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 FRKEFQPFLKKWYRVIGLSGD TQLKISFPEVVKSCDIIIST
Mouse FRKEFNPYLKKWYRIIGLSGD TQLKISFPEVVKSYDVIIST
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;
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.