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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q08211: Variant p.Lys1163Arg

ATP-dependent RNA helicase A
Gene: DHX9
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Variant information Variant position: help 1163 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 Lysine (K) to Arginine (R) at position 1163 (K1163R, p.Lys1163Arg). 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 Similar physico-chemical property. Both residues are large size and basic. The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 2 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 MRD75; likely pathogenic; does not localize to the nucleus. Any additional useful information about the variant.


Sequence information Variant position: help 1163 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 1270 The length of the canonical sequence.
Location on the sequence: help AAGINLMIGSTRYGDGPRPP K MARYDNGSGYRRGGSSYSGG 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                         AAGI---NLMIGSTRYGDGPRPPKMARYDNGSGYRR--GGSSYSGG

Mouse                         AAGI---NLMIGSVRYGDGPRPPKMARYDNGSGYRRGYGGG

Bovine                        AAGI---NLMIGTTRYGDGPRPPKMARYDNGSGYRR--GGS

Xenopus laevis                TAGI---SLVMGNSRFGDGPRPPKMARFDSGFQGNR-----

Caenorhabditis elegans        EAGPIKDSLLTDNALIQKGPAPNRLEYADWGPSNNN-----
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 – 1270 ATP-dependent RNA helicase A
Region 1150 – 1270 RGG
Motif 1155 – 1173 Nuclear localization signal (NLS2)
Modified residue 1166 – 1166 Asymmetric dimethylarginine
Modified residue 1175 – 1175 Omega-N-methylarginine
Mutagenesis 1160 – 1160 R -> A. Localizes in the nucleus and interacts with the importin complex.
Mutagenesis 1163 – 1163 K -> A. Localizes in the cytoplasm and does not interact with the importin complex.
Mutagenesis 1163 – 1163 Missing. Abolishes nuclear localization.
Mutagenesis 1166 – 1166 R -> A. Localizes in the nucleus and the cytoplasm and interacts weakly with the importin complex.
Mutagenesis 1166 – 1166 R -> L. Abolishes nuclear localization.
Mutagenesis 1166 – 1166 Missing. Abolishes nuclear localization.



Literature citations
Monoallelic variation in DHX9, the gene encoding the DExH-box helicase DHX9, underlies neurodevelopment disorders and Charcot-Marie-Tooth disease.
Calame D.G.; Guo T.; Wang C.; Garrett L.; Jolly A.; Dawood M.; Kurolap A.; Henig N.Z.; Fatih J.M.; Herman I.; Du H.; Mitani T.; Becker L.; Rathkolb B.; Gerlini R.; Seisenberger C.; Marschall S.; Hunter J.V.; Gerard A.; Heidlebaugh A.; Challman T.; Spillmann R.C.; Jhangiani S.N.; Coban-Akdemir Z.; Lalani S.; Liu L.; Revah-Politi A.; Iglesias A.; Guzman E.; Baugh E.; Boddaert N.; Rondeau S.; Ormieres C.; Barcia G.; Tan Q.K.G.; Thiffault I.; Pastinen T.; Sheikh K.; Biliciler S.; Mei D.; Melani F.; Shashi V.; Yaron Y.; Steele M.; Wakeling E.; Oestergaard E.; Nazaryan-Petersen L.; Millan F.; Santiago-Sim T.; Thevenon J.; Bruel A.L.; Thauvin-Robinet C.; Popp D.; Platzer K.; Gawlinski P.; Wiszniewski W.; Marafi D.; Pehlivan D.; Posey J.E.; Gibbs R.A.; Gailus-Durner V.; Guerrini R.; Fuchs H.; Hrabe de Angelis M.; Hoelter S.M.; Cheung H.H.; Gu S.; Lupski J.R.;
Am. J. Hum. Genet. 110:1394-1413(2023)
Cited for: VARIANTS MRD75 GLN-141; 229-ARG--TYR-1270 DEL; GLU-411; ILE-473; GLY-608; TRP-761; GLN-761; 764-ARG--TYR-1270 DEL; GLN-1052; ARG-1163; PRO-1166 AND 1263-GLN--TYR-1270 DEL; VARIANTS THR-837; GLY-846 AND THR-1255; INVOLVEMENT IN MRD75; CHARACTERIZATION OF VARIANTS MRD75 GLU-411; ILE-473; GLY-608; GLN-761; ARG-1163 AND PRO-1166; FUNCTION; SUBCELLULAR LOCATION;
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.