UniProtKB/Swiss-Prot P49747: Variant p.Glu50Asp

Cartilage oligomeric matrix protein
Gene: COMP
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Variant information Variant position:

50 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:

LB/B 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:

From Glutamate (E) to Aspartate (D) at position 50 (E50D, p.Glu50Asp). 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 acidic. 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

Sequence information Variant position:

50 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length:

757 The length of the canonical sequence.
Location on the sequence:

LGPQMLRELQETNAALQDVR E LLRQQVREITFLKNTVMECD 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                         LGPQMLRELQETNAALQDVRELLRQQVREITFLKNTVMECD

Mouse                         LAPQMLRELQETNAALQDVRELLRQQVKEITFLKNTVMECD

Rat                           LAPQMLRELQETNAALQDVRELLRHRVKEITFLKNTVMECD

Bovine                        LGPQMLRELQETNAALQDVRDLLRQQVKEITFLKNTVMECD

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.

Type	Positions	Description
Chain	21 – 757	Cartilage oligomeric matrix protein
Region	22 – 86	COMP N-terminal
Disulfide bond	69 – 69	Interchain

Literature citations
Characterization of human and mouse cartilage oligomeric matrix protein.
Newton G.; Weremowicz S.; Morton C.C.; Copeland N.G.; Gilbert D.J.; Jenkins N.A.; Lawler J.;
Genomics 24:435-439(1994)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1); VARIANTS ASP-50; TRP-51; GLY-109; GLY-224 AND PRO-285; Human comp cDNA with 5 SNIPs.
Hashimoto Y.; Mori H.;
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1); VARIANTS ASP-50; TRP-51; GLY-109; GLY-224 AND PRO-285; 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;

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