UniProtKB/Swiss-Prot P00966: Variant p.Gly324Ser

Argininosuccinate synthase
Gene: ASS1
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Variant information Variant position:

324 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 Glycine (G) to Serine (S) at position 324 (G324S, p.Gly324Ser). 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 glycine (G) to small size and polar (S) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

0 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.

Variant rs121908639 [ dbSNP | Ensembl ]

Sequence information Variant position:

324 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:

REVRKIKQGLGLKFAELVYT G FWHSPECEFVRHCIAKSQER 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                         REVRKIKQGL-GLKFAELVYTGFWHSPECEFVRHCIAKSQER

Mouse                         REVRKIKQGL-GLKFAELVYTGFWHSPECEFVRHCIQKSQE

Rat                           REVRKIKQGL-GLKFAELVYTGFWHSPECEFVRHCIDKSQE

Bovine                        REVRKIKQGL-GLKFAELVYTGFWHSPECEFVRHCIAKSQE

Chicken                       REVRKIKQGL-SLKFSELVYNGFWYSPECEFLKHCIARSQQ

Xenopus laevis                REMRKIKQQL-SQRFAEQIYNGFWYSPECEFVRSCISKSQE

Xenopus tropicalis            REVRKIKQHL-SQRFAEQIYNGFWYSPECEFVRSCITKSQE

Zebrafish                     REVRKIKQSL-GIKFSELIYNGFWFSPECEFVRECVERSQK

Drosophila                    REVLRTKQVL-RDRMADYVYNGFWFSPEAIYARKCIELAEQ

Baker's yeast                 KEVRQLRDSFVTPNYSRLIYNGSYFTPECEYIRSMIQPSQN

Fission yeast                 REVRALRDQFVTFNLAKILYNGQFFSPCTRMLLAANNVSQE

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.

Type	Positions	Description
Chain	1 – 412	Argininosuccinate synthase

Literature citations
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; 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; Mild citrullinemia in Caucasians is an allelic variant of argininosuccinate synthetase deficiency (citrullinemia type 1).
Haeberle J.; Pauli S.; Schmidt E.; Schulze-Eilfing B.; Berning C.; Koch H.G.;
Mol. Genet. Metab. 80:302-306(2003)
Cited for: VARIANTS CTLN1 SER-14; LEU-40; GLN-127; ARG-179; ASP-190; GLU-202; MET-263; MET-269; SER-324; GLY-345 AND VAL-362; 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; 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 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.