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Q92838

- EDA_HUMAN

UniProt

Q92838 - EDA_HUMAN

Protein

Ectodysplasin-A

Gene

EDA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 2 (15 Jul 1999)
      Previous versions | rss
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    Functioni

    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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei159 – 1602Cleavage; by furin

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. receptor binding Source: HGNC

    GO - Biological processi

    1. cell differentiation Source: UniProtKB-KW
    2. cell-matrix adhesion Source: Ensembl
    3. ectoderm development Source: ProtInc
    4. gene expression Source: Ensembl
    5. hair follicle placode formation Source: Ensembl
    6. immune response Source: InterPro
    7. odontogenesis of dentin-containing tooth Source: Ensembl
    8. pigmentation Source: Ensembl
    9. positive regulation of canonical Wnt signaling pathway Source: Ensembl
    10. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: Ensembl
    11. positive regulation of NF-kappaB import into nucleus Source: Ensembl
    12. positive regulation of NF-kappaB transcription factor activity Source: HGNC
    13. salivary gland cavitation Source: Ensembl
    14. signal transduction Source: ProtInc
    15. trachea gland development Source: Ensembl

    Keywords - Molecular functioni

    Developmental protein

    Keywords - Biological processi

    Differentiation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ectodysplasin-A
    Alternative name(s):
    Ectodermal dysplasia protein
    Short name:
    EDA protein
    Cleaved into the following 2 chains:
    Gene namesi
    Name:EDA
    Synonyms:ED1, EDA2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:3157. EDA.

    Subcellular locationi

    GO - Cellular componenti

    1. apical part of cell Source: Ensembl
    2. collagen trimer Source: UniProtKB-KW
    3. cytoskeleton Source: ProtInc
    4. endoplasmic reticulum membrane Source: Ensembl
    5. extracellular region Source: UniProtKB-SubCell
    6. integral component of membrane Source: ProtInc
    7. integral component of plasma membrane Source: Ensembl
    8. intracellular membrane-bounded organelle Source: HPA
    9. membrane Source: ProtInc
    10. plasma membrane Source: ProtInc

