Q12906 · ILF3_HUMAN
- ProteinInterleukin enhancer-binding factor 3
- GeneILF3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids894 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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).
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).
(Microbial infection) Plays a positive role in HIV-1 virus production by binding to and thereby stabilizing HIV-1 RNA, together with ILF3.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | extracellular region | |
Cellular Component | membrane | |
Cellular Component | mitochondrion | |
Cellular Component | nucleolus | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Cellular Component | ribonucleoprotein complex | |
Molecular Function | DNA binding | |
Molecular Function | double-stranded RNA binding | |
Molecular Function | mRNA 3'-UTR AU-rich region binding | |
Molecular Function | RNA binding | |
Molecular Function | single-stranded RNA binding | |
Molecular Function | virus receptor activity | |
Biological Process | defense response to virus | |
Biological Process | negative regulation of DNA-templated transcription | |
Biological Process | negative regulation of translation | |
Biological Process | negative regulation of viral genome replication | |
Biological Process | positive regulation of DNA-templated transcription | |
Biological Process | protein phosphorylation | |
Biological Process | spliceosome-depend formation of circular RNA |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameInterleukin enhancer-binding factor 3
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ12906
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: 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-ILF3 complex resulting in a cytoplasmic sequestration of ILF3. Localized in cytoplasmic mRNP granules containing untranslated mRNAs.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_022159 | 50 | in dbSNP:rs1064493 | |||
Sequence: D → H | ||||||
Natural variant | VAR_048906 | 501 | in dbSNP:rs34520379 | |||
Sequence: A → S |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,000 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue, cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000126070 | 1-894 | UniProt | Interleukin enhancer-binding factor 3 | |||
Sequence: MRPMRIFVNDDRHVMAKHSSVYPTQEELEAVQNMVSHTERALKAVSDWIDEQEKGSSEQAESDNMDVPPEDDSKEGAGEQKTEHMTRTLRGVMRVGLVAKGLLLKGDLDLELVLLCKEKPTTALLDKVADNLAIQLAAVTEDKYEILQSVDDAAIVIKNTKEPPLSLTIHLTSPVVREEMEKVLAGETLSVNDPPDVLDRQKCLAALASLRHAKWFQARANGLKSCVIVIRVLRDLCTRVPTWGPLRGWPLELLCEKSIGTANRPMGAGEALRRVLECLASGIVMPDGSGIYDPCEKEATDAIGHLDRQQREDITQSAQHALRLAAFGQLHKVLGMDPLPSKMPKKPKNENPVDYTVQIPPSTTYAITPMKRPMEEDGEEKSPSKKKKKIQKKEEKAEPPQAMNALMRLNQLKPGLQYKLVSQTGPVHAPIFTMSVEVDGNSFEASGPSKKTAKLHVAVKVLQDMGLPTGAEGRDSSKGEDSAEETEAKPAVVAPAPVVEAVSTPSAAFPSDATAEQGPILTKHGKNPVMELNEKRRGLKYELISETGGSHDKRFVMEVEVDGQKFQGAGSNKKVAKAYAALAALEKLFPDTPLALDANKKKRAPVPVRGGPKFAAKPHNPGFGMGGPMHNEVPPPPNLRGRGRGGSIRGRGRGRGFGGANHGGYMNAGAGYGSYGYGGNSATAGYSQFYSNGGHSGNASGGGGGGGGGSSGYGSYYQGDNYNSPVPPKHAGKKQPHGGQQKPSYGSGYQSHQGQQQSYNQSPYSNYGPPQGKQKGYNHGQGSYSYSNSYNSPGGGGGSDYNYESKFNYSGSGGRSGGNSYGSGGASYNPGSHGGYGGGSGGGSSYQGKQGGYSQSNYNSPGSGQNYSGPPSSYQSSQGGYGRNADHSMNYQYR | |||||||
Modified residue (large scale data) | 22 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 62 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 62 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 73 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 100 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 188 | UniProt | Phosphothreonine; by PKR | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 188 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 190 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 190 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 297 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Modified residue | 315 | UniProt | Phosphothreonine; by PKR | ||||
Sequence: T | |||||||
Cross-link | 348 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 362 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 368 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 382 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 382 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 384 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 384 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 396 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 460 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 469 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 476 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 476 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 477 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 477 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 482 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 482 | UniProt | In isoform Q12906-4; Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 482 | UniProt | In isoform Q12906-6; Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 482 | UniProt | In isoform Q12906-7; Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 482 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 486 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Cross-link | 489 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 504 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 506 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 592 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 592 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 762 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 792 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 792 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 799 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 810 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 810 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 812 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 812 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 816 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 860 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 863 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 888 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated at Thr-188 and Thr-315 by PKR in response to certain RNA viruses. This phosphorylation results in the dissociation of ILF2 from the ILF2-ILF3 complex resulting in a cytoplasmic sequestration of ILF3 where it can bind to viral RNAs and impede viral replication.
