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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P00966: Variant p.Thr91Pro

Argininosuccinate synthase
Gene: ASS1
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Variant information Variant position: help 91 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 Threonine (T) to Proline (P) at position 91 (T91P, p.Thr91Pro). 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 (T) to medium size and hydrophobic (P) 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 CTLN1; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 91 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 412 The length of the canonical sequence.
Location on the sequence: help EFIWPAIQSSALYEDRYLLG T SLARPCIARKQVEIAQREGA 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                         EFIWPAIQSSALYEDRYLLGTSLARPCIARKQVEIAQREGA

Mouse                         EFIWPAVQSSALYEDRYLLGTSLARPCIARRQVEIAQREGA

Rat                           EFIWPAVQSSALYEDRYLLGTSLARPCIARKQVEIAQREGA

Bovine                        EFIWPAIQSSALYEDRYLLGTSLARPCIARKQVEIAQREGA

Chicken                       DFIWPAVRANALYEDRYMLGSALARPCIARHLVLIAQEEGA

Xenopus laevis                EYIWPAVQANAIYEDRYLLGTSLARPCIAKKQVEIAKKEAA

Xenopus tropicalis            EYIWPAVQANAIYEDRYLLGTSLARPCIAKKQVEIAKKEAA

Zebrafish                     EFIWPALQANALYEDRYLLGTSIARPCIARRQVQIAQREGA

Drosophila                    DYIWPAVQMGLVYEERYLLGTSLARPCISVALMEVAREYGA

Baker's yeast                 DILFPAVQVNAVYEDVYLLGTSLARPVIAKAQIDVAKQEGC

Fission yeast                 DTVIPAAQANAIYENVYLLGTSLARPIIARRQIQIAEKENC
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 1 – 412 Argininosuccinate synthase
Binding site 87 – 87
Binding site 92 – 92
Modified residue 87 – 87 Phosphotyrosine
Turn 90 – 93



Literature citations
Improved standards for prenatal diagnosis of citrullinemia.
Miller M.J.; Soler-Alfonso C.R.; Grund J.E.; Fang P.; Sun Q.; Elsea S.H.; Sutton V.R.;
Mol. Genet. Metab. 112:205-209(2014)
Cited for: VARIANTS CTLN1 PRO-91; CYS-157; ILE-180; LYS-283 AND ARG-390; VARIANT LEU-127; 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.