UniProtKB/Swiss-Prot P12107: Variant p.Gly796Arg

Collagen alpha-1(XI) chain
Gene: COL11A1
Chromosomal location: 1p21
Variant information

Variant position:  796
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 have been found in patients and disease-association is reported in literature. However, this classification is not a definitive assessment of variant pathogenicity.
  • Polymorphism: No disease-association has been reported.
  • Unclassified: Variants have been found in patients but disease-association remains unclear.

Residue change:  From Glycine (G) to Arginine (R) at position 796 (G796R, p.Gly796Arg).
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 large size and basic (R)
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

Involvement in disease:  Fibrochondrogenesis 1 (FBCG1) [MIM:228520]: A severe short-limbed skeletal dysplasia characterized by broad long-bone metaphyses, pear-shaped vertebral bodies, and characteristic morphology of the growth plate, in which the chondrocytes have a fibroblastic appearance and there are regions of fibrous cartilage extracellular matrix. Clinical features include a flat midface with a small nose and anteverted nares, significant shortening of all limb segments but relatively normal hands and feet, and a small bell-shaped thorax with a protuberant abdomen. 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 FBCG1.
Any additional useful information about the variant.



Sequence information

Variant position:  796
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  1806
The length of the canonical sequence.

Location on the sequence:   SKGEKGEDGFPGFKGDMGLK  G DRGEVGQIGPRGEDGPEGPK
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.

Human                         SKGEKGEDGFPGFKGDMGLKGDRGEVGQIGPRGEDGPEGPK

Mouse                         SKGEKGEDGFPGFKGDMGLKGDRGEVGQVGPRGEDGPEGPK

Rat                           SKGEKGEDGFPGFKGDMGLKGDRGEVGQVGPRGEDGPEGPK

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.

TypePositionsDescription
Chain 512 – 1563 Collagen alpha-1(XI) chain
Region 529 – 1542 Triple-helical region


Literature citations

Fibrochondrogenesis results from mutations in the COL11A1 type XI collagen gene.
Tompson S.W.; Bacino C.A.; Safina N.P.; Bober M.B.; Proud V.K.; Funari T.; Wangler M.F.; Nevarez L.; Ala-Kokko L.; Wilcox W.R.; Eyre D.R.; Krakow D.; Cohn D.H.;
Am. J. Hum. Genet. 87:708-712(2010)
Cited for: VARIANTS FBCG1 ARG-796 AND ARG-1042;

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.