ILF3_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ILF3_MOUSE
• UniProt AC: Q9Z1X4
• Protein Name: Interleukin enhancer-binding factor 3
• Gene Name: Ilf3
• Organism: Mus musculus (Mouse).
• Sequence Length: 898
• Subcellular Localization: Nucleus, nucleolus . Cytoplasm . Nucleus . Localizes in the cytoplasm in response to viral infection. The unphosphorylated form is retained in the nucleus by ILF2. Phosphorylation at Thr-188 and Thr-315 causes the dissociation of ILF2 from the ILF2-I
• Protein Description: 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. As a consequence, participates in a wide range of transcriptional and post-transcriptional processes. Upon viral infection, ILF3 accumulates in the cytoplasm and participates in the innate antiviral response. 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..
• Protein Sequence: MRPMRIFVNDDRHVMAKHSSVYPTQEELEAVQNMVSHTERALKAVSDWIDEQEKGNSELSEAENMDTPPDDESKEGAGEQKAEHMTRTLRGVMRVGLVAKGLLLKGDLDLELVLLCKEKPTTALLDKVADNLAIQLTTVTEDKYEILQSVDDAAIVIKNTKEPPLSLTIHLTSPVVREEMEKVLAGETLSVNDPPDVLDRQKCLAALASLRHAKWFQARANGLKSCVIVIRVLRDLCTRVPTWGPLRGWPLELLCEKSIGTANRPMGAGEALRRVLECLASGIVMPDGSGIYDPCEKEATDAIGHLDRQQREDITQSAQHALRLAAFGQLHKVLGMDPLPSKMPKKPKNENPVDYTVQIPPSTTYAITPMKRPMEEDGEEKSPSKKKKKIQKKEEKADPPQAMNALMRLNQLKPGLQYKLISQTGPVHAPIFTMSVEVDGSNFEASGPSKKTAKLHVAVKVLQDMGLPTGAEGRDSSKGEDSAEESDGKPAIVAPPPVVEAVSNPSSVFPSDATTEQGPILTKHGKNPVMELNEKRRGLKYELISETGGSHDKRFVMEVEVDGQKFQGAGSNKKVAKAYAALAALEKLFPDTPLALEANKKKRTPVPVRGGPKFAAKPHNPGFGMGGPMHNEVPPPPNIRGRGRGGNIRGRGRGRGFGGANHGGGYMNAGAGYGSYGYSSNSATAGYSQFYSNGGHSGNAGGGGSGGGGGSSSYSSYYQGDSYNSPVPPKHAGKKPLHGGQQKASYSSGYQSHQGQQQPYNQSQYSSYGTPQGKQKGYGHGQGSYSSYSNSYNSPGGGGGSDYSYDSKFNYSGSGGRSGGNSYGSSGSSSYNTGSHGGYGTGSGGSSSYQGKQGGYSSQSNYSSPGSSQSYSGPASSYQSSQGGYSRNTEHSMNYQYR

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
57	Phosphorylation	DEQEKGNSELSEAEN HHHHCCCCCCHHHHH	48.89	27087446
60	Phosphorylation	EKGNSELSEAENMDT HCCCCCCHHHHHCCC	30.61	25521595
67	Phosphorylation	SEAENMDTPPDDESK HHHHHCCCCCCCCCC	26.42	25521595
73	Phosphorylation	DTPPDDESKEGAGEQ CCCCCCCCCCCCCHH	42.89	25521595
100	Acetylation	MRVGLVAKGLLLKGD HHHHHHHHCHHHCCC	42.48	-
100 (in isoform 3)	Ubiquitination	-	42.48	22790023
100	Ubiquitination	MRVGLVAKGLLLKGD HHHHHHHHCHHHCCC	42.48	22790023
113 (in isoform 3)	Ubiquitination	-	2.54	-
188	Phosphorylation	EKVLAGETLSVNDPP HHHHCCCCCCCCCCC	24.34	25159016
190	Phosphorylation	VLAGETLSVNDPPDV HHCCCCCCCCCCCCC	26.71	25159016
209	Phosphorylation	KCLAALASLRHAKWF HHHHHHHHHHHHHHH	27.13	-
292	Phosphorylation	MPDGSGIYDPCEKEA CCCCCCCCCCCHHHH	19.84	22817900
