Variant position: 26 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:
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 MAAAAGGGAGAARSL---SRFRG CLAGALLGDCVGSFYEAHDTV
Mouse MSAAGGGGASAARSI---SRFRG CLAGALLGDCVGAVYEAH
Bovine MTAAGCGGAGAARSL---SRFRG CLAGALLGDCVGAVYEAR
Chicken AAGAGSGRAAVSRSRPPPARFRG CLAGALLGDCLGAVFEGR
Xenopus tropicalis MMAAGV------------SRFRG SLLGALLGDCIGAVFEGH
Zebrafish -MSAAARVVAPVMML---SRFRG ALVGSVLGDCIGGEFEGA
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
1 – 363 ADP-ribosylhydrolase ARH3
41 – 41 Magnesium 2
41 – 41 Glutamate flap
34 – 34 D -> G. Reduces hydrolase activity.
41 – 41 E -> AQ. Significant loss of activity. Does not affect recruitment to DNA lesion regions following DNA damage. Strongly reduced ability to hydrolyze proteins ADP-ribosylated on serine.
19 – 42
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;
Unrestrained poly-ADP-ribosylation provides insights into chromatin regulation and human disease.
Prokhorova E.; Agnew T.; Wondisford A.R.; Tellier M.; Kaminski N.; Beijer D.; Holder J.; Groslambert J.; Suskiewicz M.J.; Zhu K.; Reber J.M.; Krassnig S.C.; Palazzo L.; Murphy S.; Nielsen M.L.; Mangerich A.; Ahel D.; Baets J.; O'Sullivan R.J.; Ahel I.;
Mol. Cell 81:2640-2655.e8(2021)
Cited for: VARIANT CONDSIAS PHE-26; FUNCTION; MUTAGENESIS OF ASP-77 AND ASP-78;
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.