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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P02452: Variant p.Gly1040Ser

Collagen alpha-1(I) chain
Gene: COL1A1
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Variant information Variant position: help 1040 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 Serine (S) at position 1040 (G1040S, p.Gly1040Ser). 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 small size and polar (S) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 0 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 and OI3; moderate to lethal form. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 1040 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 AEGSPGRDGSPGAKGDRGET G PAGPPGAPGAPGAPGPVGPA 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                         AEGSPGRDGSPGAKGDRGETGPAGPPGAPGAPGAPGPVGPA

                              AEGSPGRDGSPGPKGDRGETGPAGPPGAPGAPGAPGPVGPA

Mouse                         AEGSPGRDGAPGAKGDRGETGPAGPPGAPGAPGAPGPVGPA

Rat                           AEGSPGRDGAPGAKGDRGETGPAGPPGAPGAPGAPGPVGPA

Bovine                        AEGSPGRDGSPGAKGDRGETGPAGPPGAPGAPGAPGPVGPA

Chicken                       AEGAPGRDGAAGPKGDRGETGPAGPPGAPGAPGAPGPVGPA
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 1024 – 1024 4-hydroxyproline
Modified residue 1033 – 1033 5-hydroxylysine
Modified residue 1045 – 1045 4-hydroxyproline
Modified residue 1048 – 1048 4-hydroxyproline
Modified residue 1051 – 1051 4-hydroxyproline



Literature citations
Serine for glycine substitutions in the C-terminal third of the alpha 1(I) chain of collagen I in five patients with nonlethal osteogenesis imperfecta.
Lund A.M.; Skovby F.; Schwartz M.;
Hum. Mutat. 9:378-382(1997)
Cited for: VARIANTS OI3 SER-821; SER-1040; SER-1049; SER-1058 AND SER-1076; Two novel COL1A1 mutations in patients with osteogenesis imperfecta (OI) affect the stability of the collagen type I triple-helix.
Witecka J.; Augusciak-Duma A.M.; Kruczek A.; Szydlo A.; Lesiak M.; Krzak M.; Pietrzyk J.J.; Mannikko M.; Sieron A.L.;
J. Appl. Genet. 49:283-295(2008)
Cited for: VARIANTS OI1 VAL-200 AND PHE-349; VARIANT OI2 SER-866; VARIANT OI3 SER-1040;
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.