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Q92838 (EDA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ectodysplasin-A
Alternative name(s):
Ectodermal dysplasia protein
Short name=EDA protein

Cleaved into the following 2 chains:

  1. Ectodysplasin-A, membrane form
  2. Ectodysplasin-A, secreted form
Gene names
Name:EDA
Synonyms:ED1, EDA2
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length391 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Seems to be involved in epithelial-mesenchymal signaling during morphogenesis of ectodermal organs. Isoform 1 binds only to the receptor EDAR, while isoform 3 binds exclusively to the receptor XEDAR.

Subunit structure

Homotrimer. The homotrimers may then dimerize and form higher order oligomers. Ref.10

Subcellular location

Cell membrane; Single-pass type II membrane protein.

Ectodysplasin-A, secreted form: Secreted.

Tissue specificity

Not abundant; expressed in specific cell types of ectodermal (but not mesodermal) origin of keratinocytes, hair follicles, sweat glands. Also in adult heart, liver, muscle, pancreas, prostate, fetal liver, uterus, small intestine and umbilical chord. Ref.6

Post-translational modification

N-glycosylated.

Processing by furin produces a secreted form.

Involvement in disease

Defects in EDA are the cause of ectodermal dysplasia type 1 (ED1) [MIM:305100]; also known as Christ-Siemens-Touraine syndrome or X-linked hypohidrotic ectodermal dysplasia (XLHED). Ectodermal dysplasia defines a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. ED1 is a disease characterized by sparse hair (atrichosis or hypotrichosis), abnormal or missing teeth and the inability to sweat due to the absence of sweat glands. ED1 is the most common form of over 150 clinically distinct ectodermal dysplasias. Ref.1 Ref.2 Ref.3 Ref.8 Ref.9 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.23 Ref.24 Ref.26 Ref.27 Ref.28 Ref.29

Defects in EDA are the cause of tooth agenesis selective X-linked type 1 (STHAGX1) [MIM:313500]. A form of selective tooth agenesis, a common anomaly characterized by the congenital absence of one or more teeth. Selective tooth agenesis without associated systemic disorders has sometimes been divided into 2 types: oligodontia, defined as agenesis of 6 or more permanent teeth, and hypodontia, defined as agenesis of less than 6 teeth. The number in both cases does not include absence of third molars (wisdom teeth). Ref.21 Ref.25

Sequence similarities

Belongs to the tumor necrosis factor family.

Contains 1 collagen-like domain.

Sequence caution

The sequence AAC77372.1 differs from that shown. Reason: Intron retention.

The sequence CAI39805.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI41611.1 differs from that shown. Reason: Erroneous gene model prediction.

Alternative products

This entry describes 8 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: Q92838-1)

Also known as: A1; II;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q92838-2)

Also known as: I;

The sequence of this isoform differs from the canonical sequence as follows:
     133-135: MAL → GHQ
     136-391: Missing.
Isoform 3 (identifier: Q92838-3)

Also known as: A2;

The sequence of this isoform differs from the canonical sequence as follows:
     307-308: Missing.
Isoform 4 (identifier: Q92838-5)

Also known as: C;

The sequence of this isoform differs from the canonical sequence as follows:
     133-147: MALLNFFFPDEKPYS → VSHLVGAAAAPSPRG
     148-391: Missing.
Isoform 5 (identifier: Q92838-6)

Also known as: D;

The sequence of this isoform differs from the canonical sequence as follows:
     133-142: MALLNFFFPD → ACFPQVLLSL
     143-391: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Isoform 6 (identifier: Q92838-7)

Also known as: E;

The sequence of this isoform differs from the canonical sequence as follows:
     133-147: MALLNFFFPDEKPYS → DFDYIISFSYGLQGFC
     148-391: Missing.
Isoform 7 (identifier: Q92838-8)

Also known as: F;

The sequence of this isoform differs from the canonical sequence as follows:
     133-147: MALLNFFFPDEKPYS → LHVSFSLRKKKAGHQ
     148-391: Missing.
Isoform 8 (identifier: Q92838-9)

