Home  |  Contact

UniProtKB/Swiss-Prot Q04695: Variant p.Asn92Ser

Keratin, type I cytoskeletal 17
Gene: KRT17
Variant information

Variant position:  92
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 Serine (S) at position 92 (N92S, p.Asn92Ser).
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 small size and polar (S)
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:  92
The position of the amino-acid change on the UniProtKB canonical protein sequence.

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

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.






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.

Chain 1 – 432 Keratin, type I cytoskeletal 17
Domain 84 – 395 IF rod
Region 84 – 120 Coil 1A
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

Missense mutations in keratin 17 cause either pachyonychia congenita type 2 or a phenotype resembling steatocystoma multiplex.
Smith F.J.D.; Corden L.D.; Rugg E.L.; Ratnavel R.; Leigh I.M.; Moss C.; Tidman M.J.; Hohl D.; Huber M.; Kunkeler L.; Munro C.S.; Lane E.B.; McLean W.H.I.;
J. Invest. Dermatol. 108:220-223(1997)

Keratin 17 mutations cause either steatocystoma multiplex or pachyonychia congenita type 2.
Covello S.P.; Smith F.J.D.; Sillevis Smitt J.H.; Paller A.S.; Munro C.S.; Jonkman M.F.; Uitto J.; McLean W.H.I.;
Br. J. Dermatol. 139:475-480(1998)

The genetic basis of pachyonychia congenita.
Smith F.J.; Liao H.; Cassidy A.J.; Stewart A.; Hamill K.J.; Wood P.; Joval I.; van Steensel M.A.; Bjoerck E.; Callif-Daley F.; Pals G.; Collins P.; Leachman S.A.; Munro C.S.; McLean W.H.;
J. Investig. Dermatol. Symp. Proc. 10:21-30(2005)
Cited for: VARIANTS PC2 SER-92 AND PRO-388;

A spectrum of mutations in keratins K6a, K16 and K17 causing pachyonychia congenita.
Liao H.; Sayers J.M.; Wilson N.J.; Irvine A.D.; Mellerio J.E.; Baselga E.; Bayliss S.J.; Uliana V.; Fimiani M.; Lane E.B.; McLean W.H.; Leachman S.A.; Smith F.J.;
J. Dermatol. Sci. 48:199-205(2007)
Cited for: VARIANT PC2 SER-92;

Novel missense mutation of keratin in Chinese family with steatocystoma multiplex.
Wang J.F.; Lu W.S.; Sun L.D.; Lv Y.M.; Zhou F.S.; Fang Q.Y.; Tang H.Y.; Cui Y.; Yang S.; Zhang X.J.;
J. Eur. Acad. Dermatol. Venereol. 23:723-724(2009)
Cited for: VARIANTS PC2 SER-92 AND HIS-94;

A large mutational study in pachyonychia congenita.
Wilson N.J.; Leachman S.A.; Hansen C.D.; McMullan A.C.; Milstone L.M.; Schwartz M.E.; McLean W.H.; Hull P.R.; Smith F.J.;
J. Invest. Dermatol. 131:1018-1024(2011)
Cited for: VARIANTS PC2 92-ASN--LEU-99 DEL AND SER-92;

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.