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Reviewed, UniProtKB/Swiss-Prot Q15628 (TRADD_HUMAN)

Last modified January 19, 2010. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Tumor necrosis factor receptor type 1-associated DEATH domain protein
      Short name=TNFR1-associated DEATH domain protein
Alternative name(s):
    TNFRSF1A-associated via death domain
Gene names
Name: TRADD
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length312 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Adapter molecule for TNFRSF1A/TNFR1 that specifically associates with the cytoplasmic domain of activated TNFRSF1A/TNFR1 mediating its interaction with FADD. Overexpression of TRADD leads to two major TNF-induced responses, apoptosis and activation of NF-kappa-B.

Subunit structure

Heterodimer with TNFRSF1A/TNFR1. Interacts with DAB2IP, FADD, HIPK2, KRT14, KRT16, KRT17, KRT18, RIPK1, SQSTM1, TRAF1, TRAF2 and TRPC4AP. Ref.9 Ref.10 Ref.11 Ref.12 Ref.13

Subcellular location

Cytoplasmcytoskeleton Ref.12.

Tissue specificity

Found in all examined tissues.

Domain

Requires the intact DEATH domain to associate with TNFRSF1A/TNFR1.

Sequence similarities

Contains 1 death domain.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 312312Tumor necrosis factor receptor type 1-associated DEATH domain protein
PRO_0000065602

Regions

Domain179 – 289111Death
Region222 – 28968Interaction with KRT14 and KRT18
Compositional bias192 – 1987Poly-Pro

Secondary structure

........................ 312
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q15628-1 [UniParc].

Last modified July 15, 1999. Version 2.
Checksum: 5645D7E63E5FF05A

FASTA31234,247
        10         20         30         40         50         60 
MAAGQNGHEE WVGSAYLFVE SSLDKVVLSD AYAHPQQKVA VYRALQAALA ESGGSPDVLQ 

        70         80         90        100        110        120 
MLKIHRSDPQ LIVQLRFCGR QPCGRFLRAY REGALRAALQ RSLAAALAQH SVPLQLELRA 

       130        140        150        160        170        180 
GAERLDALLA DEERCLSCIL AQQPDRLRDE ELAELEDALR NLKCGSGARG GDGEVASAPL 

       190        200        210        220        230        240 
QPPVPSLSEV KPPPPPPPAQ TFLFQGQPVV NRPLSLKDQQ TFARSVGLKW RKVGRSLQRG 

       250        260        270        280        290        300 
CRALRDPALD SLAYEYEREG LYEQAFQLLR RFVQAEGRRA TLQRLVEALE ENELTSLAED 