The sequence of this isoform differs from the canonical sequence as follows:
     265-267: Missing.
     307-308: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 391391Ectodysplasin-A, membrane form
PRO_0000034538
Chain160 – 391232Ectodysplasin-A, secreted form
PRO_0000034539

Regions

Topological domain1 – 4141Cytoplasmic Potential
Transmembrane42 – 6221Helical; Signal-anchor for type II membrane protein; Potential
Topological domain63 – 391329Extracellular Potential
Domain180 – 22950Collagen-like

Sites

Site159 – 1602Cleavage; by furin

Amino acid modifications

Glycosylation3131N-linked (GlcNAc...) Potential
Glycosylation3721N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence133 – 14715MALLN…EKPYS → VSHLVGAAAAPSPRG in isoform 4.
VSP_006458
Alternative sequence133 – 14715MALLN…EKPYS → DFDYIISFSYGLQGFC in isoform 6.
VSP_006459
Alternative sequence133 – 14715MALLN…EKPYS → LHVSFSLRKKKAGHQ in isoform 7.
VSP_006460
Alternative sequence133 – 14210MALLNFFFPD → ACFPQVLLSL in isoform 5.
VSP_006456
Alternative sequence133 – 1353MAL → GHQ in isoform 2.
VSP_006454
Alternative sequence136 – 391256Missing in isoform 2.
VSP_006455
Alternative sequence143 – 391249Missing in isoform 5.
VSP_006457
Alternative sequence148 – 391244Missing in isoform 4, isoform 6 and isoform 7.
VSP_006461
Alternative sequence265 – 2673Missing in isoform 8.
VSP_038402
Alternative sequence307 – 3082Missing in isoform 3 and isoform 8.
VSP_006464
Natural variant541H → Y in ED1. Ref.11
VAR_010611
Natural variant551L → R in ED1. Ref.13
VAR_010612
Natural variant601C → R in ED1. Ref.16
VAR_013484
Natural variant611Y → H in ED1. Ref.1
VAR_005179
Natural variant631E → K in ED1. Ref.12
VAR_005180
Natural variant651R → G in STHAGX1. Ref.21
VAR_029534
Natural variant691R → L in ED1. Ref.1
VAR_005181
Natural variant1181P → L in a colorectal cancer sample; somatic mutation. Ref.22
VAR_036590
Natural variant1531R → C in ED1; abolishes proteolytic processing. Ref.8 Ref.9 Ref.18 Ref.26
VAR_054454
Natural variant1551R → C in ED1; abolishes proteolytic processing. Ref.9 Ref.18 Ref.24 Ref.26 Ref.28
VAR_005182
Natural variant1561R → C in ED1; abolishes proteolytic processing. Ref.9 Ref.17 Ref.18 Ref.24
VAR_005183
Natural variant1561R → G in ED1. Ref.29
VAR_064858
Natural variant1561R → H in ED1; abolishes proteolytic processing. Ref.8 Ref.9 Ref.17 Ref.18 Ref.24
VAR_005184
Natural variant1561R → S in ED1. Ref.14
VAR_054455
Natural variant1581K → N in ED1; abolishes proteolytic processing. Ref.9 Ref.18
VAR_054456
Natural variant183 – 19412Missing in ED1.
VAR_054457
Natural variant184 – 1896Missing in ED1.
VAR_054458
Natural variant185 – 19612Missing in ED1.
VAR_054459
Natural variant1891G → E in ED1. Ref.18
VAR_054460
Natural variant191 – 1966Missing in ED1.
VAR_054461
Natural variant192 – 1976Missing in ED1.
VAR_064859
Natural variant1981G → A in ED1. Ref.19
VAR_054462
Natural variant2071G → R in ED1. Ref.18
VAR_054463
Natural variant2071G → V in ED1. Ref.29
VAR_064860
Natural variant2091P → L in ED1.
VAR_005185
Natural variant2111T → R in ED1. Ref.29
VAR_064861
Natural variant218 – 2236Missing in ED1.
VAR_054465
Natural variant2181G → D in ED1. Ref.18
VAR_054464
Natural variant2241G → A in ED1.
VAR_005186
Natural variant2521H → L in ED1.
VAR_005187
Natural variant2521H → Y in ED1. Ref.16
VAR_013485
Natural variant2551G → C in ED1. Ref.17
VAR_011077
Natural variant2551G → D in ED1; mild. Ref.17
VAR_011078
Natural variant2661L → R in ED1. Ref.29
VAR_064862
Natural variant2691G → V in ED1. Ref.16
VAR_013486
Natural variant2741W → G in ED1. Ref.17
VAR_011079
Natural variant2741W → R in ED1. Ref.29
VAR_064863
Natural variant2911G → R in ED1. Ref.18 Ref.24
VAR_010613
Natural variant2911G → W in ED1.
VAR_010614
Natural variant2931L → P in ED1. Ref.29
VAR_064864
Natural variant2961L → V in ED1. Ref.29
VAR_064865
Natural variant2981D → H in ED1.
VAR_010615
Natural variant2981D → Y in ED1. Ref.24
VAR_054466
Natural variant2991G → D in ED1. Ref.29
VAR_064866
Natural variant2991G → S in ED1. Ref.18
VAR_005188
Natural variant3021F → S in ED1. Ref.16
VAR_013487
Natural variant3061Q → H in ED1. Ref.20
VAR_054467
Natural variant3071V → G in ED1. Ref.24
VAR_054468
Natural variant3201Y → C in ED1. Ref.18
VAR_054469
Natural variant3231V → G in ED1. Ref.29
VAR_064867
Natural variant3321C → Y in ED1. Ref.17
VAR_011080
Natural variant3381T → M in STHAGX1. Ref.25
VAR_064868
Natural variant3431Y → C in ED1. Ref.18
VAR_054470
Natural variant3461C → Y in ED1. Ref.29
VAR_064869
Natural variant3491A → T in ED1. Ref.15 Ref.17 Ref.26
VAR_005189
Natural variant3561A → D in ED1.
VAR_005190
Natural variant3561A → V in ED1. Ref.29
VAR_064870
Natural variant3571R → P in ED1.
VAR_005191
Natural variant3581Q → E in ED1. Ref.23
VAR_054471
Natural variant3601I → N in ED1. Ref.15
VAR_054472
Natural variant3721N → D in ED1. Ref.24
VAR_054473
Natural variant3731M → I in ED1. Ref.24
VAR_054474
Natural variant3741S → R in ED1. Ref.18
VAR_054475
Natural variant3781T → M in ED1. Ref.16 Ref.18 Ref.19
VAR_013488
Natural variant3781T → P in ED1. Ref.18
VAR_054476
Natural variant3811G → R in ED1. Ref.27
VAR_064871

