UniProtKB/Swiss-Prot Q08211: Variant p.Ala1255Thr

ATP-dependent RNA helicase A
Gene: DHX9
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Variant information Variant position:

1255 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:

US 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:

From Alanine (A) to Threonine (T) at position 1255 (A1255T, p.Ala1255Thr). 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:

Change from small size and hydrophobic (A) to medium size and polar (T) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

0 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:

Found in a patient with Charcot-Marie-Tooth disease axonal type; uncertain significance. Any additional useful information about the variant.
Other resources:

Links to websites of interest for the variant.

Variant rs201196588 [ dbSNP | Ensembl ]

Sequence information Variant position:

1255 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length:

1270 The length of the canonical sequence.
Location on the sequence:

RGPSGGYRGSGGFQRGGGRG A YGTGYFGQGRGGGGY 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                         RGPS-GGYRGSG-GFQRGGG--RGAYGTGYFGQGR---GGG-GY-----

Mouse                         RGSS-GDYRGSGGGYRGSGGFQRRGYGGGYFGQGRG

Bovine                        RGESGGGYRGSG-GFQRGGG--RGGYGGGYFGQGR-

Xenopus laevis                R----GGYQSQG-GYQSQGG---GGYGGNFQGRGG-

Caenorhabditis elegans        NAGR-GNYGNVGSGYRGAGG--GGGYRGGRGGRGGG

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	1 – 1270	ATP-dependent RNA helicase A
Region	1150 – 1270	RGG
Modified residue	1235 – 1235	Asymmetric dimethylarginine
Modified residue	1242 – 1242	Asymmetric dimethylarginine
Modified residue	1249 – 1249	Asymmetric dimethylarginine
Modified residue	1265 – 1265	Asymmetric dimethylarginine

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.