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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9Y5I7: Variant p.Gly128Ala

Claudin-16
Gene: CLDN16
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Variant information Variant position: help 128 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 Glycine (G) to Alanine (A) at position 128 (G128A, p.Gly128Ala). 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 glycine (G) to small size and hydrophobic (A) 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 HOMG3; localizes at tight junctions; fails to increase paracellular magnesium transport. Any additional useful information about the variant.


Sequence information Variant position: help 128 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 DEPYIKVRICFVAGATLLIA G TPGIIGSVWYAVDVYVERST 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                         DEPYIKVRICFVAGATLLIAGTPGIIGSVWYAVDVYVERST

Mouse                         DDPQIKVRLCFVAGTTLLIAGTPGIIGSVWYAVDVYVERSS

Rat                           DEPHIKVRLCFVAGTVLLIAGTPGIIGSVWYAVDVYVERSS

Bovine                        DEPYIKVRISFVAGTTLLIAGAPGIIGSVWYAVDVYVERSS
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
Transmembrane 116 – 136 Helical



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; 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; A novel claudin 16 mutation associated with childhood hypercalciuria abolishes binding to ZO-1 and results in lysosomal mistargeting.
Mueller D.; Kausalya P.J.; Claverie-Martin F.; Meij I.C.; Eggert P.; Garcia-Nieto V.; Hunziker W.;
Am. J. Hum. Genet. 73:1293-1301(2003)
Cited for: INVOLVEMENT IN HOMG3; CHARACTERIZATION OF VARIANTS HOMG3 ALA-128 AND ARG-233; SUBCELLULAR LOCATION; INTERACTION WITH TJP1; MOTIF; 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.