ASpdb: an integrative knowledgebase of human protein isoforms from experimental and AI-predicted structures

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	Protein Summary
	AS Summary
	Protein Functional Features
	Gene Isoform Structures and Expression Levels
	Protein Structures
	pLDDT Score Distribution
	Ramachandran Plot of Protein Structures
	Potential Active Site Information
	Protein Structure and Feature Comparision
	Protein-Protein Interaction
	Related Drugs
	Related Diseases
	Clinically Important Variants

Protein:EDA

Protein Summary

Gene summary

Gene name: EDA
ASpdb.0 ID: 1896
	Gene
Gene symbol	EDA
Gene ID	1896
Gene name	ectodysplasin A
Synonyms	ECTD1\|ED1\|ED1-A1\|ED1-A2\|EDA-A1\|EDA-A2\|EDA1\|EDA2\|HED\|HED1\|ODT1\|STHAGX1\|TNLG7C\|XHED\|XLHED
Cytomap	Xq13.1
Type of gene	protein-coding
Description	ectodysplasin-AX-linked anhidroitic ectodermal dysplasia proteinoligodontia 1tumor necrosis factor ligand 7C
Modification date	20240403
UniProtAcc	Q92838

Gene ontology of this gene with evidence of Inferred from Direct Assay (IDA) from Entrez

Partner	Gene	GO ID	GO term	PubMed ID
Gene	EDA	GO:0005102	signaling receptor binding	11039935
Gene	EDA	GO:0005811	lipid droplet	-
Gene	EDA	GO:0043231	intracellular membrane-bounded organelle	-
Gene	EDA	GO:0051092	positive regulation of NF-kappaB transcription factor activity	11039935

AS Summary

Information of the canonical protein with experimentally identified structure from PDB (2023).

UniProt Acc	File name	PDB ID	Method	Resolution	Chain	Start	End
Q92838-1	Q92838-1_1rj7_E.pdb	1RJ7	X-ray	2.3	E	242	390

ASpdb's canonical and alternatively spliced isoform information.

accession_id	gene_name	canonical_id	alternative_id	canonical_length	alternative_length	canonical_start	canonical_end	type	originalSEQ	variationSEQ	alternative_start	alternative_end
Q92838	EDA	Q92838-1	Q92838-2	391	135	133	135	Substitution	MAL	GHQ	133	135
Q92838	EDA	Q92838-1	Q92838-2	391	135	136	391	Deletion	none	none	135	135
Q92838	EDA	Q92838-1	Q92838-3	391	389	307	308	Deletion	none	none	306	306
Q92838	EDA	Q92838-1	Q92838-5	391	147	133	147	Substitution	MALLNFFFPDEKPYS	VSHLVGAAAAPSPRG	133	147
Q92838	EDA	Q92838-1	Q92838-5	391	147	148	391	Deletion	none	none	147	147
Q92838	EDA	Q92838-1	Q92838-6	391	142	133	142	Substitution	MALLNFFFPD	ACFPQVLLSL	133	142
Q92838	EDA	Q92838-1	Q92838-6	391	142	143	391	Deletion	none	none	142	142
Q92838	EDA	Q92838-1	Q92838-7	391	148	133	147	Substitution	MALLNFFFPDEKPYS	DFDYIISFSYGLQGFC	133	148
Q92838	EDA	Q92838-1	Q92838-7	391	148	148	391	Deletion	none	none	148	148
Q92838	EDA	Q92838-1	Q92838-8	391	147	133	147	Substitution	MALLNFFFPDEKPYS	LHVSFSLRKKKAGHQ	133	147
Q92838	EDA	Q92838-1	Q92838-8	391	147	148	391	Deletion	none	none	147	147
Q92838	EDA	Q92838-1	Q92838-9	391	386	265	267	Deletion	none	none	264	264
Q92838	EDA	Q92838-1	Q92838-9	391	386	307	308	Deletion	none	none	303	303

Multiple sequence alignment of our canonical and alternatively spliced EDA

Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of EDA

UniProt-id	ENSG	ENST	ENSP
Q92838-1	ENSG00000158813.18	ENST00000374552.9	ENSP00000363680.4
Q92838-2	ENSG00000158813.18	ENST00000525810.5	ENSP00000434195.1
Q92838-3	ENSG00000158813.18	ENST00000374553.6	ENSP00000363681.2
Q92838-5	ENSG00000158813.18	ENST00000338901.4	ENSP00000340611.4
Q92838-7	ENSG00000158813.18	ENST00000527388.5	ENSP00000434861.1
Q92838-9	ENSG00000158813.18	ENST00000524573.5	ENSP00000432585.1

