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ILF3

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ILF3
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesILF3, CBTF, DRBF, DRBP76, MMP4, MPHOSPH4, MPP4, NF-AT-90, NF110, NF110b, NF90, NF90a, NF90b, NFAR, NFAR-1, NFAR2, TCP110, TCP80, interleukin enhancer binding factor 3, NFAR110, MPP4110, NFAR-2, NF90c, NFAR90, NF90ctv
External IDsOMIM: 603182; MGI: 1339973; HomoloGene: 7785; GeneCards: ILF3; OMA:ILF3 - orthologs
Orthologs
SpeciesHumanMouse
Entrez

3609

16201

Ensembl

ENSG00000129351

ENSMUSG00000032178

UniProt

Q12906

Q9Z1X4

RefSeq (mRNA)

NM_001137673
NM_004516
NM_012218
NM_017620
NM_153464

RefSeq (protein)

NP_001131145
NP_004507
NP_036350
NP_060090
NP_703194

Location (UCSC)Chr 19: 10.65 – 10.69 MbChr 9: 21.28 – 21.32 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Interleukin enhancer-binding factor 3 is a protein that in humans is encoded by the ILF3 gene.[5][6]

Function

Nuclear factor of activated T-cells (NFAT) is a transcription factor required for T-cell expression of interleukin 2. NFAT binds to a sequence in the IL2 enhancer known as the antigen receptor response element 2. In addition, NFAT can bind RNA and is an essential component for encapsidation and protein priming of hepatitis B viral polymerase. NFAT is a heterodimer of 45 kDa and 90 kDa proteins, the larger of which is the product of this gene. The encoded protein, which is primarily localized to ribosomes, probably regulates transcription at the level of mRNA elongation. At least three transcript variants encoding three different isoforms have been found for this gene.[7]

Interactions

ILF3 has been shown to interact with:

Small NF90/ILF3-associated RNAs (snaR) (~120 nucleotides long) and are known to interact with ILF3 double-stranded RNA-binding motifs.[17] snaR-A is abundant in human testis and has been shown to associate with ribosomes in HeLa cells. snaR-A is present in human and gorilla but not in chimpanzee. Other snaR RNAs are found in African Great Apes (including chimpanzee and bonobo).[18]

