Micron Document
<!DOCTYPE html>
<html class="client-nojs vector-feature-night-mode-disabled vector-feature-language-in-header-enabled vector-feature-language-in-main-page-header-disabled vector-feature-page-tools-pinned-disabled vector-feature-toc-pinned-clientpref-1 vector-feature-main-menu-pinned-disabled vector-feature-limited-width-clientpref-1 vector-feature-limited-width-content-enabled vector-feature-custom-font-size-clientpref-1 vector-feature-appearance-pinned-clientpref-1 vector-sticky-header-enabled" lang="en" dir="ltr"><head>
<meta charset="UTF-8">
<title>FADD</title>
<meta name="viewport" content="width=device-width, initial-scale=1.0">
<link rel="canonical" href="https://en.wikipedia.org/wiki/FADD"> <link href="./mw/ext.cite.styles.css" rel="stylesheet" type="text/css">
<link href="./mw/mediawiki.page.gallery.styles.css" rel="stylesheet" type="text/css">
<link href="./mw/skins.vector.icons.css" rel="stylesheet" type="text/css">
<link href="./mw/skins.vector.search.codex.styles.css" rel="stylesheet" type="text/css">
<link href="./mw/skins.vector.styles.css" rel="stylesheet" type="text/css">
<link href="./mw/user.styles.css" rel="stylesheet" type="text/css">
<meta name="ResourceLoaderDynamicStyles" content="">
<link rel="stylesheet" type="text/css" href="./mw/site.styles.css">
<link rel="stylesheet" type="text/css" href="./mw/noscript.css">
<link rel="stylesheet" type="text/css" href="./footer.css">
<link rel="stylesheet" type="text/css" href="./vector-2022.css">
</head>
<body class="skin--responsive skin-vector skin-vector-search-vue mediawiki ltr sitedir-ltr mw-hide-empty-elt ns-0 ns-subject page-FADD rootpage-FADD skin-vector-2022 action-view">
<div class="mw-page-container">
<div class="mw-page-container-inner">
<div class="mw-content-container">
<main id="content" class="mw-body">
<header class="mw-body-header vector-page-titlebar">
<h1 id="firstHeading" class="firstHeading mw-first-heading">
<span id="openzim-page-title" class="mw-page-title-main"><span class="mw-page-title-main">FADD</span></span>
</h1>
</header>
<a id="top"></a>
<div id="bodyContent" class="vector-body ve-init-mw-desktopArticleTarget-targetContainer" aria-labelledby="firstHeading" data-mw-ve-target-container="">
<div id="mw-content-text" class="mw-body-content mw-content-ltr" lang="en" dir="ltr"><div class="mw-content-ltr mw-parser-output" lang="en" dir="ltr"><p class="mw-empty-elt">
</p>

<style data-mw-deduplicate="TemplateStyles:r1236090951">
/* start https://en.wikipedia.org/ */


.mw-parser-output .hatnote{font-style:italic}.mw-parser-output div.hatnote{padding-left:1.6em;margin-bottom:0.5em}.mw-parser-output .hatnote i{font-style:normal}.mw-parser-output .hatnote+link+.hatnote{margin-top:-0.5em}@media print{body.ns-0 .mw-parser-output .hatnote{display:none!important}}