    Keywords - Cellular componenti

    Cell membrane, Membrane, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Ectodermal dysplasia 1, hypohidrotic, X-linked (XHED) [MIM:305100]: A form of ectodermal dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. Characterized by sparse hair (atrichosis or hypotrichosis), abnormal or missing teeth and the inability to sweat due to the absence of sweat glands. It is the most common form of over 150 clinically distinct ectodermal dysplasias.21 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti54 – 541H → Y in XHED. 1 Publication
    VAR_010611
    Natural varianti55 – 551L → R in XHED. 1 Publication
    VAR_010612
    Natural varianti60 – 601C → R in XHED. 1 Publication
    VAR_013484
    Natural varianti61 – 611Y → H in XHED. 1 Publication
    VAR_005179
    Natural varianti63 – 631E → K in XHED. 1 Publication
    VAR_005180
    Natural varianti69 – 691R → L in XHED. 1 Publication
    Corresponds to variant rs132630309 [ dbSNP | Ensembl ].
    VAR_005181
    Natural varianti153 – 1531R → C in XHED; abolishes proteolytic processing. 2 Publications
    VAR_054454
    Natural varianti155 – 1551R → C in XHED; abolishes proteolytic processing. 4 Publications
    VAR_005182
    Natural varianti156 – 1561R → C in XHED; abolishes proteolytic processing. 3 Publications
    VAR_005183
    Natural varianti156 – 1561R → G in XHED. 1 Publication
    VAR_064858
    Natural varianti156 – 1561R → H in XHED; abolishes proteolytic processing. 3 Publications
    VAR_005184
    Natural varianti156 – 1561R → S in XHED. 1 Publication
    VAR_054455
    Natural varianti158 – 1581K → N in XHED; abolishes proteolytic processing. 1 Publication
    VAR_054456
    Natural varianti183 – 19412Missing in XHED.
    VAR_054457Add
    BLAST
    Natural varianti184 – 1896Missing in XHED.
    VAR_054458
    Natural varianti185 – 19612Missing in XHED.
    VAR_054459Add
    BLAST
    Natural varianti189 – 1891G → E in XHED. 1 Publication
    VAR_054460
    Natural varianti191 – 1966Missing in XHED.
    VAR_054461
    Natural varianti192 – 1976Missing in XHED.
    VAR_064859
    Natural varianti198 – 1981G → A in XHED. 1 Publication
    VAR_054462
    Natural varianti207 – 2071G → R in XHED. 1 Publication
    VAR_054463
    Natural varianti207 – 2071G → V in XHED. 1 Publication
    VAR_064860
    Natural varianti209 – 2091P → L in XHED.
    VAR_005185
    Natural varianti211 – 2111T → R in XHED. 1 Publication
    VAR_064861
    Natural varianti218 – 2236Missing in XHED. 1 Publication
    VAR_054465
    Natural varianti218 – 2181G → D in XHED. 1 Publication
    VAR_054464
    Natural varianti224 – 2241G → A in XHED.
    VAR_005186
    Natural varianti252 – 2521H → L in XHED.
    VAR_005187
    Natural varianti252 – 2521H → Y in XHED. 1 Publication
    VAR_013485
    Natural varianti255 – 2551G → C in XHED. 1 Publication
    VAR_011077
    Natural varianti255 – 2551G → D in XHED; mild. 1 Publication
    VAR_011078
    Natural varianti266 – 2661L → R in XHED. 1 Publication
    VAR_064862
    Natural varianti269 – 2691G → V in XHED. 1 Publication
    VAR_013486
    Natural varianti274 – 2741W → G in XHED. 1 Publication
    VAR_011079
    Natural varianti274 – 2741W → R in XHED. 1 Publication
    VAR_064863
    Natural varianti291 – 2911G → R in XHED. 2 Publications
    VAR_010613
    Natural varianti291 – 2911G → W in XHED.
    VAR_010614
    Natural varianti293 – 2931L → P in XHED. 1 Publication
    VAR_064864
    Natural varianti296 – 2961L → V in XHED. 1 Publication
    VAR_064865
    Natural varianti298 – 2981D → H in XHED.
    VAR_010615
    Natural varianti298 – 2981D → Y in XHED. 1 Publication
    VAR_054466
    Natural varianti299 – 2991G → D in XHED. 1 Publication
    VAR_064866
    Natural varianti299 – 2991G → S in XHED. 1 Publication
    VAR_005188
    Natural varianti302 – 3021F → S in XHED. 1 Publication
    VAR_013487
    Natural varianti306 – 3061Q → H in XHED. 1 Publication
    VAR_054467
    Natural varianti307 – 3071V → G in XHED. 1 Publication
    VAR_054468
    Natural varianti319 – 3191S → R in XHED. 1 Publication
    VAR_067319
    Natural varianti320 – 3201Y → C in XHED. 1 Publication
    VAR_054469
    Natural varianti323 – 3231V → G in XHED. 1 Publication
    VAR_064867
    Natural varianti332 – 3321C → Y in XHED. 1 Publication
    VAR_011080
    Natural varianti343 – 3431Y → C in XHED. 1 Publication
    VAR_054470
    Natural varianti346 – 3461C → Y in XHED. 1 Publication
    VAR_064869
    Natural varianti349 – 3491A → T in XHED. 3 Publications
    VAR_005189
    Natural varianti354 – 3541L → P in XHED. 1 Publication
    VAR_067250
    Natural varianti356 – 3561A → D in XHED.
    VAR_005190
    Natural varianti356 – 3561A → V in XHED. 1 Publication
    VAR_064870
    Natural varianti357 – 3571R → P in XHED.
    VAR_005191
    Natural varianti358 – 3581Q → E in XHED. 1 Publication
    VAR_054471
    Natural varianti360 – 3601I → N in XHED. 1 Publication
    VAR_054472
    Natural varianti372 – 3721N → D in XHED. 1 Publication
    VAR_054473
    Natural varianti373 – 3731M → I in XHED. 1 Publication
    VAR_054474
    Natural varianti374 – 3741S → R in XHED. 1 Publication
    VAR_054475
    Natural varianti378 – 3781T → M in XHED. 3 Publications
    VAR_013488
    Natural varianti378 – 3781T → P in XHED. 1 Publication
    VAR_054476
    Natural varianti381 – 3811G → R in XHED. 1 Publication
    VAR_064871
    Tooth agenesis selective X-linked 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).2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti65 – 651R → G in STHAGX1. 1 Publication
    VAR_029534
    Natural varianti338 – 3381T → M in STHAGX1. 1 Publication
    VAR_064868