ILF2 and ILF3 have been identified as autoantigens in mice with induced lupus,[19][20] in canine systemic rheumatic autoimmune disease,[21] and as a rare finding in humans with autoimmune disease.[22]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000129351 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000032178 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Kao PN, Chen L, Brock G, Ng J, Kenny J, Smith AJ, Corthésy B (August 1994). "Cloning and expression of cyclosporin A- and FK506-sensitive nuclear factor of activated T-cells: NF45 and NF90". The Journal of Biological Chemistry. 269 (32): 20691–9. PMID 7519613.
  6. ^ Matsumoto-Taniura N, Pirollet F, Monroe R, Gerace L, Westendorf JM (September 1996). "Identification of novel M phase phosphoproteins by expression cloning". Molecular Biology of the Cell. 7 (9): 1455–69. doi:10.1091/mbc.7.9.1455. PMC 275994. PMID 8885239.
  7. ^ "Entrez Gene: ILF3 interleukin enhancer binding factor 3, 90kDa".
  8. ^ Ting NS, Kao PN, Chan DW, Lintott LG, Lees-Miller SP (January 1998). "DNA-dependent protein kinase interacts with antigen receptor response element binding proteins NF90 and NF45". The Journal of Biological Chemistry. 273 (4): 2136–45. CiteSeerX 10.1.1.615.1747. doi:10.1074/jbc.273.4.2136. PMID 9442054.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  9. ^ a b Saunders LR, Perkins DJ, Balachandran S, Michaels R, Ford R, Mayeda A, Barber GN (August 2001). "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". The Journal of Biological Chemistry. 276 (34): 32300–12. doi:10.1074/jbc.M104207200. PMID 11438536.
  10. ^ Tang J, Kao PN, Herschman HR (June 2000). "Protein-arginine methyltransferase I, the predominant protein-arginine methyltransferase in cells, interacts with and is regulated by interleukin enhancer-binding factor 3". The Journal of Biological Chemistry. 275 (26): 19866–76. doi:10.1074/jbc.M000023200. PMID 10749851.
  11. ^ Lee J, Bedford MT (March 2002). "PABP1 identified as an arginine methyltransferase substrate using high-density protein arrays". EMBO Reports. 3 (3): 268–73. doi:10.1093/embo-reports/kvf052. PMC 1084016. PMID 11850402.
  12. ^ Langland JO, Kao PN, Jacobs BL (May 1999). "Nuclear factor-90 of activated T-cells: A double-stranded RNA-binding protein and substrate for the double-stranded RNA-dependent protein kinase, PKR". Biochemistry. 38 (19): 6361–8. doi:10.1021/bi982410u. PMID 10320367.
  13. ^ Parker LM, Fierro-Monti I, Mathews MB (August 2001). "Nuclear factor 90 is a substrate and regulator of the eukaryotic initiation factor 2 kinase double-stranded RNA-activated protein kinase". The Journal of Biological Chemistry. 276 (35): 32522–30. doi:10.1074/jbc.M104408200. PMID 11438540.
  14. ^ Patel RC, Vestal DJ, Xu Z, Bandyopadhyay S, Guo W, Erme SM, Williams BR, Sen GC (July 1999). "DRBP76, a double-stranded RNA-binding nuclear protein, is phosphorylated by the interferon-induced protein kinase, PKR". The Journal of Biological Chemistry. 274 (29): 20432–7. doi:10.1074/jbc.274.29.20432. PMID 10400669.
  15. ^ Brownawell AM, Macara IG (January 2002). "Exportin-5, a novel karyopherin, mediates nuclear export of double-stranded RNA binding proteins". The Journal of Cell Biology. 156 (1): 53–64. doi:10.1083/jcb.200110082. PMC 2173575. PMID 11777942.
  16. ^ Chu L, Su MY, Maggi LB, Lu L, Mullins C, Crosby S, Huang G, Chng WJ, Vij R, Tomasson MH (August 2012). "Multiple myeloma-associated chromosomal translocation activates orphan snoRNA ACA11 to suppress oxidative stress". The Journal of Clinical Investigation. 122 (8): 2793–806. doi:10.1172/jci63051. PMC 3408744. PMID 22751105.
  17. ^ Parrott AM, Mathews MB (2007). "Novel rapidly evolving hominid RNAs bind nuclear factor 90 and display tissue-restricted distribution". Nucleic Acids Research. 35 (18): 6249–58. doi:10.1093/nar/gkm668. PMC 2094060. PMID 17855395.
  18. ^ Parrott AM, Tsai M, Batchu P, Ryan K, Ozer HL, Tian B, Mathews MB (March 2011). "The evolution and expression of the snaR family of small non-coding RNAs". Nucleic Acids Research. 39 (4): 1485–500. doi:10.1093/nar/gkq856. PMC 3045588. PMID 20935053.
  19. ^ Satoh M, Shaheen VM, Kao PN, Okano T, Shaw M, Yoshida H, Richards HB, Reeves WH (December 1999). "Autoantibodies define a family of proteins with conserved double-stranded RNA-binding domains as well as DNA binding activity". The Journal of Biological Chemistry. 274 (49): 34598–604. doi:10.1074/jbc.274.49.34598. PMID 10574923.
  20. ^ Kuroda Y, Ono N, Akaogi J, Nacionales DC, Yamasaki Y, Barker TT, Reeves WH, Satoh M (February 2006). "Induction of lupus-related specific autoantibodies by non-specific inflammation caused by an intraperitoneal injection of n-hexadecane in BALB/c mice". Toxicology. 218 (2–3): 186–96. doi:10.1016/j.tox.2005.10.011. PMID 16309812.
  21. ^ Bremer HD, Landegren N, Sjöberg R, Hallgren Å, Renneker S, Lattwein E, Leonard D, Eloranta ML, Rönnblom L, Nordmark G, Nilsson P, Andersson G, Lilliehöök I, Lindblad-Toh K, Kämpe O, Hansson-Hamlin H (March 2018). "ILF2 and ILF3 are autoantigens in canine systemic autoimmune disease". Scientific Reports. 8 (1): 4852. Bibcode:2018NatSR...8.4852B. doi:10.1038/s41598-018-23034-w. PMC 5859008. PMID 29556082.
  22. ^ Satoh M, Shaheen VM, Kao PN, Okano T, Shaw M, Yoshida H, Richards HB, Reeves WH (December 1999). "Autoantibodies define a family of proteins with conserved double-stranded RNA-binding domains as well as DNA binding activity". The Journal of Biological Chemistry. 274 (49): 34598–604. doi:10.1074/jbc.274.49.34598. PMID 10574923.

Further reading

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

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