UniProtKB/Swiss-Prot Q14653: Variant p.Glu377Lys

Interferon regulatory factor 3
Gene: IRF3
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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.

Variant rs1049486 [ dbSNP | Ensembl ]

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.

Type	Positions	Description
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.