UniProtKB/Swiss-Prot P16112: Variant p.Val2303Met

Aggrecan core protein
Gene: ACAN
Chromosomal location: 15q26.1
Variant information

Variant position:  2303
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 Valine (V) to Methionine (M) at position 2303 (V2303M, p.Val2303Met).
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:  Similar physico-chemical property. Both residues are medium size and hydrophobic.
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  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:  In OD.
Any additional useful information about the variant.



Sequence information

Variant position:  2303
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  2415
The length of the canonical sequence.

Location on the sequence:   FENWRPNQPDNFFAAGEDCV  V MIWHEKGEWNDVPCNYHLPF
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                         FENWRPNQPDNFFAAGEDCVVMIWHEKGEWNDVPCNYHLPF

Mouse                         FEKWRPNQPDNFFATGEDCVVMIWHERGEWNDVPCNYQLPF

Rat                           FEKWRPNQPDNFFATGEDCVVMIWHERGEWNDVPCNYQLPF

Bovine                        FENWRPNQPDNFFATGEDCVVMIWHEKGEWNDVPCNYQLPF

Dog                           FENWRPNQPDNFFVSGEDCVVMIWHEKGEWNDVPCNYYLPF

Chicken                       FENWRPNQPDNFFFAGEDCVVMIWHEQGEWNDVPCNYHLPF

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 17 – 2415 Aggrecan core protein
Chain 393 – 2415 Aggrecan core protein 2
Domain 2201 – 2327 C-type lectin
Region 2163 – 2415 G3
Metal binding 2290 – 2290 Calcium 2
Metal binding 2292 – 2292 Calcium 2
Metal binding 2293 – 2293 Calcium 1
Metal binding 2299 – 2299 Calcium 1; via carbonyl oxygen
Metal binding 2299 – 2299 Calcium 2
Metal binding 2300 – 2300 Calcium 1
Metal binding 2300 – 2300 Calcium 3
Metal binding 2313 – 2313 Calcium 2
Metal binding 2314 – 2314 Calcium 2
Metal binding 2314 – 2314 Calcium 2; via carbonyl oxygen
Disulfide bond 2233 – 2325
Disulfide bond 2301 – 2317


Literature citations

A missense mutation in the aggrecan C-type lectin domain disrupts extracellular matrix interactions and causes dominant familial osteochondritis dissecans.
Stattin E.L.; Wiklund F.; Lindblom K.; Onnerfjord P.; Jonsson B.A.; Tegner Y.; Sasaki T.; Struglics A.; Lohmander S.; Dahl N.; Heinegard D.; Aspberg A.;
Am. J. Hum. Genet. 86:126-137(2010)
Cited for: VARIANT OD MET-2303; DETECTION OF VARIANT OD MET-2303 BY MASS SPECTROMETRY;

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.