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UniProtKB/Swiss-Prot P08123: Variant p.Ala1119Thr

Collagen alpha-2(I) chain
Gene: COL1A2
Chromosomal location: 7q22.1
Variant information

Variant position:  1119
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  Unclassified
The variants are classified into three categories: Disease, Polymorphism and Unclassified.
  • Disease: Variants implicated in disease according to literature reports.
  • Polymorphism: Variants not reported to be implicated in disease.
  • Unclassified: Variants with uncertain implication in disease according to literature reports. Evidence against or in favor of a pathogenic role is limited and/or conflicting.

Residue change:  From Alanine (A) to Threonine (T) at position 1119 (A1119T, p.Ala1119Thr).
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:  Change from small size and hydrophobic (A) to medium size and polar (T)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  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:  Found in a patient with mild osteogenesis imperfecta associated with increased bone mineral density; results in defective type I procollagen processing; incorporation of the immature procollagen into the matrix leads to increased bone matrix mineralization and altered collagen fibril structure.
Any additional useful information about the variant.



Sequence information

Variant position:  1119
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  1366
The length of the canonical sequence.

Location on the sequence:   GPPGVSGGGYDFGYDGDFYR  A DQPRSAPSLRPKDYEVDATL
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: 
The multiple alignment of the region surrounding the variant against various orthologous sequences.

Human                         GPPGVSGGGYDFGYDGDFYRADQPRSAPSLRPKDYEVDATL

                              GPPGPSGGGYDFGYEGDFYRADQPRSPPSLRPKDYEVDATL

Mouse                         GPPGVSGGGYDFGFEGDFYRADQPRSQPSLRPKDYEVDATL

Rat                           GPPGVSGGGYDFGFEGGFYRADQPRSQPSLRPKDYEVDATL

Bovine                        GPPGPSGGGYEFGFDGDFYRADQPRSPTSLRPKDYEVDATL

Chicken                       GPPGPNGGGYEVGFDAEYYRADQP----SLRPKDYEVDATL

Sequence annotation in neighborhood:  
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


Literature citations

COL1 C-propeptide cleavage site mutations cause high bone mass osteogenesis imperfecta.
Lindahl K.; Barnes A.M.; Fratzl-Zelman N.; Whyte M.P.; Hefferan T.E.; Makareeva E.; Brusel M.; Yaszemski M.J.; Rubin C.J.; Kindmark A.; Roschger P.; Klaushofer K.; McAlister W.H.; Mumm S.; Leikin S.; Kessler E.; Boskey A.L.; Ljunggren O.; Marini J.C.;
Hum. Mutat. 32:598-609(2011)
Cited for: VARIANT THR-1119; CHARACTERIZATION OF VARIANT THR-1119;

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.