300	Phosphorylation	DPCEKEATDAIGHLD CCCHHHHHHHHCCCC	27.36	18779572
315	Phosphorylation	RQQREDITQSAQHAL HHHHHHHHHHHHHHH	28.88	22817900
362	Phosphorylation	YTVQIPPSTTYAITP EEEECCCCCEEEECC	28.20	26643407
363	Phosphorylation	TVQIPPSTTYAITPM EEECCCCCEEEECCC	29.60	26643407
364	Phosphorylation	VQIPPSTTYAITPMK EECCCCCEEEECCCC	18.45	26643407
365	Phosphorylation	QIPPSTTYAITPMKR ECCCCCEEEECCCCC	8.97	26643407
368	Phosphorylation	PSTTYAITPMKRPME CCCEEEECCCCCCCC	14.79	26643407
382	Phosphorylation	EEDGEEKSPSKKKKK CCCCCCCCCCHHHHH	37.37	25521595
384	Phosphorylation	DGEEKSPSKKKKKIQ CCCCCCCCHHHHHHH	65.29	21930439
460	Acetylation	AKLHVAVKVLQDMGL CHHHHHHHHHHHCCC	27.73	-
469	Phosphorylation	LQDMGLPTGAEGRDS HHHCCCCCCCCCCCC	54.81	22817900
476	Phosphorylation	TGAEGRDSSKGEDSA CCCCCCCCCCCCCCC	32.37	25521595
477	Phosphorylation	GAEGRDSSKGEDSAE CCCCCCCCCCCCCCC	49.31	21082442
482	Phosphorylation	DSSKGEDSAEESDGK CCCCCCCCCCCCCCC	33.02	26824392
486	Phosphorylation	GEDSAEESDGKPAIV CCCCCCCCCCCCEEE	43.07	22942356
503	Phosphorylation	PPVVEAVSNPSSVFP CCCEEECCCCCCCCC	50.50	24068923
506	Phosphorylation	VEAVSNPSSVFPSDA EEECCCCCCCCCCCC	43.30	24068923
507	Phosphorylation	EAVSNPSSVFPSDAT EECCCCCCCCCCCCC	29.09	24068923
511	Phosphorylation	NPSSVFPSDATTEQG CCCCCCCCCCCCCCC	28.54	24068923
514	Phosphorylation	SVFPSDATTEQGPIL CCCCCCCCCCCCCCC	35.54	24068923
515	Phosphorylation	VFPSDATTEQGPILT CCCCCCCCCCCCCCC	28.21	24068923
522	Phosphorylation	TEQGPILTKHGKNPV CCCCCCCCCCCCCCC	23.01	24068923
592	Phosphorylation	LEKLFPDTPLALEAN HHHHCCCCCCHHHCC	22.05	26745281
604	Phosphorylation	EANKKKRTPVPVRGG HCCCCCCCCCCCCCC	37.20	26239621
609	Dimethylation	KRTPVPVRGGPKFAA CCCCCCCCCCCCCCC	37.98	-
609	Methylation	KRTPVPVRGGPKFAA CCCCCCCCCCCCCCC	37.98	12229367
675	Phosphorylation	NAGAGYGSYGYSSNS CCCCCCCCCCCCCCC	13.60	-
676	Phosphorylation	AGAGYGSYGYSSNSA CCCCCCCCCCCCCCC	18.73	-
760	Phosphorylation	HQGQQQPYNQSQYSS CCCCCCCCCHHHHHC	22.84	23984901
763	Phosphorylation	QQQPYNQSQYSSYGT CCCCCCHHHHHCCCC	27.70	23984901
765	Phosphorylation	QPYNQSQYSSYGTPQ CCCCHHHHHCCCCCC	12.58	23984901
766	Phosphorylation	PYNQSQYSSYGTPQG CCCHHHHHCCCCCCC	14.94	23984901
767	Phosphorylation	YNQSQYSSYGTPQGK CCHHHHHCCCCCCCC	23.73	23984901
768	Phosphorylation	NQSQYSSYGTPQGKQ CHHHHHCCCCCCCCC	21.05	26745281
770	Phosphorylation	SQYSSYGTPQGKQKG HHHHCCCCCCCCCCC	12.28	26745281
778	Phosphorylation	PQGKQKGYGHGQGSY CCCCCCCCCCCCCCC	17.00	23984901
784	Phosphorylation	GYGHGQGSYSSYSNS CCCCCCCCCCCCCCC	17.60	23984901
785	Phosphorylation	YGHGQGSYSSYSNSY CCCCCCCCCCCCCCC	14.41	23984901
786	Phosphorylation	GHGQGSYSSYSNSYN CCCCCCCCCCCCCCC	25.21	23984901
