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Q15628

- TRADD_HUMAN

UniProt

Q15628 - TRADD_HUMAN

Protein

Tumor necrosis factor receptor type 1-associated DEATH domain protein

Gene

TRADD

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 2 (15 Jul 1999)
      Previous versions | rss
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    Functioni

    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 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.By similarity

    GO - Molecular functioni

    1. binding, bridging Source: BHF-UCL
    2. death domain binding Source: BHF-UCL
    3. identical protein binding Source: IntAct
    4. kinase binding Source: BHF-UCL
    5. protein binding Source: UniProtKB
    6. signal transducer activity Source: InterPro

    GO - Biological processi

    1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: Reactome
    2. apoptotic process Source: Reactome
    3. apoptotic signaling pathway Source: Reactome
    4. extrinsic apoptotic signaling pathway Source: UniProtKB
    5. extrinsic apoptotic signaling pathway via death domain receptors Source: BHF-UCL
    6. positive regulation of apoptotic process Source: UniProtKB
    7. positive regulation of hair follicle development Source: Ensembl
    8. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    9. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
    10. protein heterooligomerization Source: Ensembl
    11. regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: Reactome
    12. signal transduction Source: ProtInc
    13. tumor necrosis factor-mediated signaling pathway Source: BHF-UCL

    Keywords - Biological processi

    Apoptosis

    Enzyme and pathway databases

    ReactomeiREACT_1432. TNF signaling.
    REACT_1503. Caspase-8 activation.
    REACT_164011. Regulation by c-FLIP.
    REACT_832. Dimerization of procaspase-8.
    SignaLinkiQ15628.

    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:TRADD
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:12030. TRADD.

    Subcellular locationi

    Nucleus By similarity. Cytoplasm By similarity. Cytoplasmcytoskeleton 1 Publication
    Note: Shuttles between the cytoplasm and the nucleus.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytoskeleton Source: UniProtKB-SubCell
    3. cytosol Source: Reactome
    4. death-inducing signaling complex Source: UniProtKB
    5. membrane raft Source: Ensembl
    6. nucleus Source: UniProtKB-SubCell
    7. receptor complex Source: BHF-UCL

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA36707.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 312312Tumor necrosis factor receptor type 1-associated DEATH domain proteinPRO_0000065602Add
    BLAST

    Proteomic databases

    MaxQBiQ15628.
    PaxDbiQ15628.
    PRIDEiQ15628.

    PTM databases

    PhosphoSiteiQ15628.

    Expressioni

    Tissue specificityi

    Found in all examined tissues.

    Gene expression databases

    ArrayExpressiQ15628.
    BgeeiQ15628.
    CleanExiHS_TRADD.
    GenevestigatoriQ15628.

    Organism-specific databases

    HPAiCAB004602.

    Interactioni

    Subunit structurei

    Interacts with TRIP12 By similarity. Heterodimer with TNFRSF1A/TNFR1. Interacts with DAB2IP, FADD, HIPK2, KRT14, KRT16, KRT17, KRT18, RIPK1, SQSTM1, TRAF1, TRAF2 and TRPC4AP.By similarity6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-359215,EBI-359215
    KRT18P0578311EBI-359215,EBI-297888
    TNFRSF1AP1943811EBI-359215,EBI-299451
    TRAF2Q129333EBI-359215,EBI-355744

    Protein-protein interaction databases

    BioGridi114257. 41 interactions.
    DIPiDIP-285N.
    IntActiQ15628. 15 interactions.
    MINTiMINT-99115.
    STRINGi9606.ENSP00000341268.

    Structurei

    Secondary structure

    1
    312
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi12 – 2514
    Helixi28 – 336
    Turni35 – 373
    Helixi38 – 5215
    Turni56 – 583
    Beta strandi59 – 668
    Beta strandi68 – 7912
    Helixi80 – 9112
    Helixi94 – 10613
    Beta strandi114 – 1207
    Helixi125 – 1284
    Helixi132 – 14110
    Helixi150 – 16213

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1F2HNMR-A1-169[»]
    1F3VX-ray2.00A1-179[»]
    ProteinModelPortaliQ15628.
    SMRiQ15628. Positions 1-169.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ15628.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini179 – 289111DeathPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni222 – 28968Interaction with KRT14 and KRT18Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi147 – 16317Nuclear export signalBy similarityAdd
    BLAST
    Motifi231 – 24414Nuclear localization signalBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi192 – 1987Poly-Pro

    Domaini

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

    Sequence similaritiesi

    Contains 1 death domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG47236.
    HOGENOMiHOG000059664.
    HOVERGENiHBG054083.
    InParanoidiQ15628.
    KOiK03171.
    OMAiLRFCGRQ.
    OrthoDBiEOG7QRQVQ.
    PhylomeDBiQ15628.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q15628-1) [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

    MAAGQNGHEE WVGSAYLFVE SSLDKVVLSD AYAHPQQKVA VYRALQAALA    50
    ESGGSPDVLQ MLKIHRSDPQ LIVQLRFCGR QPCGRFLRAY REGALRAALQ 100
    RSLAAALAQH SVPLQLELRA GAERLDALLA DEERCLSCIL AQQPDRLRDE 150
    ELAELEDALR NLKCGSGARG GDGEVASAPL QPPVPSLSEV KPPPPPPPAQ 200
    TFLFQGQPVV NRPLSLKDQQ TFARSVGLKW RKVGRSLQRG CRALRDPALD 250
    SLAYEYEREG LYEQAFQLLR RFVQAEGRRA TLQRLVEALE ENELTSLAED 300
    LLGLTDPNGG LA 312
    Length:312
    Mass (Da):34,247
    Last modified:July 15, 1999 - v2
    Checksum:i5645D7E63E5FF05A
    GO
    Isoform 2 (identifier: Q15628-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-60: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:252
    Mass (Da):27,904
    Checksum:i669B381D012B108A
    GO

