UniProtKB/Swiss-Prot P02533: Variant p.Arg125Cys

Keratin, type I cytoskeletal 14
Gene: KRT14
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Variant information Variant position:

125 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:

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:

From Arginine (R) to Cysteine (C) at position 125 (R125C, p.Arg125Cys). 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 large size and basic (R) to medium size and polar (C) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

-3 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 EBS1A. Any additional useful information about the variant.
Other resources:

Links to websites of interest for the variant.

Variant rs60399023 [ dbSNP | Ensembl ]

Sequence information Variant position:

125 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length:

472 The length of the canonical sequence.
Location on the sequence:

AGGDGLLVGSEKVTMQNLND R LASYLDKVRALEEANADLEV 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                         AG--GDGLLVGSEKVTMQNLNDRLASYLDKVRALEEANADLEV

Mouse                         GGGIGDGLLVGSEKVTMQNLNDRLATYLDKVRALEEANTEL

Rat                           GGGLGDGLLVGSEKVTMQNLNDRLATYLDKVRALEEANSDL

Chicken                       GG--GDGILPAGEKETMQNLNDRLAAYLDKVRALEEANTDL

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 – 472	Keratin, type I cytoskeletal 14
Domain	115 – 426	IF rod
Region	115 – 150	Coil 1A

Literature citations
Point mutations in human keratin 14 genes of epidermolysis bullosa simplex patients: genetic and functional analyses.
Coulombe P.A.; Hutton M.E.; Letai A.; Hebert A.; Paller A.S.; Fuchs E.;
Cell 66:1301-1311(1991)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 118-126; VARIANTS EBS1A PHE-122; CYS-125 AND HIS-125; Keratin 14 gene mutations in patients with epidermolysis bullosa simplex.
Chen H.; Bonifas J.M.; Matsumura K.; Ikeda S.; Leyden W.A.; Epstein E.H. Jr.;
J. Invest. Dermatol. 105:629-632(1995)
Cited for: VARIANTS EBS1C ILE-119; ASP-274; ASN-377 AND CYS-388; VARIANTS EBS1A ARG-120; CYS-125 AND SER-125; A recurrent keratin 14 mutation in Dowling-Meara epidermolysis bullosa simplex.
Sasaki Y.; Shimizu H.; Akiyama M.; Hiraoka Y.; Takizawa Y.; Yamada S.; Morishima Y.; Yamanishi K.; Aiso S.; Nishikawa T.;
Br. J. Dermatol. 141:747-748(1999)
Cited for: VARIANT EBS1A CYS-125; Exempting homologous pseudogene sequences from polymerase chain reaction amplification allows genomic keratin 14 hotspot analysis.
Hut P.H.L.; van der Vlies P.; Jonkman M.F.; Verlind E.; Shimizu H.; Buys C.H.C.M.; Scheffer H.;
J. Invest. Dermatol. 114:616-619(2000)
Cited for: VARIANTS EBS1A CYS-125; HIS-125 AND GLN-419; VARIANTS EBS1B ASP-247 AND HIS-415; VARIANT EBS1C LYS-422; DNA based prenatal testing for the skin blistering disorder epidermolysis bullosa simplex.
Rugg E.L.; Baty D.; Shemanko C.S.; Magee G.; Polak S.; Bergman R.; Kadar T.; Boxer M.; Falik-Zaccai T.; Borochowitz Z.; Lane E.B.;
Prenat. Diagn. 20:371-377(2000)
Cited for: VARIANTS EBS1A CYS-125 AND HIS-415; VARIANT EBS1B PRO-134; Epidermolysis bullosa simplex in Japanese and Korean patients: genetic studies in 19 cases.
Yasukawa K.; Sawamura D.; Goto M.; Nakamura H.; Jung S.-Y.; Kim S.-C.; Shimizu H.;
Br. J. Dermatol. 155:313-317(2006)
Cited for: VARIANT EBS1C VAL-119; VARIANTS EBS1A HIS-125 AND CYS-125; Novel and recurrent mutations in keratin KRT5 and KRT14 genes in epidermolysis bullosa simplex: implications for disease phenotype and keratin filament assembly.
Mueller F.B.; Kuester W.; Wodecki K.; Almeida H. Jr.; Bruckner-Tuderman L.; Krieg T.; Korge B.P.; Arin M.J.;
Hum. Mutat. 27:719-720(2006)
Cited for: VARIANTS EBS1A LYS-123; CYS-125; HIS-125 AND PRO-417; VARIANTS EBS1B LEU-133; THR-272 AND PRO-384; VARIANTS EBS1C PRO-211 AND GLU-411 DEL; 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: VARIANTS EBS1C ASN-377; THR-377; CYS-388; MET-408; GLU-411 DEL AND PHE-412; VARIANTS EBS1A SER-123; CYS-125; PRO-130; ARG-272 AND GLN-419; 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: VARIANTS EBS1A THR-119; SER-123; CYS-125; HIS-125 AND ASP-129; VARIANTS EBS1C MET-133; ALA-270; THR-272; THR-413 AND GLN-418; VARIANTS EPIDERMOLYSIS BULLOSA SIMPLEX LEU-125; CYS-388 AND GLU-411 DEL;

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.