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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P00966: Variant p.Arg304Trp

Argininosuccinate synthase
Gene: ASS1
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Variant information Variant position: help 304 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 Tryptophan (W) at position 304 (R304W, p.Arg304Trp). 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 large size and aromatic (W) 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; decreased protein abundance. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 304 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 TPAGTILYHAHLDIEAFTMD R EVRKIKQGLGLKFAELVYTG 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                         TPAGTILYHAHLDIEAFTMDREVRKIKQGL-GLKFAELVYTG

Mouse                         TPAGTILYHAHLDIEAFTMDREVRKIKQGL-GLKFAELVYT

Rat                           TPAGTILYHAHLDIEAFTMDREVRKIKQGL-GLKFAELVYT

Bovine                        TPAGTILYHAHLDIEAFTMDREVRKIKQGL-GLKFAELVYT

Chicken                       TPAGTILYHAHLDIEAFTMDREVRKIKQGL-SLKFSELVYN

Xenopus laevis                TPAGTILYQAHLDIEAFTMDREMRKIKQQL-SQRFAEQIYN

Xenopus tropicalis            TPAGTILYQAHLDVEAFTMDREVRKIKQHL-SQRFAEQIYN

Zebrafish                     TPGGTVLLQAHLDIETFTMDREVRKIKQSL-GIKFSELIYN

Drosophila                    TPGGTILFAAHQDLEVFALDREVLRTKQVL-RDRMADYVYN

Baker's yeast                 QAPLTVLRKAHVDLEGLTLDKEVRQLRDSFVTPNYSRLIYN

Fission yeast                 TPGLTILRTAHMDLEGLTMEREVRALRDQFVTFNLAKILYN
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
Helix 304 – 323



Literature citations
Characterization of human wild-type and mutant argininosuccinate synthetase proteins expressed in bacterial cells.
Shaheen N.; Kobayashi K.; Terazono H.; Fukushige T.; Horiuchi M.; Saheki T.;
Enzyme Protein 48:251-264(1994)
Cited for: CHARACTERIZATION OF VARIANTS CLNT1 VAL-192; ARG-280; CYS-272 AND TRP-304; FUNCTION; CATALYTIC ACTIVITY; PATHWAY; Heterogeneity of mutations in argininosuccinate synthetase causing human citrullinemia.
Kobayashi K.; Jackson M.J.; Tick D.B.; O'Brien W.E.; Beaudet A.L.;
J. Biol. Chem. 265:11361-11367(1990)
Cited for: INVOLVEMENT IN CTLN1; VARIANTS CTLN1 SER-14; HIS-157; ASN-180; TRP-304; SER-324; TRP-363 AND ARG-390; Mutations in argininosuccinate synthetase mRNA of Japanese patients, causing classical citrullinemia.
Kobayashi K.; Shaheen N.; Terazono H.; Saheki T.;
Am. J. Hum. Genet. 55:1103-1112(1994)
Cited for: VARIANTS CTLN1 THR-118; VAL-192; CYS-272; ARG-280; TRP-304 AND LEU-363; 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;
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.