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Protein

Tumor necrosis factor receptor type 1-associated DEATH domain protein

Gene

Tradd

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 (By similarity). The nuclear form acts as a tumor suppressor by preventing ubiquitination and degradation of isoform p19ARF/ARF of CDKN2A by TRIP12: acts by interacting with TRIP12, leading to disrupt interaction between TRIP12 and isoform p19ARF/ARF of CDKN2A.By similarity1 Publication

GO - Molecular functioni

GO - Biological processi

  • extrinsic apoptotic signaling pathway Source: MGI
  • positive regulation of hair follicle development Source: UniProtKB
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: Ensembl
  • protein heterooligomerization Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Apoptosis

Enzyme and pathway databases

ReactomeiR-MMU-3371378. Regulation by c-FLIP.
R-MMU-5213460. RIPK1-mediated regulated necrosis.
R-MMU-5218900. CASP8 activity is inhibited.
R-MMU-5357786. TNFR1-induced proapoptotic signaling.
R-MMU-5357905. Regulation of TNFR1 signaling.
R-MMU-5357956. TNFR1-induced NFkappaB signaling pathway.
R-MMU-69416. Dimerization of procaspase-8.
R-MMU-75893. TNF signaling.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:TraddImported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:109200. Tradd.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytoskeleton Source: UniProtKB-SubCell
  • membrane raft Source: Ensembl
  • nucleus Source: UniProtKB-SubCell
  • plasma membrane Source: MGI
  • receptor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Disruption phenotypei

Mice develop tumors. In a C57BL/6 genetic background, mice exhibit a shorter lifespan than wild-type, but exhibit low incidences of observable tumor formation. In the FVB/N background, which is more tumor-prone, mice show a significant increas in the spontaneous development of a broad range of tumor types.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi297 – 2993EDL → AAA: Dominant-negative mutant, leading to enhanced ubiquitination and degradation of isoform p19ARF/ARF of CDKN2A. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 310310Tumor necrosis factor receptor type 1-associated DEATH domain proteinPRO_0000291660Add
BLAST

Proteomic databases

EPDiQ3U0V2.
MaxQBiQ3U0V2.
PaxDbiQ3U0V2.
PRIDEiQ3U0V2.

PTM databases

iPTMnetiQ3U0V2.
PhosphoSiteiQ3U0V2.

Expressioni

Gene expression databases

BgeeiQ3U0V2.
CleanExiMM_TRADD.
ExpressionAtlasiQ3U0V2. baseline and differential.
GenevisibleiQ3U0V2. MM.

Interactioni

Subunit structurei

Heterodimer with TNFRSF1A/TNFR1. Interacts with DAB2IP, FADD, HIPK2, KRT18, RIPK1, SQSTM1, TRAF1, TRAF2 and TRPC4AP (By similarity). Interacts with KRT14, KRT16 and KRT17. Interacts with TRIP12.By similarity2 Publications

GO - Molecular functioni

Protein-protein interaction databases

BioGridi214812. 1 interaction.
DIPiDIP-38039N.
IntActiQ3U0V2. 4 interactions.
STRINGi10090.ENSMUSP00000034359.

Structurei

3D structure databases

ProteinModelPortaliQ3U0V2.
SMRiQ3U0V2. Positions 1-164.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini213 – 30391DeathPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni220 – 28768Interaction with KRT14 and KRT18By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi147 – 16317Nuclear export signalAdd
BLAST
Motifi229 – 24214Nuclear localization signalAdd
BLAST

Domaini

Requires the intact death domain to associate with TNFRSF1A/TNFR1.By similarity

Sequence similaritiesi

Contains 1 death domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410IF81. Eukaryota.
ENOG4111IRA. LUCA.
GeneTreeiENSGT00390000002016.
HOGENOMiHOG000059664.
HOVERGENiHBG054083.
InParanoidiQ3U0V2.
KOiK03171.
OMAiLRFCGRQ.
OrthoDBiEOG7QRQVQ.
PhylomeDBiQ3U0V2.
TreeFamiTF331882.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
3.30.70.680. 1 hit.
InterProiIPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR009095. TRADD_N.
[Graphical view]
PfamiPF00531. Death. 1 hit.
PF09034. TRADD_N. 1 hit.
[Graphical view]
ProDomiPD182470. TRADD_N. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00005. DEATH. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
SSF55044. SSF55044. 1 hit.
PROSITEiPS50017. DEATH_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q3U0V2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAGQNGHEE WVGSAYLFLE SAVDKVILSE AYTDPKKKVA IYKALQTALS
60 70 80 90 100
ESGDSSDVLQ ILKIHCSDPQ LIVQLRFCGR VLCGRFLQAY REGALRTALQ
110 120 130 140 150
RCMAPALAQE ALRLQLELRA GAEQLDSWLT DEERCLNYIL AQKPDRLRDE
160 170 180 190 200
ELAELEDELC KLTCDCTGQG GAIQVASAGS KFPVSSPTEE KPLPAACQTF
210 220 230 240 250
LFHGQLVVNR PLTLQDQQTF ARSVGLKWRR VGRSLQRNCR ALRDPALDSL
260 270 280 290 300
AYEYERDGLY EQAFQLLRRF MQAEGRRATL QRLVEALEEN ELTSLAEDLL
310
GQAEPDGGLA
Length:310
Mass (Da):34,577
Last modified:October 11, 2005 - v1
Checksum:i225F00D4022691BB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK156540 mRNA. Translation: BAE33749.1.
BC132607 mRNA. Translation: AAI32608.1.
CCDSiCCDS22594.1.
RefSeqiNP_001028333.1. NM_001033161.2.
XP_011236434.1. XM_011238132.1.
UniGeneiMm.264255.

