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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9NRA2: Variant p.His183Arg

Sialin
Gene: SLC17A5
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Variant information Variant position: help 183 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 Histidine (H) to Arginine (R) at position 183 (H183R, p.His183Arg). 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 (H) to large size and basic (R) 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 ISSD; alters intracellular localization, only partially targeted to lysosomes and mainly detected in LAMP1-negative vesicles and in the Golgi apparatus; abolishes H(+)-coupled sialic acid transporter activity; has normal L-aspartate and L-glutamate transporter activity. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 183 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 495 The length of the canonical sequence.
Location on the sequence: help PLIVLRALEGLGEGVTFPAM H AMWSSWAPPLERSKLLSISY 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                         PLIVLRALEGLGEGVTFPAMHAMWSSWAPPLERSKLLSISY

Mouse                         TLVVLRALEGLGEGVTFPAMHAMWSSWAPPLERSKLLTISY

Rat                           ALIVLRALEGLGEGVTFPAMHAMWSSWAPPLERSKLLTISY

Sheep                         ALVALRALEGLGEGVTYPAMHAMWSSWAPPLERSKLLSISY

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 – 495 Sialin
Topological domain 180 – 200 Cytoplasmic
Helix 178 – 189



Literature citations
A new gene, encoding an anion transporter, is mutated in sialic acid storage diseases.
Verheijen F.W.; Verbeek E.; Aula N.; Beerens C.E.M.T.; Havelaar A.C.; Joosse M.; Peltonen L.; Aula P.; Galjaard H.; Van der Spek P.J.; Mancini G.M.S.;
Nat. Genet. 23:462-465(1999)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1); TISSUE SPECIFICITY; VARIANT SD CYS-39; VARIANTS ISSD 268-SER--ASN-272 DEL; ARG-183 AND ARG-334; Functional characterization of wild-type and mutant human sialin.
Morin P.; Sagne C.; Gasnier B.;
EMBO J. 23:4560-4570(2004)
Cited for: FUNCTION; TRANSPORT ACTIVITY; BIOPHYSICOCHEMICAL PROPERTIES; SUBCELLULAR LOCATION; DILEUCINE MOTIF; MUTAGENESIS OF 22-LEU-LEU-23; 198-LEU-LEU-199 AND 266-ILE-LEU-267; CHARACTERIZATION OF VARIANTS SD CYS-39 AND GLU-136; CHARACTERIZATION OF VARIANTS ISSD ARG-183; 268-SER--ASN-272 DEL AND ARG-334; Functional characterization of vesicular excitatory amino acid transport by human sialin.
Miyaji T.; Omote H.; Moriyama Y.;
J. Neurochem. 119:1-5(2011)
Cited for: FUNCTION; TRANSPORT ACTIVITY; BIOPHYSICOCHEMICAL PROPERTIES; SUBCELLULAR LOCATION; CHARACTERIZATION OF VARIANTS SD CYS-39 AND GLU-136; CHARACTERIZATION OF VARIANTS ISSD ARG-183; 268-SER--ASN-272 DEL; GLU-328; ARG-334 AND VAL-371; Sialin (SLC17A5) functions as a nitrate transporter in the plasma membrane.
Qin L.; Liu X.; Sun Q.; Fan Z.; Xia D.; Ding G.; Ong H.L.; Adams D.; Gahl W.A.; Zheng C.; Qi S.; Jin L.; Zhang C.; Gu L.; He J.; Deng D.; Ambudkar I.S.; Wang S.;
Proc. Natl. Acad. Sci. U.S.A. 109:13434-13439(2012)
Cited for: FUNCTION; TRANSPORT ACTIVITY; SUBCELLULAR LOCATION; TISSUE SPECIFICITY; MUTAGENESIS OF 22-LEU-LEU-23; CHARACTERIZATION OF VARIANT SD CYS-39; CHARACTERIZATION OF VARIANT ISSD ARG-183; The spectrum of SLC17A5-gene mutations resulting in free sialic acid-storage diseases indicates some genotype-phenotype correlation.
Aula N.; Salomaeki P.; Timonen R.; Verheijen F.; Mancini G.M.S.; Maensson J.-E.; Aula P.; Peltonen L.;
Am. J. Hum. Genet. 67:832-840(2000)
Cited for: VARIANTS SD CYS-39 AND GLU-136; VARIANTS ISSD 268-SER--ASN-272 DEL; ARG-183; ARG-334 AND VAL-371;
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.