IFIT1
entrez
3434
canonical
uniprot
P09914
canonical
ensembl
ENSG00000185745
resolver
ensp
ENSP00000360869
resolver
ensp
ENSP00000441968
resolver
genesymbol
IFIT1
resolver
genesymbol_syn
G10P1
resolver
genesymbol_syn
IFI56
resolver
genesymbol_syn
IFNAI1
resolver
genesymbol_syn
ISG56
resolver
hgnc
HGNC:5407
resolver
uniprot
B3KS50
resolver
uniprot
D3DR31
resolver
uniprot
Q5T7J1
resolver
uniprot
Q96QM5
resolver
uniprot_entry
IFIT1_HUMAN
resolver
uniprot_sec
B3KS50
resolver
uniprot_sec
D3DR31
resolver
uniprot_sec
Q5T7J1
resolver
uniprot_sec
Q96QM5
resolver
amino_acid_sequence
MSTNGDDHQVKDSLEQLRCHFTWELSIDDDEMPDLENRVLDQIEFLDTKYSVGIHNLLAYVKHLKGQNEEALKSLKEAENLMQEEHDNQANVRSLVTWGNFAWMYYHMGRLAEAQTYLDKVENICKKLSNPFRYRMECPEIDCEEGWALLKCGGKNYERAKACFEKVLEVDPENPESSAGYAISAYRLDGFKLATKNHKPFSLLPLRQAVRLNPDNGYIKVLLALKLQDEGQEAEGEKYIEEALANMSSQTYVFRYAAKFYRRKGSVDKALELLKKALQETPTSVLLHHQIGLCYKAQMIQIKEATKGQPRGQNREKLDKMIRSAIFHFESAVEKKPTFEVAHLDLARMYIEAGNHRKAEENFQKLLCMKPVVEETMQDIHFHYGRFQEFQKKSDVNAIIHYLKAIKIEQASLTRDKSINSLKKLVLRKLRRKALDLESLSLLGFVYKLEGNMNEALEYYERALRLAADFENSVRQGP
uniprot
proteins
function
FUNCTION: Plays a key role in the innate immune response as part of an interferon-dependent multiprotein complex, recognizing and sequestering viral RNAs that lack host-specific 2'-O-methylation at their 5' cap. By distinguishing these RNAs from host mRNAs, inhibits their translation by competing with the translation initiation factor eIF4E (PubMed:21642987, PubMed:27240734, PubMed:39009378, PubMed:23334420, PubMed:28251928, PubMed:36285486). Could also prevent viral replication through its interaction with DNA replication origin-binding protein E1 of several viruses. Causes the translocation of E1 from the nucleus to the cytoplasm and can also inhibit its helicase activity in vitro (PubMed:19008854, PubMed:21976647). Exhibits antiviral activity against many viruses from the Flaviviridae (West Nile virus, Dengue virus, hepatitis C virus), Coronaviridae (human 229E coronavirus, SARS-CoV-2 and SARS-CoV), Poxviridae (vaccinia virus) and Togaviridae (Sindbis virus) families (PubMed:19008854, PubMed:21976647, PubMed:28251928, PubMed:36285486). {ECO:0000269|PubMed:19008854, ECO:0000269|PubMed:21642987, ECO:0000269|PubMed:21976647, ECO:0000269|PubMed:23334420, ECO:0000269|PubMed:28251928, ECO:0000269|PubMed:36285486, ECO:0000269|PubMed:39009378}.
