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UniProtKB/Swiss-Prot Q14653: Variant p.Glu377Lys

Interferon regulatory factor 3
Gene: IRF3
Variant information

Variant position:  377
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  LB/B
The variants are classified into three categories: LP/P, LB/B and US.
  • LP/P: likely pathogenic or pathogenic.
  • LB/B: likely benign or benign.
  • US: uncertain significance

Residue change:  From Glutamate (E) to Lysine (K) at position 377 (E377K, p.Glu377Lys).
Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.

Physico-chemical properties:  Change from medium size and acidic (E) to large size and basic (K)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  1
The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:
  • Lowest score: -4 (low probability of substitution).
  • Highest score: 11 (high probability of substitution).
More information can be found on the following page

Other resources:  
Links to websites of interest for the variant.



Sequence information

Variant position:  377
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  427
The length of the canonical sequence.

Location on the sequence:   PWTKRLVMVKVVPTCLRALV  E MARVGGASSLENTVDLHISN
The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.

Residue conservation: 
The multiple alignment of the region surrounding the variant against various orthologous sequences.

Human                         PWTKRLVMVKVVPTCLRALVEMARVGGASSLEN-TVDLHISN

Mouse                         PWVKRLVMVKVVPTCLKELLEMAREGGASSLK--TVDLHIS

Pig                           PWVKRLVMVKVVPMCLRALVDMARDGGASSLEN-TVDLHIS

Bovine                        PWIKRLVMVKVVPMCLRVLVDIARQGGASSLEN-TVDLHIS

Chicken                       PKESKLILVKLVPQFCEYWYEQVQRGGASSLNSGNVSLQLS

Sequence annotation in neighborhood:  
The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:
  • Type: the type of sequence feature.
  • Positions: endpoints of the sequence feature.
  • Description: contains additional information about the feature.

TypePositionsDescription
Chain 1 – 427 Interferon regulatory factor 3
Region 141 – 427 Mediates interaction with ZDHHC11
Modified residue 385 – 385 Phosphoserine
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 -> ADE. Complete loss of viral infection induced phosphorylation.
Mutagenesis 386 – 386 S -> E. Phosphomimetic mutant; interacts with CREBBP; when associated with E-396.
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.