Experimental info

Mutagenesis1591R → A: Abolishes proteolytic processing. Ref.9

Secondary structure

1 ............................. 391
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (A1) (II) [UniParc].

Last modified July 15, 1999. Version 2.
Checksum: 15DB3F5053293CBA

FASTA39141,294
        10         20         30         40         50         60 
MGYPEVERRE LLPAAAPRER GSQGCGCGGA PARAGEGNSC LLFLGFFGLS LALHLLTLCC 

        70         80         90        100        110        120 
YLELRSELRR ERGAESRLGG SGTPGTSGTL SSLGGLDPDS PITSHLGQPS PKQQPLEPGE 

       130        140        150        160        170        180 
AALHSDSQDG HQMALLNFFF PDEKPYSEEE SRRVRRNKRS KSNEGADGPV KNKKKGKKAG 

       190        200        210        220        230        240 
PPGPNGPPGP PGPPGPQGPP GIPGIPGIPG TTVMGPPGPP GPPGPQGPPG LQGPSGAADK 

       250        260        270        280        290        300 
AGTRENQPAV VHLQGQGSAI QVKNDLSGGV LNDWSRITMN PKVFKLHPRS GELEVLVDGT 

       310        320        330        340        350        360 
YFIYSQVEVY YINFTDFASY EVVVDEKPFL QCTRSIETGK TNYNTCYTAG VCLLKARQKI 

       370        380        390 
AVKMVHADIS INMSKHTTFF GAIRLGEAPA S

« Hide

Isoform 2 (I) [UniParc].

