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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P00966: Variant p.Arg265Cys

Argininosuccinate synthase
Gene: ASS1
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Variant information Variant position: help 265 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 265 (R265C, p.Arg265Cys). 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 CTLN1; severe clinical course; loss of 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 265 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 QTSLELFMYLNEVAGKHGVG R IDIVENRFIGMKSRGIYETP 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                         QTSLELFMYLNEVAGKHGVGRIDIVENRFIGMKSRGIYETP

Mouse                         TTSLELFMYLNEVAGKHGVGRIDIVENRFIGMKSRGIYETP

Rat                           STSLDLFMYLNEVAGKHGVGRIDIVENRFIGMKSRGIYETP

Bovine                        STALELFLYLNEVAGKHGVGRIDIVENRFIGMKSRGIYETP

Chicken                       RSALELFVYLNDIASKHGVGRVDIVENRFVGMKSRGIYETP

Xenopus laevis                SSSLALFCYLNEVAGKHGVGRIDIVENRFIGMKSRGIYETP

Xenopus tropicalis            SSALGLFCYLNEVAGKHGVGRIDIVENRFIGMKSRGIYETP

Zebrafish                     ETPLEIFCYLNEIGGKHGVGRIDIVENRFIGMKSRGIYETP

Drosophila                    TKPLEMLDFLNKLGGSYGIGRIDIVENRFVGLKSRGVYETP

Baker's yeast                 TKPLDVFLAASNLARANGVGRIDIVEDRYINLKSRGCYEQA

Fission yeast                 SGVVSIFYQLNAIARRNGVGRIDIVENRFSGLKSRGCYETP
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 270 – 270
Binding site 282 – 282
Beta strand 265 – 271



Literature citations
Investigation of citrullinemia type I variants by in vitro expression studies.
Berning C.; Bieger I.; Pauli S.; Vermeulen T.; Vogl T.; Rummel T.; Hoehne W.; Koch H.G.; Rolinski B.; Gempel K.; Haeberle J.;
Hum. Mutat. 29:1222-1227(2008)
Cited for: VARIANTS CTLN1 CYS-265 AND VAL-302; CHARACTERIZATION OF VARIANTS CTLN1 THR-118; ARG-179; VAL-263; CYS-265; VAL-302; SER-324; VAL-362 AND ARG-390; FUNCTION; CATALYTIC ACTIVITY; PATHWAY; BIOPHYSICOCHEMICAL PROPERTIES; Mutations and polymorphisms in the human argininosuccinate synthetase (ASS1) gene.
Engel K.; Hoehne W.; Haeberle J.;
Hum. Mutat. 30:300-307(2009)
Cited for: VARIANTS CTLN1 PRO-79; HIS-96; GLN-127; TRP-127; PRO-160; GLN-191; PRO-206; CYS-265; THR-277; ILE-284; SER-291; GLY-296; VAL-324; PHE-341; ARG-347 AND ASP-359; Functional analysis of novel splicing and missense mutations identified in the ASS1 gene in classical citrullinemia patients.
Kimani J.K.; Wei T.; Chol K.; Li Y.; Yu P.; Ye S.; Huang X.; Qi M.;
Clin. Chim. Acta 438:323-329(2015)
Cited for: VARIANTS CTLN1 GLY-141 AND CYS-265; Mutations in the human argininosuccinate synthetase (ASS1) gene, impact on patients, common changes, and structural considerations.
Diez-Fernandez C.; Ruefenacht V.; Haeberle J.;
Hum. Mutat. 38:471-484(2017)
Cited for: VARIANTS CTLN1 27-GLN--LYS-412 DEL; ILE-64; PRO-79; 97-CYS--LYS-412 DEL; CYS-100; HIS-100; ASP-111; CYS-117; 138-GLN--LYS-412 DEL; SER-157; PRO-160; 163-TYR--LYS-412 DEL; PRO-164; LYS-184; ASP-190; PRO-206; ARG-230; ILE-237; PRO-258; VAL-258; CYS-265; 275-GLY--LYS-412 DEL; THR-277; 279-ARG--LYS-412 DEL; ILE-284; PRO-290; SER-291; GLY-296; ASP-299; VAL-302; GLY-306; CYS-307; 311-GLN--LYS-412 DEL; MET-321; SER-324; VAL-324; HIS-335; PHE-341; 344-ARG--LYS-412 DEL; ARG-347; VAL-356; 357-GLN--LYS-412 DEL; ASP-359; 380-GLN--LYS-412 DEL AND PRO-389;
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.