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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot O43405: Variant p.Pro51Ser

Cochlin
Gene: COCH
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Variant information Variant position: help 51 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 Proline (P) to Serine (S) at position 51 (P51S, p.Pro51Ser). 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 hydrophobic (P) to small size and polar (S) 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 DFNA9; some families may manifest Meniere disease-like symptoms; does not affect protein deposition to the extracellular matrix. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 51 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 550 The length of the canonical sequence.
Location on the sequence: help AITCFTRGLDIRKEKADVLC P GGCPLEEFSVYGNIVYASVS 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                         AITCFTRGLDIRKEKADVLCPGGCPLEEFSVYGNIVYASVS

Mouse                         PVTCFTRGLDIRKEKADVLCPGGCSLEEFSVFGNIVYASVS

Bovine                        PITCSTRGLDIRKEKADVLCPGGCPLEEFSVFGHIVYASVS

Chicken                       AITCFTRGLDLRKETEDVLCPANCPLWQFYVFGDGIYASLS
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 25 – 550 Cochlin
Domain 28 – 121 LCCL



Literature citations
A Pro51Ser mutation in the COCH gene is associated with late onset autosomal dominant progressive sensorineural hearing loss with vestibular defects.
de Kok Y.J.M.; Bom S.J.H.; Brunt T.M.; Kemperman M.H.; van Beusekom E.; van der Velde-Visser S.D.; Robertson N.G.; Morton C.C.; Huygen P.L.M.; Verhagen W.I.M.; Brunner H.G.; Cremers C.W.R.J.; Cremers F.P.M.;
Hum. Mol. Genet. 8:361-366(1999)
Cited for: VARIANT DFNA9 SER-51; High prevalence of symptoms of Meniere's disease in three families with a mutation in the COCH gene.
Fransen E.; Verstreken M.; Verhagen W.I.M.; Wuyts F.L.; Huygen P.L.M.; D'Haese P.; Robertson N.G.; Morton C.C.; McGuirt W.T.; Smith R.J.H.; Declau F.; Van de Heyning P.H.; Van Camp G.;
Hum. Mol. Genet. 8:1425-1429(1999)
Cited for: VARIANT DFNA9 SER-51; Mutations in COCH that result in non-syndromic autosomal dominant deafness (DFNA9) affect matrix deposition of cochlin.
Grabski R.; Szul T.; Sasaki T.; Timpl R.; Mayne R.; Hicks B.; Sztul E.;
Hum. Genet. 113:406-416(2003)
Cited for: CHARACTERIZATION OF VARIANTS DFNA9 SER-51; GLY-66; GLU-88; ASN-109 AND ARG-117;
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.