UniProt Accession

 ILF3_HUMAN; Q12906; A8K6F2; G5E9M5; O43409; Q6P1X1; Q86XY7; Q99544; Q99545; Q9BZH4; Q9BZH5; Q9NQ95; Q9NQ96; Q9NQ97; Q9NQ98; Q9NQ99; Q9NQA0; Q9NQA1; Q9NQA2; Q9NRN2; Q9NRN3; Q9NRN4; Q9UMZ9; Q9UN00; Q9UN84; Q9UNA2 

Genbank Protein ID

 U10324; AF147209; AF141870; AJ271741; AJ271741; AJ271741; AJ271741; AJ271744; AJ271745; AJ271746; AJ271747; AF167569; AF167570; AF320244; AF320228; AF320229; AF320230; AF320231; AF320232; AF320233; AF320234; AF320235; AF320236; AF320237; AF320238; AF320239; AF320240; AF320241; AF320242; AF320243; AF320247; AF320228; AF320229; AF320230; AF320231; AF320232; AF320233; AF320234; AF320235; AF320236; AF320237; AF320238; AF320239; AF320240; AF320241; AF320242; AF320243; AF320245; AF320246; AK291617; AC011475; CH471106; BC048314; BC064836; X98264; X98265; AF202445; AF202445; AF202445; AF007140 

Genbank Nucleotide ID

 AAA20994.1; AAD33966.1; AAD37575.1; CAC01121.1; CAC01122.1; CAC01123.1; CAC01124.1; CAC01404.1; CAC01405.1; CAC01406.1; CAC01407.1; AAD51098.1; AAD51099.1; AAK07424.1; AAK07424.1; AAK07424.1; AAK07424.1; AAK07424.1; AAK07424.1; AAK07424.1; AAK07424.1; AAK07424.1; AAK07424.1; AAK07424.1; AAK07424.1; AAK07424.1; AAK07424.1; AAK07424.1; AAK07424.1; AAK07424.1; AAK07425.1; AAK07425.1; AAK07425.1; AAK07425.1; AAK07425.1; AAK07425.1; AAK07425.1; AAK07425.1; AAK07425.1; AAK07425.1; AAK07425.1; AAK07425.1; AAK07425.1; AAK07425.1; AAK07425.1; AAK07425.1; AAK07425.1; AAK07425.1; AAK07425.1; BAF84306.1; EAW84132.1; AAH48314.1; AAH64836.1; CAA66917.1; CAA66918.1; AAF82685.1; AAF82686.1; AAF82687.1; AAC19152.1 

Protein Name

 Interleukin enhancer-binding factor 3 

Protein Synonyms/Alias

 Double-stranded RNA-binding protein 76; DRBP76; M-phase phosphoprotein 4; MPP4; Nuclear factor associated with dsRNA; NFAR; Nuclear factor of activated T-cells 90 kDa; NF-AT-90; Translational control protein 80; TCP80 

Gene Name

 ILF3 

Gene Synonyms/Alias

 DRBF; MPHOSPH4; NF90 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
100	MRVGLVAKGLLLKGD	ubiquitination	[1]
202	PDVLDRQKCLAALAS	ubiquitination	[1]
257	PLELLCEKSIGTANR	ubiquitination	[1]
342	GMDPLPSKMPKKPKN	ubiquitination	[1]

Reference

 [1] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724] 

Functional Description

 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). 

Sequence Annotation

 DOMAIN 94 342 DZF.
 DOMAIN 398 467 DRBM 1.
 DOMAIN 524 590 DRBM 2.
 REGION 609 894 Interaction with PRMT1.
 MOTIF 371 389 Bipartite nuclear localization signal
 MOD_RES 62 62 Phosphoserine.
 MOD_RES 100 100 N6-acetyllysine.
 MOD_RES 188 188 Phosphothreonine; by PKR.
 MOD_RES 190 190 Phosphoserine.
 MOD_RES 315 315 Phosphothreonine; by PKR.
 MOD_RES 382 382 Phosphoserine.
 MOD_RES 384 384 Phosphoserine.
 MOD_RES 460 460 N6-acetyllysine.
 MOD_RES 476 476 Phosphoserine.
 MOD_RES 482 482 Phosphoserine.
 MOD_RES 592 592 Phosphothreonine.
 MOD_RES 792 792 Phosphoserine.
 MOD_RES 812 812 Phosphoserine.  

Keyword

 3D-structure; Acetylation; Alternative splicing; Antiviral defense; Complete proteome; Cytoplasm; Direct protein sequencing; DNA-binding; Methylation; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; RNA-binding; Transcription; Transcription regulation. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 894 AA 

Protein Sequence

Gene Ontology

 GO:0005739; C:mitochondrion; IDA:HPA.
 GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0030529; C:ribonucleoprotein complex; IDA:UniProtKB.
 GO:0003677; F:DNA binding; IDA:UniProtKB.
 GO:0003725; F:double-stranded RNA binding; IDA:UniProtKB.
 GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
 GO:0000279; P:M phase; NAS:UniProtKB.
 GO:0045892; P:negative regulation of transcription, DNA-dependent; IDA:UniProtKB.
 GO:0017148; P:negative regulation of translation; ISS:UniProtKB.
 GO:0045071; P:negative regulation of viral genome replication; ISS:UniProtKB.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; IDA:UniProtKB.
 GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 

Interpro

 IPR001159; Ds-RNA-bd.
 IPR014720; dsRNA-bd-like_dom.
 IPR006561; DZF. 

Pfam

 PF00035; dsrm
 PF07528; DZF 

SMART

 SM00358; DSRM
 SM00572; DZF 

PROSITE

 PS50137; DS_RBD 

PRINTS