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Q92838

- EDA_HUMAN

UniProt

Q92838 - EDA_HUMAN

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Protein

Ectodysplasin-A

Gene
EDA, ED1, EDA2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4141Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei42 – 6221Helical; Signal-anchor for type II membrane protein; Reviewed predictionAdd
BLAST
Topological domaini63 – 391329Extracellular Reviewed predictionAdd
BLAST

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
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.23 Publications
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. 4 Publications
VAR_054454
Natural varianti155 – 1551R → C in XHED; abolishes proteolytic processing. 5 Publications
VAR_005182
Natural varianti156 – 1561R → C in XHED; abolishes proteolytic processing. 4 Publications
VAR_005183
Natural varianti156 – 1561R → G in XHED. 1 Publication
VAR_064858
Natural varianti156 – 1561R → H in XHED; abolishes proteolytic processing. 5 Publications
VAR_005184
Natural varianti156 – 1561R → S in XHED. 1 Publication
VAR_054455
Natural varianti158 – 1581K → N in XHED; abolishes proteolytic processing. 2 Publications
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.
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).
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
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...) Reviewed prediction
Glycosylationi372 – 3721N-linked (GlcNAc...) Reviewed prediction

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.

Miscellaneous databases

EvolutionaryTraceiQ92838.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

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. 4 Publications
VAR_054454
Natural varianti155 – 1551R → C in XHED; abolishes proteolytic processing. 5 Publications
VAR_005182
Natural varianti156 – 1561R → C in XHED; abolishes proteolytic processing. 4 Publications
VAR_005183
Natural varianti156 – 1561R → G in XHED. 1 Publication
VAR_064858
Natural varianti156 – 1561R → H in XHED; abolishes proteolytic processing. 5 Publications
VAR_005184
Natural varianti156 – 1561R → S in XHED. 1 Publication
VAR_054455
Natural varianti158 – 1581K → N in XHED; abolishes proteolytic processing. 2 Publications
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.
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. VSP_006458Add
BLAST
Alternative sequencei133 – 14715MALLN…EKPYS → DFDYIISFSYGLQGFC in isoform 6. VSP_006459Add
BLAST
Alternative sequencei133 – 14715MALLN…EKPYS → LHVSFSLRKKKAGHQ in isoform 7. VSP_006460Add
BLAST
Alternative sequencei133 – 14210MALLNFFFPD → ACFPQVLLSL in isoform 5. VSP_006456
Alternative sequencei133 – 1353MAL → GHQ in isoform 2. VSP_006454
Alternative sequencei136 – 391256Missing in isoform 2. VSP_006455Add
BLAST
Alternative sequencei143 – 391249Missing in isoform 5. VSP_006457Add
BLAST
Alternative sequencei148 – 391244Missing in isoform 4, isoform 6 and isoform 7. VSP_006461Add
BLAST
Alternative sequencei265 – 2673Missing in isoform 8. VSP_038402
Alternative sequencei307 – 3082Missing in isoform 3 and isoform 8. VSP_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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 150 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

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