Expasy logo

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot O43511: Variant p.Gly672Glu

Pendrin
Gene: SLC26A4
Feedback?
Variant information Variant position: help 672 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 Glutamate (E) at position 672 (G672E, p.Gly672Glu). 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 (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 PDS; partially affects protein localization to cell membrane; abolishes iodide transport. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 672 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 780 The length of the canonical sequence.
Location on the sequence: help KVPIHSLVLDCGAISFLDVV G VRSLRVIVKEFQRIDVNVYF 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                         KVPIHSLVLDCGAISFLDVVGVRSLRVIVKEFQRIDVNVYF

Mouse                         KVPIHSLVLDCGAVSFLDVVGVRSLRMIVKEFQRIDVNVYF

Rat                           KVPIHSLVLDCGAVSFLDVVGVRSLRMIVKEFQRIDVNVYF
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 – 780 Pendrin
Topological domain 508 – 780 Cytoplasmic
Domain 535 – 729 STAS



Literature citations
Molecular analysis of the PDS gene in Pendred syndrome (sensorineural hearing loss and goitre).
Coyle B.; Reardon W.; Herbrick J.-A.; Tsui L.-C.; Gausden E.; Lee J.; Coffey R.; Grueters A.; Grossman A.; Phelps P.D.; Luxon L.; Kendall-Taylor P.; Scherer S.W.; Trembath R.C.;
Hum. Mol. Genet. 7:1105-1112(1998)
Cited for: VARIANTS PDS PHE-138; PRO-236; GLY-384; HIS-409; MET-410; PRO-416; HIS-530; CYS-556 AND GLU-672; Pendred syndrome, DFNB4, and PDS/SLC26A4 identification of eight novel mutations and possible genotype-phenotype correlations.
Campbell C.; Cucci R.A.; Prasad S.; Green G.E.; Edeal J.B.; Galer C.E.; Karniski L.P.; Sheffield V.C.; Smith R.J.H.;
Hum. Mutat. 17:403-411(2001)
Cited for: VARIANTS PDS GLN-29; CYS-105; ASP-106; PHE-138; VAL-209; PRO-236; LEU-335; PRO-416; ASP-480; HIS-530; ALA-653 AND GLU-672; VARIANT SER-597; Mutations of the PDS gene, encoding pendrin, are associated with protein mislocalization and loss of iodide efflux: implications for thyroid dysfunction in Pendred syndrome.
Taylor J.P.; Metcalfe R.A.; Watson P.F.; Weetman A.P.; Trembath R.C.;
J. Clin. Endocrinol. Metab. 87:1778-1784(2002)
Cited for: CHARACTERIZATION OF VARIANTS PDS ARG-102; PHE-117; PHE-138; VAL-209; PRO-236; MET-410; ARG-446; CYS-556 AND GLU-672; FUNCTION; TRANSPORTER ACTIVITY; SUBCELLULAR LOCATION; Pendred syndrome and DFNB4-mutation screening of SLC26A4 by denaturing high-performance liquid chromatography and the identification of eleven novel mutations.
Prasad S.; Koelln K.A.; Cucci R.A.; Trembath R.C.; Van Camp G.; Smith R.J.H.;
Am. J. Med. Genet. A 124:1-9(2004)
Cited for: VARIANTS PDS/DFNB4 GLY-24; GLN-29; CYS-78; VAL-104; CYS-105; ASP-106; PHE-138; ALA-139; VAL-209; PRO-236; HIS-271; LEU-335; GLY-384; HIS-409; MET-410; PRO-416; ARG-421; ALA-429 DEL; TRP-445; ASP-480; HIS-530; CYS-556; TYR-565; ALA-653; GLU-672; SER-683 AND ARG-723; VARIANTS TYR-324 AND SER-597;
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.