IFIT5
entrez
24138
canonical
uniprot
Q13325
canonical
ensembl
ENSG00000152778
resolver
ensp
ENSP00000360860
resolver
genesymbol
IFIT5
resolver
genesymbol_syn
ISG58
resolver
genesymbol_syn
RI58
resolver
hgnc
HGNC:13328
resolver
uniprot
B2R5X9
resolver
uniprot
B4DDV1
resolver
uniprot
Q5T7I9
resolver
uniprot
Q6IAX3
resolver
uniprot_entry
IFIT5_HUMAN
resolver
uniprot_sec
B2R5X9
resolver
uniprot_sec
B4DDV1
resolver
uniprot_sec
Q5T7I9
resolver
uniprot_sec
Q6IAX3
resolver
amino_acid_sequence
MSEIRKDTLKAILLELECHFTWNLLKEDIDLFEVEDTIGQQLEFLTTKSRLALYNLLAYVKHLKGQNKDALECLEQAEEIIQQEHSDKEEVRSLVTWGNYAWVYYHMDQLEEAQKYTGKIGNVCKKLSSPSNYKLECPETDCEKGWALLKFGGKYYQKAKAAFEKALEVEPDNPEFNIGYAITVYRLDDSDREGSVKSFSLGPLRKAVTLNPDNSYIKVFLALKLQDVHAEAEGEKYIEEILDQISSQPYVLRYAAKFYRRKNSWNKALELLKKALEVTPTSSFLHHQMGLCYRAQMIQIKKATHNRPKGKDKLKVDELISSAIFHFKAAMERDSMFAFAYTDLANMYAEGGQYSNAEDIFRKALRLENITDDHKHQIHYHYGRFQEFHRKSENTAIHHYLEALKVKDRSPLRTKLTSALKKLSTKRLCHNALDVQSLSALGFVYKLEGEKRQAAEYYEKAQKIDPENAEFLTALCELRLSI
uniprot
proteins
function
FUNCTION: Interferon-induced RNA-binding protein involved in the human innate immune response. Has a broad and adaptable RNA structure recognition important for RNA recognition specificity in antiviral defense. Binds precursor and processed tRNAs as well as poly-U-tailed tRNA fragments (PubMed:23317505, PubMed:23774268, PubMed:25092312). Specifically binds single-stranded RNA bearing a 5'-triphosphate group (PPP-RNA), thereby acting as a sensor of viral single-stranded RNAs. Single-stranded PPP-RNAs, which lack 2'-O-methylation of the 5' cap and bear a 5'-triphosphate group instead, are specific from viruses, providing a molecular signature to distinguish between self and non-self mRNAs by the host during viral infection. Directly binds PPP-RNA in a non-sequence-specific manner (PubMed:23334420). Also recognizes and selectively binds AT-rich dsDNA (PubMed:23774268). Additionally, as a mediator in innate immunity, positively regulates IKK-NFKB signaling by sinergizing the recruitment of IKK to MAP3K7 (PubMed:26334375). {ECO:0000269|PubMed:23317505, ECO:0000269|PubMed:23334420, ECO:0000269|PubMed:23774268, ECO:0000269|PubMed:25092312, ECO:0000269|PubMed:26334375}.
uniprot
proteins
mass_dalton
55847
uniprot
proteins
mutagenesis
MUTAGEN 33; /note="E->A: No effect on RNA-binding but changes size profile of RNA bound. Reduces PPP-RNA-binding."; /evidence="ECO:0000269|PubMed:23334420, ECO:0000269|PubMed:25092312"; MUTAGEN 37; /note="T->A,V: No effect on RNA-binding but changes size profile of RNA bound."; /evidence="ECO:0000269|PubMed:25092312"; MUTAGEN 37; /note="T->V: Abolishes PPP-RNA-binding."; MUTAGEN 41; /note="Q->E: No effect on RNA-binding but changes size profile of RNA bound. Abolishes PPP-RNA-binding."; /evidence="ECO:0000269|PubMed:23334420, ECO:0000269|PubMed:25092312"; MUTAGEN 48; /note="K->A,E: Inhibits RNA-binding."; /evidence="ECO:0000269|PubMed:25092312"; MUTAGEN 150; /note="K->M: Abolishes PPP-RNA-binding."; /evidence="ECO:0000269|PubMed:23334420"; MUTAGEN 150; /note="K->N,E: Inhibits RNA-binding."; /evidence="ECO:0000269|PubMed:25092312"; MUTAGEN 150; /note="K->R: Reduces RNA-binding."; /evidence="ECO:0000269|PubMed:25092312"; MUTAGEN 156; /note="Y->F,A: No effect on RNA-binding. Reduces PPP-RNA-binding."; /evidence="ECO:0000269|PubMed:23334420, ECO:0000269|PubMed:25092312"; MUTAGEN 185..186; /note="YR->AE: Reduces binding to RNA and DNA."; /evidence="ECO:0000269|PubMed:23774268"; MUTAGEN 186; /note="R->H,A: Abolishes RNA-binding."; /evidence="ECO:0000269|PubMed:23334420, ECO:0000269|PubMed:25092312"; MUTAGEN 250; /note="Y->F: No effect on RNA-binding but changes size profile of RNA