Checksum: 90C19D0674EC540D
Show »

FASTA13514,048
Isoform 3 (A2) [UniParc].

Checksum: 9289F3104CD83454
Show »

FASTA38941,065
Isoform 4 (C) [UniParc].

Checksum: 4B46D2AF7EF8063D
Show »

FASTA14715,097
Isoform 5 (D) [UniParc].

Checksum: C0ACDCC07BE70D7F
Show »

FASTA14214,798
Isoform 6 (E) [UniParc].

Checksum: B4473D0DBEFFD289
Show »

FASTA14815,582
Isoform 7 (F) [UniParc].

Checksum: F49B7DEFB05D4336
Show »

FASTA14715,443
Isoform 8 [UniParc].

Checksum: E498990FECC30F26
Show »

FASTA38640,750

References

« Hide 'large scale' references
[1]"X-linked anhidrotic (hypohidrotic) ectodermal dysplasia is caused by mutation in a novel transmembrane protein."
Kere J., Srivastava A.K., Montonen O., Zonana J., Thomas N.S.T., Ferguson B.M., Munoz F., Morgan D., Clarke A., Baybayan P., Chen E.Y., Ezer S., Saarialho-Kere U., la Chapelle A., Schlessinger D.
Nat. Genet. 13:409-416(1996) [PubMed: 8696334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-132, VARIANTS ED1 HIS-61 AND LEU-69.
Tissue: Sweat gland.
[2]"Identification of a new splice form of the EDA1 gene permits detection of nearly all X-linked hypohidrotic ectodermal dysplasia mutations."
Monreal A.W., Zonana J., Ferguson B.M.
Am. J. Hum. Genet. 63:380-389(1998) [PubMed: 9683615] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 133-391, VARIANTS ED1.
Tissue: Fetal liver.
[3]"The anhidrotic ectodermal dysplasia gene (EDA) undergoes alternative splicing and encodes ectodysplasin-A with deletion mutations in collagenous repeats."
Bayes M., Hartung A.J., Ezer S., Pispa J., Thesleff I., Srivastava A.K., Kere J.
Hum. Mol. Genet. 7:1661-1669(1998) [PubMed: 9736768] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3; 4; 5; 6 AND 7), VARIANTS ED1.
[4]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed: 15772651] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 8).
[6]"Expression of a novel transcript isoform of the EDA gene in human umbilical cord."
Kobielak K., Kobielak A., Trzciak W.H.
Eur. J. Hum. Genet. Suppl. 7:104-104(1999)
Cited for: TISSUE SPECIFICITY, ALTERNATIVE SPLICING.
[7]"Two-amino acid molecular switch in an epithelial morphogen that regulates binding to two distinct receptors."
Yan M., Wang L.-C., Hymowitz S.G., Schilbach S., Lee J., Goddard A., de Vos A.M., Gao W.-Q., Dixit V.M.
Science 290:523-527(2000) [PubMed: 11039935] [Abstract]
Cited for: RECEPTOR INTERACTION (ISOFORMS 1 AND 3).
[8]"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) [PubMed: 11309369] [Abstract]
Cited for: PROTEOLYTIC PROCESSING, CHARACTERIZATION OF VARIANT ED1 CYS-153, CHARACTERIZATION OF VARIANT HIS-156.
[9]"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) [PubMed: 11416205] [Abstract]
Cited for: CHARACTERIZATION OF VARIANTS ED1 CYS-153; CYS-155; CYS-156; HIS-156 AND ASN-158, MUTAGENESIS OF ARG-159, CLEAVAGE SITE.
[10]"The crystal structures of EDA-A1 and EDA-A2: splice variants with distinct receptor specificity."
Hymowitz S.G., Compaan D.M., Yan M., Wallweber H.J., Dixit V.M., Starovasnik M.A., de Vos A.M.
Structure 11:1513-1520(2003) [PubMed: 14656435] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 230-391, SUBUNIT.
[11]"A novel missense mutation (402C-->T) in exon 1 in the EDA gene in a family with X-linked hypohidrotic ectodermal dysplasia."
Hertz J.M., Noergaard Hansen K., Juncker I., Kjeldsen M., Gregersen N.
Clin. Genet. 53:205-209(1998) [PubMed: 9630076] [Abstract]
