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Q9UNE0

- EDAR_HUMAN

UniProt

Q9UNE0 - EDAR_HUMAN

Protein

Tumor necrosis factor receptor superfamily member EDAR

Gene

EDAR

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 121 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    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

    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

    GO - Cellular componenti

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

    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.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti420 – 4201R → Q in ECTD10A and ECTD10B; abolishes NF-kappa-B activation and reduces JNK activation. 4 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.7 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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. 4 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 ↔ 44By similarity
    Glycosylationi38 – 381N-linked (GlcNAc...)Sequence Analysis
    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.
    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.

    Protein-protein interaction databases

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

    Structurei

    3D structure databases

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

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini27 – 187161ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini209 – 448240CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei188 – 20821HelicalSequence AnalysisAdd
    BLAST

    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.Curated
    Contains 3 TNFR-Cys repeats.Curated

    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.Curated

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti156 – 1561S → P in BAG36519. (PubMed:14702039)Curated
    Sequence conflicti262 – 2621P → S in AAD50077. (PubMed:10431241)Curated
    Isoform 2 (identifier: Q9UNE0-2)
    Sequence conflicti229 – 2291F → L in BAG59487. (PubMed:14702039)Curated

    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. 2 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. 4 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. 1 PublicationVSP_054187

    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. [Q9UNE0-1]
    ENST00000376651; ENSP00000365839; ENSG00000135960. [Q9UNE0-2]
    ENST00000409271; ENSP00000386371; ENSG00000135960. [Q9UNE0-2]
    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 . [Q9UNE0-1 ]
    ENST00000376651 ; ENSP00000365839 ; ENSG00000135960 . [Q9UNE0-2 ]
    ENST00000409271 ; ENSP00000386371 ; ENSG00000135960 . [Q9UNE0-2 ]
    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

    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: October 1, 2014
    This is version 121 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

    Dasty 3