Expasy logo

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9Y617: Variant p.Ala99Val

Phosphoserine aminotransferase
Gene: PSAT1
Feedback?
Variant information Variant position: help 99 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 Alanine (A) to Valine (V) at position 99 (A99V, p.Ala99Val). 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 hydrophobic (A) to medium size and hydrophobic (V) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 0 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 NLS2; does not affect secondary structure; does not affect dimerization; increased 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 99 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 GCGQFSAVPLNLIGLKAGRC A DYVVTGAWSAKAAEEAKKFG 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                         GCGQFSAVPLNLIGLKAGR-------CADYVVTGAWSAKAAEEAKKFG

Mouse                         GSGQFSAVPLNLIGLKAGR-------SADYVVTGAWSAKAA

Rabbit                        GCGQFSAVPLNLIGLKPGR-------CADYVVTGAWSAKAA

Caenorhabditis elegans        GTGQFAAIPLNLKGDHEH---------ADYIVTGAWSSKAA

Drosophila                    GTGQFAAVALNLIGKTGT---------ADYVITGSWSAKAA

Slime mold                    ASSLFAGIPMNLCENGVED-------IVDFIVTGSWSKQAS

Baker's yeast                 GTTGFSSVATNLAAAYVGKHG--KIAPAGYLVTGSWSQKSF

Fission yeast                 GTEQFAACLYNVYAHHALKNGNAKSLVANYIITGAWSKKAY
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 79 – 79
Binding site 80 – 80
Binding site 107 – 107
Beta strand 98 – 102



Literature citations
Neu-Laxova syndrome is a heterogeneous metabolic disorder caused by defects in enzymes of the L-serine biosynthesis pathway.
Acuna-Hidalgo R.; Schanze D.; Kariminejad A.; Nordgren A.; Kariminejad M.H.; Conner P.; Grigelioniene G.; Nilsson D.; Nordenskjold M.; Wedell A.; Freyer C.; Wredenberg A.; Wieczorek D.; Gillessen-Kaesbach G.; Kayserili H.; Elcioglu N.; Ghaderi-Sohi S.; Goodarzi P.; Setayesh H.; van de Vorst M.; Steehouwer M.; Pfundt R.; Krabichler B.; Curry C.; MacKenzie M.G.; Boycott K.M.; Gilissen C.; Janecke A.R.; Hoischen A.; Zenker M.;
Am. J. Hum. Genet. 95:285-293(2014)
Cited for: VARIANTS NLS2 VAL-99 AND LEU-179; INVOLVEMENT IN NLS2; 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.