uniprot
proteins
mass_dalton
55360
uniprot
proteins
mutagenesis
MUTAGEN 34; /note="D->A: Abolishes PPP-RNA-binding."; /evidence="ECO:0000269|PubMed:23334420"; MUTAGEN 38; /note="R->A: Loss of capped RNA-binding."; /evidence="ECO:0000269|PubMed:28251928"; MUTAGEN 38; /note="R->M: Abolishes PPP-RNA-binding."; /evidence="ECO:0000269|PubMed:23334420"; MUTAGEN 42; /note="Q->A: Decreased capped RNA-binding. Decreased translation inhibition of viral RNAs lacking 2'-O-methylation of the 5' cap."; /evidence="ECO:0000269|PubMed:28251928"; MUTAGEN 42; /note="Q->E: Reduced PPP-RNA-binding. Decreased capped RNA-binding. Decreased translation inhibition of viral RNAs lacking 2'-O-methylation of the 5' cap."; /evidence="ECO:0000269|PubMed:23334420, ECO:0000269|PubMed:28251928"; MUTAGEN 46; /note="L->A: Decreased capped RNA-binding. Decreased translation inhibition of viral RNAs lacking 2'-O-methylation of the 5' cap."; /evidence="ECO:0000269|PubMed:28251928"; MUTAGEN 48; /note="T->A: No effect on capped RNA-binding."; /evidence="ECO:0000269|PubMed:28251928"; MUTAGEN 147; /note="W->F: Decreased capped RNA-binding. Decreased translation inhibition of viral RNAs lacking 2'-O-methylation of the 5' cap."; /evidence="ECO:0000269|PubMed:28251928"; MUTAGEN 147; /note="W->M: Loss of capped RNA-binding. Loss of translation inhibition of viral RNAs lacking 2'-O-methylation of the 5' cap."; /evidence="ECO:0000269|PubMed:28251928"; MUTAGEN 151; /note="K->M: Loss of capped RNA-binding. Loss of translation inhibition of viral RNAs lacking 2'-O-methylation of the 5' cap."; /evidence="ECO:0000269|PubMed:23334420, ECO:0000269|PubMed:28251928"; MUTAGEN 157; /note="Y->F: Reduced PPP-RNA-binding. Reduced capped RNA-binding. Loss of capped RNA-binding and decreased translation inhibition of viral RNAs lacking 2'-O-methylation of the 5' cap; when associated with A-289. Loss of capped RNA-binding and decreased translation inhibition of viral RNAs lacking 2'-O-methylation of the 5' cap; when associated with E-290."; /evidence="ECO:0000269|PubMed:23334420, ECO:0000269|PubMed:28251928"; MUTAGEN 176; /note="E->A: Decreased capped RNA-binding. Decreased translation inhibition of viral RNAs lacking 2'-O-methylation of the 5' cap."; /evidence="ECO:0000269|PubMed:28251928"; MUTAGEN 187; /note="R->A: Loss of capped RNA-binding. Loss of translation inhibition of viral RNAs lacking 2'-O-methylation of the 5' cap."; /evidence="ECO:0000269|PubMed:21642987, ECO:0000269|PubMed:23334420, ECO:0000269|PubMed:28251928"; MUTAGEN 187; /note="R->H: Abolishes PPP-RNA-binding. Loss of capped RNA-binding. Loss of translation inhibition of viral RNAs lacking 2'-O-methylation of the 5' cap."; /evidence="ECO:0000269|PubMed:21642987, ECO:0000269|PubMed:23334420, ECO:0000269|PubMed:28251928"; MUTAGEN 216; /note="N->A: No effect on capped RNA-binding."; /evidence="ECO:0000269|PubMed:28251928"; MUTAGEN 216; /note="N->D: No effect on capped RNA-binding."; /evidence="ECO:0000269|PubMed:28251928"; MUTAGEN 218; /note="Y->A: Decreased capped RNA-binding. Decreased translation inhibition of viral RNAs lacking 2'-O-methylation of the 5' cap."; /evidence="ECO:0000269|PubMed:28251928"; MUTAGEN 255; /note="R->M: Abolishes PPP-RNA-binding."; /evidence="ECO:0000269|PubMed:23334420"; MUTAGEN 289; /note="H->A: Decreased capped RNA-binding. Loss of capped RNA-binding and decreased translation inhibition of viral RNAs lacking 2'-O-methylation of the 5' cap; when associated with F-157."; /evidence="ECO:0000269|PubMed:28251928"; MUTAGEN 290; /note="Q->E: Decreased capped RNA-binding. Loss of capped RNA-binding and decreased translation inhibition of viral RNAs lacking 2'-O-methylation of the 5' cap; when associated with F-157."; /evidence="ECO:0000269|PubMed:28251928
uniprot
proteins
post_translational_modification
PTM: Phosphorylated. {ECO:0000269|PubMed:19416887}.; PTM: ISGylated. {ECO:0000269|PubMed:16009940}.
uniprot
proteins
protein_family
IFIT family
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15164054
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16009940
uniprot
proteins
pubmed
16023166
uniprot
proteins
pubmed
19008854
uniprot
proteins
pubmed
19416887
uniprot
proteins
pubmed
21190939
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21612406
uniprot
proteins
pubmed
21642987
uniprot
proteins
pubmed
21976647
uniprot
proteins
pubmed
23334420
uniprot
proteins
pubmed
27240734
uniprot
proteins
pubmed
28251928
uniprot
proteins
pubmed
3121313
uniprot
proteins
pubmed
3360121
uniprot
proteins
pubmed
36285486
uniprot
proteins
pubmed
3753936
uniprot
proteins
pubmed
39009378
uniprot
proteins
pubmed
6186990
uniprot
proteins
sequence_length
478
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19008854, ECO:0000269|PubMed:21642987}.
uniprot
proteins