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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P08243: Variant p.Arg550Cys

Asparagine synthetase [glutamine-hydrolyzing]
Gene: ASNS
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Variant information Variant position: help 550 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 Cysteine (C) at position 550 (R550C, p.Arg550Cys). 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 medium size and polar (C) 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 ASNSD; increases level of 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 550 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 561 The length of the canonical sequence.
Location on the sequence: help ADWLSHYWMPKWINATDPSA R TLTHYKSAVKA 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                         ADWLSHYWMPK--WINATDPSARTLTHYKSAVKA

Mouse                         ADWLTHYWMPK--WINATDPSARTLTHYKSAA

Rat                           ADWLTHYWMPK--WINATDPSARTLTHYKSTA

Bovine                        ADWLPHYWMPR--WTNATDPSARTLTHYKAAA

Chicken                       SSWLPHYWMPR--WVEATDPSARTLKHYKSAI

Slime mold                    CMETVQRWIPT--WGASQDPSGRAQKVHLSTT

Fission yeast                 CADTVMRWVPKAEWGCPEDPSGRYQAGHVAAL
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 2 – 561 Asparagine synthetase [glutamine-hydrolyzing]
Modified residue 545 – 545 Phosphothreonine
Modified residue 557 – 557 Phosphoserine



Literature citations
Deficiency of asparagine synthetase causes congenital microcephaly and a progressive form of encephalopathy.
Ruzzo E.K.; Capo-Chichi J.M.; Ben-Zeev B.; Chitayat D.; Mao H.; Pappas A.L.; Hitomi Y.; Lu Y.F.; Yao X.; Hamdan F.F.; Pelak K.; Reznik-Wolf H.; Bar-Joseph I.; Oz-Levi D.; Lev D.; Lerman-Sagie T.; Leshinsky-Silver E.; Anikster Y.; Ben-Asher E.; Olender T.; Colleaux L.; Decarie J.C.; Blaser S.; Banwell B.; Joshi R.B.; He X.P.; Patry L.; Silver R.J.; Dobrzeniecka S.; Islam M.S.; Hasnat A.; Samuels M.E.; Aryal D.K.; Rodriguiz R.M.; Jiang Y.H.; Wetsel W.C.; McNamara J.O.; Rouleau G.A.; Silver D.L.; Lancet D.; Pras E.; Mitchell G.A.; Michaud J.L.; Goldstein D.B.;
Neuron 80:429-441(2013)
Cited for: VARIANTS ASNSD GLU-6; VAL-362 AND CYS-550; CHARACTERIZATION OF VARIANTS ASNSD GLU-6; VAL-362 AND CYS-550;
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.