UniProtKB/SwissProt variant VAR

Variant information

Variant position:

393

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

Type of variant:

Disease [Disclaimer]

The variants are classified into three categories: Disease, Polymorphism and Unclassified.

Disease: Variants implicated in disease according to literature reports.
Polymorphism: Variants not reported to be implicated in disease.
Unclassified: Variants with uncertain implication in disease according to literature reports. Evidence against or in favor of a pathogenic role is limited and/or conflicting.

Residue change:

From Aspartate (D) to Valine (V) at position 393 (D393V, p.Asp393Val).

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 (D) to medium size and hydrophobic (V)

The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:

-3

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

Variant description:

In AGS7; enhances the interferon signaling pathway activation; enhances the stability of filament formation; enhances dsRNA binding activity; no loss of ATP hydrolysis.

Any additional useful information about the variant.

Other resources:

Links to websites of interest for the variant.

Variant rs587777449 [ dbSNP | Ensembl ]

Sequence information

Variant position:

393

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

Protein sequence length:

1025

The length of the canonical sequence.

Location on the sequence:

FRKEFQPFLKKWYRVIGLSG D TQLKISFPEVVKSCDIIIST

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                         FRKEFQPFLKKWYRVIGLSGDTQLKISFPEVVKSCDIIIST

Mouse                         FRKEFNPYLKKWYRIIGLSGDTQLKISFPEVVKSYDVIIST

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 – 1025	Interferon-induced helicase C domain-containing protein 1
Domain	316 – 509	Helicase ATP-binding
Alternative sequence	222 – 1025	Missing. In isoform 2.

Literature citations

Gain-of-function mutations in IFIH1 cause a spectrum of human disease phenotypes associated with upregulated type I interferon signaling.
Rice G.I.; del Toro Duany Y.; Jenkinson E.M.; Forte G.M.; Anderson B.H.; Ariaudo G.; Bader-Meunier B.; Baildam E.M.; Battini R.; Beresford M.W.; Casarano M.; Chouchane M.; Cimaz R.; Collins A.E.; Cordeiro N.J.; Dale R.C.; Davidson J.E.; De Waele L.; Desguerre I.; Faivre L.; Fazzi E.; Isidor B.; Lagae L.; Latchman A.R.; Lebon P.; Li C.; Livingston J.H.; Lourenco C.M.; Mancardi M.M.; Masurel-Paulet A.; McInnes I.B.; Menezes M.P.; Mignot C.; O'Sullivan J.; Orcesi S.; Picco P.P.; Riva E.; Robinson R.A.; Rodriguez D.; Salvatici E.; Scott C.; Szybowska M.; Tolmie J.L.; Vanderver A.; Vanhulle C.; Vieira J.P.; Webb K.; Whitney R.N.; Williams S.G.; Wolfe L.A.; Zuberi S.M.; Hur S.; Crow Y.J.;
Nat. Genet. 46:503-509(2014)
Cited for: INVOLVEMENT IN AGS7; VARIANTS AGS7 GLY-337; VAL-393; ARG-495; GLN-720; HIS-779 AND CYS-779; CHARACTERIZATION OF VARIANTS AGS7 GLY-337; VAL-393; ARG-495; GLN-720; HIS-779 AND CYS-779;

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9BYX4: Variant p.Asp393Val