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi159 – 1591R → A: Abolishes proteolytic processing. 1 Publication

    Keywords - Diseasei

    Disease mutation, Ectodermal dysplasia

    Organism-specific databases

    MIMi305100. phenotype.
    313500. phenotype.
    Orphaneti2227. Hypodontia.
    99798. Oligodontia.
    181. X-linked hypohidrotic ectodermal dysplasia.
    PharmGKBiPA27601.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 391391Ectodysplasin-A, membrane formPRO_0000034538Add
    BLAST
    Chaini160 – 391232Ectodysplasin-A, secreted formPRO_0000034539Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi313 – 3131N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi372 – 3721N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    N-glycosylated.
    Processing by furin produces a secreted form.

    Keywords - PTMi

    Cleavage on pair of basic residues, Glycoprotein

    Proteomic databases

    PaxDbiQ92838.
    PRIDEiQ92838.

    PTM databases

    PhosphoSiteiQ92838.

    Miscellaneous databases

    PMAP-CutDBQ92838.

    Expressioni

    Tissue specificityi

    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.1 Publication

    Gene expression databases

    ArrayExpressiQ92838.
    BgeeiQ92838.
    GenevestigatoriQ92838.

    Organism-specific databases

    HPAiCAB012644.
    HPA037972.
    HPA037973.

    Interactioni

    Subunit structurei

    Homotrimer. The homotrimers may then dimerize and form higher-order oligomers.1 Publication

    Protein-protein interaction databases

    BioGridi108224. 1 interaction.
    IntActiQ92838. 1 interaction.

    Structurei

    Secondary structure

    1
    391
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi249 – 2546
    Beta strandi257 – 2615
    Helixi262 – 2643
    Helixi266 – 2694
    Beta strandi275 – 2795
    Turni281 – 2833
    Beta strandi284 – 2863
    Turni288 – 2903
    Beta strandi293 – 2953
    Beta strandi299 – 3057
    Beta strandi308 – 3169
    Beta strandi318 – 3247
    Beta strandi327 – 33610
    Beta strandi338 – 3403
    Beta strandi342 – 35413
    Beta strandi359 – 3646
    Beta strandi370 – 3723
    Turni375 – 3773
    Beta strandi378 – 3869

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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/G230-389[»]
    DisProtiDP00460.
    ProteinModelPortaliQ92838.
    SMRiQ92838. Positions 242-390.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ92838.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 4141CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini63 – 391329ExtracellularSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei42 – 6221Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini180 – 22950Collagen-likeAdd
    BLAST

    Sequence similaritiesi

    Belongs to the tumor necrosis factor family.Curated
    Contains 1 collagen-like domain.Curated

    Keywords - Domaini

    Collagen, Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG82078.
    HOVERGENiHBG005564.
    InParanoidiQ92838.
    KOiK05480.
    OMAiSHGYELE.
    OrthoDBiEOG7FNC89.
    PhylomeDBiQ92838.
    TreeFamiTF332099.

