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UniProtKB/Swiss-Prot P02452: Variant p.Arg1014Cys

Collagen alpha-1(I) chain
Gene: COL1A1
Chromosomal location: 17q21.3-q22
Variant information

Variant position:  1014
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  Disease [Disclaimer]
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 Arginine (R) to Cysteine (C) at position 1014 (R1014C, p.Arg1014Cys).
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 large size and basic (R) to medium size and polar (C)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  -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

Involvement in disease:  Caffey disease (CAFFD) [MIM:114000]: Characterized by an infantile episode of massive subperiosteal new bone formation that typically involves the diaphyses of the long bones, mandible, and clavicles. The involved bones may also appear inflamed, with painful swelling and systemic fever often accompanying the illness. The bone changes usually begin before 5 months of age and resolve before 2 years of age. {ECO:0000269|PubMed:15864348}. Note=The disease is caused by mutations affecting the gene represented in this entry.
The name and a short description of the disease associated with the variant. For more information about the disease, the user can refer to OMIM, following the link provided after the disease acronym.

Variant description:  In CAFFD.
Any additional useful information about the variant.



Sequence information

Variant position:  1014
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  1464
The length of the canonical sequence.

Location on the sequence:   RGPPGPMGPPGLAGPPGESG  R EGAPGAEGSPGRDGSPGAKG
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                         RGPPGPMGPPGLAGPPGESGREGAPGAEGSPGRDGSPGAKG

                              RGPPGPMGPPGLAGPPGESGREGSPGAEGSPGRDGSPGPKG

Mouse                         RGPPGPMGPPGLAGPPGESGREGSPGAEGSPGRDGAPGAKG

Rat                           RGPPGPMGPPGLAGPPGESGREGSPGAEGSPGRDGAPGAKG

Bovine                        RGPPGPMGPPGLAGPPGESGREGAPGAEGSPGRDGSPGAKG

Chicken                       RGPPGPMGPPGLAGPPGEAGREGAPGAEGAPGRDGAAGPKG

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 162 – 1218 Collagen alpha-1(I) chain
Region 179 – 1192 Triple-helical region
Modified residue 997 – 997 4-hydroxyproline
Modified residue 1003 – 1003 4-hydroxyproline
Modified residue 1009 – 1009 4-hydroxyproline
Modified residue 1018 – 1018 4-hydroxyproline
Modified residue 1024 – 1024 4-hydroxyproline
Modified residue 1033 – 1033 5-hydroxylysine


Literature citations

A novel COL1A1 mutation in infantile cortical hyperostosis (Caffey disease) expands the spectrum of collagen-related disorders.
Gensure R.C.; Maekitie O.; Barclay C.; Chan C.; Depalma S.R.; Bastepe M.; Abuzahra H.; Couper R.; Mundlos S.; Sillence D.; Ala-Kokko L.; Seidman J.G.; Cole W.G.; Jueppner H.;
J. Clin. Invest. 115:1250-1257(2005)
Cited for: VARIANT CAFFD CYS-1014;

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.