Sequence information
Variant position: 235 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 299 The length of the canonical sequence.
Location on the sequence:
KTKAWLKEHVEPVFGFPQFV
R FSWRTAQTILEKEAEDVIWE
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 KTKAWLKEHVEPVFGFP-QFVR FSWRTAQTILE---KE--AEDVIWE
Mouse KTKAWLRKHVDPVFGFP-QFVR FSWSTAQAILE---KE--A
Rat KTKAWLRKHVDPVFGFP-QFVR FSWSTAQAILE---KE--A
Bovine KTKAWLRKHVDPVFGFP-QFVR FSWRTAQSILE---SE--A
Caenorhabditis elegans NTKKFLQLSVEPVFGFC-SLVR SSWKTASTIVE---KR--C
Drosophila VTRRFLTEYIDLVFGFP-RLVR FSWSTAENALA---DK--A
Slime mold LSKKWLVKNRDKVFGYP-NFIR FSWKTTETAMR---GA--C
Baker's yeast KTVAWLKRNQTSLMGWPANMVR FSWQTCQTLLDDASKN--S
Fission yeast RTTEWLKVNVDKIFGWKGDIVR YSWKTAKDLLELPSKSQSS
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 – 299
Ribonuclease H2 subunit A
Domain
28 – 250
RNase H type-2
Modified residue
216 – 216
Phosphothreonine
Mutagenesis
240 – 240
T -> A. Strongly reduced enzyme activity.
Literature citations
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 AGS4 SER-37; TRP-108; TRP-186; LEU-230; GLN-235; MET-240 AND HIS-291; VARIANTS ASP-99; SER-202; GLU-205 AND GLY-260;
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.