Genome annotation databases

EnsembliENSMUST00000034359; ENSMUSP00000034359; ENSMUSG00000031887.
GeneIDi105242493.
71609.
KEGGimmu:105242493.
mmu:71609.
UCSCiuc009nby.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK156540 mRNA. Translation: BAE33749.1.
BC132607 mRNA. Translation: AAI32608.1.
CCDSiCCDS22594.1.
RefSeqiNP_001028333.1. NM_001033161.2.
XP_011236434.1. XM_011238132.1.
UniGeneiMm.264255.

3D structure databases

ProteinModelPortaliQ3U0V2.
SMRiQ3U0V2. Positions 1-164.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi214812. 1 interaction.
DIPiDIP-38039N.
IntActiQ3U0V2. 4 interactions.
STRINGi10090.ENSMUSP00000034359.

PTM databases

iPTMnetiQ3U0V2.
PhosphoSiteiQ3U0V2.

Proteomic databases

EPDiQ3U0V2.
MaxQBiQ3U0V2.
PaxDbiQ3U0V2.
PRIDEiQ3U0V2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034359; ENSMUSP00000034359; ENSMUSG00000031887.
GeneIDi105242493.
71609.
KEGGimmu:105242493.
mmu:71609.
UCSCiuc009nby.1. mouse.

Organism-specific databases

CTDi8717.
MGIiMGI:109200. Tradd.

Phylogenomic databases

eggNOGiENOG410IF81. Eukaryota.
ENOG4111IRA. LUCA.
GeneTreeiENSGT00390000002016.
HOGENOMiHOG000059664.
HOVERGENiHBG054083.
InParanoidiQ3U0V2.
KOiK03171.
OMAiLRFCGRQ.
OrthoDBiEOG7QRQVQ.
PhylomeDBiQ3U0V2.
TreeFamiTF331882.

Enzyme and pathway databases

ReactomeiR-MMU-3371378. Regulation by c-FLIP.
R-MMU-5213460. RIPK1-mediated regulated necrosis.
R-MMU-5218900. CASP8 activity is inhibited.
R-MMU-5357786. TNFR1-induced proapoptotic signaling.
R-MMU-5357905. Regulation of TNFR1 signaling.
R-MMU-5357956. TNFR1-induced NFkappaB signaling pathway.
R-MMU-69416. Dimerization of procaspase-8.
R-MMU-75893. TNF signaling.

Miscellaneous databases

PROiQ3U0V2.
SOURCEiSearch...

Gene expression databases

BgeeiQ3U0V2.
CleanExiMM_TRADD.
ExpressionAtlasiQ3U0V2. baseline and differential.
GenevisibleiQ3U0V2. MM.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
3.30.70.680. 1 hit.
InterProiIPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR009095. TRADD_N.
[Graphical view]
PfamiPF00531. Death. 1 hit.
PF09034. TRADD_N. 1 hit.
[Graphical view]
ProDomiPD182470. TRADD_N. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00005. DEATH. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
SSF55044. SSF55044. 1 hit.
PROSITEiPS50017. DEATH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: NODImported.
    Tissue: SpleenImported.
  2. "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: BrainImported.
  3. "Keratin 17 modulates hair follicle cycling in a TNFalpha-dependent fashion."
    Tong X., Coulombe P.A.
    Genes Dev. 20:1353-1364(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KRT14; KRT16 AND KRT17, SUBCELLULAR LOCATION.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  5. "TRADD contributes to tumour suppression by regulating ULF-dependent p19Arf ubiquitylation."
    Chio I.I., Sasaki M., Ghazarian D., Moreno J., Done S., Ueda T., Inoue S., Chang Y.L., Chen N.J., Mak T.W.
    Nat. Cell Biol. 14:625-633(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, INTERACTION WITH TRIP12, MUTAGENESIS OF 297-GLU--LEU-299.

Entry informationi

Entry nameiTRADD_MOUSE
AccessioniPrimary (citable) accession number: Q3U0V2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: October 11, 2005
Last modified: June 8, 2016
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.