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Protein

Tumor necrosis factor receptor superfamily member EDAR

Gene

EDAR

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

Functioni

Receptor for EDA isoform A1, but not for EDA isoform A2. Mediates the activation of NF-kappa-B and JNK. May promote caspase-independent cell death.

GO - Molecular functioni

  • receptor activity Source: HGNC
  • transmembrane signaling receptor activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Receptor

Keywords - Biological processi

Apoptosis, Differentiation

Enzyme and pathway databases

BioCyciZFISH:ENSG00000135960-MONOMER.
ReactomeiR-HSA-5669034. TNFs bind their physiological receptors.
SIGNORiQ9UNE0.

Names & Taxonomyi

Protein namesi
Recommended name:
Tumor necrosis factor receptor superfamily member EDAR
Alternative name(s):
Anhidrotic ectodysplasin receptor 1
Downless homolog
EDA-A1 receptor
Ectodermal dysplasia receptor
Ectodysplasin-A receptor
Gene namesi
Name:EDAR
Synonyms:DL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:2895. EDAR.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini27 – 187ExtracellularSequence analysisAdd BLAST161
Transmembranei188 – 208HelicalSequence analysisAdd BLAST21
Topological domaini209 – 448CytoplasmicSequence analysisAdd BLAST240

GO - Cellular componenti

  • apical part of cell Source: Ensembl
  • integral component of membrane Source: UniProtKB
  • plasma membrane Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

Ectodermal dysplasia 10A, hypohidrotic/hair/nail type, autosomal dominant (ECTD10A)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of ectodermal dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. It is an autosomal dominant condition characterized by hypotrichosis, abnormal or missing teeth, and hypohidrosis due to the absence of sweat glands.
See also OMIM:129490
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_013450420R → Q in ECTD10A and ECTD10B; abolishes NF-kappa-B activation and reduces JNK activation. 5 PublicationsCorresponds to variant rs121908453dbSNPEnsembl.1
Ectodermal dysplasia 10B, hypohidrotic/hair/tooth type, autosomal recessive (ECTD10B)7 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder due to abnormal development of two or more ectodermal structures, and characterized by sparse hair (atrichosis or hypotrichosis), abnormal or missing teeth and the inability to sweat due to the absence of sweat glands.
See also OMIM:224900
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05444447C → Y in ECTD10B. 1 PublicationCorresponds to variant rs778903951dbSNPEnsembl.1
Natural variantiVAR_01344887C → R in ECTD10B. 1 PublicationCorresponds to variant rs121908451dbSNPEnsembl.1
Natural variantiVAR_01344989R → H in ECTD10B. 4 PublicationsCorresponds to variant rs121908450dbSNPEnsembl.1
Natural variantiVAR_06483098R → Q in ECTD10B. 1 PublicationCorresponds to variant rs144473052dbSNPEnsembl.1
Natural variantiVAR_054445110D → A in ECTD10B. 2 PublicationsCorresponds to variant rs121908455dbSNPEnsembl.1
Natural variantiVAR_054446148C → R in ECTD10B. 1 Publication1
Natural variantiVAR_064831358R → Q in ECTD10B. 2 Publications1
Natural variantiVAR_054447375R → H in ECTD10B; the mutant protein does not interact with EDARADD and is functionally inactive. 1 PublicationCorresponds to variant rs121908454dbSNPEnsembl.1
Natural variantiVAR_054448377L → F in ECTD10B. 1 Publication1
Natural variantiVAR_054449382G → S in ECTD10B. 1 PublicationCorresponds to variant rs747806672dbSNPEnsembl.1
Natural variantiVAR_064832396Q → QQ in ECTD10B. 1 Publication1
Natural variantiVAR_054450403T → M in ECTD10B. 2 Publications1
Natural variantiVAR_064833408I → F in ECTD10B. 1 Publication1
Natural variantiVAR_054451413T → P in ECTD10B. 1 Publication1
Natural variantiVAR_054452418I → T in ECTD10B. 1 Publication1
Natural variantiVAR_013450420R → Q in ECTD10A and ECTD10B; abolishes NF-kappa-B activation and reduces JNK activation. 5 PublicationsCorresponds to variant rs121908453dbSNPEnsembl.1
Natural variantiVAR_054453434W → C in ECTD10B. 1 PublicationCorresponds to variant rs528478080dbSNPEnsembl.1
Natural variantiVAR_064834434W → R in ECTD10B. 1 PublicationCorresponds to variant rs773885029dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi379E → K: Reduces activation of NF-kappa-B. 1 Publication1

Keywords - Diseasei

Disease mutation, Ectodermal dysplasia

Organism-specific databases

DisGeNETi10913.
MalaCardsiEDAR.
MIMi129490. phenotype.
224900. phenotype.
612630. phenotype.
OpenTargetsiENSG00000135960.
Orphaneti1810. Autosomal dominant hypohidrotic ectodermal dysplasia.
248. Autosomal recessive hypohidrotic ectodermal dysplasia.
PharmGKBiPA27602.

