Sequence information
Variant position: 177 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 363 The length of the canonical sequence.
Location on the sequence:
VAGISLAYSSVQDVQKFARL
S AQLTHASSLGYNGAILQALA
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 VAGISLAYSSVQDVQKFARLS AQLTHASSLGYNGAILQALA
Mouse VAGISLAYSSVQDVQKFARLS AQLTHASSLGYNGAILQALA
Bovine VAGISLAYSSVQDVQKFARLS AQLTHASSLGYNGAILQALA
Chicken VAGIPLTYSDVQDVKKFAKLS AELTHANSLGYNGAILQALA
Xenopus tropicalis VVGISLAYPRIPDIIEYARTS GMLTHASSLGYNGAILQALA
Zebrafish AVPFALAFRSRADVRKYSRFG AMLTHSCSLGYNGAALQALA
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 – 363
ADP-ribosylhydrolase ARH3
Binding site
182 – 182
Substrate
Mutagenesis
182 – 182
H -> QA. Complete loss of activity. Abolished recruitment to DNA lesion regions following DNA damage. Abolished ability to hydrolyze proteins ADP-ribosylated on serine.
Mutagenesis
185 – 185
S -> P. No effect on hydrolase activity.
Mutagenesis
186 – 186
L -> V. No effect on hydrolase activity.
Helix
167 – 179
Literature citations
Biallelic mutations in ADPRHL2, encoding ADP-ribosylhydrolase 3, lead to a degenerative pediatric stress-induced epileptic ataxia syndrome.
Ghosh S.G.; Becker K.; Huang H.; Dixon-Salazar T.; Chai G.; Salpietro V.; Al-Gazali L.; Waisfisz Q.; Wang H.; Vaux K.K.; Stanley V.; Manole A.; Akpulat U.; Weiss M.M.; Efthymiou S.; Hanna M.G.; Minetti C.; Striano P.; Pisciotta L.; De Grandis E.; Altmueller J.; Nuernberg P.; Thiele H.; Yis U.; Okur T.D.; Polat A.I.; Amiri N.; Doosti M.; Karimani E.G.; Toosi M.B.; Haddad G.; Karakaya M.; Wirth B.; van Hagen J.M.; Wolf N.I.; Maroofian R.; Houlden H.; Cirak S.; Gleeson J.G.;
Am. J. Hum. Genet. 103:431-439(2018)
Cited for: INVOLVEMENT IN CONDSIAS; VARIANTS CONDSIAS ASN-34; PRO-79; 106-GLN--SER-363 DEL; LEU-177 AND 334-GLN--SER-363 DEL; CHARACTERIZATION OF VARIANTS CONDSIAS PRO-79; 106-GLN--SER-363 DEL AND 334-GLN--SER-363 DEL;
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.