Sequence information
Variant position: 156 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 391 The length of the canonical sequence.
Location on the sequence:
LNFFFPDEKPYSEEESRRVR
R NKRSKSNEGADGPVKNKKKG
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 LNFFFPDEKPYSEEESRRVRR NKRSKSNEGADGPVKNKKKG
Mouse LNFFFPDEKAYSEEESRRVRR NKRSKSGEGADGPVKNKKKG
Bovine VNFFIPKEKSYSEEESRRVRR NKRSKSSEGADGPVKNKKKG
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.
Type Positions Description
Chain
1 – 391
Ectodysplasin-A, membrane form
Topological domain
63 – 391
Extracellular
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.
Mutagenesis
159 – 159
R -> A. Abolishes proteolytic processing.
Literature citations
Only four genes (EDA1, EDAR, EDARADD, and WNT10A) account for 90% of hypohidrotic/anhidrotic ectodermal dysplasia cases.
Cluzeau C.; Hadj-Rabia S.; Jambou M.; Mansour S.; Guigue P.; Masmoudi S.; Bal E.; Chassaing N.; Vincent M.C.; Viot G.; Clauss F.; Maniere M.C.; Toupenay S.; Le Merrer M.; Lyonnet S.; Cormier-Daire V.; Amiel J.; Faivre L.; de Prost Y.; Munnich A.; Bonnefont J.P.; Bodemer C.; Smahi A.;
Hum. Mutat. 32:70-72(2011)
Cited for: VARIANTS XHED GLY-156; 192-GLY--GLN-197 DEL; VAL-207; ARG-211; ARG-266; ARG-274; PRO-293; VAL-296; ASP-299; GLY-323; TYR-346 AND VAL-356;
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.