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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9Y5I7: Variant p.His71Asp

Claudin-16
Gene: CLDN16
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Variant information Variant position: help 71 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 Aspartate (D) at position 71 (H71D, p.His71Asp). 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 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 HOMG3; localizes at tight junctions; fails to increase paracellular magnesium transport. Any additional useful information about the variant.


Sequence information Variant position: help 71 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 235 The length of the canonical sequence.
Location on the sequence: help VTNAFDGIRTCDEYDSILAE H PLKLVVTRALMITADILAGF 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                         VTNAFDGIRTCDEYDSILAEHPLKLVVTRALMITADILAGF

Mouse                         VTNAFDGIRTCDEYDSIYAEHPLKLVVTRALMITADILAGF

Rat                           VTNAFDGIRTCDEYDSIYAEHPLKLVVTRALMITADILAGF

Bovine                        VTNAFDGIRTCDEYDSILAEHSLKLVVTRALMITADILAGF
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 – 235 Claudin-16
Topological domain 25 – 79 Extracellular
Mutagenesis 56 – 56 D -> S. Localizes at tight junctions; partial loss of paracellular sodium-selective transport.
Mutagenesis 59 – 59 R -> T. No significant effect on protein subcellular localization or paracellular sodium-selective transport.
Mutagenesis 62 – 62 D -> S. No significant effect on protein subcellular localization or paracellular sodium-selective transport.
Mutagenesis 63 – 63 E -> T. No significant effect on protein subcellular localization or paracellular sodium-selective transport.
Mutagenesis 65 – 65 D -> S. No significant effect on protein subcellular localization or paracellular sodium-selective transport.
Mutagenesis 70 – 70 E -> T. Localizes at tight junctions; partial loss of paracellular sodium-selective transport.
Mutagenesis 74 – 74 K -> S. No significant effect on protein subcellular localization or paracellular sodium-selective transport.
Mutagenesis 79 – 79 R -> T. Low protein expression mostly retained in the endoplasmic reticulum; loss of paracellular sodium-selective transport.



Literature citations
Disease-associated mutations affect intracellular traffic and paracellular Mg2+ transport function of Claudin-16.
Kausalya P.J.; Amasheh S.; Guenzel D.; Wurps H.; Mueller D.; Fromm M.; Hunziker W.;
J. Clin. Invest. 116:878-891(2006)
Cited for: FUNCTION; TRANSPORTER ACTIVITY; SUBCELLULAR LOCATION; CHARACTERIZATION OF VARIANTS HOMG3 47-TRP--VAL-235 DEL; VAL-69; ASP-71; PRO-75; 79-ARG--VAL-235 DEL; LEU-79; TRP-81; PHE-81; VAL-92; PRO-97; ARG-121; ALA-128; THR-139; THR-146; CYS-162; ASP-163; PHE-165; PRO-165; ARG-169 AND ARG-233; Familial hypomagnesaemia with hypercalciuria and nephrocalcinosis maps to chromosome 3q27 and is associated with mutations in the PCLN-1 gene.
Weber S.; Hoffmann K.; Jeck N.; Saar K.; Boeswald M.; Kuwertz-Broeking E.; Meij I.I.; Knoers N.V.; Cochat P.; Sulakova T.; Bonzel K.E.; Soergel M.; Manz F.; Schaerer K.; Seyberth H.W.; Reis A.; Konrad M.;
Eur. J. Hum. Genet. 8:414-422(2000)
Cited for: INVOLVEMENT IN HOMG3; VARIANTS HOMG3 ASP-71; PRO-75; PHE-81; PRO-81; TRP-81; ASP-128 AND ARG-169; Novel paracellin-1 mutations in 25 families with familial hypomagnesemia with hypercalciuria and nephrocalcinosis.
Weber S.; Schneider L.; Peters M.; Misselwitz J.; Roennefarth G.; Boeswald M.; Bonzel K.E.; Seeman T.; Sulakova T.; Kuwertz-Broeking E.; Gregoric A.; Palcoux J.-B.; Tasic V.; Manz F.; Schaerer K.; Seyberth H.W.; Konrad M.;
J. Am. Soc. Nephrol. 12:1872-1881(2001)
Cited for: INVOLVEMENT IN HOMG3; VARIANTS HOMG3 ASP-71; PRO-75; LEU-79; PHE-81; TRP-81; ALA-128; THR-139; THR-146; PRO-165 AND ARG-169; FUNCTION;
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.