UniProt-id	NM ID	NP ID
Q92838-1	NM_001399.4	NP_001390.1
Q92838-2	NM_001005610.3	NP_001005610.2
Q92838-3	NM_001005609.1	NP_001005609.1
Q92838-7	NM_001005613.3	NP_001005613.1
Q92838-9	NM_001005612.2	NP_001005612.2

Amino acid sequences of our canonical and alternatively spliced EDA

accession_id	Protein sequence
Q92838-1	MGYPEVERRELLPAAAPRERGSQGCGCGGAPARAGEGNSCLLFLGFFGLSLALHLLTLCCYLELRSELRRERGAESRLGGSGTPGTSGTL SSLGGLDPDSPITSHLGQPSPKQQPLEPGEAALHSDSQDGHQMALLNFFFPDEKPYSEEESRRVRRNKRSKSNEGADGPVKNKKKGKKAG PPGPNGPPGPPGPPGPQGPPGIPGIPGIPGTTVMGPPGPPGPPGPQGPPGLQGPSGAADKAGTRENQPAVVHLQGQGSAIQVKNDLSGGV LNDWSRITMNPKVFKLHPRSGELEVLVDGTYFIYSQVEVYYINFTDFASYEVVVDEKPFLQCTRSIETGKTNYNTCYTAGVCLLKARQKI
Q92838-2	MGYPEVERRELLPAAAPRERGSQGCGCGGAPARAGEGNSCLLFLGFFGLSLALHLLTLCCYLELRSELRRERGAESRLGGSGTPGTSGTL
Q92838-3	MGYPEVERRELLPAAAPRERGSQGCGCGGAPARAGEGNSCLLFLGFFGLSLALHLLTLCCYLELRSELRRERGAESRLGGSGTPGTSGTL SSLGGLDPDSPITSHLGQPSPKQQPLEPGEAALHSDSQDGHQMALLNFFFPDEKPYSEEESRRVRRNKRSKSNEGADGPVKNKKKGKKAG PPGPNGPPGPPGPPGPQGPPGIPGIPGIPGTTVMGPPGPPGPPGPQGPPGLQGPSGAADKAGTRENQPAVVHLQGQGSAIQVKNDLSGGV LNDWSRITMNPKVFKLHPRSGELEVLVDGTYFIYSQVYYINFTDFASYEVVVDEKPFLQCTRSIETGKTNYNTCYTAGVCLLKARQKIAV
Q92838-5	MGYPEVERRELLPAAAPRERGSQGCGCGGAPARAGEGNSCLLFLGFFGLSLALHLLTLCCYLELRSELRRERGAESRLGGSGTPGTSGTL
Q92838-6	MGYPEVERRELLPAAAPRERGSQGCGCGGAPARAGEGNSCLLFLGFFGLSLALHLLTLCCYLELRSELRRERGAESRLGGSGTPGTSGTL
Q92838-7	MGYPEVERRELLPAAAPRERGSQGCGCGGAPARAGEGNSCLLFLGFFGLSLALHLLTLCCYLELRSELRRERGAESRLGGSGTPGTSGTL
Q92838-8	MGYPEVERRELLPAAAPRERGSQGCGCGGAPARAGEGNSCLLFLGFFGLSLALHLLTLCCYLELRSELRRERGAESRLGGSGTPGTSGTL
Q92838-9	MGYPEVERRELLPAAAPRERGSQGCGCGGAPARAGEGNSCLLFLGFFGLSLALHLLTLCCYLELRSELRRERGAESRLGGSGTPGTSGTL SSLGGLDPDSPITSHLGQPSPKQQPLEPGEAALHSDSQDGHQMALLNFFFPDEKPYSEEESRRVRRNKRSKSNEGADGPVKNKKKGKKAG PPGPNGPPGPPGPPGPQGPPGIPGIPGIPGTTVMGPPGPPGPPGPQGPPGLQGPSGAADKAGTRENQPAVVHLQGQGSAIQVKNGGVLND WSRITMNPKVFKLHPRSGELEVLVDGTYFIYSQVYYINFTDFASYEVVVDEKPFLQCTRSIETGKTNYNTCYTAGVCLLKARQKIAVKMV

Protein Functional Features

Main function of this protein. (from UniProt)

EDA (go to UniProt):Q92838

Retention analysis result of protein across 39 protein features of UniProt such as six molecule processing features, 13 region features, four site features, six amino acid modification features, two natural variation features, five experimental info features, and 3 secondary structure features. Here, because of limited space for viewing, we only show the protein feature retention information belong to the 13 regional features. All retention annotation result can be downloaded at
download page
* Minus value of BPloci means that the break pointn is located before the CDS.