Methylated by protein arginine N-methyltransferase 1.
Ubiquitinated at Lys-297 in a TRIM47-dependent manner; this 'Lys-48'-linked ubiquitination promotes ILF3 degradation.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Ubiquitous.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with FUS and SMN. Interacts (via C-terminus) with PRMT1. Forms a complex with ILF2. Can also bind to PRKDC/XRCC7: this may stabilize the interaction of PRKDC/XRCC7 and the heterodimeric complex of XRCC6/KU70 and XRCC5/KU80. Forms a heteromeric complex with ZNF346 and ILF3. Found in a nuclear export complex with XPO5, ILF3, Ran and double-stranded RNA or double-stranded minihelix VA1 RNA. Found in a nuclear export complex with XPO5, RAN, ILF3, ZNF346 and double-stranded RNA. Interacts with XPO5 and ZNF346. Forms a complex with ILF2, YLPM1, KHDRBS1, RBMX, NCOA5 and PPP1CA. Interacts with AGO1 and AGO2. Interacts with DHX36; this interaction occurs in a RNA-dependent manner (PubMed:14731398).
Interacts with ELAVL1; this interaction occurs in a RNA-dependent manner (PubMed:14731398).
Interacts with HAVCR2; this interaction promotes ILF3 ubiquitination and subsequent degradation (PubMed:34110282).
Interacts with ELAVL1; this interaction occurs in a RNA-dependent manner (PubMed:14731398).
Interacts with HAVCR2; this interaction promotes ILF3 ubiquitination and subsequent degradation (PubMed:34110282).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q12906 | HNRNPA2B1 P22626 | 3 | EBI-78756, EBI-299649 | |
BINARY | Q12906 | HNRNPL P14866-1 | 2 | EBI-78756, EBI-16071645 | |
XENO | Q12906 | M P08325 | 2 | EBI-78756, EBI-15693250 | |
XENO | Q12906 | NS P03496 | 3 | EBI-78756, EBI-2547442 | |
BINARY | Q12906 | PRMT1 Q99873 | 3 | EBI-78756, EBI-78738 | |
XENO | Q12906 | VP35 Q05127 | 6 | EBI-78756, EBI-6148294 | |
BINARY | Q12906-6 | TARDBP Q13148 | 6 | EBI-12904528, EBI-372899 | |
BINARY | Q12906-6 | VPS37C A5D8V6 | 3 | EBI-12904528, EBI-2559305 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 5-378 | DZF | ||||
Sequence: RIFVNDDRHVMAKHSSVYPTQEELEAVQNMVSHTERALKAVSDWIDEQEKGSSEQAESDNMDVPPEDDSKEGAGEQKTEHMTRTLRGVMRVGLVAKGLLLKGDLDLELVLLCKEKPTTALLDKVADNLAIQLAAVTEDKYEILQSVDDAAIVIKNTKEPPLSLTIHLTSPVVREEMEKVLAGETLSVNDPPDVLDRQKCLAALASLRHAKWFQARANGLKSCVIVIRVLRDLCTRVPTWGPLRGWPLELLCEKSIGTANRPMGAGEALRRVLECLASGIVMPDGSGIYDPCEKEATDAIGHLDRQQREDITQSAQHALRLAAFGQLHKVLGMDPLPSKMPKKPKNENPVDYTVQIPPSTTYAITPMKRPMEEDG | ||||||