Chemistry databases

ChEMBLiCHEMBL1250376.

Polymorphism and mutation databases

BioMutaiEDAR.
DMDMi21263572.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 261 PublicationAdd BLAST26
ChainiPRO_000003460827 – 448Tumor necrosis factor receptor superfamily member EDARAdd BLAST422

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi31 ↔ 44By similarity
Glycosylationi38N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi47 ↔ 60By similarity
Disulfide bondi50 ↔ 71By similarity
Disulfide bondi74 ↔ 87By similarity
Disulfide bondi93 ↔ 113By similarity
Disulfide bondi135 ↔ 148By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9UNE0.
PeptideAtlasiQ9UNE0.
PRIDEiQ9UNE0.

PTM databases

iPTMnetiQ9UNE0.
PhosphoSitePlusiQ9UNE0.

Expressioni

Tissue specificityi

Detected in fetal kidney, lung, skin and cultured neonatal epidermal keratinocytes. Not detected in lymphoblast and fibroblast cell lines.

Developmental stagei

Found in craniofacial tissues from embryonic day 42-53. Expressed in fetal skin 11 and 15 weeks after gestation.

Gene expression databases

BgeeiENSG00000135960.
CleanExiHS_EDAR.
GenevisibleiQ9UNE0. HS.

Organism-specific databases

HPAiHPA042292.

Interactioni

Subunit structurei

Binds to EDARADD. Associates with TRAF1, TRAF2, TRAF3 and NIK.

Protein-protein interaction databases

BioGridi116118. 7 interactors.
IntActiQ9UNE0. 6 interactors.
STRINGi9606.ENSP00000258443.

Structurei

3D structure databases

ProteinModelPortaliQ9UNE0.
SMRiQ9UNE0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati30 – 71TNFR-Cys 1Add BLAST42
Repeati73 – 113TNFR-Cys 2Add BLAST41
Repeati115 – 148TNFR-Cys 3Add BLAST34
Domaini358 – 431DeathAdd BLAST74

Sequence similaritiesi

Contains 1 death domain.Curated
Contains 3 TNFR-Cys repeats.Curated

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IGTD. Eukaryota.
ENOG41104RU. LUCA.
GeneTreeiENSGT00730000111254.
HOGENOMiHOG000112327.
HOVERGENiHBG031530.
InParanoidiQ9UNE0.
KOiK05162.
OMAiPNTKECV.
OrthoDBiEOG091G0ADI.
PhylomeDBiQ9UNE0.
TreeFamiTF331385.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
InterProiIPR011029. DEATH-like_dom.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9UNE0-1) [UniParc]FASTAAdd to basket

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

        10         20         30         40         50
MAHVGDCTQT PWLPVLVVSL MCSARAEYSN CGENEYYNQT TGLCQECPPC
60 70 80 90 100
GPGEEPYLSC GYGTKDEDYG CVPCPAEKFS KGGYQICRRH KDCEGFFRAT
110 120 130 140 150
VLTPGDMEND AECGPCLPGY YMLENRPRNI YGMVCYSCLL APPNTKECVG
160 170 180 190 200
ATSGASANFP GTSGSSTLSP FQHAHKELSG QGHLATALII AMSTIFIMAI
210 220 230 240 250
AIVLIIMFYI LKTKPSAPAC CTSHPGKSVE AQVSKDEEKK EAPDNVVMFS
260 270 280 290 300
EKDEFEKLTA TPAKPTKSEN DASSENEQLL SRSVDSDEEP APDKQGSPEL
310 320 330 340 350
CLLSLVHLAR EKSATSNKSA GIQSRRKKIL DVYANVCGVV EGLSPTELPF
360 370 380 390 400
DCLEKTSRML SSTYNSEKAV VKTWRHLAES FGLKRDEIGG MTDGMQLFDR
410 420 430 440
ISTAGYSIPE LLTKLVQIER LDAVESLCAD ILEWAGVVPP ASQPHAAS
Length:448
Mass (Da):48,582
Last modified:May 1, 2000 - v1
Checksum:iAC8D61249D608439
GO
Isoform 2 (identifier: Q9UNE0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     219-219: A → GDGPHAPVPCFLDSPSTPPVGEPGCSLPPLSPA