- Retained protein feature among the 13 regional features.

Accession_id	Subsection	Start	End	Funcitonal feature	Splicing information
Q92838	Topological domain	63	391	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=133;End=135
Q92838	Topological domain	63	391	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=136;End=391
Q92838	Topological domain	63	391	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=307;End=308
Q92838	Topological domain	63	391	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=133;End=147
Q92838	Topological domain	63	391	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=148;End=391
Q92838	Topological domain	63	391	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=133;End=142
Q92838	Topological domain	63	391	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=143;End=391
Q92838	Topological domain	63	391	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=133;End=147
Q92838	Topological domain	63	391	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=148;End=391
Q92838	Topological domain	63	391	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=133;End=147
Q92838	Topological domain	63	391	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=148;End=391
Q92838	Topological domain	63	391	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=265;End=267
Q92838	Topological domain	63	391	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=307;End=308
Q92838	Domain	180	229	Note=Collagen-like	Type=Deletion;Start=136;End=391
Q92838	Domain	180	229	Note=Collagen-like	Type=Deletion;Start=148;End=391
Q92838	Domain	180	229	Note=Collagen-like	Type=Deletion;Start=143;End=391
Q92838	Domain	180	229	Note=Collagen-like	Type=Deletion;Start=148;End=391
Q92838	Domain	180	229	Note=Collagen-like	Type=Deletion;Start=148;End=391
Q92838	Region	146	245	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=136;End=391
Q92838	Region	146	245	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=133;End=147
Q92838	Region	146	245	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=148;End=391
Q92838	Region	146	245	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=143;End=391
Q92838	Region	146	245	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=133;End=147
Q92838	Region	146	245	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=148;End=391
Q92838	Region	146	245	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=133;End=147
Q92838	Region	146	245	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=148;End=391
Q92838	Compositional bias	146	174	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=136;End=391
Q92838	Compositional bias	146	174	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=133;End=147
Q92838	Compositional bias	146	174	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=148;End=391
Q92838	Compositional bias	146	174	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=143;End=391
Q92838	Compositional bias	146	174	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=133;End=147
Q92838	Compositional bias	146	174	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=148;End=391
Q92838	Compositional bias	146	174	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=133;End=147
Q92838	Compositional bias	146	174	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=148;End=391
Q92838	Compositional bias	181	230	Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=136;End=391
Q92838	Compositional bias	181	230	Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=148;End=391
Q92838	Compositional bias	181	230	Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=143;End=391
Q92838	Compositional bias	181	230	Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=148;End=391
Q92838	Compositional bias	181	230	Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=148;End=391

Gene Isoform Structures and Expression Levels for EDA

Gene structures of our canonical and alternative spliced genes of EDA
* Click on the image to open the UCSC genome browser with custom track showing this image in a new window.

Expression levels of gene isoforms across GTEx.

Expression levels of gene isoforms across TCGA.

Protein Structures

PDB and CIF files of the predicted protein structures
* Here we show the 3D structure of the proteins using Mol*. AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Model confidence is shown from the pLDDT values per residue. pLDDT corresponds to the model’s prediction of its score on the local Distance Difference Test. It is a measure of local accuracy (from AlphfaFold website). To color code individual residues, we transformed individual PDB files into CIF format.

3D view using mol* of Q92838-1

3D view using mol* of Q92838-2

3D view using mol* of Q92838-3

3D view using mol* of Q92838-5

3D view using mol* of Q92838-6

3D view using mol* of Q92838-7

3D view using mol* of Q92838-8

3D view using mol* of Q92838-9

pLDDT Score Distribution

pLDDT score distribution of the predicted protein structures from AlphaFold2
* AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100.

pLDDT distribution across the protein length of Q92838-1

pLDDT distribution across the protein length of Q92838-2

pLDDT distribution across the protein length of Q92838-3

pLDDT distribution across the protein length of Q92838-5

pLDDT distribution across the protein length of Q92838-6

pLDDT distribution across the protein length of Q92838-7

pLDDT distribution across the protein length of Q92838-8

pLDDT distribution across the protein length of Q92838-9

Ramachandran Plot of Protein Structures

Ramachandran plot of the torsional angles - phi (φ)and psi (ψ) - of the residues (amino acids) contained in this protein peptide.

