Expasy logo

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P08123: Variant p.Asp1189Glu

Collagen alpha-2(I) chain
Gene: COL1A2
Feedback?
Variant information Variant position: help 1189 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help 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: help From Aspartate (D) to Glutamate (E) at position 1189 (D1189E, p.Asp1189Glu). 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 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: 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

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


Sequence information Variant position: help 1189 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 1366 The length of the canonical sequence.
Location on the sequence: help SHPEWSSGYYWIDPNQGCTM D AIKVYCDFSTGETCIRAQPE 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                         SHPEWSSGYYWIDPNQGCTMDAIKVYCDFSTGETCIRAQPE

                              SHPEWSSGYYWIDPNQGCTMDAIKVYCDFSTGETCIRAQPE

Mouse                         SHPEWNSDYYWIDPNQGCTMDAIKVYCDFSTGETCIQAQPV

Rat                           SHPEWKSDYYWIDPNQGCTMDAIKVYCDFSTGETCIQAQPV

Bovine                        SHPEWSSGYYWIDPNQGCTMDAIKVYCDFSTGETCIRAQPE

Chicken                       SHPEWSSGFYWIDPNQGCTADAIRAYCDFATGETCIHASLE

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
Propeptide 1120 – 1366 C-terminal propeptide
Domain 1133 – 1366 Fibrillar collagen NC1
Binding site 1181 – 1181
Binding site 1183 – 1183
Binding site 1184 – 1184
Binding site 1186 – 1186
Binding site 1189 – 1189
Disulfide bond 1163 – 1195



Literature citations
Organization of the human pro-alpha 2(I) collagen gene.
de Wet W.J.; Bernard M.P.; Benson-Chanda V.; Chu M.-L.; Dickson L.A.; Weil D.; Ramirez F.;
J. Biol. Chem. 262:16032-16036(1987)
Cited for: NUCLEOTIDE SEQUENCE [MRNA]; VARIANTS ASN-249; THR-276; VAL-483; ALA-549; HIS-678; GLY-743; PHE-1022; GLU-1189; PRO-1198 AND HIS-1354; Analysis of the COL1A1 and COL1A2 genes by PCR amplification and scanning by conformation-sensitive gel electrophoresis identifies only COL1A1 mutations in 15 patients with osteogenesis imperfecta type I: identification of common sequences of null-allele mutations.
Korkko J.M.; Ala-Kokko L.; De Paepe A.; Nuytinck L.; Earley J.J.; Prockop D.J.;
Am. J. Hum. Genet. 62:98-110(1998)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]; VARIANTS ILE-270; VAL-483; HIS-678; GLY-743; PHE-1022; GLU-1189; PRO-1198 AND HIS-1354; Structure of a cDNA for the pro alpha 2 chain of human type I procollagen. Comparison with chick cDNA for pro alpha 2(I) identifies structurally conserved features of the protein and the gene.
Bernard M.P.; Myers J.C.; Chu M.-L.; Ramirez F.; Eikenberry E.F.; Prockop D.J.;
Biochemistry 22:1139-1145(1983)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 623-1366; VARIANTS HIS-678; PHE-1022; GLU-1189; PRO-1198 AND HIS-1354;
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.