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Q15628

- TRADD_HUMAN

UniProt

Q15628 - TRADD_HUMAN

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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

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. 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
Complete GO annotation...

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-KW
  3. cytosol Source: Reactome
  4. death-inducing signaling complex Source: UniProtKB
  5. membrane raft Source: Ensembl
  6. nucleus Source: UniProtKB-KW
  7. receptor complex Source: BHF-UCL
Complete GO annotation...

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

BgeeiQ15628.
CleanExiHS_TRADD.
ExpressionAtlasiQ15628. baseline and differential.
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.
GeneTreeiENSGT00390000002016.
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

        10         20         30         40         50
MAAGQNGHEE WVGSAYLFVE SSLDKVVLSD AYAHPQQKVA VYRALQAALA
60 70 80 90 100
ESGGSPDVLQ MLKIHRSDPQ LIVQLRFCGR QPCGRFLRAY REGALRAALQ
110 120 130 140 150
RSLAAALAQH SVPLQLELRA GAERLDALLA DEERCLSCIL AQQPDRLRDE
160 170 180 190 200
ELAELEDALR NLKCGSGARG GDGEVASAPL QPPVPSLSEV KPPPPPPPAQ
210 220 230 240 250
TFLFQGQPVV NRPLSLKDQQ TFARSVGLKW RKVGRSLQRG CRALRDPALD
260 270 280 290 300
SLAYEYEREG LYEQAFQLLR RFVQAEGRRA TLQRLVEALE ENELTSLAED
310
LLGLTDPNGG LA
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. [Q15628-1]
PIRiA56911.
RefSeqiNP_003780.1. NM_003789.3.
XP_005256270.1. XM_005256213.1.
UniGeneiHs.460996.

Genome annotation databases

EnsembliENST00000345057; ENSP00000341268; ENSG00000102871. [Q15628-1]
ENST00000486556; ENSP00000462591; ENSG00000102871. [Q15628-2]
GeneIDi8717.
KEGGihsa:8717.
UCSCiuc002erh.1. human. [Q15628-1]

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. [Q15628-1 ]
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 . [Q15628-1 ]
ENST00000486556 ; ENSP00000462591 ; ENSG00000102871 . [Q15628-2 ]
GeneIDi 8717.
KEGGi hsa:8717.
UCSCi uc002erh.1. human. [Q15628-1 ]

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.
GeneTreei ENSGT00390000002016.
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

Bgeei Q15628.
CleanExi HS_TRADD.
ExpressionAtlasi Q15628. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 144 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