/* end https://en.wikipedia.org/ */
</style><div role="note" class="hatnote navigation-not-searchable">This article is about molecular biology. For other uses, see <a href="Fadd_(disambiguation)" class="mw-redirect mw-disambig" title="Fadd (disambiguation)">Fadd (disambiguation)</a>.</div>
<table class="infobox" style="width:26.4em"><tbody><tr><th colspan="4" style="text-align:center;font-size:125%;font-weight:bold">FADD</th></tr><tr><td colspan="4" style="text-align:center"><span typeof="mw:File"></span></td></tr><tr><td colspan="4" style="text-align:center;background-color:light-dark(#eee, #27292d) !important;color:inherit"><table style="padding:0;border:none;margin:0;width:100%;text-align:left"><tbody><tr><th colspan="4" style="text-align:center;background-color:light-dark(#ddd, #404244) !important;color:inherit">Available structures</th></tr><tr><th rowspan="2" style="background-color:light-dark(#c3fdb8, #003500) !important;color:inherit;width:43px"><a href="Protein_Data_Bank" title="Protein Data Bank">PDB</a></th><td colspan="2" style="background-color:light-dark(#eee, #27292d) !important;color:inherit">Ortholog search: <span class=""><a rel="nofollow" class="external text" href="https://www.ebi.ac.uk/pdbe/searchResults.html?display=both&amp;term=Q61160%20or%20Q13158">PDBe</a> <a rel="nofollow" class="external text" href="https://www.rcsb.org/search?q=rcsb_polymer_entity_container_identifiers.reference_sequence_identifiers.database_name:UniProt%20AND%20rcsb_polymer_entity_container_identifiers.reference_sequence_identifiers.database_accession:Q61160,Q13158">RCSB</a> </span></td></tr><tr><td><table class="collapsible collapsed" style="padding:0;border:none;margin:0;width:100%;text-align:left"><tbody><tr style="text-align:center"><th colspan="2" style="background-color:light-dark(#ddd, #404244) !important;color:inherit">List of PDB id codes</th></tr><tr><td colspan="2" style="background-color:light-dark(#eee, #27292d) !important;color:inherit"><p><span class=""><a rel="nofollow" class="external text" href="https://www.rcsb.org/structure/3OQ9">3OQ9</a>, <a rel="nofollow" class="external text" href="https://www.rcsb.org/structure/1A1W">1A1W</a>, <a rel="nofollow" class="external text" href="https://www.rcsb.org/structure/1A1Z">1A1Z</a>, <a rel="nofollow" class="external text" href="https://www.rcsb.org/structure/1E3Y">1E3Y</a>, <a rel="nofollow" class="external text" href="https://www.rcsb.org/structure/1E41">1E41</a>, <a rel="nofollow" class="external text" href="https://www.rcsb.org/structure/2GF5">2GF5</a>, <a rel="nofollow" class="external text" href="https://www.rcsb.org/structure/3EZQ">3EZQ</a></span></p></td></tr></tbody></table></td></tr></tbody></table></td></tr><tr><th colspan="4" style="text-align:center;background-color:light-dark(#ddd, #404244) !important;color:inherit">Identifiers</th></tr><tr><th scope="row" style="background-color:light-dark(#c3fdb8, #003500) !important;color:inherit"><span class=""><a href="Gene_nomenclature" title="Gene nomenclature">Aliases</a></span></th><td colspan="3" style="background:light-dark(#eee, #27292d) !important;color:inherit"><span class=""><a rel="nofollow" class="external text" href="https://www.genenames.org/data/gene-symbol-report/#!/hgnc_id/3573">FADD</a></span>, GIG3, MORT1, Fas associated via death domain, IMD90</td></tr><tr><th scope="row" style="background-color:light-dark(#c3fdb8, #003500) !important;color:inherit">External IDs</th><td colspan="3" style="background-color:light-dark(#eee, #27292d) !important;color:inherit"><span class=""><a href="Mendelian_Inheritance_in_Man" class="mw-redirect" title="Mendelian Inheritance in Man">OMIM</a>: <a rel="nofollow" class="external text" href="https://omim.org/entry/602457">602457</a>; <a href="Mouse_Genome_Informatics" title="Mouse Genome Informatics">MGI</a>: <a rel="nofollow" class="external text" href="http://www.informatics.jax.org/marker/MGI:109324">109324</a>; <a href="HomoloGene" title="HomoloGene">HomoloGene</a>: <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&amp;db=homologene&amp;dopt=HomoloGene&amp;list_uids=2836">2836</a>; <a href="GeneCards" title="GeneCards">GeneCards</a>: <a rel="nofollow" class="external text" href="https://www.genecards.org/cgi-bin/carddisp.pl?gene=FADD">FADD</a>; <a href="Orthologous_MAtrix" title="Orthologous MAtrix">OMA</a>:<a rel="nofollow" class="external text" href="https://omabrowser.org/oma/vps/ENSG00000168040">FADD - orthologs</a></span></td></tr><tr><td colspan="4" style="text-align:center;background-color:light-dark(#eee, #27292d) !important;color:inherit"><table class="collapsible collapsed" style="padding:0;border:none;margin:0;width:100%;text-align:left"><tbody><tr><th colspan="4" style="text-align:center;background-color:light-dark(#ddd, #404244) !important;color:inherit">Gene location (<a href="Human_genome" title="Human genome">Human</a>)</th></tr><tr><td colspan="4" style="text-align:center;background-color:light-dark(#eee, #27292d) !important;color:inherit"><span typeof="mw:File"></span></td></tr><tr><th scope="row" width="15%" style="background-color:light-dark(#c3fdb8, #003500) !important;color:inherit"><a href="Chromosome" title="Chromosome">Chr.</a></th><td colspan="3" width="85%" style="background-color:light-dark(#eee, #27292d) !important;color:inherit"><span class=""><a href="Chromosome_11_(human)" class="mw-redirect" title="Chromosome 11 (human)">Chromosome 11 (human)</a><sup id="cite_ref-refGRCh38Ensembl_1-0" class="reference"><a href="#cite_note-refGRCh38Ensembl-1"><span class="cite-bracket">[</span>1<span class="cite-bracket">]</span></a></sup></span></td></tr><tr><td colspan="4" style="text-align:center;background-color:light-dark(#eee, #27292d) !important;color:inherit"><div align="center"><div style="position: relative; width: 300px;"><span typeof="mw:File"></span><div style="position: absolute; left: 147.46282155821px; top: 2px; padding: 0;"><span typeof="mw:File"></span></div><div style="position: absolute; left: 153.5px; top: 19px; padding: 0;"><span typeof="mw:File"></span></div></div></div></td></tr><tr><th scope="row" rowspan="2" width="15%" style="background-color:light-dark(#c3fdb8, #003500) !important;color:inherit"><a href="Locus_(genetics)" title="Locus (genetics)">Band</a></th><td rowspan="2" width="35%" style="background-color:light-dark(#eee, #27292d) !important;color:inherit"><span class="">11q13.3</span></td><th scope="row" style="background-color:light-dark(#c3fdb8, #003500) !important;color:inherit">Start</th><td style="background-color:light-dark(#eee, #27292d) !important;color:inherit"><span class="">70,203,296 <a href="Base_pair" title="Base pair">bp</a><sup id="cite_ref-refGRCh38Ensembl_1-1" class="reference"><a href="#cite_note-refGRCh38Ensembl-1"><span class="cite-bracket">[</span>1<span class="cite-bracket">]</span></a></sup></span></td></tr><tr><th scope="row" style="background-color:light-dark(#c3fdb8, #003500) !important;color:inherit">End</th><td style="background-color:light-dark(#eee, #27292d) !important;color:inherit"><span class="">70,207,390 <a href="Base_pair" title="Base pair">bp</a><sup id="cite_ref-refGRCh38Ensembl_1-2" class="reference"><a href="#cite_note-refGRCh38Ensembl-1"><span class="cite-bracket">[</span>1<span class="cite-bracket">]</span></a></sup></span></td></tr></tbody></table></td></tr><tr><td colspan="4" style="text-align:center;background-color:light-dark(#eee, #27292d) !important;color:inherit"><table class="collapsible collapsed" style="padding:0;border:none;margin:0;width:100%;text-align:left"><tbody><tr><th colspan="4" style="text-align:center;background-color:light-dark(#ddd, #404244) !important;color:inherit"><a href="Gene_expression" title="Gene expression">RNA expression</a> pattern</th></tr><tr><th scope="row" style="background-color:light-dark(#c3fdb8, #003500) !important;color:inherit"><a rel="nofollow" class="external text" href="https://www.bgee.org/">Bgee</a></th><td><table class="none" style="padding:0;border:none;margin:0;width:100%;text-align:left"><tbody><tr><th><b><a href="Human_genome" title="Human genome">Human</a></b></th><th><b><a href="Laboratory_mouse" title="Laboratory mouse">Mouse</a> (ortholog)</b></th></tr><tr><td><table class="none" style="padding:0;border:none;margin:0;width:100%;text-align:center"><tbody><tr><td colspan="1"><span class="" style="margin:-3px"><a rel="nofollow" class="external text" href="https://www.bgee.org/gene/ENSG00000168040">Top expressed in</a></span></td></tr><tr><td colspan="1"><div class="" style="margin:-12px 0px -10px 0px"><ul style="line-height:15%;margin:9px"><li style="line-height: 137%;">granulocyte</li><br><li style="line-height: 137%;">tendon of biceps brachii</li><br><li style="line-height: 137%;">stromal cell of endometrium</li><br><li style="line-height: 137%;">mucosa of transverse colon</li><br><li style="line-height: 137%;">blood</li><br><li style="line-height: 137%;">parotid gland</li><br><li style="line-height: 137%;">right adrenal gland</li><br><li style="line-height: 137%;">right adrenal cortex</li><br><li style="line-height: 137%;">left adrenal gland</li><br><li style="line-height: 137%;">epithelium of esophagus</li></ul></div></td></tr></tbody></table></td><td><table class="none" style="padding:0;border:none;margin:0;width:100%;text-align:center"><tbody><tr><td colspan="1"></td></tr><tr><td colspan="1"><div class="" style="margin:-12px 0px -10px 0px"><ul style="line-height:15%;margin:9px">n/a</ul></div></td></tr></tbody></table></td></tr><tr><td colspan="4" style="text-align:center;background-color:light-dark(#eee, #27292d) !important;color:inherit"><span class=""><a rel="nofollow" class="external text" href="https://www.bgee.org/gene/ENSG00000168040">More reference expression data</a></span></td></tr></tbody></table></td></tr><tr><th scope="row" style="background-color:light-dark(#c3fdb8, #003500) !important;color:inherit"><a rel="nofollow" class="external text" href="http://biogps.org/">BioGPS</a></th><td><table class="none" style="padding:0;border:none;margin:0;width:100%;text-align:left"><tbody><tr><td colspan="4" style="text-align:center;background-color:light-dark(#eee, #27292d) !important;color:inherit"><span typeof="mw:File"></span></td></tr><tr><td colspan="4" style="text-align:center;background-color:light-dark(#eee, #27292d) !important;color:inherit"><span class=""><a rel="nofollow" class="external text" href="http://biogps.org/gene/8772/">More reference expression data</a></span></td></tr></tbody></table></td></tr></tbody></table></td></tr><tr><td colspan="4" style="text-align:center;background-color:light-dark(#eee, #27292d) !important;color:inherit"><table class="collapsible collapsed" style="padding:0;border:none;margin:0;width:100%;text-align:left"><tbody><tr><th colspan="4" style="text-align:center;background-color:light-dark(#ddd, #404244) !important;color:inherit"><a href="Gene_ontology" class="mw-redirect" title="Gene ontology">Gene ontology</a></th></tr><tr><td style="background-color:light-dark(#c3fdb8, #003500) !important;color:inherit;font-weight:bold">Molecular function</td><td style="background-color:light-dark(#eee, #27292d) !important;color:inherit"><div class="">
<ul><li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0042802">identical protein binding</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0032813">tumor necrosis factor receptor superfamily binding</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0035877">death effector domain binding</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0089720">caspase binding</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0005515">protein binding</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0002020">protease binding</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0005123">death receptor binding</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0005164">tumor necrosis factor receptor binding</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0033612">receptor serine/threonine kinase binding</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0044877">protein-containing complex binding</a></li></ul>
</div></td></tr><tr><td style="background-color:light-dark(#c3fdb8, #003500) !important;color:inherit;font-weight:bold">Cellular component</td><td style="background-color:light-dark(#eee, #27292d) !important;color:inherit"><div class="">
<ul><li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0005829">cytosol</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0045121">membrane raft</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0097342">ripoptosome</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0044297">cell body</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0043005">neuron projection</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0031265">CD95 death-inducing signaling complex</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0005886">plasma membrane</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0031264">death-inducing signaling complex</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0005737">cytoplasm</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0005634">nucleus</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0032991">protein-containing complex</a></li></ul>
</div></td></tr><tr><td style="background-color:light-dark(#c3fdb8, #003500) !important;color:inherit;font-weight:bold">Biological process</td><td style="background-color:light-dark(#eee, #27292d) !important;color:inherit"><div class="">
<ul><li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0036462">TRAIL-activated apoptotic signaling pathway</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:1902041">regulation of extrinsic apoptotic signaling pathway via death domain receptors</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0097049">motor neuron apoptotic process</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0002376">immune system process</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0097527">necroptotic signaling pathway</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0006919">activation of cysteine-type endopeptidase activity involved in apoptotic process</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0060546">negative regulation of necroptotic process</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0032757">positive regulation of interleukin-8 production</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0060340">positive regulation of type I interferon-mediated signaling pathway</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0007166">cell surface receptor signaling pathway</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0035666">TRIF-dependent toll-like receptor signaling pathway</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0045651">positive regulation of macrophage differentiation</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0051607">defense response to virus</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0097202">activation of cysteine-type endopeptidase activity</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0097190">apoptotic signaling pathway</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0071260">cellular response to mechanical stimulus</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0097192">extrinsic apoptotic signaling pathway in absence of ligand</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0045944">positive regulation of transcription by RNA polymerase II</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0008625">extrinsic apoptotic signaling pathway via death domain receptors</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0042981">regulation of apoptotic process</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0071550">death-inducing signaling complex assembly</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:1902043">positive regulation of extrinsic apoptotic signaling pathway via death domain receptors</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0032760">positive regulation of tumor necrosis factor production</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0043123">positive regulation of I-kappaB kinase/NF-kappaB signaling</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0007165">signal transduction</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0045862">positive regulation of proteolysis</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0016032">viral process</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0006915">apoptotic process</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0042104">positive regulation of activated T cell proliferation</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0097191">extrinsic apoptotic signaling pathway</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0001916">positive regulation of T cell mediated cytotoxicity</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:2001238">positive regulation of extrinsic apoptotic signaling pathway</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0048538">thymus development</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0002821">positive regulation of adaptive immune response</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0033077">T cell differentiation in thymus</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0045087">innate immune response</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0048536">spleen development</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0070236">negative regulation of activation-induced cell death of T cells</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:1902042">negative regulation of extrinsic apoptotic signaling pathway via death domain receptors</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0032729">positive regulation of interferon-gamma production</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:2000454">positive regulation of CD8-positive, alpha-beta cytotoxic T cell extravasation</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0048535">lymph node development</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0043029">T cell homeostasis</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0042220">response to cocaine</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0043278">response to morphine</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0048148">behavioral response to cocaine</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0060544">regulation of necroptotic process</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0043065">positive regulation of apoptotic process</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0034138">toll-like receptor 3 signaling pathway</a></li>
<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0001822">kidney development</a></li></ul>
</div></td></tr><tr><td colspan="4" style="background-color:light-dark(#eee, #27292d) !important;color:inherit;text-align:center">Sources:<a rel="nofollow" class="external text" href="http://amigo.geneontology.org/">Amigo</a> / <a rel="nofollow" class="external text" href="https://www.ebi.ac.uk/QuickGO/">QuickGO</a></td></tr></tbody></table></td></tr><tr><td colspan="4" style="text-align:center;background-color:light-dark(#eee, #27292d) !important;color:inherit"><table class="collapsible" style="padding:0;border:none;margin:0;width:100%;text-align:left"><tbody><tr><th colspan="4" style="text-align:center;background-color:light-dark(#ddd, #404244) !important;color:inherit"><a href="Orthologs" class="mw-redirect" title="Orthologs">Orthologs</a></th></tr><tr><th scope="row" style="background-color:light-dark(#c3fdb8, #003500) !important;color:inherit">Species</th><td><b>Human</b></td><td><b>Mouse</b></td></tr><tr><th scope="row" style="background-color:light-dark(#c3fdb8, #003500) !important;color:inherit"><a href="Entrez" title="Entrez">Entrez</a></th><td><table class="none" style="padding:0;border:none;margin:0;width:100%;text-align:right"><tbody><tr><th colspan="1"></th></tr><tr><td colspan="1"><p class=""><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=gene&amp;cmd=retrieve&amp;dopt=default&amp;list_uids=8772&amp;rn=1">8772</a></p></td></tr></tbody></table></td><td><table class="none" style="padding:0;border:none;margin:0;width:100%;text-align:right"><tbody><tr><th colspan="1"></th></tr><tr><td colspan="1"><p class=""><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=gene&amp;cmd=retrieve&amp;dopt=default&amp;list_uids=14082&amp;rn=1">14082</a></p></td></tr></tbody></table></td></tr><tr><th scope="row" style="background-color:light-dark(#c3fdb8, #003500) !important;color:inherit"><a href="Ensembl" class="mw-redirect" title="Ensembl">Ensembl</a></th><td><table class="none" style="padding:0;border:none;margin:0;width:100%;text-align:right"><tbody><tr><th colspan="1"></th></tr><tr><td colspan="1"><p class=""><a rel="nofollow" class="external text" href="http://www.ensembl.org/Homo_sapiens/geneview?gene=ENSG00000168040;db=core">ENSG00000168040</a></p></td></tr></tbody></table></td><td><table class="none" style="padding:0;border:none;margin:0;width:100%;text-align:right"><tbody><tr><th colspan="1"></th></tr><tr><td colspan="1"><p class=""><a rel="nofollow" class="external text" href="http://www.ensembl.org/Mus_musculus/geneview?gene=ENSMUSG00000031077;db=core">ENSMUSG00000031077</a></p></td></tr></tbody></table></td></tr><tr><th scope="row" style="background-color:light-dark(#c3fdb8, #003500) !important;color:inherit"><a href="UniProt" title="UniProt">UniProt</a></th><td><table class="none" style="padding:0;border:none;margin:0;width:100%;text-align:right"><tbody><tr><th colspan="1"></th></tr><tr><td colspan="1"><p class=""><a rel="nofollow" class="external text" href="https://www.uniprot.org/uniprot/Q13158">Q13158</a></p></td></tr></tbody></table></td><td><table class="none" style="padding:0;border:none;margin:0;width:100%;text-align:right"><tbody><tr><th colspan="1"></th></tr><tr><td colspan="1"><p class=""><a rel="nofollow" class="external text" href="https://www.uniprot.org/uniprot/Q61160">Q61160</a></p></td></tr></tbody></table></td></tr><tr><th scope="row" style="background-color:light-dark(#c3fdb8, #003500) !important;color:inherit">RefSeq (mRNA)</th><td><table class="none" style="padding:0;border:none;margin:0;width:100%;text-align:right"><tbody><tr><th colspan="1" class=""></th></tr><tr><td colspan="1"><p><span class=""><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?val=NM_003824">NM_003824</a></span></p></td></tr></tbody></table></td><td><table class="none" style="padding:0;border:none;margin:0;width:100%;text-align:right"><tbody><tr><th colspan="1" class=""></th></tr><tr><td colspan="1"><p><span class=""><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?val=NM_010175">NM_010175</a></span></p></td></tr></tbody></table></td></tr><tr><th scope="row" style="background-color:light-dark(#c3fdb8, #003500) !important;color:inherit">RefSeq (protein)</th><td><table class="none" style="padding:0;border:none;margin:0;width:100%;text-align:right"><tbody><tr><th colspan="1" class=""></th></tr><tr><td colspan="1"><p><span class=""><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?val=NP_003815">NP_003815</a></span></p></td></tr></tbody></table></td><td><table class="none" style="padding:0;border:none;margin:0;width:100%;text-align:right"><tbody><tr><th colspan="1" class=""></th></tr><tr><td colspan="1"><p><span class=""><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?val=NP_034305">NP_034305</a></span></p></td></tr></tbody></table></td></tr><tr><th scope="row" style="background-color:light-dark(#c3fdb8, #003500) !important;color:inherit">Location (UCSC)</th><td><span class=""><a rel="nofollow" class="external text" href="https://genome.ucsc.edu/cgi-bin/hgTracks?org=Human&amp;db=hg38&amp;position=chr11:70203296-70207390">Chr 11: 70.2 – 70.21 Mb</a></span></td><td><span class="">n/a</span></td></tr><tr><th scope="row" style="background-color:light-dark(#c3fdb8, #003500) !important;color:inherit"><a href="PubMed" title="PubMed">PubMed</a> search</th><td><span class=""><sup id="cite_ref-2" class="reference"><a href="#cite_note-2"><span class="cite-bracket">[</span>2<span class="cite-bracket">]</span></a></sup></span></td><td><span class=""><sup id="cite_ref-3" class="reference"><a href="#cite_note-3"><span class="cite-bracket">[</span>3<span class="cite-bracket">]</span></a></sup></span></td></tr></tbody></table></td></tr><tr><td colspan="4" style="text-align:center;background-color:light-dark(#eee, #27292d) !important;color:inherit"><a href="Wikidata" title="Wikidata">Wikidata</a></td></tr><tr><td colspan="4" style="text-align:center;background-color:light-dark(#eee, #27292d) !important;color:inherit"><table style="padding:0;border:none;margin:0;width:100%;text-align:center"><tbody><tr><td colspan="2" style="background-color:light-dark(#eee, #27292d) !important;color:inherit;text-align:center"><a href="https://www.wikidata.org/wiki/Q14907137" class="extiw external" title="d:Q14907137">View/Edit Human</a></td><td colspan="2" style="background-color:light-dark(#eee, #27292d) !important;color:inherit;text-align:center"><a href="https://www.wikidata.org/wiki/Q14907138" class="extiw external" title="d:Q14907138">View/Edit Mouse</a></td></tr></tbody></table></td></tr></tbody></table>
<p><b>FAS-associated death domain protein</b>, also called <b>MORT1</b>, is encoded by the <i><b>FADD</b></i> gene on the 11q13.3 region of chromosome 11 in humans.<sup id="cite_ref-Kim1996_4-0" class="reference"><a href="#cite_note-Kim1996-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup>
</p><p>FADD is an <a href="Signal_transducing_adaptor_protein" title="Signal transducing adaptor protein">adaptor protein</a> that bridges members of the <a href="Tumor_necrosis_factor_receptor" class="mw-redirect" title="Tumor necrosis factor receptor">tumor necrosis factor receptor superfamily</a>, such as the <a href="FasR" class="mw-redirect" title="FasR">Fas-receptor</a>, to <a href="Caspase_8" title="Caspase 8">procaspases 8</a> and <a href="Caspase_10" title="Caspase 10">10</a> to form the <a href="Death-inducing_signaling_complex" title="Death-inducing signaling complex">death-inducing signaling complex</a> (DISC) during <a href="Apoptosis" title="Apoptosis">apoptosis</a>. As well as its most well known role in apoptosis, FADD has also been seen to play a role in other processes including proliferation, cell cycle regulation and development.
</p>
<meta property="mw:PageProp/toc">
<div class="mw-heading mw-heading2"><h2 id="Structure">Structure</h2></div>
<p>FADD is a 23 kDa protein, made up of 208 amino acids. It contains two main domains: a C terminal <a href="Death_domain" title="Death domain">death domain</a> (DD) and an N terminal <a href="Death_effector_domain" title="Death effector domain">death effector domain</a> (DED). Each domain, although sharing very little sequence similarity, are structurally similar to one another, with each consisting of 6 α helices.<sup id="cite_ref-Huang1996_5-0" class="reference"><a href="#cite_note-Huang1996-5"><span class="cite-bracket">[</span>5<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-Eberstadt1998_6-0" class="reference"><a href="#cite_note-Eberstadt1998-6"><span class="cite-bracket">[</span>6<span class="cite-bracket">]</span></a></sup> The DD of FADD binds to receptors such as the Fas receptor at the plasma membrane via their DD.<sup id="cite_ref-Boldin1995_7-0" class="reference"><a href="#cite_note-Boldin1995-7"><span class="cite-bracket">[</span>7<span class="cite-bracket">]</span></a></sup> The interaction between the death domains are <a href="Electrostatic_interactions" class="mw-redirect" title="Electrostatic interactions">electrostatic interactions</a> involving α helices 2 and 3 of the 6 helix domain.<sup id="cite_ref-Jeong1999_8-0" class="reference"><a href="#cite_note-Jeong1999-8"><span class="cite-bracket">[</span>8<span class="cite-bracket">]</span></a></sup> The DED binds to the DED of intracellular molecules such as procaspase 8.<sup id="cite_ref-Boldin1996_9-0" class="reference"><a href="#cite_note-Boldin1996-9"><span class="cite-bracket">[</span>9<span class="cite-bracket">]</span></a></sup> It is thought that this interaction occurs through <a href="Hydrophobic_effect" title="Hydrophobic effect">hydrophobic interactions</a>.<sup id="cite_ref-Eberstadt1998_6-1" class="reference"><a href="#cite_note-Eberstadt1998-6"><span class="cite-bracket">[</span>6<span class="cite-bracket">]</span></a></sup>
</p>
<div class="mw-heading mw-heading2"><h2 id="Functions">Functions</h2></div>
<div class="mw-heading mw-heading3"><h3 id="Extrinsic_apoptosis">Extrinsic apoptosis</h3></div>
<p>Upon stimulation by the <a href="Fas_ligand" title="Fas ligand">Fas ligand</a>, the Fas receptor trimerises. Many receptors, including Fas, contain a cytoplasmic DD and are therefore named <a href="Tumor_necrosis_factor_receptor" class="mw-redirect" title="Tumor necrosis factor receptor">death receptors</a>. FADD binds to the DD of this trimeric structure via its death domain <sup id="cite_ref-Boldin1995_7-1" class="reference"><a href="#cite_note-Boldin1995-7"><span class="cite-bracket">[</span>7<span class="cite-bracket">]</span></a></sup> resulting in unmasking of FADD's DED and subsequent recruitment of procaspase 8 and 10 via an interaction between the DEDs of both FADD and the procaspases.<sup id="cite_ref-Kischkel2001_10-0" class="reference"><a href="#cite_note-Kischkel2001-10"><span class="cite-bracket">[</span>10<span class="cite-bracket">]</span></a></sup> This generates a complex known as the death inducing signalling complex (DISC).<sup id="cite_ref-Kischkel1995_11-0" class="reference"><a href="#cite_note-Kischkel1995-11"><span class="cite-bracket">[</span>11<span class="cite-bracket">]</span></a></sup> Procaspase 8 and 10 are known as initiator <a href="Caspases" class="mw-redirect" title="Caspases">caspases</a>. These are inactive molecules, but when bought into close proximity with other procaspases of the same type, autocatalytic cleavage occurs at an <a href="Aspartic_acid" title="Aspartic acid">aspartate</a> residue within their own structures, resulting in an activated protein. This activated protein can then go on to cleave and activate further caspases, initiating the <a href="Caspase#caspase_cascade" title="Caspase">caspase cascade</a>.<sup id="cite_ref-Weinlich2011_12-0" class="reference"><a href="#cite_note-Weinlich2011-12"><span class="cite-bracket">[</span>12<span class="cite-bracket">]</span></a></sup> The activated caspases can go on to cleave intracellular proteins such as <a href="DFFA" title="DFFA">inhibitor of caspase-activated DNase</a> (ICAD), which ultimately leads to apoptosis of the cell.<sup id="cite_ref-Lee2012_13-0" class="reference"><a href="#cite_note-Lee2012-13"><span class="cite-bracket">[</span>13<span class="cite-bracket">]</span></a></sup>
</p><p>Binding of <a href="TRAIL" title="TRAIL">TRAIL</a> to death receptors four and five (<a href="TNFRSF10A" class="mw-redirect" title="TNFRSF10A">DR4</a> and <a href="TNFRSF10B" class="mw-redirect" title="TNFRSF10B">DR5</a>) can lead to apoptosis by the same mechanism.<sup id="cite_ref-Bodmer2000_14-0" class="reference"><a href="#cite_note-Bodmer2000-14"><span class="cite-bracket">[</span>14<span class="cite-bracket">]</span></a></sup>
</p><p>Apoptosis can also be triggered by binding of a ligand to <a href="CD120" title="CD120">tumor necrosis factor receptor 1</a> (TNFR1); however, the mechanism by which this occurs is slightly more complex. Another DD-containing adaptor protein named <a href="TRADD" title="TRADD">TRADD</a>, along with other proteins, binds to activated TNF1R, forming what is known as complex I. This results in activation of the <a href="NF%CE%BAB" class="mw-redirect" title="NFκB">NFκB</a> pathway, which promotes cell survival. This complex is then internalised, and FADD binds to TRADD via an interaction of the DD's of the two adapter proteins, forming what is known as complex II. FADD again recruits procaspase 8, which initiates the caspase cascade leading to apoptosis.<sup id="cite_ref-micheau2003_15-0" class="reference"><a href="#cite_note-micheau2003-15"><span class="cite-bracket">[</span>15<span class="cite-bracket">]</span></a></sup>
</p>

