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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot O60931: Variant p.Leu158Pro

Cystinosin
Gene: CTNS
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Variant information Variant position: help 158 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 Leucine (L) to Proline (P) at position 158 (L158P, p.Leu158Pro). 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 Similar physico-chemical property. Both residues are medium size and hydrophobic. The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -3 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 CTNS; abolished cystine transport. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 158 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 367 The length of the canonical sequence.
Location on the sequence: help WSISFYPQVIMNWRRKSVIG L SFDFVALNLTGFVAYSVFNI 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                         WSISFYPQVIMNWRRKSVIGLSFDFVALNLTGFVAYSVFNI

Mouse                         WSVSFYPQVIQNWRRKSVIGLSFDFLALNLTGFVAYSVFNI

Bovine                        WSVSFYPQVITNWRRKSVVGLSFDFVVLNLMGFVAYSVFNI

Caenorhabditis elegans        WSISFYPQMYLNFKRKSVVGLNFDFLSLNLVGFCAYAIFNL

Drosophila                    WSVSFYPQIWSNYRRKSVEGLNFDFLALNIVGFTLYSMFNC

Slime mold                    WSLSFYPQVILNFRKKNVIGLSFDFLLFNITGYACYSVFNS
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 23 – 367 Cystinosin
Topological domain 151 – 159 Cytoplasmic
Domain 123 – 189 PQ-loop 1
Binding site 166 – 166
Mutagenesis 138 – 138 W -> F. Abolished cystine transport.
Mutagenesis 142 – 142 F -> A. Abolished cystine transport.
Mutagenesis 143 – 143 Y -> F. Slightly decreased midpoint potential. Impaired dielectric distance.
Mutagenesis 145 – 145 Q -> A. Increased cystine uptake activity.
Mutagenesis 152 – 152 R -> Q. Impaired dielectric distance.
Mutagenesis 161 – 161 D -> N. Strongly reduced steady-state transport current. Slightly decreased midpoint potential.
Mutagenesis 166 – 166 N -> A. Abolished cystine transport.
Mutagenesis 170 – 170 F -> A. Strongly decreased cystine transport.
Beta strand 156 – 158



Literature citations
Molecular analysis of cystinosis: probable Irish origin of the most common French Canadian mutation.
McGowan-Jordan J.; Stoddard K.; Podolsky L.; Orrbine E.; McLaine P.; Town M.; Goodyer P.; MacKenzie A.; Heick H.;
Eur. J. Hum. Genet. 7:671-678(1999)
Cited for: VARIANTS CTNS PHE-133 AND PRO-158; Molecular pathogenesis of cystinosis: effect of CTNS mutations on the transport activity and subcellular localization of cystinosin.
Kalatzis V.; Nevo N.; Cherqui S.; Gasnier B.; Antignac C.;
Hum. Mol. Genet. 13:1361-1371(2004)
Cited for: FUNCTION; SUBCELLULAR LOCATION; CHARACTERIZATION OF VARIANTS CTNS VAL-110; PHE-133; PHE-139; PHE-141; PRO-158; ASP-169; SER-177; ARG-182; ASN-205; ASP-205 DEL; ARG-222; SER-270 DEL; LYS-288; ASN-298; TYR-305; ARG-308; PRO-338; ARG-339; 343-ILE--ASP-346 DEL; ASP-346--349-PHE DEL AND ASP-VAL-GLU-PHE-349 INS; CHARACTERIZATION OF VARIANT CTNSJAN 67-ILE--PRO-73 DEL; PRO-CYS-SER-154 INS; LEU-200; ARG-280; LYS-323 AND ASN-346; CHARACTERIZATION OF VARIANT CTNSANN ARG-197; CHARACTERIZATION OF VARIANT ILE-42 AND ILE-260;
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.