    Family and domain databases

    Gene3Di2.60.120.40. 1 hit.
    InterProiIPR008160. Collagen.
    IPR006052. TNF_dom.
    IPR008983. Tumour_necrosis_fac-like_dom.
    [Graphical view]
    PfamiPF01391. Collagen. 1 hit.
    PF00229. TNF. 1 hit.
    [Graphical view]
    SMARTiSM00207. TNF. 1 hit.
    [Graphical view]
    SUPFAMiSSF49842. SSF49842. 1 hit.
    PROSITEiPS50049. TNF_2. 1 hit.
    [Graphical view]

    Sequences (8)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 8 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform 1 (identifier: Q92838-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MGYPEVERRE LLPAAAPRER GSQGCGCGGA PARAGEGNSC LLFLGFFGLS    50
    LALHLLTLCC YLELRSELRR ERGAESRLGG SGTPGTSGTL SSLGGLDPDS 100
    PITSHLGQPS PKQQPLEPGE AALHSDSQDG HQMALLNFFF PDEKPYSEEE 150
    SRRVRRNKRS KSNEGADGPV KNKKKGKKAG PPGPNGPPGP PGPPGPQGPP 200
    GIPGIPGIPG TTVMGPPGPP GPPGPQGPPG LQGPSGAADK AGTRENQPAV 250
    VHLQGQGSAI QVKNDLSGGV LNDWSRITMN PKVFKLHPRS GELEVLVDGT 300
    YFIYSQVEVY YINFTDFASY EVVVDEKPFL QCTRSIETGK TNYNTCYTAG 350
    VCLLKARQKI AVKMVHADIS INMSKHTTFF GAIRLGEAPA S 391
    Length:391
    Mass (Da):41,294
    Last modified:July 15, 1999 - v2
    Checksum:i15DB3F5053293CBA
    GO
    Isoform 2 (identifier: Q92838-2) [UniParc]FASTAAdd to Basket

    Also known as: I

    The sequence of this isoform differs from the canonical sequence as follows:
         133-135: MAL → GHQ
         136-391: Missing.

    Show »
    Length:135
    Mass (Da):14,048
    Checksum:i90C19D0674EC540D
    GO
    Isoform 3 (identifier: Q92838-3) [UniParc]FASTAAdd to Basket

    Also known as: A2

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

    Show »
    Length:389
    Mass (Da):41,065
    Checksum:i9289F3104CD83454
    GO
    Isoform 4 (identifier: Q92838-5) [UniParc]FASTAAdd to Basket

    Also known as: C

    The sequence of this isoform differs from the canonical sequence as follows:
         133-147: MALLNFFFPDEKPYS → VSHLVGAAAAPSPRG
         148-391: Missing.

    Show »
    Length:147
    Mass (Da):15,097
    Checksum:i4B46D2AF7EF8063D
    GO
    Isoform 5 (identifier: Q92838-6) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:142
    Mass (Da):14,798
    Checksum:iC0ACDCC07BE70D7F
    GO
    Isoform 6 (identifier: Q92838-7) [UniParc]FASTAAdd to Basket

    Also known as: E

    The sequence of this isoform differs from the canonical sequence as follows:
         133-147: MALLNFFFPDEKPYS → DFDYIISFSYGLQGFC
         148-391: Missing.

    Show »
    Length:148
    Mass (Da):15,582
    Checksum:iB4473D0DBEFFD289
    GO
    Isoform 7 (identifier: Q92838-8) [UniParc]FASTAAdd to Basket

    Also known as: F

    The sequence of this isoform differs from the canonical sequence as follows:
         133-147: MALLNFFFPDEKPYS → LHVSFSLRKKKAGHQ
         148-391: Missing.

    Show »
    Length:147
    Mass (Da):15,443
    Checksum:iF49B7DEFB05D4336
    GO
    Isoform 8 (identifier: Q92838-9) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:386
    Mass (Da):40,750
    Checksum:iE498990FECC30F26
    GO