<div class="mw-heading mw-heading3"><h3 id="Necroptosis">Necroptosis</h3></div>
<p>FADD also plays a role in regulating <a href="Necroptosis" title="Necroptosis">necroptosis</a>, a process requiring the <a href="Serine/threonine-specific_protein_kinase" title="Serine/threonine-specific protein kinase">serine/threonine kinases</a>, <a href="RIPK1" title="RIPK1">RIPK1</a> and <a href="RIPK3" title="RIPK3">RIPK3</a>. Activated caspase 8 cleaves these <a href="Kinases" class="mw-redirect" title="Kinases">kinases</a>, inhibiting necroptosis. Since activation of caspase 8 requires FADD in order to bring the procaspase 8 molecules into close proximity to one another to facilitate their activation, FADD is required for negatively regulating necroptosis. In accordance, cells deficient in FADD induce necroptosis as they are unable to recruit and activate procaspase 8.
FADD can also bind to RIPK1 and RIPK3 directly, however the significance of this interaction is currently unclear.<sup id="cite_ref-Lee2012_13-1" class="reference"><a href="#cite_note-Lee2012-13"><span class="cite-bracket">[</span>13<span class="cite-bracket">]</span></a></sup>
</p>
<div class="mw-heading mw-heading3"><h3 id="Autophagic_cell_death">Autophagic cell death</h3></div>
<p><a href="Autophagy" title="Autophagy">Autophagy</a> is a process which allows cell survival under stressed conditions but can also lead to cell death.
</p><p>Using its DD, FADD interacts with <a href="ATG5" class="mw-redirect" title="ATG5">ATG5</a>, a protein involved in autophagy. This interaction has been shown to be essential for autophagic cell death, which is induced by <a href="IFN-%CE%B3" class="mw-redirect" title="IFN-γ">IFN-γ</a>.<sup id="cite_ref-Pyo2005_16-0" class="reference"><a href="#cite_note-Pyo2005-16"><span class="cite-bracket">[</span>16<span class="cite-bracket">]</span></a></sup>
</p><p>In contrast, it has also been found to inhibit autophagic cell death and therefore promote cell survival. FADD binds to ATG5 in a complex which also contains <a href="ATG12" title="ATG12">ATG12</a>, Caspase 8 and RIPK1. The formation of this complex is stimulated by autophagic signalling. Caspase 8 then cleaves RIPK1, leading to inhibition of this signalling, inhibiting cell death.<sup id="cite_ref-Bell2008_17-0" class="reference"><a href="#cite_note-Bell2008-17"><span class="cite-bracket">[</span>17<span class="cite-bracket">]</span></a></sup>
</p>
<div class="mw-heading mw-heading3"><h3 id="Development">Development</h3></div>
<p>FADD knockout in mouse embryos is lethal, showing a role for FADD in <a href="Embryogenesis" class="mw-redirect" title="Embryogenesis">embryonic development</a>. This is thought to be due to abnormal development of the <a href="Heart" title="Heart">heart</a>.<sup id="cite_ref-Yeh1998_18-0" class="reference"><a href="#cite_note-Yeh1998-18"><span class="cite-bracket">[</span>18<span class="cite-bracket">]</span></a></sup> This abnormal heart development may be due to FADD dependent regulation of the NFκB pathway.<sup id="cite_ref-Sakamaki2012_19-0" class="reference"><a href="#cite_note-Sakamaki2012-19"><span class="cite-bracket">[</span>19<span class="cite-bracket">]</span></a></sup>
</p><p>FADD also plays a role in the development of the <a href="Eyes" class="mw-redirect" title="Eyes">eyes</a> of <a href="Zebrafish" title="Zebrafish">zebrafish</a>.<sup id="cite_ref-Gregory-Evans2007_20-0" class="reference"><a href="#cite_note-Gregory-Evans2007-20"><span class="cite-bracket">[</span>20<span class="cite-bracket">]</span></a></sup>
</p>
<div class="mw-heading mw-heading3"><h3 id="Cell_cycle_regulation">Cell cycle regulation</h3></div>
<p>FADD is thought to have a role in regulating the cell cycle of <a href="T_cell" title="T cell">T lymphocytes</a>. This regulation is dependent on phosphorylation of FADD on Serine 194, which is carried out by <a href="Casein_kinase_1%2C_alpha_1" title="Casein kinase 1, alpha 1">Casein Kinase 1a</a> (CKIα). This phosphorylated form of FADD is found mainly in the <a href="Cell_nucleus" title="Cell nucleus">nucleus</a> and the abundance of phosphorylated FADD increases significantly in the <a href="G2_phase" title="G2 phase">G2 phase</a> of the <a href="Cell_cycle" title="Cell cycle">cell cycle</a> compared to the <a href="G1_phase" title="G1 phase">G1 phase</a> where only very little can be detected. As it is found at the <a href="Spindle_apparatus" title="Spindle apparatus">mitotic spindle</a> during G2, it has been proposed to mediate the G2/M transition, however, the mechanism by which it does this it not yet known.<sup id="cite_ref-Alappat2005_21-0" class="reference"><a href="#cite_note-Alappat2005-21"><span class="cite-bracket">[</span>21<span class="cite-bracket">]</span></a></sup>
</p>
<div class="mw-heading mw-heading3"><h3 id="Lymphocyte_proliferation">Lymphocyte proliferation</h3></div>
<p>FADD is essential for <a href="T_cell" title="T cell">T cell</a> proliferation when the <a href="T_cell_receptor" class="mw-redirect" title="T cell receptor">T cell receptor</a> is stimulated by <a href="Antigen" title="Antigen">antigen</a>.<sup id="cite_ref-Zhang1998_22-0" class="reference"><a href="#cite_note-Zhang1998-22"><span class="cite-bracket">[</span>22<span class="cite-bracket">]</span></a></sup> In contrast, FADD has no effect on the proliferation of <a href="B_cells" class="mw-redirect" title="B cells">B cells</a> induced by stimulation of the <a href="B_cell_receptor" class="mw-redirect" title="B cell receptor">B cell receptor</a>. However, it is required for B cell proliferation induced by stimulation of <a href="TLR3" class="mw-redirect" title="TLR3">TLR3</a> and <a href="TLR4" class="mw-redirect" title="TLR4">TLR4</a>.<sup id="cite_ref-Imtiyaz2006_23-0" class="reference"><a href="#cite_note-Imtiyaz2006-23"><span class="cite-bracket">[</span>23<span class="cite-bracket">]</span></a></sup>
</p>
<div class="mw-heading mw-heading3"><h3 id="Inflammation">Inflammation</h3></div>
<p>Activation of nuclear factor kappa B (NFκB) signalling leads to <a href="Transcription_(genetics)" class="mw-redirect" title="Transcription (genetics)">transcription</a> of various <a href="Proinflammatory_cytokines" class="mw-redirect" title="Proinflammatory cytokines">proinflammatory cytokines</a> as well as anti-apoptotic genes. It was found that NFκB signalling was inhibited in FADD-deficient cells after stimulation of the TNF-R1 or Fas receptors. This suggests a role of FADD in activation of the NFκB pathway. Conversely, FADD also has a role in inhibition of this pathway. Normally, upon stimulation of the receptors TL4 or <a href="Interleukin_1_receptor%2C_type_I" title="Interleukin 1 receptor, type I">IL-1R1</a>, the adaptor protein, <a href="MyD88" class="mw-redirect" title="MyD88">MyD88</a>, is recruited to the <a href="Cell_membrane" title="Cell membrane">plasma membrane</a> where is binds to <a href="IRAK1" title="IRAK1">IL-1 receptor associated Kinase</a> (IRAK) via a DD-DD interaction. This activates a signalling pathway which results in translocation of NFκB to the nucleus, where it induces the transcription of the inflammatory cytokines. FADD can interfere with the interaction between MyD88 and IRAK, by binding to MyD88 via its DD and therefore this disrupts the cascade which would lead to NFκB translocation and inflammation.<sup id="cite_ref-Wajant2000_24-0" class="reference"><a href="#cite_note-Wajant2000-24"><span class="cite-bracket">[</span>24<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-Tourneur2010_25-0" class="reference"><a href="#cite_note-Tourneur2010-25"><span class="cite-bracket">[</span>25<span class="cite-bracket">]</span></a></sup>
</p>
<div class="mw-heading mw-heading3"><h3 id="Other">Other</h3></div>
<p>FADD is required for an efficient antiviral response. Upon viral infection, FADD is needed to increase the levels of <a href="IRF7" title="IRF7">Irf7</a> a molecule which is needed for the production of <a href="Interferon_type_I" title="Interferon type I">IFN-α</a>. IFN-α is a key molecule involved in the response against <a href="Viruses" class="mw-redirect" title="Viruses">viruses</a>.<sup id="cite_ref-Balachandran2007_26-0" class="reference"><a href="#cite_note-Balachandran2007-26"><span class="cite-bracket">[</span>26<span class="cite-bracket">]</span></a></sup>
</p><p>FADD is involved in the activation of the <a href="Phosphatases" class="mw-redirect" title="Phosphatases">phosphatases</a> which dephosphorylate and deactivate <a href="Protein_Kinase_C" class="mw-redirect" title="Protein Kinase C">Protein Kinase C</a> (PKC). Without FADD, PKC remains active and is able to continue signalling cascades leading to processes including cytoskeletal rearrangements and <a href="Cell_migration" title="Cell migration">cell motility</a>.<sup id="cite_ref-Cheng2012_27-0" class="reference"><a href="#cite_note-Cheng2012-27"><span class="cite-bracket">[</span>27<span class="cite-bracket">]</span></a></sup>
</p><p>Recent research has also shown that it may have a role in regulating <a href="Glucose" title="Glucose">glucose</a> levels and the phosphorylated form of FADD is important for this function.<sup id="cite_ref-Yao2013_28-0" class="reference"><a href="#cite_note-Yao2013-28"><span class="cite-bracket">[</span>28<span class="cite-bracket">]</span></a></sup>
</p>
<div class="mw-heading mw-heading2"><h2 id="Regulation">Regulation</h2></div>

