Variant position: 303 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 484 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 EKQQIGSSAMPYKRNPMRSE RCCSLARHLMTLVMDPLQTAS
Mouse EKQQIGSSAMPYKRNPMRSE RCCSLARHLMALTMDPLQTAS
Bovine EKQQIGSSAMPYKRNPMRSE RCCSLARHLMALVMDPLQTAS
Chicken EKDQIGSSAMPYKRNPMRSE RCCSLARHLMTLVLDPLQTAS
Caenorhabditis elegans EKDQIGSSAMPYKKNPMKSE RCCALSRKLINAPQEALTILA
Slime mold VKGEVGSSTMPHKVNPIDFE NAEGNMGVANALYEHLSAKLP
Baker's yeast EKSQIGSSAMAYKRNPMRCE RVCSLARHLGSLFSDAVQTAS
Fission yeast EAGQIGSSAMAYKRNPMRCE RICSQARYIMNLIPNALNTAS
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
2 – 484 Adenylosuccinate lyase
289 – 289 Proton donor/acceptor
303 – 303 Substrate; shared with neighboring subunit
295 – 295 N6-acetyllysine
299 – 313
Structural and biochemical characterization of human adenylosuccinate lyase (ADSL) and the R303C ADSL deficiency-associated mutation.
Ray S.P.; Deaton M.K.; Capodagli G.C.; Calkins L.A.; Sawle L.; Ghosh K.; Patterson D.; Pegan S.D.;
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF WILD-TYPE AND VARIANT ADSLD CYS-303; CATALYTIC ACTIVITY; CHARACTERIZATION OF VARIANT ADSLD CYS-303; ACTIVE SITE; ACTIVITY REGULATION; SUBUNIT;
Mutation analysis in adenylosuccinate lyase deficiency: eight novel mutations in the re-evaluated full ADSL coding sequence.
Marie S.; Cuppens H.; Heuterspreute M.; Jaspers M.; Tola E.Z.; Gu X.X.; Legius E.; Vincent M.-F.; Jaeken J.; Cassiman J.-J.; van den Berghe G.;
Hum. Mutat. 13:197-202(1999)
Cited for: VARIANTS ADSLD VAL-72; TRP-141; GLN-190; GLU-246; CYS-303; ARG-395 AND HIS-426;
Clinical, biochemical and molecular genetic correlations in adenylosuccinate lyase deficiency.
Race V.; Marie S.; Vincent M.-F.; Van den Berghe G.;
Hum. Mol. Genet. 9:2159-2165(2000)
Cited for: CHARACTERIZATION OF VARIANTS ADSLD VAL-2; LEU-26; TRP-141; CYS-303; ARG-395; HIS-426 AND SER-450;
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.