    Sequence cautioni

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

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti54 – 541H → Y in XHED. 1 Publication
    VAR_010611
    Natural varianti55 – 551L → R in XHED. 1 Publication
    VAR_010612
    Natural varianti60 – 601C → R in XHED. 1 Publication
    VAR_013484
    Natural varianti61 – 611Y → H in XHED. 1 Publication
    VAR_005179
    Natural varianti63 – 631E → K in XHED. 1 Publication
    VAR_005180
    Natural varianti65 – 651R → G in STHAGX1. 1 Publication
    VAR_029534
    Natural varianti69 – 691R → L in XHED. 1 Publication
    Corresponds to variant rs132630309 [ dbSNP | Ensembl ].
    VAR_005181
    Natural varianti118 – 1181P → L in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036590
    Natural varianti153 – 1531R → C in XHED; abolishes proteolytic processing. 2 Publications
    VAR_054454
    Natural varianti155 – 1551R → C in XHED; abolishes proteolytic processing. 4 Publications
    VAR_005182
    Natural varianti156 – 1561R → C in XHED; abolishes proteolytic processing. 3 Publications
    VAR_005183
    Natural varianti156 – 1561R → G in XHED. 1 Publication
    VAR_064858
    Natural varianti156 – 1561R → H in XHED; abolishes proteolytic processing. 3 Publications
    VAR_005184
    Natural varianti156 – 1561R → S in XHED. 1 Publication
    VAR_054455
    Natural varianti158 – 1581K → N in XHED; abolishes proteolytic processing. 1 Publication
    VAR_054456
    Natural varianti183 – 19412Missing in XHED.
    VAR_054457Add
    BLAST
    Natural varianti184 – 1896Missing in XHED.
    VAR_054458
    Natural varianti185 – 19612Missing in XHED.
    VAR_054459Add
    BLAST
    Natural varianti189 – 1891G → E in XHED. 1 Publication
    VAR_054460
    Natural varianti191 – 1966Missing in XHED.
    VAR_054461
    Natural varianti192 – 1976Missing in XHED.
    VAR_064859
    Natural varianti198 – 1981G → A in XHED. 1 Publication
    VAR_054462
    Natural varianti207 – 2071G → R in XHED. 1 Publication
    VAR_054463
    Natural varianti207 – 2071G → V in XHED. 1 Publication
    VAR_064860
    Natural varianti209 – 2091P → L in XHED.
    VAR_005185
    Natural varianti211 – 2111T → R in XHED. 1 Publication
    VAR_064861
    Natural varianti218 – 2236Missing in XHED. 1 Publication
    VAR_054465
    Natural varianti218 – 2181G → D in XHED. 1 Publication
    VAR_054464
    Natural varianti224 – 2241G → A in XHED.
    VAR_005186
    Natural varianti252 – 2521H → L in XHED.
    VAR_005187
    Natural varianti252 – 2521H → Y in XHED. 1 Publication
    VAR_013485
    Natural varianti255 – 2551G → C in XHED. 1 Publication
    VAR_011077
    Natural varianti255 – 2551G → D in XHED; mild. 1 Publication
    VAR_011078
    Natural varianti266 – 2661L → R in XHED. 1 Publication
    VAR_064862
    Natural varianti269 – 2691G → V in XHED. 1 Publication
    VAR_013486
    Natural varianti274 – 2741W → G in XHED. 1 Publication
    VAR_011079
    Natural varianti274 – 2741W → R in XHED. 1 Publication
    VAR_064863
    Natural varianti291 – 2911G → R in XHED. 2 Publications
    VAR_010613
    Natural varianti291 – 2911G → W in XHED.
    VAR_010614
    Natural varianti293 – 2931L → P in XHED. 1 Publication
    VAR_064864
    Natural varianti296 – 2961L → V in XHED. 1 Publication
    VAR_064865
    Natural varianti298 – 2981D → H in XHED.
    VAR_010615
    Natural varianti298 – 2981D → Y in XHED. 1 Publication
    VAR_054466
    Natural varianti299 – 2991G → D in XHED. 1 Publication
    VAR_064866
    Natural varianti299 – 2991G → S in XHED. 1 Publication
    VAR_005188
    Natural varianti302 – 3021F → S in XHED. 1 Publication
    VAR_013487
    Natural varianti306 – 3061Q → H in XHED. 1 Publication
    VAR_054467
    Natural varianti307 – 3071V → G in XHED. 1 Publication
    VAR_054468
    Natural varianti319 – 3191S → R in XHED. 1 Publication
    VAR_067319
    Natural varianti320 – 3201Y → C in XHED. 1 Publication
    VAR_054469
    Natural varianti323 – 3231V → G in XHED. 1 Publication
    VAR_064867
    Natural varianti332 – 3321C → Y in XHED. 1 Publication
    VAR_011080
    Natural varianti338 – 3381T → M in STHAGX1. 1 Publication
    VAR_064868
    Natural varianti343 – 3431Y → C in XHED. 1 Publication
    VAR_054470
    Natural varianti346 – 3461C → Y in XHED. 1 Publication
    VAR_064869
    Natural varianti349 – 3491A → T in XHED. 3 Publications
    VAR_005189
    Natural varianti354 – 3541L → P in XHED. 1 Publication
    VAR_067250
    Natural varianti356 – 3561A → D in XHED.
    VAR_005190
    Natural varianti356 – 3561A → V in XHED. 1 Publication
    VAR_064870
    Natural varianti357 – 3571R → P in XHED.
    VAR_005191
    Natural varianti358 – 3581Q → E in XHED. 1 Publication
    VAR_054471
    Natural varianti360 – 3601I → N in XHED. 1 Publication
    VAR_054472
    Natural varianti372 – 3721N → D in XHED. 1 Publication
    VAR_054473
    Natural varianti373 – 3731M → I in XHED. 1 Publication
    VAR_054474
    Natural varianti374 – 3741S → R in XHED. 1 Publication
    VAR_054475
    Natural varianti378 – 3781T → M in XHED. 3 Publications
    VAR_013488
    Natural varianti378 – 3781T → P in XHED. 1 Publication
    VAR_054476
    Natural varianti381 – 3811G → R in XHED. 1 Publication
    VAR_064871

