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UniProtKB/Swiss-Prot P00966: Variant p.Asp124Asn

Argininosuccinate synthase
Gene: ASS1
Variant information

Variant position:  124
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  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:  From Aspartate (D) to Asparagine (N) at position 124 (D124N, p.Asp124Asn).
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:  Change from medium size and acidic (D) to medium size and polar (N)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  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:  In CTLN1; loss of argininosuccinate synthase activity.
Any additional useful information about the variant.

Other resources:  
Links to websites of interest for the variant.



Sequence information

Variant position:  124
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  412
The length of the canonical sequence.

Location on the sequence:   EIAQREGAKYVSHGATGKGN  D QVRFELSCYSLAPQIKVIAP
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                         EIAQREGAKYVSHGATGKGNDQVRFELSCYSLAPQIKVIAP

Mouse                         EIAQREGAKYVSHGATGKGNDQVRFELTCYSLAPQIKVIAP

Rat                           EIAQREGAKYVSHGATGKGNDQVRFELTCYSLAPQIKVIAP

Bovine                        EIAQREGAKYVSHGATGKGNDQIRFELTCYSLAPQIKVIAP

Chicken                       LIAQEEGARYIAHGATGKGNDQVRFELGCYALCPSIKVIAP

Xenopus laevis                EIAKKEAAEYVSHGATGKGNDQIRFELTCYSLYPEVKIIAP

Xenopus tropicalis            EIAKKEAAEYVSHGATGKGNDQIRFELTCYALYPEVKIIAP

Zebrafish                     QIAQREGAQYVSHGATGKGNDQVRFELTCYALYPQVQVIAP

Drosophila                    EVAREYGAKYLAHGATGKGNDQVRFELCAYALKPDLKIIAP

Baker's yeast                 DVAKQEGCFAVSHGCTGKGNDQIRFELSFYALKPDVKCITP

Fission yeast                 QIAEKENCIAVSHGCTGKGNDQVRFELAYYALKPDVQVIAP

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.

TypePositionsDescription
Chain 1 – 412 Argininosuccinate synthase
Binding site 119 – 119 Aspartate
Binding site 123 – 123 Aspartate
Binding site 123 – 123 Citrulline
Binding site 124 – 124 Aspartate
Binding site 127 – 127 Citrulline
Modified residue 112 – 112 N6-acetyllysine
Modified residue 113 – 113 Phosphotyrosine
Helix 124 – 135


Literature citations

Prenatal diagnosis of citrullinemia and argininosuccinic aciduria: evidence for a transmission ratio distortion in citrullinemia.
Kleijer W.J.; Garritsen V.H.; van der Sterre M.L.; Berning C.; Haeberle J.; Huijmans J.G.M.;
Prenat. Diagn. 26:242-247(2006)
Cited for: VARIANTS CTLN1 ASN-124; HIS-157; GLN-270; GLN-279; LYS-283; SER-324; GLY-363 AND ARG-390;

Kinetic mutations in argininosuccinate synthetase deficiency: characterisation and in vitro correction by substrate supplementation.
Diez-Fernandez C.; Wellauer O.; Gemperle C.; Ruefenacht V.; Fingerhut R.; Haeberle J.;
J. Med. Genet. 53:710-719(2016)
Cited for: VARIANTS CTLN1 PRO-91; LEU-96; SER-117; THR-118; ILE-119; ASN-124; CYS-157; HIS-157; CYS-272; HIS-272 AND LEU-272; CHARACTERIZATION OF VARIANTS CTLN1 PRO-91; SER-95; HIS-96; LEU-96; SER-96; SER-117; THR-118; ILE-119; ASN-124; GLN-127; TRP-127; CYS-157; HIS-157; ASN-180; ILE-180; GLN-191; GLN-270; CYS-272; HIS-272 AND LEU-272; CHARACTERIZATION OF VARIANT LEU-127; CATALYTIC ACTIVITY; PATHWAY; FUNCTION; SUBCELLULAR LOCATION;

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.