<div class="mw-heading mw-heading3"><h3 id="Subcellular_localisation">Subcellular localisation</h3></div>
<p>FADD can be found in both the nucleus and <a href="Cytoplasm" title="Cytoplasm">cytoplasm</a> of cells. Phosphorylation of Ser194 of FADD in humans (or Ser191 in mice) is thought to regulate its subcellular localisation. A <a href="Nuclear_localization_sequence" title="Nuclear localization sequence">nuclear localization sequence</a> and <a href="Nuclear_export_signal" title="Nuclear export signal">nuclear export signal</a>, both located in the DED of FADD, are also required for it to enter and exit the nucleus.
Depending on its <a href="Subcellular_localisation" class="mw-redirect" title="Subcellular localisation">subcellular localisation</a>, FADD can have different roles. In the cytoplasm, its main function is to induce apoptosis. However, in the nucleus, it can have the opposite effect and instead promote survival.<sup id="cite_ref-Tourneur2010_25-1" class="reference"><a href="#cite_note-Tourneur2010-25"><span class="cite-bracket">[</span>25<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-Gomez-Angelats2003_29-0" class="reference"><a href="#cite_note-Gomez-Angelats2003-29"><span class="cite-bracket">[</span>29<span class="cite-bracket">]</span></a></sup>
</p>
<div class="mw-heading mw-heading3"><h3 id="c-FLIP">c-FLIP</h3></div>
<p><a href="CFLAR" title="CFLAR">Cellular FLICE inhibitory protein</a> (c-FLIP) is a regulatory protein which contains two DEDs. There are two isoforms of C-FLIP: C-FLIP<sub>S</sub> and FLIP<sub>L</sub>. It was originally thought to act as a negative regulator of apoptosis by binding to the DED of FADD and therefore preventing procaspase 8 from binding and inhibiting formation of the DISC.<sup id="cite_ref-Krueger2001_30-0" class="reference"><a href="#cite_note-Krueger2001-30"><span class="cite-bracket">[</span>30<span class="cite-bracket">]</span></a></sup>
However, it has been seen that both c-FLIP and procaspase 8 can be found at the same DISC.<sup id="cite_ref-Scaffidi1999_31-0" class="reference"><a href="#cite_note-Scaffidi1999-31"><span class="cite-bracket">[</span>31<span class="cite-bracket">]</span></a></sup> Therefore, it has been proposed that the presence of c-FLIP inhibits the close interaction of the procaspases to one another. Without this close proximity, the procaspases cannot be completely cleaved and remain in an inactive state.<sup id="cite_ref-Krueger2001_30-1" class="reference"><a href="#cite_note-Krueger2001-30"><span class="cite-bracket">[</span>30<span class="cite-bracket">]</span></a></sup>
</p>
<div class="mw-heading mw-heading3"><h3 id="PKC">PKC</h3></div>
<p>The activity of protein kinase C has a negative effect on Fas receptor mediated apoptosis. This is because it inhibits the recruitment of FADD to the receptor and so a DISC is not formed. It has been shown that by either increasing or decreasing the amount of PKC in T cells, more or less FADD is recruited to FasR respectively, when the FasR is stimulated.<sup id="cite_ref-Gomez-Angelats2001_32-0" class="reference"><a href="#cite_note-Gomez-Angelats2001-32"><span class="cite-bracket">[</span>32<span class="cite-bracket">]</span></a></sup>
</p>
<div class="mw-heading mw-heading3"><h3 id="MKRN1">MKRN1</h3></div>
<p>MKRN1 is an <a href="Ubiquitin_ligase" title="Ubiquitin ligase">E3 ubiquitin ligase</a> which negatively regulates FADD by targeting it for ubiquitin mediated degradation. In doing so, MKRN1 is able to control the level of apoptosis.<sup id="cite_ref-LeeEW2012_33-0" class="reference"><a href="#cite_note-LeeEW2012-33"><span class="cite-bracket">[</span>33<span class="cite-bracket">]</span></a></sup>
</p>
<div class="mw-heading mw-heading2"><h2 id="Roles_in_inflammatory_diseases">Roles in inflammatory diseases</h2></div>
<p>Increased levels of FADD were found in the <a href="White_blood_cell" title="White blood cell">leukocytes</a> of patients with relapsing remitting <a href="Multiple_sclerosis" title="Multiple sclerosis">multiple sclerosis</a>, contributing to <a href="Inflammation" title="Inflammation">inflammation</a>.<sup id="cite_ref-Reuss2014_34-0" class="reference"><a href="#cite_note-Reuss2014-34"><span class="cite-bracket">[</span>34<span class="cite-bracket">]</span></a></sup>
In <a href="Rheumatoid_arthritis" title="Rheumatoid arthritis">rheumatoid arthritis</a>, it is thought that stimulation of Fas receptors on <a href="Macrophages" class="mw-redirect" title="Macrophages">macrophages</a>, leads to formation of the FADD containing DISCs. Formation of these sequesters FADD away from MyD88 allowing MyD88 to interact with IRAK and induce the enhanced inflammation associated with this disease.<sup id="cite_ref-Ma2004_35-0" class="reference"><a href="#cite_note-Ma2004-35"><span class="cite-bracket">[</span>35<span class="cite-bracket">]</span></a></sup>
</p>
<div class="mw-heading mw-heading2"><h2 id="Roles_in_cancer">Roles in cancer</h2></div>
<p>As FADD has such an important role in apoptosis, loss of FADD can give cancer cells a proliferative advantage as apoptosis would no longer be induced when the Fas receptors are stimulated.<sup id="cite_ref-Tourneur2010_25-2" class="reference"><a href="#cite_note-Tourneur2010-25"><span class="cite-bracket">[</span>25<span class="cite-bracket">]</span></a></sup>
</p><p>However, there is significant upregulation of FADD in <a href="Ovarian_cancer" title="Ovarian cancer">ovarian cancer</a><sup id="cite_ref-:0_36-0" class="reference"><a href="#cite_note-:0-36"><span class="cite-bracket">[</span>36<span class="cite-bracket">]</span></a></sup> and <a href="Head_and_neck_cancer" title="Head and neck cancer">head and neck</a> <a href="Squamous_cell_carcinoma" class="mw-redirect" title="Squamous cell carcinoma">squamous cell carcinoma</a>. It is not yet clear what advantage this has on the cancer cells, but given FADDs roles in cell cycle regulation and cell survival, it likely that it may be related to this.<sup id="cite_ref-Pattje2013_37-0" class="reference"><a href="#cite_note-Pattje2013-37"><span class="cite-bracket">[</span>37<span class="cite-bracket">]</span></a></sup>
There are also elevated levels of FADD in <a href="Lung_cancer" title="Lung cancer">non small cell lung cancer</a>. FADD can be used as a <a href="Prognosis" title="Prognosis">prognosis</a> marker for both of these diseases, with high levels of FADD being correlated with poor outcome.<sup id="cite_ref-Cimino2012_38-0" class="reference"><a href="#cite_note-Cimino2012-38"><span class="cite-bracket">[</span>38<span class="cite-bracket">]</span></a></sup>
</p>
<div class="mw-heading mw-heading3"><h3 id="Therapeutic_target">Therapeutic target</h3></div>
<p><a href="Paclitaxel" title="Paclitaxel">Taxol</a> is a drug used in anticancer therapies due to its ability to interfere with <a href="Microtubule" title="Microtubule">microtubule</a> assembly, which leads to cell cycle arrest. FADD phosphorylated at Ser194 makes cells more sensitive to cell cycle arrest induced by taxol.<sup id="cite_ref-Alappat2005_21-1" class="reference"><a href="#cite_note-Alappat2005-21"><span class="cite-bracket">[</span>21<span class="cite-bracket">]</span></a></sup> Taxol can also cause apoptosis of cells and this requires procaspase 10, which is activated by recruitment to FADD.<sup id="cite_ref-Park2004_39-0" class="reference"><a href="#cite_note-Park2004-39"><span class="cite-bracket">[</span>39<span class="cite-bracket">]</span></a></sup>
</p><p>It has been shown that the activation of <a href="C-Jun_N-terminal_kinases" title="C-Jun N-terminal kinases">JNK</a> leads to the phosphorylation of FADD. Phosphorylated FADD can induce G2/M cell cycle arrest, potentially by increasing the stability of p53. Therefore, drugs which can activate this pathway may have a therapeutic potential.<sup id="cite_ref-Matsuyoshi2006_40-0" class="reference"><a href="#cite_note-Matsuyoshi2006-40"><span class="cite-bracket">[</span>40<span class="cite-bracket">]</span></a></sup>
However, high levels of phosphorylated FADD have been correlated with a poor prognosis in many cancers such as that of the head and neck. This is likely to be due to its activation of the NF-κB pathway, which is antiapoptotic. Therefore, inhibition of FADD phosphorylation may be developed as a potential anti cancer strategy.<sup id="cite_ref-Schinske2011_41-0" class="reference"><a href="#cite_note-Schinske2011-41"><span class="cite-bracket">[</span>41<span class="cite-bracket">]</span></a></sup> For example, It has been suggested that inhibition of FADD might work as a potential <a href="Targeted_therapy" title="Targeted therapy">targeted therapy</a> for <a href="Drug_resistance" title="Drug resistance">drug-resistant</a> <a href="Ovarian_cancer" title="Ovarian cancer">ovarian cancer</a>.<sup id="cite_ref-:0_36-1" class="reference"><a href="#cite_note-:0-36"><span class="cite-bracket">[</span>36<span class="cite-bracket">]</span></a></sup>
</p>
<div class="mw-heading mw-heading2"><h2 id="Interactions">Interactions</h2></div>
<p>FADD has been seen to interact with <a href="Fas_receptor" title="Fas receptor">Fas receptor</a>,:<sup id="cite_ref-Boldin1995_7-2" class="reference"><a href="#cite_note-Boldin1995-7"><span class="cite-bracket">[</span>7<span class="cite-bracket">]</span></a></sup>
</p>
<style data-mw-deduplicate="TemplateStyles:r1184024115">
/* start https://en.wikipedia.org/ */


.mw-parser-output .div-col{margin-top:0.3em;column-width:30em}.mw-parser-output .div-col-small{font-size:90%}.mw-parser-output .div-col-rules{column-rule:1px solid #aaa}.mw-parser-output .div-col dl,.mw-parser-output .div-col ol,.mw-parser-output .div-col ul{margin-top:0}.mw-parser-output .div-col li,.mw-parser-output .div-col dd{page-break-inside:avoid;break-inside:avoid-column}


/* end https://en.wikipedia.org/ */
</style><div class="div-col" style="column-width: 20em;">
<ul><li><a href="ABCA1" title="ABCA1">ABCA1</a>,<sup id="cite_ref-pmid12235128_42-0" class="reference"><a href="#cite_note-pmid12235128-42"><span class="cite-bracket">[</span>42<span class="cite-bracket">]</span></a></sup></li>
<li><a href="ATG5" class="mw-redirect" title="ATG5">ATG5</a>,<sup id="cite_ref-Pyo2005_16-1" class="reference"><a href="#cite_note-Pyo2005-16"><span class="cite-bracket">[</span>16<span class="cite-bracket">]</span></a></sup></li>
<li><a href="CFLR" class="mw-redirect" title="CFLR">C-FLIP</a>,<sup id="cite_ref-Scaffidi1999_31-1" class="reference"><a href="#cite_note-Scaffidi1999-31"><span class="cite-bracket">[</span>31<span class="cite-bracket">]</span></a></sup> MKRN1,<sup id="cite_ref-LeeEW2012_33-1" class="reference"><a href="#cite_note-LeeEW2012-33"><span class="cite-bracket">[</span>33<span class="cite-bracket">]</span></a></sup></li>
<li><a href="Casein_kinase_1%2C_alpha_1" title="Casein kinase 1, alpha 1">Casein Kinase 1a</a>,<sup id="cite_ref-Alappat2005_21-2" class="reference"><a href="#cite_note-Alappat2005-21"><span class="cite-bracket">[</span>21<span class="cite-bracket">]</span></a></sup></li>
<li><a href="DEDD" title="DEDD">DEDD</a>,<sup id="cite_ref-pmid11741985_43-0" class="reference"><a href="#cite_note-pmid11741985-43"><span class="cite-bracket">[</span>43<span class="cite-bracket">]</span></a></sup></li>
<li><a href="MBD4" title="MBD4">MBD4</a><sup id="cite_ref-pmid12702765_44-0" class="reference"><a href="#cite_note-pmid12702765-44"><span class="cite-bracket">[</span>44<span class="cite-bracket">]</span></a></sup></li>
<li><a href="MYD88" title="MYD88">MyD88</a>,<sup id="cite_ref-Tourneur2010_25-3" class="reference"><a href="#cite_note-Tourneur2010-25"><span class="cite-bracket">[</span>25<span class="cite-bracket">]</span></a></sup></li>
<li><a href="NACA_(gene)" title="NACA (gene)">NACA</a>,<sup id="cite_ref-pmid12684039_45-0" class="reference"><a href="#cite_note-pmid12684039-45"><span class="cite-bracket">[</span>45<span class="cite-bracket">]</span></a></sup></li>
<li><a href="PEA15" title="PEA15">PEA15</a>,<sup id="cite_ref-pmid10442631_46-0" class="reference"><a href="#cite_note-pmid10442631-46"><span class="cite-bracket">[</span>46<span class="cite-bracket">]</span></a></sup></li>
<li><a href="RIPK1" title="RIPK1">RIPK1</a>,<sup id="cite_ref-Lee2012_13-2" class="reference"><a href="#cite_note-Lee2012-13"><span class="cite-bracket">[</span>13<span class="cite-bracket">]</span></a></sup></li>
<li><a href="RIPK3" title="RIPK3">RIPK3</a>,<sup id="cite_ref-Lee2012_13-3" class="reference"><a href="#cite_note-Lee2012-13"><span class="cite-bracket">[</span>13<span class="cite-bracket">]</span></a></sup></li>
<li><a href="TRADD" title="TRADD">TRADD</a>,<sup id="cite_ref-micheau2003_15-1" class="reference"><a href="#cite_note-micheau2003-15"><span class="cite-bracket">[</span>15<span class="cite-bracket">]</span></a></sup></li>
<li><a href="TRAIL" title="TRAIL">TRAIL</a>,<sup id="cite_ref-Bodmer2000_14-1" class="reference"><a href="#cite_note-Bodmer2000-14"><span class="cite-bracket">[</span>14<span class="cite-bracket">]</span></a></sup></li>
<li><a href="Caspase_10" title="Caspase 10">procaspase 10</a>,<sup id="cite_ref-Kischkel2001_10-1" class="reference"><a href="#cite_note-Kischkel2001-10"><span class="cite-bracket">[</span>10<span class="cite-bracket">]</span></a></sup> and</li>
<li><a href="Caspase_8" title="Caspase 8">Procaspase 8</a>.<sup id="cite_ref-Kischkel2001_10-2" class="reference"><a href="#cite_note-Kischkel2001-10"><span class="cite-bracket">[</span>10<span class="cite-bracket">]</span></a></sup></li></ul>
</div>
<div class="mw-heading mw-heading2"><h2 id="See_also">See also</h2></div>
<ul><li><a href="TRADD" title="TRADD">TRADD</a></li>
<li><a href="Intrinsic_apoptosis" class="mw-redirect" title="Intrinsic apoptosis">Intrinsic apoptosis</a></li></ul>
<div class="mw-heading mw-heading2"><h2 id="References">References</h2></div>
<style data-mw-deduplicate="TemplateStyles:r1239543626">
/* start https://en.wikipedia.org/ */


.mw-parser-output .reflist{margin-bottom:0.5em;list-style-type:decimal}@media screen{.mw-parser-output .reflist{font-size:90%}}.mw-parser-output .reflist .references{font-size:100%;margin-bottom:0;list-style-type:inherit}.mw-parser-output .reflist-columns-2{column-width:30em}.mw-parser-output .reflist-columns-3{column-width:25em}.mw-parser-output .reflist-columns{margin-top:0.3em}.mw-parser-output .reflist-columns ol{margin-top:0}.mw-parser-output .reflist-columns li{page-break-inside:avoid;break-inside:avoid-column}.mw-parser-output .reflist-upper-alpha{list-style-type:upper-alpha}.mw-parser-output .reflist-upper-roman{list-style-type:upper-roman}.mw-parser-output .reflist-lower-alpha{list-style-type:lower-alpha}.mw-parser-output .reflist-lower-greek{list-style-type:lower-greek}.mw-parser-output .reflist-lower-roman{list-style-type:lower-roman}


/* end https://en.wikipedia.org/ */
</style><div class="reflist reflist-columns references-column-width" style="column-width: 35em;">
<ol class="references">
<li id="cite_note-refGRCh38Ensembl-1"><span class="mw-cite-backlink">^ <a href="#cite_ref-refGRCh38Ensembl_1-0"><sup><i><b>a</b></i></sup></a> <a href="#cite_ref-refGRCh38Ensembl_1-1"><sup><i><b>b</b></i></sup></a> <a href="#cite_ref-refGRCh38Ensembl_1-2"><sup><i><b>c</b></i></sup></a></span> <span class="reference-text"><a rel="nofollow" class="external text" href="http://May2017.archive.ensembl.org/Homo_sapiens/Gene/Summary?db=core;g=ENSG00000168040">GRCh38: Ensembl release 89: ENSG00000168040</a> – <a href="Ensembl_genome_database_project" title="Ensembl genome database project">Ensembl</a>, May 2017</span>
</li>
<li id="cite_note-2"><span class="mw-cite-backlink"><b><a href="#cite_ref-2">^</a></b></span> <span class="reference-text"><style data-mw-deduplicate="TemplateStyles:r1238218222">
/* start https://en.wikipedia.org/ */


.mw-parser-output cite.citation{font-style:inherit;word-wrap:break-word}.mw-parser-output .citation q{quotes:"\"""\"""'""'"}.mw-parser-output .citation:target{background-color:rgba(0,127,255,0.133)}.mw-parser-output .id-lock-free.id-lock-free a{background:url("./mw/Lock-green.svg")right 0.1em center/9px no-repeat}.mw-parser-output .id-lock-limited.id-lock-limited a,.mw-parser-output .id-lock-registration.id-lock-registration a{background:url("./mw/Lock-gray-alt-2.svg")right 0.1em center/9px no-repeat}.mw-parser-output .id-lock-subscription.id-lock-subscription a{background:url("./mw/Lock-red-alt-2.svg")right 0.1em center/9px no-repeat}.mw-parser-output .cs1-ws-icon a{background:url("./mw/Wikisource-logo.svg")right 0.1em center/12px no-repeat}body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-free a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-limited a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-registration a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-subscription a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .cs1-ws-icon a{background-size:contain;padding:0 1em 0 0}.mw-parser-output .cs1-code{color:inherit;background:inherit;border:none;padding:inherit}.mw-parser-output .cs1-hidden-error{display:none;color:var(--color-error,#d33)}.mw-parser-output .cs1-visible-error{color:var(--color-error,#d33)}.mw-parser-output .cs1-maint{display:none;color:#085;margin-left:0.3em}.mw-parser-output .cs1-kern-left{padding-left:0.2em}.mw-parser-output .cs1-kern-right{padding-right:0.2em}.mw-parser-output .citation .mw-selflink{font-weight:inherit}@media screen{.mw-parser-output .cs1-format{font-size:95%}html.skin-theme-clientpref-night .mw-parser-output .cs1-maint{color:#18911f}}@media screen and (prefers-color-scheme:dark){html.skin-theme-clientpref-os .mw-parser-output .cs1-maint{color:#18911f}}


