Search Results

Overview

Uniprot IDQ12906
Protein NameInterleukin enhancer-binding factor 3
Gene NameILF3
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
100 MRVGLVAKGLLLKGD
182 VVREEMEKVLAGETL
214 LASLRHAKWFQARAN
342 GMDPLPSKMPKKPKN
393 KKKKIQKKEEKAEPP
396 KIQKKEEKAEPPQAM
413 LMRLNQLKPGLQYKL
454 GPSKKTAKLHVAVKV
553 ETGGSHDKRFVMEVE
577 GSNKKVAKAYAALAA
600 PLALDANKKKRAPVP
601 LALDANKKKRAPVPV
602 ALDANKKKRAPVPVR
775 GPPQGKQKGYNHGQG

Function

RNA-binding protein that plays an essential role in the biogenesis of circular RNAs (circRNAs) which are produced by back-splicing circularization of pre-mRNAs. Within the nucleus, promotes circRNAs processing by stabilizing the regulatory elements residing in the flanking introns of the circularized exons. Plays thereby a role in the back-splicing of a subset of circRNAs (PubMed:28625552). As a consequence, participates in a wide range of transcriptional and post-transcriptional processes. Binds to poly-U elements and AU-rich elements (AREs) in the 3'-UTR of target mRNAs (PubMed:14731398). Upon viral infection, ILF3 accumulates in the cytoplasm and participates in the innate antiviral response (PubMed:21123651, PubMed:34110282). Mechanistically, ILF3 becomes phosphorylated and activated by the double-stranded RNA-activated protein kinase/PKR which releases ILF3 from cellular mature circRNAs. In turn, unbound ILF3 molecules are able to interact with and thus inhibit viral mRNAs (PubMed:21123651, PubMed:28625552)

Protein Sequence

10 MRPMRIFVND 20 DRHVMAKHSS 30 VYPTQEELEA 40 VQNMVSHTER 50 ALKAVSDWID 60 EQEKGSSEQA 70 ESDNMDVPPE 80 DDSKEGAGEQ 90 KTEHMTRTLR 100 GVMRVGLVAK 110 GLLLKGDLDL 120 ELVLLCKEKP 130 TTALLDKVAD 140 NLAIQLAAVT 150 EDKYEILQSV 160 DDAAIVIKNT 170 KEPPLSLTIH 180 LTSPVVREEM 190 EKVLAGETLS 200 VNDPPDVLDR 210 QKCLAALASL 220 RHAKWFQARA 230 NGLKSCVIVI 240 RVLRDLCTRV 250 PTWGPLRGWP 260 LELLCEKSIG 270 TANRPMGAGE 280 ALRRVLECLA 290 SGIVMPDGSG 300 IYDPCEKEAT 310 DAIGHLDRQQ 320 REDITQSAQH 330 ALRLAAFGQL 340 HKVLGMDPLP 350 SKMPKKPKNE 360 NPVDYTVQIP 370 PSTTYAITPM 380 KRPMEEDGEE 390 KSPSKKKKKI 400 QKKEEKAEPP 410 QAMNALMRLN 420 QLKPGLQYKL 430 VSQTGPVHAP 440 IFTMSVEVDG 450 NSFEASGPSK 460 KTAKLHVAVK 470 VLQDMGLPTG 480 AEGRDSSKGE 490 DSAEETEAKP 500 AVVAPAPVVE 510 AVSTPSAAFP 520 SDATAEQGPI 530 LTKHGKNPVM 540 ELNEKRRGLK 550 YELISETGGS 560 HDKRFVMEVE 570 VDGQKFQGAG 580 SNKKVAKAYA 590 ALAALEKLFP 600 DTPLALDANK 610 KKRAPVPVRG 620 GPKFAAKPHN 630 PGFGMGGPMH 640 NEVPPPPNLR 650 GRGRGGSIRG 660 RGRGRGFGGA 670 NHGGYMNAGA 680 GYGSYGYGGN 690 SATAGYSQFY 700 SNGGHSGNAS 710 GGGGGGGGGS 720 SGYGSYYQGD 730 NYNSPVPPKH 740 AGKKQPHGGQ 750 QKPSYGSGYQ 760 SHQGQQQSYN 770 QSPYSNYGPP 780 QGKQKGYNHG 790 QGSYSYSNSY 800 NSPGGGGGSD 810 YNYESKFNYS 820 GSGGRSGGNS 830 YGSGGASYNP 840 GSHGGYGGGS 850 GGGSSYQGKQ 860 GGYSQSNYNS 870 PGSGQNYSGP 880 PSSYQSSQGG 890 YGRNADHSMN YQYR

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005576 extracellular region
Cellular Component GO:0016020 membrane
Cellular Component GO:0005739 mitochondrion
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:1990904 ribonucleoprotein complex
Molecular Function GO:0003677 DNA binding
Molecular Function GO:0003725 double-stranded RNA binding
Molecular Function GO:0035925 mRNA 3'-UTR AU-rich region binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0003727 single-stranded RNA binding
Molecular Function GO:0001618 virus receptor activity
Biological Process GO:0051607 defense response to virus
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0045892 negative regulation of DNA-templated transcription
Biological Process GO:0017148 negative regulation of translation
Biological Process GO:0045071 negative regulation of viral genome replication
Biological Process GO:0045893 positive regulation of DNA-templated transcription
Biological Process GO:0006468 protein phosphorylation
Biological Process GO:0160091 spliceosome-depend formation of circular RNA

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[3] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.

[4] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.

[5] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[6] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.