Variant position: 390 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 483 The length of the canonical sequence.
Location on the sequence:
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 QEHRNRVFHDFRNGLCRNLV CTDLFTRGIDIQAVNVVINFD
Mouse QEHRNRVFHDFRNGLCRNLV CTDLFTRGIDIQAVNVVINFD
Chicken QEHRNRVFHDFRNGLCRNLV CTDLFTRGIDIQAVNVVINFD
Xenopus laevis QEHRNRVFHDFRNGLCRNLV CTDLFTRGIDIQAVNVVINFD
Xenopus tropicalis QEHRNRVFHDFRNGLCRNLV CTDLFTRGIDIQAVNVVINFD
Drosophila QAHRNRVFHDFRQGLCRNLV CSDLFTRGIDVQAVNVVINFD
Slime mold QAHRNRVFHDFRNGACRNLV SSDLFTRGIDIQDVNVVINFD
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
1 – 483 Probable ATP-dependent RNA helicase DDX6
308 – 468 Helicase C-terminal
307 – 483 RecA-like domain 2
386 – 386 R -> E. Abolished ability to regulate RNA metabolism.
384 – 390
Rare de novo missense variants in RNA helicase DDX6 cause intellectual disability and dysmorphic features and lead to P-body defects and RNA dysregulation.
Balak C.; Benard M.; Schaefer E.; Iqbal S.; Ramsey K.; Ernoult-Lange M.; Mattioli F.; Llaci L.; Geoffroy V.; Courel M.; Naymik M.; Bachman K.K.; Pfundt R.; Rump P.; Ter Beest J.; Wentzensen I.M.; Monaghan K.G.; McWalter K.; Richholt R.; Le Bechec A.; Jepsen W.; De Both M.; Belnap N.; Boland A.; Piras I.S.; Deleuze J.F.; Szelinger S.; Dollfus H.; Chelly J.; Muller J.; Campbell A.; Lal D.; Rangasamy S.; Mandel J.L.; Narayanan V.; Huentelman M.; Weil D.; Piton A.;
Am. J. Hum. Genet. 105:509-525(2019)
Cited for: FUNCTION; SUBCELLULAR LOCATION; INTERACTION WITH LSM14A; LSM14B; EIF4ENIF1; PATL1; EDC3 AND EDC4; INVOLVEMENT IN IDDILF; VARIANTS IDDILF ARG-372; GLN-373; ARG-390; ILE-391 AND PRO-391; CHARACTERIZATION OF VARIANTS IDDILF GLN-373; ARG-390; ILE-391 AND PRO-391;
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.