Expasy logo

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P82251: Variant p.Asn227Asp

b(0,+)-type amino acid transporter 1
Gene: SLC7A9
Feedback?
Variant information Variant position: help 227 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 Aspartate (D) at position 227 (N227D, p.Asn227Asp). 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 medium size and acidic (D) 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 CSNU; decreased amino acid transport activity. Any additional useful information about the variant.


Sequence information Variant position: help 227 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 487 The length of the canonical sequence.
Location on the sequence: help FDNSFEGAQLSVGAISLAFY N GLWAYDGWNQLNYITEELRN 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                         FDNSFEGAQLSVGAISLAFYNGLWAYDGWNQLNYITEELRN

Mouse                         FQNSFEGTQTSVGAISLAFYNGLWAYDGWNQLNYITEELRN

Rat                           FQNSFEGSQTSVGSISLAFYNGLWAYDGWNQLNYITEELRN

Rabbit                        FENSFEGAEVSVGAISLALYNGLWAYDGWNQLNYITEELRN

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 – 487 b(0,+)-type amino acid transporter 1
Transmembrane 218 – 238 Helical
Binding site 233 – 233
Mutagenesis 230 – 230 W -> A. Abolishes amino acid transport activity.
Mutagenesis 233 – 233 D -> A. Complete loss of amino acid transport activity.
Mutagenesis 235 – 235 W -> A. Complete loss of amino acid transport activity.
Mutagenesis 237 – 237 Q -> A. Reduces amino acid transport activity.
Helix 220 – 230



Literature citations
A novel missense mutation of SLC7A9 frequent in Japanese cystinuria cases affecting the C-terminus of the transporter.
Shigeta Y.; Kanai Y.; Chairoungdua A.; Ahmed N.; Sakamoto S.; Matsuo H.; Kim D.K.; Fujimura M.; Anzai N.; Mizoguchi K.; Ueda T.; Akakura K.; Ichikawa T.; Ito H.; Endou H.;
Kidney Int. 69:1198-1206(2006)
Cited for: VARIANTS CSNU ARG-195; ASP-227; GLN-333 AND LEU-482; CHARACTERIZATION OF VARIANTS CSNU ARG-195; ASP-227; GLN-333 AND LEU-482; VARIANTS ALA-142 AND MET-223; CHARACTERIZATION OF VARIANTS ALA-142 AND MET-223; FUNCTION; SUBCELLULAR LOCATION; MUTAGENESIS OF PRO-482;
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.