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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q92838: Variant p.Gly299Ser

Ectodysplasin-A
Gene: EDA
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Variant information Variant position: help 299 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 Glycine (G) to Serine (S) at position 299 (G299S, p.Gly299Ser). 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 glycine (G) to small size and polar (S) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 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
Variant description: help In XHED. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 299 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 MNPKVFKLHPRSGELEVLVD G TYFIYSQVEVYYINFTDFAS 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                         MNPKVFKLHPRSGELEVLVDGTYFIYSQVEVYYINFTDFAS

Mouse                         MNPKVFKLHPRSGELEVLVDGTYFIYSQVEVYYINFTDFAS

Bovine                        MNPKVFKLHPRSGELEVLVDGTYFIYSQVEVYYINFTDFAS
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
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 299 – 307



Literature citations
Mutations leading to X-linked hypohidrotic ectodermal dysplasia affect three major functional domains in the tumor necrosis factor family member ectodysplasin-A.
Schneider P.; Street S.L.; Gaide O.; Hertig S.; Tardivel A.; Tschopp J.; Runkel L.; Alevizopoulos K.; Ferguson B.M.; Zonana J.;
J. Biol. Chem. 276:18819-18827(2001)
Cited for: VARIANTS XHED CYS-153; CYS-155; CYS-156; HIS-156; ASN-158; 183-GLY--PRO-194 DEL; 185-ASN--PRO-196 DEL; GLU-189; 191-PRO--PRO-196 DEL; ARG-207; ASP-218; 218-GLY--PRO-223 DEL; ARG-291; SER-299; CYS-320; CYS-343; ARG-374; PRO-378 AND MET-378; 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; Eight mutations of three genes (EDA, EDAR, and WNT10A) identified in seven hypohidrotic ectodermal dysplasia patients.
Zeng B.; Xiao X.; Li S.; Lu H.; Lu J.; Zhu L.; Yu D.; Zhao W.;
Genes (Basel) 7:0-0(2016)
Cited for: VARIANTS XHED CYS-155; ASP-221; SER-299 AND MET-338;
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.