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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q8N159: Variant p.Leu430Pro

N-acetylglutamate synthase, mitochondrial
Gene: NAGS
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Variant information Variant position: help 430 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 Leucine (L) to Proline (P) at position 430 (L430P, p.Leu430Pro). 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 Similar physico-chemical property. Both residues are medium size and hydrophobic. 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 NAGSD; markedly decreases activity. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 430 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 534 The length of the canonical sequence.
Location on the sequence: help SLRPRLHSIYVSEGYNAAAI L TMEPVLGGTPYLDKFVVSSS 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                         SLRPRLHSIYVSEGYNAAAILTMEPVLGGT----PYLDKFVVSSS

Mouse                         SLRPRLHSIYVSEGYNAAAILTVEPVLGGT----PYLDKFV

Zebrafish                     SLEGRLHSVYLSEGYSAAAIITTEPVNSGT----PYLDKFV

Baker's yeast                 RINGKIATIIVIGDYEGIAILTYEGSEENSFV---YLDKFA

Fission yeast                 RLKNSLAAVIIAGDYLGTAIVTYEQPDGTTNEKVPYLDKLA
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 19 – 534 N-acetylglutamate synthase long form
Chain 51 – 534 N-acetylglutamate synthase short form
Chain 92 – 534 N-acetylglutamate synthase conserved domain form
Domain 375 – 526 N-acetyltransferase
Binding site 444 – 444
Mutagenesis 441 – 441 Y -> F. 15% reduction in catalytic activity.
Beta strand 424 – 435



Literature citations
Mutation analysis in patients with N-acetylglutamate synthase deficiency.
Haeberle J.; Schmidt E.; Pauli S.; Kreuder J.G.; Plecko B.; Galler A.; Wermuth B.; Harms E.; Koch H.G.;
Hum. Mutat. 21:593-597(2003)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]; TISSUE SPECIFICITY; VARIANTS NAGSD PRO-279; PRO-430 AND ARG-484; Identification of novel mutations of the human N-acetylglutamate synthase gene and their functional investigation by expression studies.
Schmidt E.; Nuoffer J.-M.; Haeberle J.; Pauli S.; Guffon N.; Vianey-Saban C.; Wermuth B.; Koch H.G.;
Biochim. Biophys. Acta 1740:54-59(2005)
Cited for: VARIANTS NAGSD ARG-200; PRO-410; PRO-430; ARG-484 AND THR-518; CHARACTERIZATION OF VARIANTS NAGSD ARG-200; PRO-410; PRO-430; ARG-484 AND THR-518;
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.