bound. Abolishes PPP-RNA-binding."; /evidence="ECO:0000269|PubMed:23334420, ECO:0000269|PubMed:25092312"; MUTAGEN 253..254; /note="RY->EA: Reduces binding to RNA and DNA."; /evidence="ECO:0000269|PubMed:23774268"; MUTAGEN 253; /note="R->M: Abolishes RNA-binding."; /evidence="ECO:0000269|PubMed:23334420, ECO:0000269|PubMed:25092312"; MUTAGEN 254; /note="Y->F: Abolishes RNA-binding."; /evidence="ECO:0000269|PubMed:23334420, ECO:0000269|PubMed:25092312"; MUTAGEN 257; /note="K->E: Reduces binding to RNA and DNA."; /evidence="ECO:0000269|PubMed:23774268"; MUTAGEN 260; /note="R->E: Abolishes PPP-RNA-binding."; /evidence="ECO:0000269|PubMed:23334420"; MUTAGEN 284; /note="F->A: Strongly reduces binding to dsDNA. No effect on ssRNA binding."; /evidence="ECO:0000269|PubMed:23774268"; MUTAGEN 287; /note="H->A: Reduces PPP-RNA-binding."; /evidence="ECO:0000269|PubMed:23334420"; MUTAGEN 288; /note="Q->E: Abolishes RNA-binding."; /evidence="ECO:0000269|PubMed:23334420, ECO:0000269|PubMed:25092312"; MUTAGEN 291; /note="L->A: No effect RNA-binding."; /evidence="ECO:0000269|PubMed:23317505, ECO:0000269|PubMed:25092312"; MUTAGEN 294; /note="R->E: Strongly reduces binding to dsDNA. No effect on ssRNA binding."; /evidence="ECO:0000269|PubMed:23774268"; MUTAGEN 302; /note="K->A: Reduces RNA-binding."; /evidence="ECO:0000269|PubMed:23317505"; MUTAGEN 307; /note="R->A: Reduces RNA-binding. 25 fold reduction in tRNA-binding."; /evidence="ECO:0000269|PubMed:23317505, ECO:0000269|PubMed:25092312"; MUTAGEN 309; /note="K->A: Reduces RNA-binding."; /evidence="ECO:0000269|PubMed:23317505"; MUTAGEN 334; /note="D->A: No effect on RNA-binding but changes size profile of RNA bound."; /evidence="ECO:0000269|PubMed:25092312"; MUTAGEN 337..339; /note="FAF->AAA: Reduces binding to RNA and DNA."; /evidence="ECO:0000269|PubMed:23774268"; MUTAGEN 337; /note="F->A: Abolishes PPP-RNA-binding."; /evidence="ECO:0000269|PubMed:23334420"; MUTAGEN 339; /note="F->A: Reduces RNA-binding."; /evidence="ECO:0000269|PubMed:25092312"; MUTAGEN 384; /note="R->E: Reduces binding to RNA and DNA and impairs antiviral activity; when associated with E-415."; /evidence="ECO:0000269|PubMed:23774268"; MUTAGEN 388..389; /note="FH->AA: Reduces RNA-binding."; /evidence="ECO:0000269|PubMed:23317505"; MUTAGEN 415; /note="K->A: Reduces RNA-binding. 25 fold reduction in tRNA-binding."; /evidence="ECO:0000269|PubMed:23317505, ECO:0000269|PubMed:25092312"; MUTAGEN 415; /note="K->E: Reduces binding to RNA and DNA and impairs antiviral activity; when associated with E-384."; /evidence="ECO:0000269|PubMed:23774268"; MUTAGEN 422..426; /note="KLSTK->ELSTE: Reduces binding to RNA and DNA."; /evidence="ECO:0000269|PubMed:23774268"; MUTAGEN 422; /note="K->A: Reduced RNA-binding."; /evidence="ECO:0000269|PubMed:23317505, ECO:0000269|PubMed:25092312"; MUTAGEN 426; /note="K->A: Reduces RNA-binding. 5 fold reduction in tRNA-binding."; /evidence="ECO:0000269|PubMed:23317505
uniprot
proteins
protein_family
IFIT family
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15164054
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
20950130
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21642987
uniprot
proteins
pubmed
23317505
uniprot
proteins
pubmed
23334420
uniprot
proteins
pubmed
23774268
uniprot
proteins
pubmed
25092312
uniprot
proteins
pubmed
26334375
uniprot
proteins
pubmed
9398535
uniprot
proteins
sequence_length
482
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell projection, ruffle membrane {ECO:0000269|PubMed:23317505}. Note=Colocalized with RIGI at cell surface ruffles. Localizes to actin-rich protrusions from the apical cell surface.
uniprot
proteins