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Protein

Tumor necrosis factor receptor superfamily member 27

Gene

EDA2R

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

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

  • receptor activity Source: HGNC
  • tumor necrosis factor-activated receptor activity Source: UniProtKB

GO - Biological processi

  • ectodermal cell differentiation Source: BHF-UCL
  • epidermis development Source: UniProtKB
  • intrinsic apoptotic signaling pathway by p53 class mediator Source: Ensembl
  • multicellular organismal development Source: UniProtKB-KW
  • positive regulation of JNK cascade Source: HGNC
  • positive regulation of NF-kappaB transcription factor activity Source: HGNC
  • tumor necrosis factor-mediated signaling pathway Source: GOC
Complete GO annotation...

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 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:17756. EDA2R.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 138138ExtracellularSequence AnalysisAdd
BLAST
Transmembranei139 – 15921Helical; Signal-anchor for type III membrane proteinSequence AnalysisAdd
BLAST
Topological domaini160 – 297138CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: HGNC
  • integral component of plasma membrane Source: InterPro
  • intracellular Source: GOC
Complete GO annotation...

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.

Polymorphism and mutation databases

BioMutaiEDA2R.
DMDMi313104030.

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

BgeeiQ9HAV5.
CleanExiHS_EDA2R.
GenevisibleiQ9HAV5. HS.

Organism-specific databases

HPAiCAB015945.

Interactioni

Subunit structurei

Associates with TRAF1, TRAF3 and TRAF6.

Protein-protein interaction databases

BioGridi121904. 12 interactions.
IntActiQ9HAV5. 8 interactions.
STRINGi9606.ENSP00000253392.

Structurei

3D structure databases

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

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.
GeneTreeiENSGT00730000110978.
HOGENOMiHOG000132464.
HOVERGENiHBG059312.
InParanoidiQ9HAV5.
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. AlignAdd to basket

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

        10         20         30         40         50
MDCQENEYWD QWGRCVTCQR CGPGQELSKD CGYGEGGDAY CTACPPRRYK
60 70 80 90 100
SSWGHHRCQS CITCAVINRV QKVNCTATSN AVCGDCLPRF YRKTRIGGLQ
110 120 130 140 150
DQECIPCTKQ TPTSEVQCAF QLSLVEADTP TVPPQEATLV ALVSSLLVVF
160 170 180 190 200
TLAFLGLFFL YCKQFFNRHC QRGGLLQFEA DKTAKEESLF PVPPSKETSA
210 220 230 240 250
ESQVSENIFQ TQPLNPILED DCSSTSGFPT QESFTMASCT SESHSHWVHS
260 270 280 290
PIECTELDLQ KFSSSASYTG AETLGGNTVE STGDRLELNV PFEVPSP
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:
EMBLi
GenBanki
DDBJi
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. [Q9HAV5-2]
ENST00000451436; ENSP00000415242; ENSG00000131080. [Q9HAV5-1]
GeneIDi60401.
KEGGihsa:60401.
UCSCiuc004dwq.3. human. [Q9HAV5-1]
uc004dwt.2. human. [Q9HAV5-2]
uc022byh.1. human. [Q9HAV5-3]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi121904. 12 interactions.
IntActiQ9HAV5. 8 interactions.
STRINGi9606.ENSP00000253392.

Chemistry

GuidetoPHARMACOLOGYi1896.

PTM databases

PhosphoSiteiQ9HAV5.

Polymorphism and mutation databases

BioMutaiEDA2R.
DMDMi313104030.

Proteomic databases

PaxDbiQ9HAV5.
PRIDEiQ9HAV5.

Protocols and materials databases

DNASUi60401.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000253392; ENSP00000253392; ENSG00000131080. [Q9HAV5-2]
ENST00000374719; ENSP00000363851; ENSG00000131080. [Q9HAV5-1]
ENST00000396050; ENSP00000379365; ENSG00000131080. [Q9HAV5-2]
ENST00000451436; ENSP00000415242; ENSG00000131080. [Q9HAV5-1]
GeneIDi60401.
KEGGihsa:60401.
UCSCiuc004dwq.3. human. [Q9HAV5-1]
uc004dwt.2. human. [Q9HAV5-2]
uc022byh.1. human. [Q9HAV5-3]

Organism-specific databases

CTDi60401.
GeneCardsiGC0XM065732.
HGNCiHGNC:17756. EDA2R.
HPAiCAB015945.
MIMi300276. gene.
neXtProtiNX_Q9HAV5.
Orphaneti181. X-linked hypohidrotic ectodermal dysplasia.
PharmGKBiPA134974675.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG28936.
GeneTreeiENSGT00730000110978.
HOGENOMiHOG000132464.
HOVERGENiHBG059312.
InParanoidiQ9HAV5.
KOiK05163.
OMAiSFTMASC.
OrthoDBiEOG7Z3F4G.
PhylomeDBiQ9HAV5.
TreeFamiTF331385.

Enzyme and pathway databases

SignaLinkiQ9HAV5.

Miscellaneous databases

GeneWikiiEctodysplasin_A2_receptor.
GenomeRNAii60401.
NextBioi65314.
PROiQ9HAV5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9HAV5.
CleanExiHS_EDA2R.
GenevisibleiQ9HAV5. HS.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: June 24, 2015
This is version 119 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

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 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.