Expasy logo

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P13645: Variant p.Arg156His

Keratin, type I cytoskeletal 10
Gene: KRT10
Feedback?
Variant information Variant position: help 156 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LP/P [Disclaimer] 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: help From Arginine (R) to Histidine (H) at position 156 (R156H, p.Arg156His). 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: help Change from large size and basic (R) to medium size and polar (H) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 0 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: help In EHK2A. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 156 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 584 The length of the canonical sequence.
Location on the sequence: help GGDGGLLSGNEKVTMQNLND R LASYLDKVRALEESNYELEG 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences. 
Human                         GGDGG-LLSGNEKVTMQNLNDRLASYLDKVRALEESNYELEG

                              GGDGG-LLSGNEKVTMQNLNDRLASYLDKVRALEESNYELE

Mouse                         GGDGGSLLSGNGRVTMQNLNDRLASYMDKVRALEESNYELE

Rat                           GGDGGGLLSGNEKVTMQNLNDRLASYMNKVRDLEESNYELE

Bovine                        -GDGG-LISGNQKITMQNLNDRLASYLDKVRALEESNYELE
Sequence annotation in neighborhood: help 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 1 – 584 Keratin, type I cytoskeletal 10
Domain 146 – 460 IF rod
Region 146 – 181 Coil 1A
Modified residue 170 – 170 Phosphoserine



Literature citations
Prenatal diagnosis of epidermolytic hyperkeratosis by direct gene sequencing.
Rothnagel J.A.; Longley M.A.; Holder R.A.; Kuster W.; Roop D.R.;
J. Invest. Dermatol. 102:13-16(1994)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 147-161; VARIANTS EHK2A HIS-156 AND ASN-160; The genetic basis of epidermolytic hyperkeratosis: a disorder of differentiation-specific epidermal keratin genes.
Cheng J.; Syder A.J.; Yu Q.-C.; Letai A.; Paller A.S.; Fuchs E.;
Cell 70:811-819(1992)
Cited for: INVOLVEMENT IN EHK2A; VARIANT EHK2A HIS-156; Mutations in the rod domains of keratins 1 and 10 in epidermolytic hyperkeratosis.
Rothnagel J.A.; Dominey A.M.; Dempsey L.D.; Longley M.A.; Greenhalgh D.A.; Gagne T.A.; Huber M.; Frenk E.; Hohl D.; Roop D.R.;
Science 257:1128-1130(1992)
Cited for: VARIANTS EHK2A HIS-156 AND SER-161; INVOLVEMENT IN EHK2A; Preferential sites in keratin 10 that are mutated in epidermolytic hyperkeratosis.
Chipev C.C.; Yang J.-M.; Digiovanna J.J.; Steinert P.M.; Marekov L.; Compton J.G.; Bale S.J.;
Am. J. Hum. Genet. 54:179-190(1994)
Cited for: VARIANTS EHK2A HIS-154; CYS-156; HIS-156; ASP-160 AND GLN-442; INVOLVEMENT IN EHK2A; Expanding the keratin mutation database: novel and recurrent mutations and genotype-phenotype correlations in 28 patients with epidermolytic ichthyosis.
Arin M.J.; Oji V.; Emmert S.; Hausser I.; Traupe H.; Krieg T.; Grimberg G.;
Br. J. Dermatol. 164:442-447(2011)
Cited for: VARIANTS EHK2A ARG-150; THR-150; CYS-156; HIS-156 AND CYS-449;
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.