Expasy logo

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q92838: Variant p.Ser319Arg

Ectodysplasin-A
Gene: EDA
Feedback?
Variant information Variant position: help 319 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help 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: help From Serine (S) to Arginine (R) at position 319 (S319R, p.Ser319Arg). 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: help Change from small size and polar (S) to large size and basic (R) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -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: help In XHED. Any additional useful information about the variant.


Sequence information Variant position: help 319 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 391 The length of the canonical sequence.
Location on the sequence: help GTYFIYSQVEVYYINFTDFA S YEVVVDEKPFLQCTRSIETG 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences. 
Human                         GTYFIYSQVEVYYINFTDFASYEVVVDEKPFLQCTRSIETG

Mouse                         GTYFIYSQVEVYYINFTDFASYEVVVDEKPFLQCTRSIETG

Bovine                        GTYFIYSQVEVYYINFTDFASYEVVVDEKPFLQCTRSIETG
Sequence annotation in neighborhood: help 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 – 391 Ectodysplasin-A, membrane form
Chain 160 – 391 Ectodysplasin-A, secreted form
Topological domain 63 – 391 Extracellular
Domain 249 – 385 THD
Glycosylation 313 – 313 N-linked (GlcNAc...) asparagine
Alternative sequence 136 – 391 Missing. In isoform 2.
Alternative sequence 143 – 391 Missing. In isoform 5.
Alternative sequence 148 – 391 Missing. In isoform 4, isoform 6 and isoform 7.
Beta strand 318 – 324



Literature citations
A new mutation in EDA gene in X-linked hypohidrotic ectodermal dysplasia associated with keratoconus.
Piccione M.; Serra G.; Sanfilippo C.; Andreucci E.; Sani I.; Corsello G.;
Minerva Pediatr. 64:59-64(2012)
Cited for: VARIANT XHED ARG-319; Phenotypic heterogeneity and mutational spectrum in a cohort of 45 Italian males subjects with X-linked ectodermal dysplasia.
Guazzarotti L.; Tadini G.; Mancini G.E.; Giglio S.; Willoughby C.E.; Callea M.; Sani I.; Nannini P.; Mameli C.; Tenconi A.A.; Mauri S.; Bottero A.; Caimi A.; Morelli M.; Zuccotti G.V.;
Clin. Genet. 87:338-342(2015)
Cited for: VARIANTS XHED GLN-51; CYS-125; PRO-132; HIS-153; CYS-155; HIS-156; 183-GLY--PRO-194 DEL; 185-ASN--PRO-196 DEL; 191-PRO--PRO-196 DEL; 193-PRO--GLY-201 DEL; 219-PRO--GLY-230 DEL; GLY-274; ARG-291; SER-299; HIS-304; GLU-316; ARG-319; SER-319 DEL; PHE-332; ASP-350; HIS-358 AND VAL-381;
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.