Sequence information
Variant position: 335 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:
TDTIATMAGAIAGAYYGMDQ
V PESWQQSCEGYEETDILAQS
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 TDTIATMAGAIAGAYYGMDQV PESWQQSCEGYEETDILAQS
Mouse TDTIATMAGAIAGAYYGMEQV PESWQQSCEGFEETDVLAQS
Bovine TDTIATMAGAIAGAYYGMEQV PESWQQSCEGYEETDVLAQS
Chicken TNTIATMAGAIAGAYYGEEQV PPSWEQSCEAFQETQKMANS
Xenopus tropicalis TDTIATMAAAIAGAYHGEEQI PLNWKLSAEGYKDAEDWGEK
Zebrafish TDTIACMAGAIAGAHYGIDSI PLSWQVSCEGVDEADDLARR
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
Metal binding
316 – 316
Magnesium 1
Metal binding
316 – 316
Magnesium 2
Metal binding
317 – 317
Magnesium 2
Mutagenesis
316 – 316
D -> A. Abolishes hydrolase activity.
Mutagenesis
317 – 317
T -> A. Complete loss of activity. Does not affect recruitment to DNA lesion regions following DNA damage. Retains ability to bind proteins ADP-ribosylated on serine but is unable to hydrolyze them.
Mutagenesis
317 – 317
T -> S. Partial loss of activity.
Literature citations
Bi-allelic ADPRHL2 mutations cause neurodegeneration with developmental delay, ataxia, and axonal neuropathy.
Danhauser K.; Alhaddad B.; Makowski C.; Piekutowska-Abramczuk D.; Syrbe S.; Gomez-Ospina N.; Manning M.A.; Kostera-Pruszczyk A.; Krahn-Peper C.; Berutti R.; Kovacs-Nagy R.; Gusic M.; Graf E.; Laugwitz L.; Roeblitz M.; Wroblewski A.; Hartmann H.; Das A.M.; Bueltmann E.; Fang F.; Xu M.; Schatz U.A.; Karall D.; Zellner H.; Haberlandt E.; Feichtinger R.G.; Mayr J.A.; Meitinger T.; Prokisch H.; Strom T.M.; Ploski R.; Hoffmann G.F.; Pronicki M.; Bonnen P.E.; Morlot S.; Haack T.B.;
Am. J. Hum. Genet. 103:817-825(2018)
Cited for: INVOLVEMENT IN CONDSIAS; VARIANTS CONDSIAS 248-LYS-ILE-249 DELINS ASN; GLY-335 AND 346-TYR--SER-363 DEL; FUNCTION; CHARACTERIZATION OF VARIANTS CONDSIAS 248-LYS-ILE-249 DELINS ASN AND GLY-335;
Biallelic ADPRHL2 mutations in complex neuropathy affect ADP ribosylation and DNA damage response.
Beijer D.; Agnew T.; Rack J.G.M.; Prokhorova E.; Deconinck T.; Ceulemans B.; Peric S.; Milic Rasic V.; De Jonghe P.; Ahel I.; Baets J.;
Life. Sci Alliance 4:0-0(2021)
Cited for: CHARACTERIZATION OF VARIANTS CONDSIAS PHE-26 AND GLY-335; FUNCTION; SUBCELLULAR LOCATION; MUTAGENESIS OF ASP-77 AND ASP-78;
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.