Region | 50-86 | Disordered | ||||
Sequence: DEQEKGSSEQAESDNMDVPPEDDSKEGAGEQKTEHMT | ||||||
Compositional bias | 67-86 | Basic and acidic residues | ||||
Sequence: VPPEDDSKEGAGEQKTEHMT | ||||||
Region | 363-401 | Disordered | ||||
Sequence: TTYAITPMKRPMEEDGEEKSPSKKKKKIQKKEEKAEPPQ | ||||||
Motif | 371-389 | Bipartite nuclear localization signal | ||||
Sequence: KRPMEEDGEEKSPSKKKKK | ||||||
Compositional bias | 372-399 | Basic and acidic residues | ||||
Sequence: RPMEEDGEEKSPSKKKKKIQKKEEKAEP | ||||||
Domain | 398-467 | DRBM 1 | ||||
Sequence: EPPQAMNALMRLNQLKPGLQYKLVSQTGPVHAPIFTMSVEVDGNSFEASGPSKKTAKLHVAVKVLQDMGL | ||||||
Region | 466-524 | Disordered | ||||
Sequence: GLPTGAEGRDSSKGEDSAEETEAKPAVVAPAPVVEAVSTPSAAFPSDATAEQGPILTKH | ||||||
Domain | 524-590 | DRBM 2 | ||||
Sequence: HGKNPVMELNEKRRGLKYELISETGGSHDKRFVMEVEVDGQKFQGAGSNKKVAKAYAALAALEKLFP | ||||||
Region | 609-894 | Interaction with PRMT1 | ||||
Sequence: RGGPKFAAKPHNPGFGMGGPMHNEVPPPPNLRGRGRGGSIRGRGRGRGFGGANHGGYMNAGAGYGSYGYGGNSATAGYSQFYSNGGHSGNASGGGGGGGGGSSGYGSYYQGDNYNSPVPPKHAGKKQPHGGQQKPSYGSGYQSHQGQQQSYNQSPYSNYGPPQGKQKGYNHGQGSYSYSNSYNSPGGGGGSDYNYESKFNYSGSGGRSGGNSYGSGGASYNPGSHGGYGGGSGGGSSYQGKQGGYSQSNYNSPGSGQNYSGPPSSYQSSQGGYGRNADHSMNYQYR | ||||||
Region | 625-660 | Disordered | ||||
Sequence: MGGPMHNEVPPPPNLRGRGRGGSIRGRGRGRGFGGA | ||||||
Region | 718-894 | Disordered | ||||
Sequence: QGDNYNSPVPPKHAGKKQPHGGQQKPSYGSGYQSHQGQQQSYNQSPYSNYGPPQGKQKGYNHGQGSYSYSNSYNSPGGGGGSDYNYESKFNYSGSGGRSGGNSYGSGGASYNPGSHGGYGGGSGGGSSYQGKQGGYSQSNYNSPGSGQNYSGPPSSYQSSQGGYGRNADHSMNYQYR | ||||||
Compositional bias | 740-827 | Polar residues | ||||
Sequence: QQKPSYGSGYQSHQGQQQSYNQSPYSNYGPPQGKQKGYNHGQGSYSYSNSYNSPGGGGGSDYNYESKFNYSGSGGRSGGNSYGSGGAS | ||||||
Compositional bias | 843-894 | Polar residues | ||||
Sequence: GSSYQGKQGGYSQSNYNSPGSGQNYSGPPSSYQSSQGGYGRNADHSMNYQYR |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 7 isoforms produced by Alternative splicing.
Q12906-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- SynonymsNFAR-2, ILF3-E
- Length894
- Mass (Da)95,338
- Last updated2005-04-12 v3
- Checksum20903ABD0331F370
Q12906-2
- Name2
- SynonymsNFAR-1, DRBP76
Q12906-3
- Name3
- NoteDubious isoform produced through aberrant splice sites.