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei133 – 14715MALLN…EKPYS → VSHLVGAAAAPSPRG in isoform 4. 1 PublicationVSP_006458Add
    BLAST
    Alternative sequencei133 – 14715MALLN…EKPYS → DFDYIISFSYGLQGFC in isoform 6. 1 PublicationVSP_006459Add
    BLAST
    Alternative sequencei133 – 14715MALLN…EKPYS → LHVSFSLRKKKAGHQ in isoform 7. 1 PublicationVSP_006460Add
    BLAST
    Alternative sequencei133 – 14210MALLNFFFPD → ACFPQVLLSL in isoform 5. 1 PublicationVSP_006456
    Alternative sequencei133 – 1353MAL → GHQ in isoform 2. 1 PublicationVSP_006454
    Alternative sequencei136 – 391256Missing in isoform 2. 1 PublicationVSP_006455Add
    BLAST
    Alternative sequencei143 – 391249Missing in isoform 5. 1 PublicationVSP_006457Add
    BLAST
    Alternative sequencei148 – 391244Missing in isoform 4, isoform 6 and isoform 7. 1 PublicationVSP_006461Add
    BLAST
    Alternative sequencei265 – 2673Missing in isoform 8. 1 PublicationVSP_038402
    Alternative sequencei307 – 3082Missing in isoform 3 and isoform 8. 2 PublicationsVSP_006464

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U59227 Genomic DNA. Translation: AAC50678.1.
    U59228 mRNA. Translation: AAC50679.1.
    AH006445 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 Genomic DNA. No translation available.
    AL158141 Genomic DNA. No translation available.
    FO393403 Genomic DNA. No translation available.
    BC126143 mRNA. Translation: AAI26144.1.
    BC144049 mRNA. Translation: AAI44050.1.
    BC144051 mRNA. Translation: AAI44052.1.
    CCDSiCCDS14394.1. [Q92838-1]
    CCDS35318.2. [Q92838-2]
    CCDS35319.2. [Q92838-9]
    CCDS43966.1. [Q92838-3]
    CCDS55436.1. [Q92838-7]
    RefSeqiNP_001005609.1. NM_001005609.1. [Q92838-3]
    NP_001005610.2. NM_001005610.3. [Q92838-2]
    NP_001005612.2. NM_001005612.2. [Q92838-9]
    NP_001005613.1. NM_001005613.3. [Q92838-7]
    NP_001390.1. NM_001399.4. [Q92838-1]
    UniGeneiHs.105407.

