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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P08123: Variant p.Gly109Asp

Collagen alpha-2(I) chain
Gene: COL1A2
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Variant information Variant position: help 109 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 Aspartate (D) at position 109 (G109D, p.Gly109Asp). 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 medium size and acidic (D) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -1 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 OIEDS2; decreased N-terminal propeptide processing. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 109 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 GPGPMGLMGPRGPPGAAGAP G PQGFQGPAGEPGEPGQTGPA 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                         GPGPMGLMGPRGPPGAAGAPGPQGFQGPAGEPGEPGQTGPA

                              GPGPMGLMGPRGPPGASGAPGPQGFQGPAGEPGEPGQTGPA

Mouse                         GPGPMGLMGPRGPPGAVGAPGPQGFQGPAGEPGEPGQTGPA

Rat                           GPGPMGLMGPRGPPGAVGAPGPQGFQGPAGEPGEPGQTGPA

Bovine                        GPGPMGLMGPRGPPGASGAPGPQGFQGPPGEPGEPGQTGPA

Chicken                       GPGPMGLMGPRGPPGASGPPGPPGFQGVPGEPGEPGQTGPQ
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 80 – 1119 Collagen alpha-2(I) chain
Region 28 – 1130 Disordered
Modified residue 102 – 102 4-hydroxyproline
Modified residue 108 – 108 4-hydroxyproline



Literature citations
Helical mutations in type I collagen that affect the processing of the amino-propeptide result in an Osteogenesis Imperfecta/Ehlers-Danlos Syndrome overlap syndrome.
Malfait F.; Symoens S.; Goemans N.; Gyftodimou Y.; Holmberg E.; Lopez-Gonzalez V.; Mortier G.; Nampoothiri S.; Petersen M.B.; De Paepe A.;
Orphanet J. Rare Dis. 8:78-78(2013)
Cited for: VARIANTS OIEDS2 ASP-109 AND VAL-196; CHARACTERIZATION OF VARIANT OIEDS2 ASP-109; INVOLVEMENT IN OIEDS2;
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.