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UniProtKB/Swiss-Prot Q9NSU2: Variant p.Val201Asp

Three-prime repair exonuclease 1
Gene: TREX1
Variant information

Variant position:  201
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  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:  From Valine (V) to Aspartate (D) at position 201 (V201D, p.Val201Asp).
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 medium size and hydrophobic (V) to medium size and acidic (D)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  -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:  In AGS1; reduces activity by 75%.
Any additional useful information about the variant.

Other resources:  
Links to websites of interest for the variant.

Sequence information

Variant position:  201
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  314
The length of the canonical 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.




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.

Chain 1 – 314 Three-prime repair exonuclease 1
Active site 195 – 195 Proton donor/acceptor
Metal binding 200 – 200 Magnesium 1
Binding site 200 – 200 Substrate

Literature citations

The crystal structure of TREX1 explains the 3' nucleotide specificity and reveals a polyproline II helix for protein partnering.
de Silva U.; Choudhury S.; Bailey S.L.; Harvey S.; Perrino F.W.; Hollis T.;
J. Biol. Chem. 282:10537-10543(2007)

Mutations in the gene encoding the 3'-5' DNA exonuclease TREX1 cause Aicardi-Goutieres syndrome at the AGS1 locus.
Crow Y.J.; Hayward B.E.; Parmar R.; Robins P.; Leitch A.; Ali M.; Black D.N.; van Bokhoven H.; Brunner H.G.; Hamel B.C.J.; Corry P.C.; Cowan F.M.; Frints S.G.; Klepper J.; Livingston J.H.; Lynch S.A.; Massey R.F.; Meritet J.F.; Michaud J.L.; Ponsot G.; Voit T.; Lebon P.; Bonthron D.T.; Jackson A.P.; Barnes D.E.; Lindahl T.;
Nat. Genet. 38:917-920(2006)
Cited for: VARIANTS AGS1 HIS-114; ASP-200 INS AND ASP-201;

Clinical and molecular phenotype of Aicardi-Goutieres syndrome.
Rice G.; Patrick T.; Parmar R.; Taylor C.F.; Aeby A.; Aicardi J.; Artuch R.; Montalto S.A.; Bacino C.A.; Barroso B.; Baxter P.; Benko W.S.; Bergmann C.; Bertini E.; Biancheri R.; Blair E.M.; Blau N.; Bonthron D.T.; Briggs T.; Brueton L.A.; Brunner H.G.; Burke C.J.; Carr I.M.; Carvalho D.R.; Chandler K.E.; Christen H.J.; Corry P.C.; Cowan F.M.; Cox H.; D'Arrigo S.; Dean J.; De Laet C.; De Praeter C.; Dery C.; Ferrie C.D.; Flintoff K.; Frints S.G.; Garcia-Cazorla A.; Gener B.; Goizet C.; Goutieres F.; Green A.J.; Guet A.; Hamel B.C.; Hayward B.E.; Heiberg A.; Hennekam R.C.; Husson M.; Jackson A.P.; Jayatunga R.; Jiang Y.H.; Kant S.G.; Kao A.; King M.D.; Kingston H.M.; Klepper J.; van der Knaap M.S.; Kornberg A.J.; Kotzot D.; Kratzer W.; Lacombe D.; Lagae L.; Landrieu P.G.; Lanzi G.; Leitch A.; Lim M.J.; Livingston J.H.; Lourenco C.M.; Lyall E.G.; Lynch S.A.; Lyons M.J.; Marom D.; McClure J.P.; McWilliam R.; Melancon S.B.; Mewasingh L.D.; Moutard M.L.; Nischal K.K.; Ostergaard J.R.; Prendiville J.; Rasmussen M.; Rogers R.C.; Roland D.; Rosser E.M.; Rostasy K.; Roubertie A.; Sanchis A.; Schiffmann R.; Scholl-Burgi S.; Seal S.; Shalev S.A.; Corcoles C.S.; Sinha G.P.; Soler D.; Spiegel R.; Stephenson J.B.; Tacke U.; Tan T.Y.; Till M.; Tolmie J.L.; Tomlin P.; Vagnarelli F.; Valente E.M.; Van Coster R.N.; Van der Aa N.; Vanderver A.; Vles J.S.; Voit T.; Wassmer E.; Weschke B.; Whiteford M.L.; Willemsen M.A.; Zankl A.; Zuberi S.M.; Orcesi S.; Fazzi E.; Lebon P.; Crow Y.J.;
Am. J. Hum. Genet. 81:713-725(2007)
Cited for: VARIANTS AGS1 HIS-114; ALA-122; ASN-200; ASP-201 AND PRO-303;

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.