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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P49591: Variant p.Asp172Asn

Serine--tRNA ligase, cytoplasmic
Gene: SARS1
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Variant information Variant position: help 172 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 Aspartate (D) to Asparagine (N) at position 172 (D172N, p.Asp172Asn). 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 medium size and acidic (D) to medium size and polar (N) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 1 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 NEDMAS; impaired serine-activation of enzyme resulting in a significant decrease in the first step of the aminoacylation reaction; reduced protein stability; reduced protein expression. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 172 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 514 The length of the canonical sequence.
Location on the sequence: help DNKVERIWGDCTVRKKYSHV D LVVMVDGFEGEKGAVVAGSR 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                         DNKVERIW-----------GDCTVRKK-YSHVDLVVMVDGFEGEKGAVVAGSR

Mouse                         DNKVERIW-----------GDCTVRKK-YSHVDLVVMVDGF

Rat                           DNKVERIW-----------GDCTVRKK-YSHVDLVVMVDGF

Bovine                        DNKVERIW-----------GDCTVRKK-YSHVDLVVMVDGF

Rabbit                        DNKVERIW-----------GDCTVRKK-YSHVDLVVMVDGF

Zebrafish                     DNKVERTW-----------GDCTVQKK-YSHVDLVVMVDGY

Caenorhabditis elegans        NNKIERTF-----------GDLSTKKK-YSHVDLVVMVDGF

Slime mold                    NNQIIKTW-----------GECKTSEGLLHHHELLEMIDGY

Baker's yeast                 NNELVRTWKPEDLEAVGPIASVTGKPASLSHHEILLRLDGY

Fission yeast                 NNEIIRKWAPE--------GVTVEKKNCLSHHEVLTRLDGY

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 – 514 Serine--tRNA ligase, cytoplasmic
Helix 170 – 176



Literature citations
Mutations of the aminoacyl-tRNA-synthetases SARS and WARS2 are implicated in the aetiology of autosomal recessive intellectual disability.
Musante L.; Puettmann L.; Kahrizi K.; Garshasbi M.; Hu H.; Stehr H.; Lipkowitz B.; Otto S.; Jensen L.R.; Tzschach A.; Jamali P.; Wienker T.; Najmabadi H.; Ropers H.H.; Kuss A.W.;
Hum. Mutat. 38:621-636(2017)
Cited for: VARIANT NEDMAS ASN-172; CHARACTERIZATION OF VARIANT NEDMAS ASN-172; INVOLVEMENT IN NEDMAS; FUNCTION; CATALYTIC ACTIVITY; SUBCELLULAR LOCATION; TISSUE SPECIFICITY; MUTAGENESIS OF THR-429;
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.