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UniProtKB/Swiss-Prot Q14653: Variant p.Glu377Lys

Interferon regulatory factor 3
Gene: IRF3
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Variant information Variant position: help 377
Type of variant: help LB/B
Residue change: help From Glutamate (E) to Lysine (K) at position 377 (E377K, p.Glu377Lys).
Physico-chemical properties: help Change from medium size and acidic (E) to large size and basic (K)
BLOSUM score: help 1
Other resources: help


Sequence information Variant position: help 377
Protein sequence length: help 427
Location on the sequence: help PWTKRLVMVKVVPTCLRALV E MARVGGASSLENTVDLHISN
Residue conservation: help 
Human                         PWTKRLVMVKVVPTCLRALVEMARVGGASSLEN-TVDLHISN

Mouse                         PWVKRLVMVKVVPTCLKELLEMAREGGASSLK--TVDLHIS

Pig                           PWVKRLVMVKVVPMCLRALVDMARDGGASSLEN-TVDLHIS

Bovine                        PWIKRLVMVKVVPMCLRVLVDIARQGGASSLEN-TVDLHIS

Chicken                       PKESKLILVKLVPQFCEYWYEQVQRGGASSLNSGNVSLQLS
Sequence annotation in neighborhood: help
TypePositionsDescription
Chain 1 – 427 Interferon regulatory factor 3
Region 141 – 427 Mediates interaction with ZDHHC11
Modified residue 366 – 366 N6-acetyllysine
Modified residue 385 – 385 Phosphoserine
Modified residue 386 – 386 Diphosphoserine
Modified residue 386 – 386 Phosphoserine; by TBK1
Modified residue 396 – 396 Phosphoserine; by IKKE and TBK1
Cross 360 – 360 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)
Cross 366 – 366 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)
Alternative sequence 105 – 427 Missing. In isoform 5.
Alternative sequence 328 – 427 DLITFTEGSGRSPRYALWFCVGESWPQDQPWTKRLVMVKVVPTCLRALVEMARVGGASSLENTVDLHISNSHPLSLTSDQYKAYLQDLVEGMDFQGPGES -> GSWAPRSDYLHGRKRTLTTLCPLVLCGGVMAPGPAVDQEARDGQGCAHVPQGLGRNGPGRGCLLPGEYCGPAHFQQPPTLPHLRPVQGLPAGLGGGHGFPGPWGELSPRSSWCASNPPVPHHLNQ. In isoform 4.
Mutagenesis 360 – 360 K -> R. Highly diminished ISGylation; when associated with R-193 and R-366.
Mutagenesis 366 – 366 K -> R. Highly diminished ISGylation; when associated with R-193 and R-360.
Mutagenesis 385 – 385 S -> ADE. Complete loss of viral infection induced phosphorylation.
Mutagenesis 386 – 386 S -> A. Complete loss of viral infection induced phosphorylation. Abolished pyrophosphorylation.
Mutagenesis 386 – 386 S -> E. Phosphomimetic mutant; interacts with CREBBP; when associated with E-396.
Mutagenesis 390 – 390 T -> A. Does not affect pyrophosphorylation.
Mutagenesis 396 – 396 S -> E. Phosphomimetic mutant; interacts with CREBBP; when associated with E-386.
Helix 370 – 383



Literature citations
No reference for the current variant in UniProtKB/Swiss-Prot.
Disclaimer: Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.