787	Phosphorylation	HGQGSYSSYSNSYNS CCCCCCCCCCCCCCC	25.09	25159016
788	Phosphorylation	GQGSYSSYSNSYNSP CCCCCCCCCCCCCCC	13.11	23984901
789	Phosphorylation	QGSYSSYSNSYNSPG CCCCCCCCCCCCCCC	22.65	23984901
791	Phosphorylation	SYSSYSNSYNSPGGG CCCCCCCCCCCCCCC	21.54	25159016
792	Phosphorylation	YSSYSNSYNSPGGGG CCCCCCCCCCCCCCC	24.74	23984901
794	Phosphorylation	SYSNSYNSPGGGGGS CCCCCCCCCCCCCCC	19.38	25159016
801	Phosphorylation	SPGGGGGSDYSYDSK CCCCCCCCCCCCCCC	36.33	25159016
803	Phosphorylation	GGGGGSDYSYDSKFN CCCCCCCCCCCCCCC	15.72	23984901
804	Phosphorylation	GGGGSDYSYDSKFNY CCCCCCCCCCCCCCC	27.70	23984901
805	Phosphorylation	GGGSDYSYDSKFNYS CCCCCCCCCCCCCCC	20.29	23984901
807	Phosphorylation	GSDYSYDSKFNYSGS CCCCCCCCCCCCCCC	30.80	23984901
811	Phosphorylation	SYDSKFNYSGSGGRS CCCCCCCCCCCCCCC	19.96	23984901
812	Phosphorylation	YDSKFNYSGSGGRSG CCCCCCCCCCCCCCC	27.82	26745281
814	Phosphorylation	SKFNYSGSGGRSGGN CCCCCCCCCCCCCCC	31.94	26745281
818	Phosphorylation	YSGSGGRSGGNSYGS CCCCCCCCCCCCCCC	55.09	-
856	Phosphorylation	YQGKQGGYSSQSNYS CCCCCCCCCCCCCCC	16.39	23984901
857	Phosphorylation	QGKQGGYSSQSNYSS CCCCCCCCCCCCCCC	25.77	23984901
858	Phosphorylation	GKQGGYSSQSNYSSP CCCCCCCCCCCCCCC	29.19	23984901
860	Phosphorylation	QGGYSSQSNYSSPGS CCCCCCCCCCCCCCC	39.42	23984901
862	Phosphorylation	GYSSQSNYSSPGSSQ CCCCCCCCCCCCCCC	18.77	23984901
863	Phosphorylation	YSSQSNYSSPGSSQS CCCCCCCCCCCCCCC	34.02	19060867
864	Phosphorylation	SSQSNYSSPGSSQSY CCCCCCCCCCCCCCC	23.95	27357545
867	Phosphorylation	SNYSSPGSSQSYSGP CCCCCCCCCCCCCCC	28.70	24759943
868	Phosphorylation	NYSSPGSSQSYSGPA CCCCCCCCCCCCCCC	29.12	23984901
870	Phosphorylation	SSPGSSQSYSGPASS CCCCCCCCCCCCCHH	24.18	23984901
871	Phosphorylation	SPGSSQSYSGPASSY CCCCCCCCCCCCHHC	15.26	23984901
872	Phosphorylation	PGSSQSYSGPASSYQ CCCCCCCCCCCHHCC	43.47	23984901
876	Phosphorylation	QSYSGPASSYQSSQG CCCCCCCHHCCCCCC	32.48	23984901

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
188	T	Phosphorylation	Kinase	EIF2AK2	P19525	GPS
188	T	Phosphorylation	Kinase	PKR	Q03963	Uniprot
315	T	Phosphorylation	Kinase	EIF2AK2	P19525	GPS
315	T	Phosphorylation	Kinase	PKR	Q03963	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
188	T	Phosphorylation	Phosphorylated at Thr-188 and Thr-315 by PKR in response to RNA viruses.	21123651
315	T	Phosphorylation	Phosphorylated at Thr-188 and Thr-315 by PKR in response to RNA viruses.	21123651

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of ILF3_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of ILF3_MOUSE !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.