ILF3_RAT - dbPTM
ILF3_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ILF3_RAT
UniProt AC Q9JIL3
Protein Name Interleukin enhancer-binding factor 3
Gene Name Ilf3
Organism Rattus norvegicus (Rat).
Sequence Length 897
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 MRPMRIFVNDDRHVMAKHSSVYPTQEELEAVQNMVSHTERALKAVSDWIDEQEKGNSELSEAENMDTPPDDESKEGAGEQKAEHMTRTLRGVMRVGLVAKGLLLKGDLDLELVLLCKEKPTTALLDKVADNLAIQLTTVTEDKYEILQSVDDAAIVIKNTKEPPLSLTIHLTSPVVREEMEKVLAGETLSVNDPPDVLDRQKCLAALASLRHAKWFQARANGLKSCVIVIRVLRDLCTRVPTWGPLRGWPLELLCEKSIGTANRPMGAGEALRRVLECLASGIVMPDGSGIYDPCEKEATDAIGHLDRQQREDITQSAQHALRLAAFGQLHKVLGMDPLPSKMPKKPKNENPVDYTVQIPPSTTYAITPMKRPMEEDGEEKSPSKKKKKIQKKEEKAEPPQAMNALMRLNQLKPGLQYKLISQTGPVHAPIFTMSVEVDGSTFEASGPSKKTAKLHVAVKVLQDMGLPTGAEGRDSSKGEDSAEESDGKPAVVAPPPVVEAVSNPSSVFPSDATTEQGPILTKHGKNPVMELNEKRRGLKYELISETGGSHDKRFVMEVEVDGQKFQGAGSNKKVAKAYAALAALEKLFPDAPLALEANKKKRAPVPVRGGPKFAAKPHNPGFGMGGPMHNEAPPPPNIRGRGRGGNIRGRGRGRGFGGTNHGGGYMNAGAGYGSYGYSSNSATAGYSQFYSNGGHYGNAGGGGSGGGGGSSSYSSYYQGDSYNSPVPPKHAGKKPLHGGQQKPSYSSGYQSHQGQQQPYNQSQYSSYGTPQGKQKGYGHGQGSYSSYSNSYNSPGGGGGSDYSYDSKFNYSGSGGRSGGNSYGSSGSSYNTGSHGGYGAGSGGSSSYQGKQGGYSSQSNYSSPGSSQSYSGPASSYQSSQGGYSRNTEHSMNYQYR
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 Orthologous
Protein Cluster
19PhosphorylationRHVMAKHSSVYPTQE
CCHHHHCCCCCCCHH
22.3125575281
20PhosphorylationHVMAKHSSVYPTQEE
CHHHHCCCCCCCHHH
25.9525575281
22PhosphorylationMAKHSSVYPTQEELE
HHHCCCCCCCHHHHH
11.5125575281
24PhosphorylationKHSSVYPTQEELEAV
HCCCCCCCHHHHHHH
30.8125575281
36PhosphorylationEAVQNMVSHTERALK
HHHHHHHHHHHHHHH
17.5825575281
38PhosphorylationVQNMVSHTERALKAV
HHHHHHHHHHHHHHH
21.4725575281
57PhosphorylationDEQEKGNSELSEAEN
HHHHCCCCCCHHHHH
48.8922673903
60PhosphorylationEKGNSELSEAENMDT
HCCCCCCHHHHHCCC
30.6123298284
67PhosphorylationSEAENMDTPPDDESK
HHHHHCCCCCCCCCC
26.4223298284
73PhosphorylationDTPPDDESKEGAGEQ
CCCCCCCCCCCCCHH
42.8923298284
100AcetylationMRVGLVAKGLLLKGD
HHHHHHHHCHHHCCC
42.48-
100UbiquitinationMRVGLVAKGLLLKGD
HHHHHHHHCHHHCCC
42.48-
144PhosphorylationTTVTEDKYEILQSVD
EEECCCHHHHHHHCC
22.11-
188PhosphorylationEKVLAGETLSVNDPP
HHHHCCCCCCCCCCC
24.34-
190PhosphorylationVLAGETLSVNDPPDV
HHCCCCCCCCCCCCC
26.7123984901
209PhosphorylationKCLAALASLRHAKWF
HHHHHHHHHHHHHHH
27.1323984901
214AcetylationLASLRHAKWFQARAN
HHHHHHHHHHHHHHC
42.2722902405
315PhosphorylationRQQREDITQSAQHAL
HHHHHHHHHHHHHHH
28.88-
382PhosphorylationEEDGEEKSPSKKKKK
CCCCCCCCCCHHHHH
37.3730411139
384PhosphorylationDGEEKSPSKKKKKIQ
CCCCCCCCHHHHHHH
65.2927097102
460AcetylationAKLHVAVKVLQDMGL
HHHHHHHHHHHHCCC
27.73-
469PhosphorylationLQDMGLPTGAEGRDS
HHHCCCCCCCCCCCC
54.8127097102
476PhosphorylationTGAEGRDSSKGEDSA
CCCCCCCCCCCCCCC
32.3727097102
477PhosphorylationGAEGRDSSKGEDSAE
CCCCCCCCCCCCCCC
49.3127097102
482PhosphorylationDSSKGEDSAEESDGK
