Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9HAV5

- TNR27_HUMAN

UniProt

Q9HAV5 - TNR27_HUMAN

Protein

Tumor necrosis factor receptor superfamily member 27

Gene

EDA2R

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 2 (30 Nov 2010)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Receptor for EDA isoform A2, but not for EDA isoform A1. Mediates the activation of the NF-kappa-B and JNK pathways. Activation seems to be mediated by binding to TRAF3 and TRAF6.1 Publication

    GO - Molecular functioni

    1. protein binding Source: HGNC
    2. receptor activity Source: HGNC
    3. tumor necrosis factor-activated receptor activity Source: UniProtKB

    GO - Biological processi

    1. cell differentiation Source: UniProtKB-KW
    2. embryo development Source: HGNC
    3. epidermis development Source: UniProtKB
    4. positive regulation of JNK cascade Source: HGNC
    5. positive regulation of NF-kappaB transcription factor activity Source: HGNC
    6. tumor necrosis factor-mediated signaling pathway Source: GOC

    Keywords - Molecular functioni

    Developmental protein, Receptor

    Keywords - Biological processi

    Differentiation

    Enzyme and pathway databases

    SignaLinkiQ9HAV5.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tumor necrosis factor receptor superfamily member 27
    Alternative name(s):
    X-linked ectodysplasin-A2 receptor
    Short name:
    EDA-A2 receptor
    Gene namesi
    Name:EDA2R
    Synonyms:TNFRSF27, XEDAR
    ORF Names:UNQ2448/PRO5727/PRO34080
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:17756. EDA2R.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: HGNC
    2. integral component of plasma membrane Source: InterPro

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi256 – 2561E → R: Abolishes TRAF6 association. 1 Publication

    Organism-specific databases

    Orphaneti181. X-linked hypohidrotic ectodermal dysplasia.
    PharmGKBiPA134974675.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 297297Tumor necrosis factor receptor superfamily member 27PRO_0000058938Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi3 ↔ 15PROSITE-ProRule annotation
    Disulfide bondi18 ↔ 31PROSITE-ProRule annotation
    Disulfide bondi21 ↔ 41PROSITE-ProRule annotation
    Disulfide bondi44 ↔ 58PROSITE-ProRule annotation
    Disulfide bondi61 ↔ 75PROSITE-ProRule annotation
    Disulfide bondi64 ↔ 83PROSITE-ProRule annotation
    Glycosylationi74 – 741N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi86 ↔ 104PROSITE-ProRule annotation
    Disulfide bondi107 ↔ 118PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ9HAV5.
    PRIDEiQ9HAV5.

    PTM databases

    PhosphoSiteiQ9HAV5.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9HAV5.
    BgeeiQ9HAV5.
    CleanExiHS_EDA2R.
    GenevestigatoriQ9HAV5.

    Organism-specific databases

    HPAiCAB015945.

    Interactioni

    Subunit structurei

    Associates with TRAF1, TRAF3 and TRAF6.

    Protein-protein interaction databases

    BioGridi121904. 5 interactions.
    IntActiQ9HAV5. 8 interactions.
    STRINGi9606.ENSP00000363851.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9HAV5.
    SMRiQ9HAV5. Positions 2-93.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 138138ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini160 – 297138CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei139 – 15921Helical; Signal-anchor for type III membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati2 – 4140TNFR-Cys 1Add
    BLAST
    Repeati43 – 8341TNFR-Cys 2Add
    BLAST
    Repeati85 – 11834TNFR-Cys 3Add
    BLAST

    Sequence similaritiesi

    Contains 3 TNFR-Cys repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG28936.
    HOGENOMiHOG000132464.
    HOVERGENiHBG059312.
    KOiK05163.
    OMAiSFTMASC.
    OrthoDBiEOG7Z3F4G.
    PhylomeDBiQ9HAV5.
    TreeFamiTF331385.