/* end https://en.wikipedia.org/ */
</style><cite class="citation web cs1"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&amp;cmd=Link&amp;LinkName=gene_pubmed&amp;from_uid=8772">"Human PubMed Reference:"</a>. <i>National Center for Biotechnology Information, U.S. National Library of Medicine</i>.</cite></span>
</li>
<li id="cite_note-3"><span class="mw-cite-backlink"><b><a href="#cite_ref-3">^</a></b></span> <span class="reference-text"><cite class="citation web cs1"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&amp;cmd=Link&amp;LinkName=gene_pubmed&amp;from_uid=14082">"Mouse PubMed Reference:"</a>. <i>National Center for Biotechnology Information, U.S. National Library of Medicine</i>.</cite></span>
</li>
<li id="cite_note-Kim1996-4"><span class="mw-cite-backlink"><b><a href="#cite_ref-Kim1996_4-0">^</a></b></span> <span class="reference-text"><cite id="CITEREFKim,_P.K.M.Dutra,_A.S.Chandrasekharappa,_S.C.PUCK,_J.M1996" class="citation journal cs1">Kim, P.K.M., Dutra, A.S., Chandrasekharappa, S.C., PUCK, J.M (1996). <a rel="nofollow" class="external text" href="https://doi.org/10.4049%2Fjimmunol.157.12.5461">"Genomic structure and mapping of human FADD, an intracellular mediator of lymphocyte apoptosis"</a>. <i>Journal of Immunology</i>. <b>157</b> (12): <span class="nowrap">5461–</span>5466. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://doi.org/10.4049%2Fjimmunol.157.12.5461">10.4049/jimmunol.157.12.5461</a></span>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a>&nbsp;<a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/8955195">8955195</a>.</cite></span>
</li>
<li id="cite_note-Huang1996-5"><span class="mw-cite-backlink"><b><a href="#cite_ref-Huang1996_5-0">^</a></b></span> <span class="reference-text"><cite id="CITEREFHuangEberstadtOlejniczakMeadows1996" class="citation journal cs1">Huang B, Eberstadt M, Olejniczak ET, Meadows RP, Fesik SW (1996). "NMR structure and mutagenesis of the Fas (APO-1/CD95) death domain". <i>Nature</i>. <b>384</b> (6610): <span class="nowrap">638–</span>641. <a href="Bibcode_(identifier)" class="mw-redirect" title="Bibcode (identifier)">Bibcode</a>:<a rel="nofollow" class="external text" href="https://ui.adsabs.harvard.edu/abs/1996Natur.384..638H">1996Natur.384..638H</a>. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1038%2F384638a0">10.1038/384638a0</a>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a>&nbsp;<a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/8967952">8967952</a>. <a href="S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a>&nbsp;<a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:2492303">2492303</a>.</cite></span>
</li>
<li id="cite_note-Eberstadt1998-6"><span class="mw-cite-backlink">^ <a href="#cite_ref-Eberstadt1998_6-0"><sup><i><b>a</b></i></sup></a> <a href="#cite_ref-Eberstadt1998_6-1"><sup><i><b>b</b></i></sup></a></span> <span class="reference-text"><cite id="CITEREFEberstadtHuangChenMeadows1998" class="citation journal cs1">Eberstadt M, Huang B, Chen Z, Meadows RP, Ng SC, Zheng L, Lenardo MJ, Fesik SW (1998). "NMR structure and mutagenesis of the FADD (Mort1) death-effector domain". <i>Nature</i>. <b>392</b> (6679): <span class="nowrap">941–</span>945. <a href="Bibcode_(identifier)" class="mw-redirect" title="Bibcode (identifier)">Bibcode</a>:<a rel="nofollow" class="external text" href="https://ui.adsabs.harvard.edu/abs/1998Natur.392..941E">1998Natur.392..941E</a>. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1038%2F31972">10.1038/31972</a>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a>&nbsp;<a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/9582077">9582077</a>. <a href="S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a>&nbsp;<a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:4370202">4370202</a>.</cite></span>
</li>
<li id="cite_note-Boldin1995-7"><span class="mw-cite-backlink">^ <a href="#cite_ref-Boldin1995_7-0"><sup><i><b>a</b></i></sup></a> <a href="#cite_ref-Boldin1995_7-1"><sup><i><b>b</b></i></sup></a> <a href="#cite_ref-Boldin1995_7-2"><sup><i><b>c</b></i></sup></a></span> <span class="reference-text"><cite id="CITEREFBoldin,_M._P.,_Varfolomeev,_E._E.,_Pancer,_Z.,_Mett,_I._L.,_Camonis,_J._H._&amp;_Wallach,_D.1995" class="citation journal cs1">Boldin, M. P., Varfolomeev, E. E., Pancer, Z., Mett, I. L., Camonis, J. H. &amp; Wallach, D. (1995). <a rel="nofollow" class="external text" href="https://doi.org/10.1074%2Fjbc.270.14.7795">"A Novel Protein That Interacts with the Death Domain of Fas/APO1 Contains a Sequence Motif Related to the Death Domain"</a>. <i>Journal of Biological Chemistry</i>. <b>270</b> (14): <span class="nowrap">7795–</span>7798. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://doi.org/10.1074%2Fjbc.270.14.7795">10.1074/jbc.270.14.7795</a></span>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a>&nbsp;<a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/7536190">7536190</a>.</cite><span class="cs1-maint citation-comment"><code class="cs1-code">{{cite journal}}</code>: CS1 maint: multiple names: authors list (link)</span></span>
</li>
<li id="cite_note-Jeong1999-8"><span class="mw-cite-backlink"><b><a href="#cite_ref-Jeong1999_8-0">^</a></b></span> <span class="reference-text"><cite id="CITEREFJeong,_E._J.Bang,_S.Lee,_T._H.Park,_Y._I.1999" class="citation journal cs1">Jeong, E. J., Bang, S., Lee, T. H., Park, Y. I., Sim, W. S., Kim, K. S. (1999). <a rel="nofollow" class="external text" href="https://doi.org/10.1074%2Fjbc.274.23.16337">"The solution structure of FADD death domain - Structural basis of death domain interactions of Fas and FADD"</a>. <i>Journal of Biological Chemistry</i>. <b>274</b> (23): <span class="nowrap">16337–</span>16342. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://doi.org/10.1074%2Fjbc.274.23.16337">10.1074/jbc.274.23.16337</a></span>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a>&nbsp;<a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/10347191">10347191</a>.</cite></span>
</li>
<li id="cite_note-Boldin1996-9"><span class="mw-cite-backlink"><b><a href="#cite_ref-Boldin1996_9-0">^</a></b></span> <span class="reference-text"><cite id="CITEREFBoldin,_M._P.Goncharov,_T._M.Goltsev,_Y._V.wallach,_D.1996" class="citation journal cs1">Boldin, M. P., Goncharov, T. M., Goltsev, Y. V., wallach, D. (1996). <a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fs0092-8674%2800%2981265-9">"Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death"</a>. <i>Cell</i>. <b>85</b> (6): <span class="nowrap">803–</span>815. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fs0092-8674%2800%2981265-9">10.1016/s0092-8674(00)81265-9</a></span>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a>&nbsp;<a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/8681376">8681376</a>. <a href="S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a>&nbsp;<a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:7415784">7415784</a>.</cite></span>
</li>
<li id="cite_note-Kischkel2001-10"><span class="mw-cite-backlink">^ <a href="#cite_ref-Kischkel2001_10-0"><sup><i><b>a</b></i></sup></a> <a href="#cite_ref-Kischkel2001_10-1"><sup><i><b>b</b></i></sup></a> <a href="#cite_ref-Kischkel2001_10-2"><sup><i><b>c</b></i></sup></a></span> <span class="reference-text"><cite id="CITEREFKischkelLawrenceTinelLeBlanc2001" class="citation journal cs1">Kischkel FC, Lawrence DA, Tinel A, LeBlanc H, Virmani A, Schow P, Gazdar A, Blenis J, Arnott D, Ashkenazi A (2001). <a rel="nofollow" class="external text" href="https://doi.org/10.1074%2Fjbc.M105102200">"Death receptor recruitment of endogenous caspase-10 and apoptosis initiation in the absence of caspase-8"</a>. <i>Journal of Biological Chemistry</i>. <b>276</b> (49): <span class="nowrap">46639–</span>46646. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://doi.org/10.1074%2Fjbc.M105102200">10.1074/jbc.M105102200</a></span>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a>&nbsp;<a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/11583996">11583996</a>.</cite></span>
</li>
<li id="cite_note-Kischkel1995-11"><span class="mw-cite-backlink"><b><a href="#cite_ref-Kischkel1995_11-0">^</a></b></span> <span class="reference-text"><cite id="CITEREFPruulMcDonald1995" class="citation journal cs1">Pruul H, McDonald PJ (1995). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC394672">"Cytotoxicity-dependent APO-1 (Fas/CD95)-associated proteins form a death-inducing signalling complex (DISC) with the receptor"</a>. <i>EMBO Journal</i>. <b>14</b> (22): <span class="nowrap">5579–</span>5588. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1002%2Fj.1460-2075.1995.tb00245.x">10.1002/j.1460-2075.1995.tb00245.x</a>. <a href="PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a>&nbsp;<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC394672">394672</a></span>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a>&nbsp;<a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/8521815">8521815</a>.</cite></span>
</li>
<li id="cite_note-Weinlich2011-12"><span class="mw-cite-backlink"><b><a href="#cite_ref-Weinlich2011_12-0">^</a></b></span> <span class="reference-text"><cite id="CITEREFWeinlichDillonGreen2011" class="citation journal cs1">Weinlich R, Dillon CP, Green DR (2011). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3205316">"Ripped to death"</a>. <i>Trends in Cell Biology</i>. <b>21</b> (11): <span class="nowrap">630–</span>637. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fj.tcb.2011.09.002">10.1016/j.tcb.2011.09.002</a>. <a href="PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a>&nbsp;<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3205316">3205316</a></span>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a>&nbsp;<a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/21978761">21978761</a>.</cite></span>
</li>
<li id="cite_note-Lee2012-13"><span class="mw-cite-backlink">^ <a href="#cite_ref-Lee2012_13-0"><sup><i><b>a</b></i></sup></a> <a href="#cite_ref-Lee2012_13-1"><sup><i><b>b</b></i></sup></a> <a href="#cite_ref-Lee2012_13-2"><sup><i><b>c</b></i></sup></a> <a href="#cite_ref-Lee2012_13-3"><sup><i><b>d</b></i></sup></a></span> <span class="reference-text"><cite id="CITEREFLee,_E.-W.Seo,_J.Jeong,_M.Lee,_S.2012" class="citation journal cs1">Lee, E.-W., Seo, J., Jeong, M., Lee, S., Song, J (2012). <a rel="nofollow" class="external text" href="https://doi.org/10.5483%2FBMBRep.2012.45.9.186">"The roles of FADD in extrinsic apoptosis and necroptosis"</a>. <i>BMB Reports</i>. <b>45</b> (9): <span class="nowrap">496–</span>508. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://doi.org/10.5483%2FBMBRep.2012.45.9.186">10.5483/BMBRep.2012.45.9.186</a></span>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a>&nbsp;<a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/23010170">23010170</a>.</cite></span>
</li>
<li id="cite_note-Bodmer2000-14"><span class="mw-cite-backlink">^ <a href="#cite_ref-Bodmer2000_14-0"><sup><i><b>a</b></i></sup></a> <a href="#cite_ref-Bodmer2000_14-1"><sup><i><b>b</b></i></sup></a></span> <span class="reference-text"><cite id="CITEREFBodmerHollerReynardVinciguerra2000" class="citation journal cs1">Bodmer JL, Holler N, Reynard S, Vinciguerra P, Schneider P, Juo P, Blenis J, Tschopp J (2000). "TRAIL receptor-2 signals apoptosis through FADD and caspase-8". <i>Nature Cell Biology</i>. <b>2</b> (4): <span class="nowrap">241–</span>243. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1038%2F35008667">10.1038/35008667</a>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a>&nbsp;<a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/10783243">10783243</a>. <a href="S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a>&nbsp;<a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:13547815">13547815</a>.</cite></span>
</li>
<li id="cite_note-micheau2003-15"><span class="mw-cite-backlink">^ <a href="#cite_ref-micheau2003_15-0"><sup><i><b>a</b></i></sup></a> <a href="#cite_ref-micheau2003_15-1"><sup><i><b>b</b></i></sup></a></span> <span class="reference-text"><cite id="CITEREFMicheau,_O.Tschopp,_J.2003" class="citation journal cs1">Micheau, O., Tschopp, J. (2003). <a rel="nofollow" class="external text" href="https://www.hal.inserm.fr/inserm-00527105/file/Figures_Cell_OM.pdf">"Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes"</a> <span class="cs1-format">(PDF)</span>. <i>Cell</i>. <b>114</b> (2): <span class="nowrap">181–</span>190. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fs0092-8674%2803%2900521-x">10.1016/s0092-8674(03)00521-x</a>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a>&nbsp;<a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/12887920">12887920</a>. <a href="S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a>&nbsp;<a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:17145731">17145731</a>.</cite></span>
</li>
<li id="cite_note-Pyo2005-16"><span class="mw-cite-backlink">^ <a href="#cite_ref-Pyo2005_16-0"><sup><i><b>a</b></i></sup></a> <a href="#cite_ref-Pyo2005_16-1"><sup><i><b>b</b></i></sup></a></span> <span class="reference-text"><cite id="CITEREFPyoJangKwonLee2005" class="citation journal cs1">Pyo JO, Jang MH, Kwon YK, Lee HJ, Jun JI, Woo HN, Cho DH, Choi B, Lee H, Kim JH, Mizushima N, Oshumi Y, Jung YK (2005). <a rel="nofollow" class="external text" href="https://doi.org/10.1074%2Fjbc.M413934200">"Essential roles of Atg5 and FADD in autophagic cell death - Dissection of autophagic cell death into vacuole formation and cell death"</a>. <i>Journal of Biological Chemistry</i>. <b>280</b> (21): <span class="nowrap">20722–</span>20729. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://doi.org/10.1074%2Fjbc.M413934200">10.1074/jbc.M413934200</a></span>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a>&nbsp;<a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/15778222">15778222</a>.</cite></span>
</li>
<li id="cite_note-Bell2008-17"><span class="mw-cite-backlink"><b><a href="#cite_ref-Bell2008_17-0">^</a></b></span> <span class="reference-text"><cite id="CITEREFBellLeverrierWeistNewton2008" class="citation journal cs1">Bell BD, Leverrier S, Weist BM, Newton RH, Arechiga AF, Luhrs KA, Morrissette NS, Walsh CM (2008). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2575479">". FADD and caspase-8 control the outcome of autophagic signaling in proliferating T cells"</a>. <i>Proceedings of the National Academy of Sciences of the United States of America</i>. <b>105</b> (43): <span class="nowrap">16677–</span>16682. <a href="Bibcode_(identifier)" class="mw-redirect" title="Bibcode (identifier)">Bibcode</a>:<a rel="nofollow" class="external text" href="https://ui.adsabs.harvard.edu/abs/2008PNAS..10516677B">2008PNAS..10516677B</a>. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://doi.org/10.1073%2Fpnas.0808597105">10.1073/pnas.0808597105</a></span>. <a href="PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a>&nbsp;<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2575479">2575479</a></span>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a>&nbsp;<a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/18946037">18946037</a>.</cite></span>
</li>
<li id="cite_note-Yeh1998-18"><span class="mw-cite-backlink"><b><a href="#cite_ref-Yeh1998_18-0">^</a></b></span> <span class="reference-text"><cite id="CITEREFYeh,_W._C.De_La_Pompa,_J._L.Mccurach,_M._E.Shu,_H._B.1998" class="citation journal cs1">Yeh, W. C., De La Pompa, J. L., Mccurach, M. E., Shu, H. B., Elia, A. J., Shahinian, A., Ng, M., Wakeham, A., Khoo, W., Mitchell, K., El-Deiry, W. S., Lowe, S. W., Goeddel, D. V., Mak, T. W. (1998). "FADD: Essential for embryo development and signaling from some, but not all, inducers of apoptosis". <i>Science</i>. <b>279</b> (5358): <span class="nowrap">1954–</span>1958. <a href="Bibcode_(identifier)" class="mw-redirect" title="Bibcode (identifier)">Bibcode</a>:<a rel="nofollow" class="external text" href="https://ui.adsabs.harvard.edu/abs/1998Sci...279.1954Y">1998Sci...279.1954Y</a>. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1126%2Fscience.279.5358.1954">10.1126/science.279.5358.1954</a>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a>&nbsp;<a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/9506948">9506948</a>.</cite></span>
</li>
<li id="cite_note-Sakamaki2012-19"><span class="mw-cite-backlink"><b><a href="#cite_ref-Sakamaki2012_19-0">^</a></b></span> <span class="reference-text"><cite id="CITEREFSakamakiTakagiKitayamaKurata2012" class="citation journal cs1">Sakamaki K, Takagi C, Kitayama A, Kurata T, Yamamoto TS, Chiba K, Kominami K, Jung SK, Okawa K, Nozaki M, Kubota HY, Ueno N (2012). <a rel="nofollow" class="external text" href="https://doi.org/10.1111%2Fgtc.12004">"Multiple functions of FADD in apoptosis, NF-kappa B-related signaling, and heart development in Xenopus embryos"</a>. <i>Genes to Cells</i>. <b>17</b> (11): <span class="nowrap">875–</span>896. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://doi.org/10.1111%2Fgtc.12004">10.1111/gtc.12004</a></span>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a>&nbsp;<a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/23025414">23025414</a>. <a href="S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a>&nbsp;<a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:23264540">23264540</a>.</cite></span>
</li>
<li id="cite_note-Gregory-Evans2007-20"><span class="mw-cite-backlink"><b><a href="#cite_ref-Gregory-Evans2007_20-0">^</a></b></span> <span class="reference-text"><cite id="CITEREFGregory-EvansMoosajeeHodgesMackay2007" class="citation journal cs1">Gregory-Evans CY, Moosajee M, Hodges MD, Mackay DS, Game L, Vargesson N, Bloch-Zupan A, Rüschendorf F, Santos-Pinto L, Wackens G, Gregory-Evans K (2007). <a rel="nofollow" class="external text" href="https://doi.org/10.1093%2Fhmg%2Fddm204">"SNP genome scanning localizes oto-dental syndrome to chromosome 11q13 and microdeletions at this locus implicate FGF3 in dental and inner-ear disease and FADD in ocular coloboma"</a>. <i>Human Molecular Genetics</i>. <b>16</b> (20): <span class="nowrap">2482–</span>2493. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://doi.org/10.1093%2Fhmg%2Fddm204">10.1093/hmg/ddm204</a></span>. <a href="Hdl_(identifier)" class="mw-redirect" title="Hdl (identifier)">hdl</a>:<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://hdl.handle.net/11449%2F231047">11449/231047</a></span>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a>&nbsp;<a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/17656375">17656375</a>.</cite></span>
</li>
<li id="cite_note-Alappat2005-21"><span class="mw-cite-backlink">^ <a href="#cite_ref-Alappat2005_21-0"><sup><i><b>a</b></i></sup></a> <a href="#cite_ref-Alappat2005_21-1"><sup><i><b>b</b></i></sup></a> <a href="#cite_ref-Alappat2005_21-2"><sup><i><b>c</b></i></sup></a></span> <span class="reference-text"><cite id="CITEREFAlappatFeigBoyerinasVolkland2005" class="citation journal cs1">Alappat EC, Feig C, Boyerinas B, Volkland J, Samuels M, Murmann AE, Thorburn A, Kidd VJ, Slaughter CA, Osborn SL, Winoto A, Tang WJ, Peter ME (2005). <a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fj.molcel.2005.06.024">"Phosphorylation of FADD at serine 194 by CKI alpha regulates its nonapoptotic activities"</a>. <i>Molecular Cell</i>. <b>19</b> (3): <span class="nowrap">321–</span>332. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fj.molcel.2005.06.024">10.1016/j.molcel.2005.06.024</a></span>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a>&nbsp;<a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/16061179">16061179</a>.</cite></span>
</li>
<li id="cite_note-Zhang1998-22"><span class="mw-cite-backlink"><b><a href="#cite_ref-Zhang1998_22-0">^</a></b></span> <span class="reference-text"><cite id="CITEREFZhangCadoChenKabra1998" class="citation journal cs1">Zhang J, Cado D, Chen A, Kabra NH, Winoto A (1998). "Fas-mediated apoptosis and activation-induced T-cell proliferation are defective in mice lacking FADD/Mort1". <i>Nature</i>. <b>392</b> (6673): <span class="nowrap">296–</span>300. <a href="Bibcode_(identifier)" class="mw-redirect" title="Bibcode (identifier)">Bibcode</a>:<a rel="nofollow" class="external text" href="https://ui.adsabs.harvard.edu/abs/1998Natur.392..296Z">1998Natur.392..296Z</a>. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1038%2F32681">10.1038/32681</a>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a>&nbsp;<a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/9521326">9521326</a>. <a href="S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a>&nbsp;<a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:4420585">4420585</a>.</cite></span>
</li>
<li id="cite_note-Imtiyaz2006-23"><span class="mw-cite-backlink"><b><a href="#cite_ref-Imtiyaz2006_23-0">^</a></b></span> <span class="reference-text"><cite id="CITEREFVander_Elstvan_den_BergPepermansvander_Auwera2006" class="citation journal cs1">Vander Elst P, van den Berg E, Pepermans H, vander Auwera L, Zeeuws R, Tourwe D, van Binst G (2006). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3110081">"The Fas-associated death domain protein is required in apoptosis and TLR-induced proliferative responses in B cells"</a>. <i>Journal of Immunology</i>. <b>176</b> (11): <span class="nowrap">6852–</span>6861. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.4049%2Fjimmunol.176.11.6852">10.4049/jimmunol.176.11.6852</a>. <a href="PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a>&nbsp;<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3110081">3110081</a></span>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a>&nbsp;<a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/16709845">16709845</a>.</cite></span>
</li>
