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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9BYX4: Variant p.Arg779His

Interferon-induced helicase C domain-containing protein 1
Gene: IFIH1
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Variant information Variant position: help 779 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LP/P [Disclaimer] 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: help From Arginine (R) to Histidine (H) at position 779 (R779H, p.Arg779His). 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: help Change from large size and basic (R) to medium size and polar (H) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 0 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: help In AGS7; enhances the interferon signaling pathway activation; enhances the stability of filament formation; enhances dsRNA binding activity; enhances IFNB1 promoter activation; no loss of ATP hydrolysis. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 779 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 1025 The length of the canonical sequence.
Location on the sequence: help HSSEFKPMTQNEQKEVISKF R TGKINLLIATTVAEEGLDIK 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences. 
Human                         HSSEFKPMTQNEQKEVISKFRTGKINLLIATTVAEEGLDIK

Mouse                         HSSEVKPMTQTEQKEVISKFRTGEINLLIATTVAEEGLDIK
Sequence annotation in neighborhood: help 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 – 1025 Interferon-induced helicase C domain-containing protein 1
Domain 700 – 882 Helicase C-terminal
Alternative sequence 222 – 1025 Missing. In isoform 2.



Literature citations
Aicardi-Goutieres syndrome is caused by IFIH1 mutations.
Oda H.; Nakagawa K.; Abe J.; Awaya T.; Funabiki M.; Hijikata A.; Nishikomori R.; Funatsuka M.; Ohshima Y.; Sugawara Y.; Yasumi T.; Kato H.; Shirai T.; Ohara O.; Fujita T.; Heike T.;
Am. J. Hum. Genet. 95:121-125(2014)
Cited for: INVOLVEMENT IN AGS7; VARIANTS AGS7 PHE-372; THR-452 AND HIS-779; CHARACTERIZATION OF VARIANTS AGS7 PHE-372; THR-452 AND HIS-779; 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;
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.