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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9Y617: Variant p.Ser43Arg

Phosphoserine aminotransferase
Gene: PSAT1
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Variant information Variant position: help 43 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 Serine (S) to Arginine (R) at position 43 (S43R, p.Ser43Arg). 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 small size and polar (S) to large size and basic (R) 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 PSATD; reduced O-phospho-L-serine:2-oxoglutarate aminotransferase catalytic efficiency; 3-fold increase of KM for 3-phosphohydroxypyruvate; 5-fold increase of KM for L-glutamate; decreased function in L-serine biosynthesis shown through in vitro reconstruction of the phosphorylated pathway; does not affect secondary structure; does not affect dimerization; does not affect thermal stability. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 43 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 370 The length of the canonical sequence.
Location on the sequence: help LEIQKELLDYKGVGISVLEM S HRSSDFAKIINNTENLVREL 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                         LEIQKELLDYKGVGISVLEMSHRSSDFAKIINNTENLVREL

Mouse                         LEIQKQLLDYRGLGISVLEMSHRSSDFAKIIGNTENLVREL

Rabbit                        LEIQKELLDYKGLGISVLEMSHRSSDFAKIVNNTENLVREL

Caenorhabditis elegans        LKMQEEQLNFNNLGVSVIEMSHRSKEFGALLNETISLIREL

Drosophila                    KEVQENLVNCNGSGISVMEMSHRSSNYAKIHDATISDLREL

Slime mold                    LEAQKELLNFQGCGKSIMEVSHRGKEFEGVINETKSNLKKL

Baker's yeast                 QQAAKDLINFNDIGLGIGEISHRSKDATKVIEDSKKHLIEL

Fission yeast                 EEFGKDFVNFQGLGMGVAEISHRSKQGSGIVTSAESNFRKL
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 – 370 Phosphoserine aminotransferase
Binding site 44 – 44 in other chain
Binding site 45 – 45 in other chain
Modified residue 51 – 51 N6-acetyllysine



Literature citations
Expanding the genotypic and phenotypic spectrum of severe serine biosynthesis disorders.
Abdelfattah F.; Kariminejad A.; Kahlert A.K.; Morrison P.J.; Gumus E.; Mathews K.D.; Darbro B.W.; Amor D.J.; Walsh M.; Sznajer Y.; Weiss L.; Weidensee S.; Chitayat D.; Shannon P.; Bermejo-Sanchez E.; Riano-Galan I.; Hayes I.; Poke G.; Rooryck C.; Pennamen P.; Khung-Savatovsky S.; Toutain A.; Vuillaume M.L.; Ghaderi-Sohi S.; Kariminejad M.H.; Weinert S.; Sticht H.; Zenker M.; Schanze D.;
Hum. Mutat. 41:1615-1628(2020)
Cited for: VARIANT PSATD ARG-43; VARIANTS NLS2 TRP-61; TRP-79; VAL-99; GLN-155 AND ARG-245; Phosphoserine aminotransferase pathogenetic variants in serine deficiency disorders: A functional characterization.
Marchesani F.; Michielon A.; Viale E.; Bianchera A.; Cavazzini D.; Pollegioni L.; Murtas G.; Mozzarelli A.; Bettati S.; Peracchi A.; Campanini B.; Bruno S.;
Biomolecules 13:0-0(2023)
Cited for: CHARACTERIZATION OF VARIANTS PSATD ARG-43 AND ALA-100; CHARACTERIZATION OF VARIANTS NLS2 TRP-79; VAL-99; LEU-179; ARG-245 AND TRP-342; CHARACTERIZATION OF VARIANT ALA-87; FUNCTION; PATHWAY; BIOPHYSICOCHEMICAL PROPERTIES; CATALYTIC ACTIVITY; SUBUNIT;
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.