Tumor necrosis factor receptor type 1-associated DEATH domain protein

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functionⁱ

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• death domain binding Source: BHF-UCL <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • Ref.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: IDENTIFICATION IN COMPLEX I, INTERACTION WITH RIPK1.
• identical protein binding Source: IntActInferred from physical interactionⁱ
  • Ref.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.
  • "A protein-protein interaction map of the TNF-induced NF-kappaB signal transduction pathway."
    Van Quickelberghe E., De Sutter D., van Loo G., Eyckerman S., Gevaert K.
    Sci Data 5:180289-180289(2018) [PubMed] [Europe PMC] [Abstract]
  • Ref.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), IDENTIFICATION IN COMPLEX I, INTERACTION WITH TNFRSF1A.
• kinase binding Source: BHF-UCLInferred from physical interactionⁱ
  • Ref.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: IDENTIFICATION IN COMPLEX I, INTERACTION WITH RIPK1.
• protein-containing complex binding Source: Ensembl
• transmembrane receptor protein tyrosine kinase adaptor activity Source: BHF-UCLInferred from physical interactionⁱ
  • Ref.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: IDENTIFICATION IN COMPLEX I, INTERACTION WITH RIPK1.
• tumor necrosis factor receptor binding Source: Ensembl

GO - Biological processⁱ

• activation of cysteine-type endopeptidase activity involved in apoptotic process Source: Reactome
• apoptotic process Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#tas">GO evidence code guide</a></p> Traceable author statementⁱ
  • Ref.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), IDENTIFICATION IN COMPLEX I, INTERACTION WITH TNFRSF1A.
• cellular response to tumor necrosis factor Source: ARUK-UCL <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • "MicroRNA-30c-2-3p negatively regulates NF-kappaB signaling and cell cycle progression through downregulation of TRADD and CCNE1 in breast cancer."
    Shukla K., Sharma A.K., Ward A., Will R., Hielscher T., Balwierz A., Breunig C., Munstermann E., Konig R., Keklikoglou I., Wiemann S.
    Mol Oncol 9:1106-1119(2015) [PubMed] [Europe PMC] [Abstract]
• death-inducing signaling complex assembly Source: Reactome
• extrinsic apoptotic signaling pathway Source: UniProtKBInferred from mutant phenotypeⁱ
  • "Competitive control of independent programs of tumor necrosis factor receptor-induced cell death by TRADD and RIP1."
    Zheng L., Bidere N., Staudt D., Cubre A., Orenstein J., Chan F.K., Lenardo M.
    Mol Cell Biol 26:3505-3513(2006) [PubMed] [Europe PMC] [Abstract]
• extrinsic apoptotic signaling pathway via death domain receptors Source: BHF-UCLTraceable author statementⁱ
  • Ref.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: IDENTIFICATION IN COMPLEX I, INTERACTION WITH RIPK1.
• I-kappaB kinase/NF-kappaB signaling Source: Reactome
• negative regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: Reactome
• positive regulation of apoptotic process Source: UniProtKBTraceable author statementⁱ
  • "No death without life: vital functions of apoptotic effectors."
    Galluzzi L., Joza N., Tasdemir E., Maiuri M.C., Hengartner M., Abrams J.M., Tavernarakis N., Penninger J., Madeo F., Kroemer G.
    Cell Death Differ 15:1113-1123(2008) [PubMed] [Europe PMC] [Abstract]
• positive regulation of cell migration Source: ARUK-UCLInferred from mutant phenotypeⁱ
  • "MicroRNA-30c-2-3p negatively regulates NF-kappaB signaling and cell cycle progression through downregulation of TRADD and CCNE1 in breast cancer."
    Shukla K., Sharma A.K., Ward A., Will R., Hielscher T., Balwierz A., Breunig C., Munstermann E., Konig R., Keklikoglou I., Wiemann S.
    Mol Oncol 9:1106-1119(2015) [PubMed] [Europe PMC] [Abstract]
• positive regulation of hair follicle development Source: Ensembl
• positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iep">GO evidence code guide</a></p> Inferred from expression patternⁱ
  • "Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways."
    Matsuda A., Suzuki Y., Honda G., Muramatsu S., Matsuzaki O., Nagano Y., Doi T., Shimotohno K., Harada T., Nishida E., Hayashi H., Sugano S.
    Oncogene 22:3307-3318(2003) [PubMed] [Europe PMC] [Abstract]
• positive regulation of inflammatory response Source: ARUK-UCLInferred from mutant phenotypeⁱ
  • "MicroRNA-30c-2-3p negatively regulates NF-kappaB signaling and cell cycle progression through downregulation of TRADD and CCNE1 in breast cancer."
    Shukla K., Sharma A.K., Ward A., Will R., Hielscher T., Balwierz A., Breunig C., Munstermann E., Konig R., Keklikoglou I., Wiemann S.
    Mol Oncol 9:1106-1119(2015) [PubMed] [Europe PMC] [Abstract]
• positive regulation of NF-kappaB transcription factor activity Source: ARUK-UCLInferred from mutant phenotypeⁱ
  • "MicroRNA-30c-2-3p negatively regulates NF-kappaB signaling and cell cycle progression through downregulation of TRADD and CCNE1 in breast cancer."
    Shukla K., Sharma A.K., Ward A., Will R., Hielscher T., Balwierz A., Breunig C., Munstermann E., Konig R., Keklikoglou I., Wiemann S.
    Mol Oncol 9:1106-1119(2015) [PubMed] [Europe PMC] [Abstract]
• positive regulation of NIK/NF-kappaB signaling Source: ARUK-UCLInferred from mutant phenotypeⁱ
  • "MicroRNA-30c-2-3p negatively regulates NF-kappaB signaling and cell cycle progression through downregulation of TRADD and CCNE1 in breast cancer."
    Shukla K., Sharma A.K., Ward A., Will R., Hielscher T., Balwierz A., Breunig C., Munstermann E., Konig R., Keklikoglou I., Wiemann S.
    Mol Oncol 9:1106-1119(2015) [PubMed] [Europe PMC] [Abstract]
• regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: Reactome
• regulation of tumor necrosis factor-mediated signaling pathway Source: Reactome
• signal transduction Source: ProtIncTraceable author statementⁱ
  • Ref.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), IDENTIFICATION IN COMPLEX I, INTERACTION WITH TNFRSF1A.
• tumor necrosis factor-mediated signaling pathway Source: BHF-UCLTraceable author statementⁱ
  • Ref.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: IDENTIFICATION IN COMPLEX I, INTERACTION WITH RIPK1.