Cited for: VARIANT ED1 TYR-54.
[12]"Scarcity of mutations detected in families with X linked hypohidrotic ectodermal dysplasia: diagnostic implications."
Ferguson B.M., Thomas N.S.T., Munoz F., Morgan D., Clarke A., Zonana J.
J. Med. Genet. 35:112-115(1998) [PubMed: 9507389] [Abstract]
Cited for: VARIANT ED1 LYS-63.
[13]"X-linked anhidrotic (hypohidrotic) ectodermal dysplasia caused by a novel mutation in EDA1 gene: 406T > G (Leu55Arg)."
Martinez F., Millan J.M., Orellana C., Prieto F.
J. Invest. Dermatol. 113:285-286(1999) [PubMed: 10469321] [Abstract]
Cited for: VARIANT ED1 ARG-55.
[14]"A novel arginine-->Serine mutation in EDA1 in a Japanese family with X-linked anhidrotic ectodermal dysplasia."
Aoki N., Ito K., Tachibana T., Ito M.
J. Invest. Dermatol. 115:329-330(2000) [PubMed: 10951256] [Abstract]
Cited for: VARIANT ED1 SER-156.
[15]"Mutations in the EDA gene in three unrelated families reveal no apparent correlation between phenotype and genotype in the patients with an X-linked anhidrotic ectodermal dysplasia."
Kobielak K., Kobielak A., Roszkiewicz J., Wierzba J., Limon J., Trzeciak W.H.
Am. J. Med. Genet. 100:191-197(2001) [PubMed: 11343303] [Abstract]
Cited for: VARIANTS ED1 THR-349 AND ASN-360.
[16]"Mutational spectrum of the ED1 gene in X-linked hypohidrotic ectodermal dysplasia."
Vincent M.-C., Biancalana V., Ginisty D., Mandel J.-L., Calvas P.
Eur. J. Hum. Genet. 9:355-363(2001) [PubMed: 11378824] [Abstract]
Cited for: VARIANTS ED1 ARG-60; TYR-252; VAL-269; SER-302 AND MET-378.
[17]"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) [PubMed: 11295832] [Abstract]
Cited for: VARIANTS ED1 CYS-156; HIS-156; CYS-255; ASP-255; GLY-274; TYR-332 AND THR-349.
[18]"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) [PubMed: 11279189] [Abstract]
Cited for: VARIANTS ED1 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.
[19]"Pitfalls in clinical diagnosis of female carriers of X-linked hypohidrotic ectodermal dysplasia."
Vincent M.-C., Cossee M., Vabres P., Stewart F., Bonneau D., Calvas P.
Arch. Dermatol. 138:1256-1258(2002) [PubMed: 12225002] [Abstract]
Cited for: VARIANTS ED1 ALA-198 AND MET-378.
[20]"A novel missense mutation (Gln306His) in exon 7 of the ED1 gene causing anhidrotic ectodermal dysplasia with prominent milia-like facial sebaceous papules."
Hsu M.M.L., Chao S.C., Lu A.C.H.
Br. J. Dermatol. 149:443-445(2003) [PubMed: 12932274] [Abstract]
Cited for: VARIANT ED1 HIS-306.
[21]"A novel missense mutation of the EDA gene in a Mongolian family with congenital hypodontia."
Tao R., Jin B., Guo S.Z., Qing W., Feng G.Y., Brooks D.G., Liu L., Xu J., Li T., Yan Y., He L.
J. Hum. Genet. 51:498-502(2006) [PubMed: 16583127] [Abstract]
Cited for: VARIANT STHAGX1 GLY-65.
[22]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed: 16959974] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-118.
[23]"A novel Gln358Glu mutation in ectodysplasin A associated with X-linked dominant incisor hypodontia."
Tarpey P., Pemberton T.J., Stockton D.W., Das P., Ninis V., Edkins S., Andrew Futreal P., Wooster R., Kamath S., Nayak R., Stratton M.R., Patel P.I.
Am. J. Med. Genet. A 143:390-394(2007) [PubMed: 17256800] [Abstract]
Cited for: VARIANT ED1 GLU-358.
[24]"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) [PubMed: 18231121] [Abstract]
Cited for: VARIANTS ED1 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.
