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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q8N6F1: Variant p.Gly20Asp

Claudin-19
Gene: CLDN19
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Variant information Variant position: help 20 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 Aspartate (D) at position 20 (G20D, p.Gly20Asp). 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 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 HOMG5; ER retention of the mutant protein; more than 90% decrease of homomeric interactions; loss of interaction with CLDN16; loss of cation-selective paracellular permeability; when overexpressed in the retina of PN0 mice, leads to retinal degeneration characterized by altered morphology of bipolar cells, shortened bipolar axon and dendrite lengths and decreased light response; 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 20 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 MANSGLQLLGYFLALGGWV G IIASTALPQWKQSSYAGDAI 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                         MANSGLQLLGYFLALGGWVGIIASTALPQWKQSSYAGDAI

Mouse                         MANSGLQLLGYFLALGGWVGIIASTALPQWKQSSYAGDAI

Rat                           MANSGLQLLGYFLALGGWVGIIASTALPQWKQSSYAGDAI
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
Transmembrane 8 – 28 Helical



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; Disease-associated mutations of claudin-19 disrupt retinal neurogenesis and visual function.
Wang S.B.; Xu T.; Peng S.; Singh D.; Ghiassi-Nejad M.; Adelman R.A.; Rizzolo L.J.;
Commun. Biol. 2:113-113(2019)
Cited for: FUNCTION; CHARACTERIZATION OF VARIANTS HOMG5 ASP-20 AND TRP-81; 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.