    Family and domain databases

    InterProiIPR001368. TNFR/NGFR_Cys_rich_reg.
    IPR022319. TNFR_27.
    [Graphical view]
    PfamiPF00020. TNFR_c6. 2 hits.
    [Graphical view]
    PRINTSiPR01973. TNFACTORR27.
    SMARTiSM00208. TNFR. 2 hits.
    [Graphical view]
    PROSITEiPS00652. TNFR_NGFR_1. 2 hits.
    PS50050. TNFR_NGFR_2. 2 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9HAV5-1) [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

    MDCQENEYWD QWGRCVTCQR CGPGQELSKD CGYGEGGDAY CTACPPRRYK    50
    SSWGHHRCQS CITCAVINRV QKVNCTATSN AVCGDCLPRF YRKTRIGGLQ 100
    DQECIPCTKQ TPTSEVQCAF QLSLVEADTP TVPPQEATLV ALVSSLLVVF 150
    TLAFLGLFFL YCKQFFNRHC QRGGLLQFEA DKTAKEESLF PVPPSKETSA 200
    ESQVSENIFQ TQPLNPILED DCSSTSGFPT QESFTMASCT SESHSHWVHS 250
    PIECTELDLQ KFSSSASYTG AETLGGNTVE STGDRLELNV PFEVPSP 297
    Length:297
    Mass (Da):32,759
    Last modified:November 30, 2010 - v2
    Checksum:i05DBB377DC59350C
    GO
    Isoform 2 (identifier: Q9HAV5-2) [UniParc]FASTAAdd to Basket

    Also known as: Long

    The sequence of this isoform differs from the canonical sequence as follows:
         172-172: R → REKLIIFSDPVPASLNLIPEFA

    Show »
    Length:318
    Mass (Da):35,054
    Checksum:iE18193A333561437
    GO
    Isoform 3 (identifier: Q9HAV5-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         172-172: R → RVT

    Show »
    Length:299
    Mass (Da):32,959
    Checksum:i09E894E7649780C2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti236 – 2361M → V in AAN73210. (PubMed:12270937)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti57 – 571R → K.
    Corresponds to variant rs1385699 [ dbSNP | Ensembl ].
    VAR_044511
    Natural varianti129 – 1291T → A.4 Publications
    Corresponds to variant rs1385698 [ dbSNP | Ensembl ].
    VAR_044512

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei172 – 1721R → REKLIIFSDPVPASLNLIPE FA in isoform 2. 1 PublicationVSP_011568
    Alternative sequencei172 – 1721R → RVT in isoform 3. 1 PublicationVSP_011569

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF298812 mRNA. Translation: AAG28761.1.
    AY152724 mRNA. Translation: AAN73210.1.
    AY358735 mRNA. Translation: AAQ89952.1.
    AY358736 mRNA. Translation: AAQ89953.1.
    AL353136 Genomic DNA. Translation: CAH70433.1.
    AL353136 Genomic DNA. Translation: CAH70434.1.
    BC034919 mRNA. Translation: AAH34919.1.
    CCDSiCCDS14386.1. [Q9HAV5-1]
    CCDS56603.1. [Q9HAV5-2]
    RefSeqiNP_001186616.1. NM_001199687.2.
    NP_001229239.1. NM_001242310.1.
    NP_068555.1. NM_021783.3.
    UniGeneiHs.302017.

    Genome annotation databases

    EnsembliENST00000253392; ENSP00000253392; ENSG00000131080. [Q9HAV5-2]
    ENST00000374719; ENSP00000363851; ENSG00000131080. [Q9HAV5-1]
    ENST00000396050; ENSP00000379365; ENSG00000131080. [Q9HAV5-1]
    GeneIDi60401.
    KEGGihsa:60401.
    UCSCiuc004dwq.3. human. [Q9HAV5-1]
    uc004dwt.2. human. [Q9HAV5-2]
    uc022byh.1. human. [Q9HAV5-3]

    Polymorphism databases

    DMDMi313104030.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF298812 mRNA. Translation: AAG28761.1 .
    AY152724 mRNA. Translation: AAN73210.1 .
    AY358735 mRNA. Translation: AAQ89952.1 .
    AY358736 mRNA. Translation: AAQ89953.1 .
    AL353136 Genomic DNA. Translation: CAH70433.1 .
    AL353136 Genomic DNA. Translation: CAH70434.1 .
    BC034919 mRNA. Translation: AAH34919.1 .
    CCDSi CCDS14386.1. [Q9HAV5-1 ]
    CCDS56603.1. [Q9HAV5-2 ]
    RefSeqi NP_001186616.1. NM_001199687.2.
    NP_001229239.1. NM_001242310.1.
    NP_068555.1. NM_021783.3.
    UniGenei Hs.302017.

