UniProtKB/Swiss-Prot O00571 : Variant p.Arg362Cys
ATP-dependent RNA helicase DDX3X
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Variant information
Variant position:
362
The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:
Disclaimer : Variants classification is intended for research purposes only, not for clinical and diagnostic use . The label disease variant is assigned according to literature reports on probable disease-association that can be based on theoretical reasons. This label must not be considered as a definitive proof for the pathogenic role of a variant. ]
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:
362 (R362C, p.Arg362Cys).
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:
The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:
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).following page
Variant description:
Any additional useful information about the variant.
Other resources:
Links to websites of interest for the variant.
Sequence information
Variant position:
362
The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length:
662
The length of the canonical sequence.
Location on the sequence:
R RIVEQDTMPPKGVRHTMMFS
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 KYLVLDEADRMLDMGFEPQIR RIVEQDTMPPKGVRHTMMFS
Mouse KYLVLDEADRMLDMGFEPQIR RIVEQDTMPPKGVRHTMMFS
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
2 – 662 ATP-dependent RNA helicase DDX3X
Domain
211 – 403 Helicase ATP-binding
Region
100 – 662 Interaction with GSK3B
Mutagenesis
347 – 347 D -> A. No effect on general translation; when associated with A-200; A-207; A-230 and A-348.
Mutagenesis
348 – 348 E -> A. No effect on general translation; when associated with A-200; A-207; A-230 and A-347.
Mutagenesis
348 – 348 E -> Q. Loss of both ATPase and RNA helicase activities; decreased up-regulation of CDKN1A promoter activity and HNF4A-mediated MTTP transcriptional activation; no effect on the repression of cap- and IRES-dependent translation, WNT/beta catenin signaling, nor on stress granule assembly. Does not promote the translation of HIV-1 RNA.
Mutagenesis
382 – 382 S -> L. Strong decrease in ATPase activity and RNA-unwinding activity. Does not promote the translation of mRNAs containing long structured 5'UTRs, including that of CCNE1. No effect on the translation of HIV-1 RNA.
Helix
358 – 365
Literature citations
Mutations in DDX3X are a common cause of unexplained intellectual disability with gender-specific effects on Wnt signaling.
Snijders Blok L.; Madsen E.; Juusola J.; Gilissen C.; Baralle D.; Reijnders M.R.; Venselaar H.; Helsmoortel C.; Cho M.T.; Hoischen A.; Vissers L.E.; Koemans T.S.; Wissink-Lindhout W.; Eichler E.E.; Romano C.; Van Esch H.; Stumpel C.; Vreeburg M.; Smeets E.; Oberndorff K.; van Bon B.W.; Shaw M.; Gecz J.; Haan E.; Bienek M.; Jensen C.; Loeys B.L.; Van Dijck A.; Innes A.M.; Racher H.; Vermeer S.; Di Donato N.; Rump A.; Tatton-Brown K.; Parker M.J.; Henderson A.; Lynch S.A.; Fryer A.; Ross A.; Vasudevan P.; Kini U.; Newbury-Ecob R.; Chandler K.; Male A.; Dijkstra S.; Schieving J.; Giltay J.; van Gassen K.L.; Schuurs-Hoeijmakers J.; Tan P.L.; Pediaditakis I.; Haas S.A.; Retterer K.; Reed P.; Monaghan K.G.; Haverfield E.; Natowicz M.; Myers A.; Kruer M.C.; Stein Q.; Strauss K.A.; Brigatti K.W.; Keating K.; Burton B.K.; Kim K.H.; Charrow J.; Norman J.; Foster-Barber A.; Kline A.D.; Kimball A.; Zackai E.; Harr M.; Fox J.; McLaughlin J.; Lindstrom K.; Haude K.M.; van Roozendaal K.; Brunner H.; Chung W.K.; Kooy R.F.; Pfundt R.; Kalscheuer V.; Mehta S.G.; Katsanis N.; Kleefstra T.;
Am. J. Hum. Genet. 97:343-352(2015)
Cited for: VARIANTS MRXSSB THR-214; ALA-233 DEL; VAL-233; PRO-235; PHE-300; HIS-326; GLN-351; CYS-362; CYS-376; PRO-392; PRO-417; GLY-475; SER-480; HIS-488; THR-507; ILE-509; THR-514; HIS-534; LEU-560 DEL AND LEU-568; CHARACTERIZATION OF VARIANTS MRXSSB THR-214; HIS-326; CYS-376; THR-507 AND HIS-534; INVOLVEMENT IN MRXSSB;
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.
