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UniProtKB/Swiss-Prot P02461: Variant p.Gly1284Glu

Collagen alpha-1(III) chain
Gene: COL3A1
Variant information

Variant position:  1284
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 Glycine (G) to Glutamate (E) at position 1284 (G1284E, p.Gly1284Glu).
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 glycine (G) to medium size and acidic (E)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  -2
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:  Polymicrogyria with or without vascular-type Ehlers-Danlos syndrome (PMGEDSV) [MIM:618343]: An autosomal recessive disorder with a highly variable phenotype and onset in early childhood. Disease features include cobblestone-like malformation of the cortex, polymicrogyria, intellectual and motor developmental delay, small joint hypermobility, vascular fragility, aneurysms, thin translucent skin and easy bruising, congenital heart defects, and foot deformities. Early death due to vascular dissection may occur. {ECO:0000269|PubMed:19455184, ECO:0000269|PubMed:25205403, ECO:0000269|PubMed:28258187, ECO:0000269|PubMed:28742248}. 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 PMGEDSV.
Any additional useful information about the variant.

Other resources:  
Links to websites of interest for the variant.

Sequence information

Variant position:  1284
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  1466
The length of the canonical sequence.

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.




Bovine                        -----------------------------------------

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.

Propeptide 1222 – 1466 C-terminal propeptide
Domain 1232 – 1466 Fibrillar collagen NC1
Metal binding 1280 – 1280 Calcium
Metal binding 1282 – 1282 Calcium
Metal binding 1283 – 1283 Calcium; via carbonyl oxygen
Metal binding 1285 – 1285 Calcium; via carbonyl oxygen
Metal binding 1288 – 1288 Calcium
Disulfide bond 1262 – 1294
Disulfide bond 1268 – 1268 Interchain (with C-1285)
Disulfide bond 1285 – 1285 Interchain (with C-1268)

Literature citations

Vascular Ehlers-Danlos Syndrome in siblings with biallelic COL3A1 sequence variants and marked clinical variability in the extended family.
Joergensen A.; Fagerheim T.; Rand-Hendriksen S.; Lunde P.I.; Vorren T.O.; Pepin M.G.; Leistritz D.F.; Byers P.H.;
Eur. J. Hum. Genet. 23:796-802(2015)

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.