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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P02452: Variant p.Gly842Arg

Collagen alpha-1(I) chain
Gene: COL1A1
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Variant information Variant position: help 842 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 842 (G842R, p.Gly842Arg). 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 OI2. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 842 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 1464 The length of the canonical sequence.
Location on the sequence: help QPGAKGEPGDAGAKGDAGPP G PAGPAGPPGPIGNVGAPGAK 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                         QPGAKGEPGDAGAKGDAGPPGPAGPAGPPGPIGNVGAPGAK

                              QPGAKGEPGDAGAKGDAGPPGPAGPTGPPGPIGNVGAPGPK

Mouse                         QPGAKGEPGDTGVKGDAGPPGPAGPAGPPGPIGNVGAPGPK

Rat                           QPGAKGEPGDTGVKGDAGPPGPAGPAGPPGPIGNVGAPGPK

Bovine                        QPGAKGEPGDAGAKGDAGPPGPAGPAGPPGPIGNVGAPGPK

Chicken                       QPGAKGETGDAGAKGDAGPPGPAGPTGAPGPAGZVGAPGPK
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 162 – 1218 Collagen alpha-1(I) chain
Region 98 – 1214 Disordered
Region 179 – 1192 Triple-helical region
Modified residue 823 – 823 4-hydroxyproline
Modified residue 841 – 841 4-hydroxyproline
Modified residue 850 – 850 4-hydroxyproline
Modified residue 859 – 859 4-hydroxyproline
Modified residue 862 – 862 5-hydroxylysine



Literature citations
Substitution of arginine for glycine 664 in the collagen alpha 1(I) chain in lethal perinatal osteogenesis imperfecta. Demonstration of the peptide defect by in vitro expression of the mutant cDNA.
Bateman J.F.; Lamande S.R.; Dahl H.-H.M.; Chan D.; Cole W.G.;
J. Biol. Chem. 263:11627-11630(1988)
Cited for: VARIANT OI2 ARG-842; Substitutions of aspartic acid for glycine-220 and of arginine for glycine-664 in the triple helix of the pro alpha 1(I) chain of type I procollagen produce lethal osteogenesis imperfecta and disrupt the ability of collagen fibrils to incorporate crystalline hydroxyapatite.
Culbert A.A.; Lowe M.P.; Atkinson M.; Byers P.H.; Wallis G.A.; Kadler K.E.;
Biochem. J. 311:815-820(1995)
Cited for: VARIANTS OI2 ASP-398 AND ARG-842;
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.