<li id="cite_note-Wajant2000-24"><span class="mw-cite-backlink"><b><a href="#cite_ref-Wajant2000_24-0">^</a></b></span> <span class="reference-text"><cite id="CITEREFWajantHaasSchwenzerMuhlenbeck2000" class="citation journal cs1">Wajant H, Haas E, Schwenzer R, Muhlenbeck F, Kreuz S, Schubert G, Grell M, Smith C, Scheurich P (2000). <a rel="nofollow" class="external text" href="https://doi.org/10.1074%2Fjbc.M000811200">"Inhibition of death receptor-mediated gene induction by a cycloheximide-sensitive factor occurs at the level of or upstream of Fas-associated death domain protein (FADD)"</a>. <i>Journal of Biological Chemistry</i>. <b>275</b> (32): <span class="nowrap">24357–</span>24366. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://doi.org/10.1074%2Fjbc.M000811200">10.1074/jbc.M000811200</a></span>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a>&nbsp;<a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/10823821">10823821</a>.</cite></span>
</li>
<li id="cite_note-Tourneur2010-25"><span class="mw-cite-backlink">^ <a href="#cite_ref-Tourneur2010_25-0"><sup><i><b>a</b></i></sup></a> <a href="#cite_ref-Tourneur2010_25-1"><sup><i><b>b</b></i></sup></a> <a href="#cite_ref-Tourneur2010_25-2"><sup><i><b>c</b></i></sup></a> <a href="#cite_ref-Tourneur2010_25-3"><sup><i><b>d</b></i></sup></a></span> <span class="reference-text"><cite id="CITEREFTourneurChiocchia2010" class="citation journal cs1">Tourneur L, Chiocchia G (2010). "FADD: a regulator of life and death". <i>Trends in Immunology</i>. <b>31</b> (7): <span class="nowrap">260–</span>269. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fj.it.2010.05.005">10.1016/j.it.2010.05.005</a>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a>&nbsp;<a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/20576468">20576468</a>.</cite></span>
</li>
<li id="cite_note-Balachandran2007-26"><span class="mw-cite-backlink"><b><a href="#cite_ref-Balachandran2007_26-0">^</a></b></span> <span class="reference-text"><cite id="CITEREFBalachandran,_S.Venkataraman,_T.Fisher,_P._B.Barber,_G._N2007" class="citation journal cs1">Balachandran, S., Venkataraman, T., Fisher, P. B., Barber, G. N (2007). <a rel="nofollow" class="external text" href="https://doi.org/10.4049%2Fjimmunol.178.4.2429">"Fas-associated death domain-containing protein-mediated antiviral innate immune signaling involves the regulation of Irf7"</a>. <i>Journal of Immunology</i>. <b>178</b> (4): <span class="nowrap">2429–</span>2439. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://doi.org/10.4049%2Fjimmunol.178.4.2429">10.4049/jimmunol.178.4.2429</a></span>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a>&nbsp;<a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/17277150">17277150</a>.</cite></span>
</li>
<li id="cite_note-Cheng2012-27"><span class="mw-cite-backlink"><b><a href="#cite_ref-Cheng2012_27-0">^</a></b></span> <span class="reference-text"><cite id="CITEREFChengWangZhangDu2012" class="citation journal cs1">Cheng W, Wang L, Zhang R, Du P, Yang B, Zhuang H, Tang B, Yao C, Yu M, Wang Y, Zhang J, Yin W, Li J, Zheng W, Lu M, Hua Z (2012). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3406696">"Regulation of Protein Kinase C Inactivation by Fas-associated Protein with Death Domain"</a>. <i>Journal of Biological Chemistry</i>. <b>287</b> (31): <span class="nowrap">26126–</span>26135. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://doi.org/10.1074%2Fjbc.M112.342170">10.1074/jbc.M112.342170</a></span>. <a href="PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a>&nbsp;<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3406696">3406696</a></span>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a>&nbsp;<a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/22582393">22582393</a>.</cite></span>
</li>
<li id="cite_note-Yao2013-28"><span class="mw-cite-backlink"><b><a href="#cite_ref-Yao2013_28-0">^</a></b></span> <span class="reference-text"><cite id="CITEREFYaoZhuangDuCheng2013" class="citation journal cs1">Yao C, Zhuang H, Du P, Cheng W, Yang B, Guan S, Hu Y, Zhu D, Christine M, Shi L, Hua ZC (2013). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3790283">"Domain-containing Protein (FADD) Phosphorylation in Regulating Glucose Homeostasis: from Proteomic Discovery to Physiological Validation"</a>. <i>Molecular &amp; Cellular Proteomics</i>. <b>12</b> (10): <span class="nowrap">2689–</span>2700. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://doi.org/10.1074%2Fmcp.M113.029306">10.1074/mcp.M113.029306</a></span>. <a href="PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a>&nbsp;<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3790283">3790283</a></span>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a>&nbsp;<a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/23828893">23828893</a>.</cite></span>
</li>
<li id="cite_note-Gomez-Angelats2003-29"><span class="mw-cite-backlink"><b><a href="#cite_ref-Gomez-Angelats2003_29-0">^</a></b></span> <span class="reference-text"><cite id="CITEREFGómez-AngelatsCidlowski2003" class="citation journal cs1">Gómez-Angelats M, Cidlowski JA (2003). <a rel="nofollow" class="external text" href="https://doi.org/10.1038%2Fsj.cdd.4401237">"Molecular evidence for the nuclear localization of FADD"</a>. <i>Cell Death and Differentiation</i>. <b>10</b> (7): <span class="nowrap">791–</span>797. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://doi.org/10.1038%2Fsj.cdd.4401237">10.1038/sj.cdd.4401237</a></span>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a>&nbsp;<a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/12815462">12815462</a>.</cite></span>
</li>
<li id="cite_note-Krueger2001-30"><span class="mw-cite-backlink">^ <a href="#cite_ref-Krueger2001_30-0"><sup><i><b>a</b></i></sup></a> <a href="#cite_ref-Krueger2001_30-1"><sup><i><b>b</b></i></sup></a></span> <span class="reference-text"><cite id="CITEREFKruegerBaumannKrammerKirchhoff2001" class="citation journal cs1">Krueger A, Baumann S, Krammer PH, Kirchhoff S (2001). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC99990">"FLICE-inhibitory proteins: Regulators of death receptor-mediated apoptosis"</a>. <i>Molecular and Cellular Biology</i>. <b>21</b> (24): <span class="nowrap">8247–</span>8254. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1128%2Fmcb.21.24.8247-8254.2001">10.1128/mcb.21.24.8247-8254.2001</a>. <a href="PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a>&nbsp;<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC99990">99990</a></span>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a>&nbsp;<a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/11713262">11713262</a>.</cite></span>
</li>
<li id="cite_note-Scaffidi1999-31"><span class="mw-cite-backlink">^ <a href="#cite_ref-Scaffidi1999_31-0"><sup><i><b>a</b></i></sup></a> <a href="#cite_ref-Scaffidi1999_31-1"><sup><i><b>b</b></i></sup></a></span> <span class="reference-text"><cite id="CITEREFScaffidi,_C.Schmitz,_I.Krammer,_P._H.Peter,_M._E.1999" class="citation journal cs1">Scaffidi, C., Schmitz, I., Krammer, P. H., Peter, M. E. (1999). <a rel="nofollow" class="external text" href="https://doi.org/10.1074%2Fjbc.274.3.1541">"The role of c-FLIP in modulation of CD95-induced apoptosis"</a>. <i>Journal of Biological Chemistry</i>. <b>274</b> (3): <span class="nowrap">1541–</span>1548. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://doi.org/10.1074%2Fjbc.274.3.1541">10.1074/jbc.274.3.1541</a></span>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a>&nbsp;<a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/9880531">9880531</a>.</cite></span>
</li>
<li id="cite_note-Gomez-Angelats2001-32"><span class="mw-cite-backlink"><b><a href="#cite_ref-Gomez-Angelats2001_32-0">^</a></b></span> <span class="reference-text"><cite id="CITEREFGómez-AngelatsCidlowski2001" class="citation journal cs1">Gómez-Angelats M, Cidlowski JA (2001). <a rel="nofollow" class="external text" href="https://doi.org/10.1074%2Fjbc.M104919200">"Protein kinase C regulates FADD recruitment and death-inducing signaling complex formation in Fas/CD95-induced apoptosis"</a>. <i>Journal of Biological Chemistry</i>. <b>276</b> (48): <span class="nowrap">44944–</span>44952. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://doi.org/10.1074%2Fjbc.M104919200">10.1074/jbc.M104919200</a></span>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a>&nbsp;<a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/11581255">11581255</a>.</cite></span>
</li>
<li id="cite_note-LeeEW2012-33"><span class="mw-cite-backlink">^ <a href="#cite_ref-LeeEW2012_33-0"><sup><i><b>a</b></i></sup></a> <a href="#cite_ref-LeeEW2012_33-1"><sup><i><b>b</b></i></sup></a></span> <span class="reference-text"><cite id="CITEREFLeeKimAhnSeo2012" class="citation journal cs1">Lee EW, Kim JH, Ahn YH, Seo J, Ko A, Jeong M, Kim SJ, Ro JY, Park KM, Lee HW, Park EJ, Chun KH, Song J (2012). <a rel="nofollow" class="external text" href="https://doi.org/10.1038%2Fncomms1981">"Ubiquitination and degradation of the FADD adaptor protein regulate death receptor-mediated apoptosis and necroptosis"</a>. <i>Nature Communications</i>. <b>3</b>: 978. <a href="Bibcode_(identifier)" class="mw-redirect" title="Bibcode (identifier)">Bibcode</a>:<a rel="nofollow" class="external text" href="https://ui.adsabs.harvard.edu/abs/2012NatCo...3..978L">2012NatCo...3..978L</a>. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://doi.org/10.1038%2Fncomms1981">10.1038/ncomms1981</a></span>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a>&nbsp;<a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/22864571">22864571</a>.</cite></span>
</li>
<li id="cite_note-Reuss2014-34"><span class="mw-cite-backlink"><b><a href="#cite_ref-Reuss2014_34-0">^</a></b></span> <span class="reference-text"><cite id="CITEREFReussMistarzMirauKraus2014" class="citation journal cs1">Reuss R, Mistarz M, Mirau A, Kraus J, Bödeker RH, Oschmann P (2014). "FADD is upregulated in relapsing remitting multiple". <i>Neuroimmunomodulation</i>. <b>21</b> (5): <span class="nowrap">221–</span>225. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1159%2F000356522">10.1159/000356522</a>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a>&nbsp;<a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/24603611">24603611</a>. <a href="S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a>&nbsp;<a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:207652468">207652468</a>.</cite></span>
</li>
<li id="cite_note-Ma2004-35"><span class="mw-cite-backlink"><b><a href="#cite_ref-Ma2004_35-0">^</a></b></span> <span class="reference-text"><cite id="CITEREFMaLiuTu-RappThiesen2004" class="citation journal cs1">Ma Y, Liu H, Tu-Rapp H, Thiesen HJ, Ibrahim SM, Cole SM, Pope RM (2004). "Fas ligation on macrophages enhances IL-1R1-Toll-like receptor 4 signaling and promotes chronic inflammation". <i>Nature Immunology</i>. <b>5</b> (4): <span class="nowrap">380–</span>387. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1038%2Fni1054">10.1038/ni1054</a>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a>&nbsp;<a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/15004557">15004557</a>. <a href="S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a>&nbsp;<a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:39471972">39471972</a>.</cite></span>
</li>
<li id="cite_note-:0-36"><span class="mw-cite-backlink">^ <a href="#cite_ref-:0_36-0"><sup><i><b>a</b></i></sup></a> <a href="#cite_ref-:0_36-1"><sup><i><b>b</b></i></sup></a></span> <span class="reference-text"><cite id="CITEREFRazaghiVillacrésJungMashkour2017" class="citation journal cs1">Razaghi A, Villacrés C, Jung V, Mashkour N, Butler M, Owens L, Heimann K (2017). "Improved therapeutic efficacy of mammalian expressed-recombinant interferon gamma against ovarian cancer cells". <i>Experimental Cell Research</i>. <b>359</b> (1): <span class="nowrap">20–</span>29. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fj.yexcr.2017.08.014">10.1016/j.yexcr.2017.08.014</a>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a>&nbsp;<a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/28803068">28803068</a>. <a href="S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a>&nbsp;<a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:12800448">12800448</a>.</cite></span>
</li>
<li id="cite_note-Pattje2013-37"><span class="mw-cite-backlink"><b><a href="#cite_ref-Pattje2013_37-0">^</a></b></span> <span class="reference-text"><cite id="CITEREFPattjeMelchersSlagter-MenkemaMastik2013" class="citation journal cs1">Pattje WJ, Melchers LJ, Slagter-Menkema L, Mastik MF, Schrijvers ML, Gibcus JH, Kluin PM, Hoegen-Chouvalova O, van der Laan BF, Roodenburg JL, van der Wal JE, Schuuring E, Langendijk JA (2013). "FADD expression is associated with regional and distant metastasis in squamous cell carcinoma of the head and neck". <i>Histopathology</i>. <b>63</b> (2): <span class="nowrap">263–</span>270. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1111%2Fhis.12174">10.1111/his.12174</a>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a>&nbsp;<a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/23763459">23763459</a>. <a href="S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a>&nbsp;<a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:36206578">36206578</a>.</cite></span>
</li>
<li id="cite_note-Cimino2012-38"><span class="mw-cite-backlink"><b><a href="#cite_ref-Cimino2012_38-0">^</a></b></span> <span class="reference-text"><cite id="CITEREFCiminoCostesDamotteValidire2012" class="citation journal cs1">Cimino Y, Costes A, Damotte D, Validire P, Mistou S, Cagnard N, Alifano M, Régnard JF, Chiocchia G, Sautès-Fridman C, Tourneur L (2012). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3388563">"FADD protein release mirrors the development and aggressiveness of human non-small cell lung cancer"</a>. <i>British Journal of Cancer</i>. <b>106</b> (12): <span class="nowrap">1989–</span>1996. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1038%2Fbjc.2012.196">10.1038/bjc.2012.196</a>. <a href="PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a>&nbsp;<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3388563">3388563</a></span>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a>&nbsp;<a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/22669160">22669160</a>.</cite></span>
</li>
<li id="cite_note-Park2004-39"><span class="mw-cite-backlink"><b><a href="#cite_ref-Park2004_39-0">^</a></b></span> <span class="reference-text"><cite id="CITEREFParkWuGordonZhong2004" class="citation journal cs1">Park SJ, Wu CH, Gordon JD, Zhong X, Emami A, Safa AR (2004). <a rel="nofollow" class="external text" href="https://doi.org/10.1074%2Fjbc.M406543200">"Taxol induces caspase-10-dependent apoptosis"</a>. <i>Journal of Biological Chemistry</i>. <b>279</b> (49): <span class="nowrap">51057–</span>51067. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://doi.org/10.1074%2Fjbc.M406543200">10.1074/jbc.M406543200</a></span>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a>&nbsp;<a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/15452117">15452117</a>.</cite></span>
</li>
<li id="cite_note-Matsuyoshi2006-40"><span class="mw-cite-backlink"><b><a href="#cite_ref-Matsuyoshi2006_40-0">^</a></b></span> <span class="reference-text"><cite id="CITEREFMatsuyoshiShimadaNakamuraIshida2006" class="citation journal cs1">Matsuyoshi S, Shimada K, Nakamura M, Ishida E, Konishi N (2006). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2361184">"FADD phosphorylation is critical for cell cycle regulation in breast cancer cells"</a>. <i>British Journal of Cancer</i>. <b>94</b> (4): <span class="nowrap">532–</span>539. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1038%2Fsj.bjc.6602955">10.1038/sj.bjc.6602955</a>. <a href="PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a>&nbsp;<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2361184">2361184</a></span>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a>&nbsp;<a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/16450001">16450001</a>.</cite></span>
</li>
<li id="cite_note-Schinske2011-41"><span class="mw-cite-backlink"><b><a href="#cite_ref-Schinske2011_41-0">^</a></b></span> <span class="reference-text"><cite id="CITEREFSchinskeNyatiKhanWilliams2011" class="citation journal cs1">Schinske KA, Nyati S, Khan AP, Williams TM, Johnson TD, Ross BD, Tomás RP, Rehemtulla A (2011). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3191281">"A Novel Kinase Inhibitor of FADD Phosphorylation Chemosensitizes through the Inhibition of NF-kappa B"</a>. <i>Molecular Cancer Therapeutics</i>. <b>10</b> (10): <span class="nowrap">1807–</span>1817. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1158%2F1535-7163.mct-11-0362">10.1158/1535-7163.mct-11-0362</a>. <a href="PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a>&nbsp;<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3191281">3191281</a></span>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a>&nbsp;<a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/21859840">21859840</a>.</cite></span>
</li>
<li id="cite_note-pmid12235128-42"><span class="mw-cite-backlink"><b><a href="#cite_ref-pmid12235128_42-0">^</a></b></span> <span class="reference-text"><cite id="CITEREFBuechlerBaredAslanidisRitter2002" class="citation journal cs1">Buechler C, Bared SM, Aslanidis C, Ritter M, Drobnik W, Schmitz G (Nov 2002). <a rel="nofollow" class="external text" href="https://doi.org/10.1074%2Fjbc.C200436200">"Molecular and functional interaction of the ATP-binding cassette transporter A1 with Fas-associated death domain protein"</a>. <i>J. Biol. Chem</i>. <b>277</b> (44): <span class="nowrap">41307–</span>10. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://doi.org/10.1074%2Fjbc.C200436200">10.1074/jbc.C200436200</a></span>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a>&nbsp;<a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/12235128">12235128</a>.</cite></span>
</li>
<li id="cite_note-pmid11741985-43"><span class="mw-cite-backlink"><b><a href="#cite_ref-pmid11741985_43-0">^</a></b></span> <span class="reference-text"><cite id="CITEREFRothStenner-LiewenPawlowskiGodzik2002" class="citation journal cs1">Roth W, Stenner-Liewen F, Pawlowski K, Godzik A, Reed JC (Mar 2002). <a rel="nofollow" class="external text" href="https://doi.org/10.1074%2Fjbc.M110749200">"Identification and characterization of DEDD2, a death effector domain-containing protein"</a>. <i>J. Biol. Chem</i>. <b>277</b> (9): <span class="nowrap">7501–</span>8. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://doi.org/10.1074%2Fjbc.M110749200">10.1074/jbc.M110749200</a></span>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a>&nbsp;<a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/11741985">11741985</a>.</cite></span>
</li>
<li id="cite_note-pmid12702765-44"><span class="mw-cite-backlink"><b><a href="#cite_ref-pmid12702765_44-0">^</a></b></span> <span class="reference-text"><cite id="CITEREFScreatonKiesslingSansomMillar2003" class="citation journal cs1">Screaton RA, Kiessling S, Sansom OJ, Millar CB, Maddison K, Bird A, Clarke AR, Frisch SM (Apr 2003). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC154324">"Fas-associated death domain protein interacts with methyl-CpG binding domain protein 4: a potential link between genome surveillance and apoptosis"</a>. <i>Proc. Natl. Acad. Sci. U.S.A</i>. <b>100</b> (9): <span class="nowrap">5211–</span>6. <a href="Bibcode_(identifier)" class="mw-redirect" title="Bibcode (identifier)">Bibcode</a>:<a rel="nofollow" class="external text" href="https://ui.adsabs.harvard.edu/abs/2003PNAS..100.5211S">2003PNAS..100.5211S</a>. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://doi.org/10.1073%2Fpnas.0431215100">10.1073/pnas.0431215100</a></span>. <a href="PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a>&nbsp;<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC154324">154324</a></span>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a>&nbsp;<a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/12702765">12702765</a>.</cite></span>
</li>
<li id="cite_note-pmid12684039-45"><span class="mw-cite-backlink"><b><a href="#cite_ref-pmid12684039_45-0">^</a></b></span> <span class="reference-text"><cite id="CITEREFStiloLiguorodi_JesoLeonardi2003" class="citation journal cs1">Stilo R, Liguoro D, di Jeso B, Leonardi A, Vito P (Apr 2003). "The alpha-chain of the nascent polypeptide-associated complex binds to and regulates FADD function". <i>Biochem. Biophys. Res. Commun</i>. <b>303</b> (4): <span class="nowrap">1034–</span>41. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fs0006-291x%2803%2900487-x">10.1016/s0006-291x(03)00487-x</a>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a>&nbsp;<a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/12684039">12684039</a>.</cite></span>
</li>
<li id="cite_note-pmid10442631-46"><span class="mw-cite-backlink"><b><a href="#cite_ref-pmid10442631_46-0">^</a></b></span> <span class="reference-text"><cite id="CITEREFCondorelliVigliottaCafieriTrencia1999" class="citation journal cs1">Condorelli G, Vigliotta G, Cafieri A, Trencia A, Andalò P, Oriente F, Miele C, Caruso M, Formisano P, Beguinot F (Aug 1999). "PED/PEA-15: an anti-apoptotic molecule that regulates FAS/TNFR1-induced apoptosis". <i>Oncogene</i>. <b>18</b> (31): <span class="nowrap">4409–</span>15. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1038%2Fsj.onc.1202831">10.1038/sj.onc.1202831</a>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a>&nbsp;<a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/10442631">10442631</a>. <a href="S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a>&nbsp;<a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:20510429">20510429</a>.</cite></span>
</li>
</ol></div>
<div class="mw-heading mw-heading2"><h2 id="Further_reading">Further reading</h2></div>
<style data-mw-deduplicate="TemplateStyles:r1239549316">
/* start https://en.wikipedia.org/ */