Ramachandran plot of Q92838-1

Ramachandran plot of Q92838-2

Ramachandran plot of Q92838-5

Ramachandran plot of Q92838-6

Ramachandran plot of Q92838-7

Ramachandran plot of Q92838-8

Ramachandran plot of Q92838-9

Potential Active Site Information

The potential binding sites of these proteins were identified using SiteMap, a module of the Schrodinger suite.

UniProt-id	Site score	Size	D score	Volume	Exposure	Enclosure	Contact	Phobic	Philic	Balance	Don/Acc	Residues
Q92838-1	0.863	143	0.851	57.624	0.66	0.492	0.756	0.146	1.178	0.124	1.227	188,189,191,192,193,194,195,197,198,199,200,201,22 0,221,222,223,224,225,226,227,228,229,230,231,232, 233,234,235
Q92838-2	0.42	7	0.367	15.435	0.8	0.495	0.777	0.875	0.549	1.595	0.234	65,68,69,72
Q92838-3	0.86	223	0.847	106.33	0.625	0.488	0.752	0.181	1.185	0.153	1.17	185,186,187,188,189,190,191,192,193,194,195,196,19 7,198,199,200,201,202,203,204,220,221,222,223,224, 225,226,227,228,229,230,231,232,233,234,235,236,23 7
Q92838-5	0.434	9	0.369	14.063	0.69	0.515	0.845	1.116	0.681	1.637	0.143	65,68,69,72
Q92838-6	0.441	10	0.363	20.237	0.722	0.54	0.869	0.66	0.794	0.831	0.256	61,64,65,68,69,72
Q92838-7	0.664	33	0.635	101.528	0.713	0.592	0.746	0.813	0.798	1.018	3.231	57,58,60,61,64,130,133,137
Q92838-8	0.291	2	0.192	12.005	0.933	0.485	0.713	0.38	0.711	0.534	0.367	65,69,72
Q92838-9	0.864	196	0.853	85.064	0.636	0.494	0.751	0.135	1.175	0.115	1.23	183,184,185,186,188,189,190,191,192,193,194,195,19 6,197,198,200,221,222,223,224,225,226,227,228,229, 230,231,232,233,234,235,236,237,238,240

Protein Structure and Feature Comparision

Protein Structure Comparision Using Template Modeling Scores (TM-score).

Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Canonical validated structure (PDB)(green)

3D view using mol* of Q92838-1_Q92838-1_1rj7_E.pdb

Protein Structure Comparision Visualization with mol*. between Canonical validated structure (PDB)(orange) vs Alternative predicted structure (AF2)(green)

3D view using mol* of Q92838-1_1rj7_E_Q92838-2.pdb

3D view using mol* of Q92838-1_1rj7_E_Q92838-3.pdb

3D view using mol* of Q92838-1_1rj7_E_Q92838-5.pdb

3D view using mol* of Q92838-1_1rj7_E_Q92838-6.pdb

3D view using mol* of Q92838-1_1rj7_E_Q92838-7.pdb

3D view using mol* of Q92838-1_1rj7_E_Q92838-8.pdb

3D view using mol* of Q92838-1_1rj7_E_Q92838-9.pdb

Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Alternative predicted structure (AF2)(green)

3D view using mol* of Q92838-1_Q92838-2.pdb

3D view using mol* of Q92838-1_Q92838-3.pdb

3D view using mol* of Q92838-1_Q92838-5.pdb

3D view using mol* of Q92838-1_Q92838-6.pdb

3D view using mol* of Q92838-1_Q92838-7.pdb

3D view using mol* of Q92838-1_Q92838-8.pdb

3D view using mol* of Q92838-1_Q92838-9.pdb

Protein Feature Comparison of the protein sequendary structures among the protiens.

./stats/secondary_structure/figure/Q92838-1_vs_Q92838-2.png

./stats/secondary_structure/figure/Q92838-1_vs_Q92838-3.png

./stats/secondary_structure/figure/Q92838-1_vs_Q92838-5.png

./stats/secondary_structure/figure/Q92838-1_vs_Q92838-6.png

./stats/secondary_structure/figure/Q92838-1_vs_Q92838-7.png

./stats/secondary_structure/figure/Q92838-1_vs_Q92838-8.png

./stats/secondary_structure/figure/Q92838-1_vs_Q92838-9.png

Protein Feature Comparison of the relative accessible surface area (ASA) among the protiens.

