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UniProtKB/Swiss-Prot Q13253: Variant p.Gly189Cys

Gene: NOG
Variant information

Variant position:  189
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  Disease [Disclaimer]
The variants are classified into three categories: Disease, Polymorphism and Unclassified.
  • Disease: Variants implicated in disease according to literature reports.
  • Polymorphism: Variants not reported to be implicated in disease.
  • Unclassified: Variants with uncertain implication in disease according to literature reports. Evidence against or in favor of a pathogenic role is limited and/or conflicting.

Residue change:  From Glycine (G) to Cysteine (C) at position 189 (G189C, p.Gly189Cys).
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 glycine (G) to medium size and polar (C)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  -3
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

Involvement in disease:  Symphalangism, proximal 1A (SYM1A) [MIM:185800]: A disease characterized by the hereditary absence of the proximal interphalangeal joints. Distal interphalangeal joints are less frequently involved and metacarpophalangeal joints are rarely affected whereas carpal bone malformation and fusion are common. In the lower extremities, tarsal bone coalition is common. Conductive hearing loss is seen and is due to fusion of the stapes to the petrous part of the temporal bone. {ECO:0000269|PubMed:10080184, ECO:0000269|PubMed:11846737, ECO:0000269|PubMed:11857750, ECO:0000269|PubMed:15770128}. Note=The disease is caused by mutations affecting the gene represented in this entry.
The name and a short description of the disease associated with the variant. For more information about the disease, the user can refer to OMIM, following the link provided after the disease acronym.

Variant description:  In SYM1A.
Any additional useful information about the variant.

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

Sequence information

Variant position:  189
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  232
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 28 – 232 Noggin
Disulfide bond 155 – 192
Disulfide bond 178 – 228
Disulfide bond 184 – 230

Literature citations

Heterozygous mutations in the gene encoding noggin affect human joint morphogenesis.
Gong Y.; Krakow D.; Marcelino J.; Wilkin D.; Chitayat D.; Babul-Hirji R.; Hudgins L.; Cremers C.W.; Cremers F.P.M.; Brunner H.G.; Reinker K.; Rimoin D.L.; Cohn D.H.; Goodman F.R.; Reardon W.; Patton M.; Francomano C.A.; Warman M.L.;
Nat. Genet. 21:302-304(1999)
Cited for: VARIANTS SYM1A ARG-35; CYS-189; ASN-220; CYS-222; ASP-222 AND LEU-223; VARIANT SYNS1 GLY-217;

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.