UniProtKB/Swiss-Prot P13647: Variant p.Ala438Asp

• Variant information
• Sequence information
• Literature citations
• All

Variant information

Variant position: 438 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: US The variants are classified into three categories: LP/P, LB/B and US.

• LP/P: likely pathogenic or pathogenic.
• LB/B: likely benign or benign.
• US: uncertain significance

Residue change: From Alanine (A) to Aspartate (D) at position 438 (A438D, p.Ala438Asp). 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 acidic (D) 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
Variant description: In EBS2C and EBS2B; uncertain significance. Any additional useful information about the variant.
Other resources: Links to websites of interest for the variant.

• Variant rs57845028 [ dbSNP | Ensembl ]

Sequence information

Variant position: 438 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 590 The length of the canonical sequence.
Location on the sequence: EQRGELALKDARNKLAELEE A LQKAKQDMARLLREYQELMN 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.
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.

Type	Positions	Description
Chain	1 – 590	Keratin, type II cytoskeletal 5
Domain	168 – 481	IF rod
Region	339 – 477	Coil 2
Site	419 – 419	Stutter
Mutagenesis	422 – 422	E -> A. No effect on interaction with KRT14 or keratin intermediate filament networks.
Mutagenesis	437 – 437	E -> A. No effect on interaction with KRT14 or keratin intermediate filament networks.
Mutagenesis	440 – 440	Q -> A. No effect on interaction with KRT14 or keratin intermediate filament networks.
Mutagenesis	444 – 444	Q -> A. No effect on interaction with KRT14 or keratin intermediate filament networks.
Helix	384 – 474

Literature citations

Mutation analysis of the entire keratin 5 and 14 genes in patients with epidermolysis bullosa simplex and identification of novel mutations.
Schuilenga-Hut P.H.L.; Vlies P.; Jonkman M.F.; Waanders E.; Buys C.H.C.M.; Scheffer H.;
Hum. Mutat. 21:447-447(2003)
Cited for: VARIANTS EBS2C GLU-404 AND ASP-438; VARIANTS EBS2A LYS-475 AND LYS-477; Mutations in KRT5 and KRT14 cause epidermolysis bullosa simplex in 75% of the patients.
Bolling M.C.; Lemmink H.H.; Jansen G.H.; Jonkman M.F.;
Br. J. Dermatol. 164:637-644(2011)
Cited for: VARIANT EBS2F LEU-25; VARIANTS EBS2C PRO-149; PRO-151; GLY-170; SER-177; PRO-187; MET-199; GLY-323; LYS-329; HIS-331; GLU-404; ASN-443 AND ASP-476; VARIANTS EBS2B ASP-180 AND ASP-438; VARIANTS EBS2A PRO-180; PRO-191; MET-467 AND LYS-475;