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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9NRM0: Variant p.Asn333Ser

Solute carrier family 2, facilitated glucose transporter member 9
Gene: SLC2A9
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Variant information Variant position: help 333 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 Asparagine (N) to Serine (S) at position 333 (N333S, p.Asn333Ser). 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 polar (N) to small size and polar (S) 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 RHUC2; decreased urate uptake; increased Km for urate; no effect on protein expression; no effect on glucose transport. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 333 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 540 The length of the canonical sequence.
Location on the sequence: help VRWQVVTVIVTMACYQLCGL N AIWFYTNSIFGKAGIPPAKI 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                         VRWQVVTVIVTMACYQLCGLNAIWFYTNSIFGKAGIPPAKI

Mouse                         VRWQVITVIITMASYQLCGLNAIWFYTNSIFGKAGIPQDKI
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 – 540 Solute carrier family 2, facilitated glucose transporter member 9
Transmembrane 317 – 337 Helical; Name=7
Mutagenesis 326 – 326 C -> G. No effect on urate and fructose transport.
Mutagenesis 330 – 330 C -> S. Increased fructose transport. Highly reduced urate transport.
Mutagenesis 332 – 332 L -> V. Increased fructose binding affinity and decreased fructose transport capacity.



Literature citations
Acute kidney injury in two children caused by renal hypouricaemia type 2.
Stiburkova B.; Taylor J.; Marinaki A.M.; Sebesta I.;
Pediatr. Nephrol. 27:1411-1415(2012)
Cited for: VARIANTS RHUC2 ARG-216 AND SER-333; VARIANTS ILE-282; HIS-294 AND LEU-350; Human Mutations in SLC2A9 (Glut9) Affect Transport Capacity for Urate.
Ruiz A.; Gautschi I.; Schild L.; Bonny O.;
Front. Physiol. 9:476-476(2018)
Cited for: FUNCTION; TRANSPORTER ACTIVITY; CHARACTERIZATION OF VARIANTS RHUC2 ARG-75; MET-125; CYS-171; CYS-198; ARG-216; SER-333; TRP-380 AND ARG-412; CHARACTERIZATION OF VARIANTS HIS-294 AND LEU-350; MUTAGENESIS OF CYS-210;
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.