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsⁱ

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

Keywords - Cellular componentⁱ

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechⁱ

Organism-specific databases

Miscellaneous databases

Genetic variation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressionⁱ

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityⁱ

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

GO - Molecular functionⁱ

• death domain binding Source: BHF-UCLInferred from physical interactionⁱ
  • Ref.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: IDENTIFICATION IN COMPLEX I, INTERACTION WITH RIPK1.
• identical protein binding Source: IntActInferred from physical interactionⁱ
  • Ref.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.
  • "A protein-protein interaction map of the TNF-induced NF-kappaB signal transduction pathway."
    Van Quickelberghe E., De Sutter D., van Loo G., Eyckerman S., Gevaert K.
    Sci Data 5:180289-180289(2018) [PubMed] [Europe PMC] [Abstract]
  • Ref.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), IDENTIFICATION IN COMPLEX I, INTERACTION WITH TNFRSF1A.
• kinase binding Source: BHF-UCLInferred from physical interactionⁱ
  • Ref.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: IDENTIFICATION IN COMPLEX I, INTERACTION WITH RIPK1.
• transmembrane receptor protein tyrosine kinase adaptor activity Source: BHF-UCLInferred from physical interactionⁱ
  • Ref.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: IDENTIFICATION IN COMPLEX I, INTERACTION WITH RIPK1.
• tumor necrosis factor receptor binding Source: Ensembl

Protein-protein interaction databases

Miscellaneous databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structureⁱ

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

Domains and Repeats

Region

Motif

Compositional bias

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domainⁱ

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)ⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

        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                                          

        10         20         30         40         50
MLKIHRSDPQ LIVQLRFCGR QPCGRFLRAY REGALRAALQ RSLAAALAQH 
        60         70         80         90        100
SVPLQLELRA GAERLDALLA DEERCLSCIL AQQPDRLRDE ELAELEDALR 
       110        120        130        140        150
NLKCGSGARG GDGEVASAPL QPPVPSLSEV KPPPPPPPAQ TFLFQGQPVV 
       160        170        180        190        200
NRPLSLKDQQ TFARSVGLKW RKVGRSLQRG CRALRDPALD SLAYEYEREG 
       210        220        230        240        250
LYEQAFQLLR RFVQAEGRRA TLQRLVEALE ENELTSLAED LLGLTDPNGG 

LA                                                     

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautionⁱ

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityⁱ

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ

• 100% Identity
• 90% Identity
• 50% Identity

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesⁱ

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Genetic variation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

Keywords - Technical termⁱ

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