    3D structure databases

    ProteinModelPortali Q9HAV5.
    SMRi Q9HAV5. Positions 2-93.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121904. 5 interactions.
    IntActi Q9HAV5. 8 interactions.
    STRINGi 9606.ENSP00000363851.

    Chemistry

    GuidetoPHARMACOLOGYi 1896.

    PTM databases

    PhosphoSitei Q9HAV5.

    Polymorphism databases

    DMDMi 313104030.

    Proteomic databases

    PaxDbi Q9HAV5.
    PRIDEi Q9HAV5.

    Protocols and materials databases

    DNASUi 60401.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000253392 ; ENSP00000253392 ; ENSG00000131080 . [Q9HAV5-2 ]
    ENST00000374719 ; ENSP00000363851 ; ENSG00000131080 . [Q9HAV5-1 ]
    ENST00000396050 ; ENSP00000379365 ; ENSG00000131080 . [Q9HAV5-1 ]
    GeneIDi 60401.
    KEGGi hsa:60401.
    UCSCi uc004dwq.3. human. [Q9HAV5-1 ]
    uc004dwt.2. human. [Q9HAV5-2 ]
    uc022byh.1. human. [Q9HAV5-3 ]

    Organism-specific databases

    CTDi 60401.
    GeneCardsi GC0XM065732.
    HGNCi HGNC:17756. EDA2R.
    HPAi CAB015945.
    MIMi 300276. gene.
    neXtProti NX_Q9HAV5.
    Orphaneti 181. X-linked hypohidrotic ectodermal dysplasia.
    PharmGKBi PA134974675.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG28936.
    HOGENOMi HOG000132464.
    HOVERGENi HBG059312.
    KOi K05163.
    OMAi SFTMASC.
    OrthoDBi EOG7Z3F4G.
    PhylomeDBi Q9HAV5.
    TreeFami TF331385.

    Enzyme and pathway databases

    SignaLinki Q9HAV5.

    Miscellaneous databases

    GeneWikii Ectodysplasin_A2_receptor.
    GenomeRNAii 60401.
    NextBioi 65314.
    PROi Q9HAV5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9HAV5.
    Bgeei Q9HAV5.
    CleanExi HS_EDA2R.
    Genevestigatori Q9HAV5.

    Family and domain databases

    InterProi IPR001368. TNFR/NGFR_Cys_rich_reg.
    IPR022319. TNFR_27.
    [Graphical view ]
    Pfami PF00020. TNFR_c6. 2 hits.
    [Graphical view ]
    PRINTSi PR01973. TNFACTORR27.
    SMARTi SM00208. TNFR. 2 hits.
    [Graphical view ]
    PROSITEi PS00652. TNFR_NGFR_1. 2 hits.
    PS50050. TNFR_NGFR_2. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF GLU-256, VARIANT ALA-129.
      Tissue: Fetal kidney.
    2. "Role of TRAF3 and -6 in the activation of the NF-kappa B and JNK pathways by X-linked ectodermal dysplasia receptor."
      Sinha S.K., Zachariah S., Quinones H.I., Shindo M., Chaudhary P.M.
      J. Biol. Chem. 277:44953-44961(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, VARIANT ALA-129.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), VARIANT ALA-129.
    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] (ISOFORM 1), VARIANT ALA-129.
      Tissue: Brain.

    Entry informationi

    Entry nameiTNR27_HUMAN
    AccessioniPrimary (citable) accession number: Q9HAV5
    Secondary accession number(s): Q5VYX9
    , Q5VYY0, Q6UWM2, Q8IZA6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 27, 2002
    Last sequence update: November 30, 2010
    Last modified: October 1, 2014
    This is version 114 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

    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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3