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Reviewed, UniProtKB/Swiss-Prot Q9HAV5 (TNR27_HUMAN)

Last modified January 19, 2010. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Tumor necrosis factor receptor superfamily member 27
Alternative name(s):
    X-linked ectodysplasin-A2 receptor
      Short name=EDA-A2 receptor
Gene names
Name: EDA2R
Synonyms: TNFRSF27, XEDAR
ORF Names: UNQ2448/PRO5727/PRO34080
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length297 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

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. Ref.2

Subunit structure

Associates with TRAF1, TRAF3 and TRAF6.

Subcellular location

Membrane; Single-pass type III membrane protein.

Sequence similarities

Contains 3 TNFR-Cys repeats.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9HAV5-1)

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.
Isoform 2 (identifier: Q9HAV5-2)

Also known as: Long;

The sequence of this isoform differs from the canonical sequence as follows:
     172-172: R → REKLIIFSDPVPASLNLIPEFA
Isoform 3 (identifier: Q9HAV5-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 297297Tumor necrosis factor receptor superfamily member 27
PRO_0000058938

Regions

Topological domain1 – 138138Extracellular Potential
Transmembrane139 – 15921Signal-anchor for type III membrane protein Potential
Topological domain160 – 297138Cytoplasmic Potential
Repeat2 – 4140TNFR-Cys 1
Repeat43 – 8341TNFR-Cys 2
Repeat85 – 11834TNFR-Cys 3

Amino acid modifications

Glycosylation741N-linked (GlcNAc...) Potential
Disulfide bond3 ↔ 15 By similarity
Disulfide bond18 ↔ 31 By similarity
Disulfide bond21 ↔ 41 By similarity
Disulfide bond44 ↔ 58 By similarity
Disulfide bond61 ↔ 75 By similarity
Disulfide bond64 ↔ 83 By similarity
Disulfide bond86 ↔ 104 By similarity
Disulfide bond107 ↔ 118 By similarity

Natural variations

Alternative sequence1721R → REKLIIFSDPVPASLNLIPE FA in isoform 2.
VSP_011568
Alternative sequence1721R → RVT in isoform 3.
VSP_011569
Natural variant571R → K: dbSNP rs1385699.
VAR_044511
Natural variant1291A → T: dbSNP rs1385698. Ref.4
VAR_044512

Experimental info

Mutagenesis2561E → R: Abolishes TRAF6 association. Ref.1
Sequence conflict2361M → V in AAN73210. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 0E71127C6C48240C

FASTA29732,729
        10         20         30         40         50         60 
MDCQENEYWD QWGRCVTCQR CGPGQELSKD CGYGEGGDAY CTACPPRRYK SSWGHHRCQS 

        70         80         90        100        110        120 
CITCAVINRV QKVNCTATSN AVCGDCLPRF YRKTRIGGLQ DQECIPCTKQ TPTSEVQCAF 

       130        140        150        160        170        180 
QLSLVEADAP TVPPQEATLV ALVSSLLVVF TLAFLGLFFL YCKQFFNRHC QRGGLLQFEA 

       190        200        210        220        230        240 
DKTAKEESLF PVPPSKETSA ESQVSENIFQ TQPLNPILED DCSSTSGFPT QESFTMASCT 

       250        260        270        280        290 
SESHSHWVHS PIECTELDLQ KFSSSASYTG AETLGGNTVE STGDRLELNV PFEVPSP 

« Hide

Isoform 2 (Long).

Checksum: B08CFED32F2F713E
Show »

FASTA31835,024
Isoform 3.

Checksum: 13589F4DC59C30D3
Show »

FASTA29932,929

References

« Hide 'large scale' references
[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: 11039935] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF GLU-256.
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: 12270937] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION.
[3]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed: 12975309] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
[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. expand/collapse author list , 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: 15772651] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT THR-129.
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF298812 mRNA. Translation: AAG28761.1.
AY152724 mRNA. Translation: AAN73210.1.
AY358736 mRNA. Translation: AAQ89953.1.
AY358735 mRNA. Translation: AAQ89952.1.
AL353136 Genomic DNA. Translation: CAH70433.1.
AL353136 Genomic DNA. Translation: CAH70434.1.
BC034919 mRNA. Translation: AAH34919.1.
IPIIPI00029116.
IPI00456756.
IPI00456757.
RefSeqNP_068555.1.
UniGeneHs.302017

3D structure databases

SMRQ9HAV5. Positions 6-110.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9HAV5. 5 interactions.
STRINGQ9HAV5.

Proteomic databases

PRIDEQ9HAV5.

Genome annotation databases

EnsemblENST00000374719; ENSP00000363851; ENSG00000131080; Homo sapiens. [Genome view]
ENST00000396050; ENSP00000379365; ENSG00000131080; Homo sapiens. [Genome view]
GeneID60401.
KEGGhsa:60401.
UCSCuc004dwq.1. human.

Organism-specific databases

CTD60401.
GeneCardsGC0XM065732.
H-InvDBHIX0028343.
HGNCHGNC:17756. EDA2R.
HPACAB015945.
MIM300276. gene.
PharmGKBPA134974675.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG08803.
HOVERGENQ9HAV5.

Gene expression databases

ArrayExpressQ9HAV5.
BgeeQ9HAV5.
CleanExHS_EDA2R.
GenevestigatorQ9HAV5.
GermOnlineENSG00000131080. Homo sapiens.

Family and domain databases

InterProIPR001368. TNFR_Cys_rich_reg.
[Graphical view]
PfamPF00020. TNFR_c6. 2 hits.
[Graphical view]
SMARTSM00208. TNFR. 2 hits.
[Graphical view]
PROSITEPS00652. TNFR_NGFR_1. 2 hits.
PS50050. TNFR_NGFR_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio65314.
SOURCESearch...

Entry information

Entry nameTNR27_HUMAN
AccessionPrimary (citable) accession number: Q9HAV5
Secondary accession number(s): Q5VYX9 expand/collapse secondary AC list , Q5VYY0, Q6UWM2, Q8IZA6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: March 1, 2001
Last modified: January 19, 2010
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

Relevant documents

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents