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Q9UNE0

- EDAR_HUMAN

UniProt

Q9UNE0 - EDAR_HUMAN

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Protein

Tumor necrosis factor receptor superfamily member EDAR

Gene
EDAR, DL
Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. protein binding Source: HGNC
  2. receptor activity Source: HGNC
  3. transmembrane signaling receptor activity Source: UniProtKB

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. cell differentiation Source: UniProtKB-KW
  3. epidermis development Source: HGNC
  4. hair follicle development Source: Ensembl
  5. odontogenesis of dentin-containing tooth Source: Ensembl
  6. pigmentation Source: Ensembl
  7. positive regulation of NF-kappaB import into nucleus Source: Ensembl
  8. salivary gland cavitation Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Receptor

Keywords - Biological processi

Apoptosis, Differentiation

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
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:2895. EDAR.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini27 – 187161Extracellular Reviewed predictionAdd
BLAST
Transmembranei188 – 20821Helical; Reviewed predictionAdd
BLAST
Topological domaini209 – 448240Cytoplasmic Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. apical part of cell Source: Ensembl
  2. integral component of membrane Source: UniProtKB
  3. plasma membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

Ectodermal dysplasia 10A, hypohidrotic/hair/nail type, autosomal dominant (ECTD10A) [MIM:129490]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti420 – 4201R → Q in ECTD10A and ECTD10B; abolishes NF-kappa-B activation and reduces JNK activation. 5 Publications
VAR_013450
Ectodermal dysplasia 10B, hypohidrotic/hair/tooth type, autosomal recessive (ECTD10B) [MIM:224900]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.7 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti47 – 471C → Y in ECTD10B. 1 Publication
VAR_054444
Natural varianti87 – 871C → R in ECTD10B. 1 Publication
VAR_013448
Natural varianti89 – 891R → H in ECTD10B. 4 Publications
VAR_013449
Natural varianti98 – 981R → Q in ECTD10B. 1 Publication
VAR_064830
Natural varianti110 – 1101D → A in ECTD10B. 2 Publications
VAR_054445
Natural varianti148 – 1481C → R in ECTD10B. 1 Publication
VAR_054446
Natural varianti358 – 3581R → Q in ECTD10B. 2 Publications
VAR_064831
Natural varianti375 – 3751R → H in ECTD10B; the mutant protein does not interact with EDARADD and is functionally inactive. 1 Publication
VAR_054447
Natural varianti377 – 3771L → F in ECTD10B. 1 Publication
VAR_054448
Natural varianti382 – 3821G → S in ECTD10B. 1 Publication
VAR_054449
Natural varianti396 – 3961Q → QQ in ECTD10B. 1 Publication
VAR_064832
Natural varianti403 – 4031T → M in ECTD10B. 2 Publications
VAR_054450
Natural varianti408 – 4081I → F in ECTD10B. 1 Publication
VAR_064833
Natural varianti413 – 4131T → P in ECTD10B. 1 Publication
VAR_054451
Natural varianti418 – 4181I → T in ECTD10B. 1 Publication
VAR_054452
Natural varianti420 – 4201R → Q in ECTD10A and ECTD10B; abolishes NF-kappa-B activation and reduces JNK activation. 5 Publications
VAR_013450
Natural varianti434 – 4341W → C in ECTD10B. 1 Publication
VAR_054453
Natural varianti434 – 4341W → R in ECTD10B. 1 Publication
VAR_064834

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi379 – 3791E → K: Reduces activation of NF-kappa-B. 1 Publication

Keywords - Diseasei

Disease mutation, Ectodermal dysplasia

Organism-specific databases

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 26261 PublicationAdd
BLAST
Chaini27 – 448422Tumor necrosis factor receptor superfamily member EDARPRO_0000034608Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi31 ↔ 44 By similarity
Glycosylationi38 – 381N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi47 ↔ 60 By similarity
Disulfide bondi50 ↔ 71 By similarity
Disulfide bondi74 ↔ 87 By similarity
Disulfide bondi93 ↔ 113 By similarity
Disulfide bondi135 ↔ 148 By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9UNE0.
PRIDEiQ9UNE0.

PTM databases

PhosphoSiteiQ9UNE0.

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

ArrayExpressiQ9UNE0.
BgeeiQ9UNE0.
CleanExiHS_EDAR.
GenevestigatoriQ9UNE0.

Organism-specific databases

HPAiHPA042292.

Interactioni

Subunit structurei

Binds to EDARADD. Associates with TRAF1, TRAF2, TRAF3 and NIK.2 Publications

Protein-protein interaction databases

BioGridi116118. 7 interactions.
IntActiQ9UNE0. 6 interactions.
STRINGi9606.ENSP00000258443.

Structurei

3D structure databases

ProteinModelPortaliQ9UNE0.
SMRiQ9UNE0. Positions 21-168, 346-436.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati30 – 7142TNFR-Cys 1Add
BLAST
Repeati73 – 11341TNFR-Cys 2Add
BLAST
Repeati115 – 14834TNFR-Cys 3Add
BLAST
Domaini358 – 43174DeathAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG43402.
HOGENOMiHOG000112327.
HOVERGENiHBG031530.
KOiK05162.
OMAiKECVGAT.
OrthoDBiEOG780RMB.
PhylomeDBiQ9UNE0.
TreeFamiTF331385.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
InterProiIPR011029. DEATH-like_dom.
IPR000488. Death_domain.
[Graphical view]
PfamiPF00531. Death. 1 hit.
[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. Align

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

MAHVGDCTQT PWLPVLVVSL MCSARAEYSN CGENEYYNQT TGLCQECPPC    50
GPGEEPYLSC GYGTKDEDYG CVPCPAEKFS KGGYQICRRH KDCEGFFRAT 100
VLTPGDMEND AECGPCLPGY YMLENRPRNI YGMVCYSCLL APPNTKECVG 150
ATSGASANFP GTSGSSTLSP FQHAHKELSG QGHLATALII AMSTIFIMAI 200
AIVLIIMFYI LKTKPSAPAC CTSHPGKSVE AQVSKDEEKK EAPDNVVMFS 250
EKDEFEKLTA TPAKPTKSEN DASSENEQLL SRSVDSDEEP APDKQGSPEL 300
CLLSLVHLAR EKSATSNKSA GIQSRRKKIL DVYANVCGVV EGLSPTELPF 350
DCLEKTSRML SSTYNSEKAV VKTWRHLAES FGLKRDEIGG MTDGMQLFDR 400
ISTAGYSIPE LLTKLVQIER LDAVESLCAD ILEWAGVVPP ASQPHAAS 448
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.

Show »
Length:480
Mass (Da):51,690
Checksum:i4262977A6EAE8D2A
GO

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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti47 – 471C → Y in ECTD10B. 1 Publication
VAR_054444
Natural varianti87 – 871C → R in ECTD10B. 1 Publication
VAR_013448
Natural varianti89 – 891R → H in ECTD10B. 4 Publications
VAR_013449
Natural varianti98 – 981R → Q in ECTD10B. 1 Publication
VAR_064830
Natural varianti110 – 1101D → A in ECTD10B. 2 Publications
VAR_054445
Natural varianti148 – 1481C → R in ECTD10B. 1 Publication
VAR_054446
Natural varianti358 – 3581R → Q in ECTD10B. 2 Publications
VAR_064831
Natural varianti370 – 3701V → A Associated with increase in hair thickness; results in decreased downstream activity of NFKB1 48 hours after transfection into cells. 3 Publications
Corresponds to variant rs3827760 [ dbSNP | Ensembl ].
VAR_020011
Natural varianti375 – 3751R → H in ECTD10B; the mutant protein does not interact with EDARADD and is functionally inactive. 1 Publication
VAR_054447
Natural varianti377 – 3771L → F in ECTD10B. 1 Publication
VAR_054448
Natural varianti382 – 3821G → S in ECTD10B. 1 Publication
VAR_054449
Natural varianti396 – 3961Q → QQ in ECTD10B. 1 Publication
VAR_064832
Natural varianti403 – 4031T → M in ECTD10B. 2 Publications
VAR_054450
Natural varianti408 – 4081I → F in ECTD10B. 1 Publication
VAR_064833
Natural varianti413 – 4131T → P in ECTD10B. 1 Publication
VAR_054451
Natural varianti418 – 4181I → T in ECTD10B. 1 Publication
VAR_054452
Natural varianti420 – 4201R → Q in ECTD10A and ECTD10B; abolishes NF-kappa-B activation and reduces JNK activation. 5 Publications
VAR_013450
Natural varianti434 – 4341W → C in ECTD10B. 1 Publication
VAR_054453
Natural varianti434 – 4341W → R in ECTD10B. 1 Publication
VAR_064834

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei219 – 2191A → GDGPHAPVPCFLDSPSTPPV GEPGCSLPPLSPA in isoform 2. VSP_054187

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti156 – 1561S → P in BAG36519. 1 Publication
Sequence conflicti262 – 2621P → S in AAD50077. 1 Publication
Isoform 2 (identifier: Q9UNE0-2)
Sequence conflicti229 – 2291F → L in BAG59487. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
ENST00000376651; ENSP00000365839; ENSG00000135960.
GeneIDi10913.
KEGGihsa:10913.
UCSCiuc002teq.4. human. [Q9UNE0-1]

Polymorphism databases

DMDMi21263572.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS2081.1. [Q9UNE0-1 ]
RefSeqi NP_071731.1. NM_022336.3. [Q9UNE0-1 ]
XP_006712267.1. XM_006712204.1. [Q9UNE0-2 ]
UniGenei Hs.171971.

3D structure databases

ProteinModelPortali Q9UNE0.
SMRi Q9UNE0. Positions 21-168, 346-436.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116118. 7 interactions.
IntActi Q9UNE0. 6 interactions.
STRINGi 9606.ENSP00000258443.

Chemistry

ChEMBLi CHEMBL1250376.
GuidetoPHARMACOLOGYi 2325.

PTM databases

PhosphoSitei Q9UNE0.

