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UniProtKB/Swiss-Prot Q04695: Variant p.Asn109Asp

Keratin, type I cytoskeletal 17
Gene: KRT17
Variant information

Variant position:  109
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 Asparagine (N) to Aspartate (D) at position 109 (N109D, p.Asn109Asp).
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 polar (N) to medium size and acidic (D)
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 PC2.
Any additional useful information about the variant.

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



Sequence information

Variant position:  109
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  432
The length of the canonical sequence.

Location on the sequence:   QNLNDRLASYLDKVRALEEA  N TELEVKIRDWYQRQAPGPAR
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                         QNLNDRLASYLDKVRALEEANTELEVKIRDWYQRQAPGPAR

Chimpanzee                    QNLNDRLASYLDKVRALEEANTELEVKIRDWYQRQAPGPAR

Mouse                         QNLNDRLASYLDKVRALEEANTELEVKIRDWYQKQAPGPAR

Rat                           QNLNDRLASYLDKVRALEEANTELEVKIRDWYQKQAPGPAR

Bovine                        QNLNDRLASYLDKVRALEEANTELELKIRDWYQKQAPGPAP

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 1 – 432 Keratin, type I cytoskeletal 17
Domain 84 – 395 IF rod
Region 84 – 120 Coil 1A
Region 102 – 116 Peptide epitope S1; induces T-cell and keratinocyte proliferation and IFN-gamma production
Modified residue 110 – 110 Phosphothreonine
Mutagenesis 103 – 103 R -> A. Down-regulates both proliferation of psoriatic T-cells and IFN-gamma production; suppresses keratinocyte growth when part of the altered peptide epitope S1.
Mutagenesis 106 – 106 E -> A. Down-regulates proliferation of psoriatic T-cells and IFN-gamma production when part of the altered peptide epitope S1.
Mutagenesis 109 – 109 N -> A. No significant effect on T-cell proliferation or IFN-gamma production when part of the altered peptide epitope S1.


Literature citations

DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage.
Zody M.C.; Garber M.; Adams D.J.; Sharpe T.; Harrow J.; Lupski J.R.; Nicholson C.; Searle S.M.; Wilming L.; Young S.K.; Abouelleil A.; Allen N.R.; Bi W.; Bloom T.; Borowsky M.L.; Bugalter B.E.; Butler J.; Chang J.L.; Chen C.-K.; Cook A.; Corum B.; Cuomo C.A.; de Jong P.J.; DeCaprio D.; Dewar K.; FitzGerald M.; Gilbert J.; Gibson R.; Gnerre S.; Goldstein S.; Grafham D.V.; Grocock R.; Hafez N.; Hagopian D.S.; Hart E.; Norman C.H.; Humphray S.; Jaffe D.B.; Jones M.; Kamal M.; Khodiyar V.K.; LaButti K.; Laird G.; Lehoczky J.; Liu X.; Lokyitsang T.; Loveland J.; Lui A.; Macdonald P.; Major J.E.; Matthews L.; Mauceli E.; McCarroll S.A.; Mihalev A.H.; Mudge J.; Nguyen C.; Nicol R.; O'Leary S.B.; Osoegawa K.; Schwartz D.C.; Shaw-Smith C.; Stankiewicz P.; Steward C.; Swarbreck D.; Venkataraman V.; Whittaker C.A.; Yang X.; Zimmer A.R.; Bradley A.; Hubbard T.; Birren B.W.; Rogers J.; Lander E.S.; Nusbaum C.;
Nature 440:1045-1049(2006)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]; VARIANT PC2 ASP-109;

A novel mutation in the second half of the keratin 17 1A domain in a large pedigree with delayed-onset pachyonychia congenita type 2.
Xiao S.-X.; Feng Y.-G.; Ren X.-R.; Tan S.-S.; Li L.; Wang J.-M.; Shi Y.-Z.;
J. Invest. Dermatol. 122:892-895(2004)
Cited for: VARIANT PC2 ASP-109;

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.