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UniProtKB/Swiss-Prot P58335: Variant p.Ile189Thr

Anthrax toxin receptor 2
Gene: ANTXR2
Variant information

Variant position:  189
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  Disease [Disclaimer]
The variants are classified into three categories: Disease, Polymorphism and Unclassified.
  • Disease: Variants implicated in disease according to literature reports.
  • Polymorphism: Variants not reported to be implicated in disease.
  • Unclassified: Variants with uncertain implication in disease according to literature reports. Evidence against or in favor of a pathogenic role is limited and/or conflicting.

Residue change:  From Isoleucine (I) to Threonine (T) at position 189 (I189T, p.Ile189Thr).
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 hydrophobic (I) to medium size and polar (T)
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

Involvement in disease:  Hyaline fibromatosis syndrome (HFS) [MIM:228600]: An autosomal recessive syndrome characterized by abnormal growth of hyalinized fibrous tissue usually affecting subcutaneous regions on the scalp, ears, neck, face, hands, and feet. The lesions appear as pearly papules or fleshy nodules. Additional features include gingival hypertrophy, progressive joint contractures resulting in severe limitation of mobility, osteopenia, and osteoporosis. Disease severity is variable. Some individuals manifest symptoms in infancy and have additional visceral or systemic involvement. Hyaline deposits in multiple organs, recurrent infections and intractable diarrhea often lead to early death. Surviving children may suffer from severely reduced mobility due to joint contractures. Other patients have later onset of a milder disorder affecting only the face and digits. {ECO:0000269|PubMed:12973667, ECO:0000269|PubMed:14508707, ECO:0000269|PubMed:15725249}. Note=The disease is caused by mutations affecting the gene represented in this entry.
The name and a short description of the disease associated with the variant. For more information about the disease, the user can refer to OMIM, following the link provided after the disease acronym.

Variant description:  In HFS; infantile form.
Any additional useful information about the variant.

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



Sequence information

Variant position:  189
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  489
The length of the canonical sequence.

Location on the sequence:   LGASVYCVGVLDFEQAQLER  I ADSKEQVFPVKGGFQALKGI
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                         LGASVYCVGVLDFEQAQLERIADSKEQVFPVKGGFQALKGI

Mouse                         LGASVYCVGVLDFEQAQLERIADSKDQVFPVKGGFQALKGI

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 34 – 489 Anthrax toxin receptor 2
Topological domain 34 – 318 Extracellular
Domain 44 – 213 VWFA
Disulfide bond 39 – 218
Helix 183 – 189


Literature citations

Mutations in the gene encoding capillary morphogenesis protein 2 cause juvenile hyaline fibromatosis and infantile systemic hyalinosis.
Hanks S.; Adams S.; Douglas J.; Arbour L.; Atherton D.J.; Balci S.; Bode H.; Campbell M.E.; Feingold M.; Keser G.; Kleijer W.; Mancini G.; McGrath J.A.; Muntoni F.; Nanda A.; Teare M.D.; Warman M.; Pope F.M.; Superti-Furga A.; Futreal P.A.; Rahman N.;
Am. J. Hum. Genet. 73:791-800(2003)
Cited for: VARIANTS HFS PRO-45; THR-189; ARG-218; GLN-293 INS AND CYS-381; VARIANT PRO-357; TISSUE SPECIFICITY;

Mutations in capillary morphogenesis gene-2 result in the allelic disorders juvenile hyaline fibromatosis and infantile systemic hyalinosis.
Dowling O.; Difeo A.; Ramirez M.C.; Tukel T.; Narla G.; Bonafe L.; Kayserili H.; Yuksel-Apak M.; Paller A.S.; Norton K.; Teebi A.S.; Grum-Tokars V.; Martin G.S.; Davis G.E.; Glucksman M.J.; Martignetti J.A.;
Am. J. Hum. Genet. 73:957-966(2003)
Cited for: VARIANTS HFS ASP-105; THR-189 AND ARG-329; FUNCTION;

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.