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Q15628 (TRADD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

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) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

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

General annotation (Comments)

Function

The nuclear form acts as a tumor suppressor by preventing ubiquitination and degradation of isoform p19ARF/ARFof CDKN2A by TRIP12: acts by interacting with TRIP12, leading to disrupt interaction between TRIP12 and isoform p19ARF/ARFof CDKN2A By similarity. 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

Interacts with TRIP12 By similarity. 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

Nucleus By similarity. Cytoplasm By similarity. Cytoplasmcytoskeleton. Note: Shuttles between the cytoplasm and the nucleus By similarity. 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.

Sequence caution

The sequence AAA98482.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processApoptosis
   Cellular componentCytoplasm
Cytoskeleton
Nucleus
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of cysteine-type endopeptidase activity involved in apoptotic process

Traceable author statement. Source: Reactome

apoptotic process

Traceable author statement. Source: Reactome

apoptotic signaling pathway

Traceable author statement. Source: Reactome

extrinsic apoptotic signaling pathway

Inferred from mutant phenotype PubMed 16611992. Source: UniProtKB

extrinsic apoptotic signaling pathway via death domain receptors

Traceable author statement Ref.9. Source: BHF-UCL

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from expression pattern PubMed 12761501. Source: UniProtKB

positive regulation of NF-kappaB transcription factor activity

Traceable author statement PubMed 18309324. Source: UniProtKB

positive regulation of apoptotic process

Traceable author statement PubMed 18309324. Source: UniProtKB

positive regulation of hair follicle development

Inferred from electronic annotation. Source: Ensembl

protein heterooligomerization

Inferred from electronic annotation. Source: Ensembl

regulation of extrinsic apoptotic signaling pathway in absence of ligand

Traceable author statement. Source: Reactome

signal transduction

Traceable author statement Ref.1. Source: ProtInc

tumor necrosis factor-mediated signaling pathway

Traceable author statement Ref.9. Source: BHF-UCL

   Cellular_componentcytoplasm

Inferred from direct assay Ref.12. Source: UniProtKB

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Traceable author statement. Source: Reactome

death-inducing signaling complex

Traceable author statement PubMed 18309324. Source: UniProtKB

membrane raft

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

receptor complex

Inferred from direct assay Ref.9. Source: BHF-UCL

   Molecular_functionbinding, bridging

Inferred from physical interaction Ref.9. Source: BHF-UCL

death domain binding

Inferred from physical interaction Ref.9. Source: BHF-UCL

identical protein binding

Inferred from physical interaction Ref.12Ref.1. Source: IntAct

kinase binding

Inferred from physical interaction Ref.9. Source: BHF-UCL

protein binding

Inferred from physical interaction PubMed 1040062PubMed 10848577Ref.12. Source: UniProtKB

signal transducer activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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
Motif147 – 16317Nuclear export signal By similarity
Motif231 – 24414Nuclear localization signal By similarity
Compositional bias192 – 1987Poly-Pro

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
Q15628 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DAB2IP.
[14]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"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] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-179.
[16]"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] [Europe PMC] [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.
CCDSCCDS10829.1.
PIRA56911.
RefSeqNP_003780.1. NM_003789.3.
UniGeneHs.460996.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1F2HNMR-A1-169[»]
1F3VX-ray2.00A1-179[»]
ProteinModelPortalQ15628.
SMRQ15628. Positions 1-169.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114257. 41 interactions.
DIPDIP-285N.
IntActQ15628. 15 interactions.
MINTMINT-99115.
STRING9606.ENSP00000341268.

PTM databases

PhosphoSiteQ15628.

Polymorphism databases

DMDM6094511.

Proteomic databases

MaxQBQ15628.
PaxDbQ15628.
PRIDEQ15628.

Protocols and materials databases

DNASU8717.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000345057; ENSP00000341268; ENSG00000102871.
GeneID8717.
KEGGhsa:8717.
UCSCuc002erh.1. human.

Organism-specific databases

CTD8717.
GeneCardsGC16M067188.
HGNCHGNC:12030. TRADD.
HPACAB004602.
MIM603500. gene.
neXtProtNX_Q15628.
PharmGKBPA36707.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG47236.
HOGENOMHOG000059664.
HOVERGENHBG054083.
InParanoidQ15628.
KOK03171.
OMALRFCGRQ.
OrthoDBEOG7QRQVQ.
PhylomeDBQ15628.
TreeFamTF331882.

Enzyme and pathway databases

ReactomeREACT_578. Apoptosis.
SignaLinkQ15628.

Gene expression databases

ArrayExpressQ15628.
BgeeQ15628.
CleanExHS_TRADD.
GenevestigatorQ15628.

Family and domain databases

Gene3D1.10.533.10. 1 hit.
3.30.70.680. 1 hit.
InterProIPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR009095. TRADD_N.
[Graphical view]
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]
SUPFAMSSF47986. SSF47986. 1 hit.
SSF55044. SSF55044. 1 hit.
PROSITEPS50017. DEATH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ15628.
GeneWikiTRADD.
GenomeRNAi8717.
NextBio32687.
PROQ15628.
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: July 9, 2014
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 16

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