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UniProtKB/Swiss-Prot P08253: Variant p.Asp210Tyr

72 kDa type IV collagenase
Gene: MMP2
Variant information

Variant position:  210
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  Polymorphism
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 Aspartate (D) to Tyrosine (Y) at position 210 (D210Y, p.Asp210Tyr).
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 acidic (D) to large size and aromatic (Y)
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

Sequence information

Variant position:  210
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  660
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 110 – 660 72 kDa type IV collagenase
Region 110 – 221 Collagenase-like 1
Metal binding 193 – 193 Zinc 2
Metal binding 200 – 200 Calcium 2; via carbonyl oxygen
Metal binding 202 – 202 Calcium 2; via carbonyl oxygen
Metal binding 204 – 204 Calcium 2
Metal binding 206 – 206 Zinc 2
Metal binding 208 – 208 Calcium 3
Metal binding 209 – 209 Calcium 1
Metal binding 211 – 211 Calcium 1; via carbonyl oxygen
Metal binding 211 – 211 Calcium 3
Beta strand 209 – 211

Literature citations

Mutation of the matrix metalloproteinase 2 gene (MMP2) causes a multicentric osteolysis and arthritis syndrome.
Martignetti J.A.; Aqeel A.A.; Sewairi W.A.; Boumah C.E.; Kambouris M.; Mayouf S.A.; Sheth K.V.; Eid W.A.; Dowling O.; Harris J.; Glucksman M.J.; Bahabri S.; Meyer B.F.; Desnick R.J.;
Nat. Genet. 28:261-265(2001)

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.