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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P02452: Variant p.Gly1195Cys

Collagen alpha-1(I) chain
Gene: COL1A1
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Variant information Variant position: help 1195 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 Cysteine (C) at position 1195 (G1195C, p.Gly1195Cys). 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 polar (C) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -3 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 OI1; mild form. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 1195 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 GPVGPPGPPGPPGPPGPPSA G FDFSFLPQPPQEKAHDGGRY 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                         GPVGPPGPPGPPGPPGPPSAGFDFSFLPQPPQEKAHDGGRY

                              GPVGPPGPPGPPGPPGPPSGGFDFSFLPQPPQEKAHDGGRY

Mouse                         GPAGPPGPPGPPGPPGPPSGGYDFSFLPQPPQEKSQDGGRY

Rat                           GPAGPPGPPGPPGPPGPPSGGYDFSFLPQPPQEKSQDGGRY

Bovine                        GPAGPPGPPGPPGPPGPPSGGYDLSFLPQPPQEKAHDGGRY

Chicken                       GPVGPPGPPGPPGPPGPPSGGFDLSFLPQPPQEKAHDGGRY

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 1193 – 1218 Nonhelical region (C-terminal)
Compositional bias 1176 – 1195 Pro residues
Modified residue 1179 – 1179 3-hydroxyproline
Modified residue 1180 – 1180 4-hydroxyproline
Modified residue 1182 – 1182 3-hydroxyproline
Modified residue 1183 – 1183 4-hydroxyproline
Modified residue 1185 – 1185 3-hydroxyproline
Modified residue 1186 – 1186 4-hydroxyproline
Modified residue 1189 – 1189 4-hydroxyproline
Modified residue 1192 – 1192 4-hydroxyproline
Modified residue 1208 – 1208 Allysine



Literature citations
Substitution of cysteine for glycine within the carboxyl-terminal telopeptide of the alpha 1 chain of type I collagen produces mild osteogenesis imperfecta.
Cohn D.H.; Apone S.; Eyre D.R.; Starman B.J.; Andreassen P.; Charbonneau H.; Nicholls A.C.; Pope F.M.; Byers P.H.;
J. Biol. Chem. 263:14605-14607(1988)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1187-1220; VARIANT CYS-1195; A cysteine for glycine substitution at position 1017 in an alpha 1(I) chain of type I collagen in a patient with mild dominantly inherited osteogenesis imperfecta.
Labhard M.E.; Wirtz M.K.; Pope F.M.; Nicholls A.C.; Hollister D.W.;
Mol. Biol. Med. 5:197-207(1988)
Cited for: VARIANT OI1 CYS-1195;
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.