Note: No experimental confirmation available.Curated
Show »
Length:480
Mass (Da):51,690
Checksum:i4262977A6EAE8D2A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti156S → P in BAG36519 (PubMed:14702039).Curated1
Sequence conflicti262P → S in AAD50077 (PubMed:10431241).Curated1
Isoform 2 (identifier: Q9UNE0-2)
Sequence conflicti229F → L in BAG59487 (PubMed:14702039).Curated1

Polymorphismi

Genetic variation in EDAR is associated with variations in head hair thickness and defines the hair morphology locus 1 (HRM1) [MIMi:612630]. Besides skin color and facial features, hair morphology is one of the most distinctive traits among human populations, and classical classification of human population is based on such visible traits.

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05444447C → Y in ECTD10B. 1 PublicationCorresponds to variant rs778903951dbSNPEnsembl.1
Natural variantiVAR_01344887C → R in ECTD10B. 1 PublicationCorresponds to variant rs121908451dbSNPEnsembl.1
Natural variantiVAR_01344989R → H in ECTD10B. 4 PublicationsCorresponds to variant rs121908450dbSNPEnsembl.1
Natural variantiVAR_06483098R → Q in ECTD10B. 1 PublicationCorresponds to variant rs144473052dbSNPEnsembl.1
Natural variantiVAR_054445110D → A in ECTD10B. 2 PublicationsCorresponds to variant rs121908455dbSNPEnsembl.1
Natural variantiVAR_054446148C → R in ECTD10B. 1 Publication1
Natural variantiVAR_064831358R → Q in ECTD10B. 2 Publications1
Natural variantiVAR_020011370V → A Associated with increase in hair thickness; results in decreased downstream activity of NFKB1 48 hours after transfection into cells. 3 PublicationsCorresponds to variant rs3827760dbSNPEnsembl.1
Natural variantiVAR_054447375R → H in ECTD10B; the mutant protein does not interact with EDARADD and is functionally inactive. 1 PublicationCorresponds to variant rs121908454dbSNPEnsembl.1
Natural variantiVAR_054448377L → F in ECTD10B. 1 Publication1
Natural variantiVAR_054449382G → S in ECTD10B. 1 PublicationCorresponds to variant rs747806672dbSNPEnsembl.1
Natural variantiVAR_064832396Q → QQ in ECTD10B. 1 Publication1
Natural variantiVAR_054450403T → M in ECTD10B. 2 Publications1
Natural variantiVAR_064833408I → F in ECTD10B. 1 Publication1
Natural variantiVAR_054451413T → P in ECTD10B. 1 Publication1
Natural variantiVAR_054452418I → T in ECTD10B. 1 Publication1
Natural variantiVAR_013450420R → Q in ECTD10A and ECTD10B; abolishes NF-kappa-B activation and reduces JNK activation. 5 PublicationsCorresponds to variant rs121908453dbSNPEnsembl.1
Natural variantiVAR_054453434W → C in ECTD10B. 1 PublicationCorresponds to variant rs528478080dbSNPEnsembl.1
Natural variantiVAR_064834434W → R in ECTD10B. 1 PublicationCorresponds to variant rs773885029dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_054187219A → GDGPHAPVPCFLDSPSTPPV GEPGCSLPPLSPA in isoform 2. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF130988 mRNA. Translation: AAD50076.1.
AF130996
, AF130990, AF130991, AF130992, AF130993, AF130994, AF130995 Genomic DNA. Translation: AAD50077.1.
AK296936 mRNA. Translation: BAG59487.1.
AK313781 mRNA. Translation: BAG36519.1.
AC073415 Genomic DNA. No translation available.
AC092160 Genomic DNA. No translation available.
AC133784 Genomic DNA. No translation available.
CH471182 Genomic DNA. Translation: EAW53869.1.
BC093870 mRNA. Translation: AAH93870.1.
BC093872 mRNA. Translation: AAH93872.1.
CCDSiCCDS2081.1. [Q9UNE0-1]
RefSeqiNP_071731.1. NM_022336.3. [Q9UNE0-1]
XP_006712267.1. XM_006712204.1. [Q9UNE0-2]
UniGeneiHs.171971.

