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UniProtKB/Swiss-Prot P49747: Variant p.Arg718Pro

Cartilage oligomeric matrix protein
Gene: COMP
Variant information

Variant position:  718
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 Arginine (R) to Proline (P) at position 718 (R718P, p.Arg718Pro).
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 large size and basic (R) to medium size and hydrophobic (P)
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:  Multiple epiphyseal dysplasia 1 (EDM1) [MIM:132400]: A generalized skeletal dysplasia associated with significant morbidity. Joint pain, joint deformity, waddling gait, and short stature are the main clinical signs and symptoms. Radiological examination of the skeleton shows delayed, irregular mineralization of the epiphyseal ossification centers and of the centers of the carpal and tarsal bones. Multiple epiphyseal dysplasia is broadly categorized into the more severe Fairbank and the milder Ribbing types. The Fairbank type is characterized by shortness of stature, short and stubby fingers, small epiphyses in several joints, including the knee, ankle, hand, and hip. The Ribbing type is confined predominantly to the hip joints and is characterized by hands that are normal and stature that is normal or near-normal. {ECO:0000269|PubMed:11084047, ECO:0000269|PubMed:11565064, ECO:0000269|PubMed:21922596, ECO:0000269|PubMed:7670472, ECO:0000269|PubMed:9021009, ECO:0000269|PubMed:9184241, ECO:0000269|PubMed:9452026, ECO:0000269|PubMed:9463320, ECO:0000269|PubMed:9921895}. 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 EDM1.
Any additional useful information about the variant.

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

Sequence information

Variant position:  718
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  757
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 21 – 757 Cartilage oligomeric matrix protein
Domain 532 – 746 TSP C-terminal
Region 527 – 757 Mediates cell survival and induction of the IAP family of survival proteins
Disulfide bond 520 – 741
Beta strand 716 – 728

Literature citations

Pseudoachondroplasia and multiple epiphyseal dysplasia: A 7-year comprehensive analysis of the known disease genes identify novel and recurrent mutations and provides an accurate assessment of their relative contribution.
Jackson G.C.; Mittaz-Crettol L.; Taylor J.A.; Mortier G.R.; Spranger J.; Zabel B.; Le Merrer M.; Cormier-Daire V.; Hall C.M.; Offiah A.; Wright M.J.; Savarirayan R.; Nishimura G.; Ramsden S.C.; Elles R.; Bonafe L.; Superti-Furga A.; Unger S.; Zankl A.; Briggs M.D.;
Hum. Mutat. 33:144-157(2012)
Cited for: VARIANTS PSACH SER-234; GLY-290; ARG-299; TYR-326; 341-GLU-ASP-342 DEL; 350-ASN--ASP-372 DEL; VAL-378; ARG-387; 402-GLY--GLY-404 DELINS VAL-CYS; ARG-440; ASN-446; SER-448; ASP-473 DEL; HIS-473; ASN-475; GLY-482; GLY-507; GLY-511; GLY-515; ILE-529; ARG-585 AND SER-719; VARIANTS EDM1 GLU-167; ARG-276; LEU-298; ASP-311; GLY-317; GLY-326; PHE-348; SER-371; TYR-371; ASN-374; ASN-376; ASN-385; ASP-385 DEL; TYR-385; HIS-397; ARG-404; TYR-410; LYS-415; GLU-427; 430-CYS--SER-432 DELINS LEU-TRP-CYS; GLU-457 DEL; ASP-473 INS; ASP-501; LYS-523; MET-585; PRO-718 AND TRP-718; VARIANT ARG-756;

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.