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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P30566: Variant p.Arg303Cys

Adenylosuccinate lyase
Gene: ADSL
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Variant information Variant position: help 303 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LP/P [Disclaimer] The variants are classified into three categories: LP/P, LB/B and US.
  • LP/P: likely pathogenic or pathogenic.
  • LB/B: likely benign or benign.
  • US: uncertain significance
Residue change: help From Arginine (R) to Cysteine (C) at position 303 (R303C, p.Arg303Cys). Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.
Physico-chemical properties: help Change from large size and basic (R) to medium size and polar (C) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -3 The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:
  • Lowest score: -4 (low probability of substitution).
  • Highest score: 11 (high probability of substitution).
More information can be found on the following page
Variant description: help In ADSLD; mild; strongly reduced activity with SAMP, but only slightly reduced activity with SAICAR; abolishes cooperativity. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 303 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 484 The length of the canonical sequence.
Location on the sequence: help EKQQIGSSAMPYKRNPMRSE R CCSLARHLMTLVMDPLQTAS 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences. 
Human                         EKQQIGSSAMPYKRNPMRSERCCSLARHLMTLVMDPLQTAS

Mouse                         EKQQIGSSAMPYKRNPMRSERCCSLARHLMALTMDPLQTAS

Bovine                        EKQQIGSSAMPYKRNPMRSERCCSLARHLMALVMDPLQTAS

Chicken                       EKDQIGSSAMPYKRNPMRSERCCSLARHLMTLVLDPLQTAS

Caenorhabditis elegans        EKDQIGSSAMPYKKNPMKSERCCALSRKLINAPQEALTILA

Slime mold                    VKGEVGSSTMPHKVNPIDFENAEGNMGVANALYEHLSAKLP

Baker's yeast                 EKSQIGSSAMAYKRNPMRCERVCSLARHLGSLFSDAVQTAS

Fission yeast                 EAGQIGSSAMAYKRNPMRCERICSQARYIMNLIPNALNTAS
Sequence annotation in neighborhood: help 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.
TypePositionsDescription
Chain 2 – 484 Adenylosuccinate lyase
Active site 289 – 289 Proton donor/acceptor
Binding site 303 – 303
Modified residue 295 – 295 N6-acetyllysine
Helix 299 – 313



Literature citations
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.;
Biochemistry 51:6701-6713(2012)
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;
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.