1. AF320247 , 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. 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.
IPI	IPI00219330. IPI00298788. IPI00298789. IPI00414335. IPI00418313. IPI00556173.
PIR	B54857.
RefSeq	NP_001131145.1. NP_004507.2. NP_036350.2. NP_060090.2. NP_703194.1.
UniGene	Hs.465885
3D structure databases
SMR	Q12906. Positions 403-470.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q12906. 6 interactions.
PTM databases
PhosphoSite	Q12906.
2-D gel databases
SWISS-2DPAGE	Q12906.
Proteomic databases
PRIDE	Q12906.
Genome annotation databases
Ensembl	ENSG00000129351. Homo sapiens. [Contig view]
GeneID	3609.
KEGG	hsa:3609.
UCSC	uc002mpk.1. human. uc002mpl.1. human. uc002mpm.1. human. uc002mpn.1. human. uc002mpo.1. human.
Organism-specific databases
GeneCards	GC19P010625.
H-InvDB	HIX0014753.
HGNC	HGNC:6038. ILF3.
HPA	HPA001897.
MIM	603182. gene.
PharmGKB	PA29853.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	Q12906.
OMA	Q12906. DYNYESK.
Gene expression databases
ArrayExpress	Q12906.
Bgee	Q12906.
GermOnline	ENSG00000129351. Homo sapiens.
Family and domain databases
InterPro	IPR001159. Ds-RNA_bd. IPR006561. DZF. [Graphical view]
Pfam	PF00035. dsrm. 2 hits. PF07528. DZF. 1 hit. [Graphical view]
SMART	SM00358. DSRM. 2 hits. SM00572. DZF. 1 hit. [Graphical view]
PROSITE	PS50137. DS_RBD. 2 hits. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	14109.
PMAP-CutDB	Q12906.
SOURCE	Search...

Entry information

Entry name

ILF3_HUMAN

Accession

Primary (citable) accession number: Q12906
Secondary accession number(s): A8K6F2 , 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 7, 2009
This is version 104 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)