Sequence information
Variant position: 112 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 338 The length of the canonical sequence.
Location on the sequence:
LAVHGAGNLVNTYYDFSKGI
D HKKSDDRTLVDRILEPQDVV
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 LAVHGAGNLVNTYYDFSKGID -HKKSDDRTLVDRILEPQDVV
Mouse LAVHGAGNLVNTYYDFSKGID -HKKSDDRTLVDRILEPQDV
Rat LAVHGAGNLVNTYYDFSKGID -HKKSDDRTLVDRILEPQDV
Chicken LAVHGAGNLVNTYYDFSKGID -HKKSDDRTLVDQILEPQDV
Xenopus tropicalis LAVHGAGNLVNTYYDFSKGID -HKKSDDRTLVDHILEPQDV
Zebrafish LLVHGAGNLVNTYYDFSKGID -HKKSDDRTLVDQILKPQDV
Drosophila VTVHCAGNVVNTYFDFIKGID -KQKADDRTLVDHILTKDEV
Slime mold VSLQALGNVVNSFYDCKNGND TKEKSADRTMFDFGLTEGNI
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
2 – 338
UbiA prenyltransferase domain-containing protein 1
Literature citations
Ubiad1 is an antioxidant enzyme that regulates eNOS activity by CoQ10 synthesis.
Mugoni V.; Postel R.; Catanzaro V.; De Luca E.; Turco E.; Digilio G.; Silengo L.; Murphy M.P.; Medana C.; Stainier D.Y.; Bakkers J.; Santoro M.M.;
Cell 152:504-518(2013)
Cited for: FUNCTION; SUBCELLULAR LOCATION; CHARACTERIZATION OF VARIANTS SCCD SER-102 AND GLY-112;
Mutations in the UBIAD1 gene, encoding a potential prenyltransferase, are causal for Schnyder crystalline corneal dystrophy.
Orr A.; Dube M.-P.; Marcadier J.; Jiang H.; Federico A.; George S.; Seamone C.; Andrews D.; Dubord P.; Holland S.; Provost S.; Mongrain V.; Evans S.; Higgins B.; Bowman S.; Guernsey D.; Samuels M.;
PLoS ONE 2:E685-E685(2007)
Cited for: VARIANTS SCCD SER-102; GLY-112; GLY-119; ILE-175 AND SER-232; VARIANT PHE-75;
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.