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UniProtKB/Swiss-Prot P17813: Variant p.Arg529His

Gene: ENG
Chromosomal location: 9q33-q34.1
Variant information

Variant position:  529
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 Arginine (R) to Histidine (H) at position 529 (R529H, p.Arg529His).
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 (H)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  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

Involvement in disease:  Telangiectasia, hereditary hemorrhagic, 1 (HHT1) [MIM:187300]: A multisystemic vascular dysplasia leading to dilation of permanent blood vessels and arteriovenous malformations of skin, mucosa, and viscera. The disease is characterized by recurrent epistaxis and gastro-intestinal hemorrhage. Visceral involvement includes arteriovenous malformations of the lung, liver, and brain. {ECO:0000269|PubMed:10545596, ECO:0000269|PubMed:10625079, ECO:0000269|PubMed:10982033, ECO:0000269|PubMed:15024723, ECO:0000269|PubMed:15712270, ECO:0000269|PubMed:16525724, ECO:0000269|PubMed:16752392, ECO:0000269|PubMed:20414677, ECO:0000269|PubMed:7894484, ECO:0000269|PubMed:9157574, ECO:0000269|PubMed:9245986, ECO:0000269|PubMed:9554745}. 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 HHT1.
Any additional useful information about the variant.

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

Sequence information

Variant position:  529
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  658
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.




Zebrafish                     EPCFIKDCPKRLS--------FSFQI---LQDLPAGSWDLE

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 26 – 658 Endoglin
Topological domain 26 – 586 Extracellular
Domain 363 – 533 ZP
Compositional bias 336 – 576 Ser/Thr-rich
Disulfide bond 493 – 549
Disulfide bond 516 – 516 Interchain
Mutagenesis 516 – 516 C -> S. Loss of dimerization via ZP domain.
Beta strand 529 – 532

Literature citations

Novel mutations in ENG and ACVRL1 identified in a series of 200 individuals undergoing clinical genetic testing for hereditary hemorrhagic telangiectasia (HHT): correlation of genotype with phenotype.
Bossler A.D.; Richards J.; George C.; Godmilow L.; Ganguly A.;
Hum. Mutat. 27:667-675(2006)
Cited for: VARIANTS HHT1 ASP-11; ASP-105; GLU-175; THR-220; ASP-308; SER-363; TRP-437; SER-490; HIS-529; PRO-547 AND ASP-604;

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.