UniProtKB/Swiss-Prot P13647: Variant p.Glu170Lys

• Variant information
• Sequence information
• Literature citations
• All

Variant information

Variant position: 170 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: LP/P [Disclaimer: Variants classification is intended for research purposes only, not for clinical and diagnostic use. The label disease variant is assigned according to literature reports on probable disease-association that can be based on theoretical reasons. This label must not be considered as a definitive proof for the pathogenic role of a variant.] 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 Glutamate (E) to Lysine (K) at position 170 (E170K, p.Glu170Lys). 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 medium size and acidic (E) to large size and basic (K) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: 1 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, EBS2B and EBS2D. Any additional useful information about the variant.
Other resources: Links to websites of interest for the variant.

• Variant rs59115483 [ dbSNP | Ensembl ]

Sequence information

Variant position: 170 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: LTPLNLQIDPSIQRVRTEER E QIKTLNNKFASFIDKVRFLE 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	168 – 203	Coil 1A
Modified residue	151 – 151	Phosphothreonine; by CDK1

Literature citations

Dominant and recessive compound heterozygous mutations in epidermolysis bullosa simplex demonstrate the role of the stutter region in keratin intermediate filament assembly.
Yasukawa K.; Sawamura D.; McMillan J.R.; Nakamura H.; Shimizu H.;
J. Biol. Chem. 277:23670-23674(2002)
Cited for: VARIANT EBS2C LYS-170; VARIANT EBS2D LYS-418; Novel sporadic and recurrent mutations in KRT5 and KRT14 genes in Polish epidermolysis bullosa simplex patients: further insights into epidemiology and genotype-phenotype correlation.
Wertheim-Tysarowska K.; Oldak M.; Giza A.; Kutkowska-Kazmierczak A.; Sota J.; Przybylska D.; Wozniak K.; Sniegorska D.; Niepokoj K.; Sobczynska-Tomaszewska A.; Rygiel A.M.; Ploski R.; Bal J.; Kowalewski C.;
J. Appl. Genet. 57:175-181(2016)
Cited for: VARIANT EBS2F LEU-25; VARIANTS EBS2B ALA-143; LYS-170 AND MET-186; VARIANTS EPIDERMOLYSIS BULLOSA SIMPLEX PHE-143; LYS-190; MET-203; 470-TYR--SER-590 DEL AND GLY-477; VARIANT EBS2A 144-THR-VAL-145 DEL; VARIANTS EBS2C TYR-146; LYS-170; PHE-325; HIS-471 AND ASP-476; Biallelic KRT5 mutations in autosomal recessive epidermolysis bullosa simplex, including a complete human keratin 5 'knock-out'.
Vahidnezhad H.; Youssefian L.; Daneshpazhooh M.; Mahmoudi H.; Kariminejad A.; Fischer J.; Christiansen J.; Schneider H.; Guy A.; Liu L.; McGrath J.A.; Has C.; Uitto J.;
Matrix Biol. 83:48-59(2019)
Cited for: TISSUE SPECIFICITY; VARIANTS EBS2D ASN-158 AND LYS-170;