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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P04424: Variant p.Gln286Arg

Argininosuccinate lyase
Gene: ASL
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Variant information Variant position: help 286 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 Glutamine (Q) to Arginine (R) at position 286 (Q286R, p.Gln286Arg). 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 medium size and polar (Q) to large size and basic (R) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 1 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 ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 286 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 464 The length of the canonical sequence.
Location on the sequence: help KEFSFVQLSDAYSTGSSLMP Q KKNPDSLELIRSKAGRVFGR 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                         KEFSFVQLSDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGR

Mouse                         KEFSFVQLSDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGR

Rat                           KEFNFVQLSDAYSTGSSLMPQKKNPDSLELIRSKARRVFGR

Bovine                        KEFSFVQLSDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGR

Baker's yeast                 AEFGFIQLSDAYSTGSSLMPQKKNADSLELLRGKSGRVFGD

Fission yeast                 SEFGFVTLSDAYSTGSSIMPQKKNPDSLELLRGKSGRVLGD
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 – 464 Argininosuccinate lyase
Active site 281 – 281 Proton donor
Binding site 289 – 289 in chain B
Site 294 – 294 Increases basicity of active site His
Modified residue 288 – 288 N6-acetyllysine
Mutagenesis 288 – 288 K -> R. Refractory to inhibition by TSA and NAM and by addition of extra amino acids. No effect on protein structure.



Literature citations
Mechanisms for intragenic complementation at the human argininosuccinate lyase locus.
Yu B.; Thompson G.D.; Yip P.; Howell P.L.; Davidson A.R.;
Biochemistry 40:15581-15590(2001)
Cited for: FUNCTION; CATALYTIC ACTIVITY; BIOPHYSICOCHEMICAL PROPERTIES; SUBUNIT; PATHWAY; VARIANTS ARGINSA GLY-87; ARG-286; THR-360 AND ASP-398; CHARACTERIZATION OF VARIANTS ARGINSA GLY-87; ARG-286; THR-360 AND ASP-398; Three-dimensional structure of the argininosuccinate lyase frequently complementing allele Q286R.
Sampaleanu L.M.; Vallee F.; Thompson G.D.; Howell P.L.;
Biochemistry 40:15570-15580(2001)
Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF VARIANT ARGINSA ARG-286; FUNCTION; CATALYTIC ACTIVITY; BIOPHYSICOCHEMICAL PROPERTIES; CHARACTERIZATION OF VARIANTS ARGINSA GLN-12 AND ARG-286; Analysis of naturally occurring and site-directed mutations in the argininosuccinate lyase gene.
Barbosa P.; Cialkowski M.; O'Brien W.E.;
J. Biol. Chem. 266:5286-5290(1991)
Cited for: VARIANTS ARGINSA TRP-111; GLN-193 AND ARG-286; MUTAGENESIS OF LYS-51 AND HIS-89; Intragenic complementation at the human argininosuccinate lyase locus. Identification of the major complementing alleles.
Walker D.C.; Christodoulou J.; Craig H.J.; Simard L.R.; Ploder L.; Howell P.L.; McInnes R.R.;
J. Biol. Chem. 272:6777-6783(1997)
Cited for: VARIANTS ARGINSA GLY-87; ARG-286 AND ASP-398; CHARACTERIZATION OF VARIANTS ARGINSA GLY-87 AND ARG-286; FUNCTION; CATALYTIC ACTIVITY; Argininosuccinate lyase deficiency: mutational spectrum in Italian patients and identification of a novel ASL pseudogene.
Trevisson E.; Salviati L.; Baldoin M.C.; Toldo I.; Casarin A.; Sacconi S.; Cesaro L.; Basso G.; Burlina A.B.;
Hum. Mutat. 28:694-702(2007)
Cited for: VARIANTS ARGINSA ASN-31; GLN-113; MET-178; GLN-186; TRP-236; ARG-286; LEU-335; ARG-382 AND TRP-456; Functional complementation in yeast allows molecular characterization of missense argininosuccinate lyase mutations.
Trevisson E.; Burlina A.; Doimo M.; Pertegato V.; Casarin A.; Cesaro L.; Navas P.; Basso G.; Sartori G.; Salviati L.;
J. Biol. Chem. 284:28926-28934(2009)
Cited for: VARIANTS ARGINSA ASN-31; LYS-73; GLN-113; MET-178; GLN-182; GLN-186; TRP-236; ARG-286; GLN-297; LEU-335; ARG-382 AND TRP-456; CHARACTERIZATION OF VARIANTS ARGINSA ASN-31; LYS-73; GLN-113; MET-178; GLN-182; GLN-186; TRP-236; ARG-286; GLN-297; LEU-335; ARG-382 AND TRP-456;
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.