CCCCCCCCCCCCCCC
33.0227097102
486PhosphorylationGEDSAEESDGKPAVV
CCCCCCCCCCCCCEE
43.0727097102
503PhosphorylationPPVVEAVSNPSSVFP
CCCEEECCCCCCCCC
50.5027097102
506PhosphorylationVEAVSNPSSVFPSDA
EEECCCCCCCCCCCC
43.3027097102
507PhosphorylationEAVSNPSSVFPSDAT
EECCCCCCCCCCCCC
29.0927097102
511PhosphorylationNPSSVFPSDATTEQG
CCCCCCCCCCCCCCC
28.5428432305
514PhosphorylationSVFPSDATTEQGPIL
CCCCCCCCCCCCCCC
35.5428432305
515PhosphorylationVFPSDATTEQGPILT
CCCCCCCCCCCCCCC
28.2128432305
522PhosphorylationTEQGPILTKHGKNPV
CCCCCCCCCCCCCCC
23.0128432305
571PhosphorylationQKFQGAGSNKKVAKA
EEECCCCCCHHHHHH
44.9621630457
609MethylationKRAPVPVRGGPKFAA
CCCCCCCCCCCCCCC
37.9819019797
778PhosphorylationPQGKQKGYGHGQGSY
CCCCCCCCCCCCCCC
17.0023984901
784PhosphorylationGYGHGQGSYSSYSNS
CCCCCCCCCCCCCCC
17.6023984901
785PhosphorylationYGHGQGSYSSYSNSY
CCCCCCCCCCCCCCC
14.4123984901
786PhosphorylationGHGQGSYSSYSNSYN
CCCCCCCCCCCCCCC
25.2123984901
787PhosphorylationHGQGSYSSYSNSYNS
CCCCCCCCCCCCCCC
25.0923984901
788PhosphorylationGQGSYSSYSNSYNSP
CCCCCCCCCCCCCCC
13.1123984901
789PhosphorylationQGSYSSYSNSYNSPG
CCCCCCCCCCCCCCC
22.6523984901
791PhosphorylationSYSSYSNSYNSPGGG
CCCCCCCCCCCCCCC
21.5423984901
792PhosphorylationYSSYSNSYNSPGGGG
CCCCCCCCCCCCCCC
24.7423984901
794PhosphorylationSYSNSYNSPGGGGGS
CCCCCCCCCCCCCCC
19.3823984901
801PhosphorylationSPGGGGGSDYSYDSK
CCCCCCCCCCCCCCC
36.3323984901
803PhosphorylationGGGGGSDYSYDSKFN
CCCCCCCCCCCCCCC
15.7223984901
804PhosphorylationGGGGSDYSYDSKFNY
CCCCCCCCCCCCCCC
27.7023984901
805PhosphorylationGGGSDYSYDSKFNYS
CCCCCCCCCCCCCCC
20.2923984901
811PhosphorylationSYDSKFNYSGSGGRS
CCCCCCCCCCCCCCC
19.9627097102
812PhosphorylationYDSKFNYSGSGGRSG
CCCCCCCCCCCCCCC
27.8223984901
814PhosphorylationSKFNYSGSGGRSGGN
CCCCCCCCCCCCCCC
31.9428432305
818PhosphorylationYSGSGGRSGGNSYGS
CCCCCCCCCCCCCCC
55.0928689409
822PhosphorylationGGRSGGNSYGSSGSS
CCCCCCCCCCCCCCC
33.8628689409
834PhosphorylationGSSYNTGSHGGYGAG
CCCCCCCCCCCCCCC
19.5428689409
867PhosphorylationNYSSPGSSQSYSGPA
CCCCCCCCCCCCCCC
29.1228689409
891PhosphorylationYSRNTEHSMNYQYR-
CCCCCCCCCCCCCC-
11.5127097102

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
188TPhosphorylationKinasePKR-Uniprot
315TPhosphorylationKinasePKR-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
188TPhosphorylation

-
315TPhosphorylation

-

Disease-associated PTM Sites based on SAP

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

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of ILF3_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ILF3_RAT !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ILF3_RAT

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Related Literatures of Post-Translational Modification

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