Genome annotation databases

EnsembliENST00000258443; ENSP00000258443; ENSG00000135960. [Q9UNE0-1]
ENST00000376651; ENSP00000365839; ENSG00000135960. [Q9UNE0-2]
ENST00000409271; ENSP00000386371; ENSG00000135960. [Q9UNE0-2]
GeneIDi10913.
KEGGihsa:10913.
UCSCiuc002teq.4. human. [Q9UNE0-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF130988 mRNA. Translation: AAD50076.1.
AF130996
, AF130990, AF130991, AF130992, AF130993, AF130994, AF130995 Genomic DNA. Translation: AAD50077.1.
AK296936 mRNA. Translation: BAG59487.1.
AK313781 mRNA. Translation: BAG36519.1.
AC073415 Genomic DNA. No translation available.
AC092160 Genomic DNA. No translation available.
AC133784 Genomic DNA. No translation available.
CH471182 Genomic DNA. Translation: EAW53869.1.
BC093870 mRNA. Translation: AAH93870.1.
BC093872 mRNA. Translation: AAH93872.1.
CCDSiCCDS2081.1. [Q9UNE0-1]
RefSeqiNP_071731.1. NM_022336.3. [Q9UNE0-1]
XP_006712267.1. XM_006712204.1. [Q9UNE0-2]
UniGeneiHs.171971.

3D structure databases

ProteinModelPortaliQ9UNE0.
SMRiQ9UNE0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116118. 7 interactors.
IntActiQ9UNE0. 6 interactors.
STRINGi9606.ENSP00000258443.

Chemistry databases

ChEMBLiCHEMBL1250376.

PTM databases

iPTMnetiQ9UNE0.
PhosphoSitePlusiQ9UNE0.

Polymorphism and mutation databases

BioMutaiEDAR.
DMDMi21263572.

Proteomic databases

PaxDbiQ9UNE0.
PeptideAtlasiQ9UNE0.
PRIDEiQ9UNE0.

Protocols and materials databases

DNASUi10913.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000258443; ENSP00000258443; ENSG00000135960. [Q9UNE0-1]
ENST00000376651; ENSP00000365839; ENSG00000135960. [Q9UNE0-2]
ENST00000409271; ENSP00000386371; ENSG00000135960. [Q9UNE0-2]
GeneIDi10913.
KEGGihsa:10913.
UCSCiuc002teq.4. human. [Q9UNE0-1]

Organism-specific databases

CTDi10913.
DisGeNETi10913.
GeneCardsiEDAR.
GeneReviewsiEDAR.
HGNCiHGNC:2895. EDAR.
HPAiHPA042292.
MalaCardsiEDAR.
MIMi129490. phenotype.
224900. phenotype.
604095. gene.
612630. phenotype.
neXtProtiNX_Q9UNE0.
OpenTargetsiENSG00000135960.
Orphaneti1810. Autosomal dominant hypohidrotic ectodermal dysplasia.
248. Autosomal recessive hypohidrotic ectodermal dysplasia.
PharmGKBiPA27602.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IGTD. Eukaryota.
ENOG41104RU. LUCA.
GeneTreeiENSGT00730000111254.
HOGENOMiHOG000112327.
HOVERGENiHBG031530.
InParanoidiQ9UNE0.
KOiK05162.
OMAiPNTKECV.
OrthoDBiEOG091G0ADI.
PhylomeDBiQ9UNE0.
TreeFamiTF331385.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000135960-MONOMER.
ReactomeiR-HSA-5669034. TNFs bind their physiological receptors.
SIGNORiQ9UNE0.

Miscellaneous databases

GeneWikiiEDAR.
GenomeRNAii10913.
PROiQ9UNE0.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000135960.
CleanExiHS_EDAR.
GenevisibleiQ9UNE0. HS.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
InterProiIPR011029. DEATH-like_dom.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiEDAR_HUMAN
AccessioniPrimary (citable) accession number: Q9UNE0
Secondary accession number(s): B2R9H2
, B4DLC5, D3DX74, E9PC98, Q52LL5, Q9UND9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: May 1, 2000
Last modified: November 2, 2016
This is version 139 of the entry and version 1 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.