Q12906-4
- Name4
- SynonymsDRBP76 Alpha, ILF3-A
Q12906-5
- Name5
- SynonymsDRBP76 Delta, Gamma, ILF3-C
Q12906-6
- Name6
Q12906-7
- Name7
- Differences from canonical
- 516-516: E → ENVKQ
Computationally mapped potential isoform sequences
There are 12 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
K7EJ09 | K7EJ09_HUMAN | ILF3 | 122 | ||
K7EKJ9 | K7EKJ9_HUMAN | ILF3 | 254 | ||
K7EKY0 | K7EKY0_HUMAN | ILF3 | 158 | ||
K7EM82 | K7EM82_HUMAN | ILF3 | 99 | ||
K7ELV3 | K7ELV3_HUMAN | ILF3 | 116 | ||
K7ENK6 | K7ENK6_HUMAN | ILF3 | 79 | ||
K7EMZ8 | K7EMZ8_HUMAN | ILF3 | 113 | ||
K7EPG3 | K7EPG3_HUMAN | ILF3 | 73 | ||
K7EQ75 | K7EQ75_HUMAN | ILF3 | 55 | ||
K7EQR9 | K7EQR9_HUMAN | ILF3 | 180 | ||
K7ER69 | K7ER69_HUMAN | ILF3 | 161 | ||
K7ERM6 | K7ERM6_HUMAN | ILF3 | 77 |
Sequence caution
Features
Showing features for compositional bias, sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 67-86 | Basic and acidic residues | ||||
Sequence: VPPEDDSKEGAGEQKTEHMT | ||||||
Sequence conflict | 101 | in Ref. 5; AAD51098/AAD51099 and 6; AAK07424/AAK07425 | ||||
Sequence: G → C | ||||||
Sequence conflict | 260 | in Ref. 2; AAD33966 and 11; CAA66918 | ||||
Sequence: G → V | ||||||
Compositional bias | 372-399 | Basic and acidic residues | ||||
Sequence: RPMEEDGEEKSPSKKKKKIQKKEEKAEP | ||||||
Alternative sequence | VSP_003883 | 516 | in isoform 4, isoform 6 and isoform 7 | |||
Sequence: E → ENVKQ | ||||||
Sequence conflict | 647 | in Ref. 2; AAD33966 and 6; AAK07424/AAK07425 | ||||
Sequence: S → T | ||||||
Alternative sequence | VSP_003886 | 687-690 | in isoform 5 | |||
Sequence: SQFY → TGFV | ||||||
Sequence conflict | 688-689 | in Ref. 13; AAF82687 | ||||
Sequence: QF → N | ||||||
Alternative sequence | VSP_003884 | 688-694 | in isoform 4 | |||
Sequence: QFYSNGG → KCAFLSV | ||||||
Alternative sequence | VSP_003888 | 688-702 | in isoform 2 and isoform 6 | |||
Sequence: QFYSNGGHSGNASGG → DFFTDCYGYHDFGSS | ||||||
Alternative sequence | VSP_003890 | 690-764 | in isoform 3 | |||
Sequence: YSNGGHSGNASGGGGGGGGGSSGYGSYYQGDNYNSPVPPKHAGKKQPHGGQQKPSYGSGYQSHQGQQQSYNQSPY → SRPPPPSRPRCCVVRCSGSPCGPSCDPYLAVFGTPCLQWFVSCHYNFVWVEFLSFCSSVSLCLFTLRVSGNSVCL | ||||||
Alternative sequence | VSP_003887 | 691-894 | in isoform 5 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_003885 | 695-894 | in isoform 4 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_003889 | 703-894 | in isoform 2 and isoform 6 | |||
Sequence: Missing | ||||||
Compositional bias | 740-827 | Polar residues | ||||
Sequence: QQKPSYGSGYQSHQGQQQSYNQSPYSNYGPPQGKQKGYNHGQGSYSYSNSYNSPGGGGGSDYNYESKFNYSGSGGRSGGNSYGSGGAS | ||||||
Sequence conflict | 763 | in Ref. 4; CAC01407 | ||||
Sequence: P → L | ||||||
Alternative sequence | VSP_003891 | 765-894 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 797 | in Ref. 4; CAC01124 and 6; AAK07425 | ||||
Sequence: G → R | ||||||
Sequence conflict | 799 | in Ref. 13; AAF82685 | ||||
Sequence: S → SGS | ||||||
Sequence conflict | 813 | in Ref. 6; AAK07425 | ||||
Sequence: G → E | ||||||
Compositional bias | 843-894 | Polar residues | ||||
Sequence: GSSYQGKQGGYSQSNYNSPGSGQNYSGPPSSYQSSQGGYGRNADHSMNYQYR |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U10324 EMBL· GenBank· DDBJ | AAA20994.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
AF147209 EMBL· GenBank· DDBJ | AAD33966.1 EMBL· GenBank· DDBJ | mRNA | ||
AF141870 EMBL· GenBank· DDBJ | AAD37575.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ271741 EMBL· GenBank· DDBJ | CAC01121.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ271741 EMBL· GenBank· DDBJ | CAC01122.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ271741 EMBL· GenBank· DDBJ | CAC01123.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ271741 EMBL· GenBank· DDBJ | CAC01124.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ271744 EMBL· GenBank· DDBJ | CAC01404.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ271745 EMBL· GenBank· DDBJ | CAC01405.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ271746 EMBL· GenBank· DDBJ | CAC01406.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ271747 EMBL· GenBank· DDBJ | CAC01407.1 EMBL· GenBank· DDBJ | mRNA | ||
AF167569 EMBL· GenBank· DDBJ | AAD51098.1 EMBL· GenBank· DDBJ | mRNA | ||
