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UniProtKB/Swiss-Prot Q02388: Variant p.Gly2034Arg

Collagen alpha-1(VII) chain
Gene: COL7A1
Chromosomal location: 3p21.1
Variant information

Variant position:  2034
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 Arginine (R) at position 2034 (G2034R, p.Gly2034Arg).
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 large size and basic (R)
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:  Epidermolysis bullosa dystrophica, autosomal dominant (DDEB) [MIM:131750]: A group of autosomal dominant blistering skin diseases characterized by tissue separation which occurs below the dermal-epidermal basement membrane at the level of the anchoring fibrils. Various clinical types with different severity are recognized, ranging from severe mutilating forms to mild forms with limited and localized scarring, and less frequent extracutaneous manifestations. {ECO:0000269|PubMed:10084325, ECO:0000269|PubMed:10232406, ECO:0000269|PubMed:10232407, ECO:0000269|PubMed:10232408, ECO:0000269|PubMed:10233777, ECO:0000269|PubMed:10836608, ECO:0000269|PubMed:11142768, ECO:0000269|PubMed:20598510, ECO:0000269|PubMed:7861014, ECO:0000269|PubMed:8170945, ECO:0000269|PubMed:9215684, ECO:0000269|PubMed:9668111, ECO:0000269|PubMed:9740253, ECO:0000269|PubMed:9856843}. 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.

Involvement in disease:  Epidermolysis bullosa dystrophica, with subcorneal cleavage (EBDSC) [MIM:131750]: A bullous skin disorder with variable sized clefts just beneath the level of the stratum corneum. Clinical features include blisters, milia, atrophic scarring, nail dystrophy, and oral and conjunctival involvement, as seen in dystrophic epidermolysis bullosa. {ECO:0000269|PubMed:11874498, ECO:0000269|PubMed:2653224}. 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 DDEB and EBDSC; interferes with collagen VII folding and secretion.
Any additional useful information about the variant.

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



Sequence information

Variant position:  2034
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  2944
The length of the canonical sequence.

Location on the sequence:   QGPPGLALGERGPPGPSGLA  G EPGKPGIPGLPGRAGGVGEA
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                         QGPPGLALGERGPPGPSGLAGEPGKPGIPGLPGRAGGVGEA

Mouse                         QGPPGLALGERGPPGPPGLAGEPGKPGIPGLPGRAGGSGEA

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 17 – 2944 Collagen alpha-1(VII) chain
Region 1254 – 2784 Triple-helical region
Modified residue 2036 – 2036 4-hydroxyproline
Modified residue 2039 – 2039 4-hydroxyproline


Literature citations

Epidermolysis bullosa simplex superficialis. A new variant of epidermolysis bullosa characterized by subcorneal skin cleavage mimicking peeling skin syndrome.
Fine J.-D.; Johnson L.; Wright T.;
Arch. Dermatol. 125:633-638(1989)
Cited for: VARIANT EBDSC ARG-2034;

Some, but not all, glycine substitution mutations in COL7A1 result in intracellular accumulation of collagen VII, loss of anchoring fibrils, and skin blistering.
Hammami-Hauasli N.; Schumann H.; Raghunath M.; Kilgus O.; Luethi U.; Luger T.; Bruckner-Tuderman L.;
J. Biol. Chem. 273:19228-19234(1998)
Cited for: VARIANTS DDEB ASP-1519; ASP-2006; GLU-2015 AND ARG-2034;

Clustering of COL7A1 mutations in exon 73: implications for mutation analysis in dystrophic epidermolysis bullosa.
Mecklenbeck S.; Hammami-Hauasli N.; Hoepfner B.; Schumann H.; Kramer A.; Kuester W.; Bruckner-Tuderman L.;
J. Invest. Dermatol. 112:398-400(1999)
Cited for: VARIANTS DDEB ASP-2006; GLU-2015; ARG-2034; TRP-2034; ARG-2043 AND TRP-2043; VARIANTS RDEB CYS-2008; GLY-2008 AND ARG-2009;

EB simplex superficialis resulting from a mutation in the type VII collagen gene.
Martinez-Mir A.; Liu J.; Gordon D.; Weiner M.S.; Ahmad W.; Fine J.D.; Ott J.; Gilliam T.C.; Christiano A.M.;
J. Invest. Dermatol. 118:547-549(2002)
Cited for: VARIANT EBDSC ARG-2034;

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.