    Sequence cautioni

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

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 6060Missing in isoform 2. 1 PublicationVSP_056526Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    AK090673 mRNA. Translation: BAG52211.1.
    AK315654 mRNA. Translation: BAG38020.1.
    AC074143 Genomic DNA. No translation available.
    CH471092 Genomic DNA. Translation: EAW83081.1.
    BC004491 mRNA. Translation: AAH04491.1.
    CCDSiCCDS10829.1.
    PIRiA56911.
    RefSeqiNP_003780.1. NM_003789.3.
    XP_005256270.1. XM_005256213.1.
    UniGeneiHs.460996.

    Genome annotation databases

    EnsembliENST00000345057; ENSP00000341268; ENSG00000102871.
    ENST00000486556; ENSP00000462591; ENSG00000102871.
    GeneIDi8717.
    KEGGihsa:8717.
    UCSCiuc002erh.1. human.

    Polymorphism databases

    DMDMi6094511.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    AK090673 mRNA. Translation: BAG52211.1 .
    AK315654 mRNA. Translation: BAG38020.1 .
    AC074143 Genomic DNA. No translation available.
    CH471092 Genomic DNA. Translation: EAW83081.1 .
    BC004491 mRNA. Translation: AAH04491.1 .
    CCDSi CCDS10829.1.
    PIRi A56911.
    RefSeqi NP_003780.1. NM_003789.3.
    XP_005256270.1. XM_005256213.1.
    UniGenei Hs.460996.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1F2H NMR - A 1-169 [» ]
    1F3V X-ray 2.00 A 1-179 [» ]
    ProteinModelPortali Q15628.
    SMRi Q15628. Positions 1-169.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114257. 41 interactions.
    DIPi DIP-285N.
    IntActi Q15628. 15 interactions.
    MINTi MINT-99115.
    STRINGi 9606.ENSP00000341268.

    PTM databases

    PhosphoSitei Q15628.

    Polymorphism databases

    DMDMi 6094511.

    Proteomic databases

    MaxQBi Q15628.
    PaxDbi Q15628.
    PRIDEi Q15628.

    Protocols and materials databases

    DNASUi 8717.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000345057 ; ENSP00000341268 ; ENSG00000102871 .
    ENST00000486556 ; ENSP00000462591 ; ENSG00000102871 .
    GeneIDi 8717.
    KEGGi hsa:8717.
    UCSCi uc002erh.1. human.

    Organism-specific databases

    CTDi 8717.
    GeneCardsi GC16M067188.
    HGNCi HGNC:12030. TRADD.
    HPAi CAB004602.
    MIMi 603500. gene.
    neXtProti NX_Q15628.
    PharmGKBi PA36707.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG47236.
    HOGENOMi HOG000059664.
    HOVERGENi HBG054083.
    InParanoidi Q15628.
    KOi K03171.
    OMAi LRFCGRQ.
    OrthoDBi EOG7QRQVQ.
    PhylomeDBi Q15628.
    TreeFami TF331882.

    Enzyme and pathway databases

    Reactomei REACT_1432. TNF signaling.
    REACT_1503. Caspase-8 activation.
    REACT_164011. Regulation by c-FLIP.
    REACT_832. Dimerization of procaspase-8.
    SignaLinki Q15628.

    Miscellaneous databases

    EvolutionaryTracei Q15628.
    GeneWikii TRADD.
    GenomeRNAii 8717.
    NextBioi 32687.
    PROi Q15628.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15628.
    Bgeei Q15628.
    CleanExi HS_TRADD.
    Genevestigatori Q15628.

    Family and domain databases

    Gene3Di 1.10.533.10. 1 hit.
    3.30.70.680. 1 hit.
    InterProi IPR011029. DEATH-like_dom.
    IPR000488. Death_domain.
    IPR009095. TRADD_N.
    [Graphical view ]
    Pfami PF00531. Death. 1 hit.
    PF09034. TRADD_N. 1 hit.
    [Graphical view ]
    ProDomi PD182470. TRADD_N. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SMARTi SM00005. DEATH. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47986. SSF47986. 1 hit.
    SSF55044. SSF55044. 1 hit.
    PROSITEi PS50017. DEATH_DOMAIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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] (ISOFORM 1).
    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] (ISOFORM 1).
    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.
      , 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] (ISOFORMS 1 AND 2).
      Tissue: Cerebellum and Mammary gland.
    7. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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).
      Tissue: Pancreas.
    10. "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.
    11. "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.
    12. "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.
    13. "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.
    14. "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.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "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.
    17. "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.

    Entry informationi

    Entry nameiTRADD_HUMAN
    AccessioniPrimary (citable) accession number: Q15628
    Secondary accession number(s): B2RDS3, B3KQZ9, Q52NZ1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: July 15, 1999
    Last modified: October 1, 2014
    This is version 143 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3