AF167570 EMBL· GenBank· DDBJ | AAD51099.1 EMBL· GenBank· DDBJ | mRNA | ||
AF320244 EMBL· GenBank· DDBJ | AAK07424.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF320228 EMBL· GenBank· DDBJ | AAK07424.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF320229 EMBL· GenBank· DDBJ | AAK07424.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF320230 EMBL· GenBank· DDBJ | AAK07424.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF320231 EMBL· GenBank· DDBJ | AAK07424.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF320232 EMBL· GenBank· DDBJ | AAK07424.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF320233 EMBL· GenBank· DDBJ | AAK07424.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF320234 EMBL· GenBank· DDBJ | AAK07424.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF320235 EMBL· GenBank· DDBJ | AAK07424.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF320236 EMBL· GenBank· DDBJ | AAK07424.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF320237 EMBL· GenBank· DDBJ | AAK07424.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF320238 EMBL· GenBank· DDBJ | AAK07424.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF320239 EMBL· GenBank· DDBJ | AAK07424.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF320240 EMBL· GenBank· DDBJ | AAK07424.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF320241 EMBL· GenBank· DDBJ | AAK07424.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF320242 EMBL· GenBank· DDBJ | AAK07424.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF320243 EMBL· GenBank· DDBJ | AAK07424.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF320247 EMBL· GenBank· DDBJ | AAK07425.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF320228 EMBL· GenBank· DDBJ | AAK07425.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF320229 EMBL· GenBank· DDBJ | AAK07425.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF320230 EMBL· GenBank· DDBJ | AAK07425.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF320231 EMBL· GenBank· DDBJ | AAK07425.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF320232 EMBL· GenBank· DDBJ | AAK07425.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF320233 EMBL· GenBank· DDBJ | AAK07425.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF320234 EMBL· GenBank· DDBJ | AAK07425.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF320235 EMBL· GenBank· DDBJ | AAK07425.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF320236 EMBL· GenBank· DDBJ | AAK07425.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF320237 EMBL· GenBank· DDBJ | AAK07425.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF320238 EMBL· GenBank· DDBJ | AAK07425.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF320239 EMBL· GenBank· DDBJ | AAK07425.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF320240 EMBL· GenBank· DDBJ | AAK07425.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF320241 EMBL· GenBank· DDBJ | AAK07425.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF320242 EMBL· GenBank· DDBJ | AAK07425.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF320243 EMBL· GenBank· DDBJ | AAK07425.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF320245 EMBL· GenBank· DDBJ | AAK07425.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF320246 EMBL· GenBank· DDBJ | AAK07425.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK291617 EMBL· GenBank· DDBJ | BAF84306.1 EMBL· GenBank· DDBJ | mRNA | ||
AC011475 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471106 EMBL· GenBank· DDBJ | EAW84132.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC048314 EMBL· GenBank· DDBJ | AAH48314.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
BC064836 EMBL· GenBank· DDBJ | AAH64836.1 EMBL· GenBank· DDBJ | mRNA | ||
X98264 EMBL· GenBank· DDBJ | CAA66917.1 EMBL· GenBank· DDBJ | mRNA | ||
X98265 EMBL· GenBank· DDBJ | CAA66918.1 EMBL· GenBank· DDBJ | mRNA | ||
AF202445 EMBL· GenBank· DDBJ | AAF82685.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF202445 EMBL· GenBank· DDBJ | AAF82686.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF202445 EMBL· GenBank· DDBJ | AAF82687.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF007140 EMBL· GenBank· DDBJ | AAC19152.1 EMBL· GenBank· DDBJ | mRNA |