./stats/relative_asa/Q92838-1_vs_Q92838-2.png

./stats/relative_asa/Q92838-1_vs_Q92838-3.png

./stats/relative_asa/Q92838-1_vs_Q92838-5.png

./stats/relative_asa/Q92838-1_vs_Q92838-6.png

./stats/relative_asa/Q92838-1_vs_Q92838-7.png

./stats/relative_asa/Q92838-1_vs_Q92838-8.png

./stats/relative_asa/Q92838-1_vs_Q92838-9.png

Protein-Protein Interaction

Interactors from UniProt.

Accession_id

Subsection

Start

End

Funcitonal feature

Splicing information

Interactors from STRING.

Gene name

Interactors

Related Drugs to EDA

Drugs targeting this gene/protein.
(DrugBank)

UniProt accession

Gene name

DrugBank ID

Drug name

Drug group

Actions

Related Diseases to EDA

Previous studies relating to the alternative splicing of EDA and disease information from the MeSH term (PubMed)

Gene	PMID	Title	Abstract	MeSH ID	MeSH term
EDA	9736768	The anhidrotic ectodermal dysplasia gene (EDA) undergoes alternative splicing and encodes ectodysplasin-A with deletion mutations in collagenous repeats.	Anhidrotic ectodermal dysplasia (EDA) is an X-linked recessive disorder which affects ectodermal structures. A cDNA encoding a 135 amino acid protein with mutations in 5-10% of EDA patients has been reported. We have built up a complete splicing map of the EDA gene and characterized the longest and what most probably represents the full-length EDA transcript, EDA-A. It encodes a 391 amino acid transmembrane protein with a short collagenous domain, (Gly-X-Y)19, and is highly homologous to the protein mutated in Tabby mice (Ta-A). Four new transcripts that code for truncated proteins lacking the collagenous domain were also detected. The splice variants show different expression patterns in eight tissues analyzed, suggesting a regulatory mechanism for gene expression. The EDA-A form of the protein is transported to the cell membrane and induces rounding of the cells, properties also associated with the 135 amino acid isoform. We have determined the genomic organization and the exon-intron boundaries of the EDA gene. SSCP analysis of the nine exons corresponding to EDA-A allowed the identification of mutations in 12 out of 15 EDA patients. Interestingly, three mutations removed either two or four of the Gly-X-Y repeats without interrupting the reading frame, thus suggesting a functional role for the collagenous domain. Our results will allow mutation diagnostics in the majority of patients.	D004476	Ectodermal Dysplasia
EDA	11378824	Mutational spectrum of the ED1 gene in X-linked hypohidrotic ectodermal dysplasia.	X-linked hypohidrotic ectodermal dysplasia (XLHED) is the most common form of the ectodermal dysplasias characterised by an abnormal development of eccrine sweat glands, hair and teeth. The ED1 gene responsible for the disorder undergoes extensive alternative splicing and to date few studies have concerned the full length transcript. We screened 52 unrelated families or sporadic cases for mutation in the full coding sequence of this gene. SSCA analysis or direct sequencing allowed identification of mutations in 34 families: one initiation defect, twenty-two missenses, two nonsense, eight insertions or deletions, and a large deletion encompassing all the ED1 gene. Fourteen of these mutations have not been previously described, including five missenses. One third of identified mutations were localised in codons 155 and 156, affecting CpG dinucleotides and nine of them correspond to the R156H missense. Hypothesis of a founder effect has been ruled out by haplotype analysis of flanking microsatellites. These recurrent mutations indicate the functional importance of the positively charged domain of the protein. Including our data, there are now 56 different mutations reported in 85 independent patients, that we have tabulated. Review of clinical features in the present series of affected males and female carriers showed no obvious correlation between the type of mutations, the phenotype and its severity. The X-chromosome pattern of inactivation in leucocytes showed little correlation with expressivity of the disease in female carriers. Finally this study is useful for functional studies of the protein and to define a diagnostic strategy for mutation screening of the ED1 gene.	D004476	Ectodermal Dysplasia

Clinically important variants in EDA

(ClinVar, 04/20/2024)

accession_id

uniprot_id

gene_name

Type

Variant

Clinical_significance