       310 
LLGLTDPNGG LA 

« Hide

References

« Hide 'large scale' references
[1]"The TNF receptor 1-associated protein TRADD signals cell death and NF-kappa B activation."
Hsu H., Xiong J., Goeddel D.V.
Cell 81:495-504(1995) [PubMed: 7758105] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Sequence, genomic organisation, and mutation analysis of the human TRADD gene in childhood B- and T-lineage acute lymphoblastic leukemia and ALPS."
Scheuerpflug C.G., Dechant M., Fellenberg J., Ewerbeck V., Debatin K.M.
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Cloning of the human TRADD gene locus."
Kaiser C., Kohstall B., Kieser A.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]SeattleSNPs variation discovery resource
Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"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. expand/collapse author list , 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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Mammary gland.
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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].
Tissue: Pancreas.
[9]"TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex."
Hsu H., Huang J., Shu H.-B., Baichwal V.R., Goeddel D.V.
Immunity 4:387-396(1996) [PubMed: 8612133] [Abstract]
Cited for: INTERACTION WITH RIPK1.
[10]"The interaction of p62 with RIP links the atypical PKCs to NF-kappaB activation."
Sanz L., Sanchez P., Lallena M.-J., Diaz-Meco M.T., Moscat J.
EMBO J. 18:3044-3053(1999) [PubMed: 10356400] [Abstract]
Cited for: INTERACTION WITH SQSTM1.
[11]"The serine/threonine kinase HIPK2 interacts with TRADD, but not with CD95 or TNF-R1 in 293T cells."
Li X., Wang Y., Debatin K.-M., Hug H.
Biochem. Biophys. Res. Commun. 277:513-517(2000) [PubMed: 11032752] [Abstract]
Cited for: INTERACTION WITH HIPK2.
[12]"Keratin attenuates tumor necrosis factor-induced cytotoxicity through association with TRADD."
Inada H., Izawa I., Nishizawa M., Fujita E., Kiyono T., Takahashi T., Momoi T., Inagaki M.
J. Cell Biol. 155:415-426(2001) [PubMed: 11684708] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH KRT14 AND KRT18.
[13]"AIP1/DAB2IP, a novel member of the Ras-GAP family, transduces TRAF2-induced ASK1-JNK activation."
Zhang H., Zhang R., Luo Y., D'Alessio A., Pober J.S., Min W.
J. Biol. Chem. 279:44955-44965(2004) [PubMed: 15310755] [Abstract]
Cited for: INTERACTION WITH DAB2IP.
[14]"Solution structure of N-TRADD and characterization of the interaction of N-TRADD and C-TRAF2, a key step in the TNFR1 signaling pathway."
Tsao D.H., McDonagh T., Telliez J.-B., Hsu S., Malakian K., Xu G.Y., Lin L.L.
Mol. Cell 5:1051-1057(2000) [PubMed: 10911999] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-179.
[15]"A novel mechanism of TRAF signaling revealed by structural and functional analyses of the TRADD-TRAF2 interaction."
Park Y.C., Ye H., Hsia C., Segal D., Rich R.L., Liou H.C., Myszka D.G., Wu H.
Cell 101:777-787(2000) [PubMed: 10892748] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-179 IN COMPLEX WITH TRAF2.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L41690 mRNA. Translation: AAA98482.1. Different initiation.
AJ311614, AJ311615, AJ311616 Genomic DNA. Translation: CAC38018.2.
AY995114 Genomic DNA. Translation: AAX89407.1.
BT006934 mRNA. Translation: AAP35580.1.
AY575851 Genomic DNA. Translation: AAS68637.1.
AK315654 mRNA. Translation: BAG38020.1.
CH471092 Genomic DNA. Translation: EAW83081.1.
BC004491 mRNA. Translation: AAH04491.1.
IPIIPI00018744.
PIRA56911.
RefSeqNP_003780.1.
UniGeneHs.460996

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1F2HNMR-A1-169[»]
1F3VX-ray2.00A1-179[»]
SMRQ15628. Positions 209-302.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-285N.
IntActQ15628. 45 interactions.
STRINGQ15628.

Proteomic databases

PRIDEQ15628.

Genome annotation databases

EnsemblENST00000345057; ENSP00000341268; ENSG00000102871; Homo sapiens. [Genome view]
GeneID8717.
KEGGhsa:8717.
UCSCuc002eri.1. human.

Organism-specific databases

CTD8717.
GeneCardsGC16M065745.
H-InvDBHIX0013134.
HGNCHGNC:12030. TRADD.
HPACAB004602.
MIM603500. gene.
PharmGKBPA36707.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG14288.
HOGENOMHBG715696.
HOVERGENQ15628.
InParanoidQ15628.
OMATDEERCL.
OrthoDBEOG937V08.
PhylomeDBQ15628.

Enzyme and pathway databases

Pathway_Interaction_DBcaspase_pathway. Caspase cascade in apoptosis.
ceramidepathway. Ceramide signaling pathway.
hivnefpathway. HIV-1 Nef: Negative effector of Fas and TNF-alpha.
tnfpathway. TNF receptor signaling pathway.
trail_pathway. TRAIL signaling pathway.
ReactomeREACT_578. Apoptosis.

Gene expression databases

ArrayExpressQ15628.
BgeeQ15628.
CleanExHS_TRADD.
GenevestigatorQ15628.
GermOnlineENSG00000102871. Homo sapiens.

Family and domain databases

InterProIPR000488. Death.
IPR011029. DEATH-like.
IPR009095. TRADD_N.
[Graphical view]
Gene3DG3DSA:1.10.533.10. DEATH_like. 1 hit.
G3DSA:3.30.70.680. TRADD_N. 1 hit.
PfamPF00531. Death. 1 hit.
PF09034. TRADD_N. 1 hit.
[Graphical view]
ProDomPD182470. TRADD_N. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00005. DEATH. 1 hit.
[Graphical view]
PROSITEPS50017. DEATH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio32687.
SOURCESearch...

Entry information

Entry nameTRADD_HUMAN
AccessionPrimary (citable) accession number: Q15628
Secondary accession number(s): B2RDS3, Q52NZ1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 15, 1999
Last modified: January 19, 2010
This is version 97 of the entry and version 2 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 16

Human chromosome 16: entries, gene names and cross-references to MIM

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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