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UniProtKB/Swiss-Prot P00966: Variant p.Arg95Ser

Argininosuccinate synthase
Gene: ASS1
Variant information

Variant position:  95
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 Arginine (R) to Serine (S) at position 95 (R95S, p.Arg95Ser).
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 large size and basic (R) to small size and polar (S)
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; increased thermal stability; loss of argininosuccinate synthase activity.
Any additional useful information about the variant.



Sequence information

Variant position:  95
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:   PAIQSSALYEDRYLLGTSLA  R PCIARKQVEIAQREGAKYVS
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                         PAIQSSALYEDRYLLGTSLARPCIARKQVEIAQREGAKYVS

Mouse                         PAVQSSALYEDRYLLGTSLARPCIARRQVEIAQREGAKYVS

Rat                           PAVQSSALYEDRYLLGTSLARPCIARKQVEIAQREGAKYVS

Bovine                        PAIQSSALYEDRYLLGTSLARPCIARKQVEIAQREGAKYVS

Chicken                       PAVRANALYEDRYMLGSALARPCIARHLVLIAQEEGARYIA

Xenopus laevis                PAVQANAIYEDRYLLGTSLARPCIAKKQVEIAKKEAAEYVS

Xenopus tropicalis            PAVQANAIYEDRYLLGTSLARPCIAKKQVEIAKKEAAEYVS

Zebrafish                     PALQANALYEDRYLLGTSIARPCIARRQVQIAQREGAQYVS

Drosophila                    PAVQMGLVYEERYLLGTSLARPCISVALMEVAREYGAKYLA

Baker's yeast                 PAVQVNAVYEDVYLLGTSLARPVIAKAQIDVAKQEGCFAVS

Fission yeast                 PAAQANAIYENVYLLGTSLARPIIARRQIQIAEKENCIAVS

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 87 – 87 Citrulline
Binding site 92 – 92 Citrulline
Modified residue 87 – 87 Phosphotyrosine
Modified residue 112 – 112 N6-acetyllysine
Modified residue 113 – 113 Phosphotyrosine
Helix 94 – 109


Literature citations

Identification of 16 novel mutations in the argininosuccinate synthetase gene and genotype-phenotype correlation in 38 classical citrullinemia patients.
Gao H.-Z.; Kobayashi K.; Tabata A.; Tsuge H.; Iijima M.; Yasuda T.; Kalkanoglu H.S.; Dursun A.; Tokatli A.; Coskun T.; Trefz F.K.; Skladal D.; Mandel H.; Seidel J.; Kodama S.; Shirane S.; Ichida T.; Makino S.; Yoshino M.; Kang J.-H.; Mizuguchi M.; Barshop B.A.; Fuchinoue S.; Seneca S.; Zeesman S.; Knerr I.; Rodes M.; Wasant P.; Yoshida I.; De Meirleir L.; Abdul-Jalil M.; Begum L.; Horiuchi M.; Katunuma N.; Nakagawa S.; Saheki T.;
Hum. Mutat. 22:24-34(2003)
Cited for: VARIANTS CTLN1 ARG-19; HIS-86; SER-95; SER-96; ASP-117; SER-117; CYS-157; ARG-179; LYS-191; HIS-265; MET-269; CYS-272; LYS-283; TRP-304; GLN-310; SER-324; VAL-362; GLN-363; TRP-363; ILE-389 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.