Q12906 (ILF3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	894 AA.
Sequence status	Complete.
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	Identified in a mRNP complex, at least composed of DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and YBX1. Identified in a mRNP granule complex, at least composed of ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD, HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1, NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8, RPS9, SYNCRIP, TROVE2, YBX1 and 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 EIF2C1 and EIF2C2. Ref.10 Ref.13 Ref.14 Ref.15 Ref.17 Ref.18 Ref.19 Ref.22 Ref.23 Ref.24 Ref.26
Subcellular location	Nucleus › nucleolus. Cytoplasm. Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Ref.16 Ref.24
Tissue specificity	Ubiquitous.
Post-translational modification	Phosphorylated by RNA-dependent protein kinase (EIF2AK2). 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 process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Ligand	DNA-binding RNA-binding
PTM	Acetylation Methylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	M phase Non-traceable author statement Ref.9. Source: UniProtKB negative regulation of transcription, DNA-dependent Inferred from direct assay Ref.17. Source: UniProtKB positive regulation of transcription, DNA-dependent Inferred from direct assay Ref.17. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	mitochondrion Inferred from direct assay. Source: HPA nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay Ref.17. Source: UniProtKB ribonucleoprotein complex Inferred from direct assay Ref.24. Source: UniProtKB
Molecular_function	DNA binding Inferred from direct assay Ref.13Ref.1. Source: UniProtKB double-stranded RNA binding Inferred from direct assay Ref.13. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
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.

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.

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.29 Ref.31

Modified residue

100

1

N6-acetyllysine Ref.28

Modified residue

190

1

Phosphoserine Ref.25 Ref.29 Ref.31

Modified residue

382

1

Phosphoserine Ref.29 Ref.31

Modified residue

384

1

Phosphoserine Ref.29

Modified residue

460

1

N6-acetyllysine Ref.28

Modified residue

476

1

Phosphoserine Ref.31

Modified residue

482

1

Phosphoserine Ref.20 Ref.25 Ref.27 Ref.29 Ref.31

Modified residue

592

1

Phosphothreonine Ref.20 Ref.21 Ref.27 Ref.29 Ref.31

Modified residue

792

1

Phosphoserine Ref.25 Ref.27 Ref.31

Modified residue

812

1

Phosphoserine Ref.25 Ref.29 Ref.31

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. Ref.6
Corresponds to variant rs1064493 [ dbSNP | Ensembl ].

VAR_022159

Natural variant

501

1

A → S.
Corresponds to variant rs34520379 [ dbSNP | Ensembl ].

VAR_048906

Experimental info

Sequence conflict

101

1

G → C in AAD51098. Ref.5

Sequence conflict

101

1

G → C in AAD51099. Ref.5

Sequence conflict

101

1

G → C in AAK07424. Ref.6

Sequence conflict

101

1

G → C in AAK07425. 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 in AAD33966. Ref.2

Sequence conflict

647

1

S → T in AAK07424. Ref.6

Sequence conflict

647

1

S → T in AAK07425. 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

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

894

Helix Strand Turn

Details...

Helix

528 – 535

8

Beta strand

541 – 548

8

Beta strand

554 – 561

8

Beta strand

564 – 572

9

Helix

573 – 588

16

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) [UniParc]. 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 [UniParc]. 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) [UniParc]. 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) [UniParc]. 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 [UniParc]. 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] [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. , 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 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.
[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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-10, FUNCTION, INTERACTION WITH XRCC6; 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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] [Europe PMC] [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] [Europe PMC] [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] [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.
[20]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[22]	"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.
[23]	"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 EIF2C1 AND EIF2C2.
[24]	"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.
[25]	"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 AND 6), MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[26]	"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.
[27]	"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 AND 6), MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[28]	"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, MASS SPECTROMETRY.
[29]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[30]	"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].
[31]	"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, MASS SPECTROMETRY.
[32]	"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.
[33]	"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 , 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.
IPI00556173.
IPI01018179.

PIR

B54857.

RefSeq

NP_001131145.1. NM_001137673.1.
NP_004507.2. NM_004516.3.
NP_036350.2. NM_012218.3.
NP_060090.2. NM_017620.2.
NP_703194.1. NM_153464.2.

UniGene

Hs.465885.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2L33	NMR	-	A	521-600	[»]
3P1X	X-ray	1.90	A/B	520-594	[»]

ProteinModelPortal

Q12906.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29853N.

IntAct

Q12906. 27 interactions.

MINT

MINT-4999319.

PTM databases

PhosphoSite

Q12906.

Polymorphism databases

DMDM

62512150.

2D gel databases

SWISS-2DPAGE

Q12906.

Proteomic databases

PaxDb

Q12906.

PRIDE

Q12906.

Protocols and materials databases

DNASU

3609.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000250241; ENSP00000250241; ENSG00000129351.
ENST00000318511; ENSP00000315205; ENSG00000129351.
ENST00000407004; ENSP00000384660; ENSG00000129351.
ENST00000420083; ENSP00000405436; ENSG00000129351.
ENST00000589998; ENSP00000465219; ENSG00000129351.
ENST00000590261; ENSP00000468156; ENSG00000129351.
ENST00000592763; ENSP00000465515; ENSG00000129351.

GeneID

3609.

KEGG

hsa:3609.

UCSC

uc002mpk.2. human.
uc002mpl.2. human.
uc002mpm.2. human.
uc002mpn.3. human.
uc002mpp.3. human.

Organism-specific databases

CTD

3609.

GeneCards

GC19P010764.

H-InvDB

HIX0014753.

HGNC

HGNC:6038. ILF3.

HPA

HPA001897.

MIM

603182. gene.

neXtProt

NX_Q12906.

PharmGKB

PA29853.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG307678.

HOVERGEN

HBG069915.

InParanoid

Q12906.

KO

K13090.

PhylomeDB

Q12906.

Gene expression databases

ArrayExpress

Q12906.

Bgee

Q12906.

Genevestigator

Q12906.

GermOnline

ENSG00000129351. Homo sapiens.

Family and domain databases

Gene3D

3.30.160.20. 2 hits.

InterPro

IPR001159. Ds-RNA-bd.
IPR014720. dsRNA-bd-like_dom.
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

ChiTaRS

ILF3. human.

EvolutionaryTrace

Q12906.

GenomeRNAi

3609.

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:	May 1, 2013
This is version 146 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.