Expasy logo

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P49747: Variant p.Arg718Trp

Cartilage oligomeric matrix protein
Gene: COMP
Feedback?
Variant information Variant position: help 718 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LP/P [Disclaimer] The variants are classified into three categories: LP/P, LB/B and US.
  • LP/P: likely pathogenic or pathogenic.
  • LB/B: likely benign or benign.
  • US: uncertain significance
Residue change: help From Arginine (R) to Tryptophan (W) at position 718 (R718W, p.Arg718Trp). 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: help Change from large size and basic (R) to large size and aromatic (W) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -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
Variant description: help In EDM1 and CTS2; reduced secretion in tendon cells and chondrocytes. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 718 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 757 The length of the canonical sequence.
Location on the sequence: help RFYEGPELVADSNVVLDTTM R GGRLGVFCFSQENIIWANLR 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences. 
Human                         RFYEGPELVADSNVVLDTTMRGGRLGVFCFSQENIIWANLR

Mouse                         RFYEGPELVADSNVVLDTAMRGGRLGVFCFSQENIIWANLR

Rat                           RFYEGPELVADSNVVLDTAMRGGRLGVFCFSQENIIWANLR

Bovine                        RFYEGPELVADSNVILDTTMRGGRLGVFCFSQENIIWANLR
Sequence annotation in neighborhood: help 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 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; Mutations in COMP cause familial carpal tunnel syndrome.
Li C.; Wang N.; Schaeffer A.A.; Liu X.; Zhao Z.; Elliott G.; Garrett L.; Choi N.T.; Wang Y.; Wang Y.; Wang C.; Wang J.; Chan D.; Su P.; Cui S.; Yang Y.; Gao B.;
Nat. Commun. 11:3642-3642(2020)
Cited for: VARIANTS CTS2 GLU-66 AND TRP-718; CHARACTERIZATION OF VARIANTS CTS2 GLU-66 AND TRP-718; FUNCTION; SUBUNIT; SUBCELLULAR LOCATION; TISSUE SPECIFICITY;
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.