Polymorphism databases

DMDMi 21263572.

Proteomic databases

PaxDbi Q9UNE0.
PRIDEi Q9UNE0.

Protocols and materials databases

DNASUi 10913.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000258443 ; ENSP00000258443 ; ENSG00000135960 .
ENST00000376651 ; ENSP00000365839 ; ENSG00000135960 .
GeneIDi 10913.
KEGGi hsa:10913.
UCSCi uc002teq.4. human. [Q9UNE0-1 ]

Organism-specific databases

CTDi 10913.
GeneCardsi GC02M109510.
GeneReviewsi EDAR.
HGNCi HGNC:2895. EDAR.
HPAi HPA042292.
MIMi 129490. phenotype.
224900. phenotype.
604095. gene.
612630. phenotype.
neXtProti NX_Q9UNE0.
Orphaneti 1810. Autosomal dominant hypohidrotic ectodermal dysplasia.
248. Autosomal recessive hypohidrotic ectodermal dysplasia.
PharmGKBi PA27602.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG43402.
HOGENOMi HOG000112327.
HOVERGENi HBG031530.
KOi K05162.
OMAi KECVGAT.
OrthoDBi EOG780RMB.
PhylomeDBi Q9UNE0.
TreeFami TF331385.

Miscellaneous databases

GeneWikii EDAR.
GenomeRNAii 10913.
NextBioi 35467882.
PROi Q9UNE0.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9UNE0.
Bgeei Q9UNE0.
CleanExi HS_EDAR.
Genevestigatori Q9UNE0.

Family and domain databases

Gene3Di 1.10.533.10. 1 hit.
InterProi IPR011029. DEATH-like_dom.
IPR000488. Death_domain.
[Graphical view ]
Pfami PF00531. Death. 1 hit.
[Graphical view ]
SUPFAMi SSF47986. SSF47986. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Mutations in the human homologue of mouse dl cause autosomal recessive and dominant hypohidrotic ectodermal dysplasia."
    Monreal A.W., Ferguson B.M., Headon D.J., Street S.L., Overbeek P.A., Zonana J.
    Nat. Genet. 22:366-369(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), VARIANTS ECTD10B ARG-87 AND HIS-89, VARIANT ECTD10A GLN-420.
    Tissue: Fetal heart and Skin.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANT ALA-370.
    Tissue: Tongue.
  3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. 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] (ISOFORM 1).
    Tissue: Liver.
  6. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
    Zhang Z., Henzel W.J.
    Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-41.
  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: INTERACTION WITH EDA ISOFORM A1.
  8. "The ectodermal dysplasia receptor activates the nuclear factor-kappaB, JNK, and cell death pathways and binds to ectodysplasin A."
    Kumar A., Eby M.T., Sinha S., Jasmin A., Chaudhary P.M.
    J. Biol. Chem. 276:2668-2677(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANT GLN-420, MUTAGENESIS OF GLU-379, CHARACTERIZATION, INTERACTION WITH TRAF1 AND TRAF3.
  9. "A rare case of hypohidrotic ectodermal dysplasia caused by compound heterozygous mutations in the EDAR gene."
    Shimomura Y., Sato N., Miyashita A., Hashimoto T., Ito M., Kuwano R.
    J. Invest. Dermatol. 123:649-655(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ECTD10B HIS-375, CHARACTERIZATION OF VARIANT ECTD10B HIS-375.
  10. "Novel mutations in the EDAR gene in two Pakistani consanguineous families with autosomal recessive hypohidrotic ectodermal dysplasia."
    Naeem M., Muhammad D., Ahmad W.
    Br. J. Dermatol. 153:46-50(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ECTD10B SER-382.
  11. "Mutations in EDAR account for one-quarter of non-ED1-related hypohidrotic ectodermal dysplasia."
    Chassaing N., Bourthoumieu S., Cossee M., Calvas P., Vincent M.-C.
    Hum. Mutat. 27:255-259(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS ECTD10B TYR-47; HIS-89; ALA-110; ARG-148; PHE-377; MET-403; PRO-413; THR-418; GLN-420 AND CYS-434.
  12. "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 ECTD10B HIS-89 AND ALA-110, VARIANT ECTD10A GLN-420.
  13. Cited for: VARIANT ALA-370, CHARACTERIZATION OF VARIANT ALA-370, ASSOCIATION WITH HAIR MORPHOLOGY TYPE 1.
  14. "Enhanced ectodysplasin-A receptor (EDAR) signaling alters multiple fiber characteristics to produce the East Asian hair form."
    Mou C., Thomason H.A., Willan P.M., Clowes C., Harris W.E., Drew C.F., Dixon J., Dixon M.J., Headon D.J.
    Hum. Mutat. 29:1405-1411(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANT ALA-370.
  15. "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 ECTD10B GLN-98; GLN-358 AND ARG-434.
  16. Cited for: VARIANTS ECTD10B HIS-89; GLN-358; GLN-396 INS; MET-403; PHE-408 AND GLN-420.

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: September 3, 2014
This is version 120 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

External Data

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