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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q7L2E3: Variant p.Arg782Trp

ATP-dependent RNA helicase DHX30
Gene: DHX30
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Variant information Variant position: help 782 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 Tryptophan (W) at position 782 (R782W, p.Arg782Trp). 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 large size and aromatic (W) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -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: help In NEDMIAL; changed localization to stress granules; decreased RNA-dependent ATPase activity; by inducing the formation of stress granules probably indirectly decreases global protein synthesis. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 782 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 1194 The length of the canonical sequence.
Location on the sequence: help KVSCLETVWVSRANVIQRRG R AGRCQSGFAYHLFPRSRLEK 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                         KVSCLETVWVSRANVIQRRGRAGRCQSGFAYHLFPRSRLEK

Mouse                         KVSCLETVWVSRANVIQRRGRAGRCQSGFAYHLFPRSRLEK

Rat                           KVSCLETVWVSRANVIQRRGRAGRCQSGFAYHLFPRSRLEK

Bovine                        KVSCLETVWVSRANVIQRRGRAGRCQSGFAYHLFPRSRLEK

Chicken                       KVSCLETVWVSKSNVVQRRGRAGRCQSGFAYHLFPRSRLDK
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 – 1194 ATP-dependent RNA helicase DHX30
Domain 654 – 827 Helicase C-terminal



Literature citations
De Novo Missense Mutations in DHX30 Impair Global Translation and Cause a Neurodevelopmental Disorder.
Lessel D.; Schob C.; Kuery S.; Reijnders M.R.F.; Harel T.; Eldomery M.K.; Coban-Akdemir Z.; Denecke J.; Edvardson S.; Colin E.; Stegmann A.P.A.; Gerkes E.H.; Tessarech M.; Bonneau D.; Barth M.; Besnard T.; Cogne B.; Revah-Politi A.; Strom T.M.; Rosenfeld J.A.; Yang Y.; Posey J.E.; Immken L.; Oundjian N.; Helbig K.L.; Meeks N.; Zegar K.; Morton J.; Schieving J.H.; Claasen A.; Huentelman M.; Narayanan V.; Ramsey K.; Brunner H.G.; Elpeleg O.; Mercier S.; Bezieau S.; Kubisch C.; Kleefstra T.; Kindler S.; Lupski J.R.; Kreienkamp H.J.;
Am. J. Hum. Genet. 101:716-724(2017)
Cited for: INVOLVEMENT IN NEDMIAL; VARIANTS NEDMIAL HIS-493; ARG-562; ASP-781; TRP-782; CYS-785 AND HIS-785; CHARACTERIZATION OF VARIANTS NEDMIAL HIS-493; ARG-562; ASP-781; TRP-782; CYS-785 AND HIS-785; FUNCTION; CATALYTIC ACTIVITY; SUBCELLULAR LOCATION; Lessons learned from additional research analyses of unsolved clinical exome cases.
Eldomery M.K.; Coban-Akdemir Z.; Harel T.; Rosenfeld J.A.; Gambin T.; Stray-Pedersen A.; Kuery S.; Mercier S.; Lessel D.; Denecke J.; Wiszniewski W.; Penney S.; Liu P.; Bi W.; Lalani S.R.; Schaaf C.P.; Wangler M.F.; Bacino C.A.; Lewis R.A.; Potocki L.; Graham B.H.; Belmont J.W.; Scaglia F.; Orange J.S.; Jhangiani S.N.; Chiang T.; Doddapaneni H.; Hu J.; Muzny D.M.; Xia F.; Beaudet A.L.; Boerwinkle E.; Eng C.M.; Plon S.E.; Sutton V.R.; Gibbs R.A.; Posey J.E.; Yang Y.; Lupski J.R.;
Genome Med. 9:26-26(2017)
Cited for: VARIANTS NEDMIAL HIS-493; ARG-562 AND TRP-782;
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.