    Genome annotation databases

    EnsembliENST00000338901; ENSP00000340611; ENSG00000158813. [Q92838-7]
    ENST00000374552; ENSP00000363680; ENSG00000158813. [Q92838-1]
    ENST00000374553; ENSP00000363681; ENSG00000158813. [Q92838-3]
    ENST00000524573; ENSP00000432585; ENSG00000158813. [Q92838-9]
    ENST00000525810; ENSP00000434195; ENSG00000158813. [Q92838-2]
    ENST00000527388; ENSP00000434861; ENSG00000158813. [Q92838-7]
    GeneIDi1896.
    KEGGihsa:1896.
    UCSCiuc004dxm.1. human. [Q92838-7]
    uc004dxn.1. human. [Q92838-2]
    uc004dxp.1. human. [Q92838-6]
    uc004dxr.3. human. [Q92838-3]
    uc004dxs.3. human. [Q92838-1]
    uc011mpj.2. human. [Q92838-9]

    Polymorphism databases

    DMDMi6166135.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U59227 Genomic DNA. Translation: AAC50678.1 .
    U59228 mRNA. Translation: AAC50679.1 .
    AH006445 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 Genomic DNA. No translation available.
    AL158141 Genomic DNA. No translation available.
    FO393403 Genomic DNA. No translation available.
    BC126143 mRNA. Translation: AAI26144.1 .
    BC144049 mRNA. Translation: AAI44050.1 .
    BC144051 mRNA. Translation: AAI44052.1 .
    CCDSi CCDS14394.1. [Q92838-1 ]
    CCDS35318.2. [Q92838-2 ]
    CCDS35319.2. [Q92838-9 ]
    CCDS43966.1. [Q92838-3 ]
    CCDS55436.1. [Q92838-7 ]
    RefSeqi NP_001005609.1. NM_001005609.1. [Q92838-3 ]
    NP_001005610.2. NM_001005610.3. [Q92838-2 ]
    NP_001005612.2. NM_001005612.2. [Q92838-9 ]
    NP_001005613.1. NM_001005613.3. [Q92838-7 ]
    NP_001390.1. NM_001399.4. [Q92838-1 ]
    UniGenei Hs.105407.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1RJ7 X-ray 2.30 A/B/D/E/F/G/H/I/J/K/L/M 233-391 [» ]
    1RJ8 X-ray 2.23 A/B/D/E/F/G 230-389 [» ]
    DisProti DP00460.
    ProteinModelPortali Q92838.
    SMRi Q92838. Positions 242-390.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108224. 1 interaction.
    IntActi Q92838. 1 interaction.

    PTM databases

    PhosphoSitei Q92838.

    Polymorphism databases

    DMDMi 6166135.

    Proteomic databases

    PaxDbi Q92838.
    PRIDEi Q92838.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000338901 ; ENSP00000340611 ; ENSG00000158813 . [Q92838-7 ]
    ENST00000374552 ; ENSP00000363680 ; ENSG00000158813 . [Q92838-1 ]
    ENST00000374553 ; ENSP00000363681 ; ENSG00000158813 . [Q92838-3 ]
    ENST00000524573 ; ENSP00000432585 ; ENSG00000158813 . [Q92838-9 ]
    ENST00000525810 ; ENSP00000434195 ; ENSG00000158813 . [Q92838-2 ]
    ENST00000527388 ; ENSP00000434861 ; ENSG00000158813 . [Q92838-7 ]
    GeneIDi 1896.
    KEGGi hsa:1896.
    UCSCi uc004dxm.1. human. [Q92838-7 ]
    uc004dxn.1. human. [Q92838-2 ]
    uc004dxp.1. human. [Q92838-6 ]
    uc004dxr.3. human. [Q92838-3 ]
    uc004dxs.3. human. [Q92838-1 ]
    uc011mpj.2. human. [Q92838-9 ]

