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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot O00571: Variant p.Leu235Pro

ATP-dependent RNA helicase DDX3X
Gene: DDX3X
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Variant information Variant position: help 235 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 Leucine (L) to Proline (P) at position 235 (L235P, p.Leu235Pro). 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 medium size and hydrophobic. 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 MRXSSB. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 235 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 662 The length of the canonical sequence.
Location on the sequence: help KEKRDLMACAQTGSGKTAAF L LPILSQIYSDGPGEALRAMK 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                         KEKRDLMACAQTGSGKTAAFLLPILSQIYSDGPGEALRAMK

Mouse                         KEKRDLMACAQTGSGKTAAFLLPILSQIYADGPGEALRAMK
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 2 – 662 ATP-dependent RNA helicase DDX3X
Domain 211 – 403 Helicase ATP-binding
Region 100 – 662 Interaction with GSK3B
Modified residue 240 – 240 Phosphoserine; by TBK1; in vitro
Cross 215 – 215 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Mutagenesis 230 – 230 K -> A. No effect on general translation; when associated with A-200; A-207; A-347 and A-348.
Mutagenesis 230 – 230 K -> E. Complete loss of ATPase and RNA-unwinding activities. Loss of HIV-1 mRNA nuclear export. Does not promote the translation of HIV-1 RNA. No effect on IFNB1 induction. No effect on RNA-binding. Loss of inhibition of NF-kappa-B-mediated transcriptional activity.
Mutagenesis 240 – 240 S -> A. Greatly impairs phosphorylation by TBK1 and fails to synergize with TBK1 in IFN-beta induction; when associated with A-181; A-183 and A-269.
Helix 230 – 245



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.