.mw-parser-output .refbegin{margin-bottom:0.5em}.mw-parser-output .refbegin-hanging-indents>ul{margin-left:0}.mw-parser-output .refbegin-hanging-indents>ul>li{margin-left:0;padding-left:3.2em;text-indent:-3.2em}.mw-parser-output .refbegin-hanging-indents ul,.mw-parser-output .refbegin-hanging-indents ul li{list-style:none}@media(max-width:720px){.mw-parser-output .refbegin-hanging-indents>ul>li{padding-left:1.6em;text-indent:-1.6em}}.mw-parser-output .refbegin-columns{margin-top:0.3em}.mw-parser-output .refbegin-columns ul{margin-top:0}.mw-parser-output .refbegin-columns li{page-break-inside:avoid;break-inside:avoid-column}@media screen{.mw-parser-output .refbegin{font-size:90%}}


/* end https://en.wikipedia.org/ */
</style><div class="refbegin refbegin-columns references-column-width" style="column-width: 35em">
<ul><li><cite id="CITEREFBolzeByunMcDonaldMorgan2010" class="citation journal cs1">Bolze A, Byun M, McDonald D, Morgan NV, Abhyankar A, Premkumar L, Puel A, Bacon CM, Rieux-Laucat F, Pang K, Britland A, Abel L, Cant A, Maher ER, Riedl SJ, Hambleton S, Casanova JL (2010). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2997374">"Whole-Exome-Sequencing-Based Discovery of Human FADD Deficiency"</a>. <i>Journal of Human Genetics</i>. <b>87</b> (6): <span class="nowrap">873–</span>881. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fj.ajhg.2010.10.028">10.1016/j.ajhg.2010.10.028</a>. <a href="PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a>&nbsp;<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2997374">2997374</a></span>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a>&nbsp;<a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/21109225">21109225</a>.</cite></li>
<li><cite id="CITEREFWernerWuWalsh2006" class="citation journal cs1">Werner MH, Wu C, Walsh CM (2006). <a rel="nofollow" class="external text" href="https://doi.org/10.4161%2Fcc.5.20.3385">"Emerging roles for the death adaptor FADD in death receptor avidity and cell cycle regulation"</a>. <i>Cell Cycle</i>. <b>5</b> (20): <span class="nowrap">2332–</span>2338. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://doi.org/10.4161%2Fcc.5.20.3385">10.4161/cc.5.20.3385</a></span>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a>&nbsp;<a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/17102623">17102623</a>.</cite></li>
<li><cite id="CITEREFYuShi2008" class="citation journal cs1">Yu JW, Shi Y (2008). <a rel="nofollow" class="external text" href="https://doi.org/10.1038%2Fonc.2008.299">"FLIP and the death effector domain family"</a>. <i>Oncogene</i>. <b>27</b> (48): <span class="nowrap">6216–</span>6227. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://doi.org/10.1038%2Fonc.2008.299">10.1038/onc.2008.299</a></span>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a>&nbsp;<a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/18931689">18931689</a>.</cite></li>
<li><cite id="CITEREFBhojaniChenRossBeer2007" class="citation journal cs1">Bhojani MS, Chen G, Ross BD, Beer DG, Rehemtulla A (2007). <a rel="nofollow" class="external text" href="https://doi.org/10.4161%2Fcc.4.11.2188">"Nuclear localized phosphorylated FADD induces cell proliferation and is associated with aggressive lung cancer"</a>. <i>Cell Cycle</i>. <b>4</b> (11): <span class="nowrap">1478–</span>81. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://doi.org/10.4161%2Fcc.4.11.2188">10.4161/cc.4.11.2188</a></span>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a>&nbsp;<a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/16258269">16258269</a>.</cite></li></ul>
</div>
<div class="mw-heading mw-heading2"><h2 id="External_links">External links</h2></div>
<ul><li><a rel="nofollow" class="external text" href="https://meshb.nlm.nih.gov/record/ui?name=Fas-Associating+Protein+with+Death+Domain">Fas-Associating+Protein+with+Death+Domain</a> at the U.S. National Library of Medicine <a href="Medical_Subject_Headings" title="Medical Subject Headings">Medical Subject Headings</a> (MeSH)</li>
<li>Overview of all the structural information available in the <a href="Protein_Data_Bank" title="Protein Data Bank">PDB</a> for <a href="UniProt" title="UniProt">UniProt</a>: <i><a rel="nofollow" class="external text" href="https://www.ebi.ac.uk/pdbe/pdbe-kb/proteins/Q13158">Q13158</a></i> (Human FAS-associated death domain protein) at the <a href="PDBe-KB" title="PDBe-KB">PDBe-KB</a>.</li>
<li>Overview of all the structural information available in the <a href="Protein_Data_Bank" title="Protein Data Bank">PDB</a> for <a href="UniProt" title="UniProt">UniProt</a>: <i><a rel="nofollow" class="external text" href="https://www.ebi.ac.uk/pdbe/pdbe-kb/proteins/Q61160">Q61160</a></i> (Mouse FAS-associated death domain protein) at the <a href="PDBe-KB" title="PDBe-KB">PDBe-KB</a>.</li></ul>
<div class="navbox-styles"><style data-mw-deduplicate="TemplateStyles:r1129693374">
/* start https://en.wikipedia.org/ */