    Organism-specific databases

    CTDi 1896.
    GeneCardsi GC0XP068752.
    GeneReviewsi EDA.
    HGNCi HGNC:3157. EDA.
    HPAi CAB012644.
    HPA037972.
    HPA037973.
    MIMi 300451. gene.
    305100. phenotype.
    313500. phenotype.
    neXtProti NX_Q92838.
    Orphaneti 2227. Hypodontia.
    99798. Oligodontia.
    181. X-linked hypohidrotic ectodermal dysplasia.
    PharmGKBi PA27601.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG82078.
    HOVERGENi HBG005564.
    InParanoidi Q92838.
    KOi K05480.
    OMAi SHGYELE.
    OrthoDBi EOG7FNC89.
    PhylomeDBi Q92838.
    TreeFami TF332099.

    Miscellaneous databases

    EvolutionaryTracei Q92838.
    GeneWikii EDA_(gene).
    GenomeRNAii 1896.
    NextBioi 7729.
    PMAP-CutDB Q92838.
    PROi Q92838.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q92838.
    Bgeei Q92838.
    Genevestigatori Q92838.

    Family and domain databases

    Gene3Di 2.60.120.40. 1 hit.
    InterProi IPR008160. Collagen.
    IPR006052. TNF_dom.
    IPR008983. Tumour_necrosis_fac-like_dom.
    [Graphical view ]
    Pfami PF01391. Collagen. 1 hit.
    PF00229. TNF. 1 hit.
    [Graphical view ]
    SMARTi SM00207. TNF. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49842. SSF49842. 1 hit.
    PROSITEi PS50049. TNF_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-132, VARIANTS XHED 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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 133-391, VARIANTS XHED.
      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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3; 4; 5; 6 AND 7), VARIANTS XHED.
    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.
      , 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING, CHARACTERIZATION OF VARIANT XHED 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] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANTS XHED 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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: VARIANT XHED 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] [Europe PMC] [Abstract]
      Cited for: VARIANT XHED 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] [Europe PMC] [Abstract]
      Cited for: VARIANT XHED 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] [Europe PMC] [Abstract]
      Cited for: VARIANT XHED 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] [Europe PMC] [Abstract]
      Cited for: VARIANTS XHED 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] [Europe PMC] [Abstract]
      Cited for: VARIANTS XHED 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] [Europe PMC] [Abstract]
      Cited for: VARIANTS XHED 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] [Europe PMC] [Abstract]
      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.
    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] [Europe PMC] [Abstract]
      Cited for: VARIANTS XHED 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] [Europe PMC] [Abstract]
      Cited for: VARIANT XHED 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] [Europe PMC] [Abstract]
      Cited for: VARIANT STHAGX1 GLY-65.
    22. 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] [Europe PMC] [Abstract]
      Cited for: VARIANT XHED 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] [Europe PMC] [Abstract]
      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.
    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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: VARIANTS XHED 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] [Europe PMC] [Abstract]
      Cited for: VARIANT XHED 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] [Europe PMC] [Abstract]
      Cited for: VARIANT XHED CYS-155.
    29. 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.
    30. "Mutation p.Leu354Pro in EDA causes severe hypohidrotic ectodermal dysplasia in a Chinese family."
      Liu Y., Yu X., Wang L., Li C., Archacki S., Huang C., Liu J.Y., Wang Q., Liu M., Tang Z.
      Gene 491:246-250(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT XHED PRO-354.
    31. "A new mutation in EDA gene in X-linked hypohidrotic ectodermal dysplasia associated with keratoconus."
      Piccione M., Serra G., Sanfilippo C., Andreucci E., Sani I., Corsello G.
      Minerva Pediatr. 64:59-64(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT XHED ARG-319.

    Entry informationi

    Entry nameiEDA_HUMAN
    AccessioniPrimary (citable) accession number: Q92838
    Secondary accession number(s): A0AUZ2
    , A2A337, B7ZLU2, B7ZLU4, O75910, Q5JS00, Q5JUM7, Q9UP77, Q9Y6L0, Q9Y6L1, Q9Y6L2, Q9Y6L3, Q9Y6L4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: July 15, 1999
    Last modified: October 1, 2014
    This is version 151 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3