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UniProtKB/Swiss-Prot O75445: Variant p.Cys419Phe

Gene: USH2A
Variant information

Variant position:  419
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  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:  From Cysteine (C) to Phenylalanine (F) at position 419 (C419F, p.Cys419Phe).
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:  Change from medium size and polar (C) to large size and aromatic (F)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  -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:  In USH2A and RP39.
Any additional useful information about the variant.

Other resources:  
Links to websites of interest for the variant.

Sequence information

Variant position:  419
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  5202
The length of the canonical sequence.

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: 
The multiple alignment of the region surrounding the variant against various orthologous sequences.




Sequence annotation in neighborhood:  
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.

Chain 32 – 5202 Usherin
Topological domain 32 – 5042 Extracellular
Domain 271 – 517 Laminin N-terminal

Literature citations

Genomic structure and identification of novel mutations in usherin, the gene responsible for Usher syndrome type IIa.
Weston M.D.; Eudy J.D.; Fugita S.; Yao S.-F.; Usami S.; Cremers C.; Greenberg J.; Ramesar R.; Martini A.; Moller C.; Smith R.J.; Sumegi J.; Kimberling W.J.;
Am. J. Hum. Genet. 66:1199-1210(2000)

Comprehensive screening of the USH2A gene in Usher syndrome type II and non-syndromic recessive retinitis pigmentosa.
Seyedahmadi B.J.; Rivolta C.; Keene J.A.; Berson E.L.; Dryja T.P.;
Exp. Eye Res. 79:167-173(2004)
Cited for: VARIANTS USH2A ILE-307; ILE-391; PHE-419; CYS-464; VAL-516 THR-517; SER-575; ASN-587 DEL AND LEU-1059; VARIANTS RP39/USH2A ASP-478 AND PHE-759; VARIANTS RP39 LEU-739; ASN-911 AND ARG-1470; VARIANTS THR-125; MET-230; ARG-268; PHE-365; VAL-644; ARG-713; VAL-1047 AND LYS-1486;

USH2A mutation analysis in 70 Dutch families with Usher syndrome type II.
Pennings R.J.E.; Te Brinke H.; Weston M.D.; Claassen A.; Orten D.J.; Weekamp H.; Van Aarem A.; Huygen P.L.M.; Deutman A.F.; Hoefsloot L.H.; Cremers F.P.M.; Cremers C.W.R.J.; Kimberling W.J.; Kremer H.;
Hum. Mutat. 24:185-185(2004)
Cited for: VARIANTS USH2A HIS-346; PHE-419 AND ARG-536; VARIANT ARG-713;

Next-generation genetic testing for retinitis pigmentosa.
Neveling K.; Collin R.W.; Gilissen C.; van Huet R.A.; Visser L.; Kwint M.P.; Gijsen S.J.; Zonneveld M.N.; Wieskamp N.; de Ligt J.; Siemiatkowska A.M.; Hoefsloot L.H.; Buckley M.F.; Kellner U.; Branham K.E.; den Hollander A.I.; Hoischen A.; Hoyng C.; Klevering B.J.; van den Born L.I.; Veltman J.A.; Cremers F.P.; Scheffer H.;
Hum. Mutat. 33:963-972(2012)
Cited for: VARIANTS RP39 PHE-419; PHE-759; CYS-1859; HIS-2460; TYR-3358; ARG-3669; CYS-4115; HIS-4192 AND MET-4425;

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.