[25]"Novel EDA mutation resulting in X-linked non-syndromic hypodontia and the pattern of EDA-associated isolated tooth agenesis."
Han D., Gong Y., Wu H., Zhang X., Yan M., Wang X., Qu H., Feng H., Song S.
Eur. J. Med. Genet. 51:536-546(2008) [PubMed: 18657636] [Abstract]
Cited for: VARIANT STHAGX1 MET-338.
[26]"Identification of mutations in the EDA and EDAR genes in Pakistani families with hypohidrotic ectodermal dysplasia."
Shimomura Y., Wajid M., Weiser J., Kraemer L., Ishii Y., Lombillo V., Bale S.J., Christiano A.M.
Clin. Genet. 75:582-584(2009) [PubMed: 19438931] [Abstract]
Cited for: VARIANTS ED1 CYS-153; CYS-155 AND THR-349.
[27]"Two novel mutations in the ED1 gene in Japanese families with X-linked hypohidrotic ectodermal dysplasia."
Gunadi X., Miura K., Ohta M., Sugano A., Lee M.J., Sato Y., Matsunaga A., Hayashi K., Horikawa T., Miki K., Wataya-Kaneda M., Katayama I., Nishigori C., Matsuo M., Takaoka Y., Nishio H.
Pediatr. Res. 65:453-457(2009) [PubMed: 19127222] [Abstract]
Cited for: VARIANT ED1 ARG-381.
[28]"Missense mutation of the EDA gene in a Jordanian family with X-linked hypohidrotic ectodermal dysplasia: phenotypic appearance and speech problems."
Khabour O.F., Mesmar F.S., Al-Tamimi F., Al-Batayneh O.B., Owais A.I.
Genet. Mol. Res. 9:941-948(2010) [PubMed: 20486090] [Abstract]
Cited for: VARIANT ED1 CYS-155.
[29]"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. expand/collapse author list , de Prost Y., Munnich A., Bonnefont J.P., Bodemer C., Smahi A.
Hum. Mutat. 32:70-72(2011) [PubMed: 20979233] [Abstract]
Cited for: VARIANTS ED1 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.
+Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U59227 Genomic DNA. Translation: AAC50678.1.
U59228 mRNA. Translation: AAC50679.1.
AF060998 expand/collapse EMBL AC list , AF060992, AF060993, AF060994, AF060995, AF060996, AF060997 Genomic DNA. Translation: AAC36303.1.
AF060999 mRNA. Translation: AAC36302.1.
AF040628 mRNA. Translation: AAC77363.1.
AF061189 mRNA. Translation: AAC77371.1.
AF061190 mRNA. Translation: AAC77372.1. Sequence problems.
AF061191 mRNA. Translation: AAC77373.1.
AF061192 mRNA. Translation: AAC77374.1.
AF061193 mRNA. Translation: AAC77375.1.
AF061194 mRNA. Translation: AAC77376.1.
AL158069, AL450449 Genomic DNA. Translation: CAI41611.1. Sequence problems.
AL158069, AL158141, AL450449 Genomic DNA. Translation: CAI41612.2.
AL158069, AL158141, AL450449 Genomic DNA. Translation: CAM24742.1.
AL158141, AL450449, AL158069 Genomic DNA. Translation: CAI40385.2.
AL158141, AL158069, AL450449 Genomic DNA. Translation: CAM17680.1.
AL450449, AL158069 Genomic DNA. Translation: CAI39805.1. Sequence problems.
AL450449, AL158069, AL158141 Genomic DNA. Translation: CAI39806.2.
AL450449, AL158069, AL158141 Genomic DNA. Translation: CAM14498.1.
BC126143 mRNA. Translation: AAI26144.1.
BC144049 mRNA. Translation: AAI44050.1.
BC144051 mRNA. Translation: AAI44052.1.
IPIIPI00023765.
IPI00216145.
IPI00216147.
IPI00216148.
IPI00216149.
IPI00216150.
IPI00954278.
IPI00975907.
RefSeqNP_001005609.1. NM_001005609.1.
NP_001005610.2. NM_001005610.2.
NP_001005612.2. NM_001005612.2.
NP_001005613.1. NM_001005613.2.
NP_001390.1. NM_001399.4.
UniGeneHs.105407.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1RJ7X-ray2.30A/B/D/E/F/G/H/I/J/K/L/M233-391[»]
1RJ8X-ray2.23A/B/D/E/F/G230-391[»]
ProteinModelPortalQ92838.
SMRQ92838. Positions 242-390.
DisProtDP00460.
ModBaseSearch...

