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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q8N6F1: Variant p.Gln57Glu

Claudin-19
Gene: CLDN19
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Variant information Variant position: help 57 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 Glutamine (Q) to Glutamate (E) at position 57 (Q57E, p.Gln57Glu). 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 (Q) to medium size and acidic (E) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 2 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 HOMG5; localizes throughout the apical part of polarized epithelia in a diffuse pattern; more than 90% decrease of homomeric interactions; loss of interaction with CLDN16; loss of cation-selective paracellular permeability; no effect on interaction with CLDN18. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 57 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 224 The length of the canonical sequence.
Location on the sequence: help GDAIITAVGLYEGLWMSCAS Q STGQVQCKLYDSLLALDGHI 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                         GDAIITAVGLYEGLWMSCASQSTGQVQCKLYDSLLALDGHI

Mouse                         GDAIITAVGLYEGLWMSCASQSTGQVQCKLYDSLLALDGHI

Rat                           GDAIITAVGLYEGLWMSCASQSTGQVQCKLYDSLLALDGHI
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 – 224 Claudin-19
Topological domain 29 – 81 Extracellular
Disulfide bond 54 – 64



Literature citations
Claudin-16 and claudin-19 interact and form a cation-selective tight junction complex.
Hou J.; Renigunta A.; Konrad M.; Gomes A.S.; Schneeberger E.E.; Paul D.L.; Waldegger S.; Goodenough D.A.;
J. Clin. Invest. 118:619-628(2008)
Cited for: FUNCTION; TRANSPORTER ACTIVITY; SUBUNIT; SUBCELLULAR LOCATION; INTERACTION WITH CLDN16; VARIANTS HOMG5 ASP-20; GLU-57; PRO-90 AND ARG-123; Claudin-16 and claudin-19 interaction is required for their assembly into tight junctions and for renal reabsorption of magnesium.
Hou J.; Renigunta A.; Gomes A.S.; Hou M.; Paul D.L.; Waldegger S.; Goodenough D.A.;
Proc. Natl. Acad. Sci. U.S.A. 106:15350-15355(2009)
Cited for: INTERACTION WITH CLDN10; CLDN16 AND CLDN18; CHARACTERIZATION OF VARIANTS HOMG5 ASP-20; GLU-57; PRO-90 AND ARG-123; Mutations in the tight-junction gene claudin 19 (CLDN19) are associated with renal magnesium wasting, renal failure, and severe ocular involvement.
Konrad M.; Schaller A.; Seelow D.; Pandey A.V.; Waldegger S.; Lesslauer A.; Vitzthum H.; Suzuki Y.; Luk J.M.; Becker C.; Schlingmann K.P.; Schmid M.; Rodriguez-Soriano J.; Ariceta G.; Cano F.; Enriquez R.; Jueppner H.; Bakkaloglu S.A.; Hediger M.A.; Gallati S.; Neuhauss S.C.F.; Nuernberg P.; Weber S.;
Am. J. Hum. Genet. 79:949-957(2006)
Cited for: INVOLVEMENT IN HOMG5; VARIANTS HOMG5 ASP-20; GLU-57 AND PRO-90; 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.