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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q92838: Variant p.Arg156His

Ectodysplasin-A
Gene: EDA
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Variant information Variant position: help 156 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 Arginine (R) to Histidine (H) at position 156 (R156H, p.Arg156His). 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 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: 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; abolishes proteolytic processing. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 156 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 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences. 
Human                         LNFFFPDEKPYSEEESRRVRRNKRSKSNEGADGPVKNKKKG

Mouse                         LNFFFPDEKAYSEEESRRVRRNKRSKSGEGADGPVKNKKKG

Bovine                        VNFFIPKEKSYSEEESRRVRRNKRSKSSEGADGPVKNKKKG
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
Topological domain 63 – 391 Extracellular
Region 146 – 245 Disordered
Compositional bias 146 – 174 Basic and acidic residues
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
Ectodysplasin is released by proteolytic shedding and binds to the EDAR protein.
Elomaa O.; Pulkkinen K.; Hannelius U.; Mikkola M.; Saarialho-Kere U.; Kere J.;
Hum. Mol. Genet. 10:953-962(2001)
Cited for: PROTEOLYTIC PROCESSING; CHARACTERIZATION OF VARIANT XHED CYS-153; CHARACTERIZATION OF VARIANT HIS-156; Mutations within a furin consensus sequence block proteolytic release of ectodysplasin-A and cause X-linked hypohidrotic ectodermal dysplasia.
Chen Y.; Molloy S.S.; Thomas L.; Gambee J.; Baechinger H.P.; Ferguson B.M.; Zonana J.; Thomas G.; Morris N.P.;
Proc. Natl. Acad. Sci. U.S.A. 98:7218-7223(2001)
Cited for: CHARACTERIZATION OF VARIANTS XHED CYS-153; CYS-155; CYS-156; HIS-156 AND ASN-158; MUTAGENESIS OF ARG-159; CLEAVAGE SITE; The mutation spectrum of the EDA gene in X-linked anhidrotic ectodermal dysplasia.
Paeaekkoenen K.; Cambiaghi S.; Novelli G.; Ouzts L.V.; Penttinen M.; Kere J.; Srivastava A.K.;
Hum. Mutat. 17:349-349(2001)
Cited for: VARIANTS XHED CYS-156; HIS-156; CYS-255; ASP-255; GLY-274; TYR-332 AND THR-349; 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; Mutation screening of the ectodysplasin-A receptor gene EDAR in hypohidrotic ectodermal dysplasia.
van der Hout A.H.; Oudesluijs G.G.; Venema A.; Verheij J.B.G.M.; Mol B.G.J.; Rump P.; Brunner H.G.; Vos Y.J.; van Essen A.J.;
Eur. J. Hum. Genet. 16:673-679(2008)
Cited for: VARIANTS XHED CYS-155; CYS-156; HIS-156; 183-GLY--PRO-194 DEL; 184-PRO--GLY-189 DEL; 185-ASN--PRO-196 DEL; ARG-291; TYR-298; GLY-307; ASP-372 AND ILE-373; 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.