Protein-protein interaction databases

IntActQ92838. 1 interaction.
STRINGQ92838.

Polymorphism databases

DMDM6166135.

Proteomic databases

PRIDEQ92838.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000374552; ENSP00000363680; ENSG00000158813.
ENST00000374553; ENSP00000363681; ENSG00000158813.
GeneID1896.
KEGGhsa:1896.
UCSCuc004dxl.1. human.
uc004dxm.1. human.
uc004dxn.1. human.
uc004dxp.1. human.
uc004dxq.1. human.
uc004dxr.1. human.
uc004dxs.1. human.

Organism-specific databases

CTD1896.
GeneCardsGC0XP068752.
H-InvDBHIX0056123.
HGNCHGNC:3157. EDA.
HPACAB012644.
MIM300451. gene.
305100. phenotype.
313500. phenotype.
neXtProtNX_Q92838.
Orphanet181. Christ-Siemens-Touraine syndrome.
2227. Hypodontia.
PharmGKBPA27601.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG15197.
GeneTreeENSGT00600000084395.
HOVERGENHBG005564.
InParanoidQ92838.
OMAVKNKKKX.
OrthoDBEOG4Q2DGH.
PhylomeDBQ92838.

Gene expression databases

ArrayExpressQ92838.
BgeeQ92838.
GenevestigatorQ92838.
GermOnlineENSG00000158813. Homo sapiens.

Family and domain databases

InterProIPR008160. Collagen.
IPR006052. TNF.
IPR008983. Tumour_necrosis_fac-like.
[Graphical view]
Gene3DG3DSA:2.60.120.40. Tumour_necrosis_fac-like. 1 hit.
KOK05480.
PfamPF01391. Collagen. 1 hit.
PF00229. TNF. 1 hit.
[Graphical view]
SMARTSM00207. TNF. 1 hit.
[Graphical view]
SUPFAMSSF49842. TNF_like. 1 hit.
PROSITEPS00251. TNF_1. False negative.
PS50049. TNF_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio7729.
PMAP-CutDBQ92838.
SOURCESearch...

Entry information

Entry nameEDA_HUMAN
AccessionPrimary (citable) accession number: Q92838
Secondary accession number(s): A0AUZ2 expand/collapse secondary AC list , A2A337, B7ZLU2, B7ZLU4, O75910, Q5JS00, Q5JUM7, Q9UP77, Q9Y6L0, Q9Y6L1, Q9Y6L2, Q9Y6L3, Q9Y6L4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 15, 1999
Last modified: January 25, 2012
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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