UniProtKB/Swiss-Prot P00966: Variant p.Gly390Arg

Argininosuccinate synthase
Gene: ASS1
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Variant information Variant position:

390 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 Arginine (R) at position 390 (G390R, p.Gly390Arg). 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 large size and basic (R) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

-2 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 rs121908641 [ dbSNP | Ensembl ]

Sequence information Variant position:

390 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:

YNEELVSMNVQGDYEPTDAT G FININSLRLKEYHRLQSKVT 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                         YNEELVSMNVQGDYEPTDATGFININSLRLKEYHRLQSKVT

Mouse                         YNEELVSMNVQGDYEPIDATGFININSLRLKEYHRLQSKVT

Rat                           YNEELVSMNVQGDYEPIDATGFININSLRLKEYHRLQSKVT

Bovine                        YNEELVSMNVQGDYEPVDATGFININSLRLKEYHRLQNKVT

Chicken                       YNEELVSMDVQGDYEPADATGFININALRLKEYHRLQSKVS

Xenopus laevis                YNEELVSMDVQGDYDPADACGFIKINAVRLKEYHRLQKNKK

Xenopus tropicalis            YNEELVSMDVQGDYDPADACGFIRINALRLKEFHRLQKSKK

Zebrafish                     YNEELVSMDVQGDYDPCDASGFIKINAVRLREHNRLQGAAL

Drosophila                    YNEQLVSMDVHGGYVPQDAGGFIAINAVRIREHVRAFGAYD

Baker's yeast                 YDPTESSMDELTGFLPTDTTGFIAIQAIRIKKYGESKKTKG

Fission yeast                 YDEKLSSMDELGGFDPTWTSGFIQIESMRLRNSDEGKHWM-

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
Helix	385 – 404

Literature citations
Structure of the human argininosuccinate synthetase gene and an improved system for molecular diagnostics in patients with classical and mild citrullinemia.
Haeberle J.; Pauli S.; Linnebank M.; Kleijer W.J.; Bakker H.D.; Wanders R.J.A.; Harms E.; Koch H.G.;
Hum. Genet. 110:327-333(2002)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]; VARIANTS CTLN1 LEU-108; ARG-179; VAL-362 AND ARG-390; 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; Phenotype and genotype heterogeneity in Mediterranean citrullinemia.
Vilaseca M.A.; Kobayashi K.; Briones P.; Lambruschini N.; Campistol J.; Tabata A.; Alomar A.; Rodes M.; Lluch M.; Saheki T.;
Mol. Genet. Metab. 74:396-398(2001)
Cited for: VARIANTS CTLN1 ALA-69; LEU-108; ASP-117; ILE-119; GLN-270 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; 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; 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;

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.