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UniProtKB/Swiss-Prot Q02388: Variant p.Gly2043Arg

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

Variant position:  2043
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 2043 (G2043R, p.Gly2043Arg).
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.

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

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



Sequence information

Variant position:  2043
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:   ERGPPGPSGLAGEPGKPGIP  G LPGRAGGVGEAGRPGERGER
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                         ERGPPGPSGLAGEPGKPGIPGLPGRAGGVGEAGRPGERGER

Mouse                         ERGPPGPPGLAGEPGKPGIPGLPGRAGGSGEAGRPGERGER

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

A glycine-to-arginine substitution in the triple-helical domain of type VII collagen in a family with dominant dystrophic epidermolysis bullosa.
Christiano A.M.; Morricone A.; Paradisi M.; Angelo C.; Mazzanti C.; Cavalieri R.; Uitto J.;
J. Invest. Dermatol. 104:438-440(1995)
Cited for: VARIANT DDEB ARG-2043;

Modulation of disease severity of dystrophic epidermolysis bullosa by a splice site mutation in combination with a missense mutation in the COL7A1 gene.
Winberg J.-O.; Hammami-Hauasli N.; Nilssen O.; Anton-Lamprecht I.; Naylor S.L.; Kerbacher K.; Zimmermann M.; Krajci P.; Gedde-Dahl T. Jr.; Bruckner-Tuderman L.;
Hum. Mol. Genet. 6:1125-1135(1997)
Cited for: VARIANT RDEB ARG-2009; VARIANT DDEB ARG-2043;

Novel and de novo glycine substitution mutations in the type VII collagen gene (COL7A1) in dystrophic epidermolysis bullosa: implications for genetic counseling.
Rouan F.; Pulkkinen L.; Jonkman M.F.; Bauer J.W.; Cserhalmi-Friedman P.B.; Christiano A.M.; Uitto J.;
J. Invest. Dermatol. 111:1210-1213(1998)
Cited for: VARIANTS DDEB TRP-2034; VAL-2040; ARG-2043; ARG-2064 AND ASP-2713;

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;

Analysis of the COL7A1 gene in Czech patients with dystrophic epidermolysis bullosa reveals novel and recurrent mutations.
Jerabkova B.; Kopeckova L.; Buckova H.; Vesely K.; Valickova J.; Fajkusova L.;
J. Dermatol. Sci. 59:136-140(2010)
Cited for: VARIANTS RDEB ARG-1845; ARG-1981; GLU-2049; TRP-2063; CYS-2069; GLU-2296; ARG-2557 AND TRP-2622; VARIANTS DDEB ARG-2003; ASP-2040; ARG-2043; ARG-2064; ARG-2070 AND ASP-2076;

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.