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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P02452: Variant p.Gly1184Val

Collagen alpha-1(I) chain
Gene: COL1A1
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Variant information Variant position: help 1184 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 Valine (V) at position 1184 (G1184V, p.Gly1184Val). 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 hydrophobic (V) 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 OI2. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 1184 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 PPGPRGRTGDAGPVGPPGPP G PPGPPGPPSAGFDFSFLPQP 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                         PPGPRGRTGDAGPVGPPGPPGPPGPPGPPSAGFDFSFLPQP

                              PPGPRGRTGDAGPVGPPGPPGPPGPPGPPSGGFDFSFLPQP

Mouse                         PPGPRGRTGDSGPAGPPGPPGPPGPPGPPSGGYDFSFLPQP

Rat                           PPGPRGRTGDSGPAGPPGPPGPPGPPGPPSGGYDFSFLPQP

Bovine                        PPGPRGRTGDAGPAGPPGPPGPPGPPGPPSGGYDLSFLPQP

Chicken                       PPGPRGRTGEVGPVGPPGPPGPPGPPGPPSGGFDLSFLPQP
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
Compositional bias 1176 – 1195 Pro residues
Modified residue 1164 – 1164 3-hydroxyproline
Modified residue 1165 – 1165 4-hydroxyproline
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



Literature citations
Characterization of point mutations in the collagen COL1A1 and COL1A2 genes causing lethal perinatal osteogenesis imperfecta.
Lamande S.R.; Dahl H.-H.M.; Cole W.G.; Bateman J.F.;
J. Biol. Chem. 264:15809-15812(1989)
Cited for: VARIANTS OI2 ALA-1106; VAL-1151; ARG-1154 AND VAL-1184; The clinicopathological features of three babies with osteogenesis imperfecta resulting from the substitution of glycine by valine in the pro alpha 1 (I) chain of type I procollagen.
Cole W.G.; Patterson E.; Bonadio J.; Campbell P.E.; Fortune D.W.;
J. Med. Genet. 29:112-118(1992)
Cited for: VARIANTS OI2 VAL-434; VAL-1151 AND VAL-1184;
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.