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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P49747: Variant p.Gly440Arg

Cartilage oligomeric matrix protein
Gene: COMP
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Variant information Variant position: help 440 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 Glycine (G) to Arginine (R) at position 440 (G440R, p.Gly440Arg). 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 glycine (G) to large size and basic (R) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -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
Variant description: help In PSACH. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 440 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 DVDHDFVGDACDSDQDQDGD G HQDSRDNCPTVPNSAQEDSD 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                         DVDHDFVGDACDSDQDQDGDGHQDSRDNCPTVPNSAQEDSD

Mouse                         DVDHDFVGDACDSDQDQDGDGHQDSRDNCPTVPNSAQQDSD

Rat                           DVDHDFVGDACDSDQDQDGDGHQDSRDNCPTVPNSAQQDSD

Bovine                        DVDHDFVGDACDSDQDQDGDGHQDSKDNCPTVPNSAQQDSD
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
Repeat 419 – 456 TSP type-3 6
Region 298 – 503 Disordered
Compositional bias 417 – 444 Basic and acidic residues



Literature citations
Identification of five novel mutations in cartilage oligomeric matrix protein gene in pseudoachondroplasia and multiple epiphyseal dysplasia.
Loughlin J.; Irven C.; Mustafa Z.; Briggs M.D.; Carr A.; Lynch S.-A.; Knowlton R.G.; Cohn D.H.; Sykes B.;
Hum. Mutat. Suppl. 1:S10-S17(1998)
Cited for: VARIANTS PSACH ARG-328; ASP-372 DEL; 391-PRO--ASP-394 DELINS VAL; ARG-440; SER-459 DEL; TYR-468; ASP-469 DEL AND TYR-472; VARIANTS EDM1 TYR-342; TYR-361; 367-ARG-GLY-368 DEL AND TYR-408; 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.