.mw-parser-output .hlist dl,.mw-parser-output .hlist ol,.mw-parser-output .hlist ul{margin:0;padding:0}.mw-parser-output .hlist dd,.mw-parser-output .hlist dt,.mw-parser-output .hlist li{margin:0;display:inline}.mw-parser-output .hlist.inline,.mw-parser-output .hlist.inline dl,.mw-parser-output .hlist.inline ol,.mw-parser-output .hlist.inline ul,.mw-parser-output .hlist dl dl,.mw-parser-output .hlist dl ol,.mw-parser-output .hlist dl ul,.mw-parser-output .hlist ol dl,.mw-parser-output .hlist ol ol,.mw-parser-output .hlist ol ul,.mw-parser-output .hlist ul dl,.mw-parser-output .hlist ul ol,.mw-parser-output .hlist ul ul{display:inline}.mw-parser-output .hlist .mw-empty-li{display:none}.mw-parser-output .hlist dt::after{content:": "}.mw-parser-output .hlist dd::after,.mw-parser-output .hlist li::after{content:" · ";font-weight:bold}.mw-parser-output .hlist dd:last-child::after,.mw-parser-output .hlist dt:last-child::after,.mw-parser-output .hlist li:last-child::after{content:none}.mw-parser-output .hlist dd dd:first-child::before,.mw-parser-output .hlist dd dt:first-child::before,.mw-parser-output .hlist dd li:first-child::before,.mw-parser-output .hlist dt dd:first-child::before,.mw-parser-output .hlist dt dt:first-child::before,.mw-parser-output .hlist dt li:first-child::before,.mw-parser-output .hlist li dd:first-child::before,.mw-parser-output .hlist li dt:first-child::before,.mw-parser-output .hlist li li:first-child::before{content:" (";font-weight:normal}.mw-parser-output .hlist dd dd:last-child::after,.mw-parser-output .hlist dd dt:last-child::after,.mw-parser-output .hlist dd li:last-child::after,.mw-parser-output .hlist dt dd:last-child::after,.mw-parser-output .hlist dt dt:last-child::after,.mw-parser-output .hlist dt li:last-child::after,.mw-parser-output .hlist li dd:last-child::after,.mw-parser-output .hlist li dt:last-child::after,.mw-parser-output .hlist li li:last-child::after{content:")";font-weight:normal}.mw-parser-output .hlist ol{counter-reset:listitem}.mw-parser-output .hlist ol>li{counter-increment:listitem}.mw-parser-output .hlist ol>li::before{content:" "counter(listitem)"\a0 "}.mw-parser-output .hlist dd ol>li:first-child::before,.mw-parser-output .hlist dt ol>li:first-child::before,.mw-parser-output .hlist li ol>li:first-child::before{content:" ("counter(listitem)"\a0 "}


/* end https://en.wikipedia.org/ */
</style><style data-mw-deduplicate="TemplateStyles:r1236075235">
/* start https://en.wikipedia.org/ */


.mw-parser-output .navbox{box-sizing:border-box;border:1px solid #a2a9b1;width:100%;clear:both;font-size:88%;text-align:center;padding:1px;margin:1em auto 0}.mw-parser-output .navbox .navbox{margin-top:0}.mw-parser-output .navbox+.navbox,.mw-parser-output .navbox+.navbox-styles+.navbox{margin-top:-1px}.mw-parser-output .navbox-inner,.mw-parser-output .navbox-subgroup{width:100%}.mw-parser-output .navbox-group,.mw-parser-output .navbox-title,.mw-parser-output .navbox-abovebelow{padding:0.25em 1em;line-height:1.5em;text-align:center}.mw-parser-output .navbox-group{white-space:nowrap;text-align:right}.mw-parser-output .navbox,.mw-parser-output .navbox-subgroup{background-color:#fdfdfd}.mw-parser-output .navbox-list{line-height:1.5em;border-color:#fdfdfd}.mw-parser-output .navbox-list-with-group{text-align:left;border-left-width:2px;border-left-style:solid}.mw-parser-output tr+tr>.navbox-abovebelow,.mw-parser-output tr+tr>.navbox-group,.mw-parser-output tr+tr>.navbox-image,.mw-parser-output tr+tr>.navbox-list{border-top:2px solid #fdfdfd}.mw-parser-output .navbox-title{background-color:#ccf}.mw-parser-output .navbox-abovebelow,.mw-parser-output .navbox-group,.mw-parser-output .navbox-subgroup .navbox-title{background-color:#ddf}.mw-parser-output .navbox-subgroup .navbox-group,.mw-parser-output .navbox-subgroup .navbox-abovebelow{background-color:#e6e6ff}.mw-parser-output .navbox-even{background-color:#f7f7f7}.mw-parser-output .navbox-odd{background-color:transparent}.mw-parser-output .navbox .hlist td dl,.mw-parser-output .navbox .hlist td ol,.mw-parser-output .navbox .hlist td ul,.mw-parser-output .navbox td.hlist dl,.mw-parser-output .navbox td.hlist ol,.mw-parser-output .navbox td.hlist ul{padding:0.125em 0}.mw-parser-output .navbox .navbar{display:block;font-size:100%}.mw-parser-output .navbox-title .navbar{float:left;text-align:left;margin-right:0.5em}body.skin--responsive .mw-parser-output .navbox-image img{max-width:none!important}@media print{body.ns-0 .mw-parser-output .navbox{display:none!important}}


/* end https://en.wikipedia.org/ */
</style></div><div role="navigation" class="navbox" aria-labelledby="PDB_gallery11" style="padding:3px"><table class="nowraplinks mw-collapsible mw-collapsed navbox-inner" style="border-spacing:0;background:transparent;color:inherit"><tbody><tr><th scope="col" class="navbox-title" colspan="2" style="background:#e7dcc3;color:inherit;"><style data-mw-deduplicate="TemplateStyles:r1239400231">
/* start https://en.wikipedia.org/ */


.mw-parser-output .navbar{display:inline;font-size:88%;font-weight:normal}.mw-parser-output .navbar-collapse{float:left;text-align:left}.mw-parser-output .navbar-boxtext{word-spacing:0}.mw-parser-output .navbar ul{display:inline-block;white-space:nowrap;line-height:inherit}.mw-parser-output .navbar-brackets::before{margin-right:-0.125em;content:"[ "}.mw-parser-output .navbar-brackets::after{margin-left:-0.125em;content:" ]"}.mw-parser-output .navbar li{word-spacing:-0.125em}.mw-parser-output .navbar a>span,.mw-parser-output .navbar a>abbr{text-decoration:inherit}.mw-parser-output .navbar-mini abbr{font-variant:small-caps;border-bottom:none;text-decoration:none;cursor:inherit}.mw-parser-output .navbar-ct-full{font-size:114%;margin:0 7em}.mw-parser-output .navbar-ct-mini{font-size:114%;margin:0 4em}html.skin-theme-clientpref-night .mw-parser-output .navbar li a abbr{color:var(--color-base)!important}@media(prefers-color-scheme:dark){html.skin-theme-clientpref-os .mw-parser-output .navbar li a abbr{color:var(--color-base)!important}}@media print{.mw-parser-output .navbar{display:none!important}}


/* end https://en.wikipedia.org/ */
</style><div id="PDB_gallery11" style="font-size:114%;margin:0 4em">PDB gallery</div></th></tr><tr><td colspan="2" class="navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"><ul class="nochecker gallery mw-gallery-traditional" style="line-height:130%">
<li class="gallerybox" style="width: 215px">
<div class="thumb" style="width: 210px; height: 210px;"><span typeof="mw:File"></span></div>
<div class="gallerytext"><b>1a1w</b>: FADD DEATH EFFECTOR DOMAIN, F25Y MUTANT, NMR MINIMIZED AVERAGE STRUCTURE</div>
</li>
<li class="gallerybox" style="width: 215px">
<div class="thumb" style="width: 210px; height: 210px;"><span typeof="mw:File"></span></div>
<div class="gallerytext"><b>1a1z</b>: FADD DEATH EFFECTOR DOMAIN, F25G MUTANT, NMR MINIMIZED AVERAGE STRUCTURE</div>
</li>
<li class="gallerybox" style="width: 215px">
<div class="thumb" style="width: 210px; height: 210px;"><span typeof="mw:File"></span></div>
<div class="gallerytext"><b>1e3y</b>: DEATH DOMAIN FROM HUMAN FADD/MORT1</div>
</li>
<li class="gallerybox" style="width: 215px">
<div class="thumb" style="width: 210px; height: 210px;"><span typeof="mw:File"></span></div>
<div class="gallerytext"><b>1e41</b>: DEATH DOMAIN FROM HUMAN FADD/MORT1</div>
</li>
<li class="gallerybox" style="width: 215px">
<div class="thumb" style="width: 210px; height: 210px;"><span typeof="mw:File"></span></div>
<div class="gallerytext"><b>2gf5</b>: Structure of intact FADD (MORT1)</div>
</li>
</ul></div></td></tr></tbody></table></div>
<div class="navbox-styles"></div><div role="navigation" class="navbox" aria-labelledby="Apoptosis_signaling_pathway122" style="padding:3px"><table class="nowraplinks mw-collapsible autocollapse navbox-inner" style="border-spacing:0;background:transparent;color:inherit"><tbody><tr><th scope="col" class="navbox-title" colspan="2" style="background:#e7dcc3"><div id="Apoptosis_signaling_pathway122" style="font-size:114%;margin:0 4em"><a href="Apoptosis" title="Apoptosis">Apoptosis</a> <a href="Signal_transduction" title="Signal transduction">signaling pathway</a></div></th></tr><tr><th scope="row" class="navbox-group" style="width:1%;background-color: AntiqueWhite"><a href="Apoptosis#Fas_path" title="Apoptosis">Fas path</a></th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%;background-color: AntiqueWhite"><a href="Ligand_(biochemistry)" title="Ligand (biochemistry)">Ligand</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em">
<ul><li><a href="Fas_ligand" title="Fas ligand">Fas ligand</a></li></ul>
</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%;background-color: AntiqueWhite"><a href="Receptor_(biochemistry)" title="Receptor (biochemistry)">Receptor</a></th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em">
<ul><li><a href="Fas_receptor" title="Fas receptor">Fas receptor</a></li></ul>
</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%;background-color: AntiqueWhite"><a href="Intracellular_signaling_peptides_and_proteins" class="mw-redirect" title="Intracellular signaling peptides and proteins">Intracellular</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><td colspan="2" class="navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em">
<ul><li><a href="Death-inducing_signaling_complex" title="Death-inducing signaling complex">Death-inducing signaling complex</a></li></ul>
<ul><li><a href="DAXX" class="mw-redirect" title="DAXX">DAXX</a></li>
<li><a href="ASK1" title="ASK1">ASK1</a></li></ul>
<ul>
<li><a href="Caspase_8" title="Caspase 8">Caspase 8</a></li>
<li><a href="BH3_interacting_domain_death_agonist" class="mw-redirect" title="BH3 interacting domain death agonist">BID</a></li></ul>
<ul><li><a href="Cytochrome_c" title="Cytochrome c">Cytochrome c</a></li>
<li><a href="Caspase-9" title="Caspase-9">Caspase 9</a></li>
<li><a href="Caspase_3" title="Caspase 3">Caspase 3</a></li></ul>
</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><i><a href="Bcl-2_family" title="Bcl-2 family">Bcl-2 family</a></i></th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em">
<dl><dt><i>Pro-apoptotic:</i></dt>
<dd><a href="Bcl-2-associated_X_protein" class="mw-redirect" title="Bcl-2-associated X protein">BAX</a></dd>
<dd>BAK1/<a href="Bcl-2_homologous_antagonist_killer" title="Bcl-2 homologous antagonist killer">Bcl-2 homologous antagonist killer</a></dd>
<dd><a href="Bcl-2-associated_death_promoter" title="Bcl-2-associated death promoter">Bcl-2-associated death promoter</a></dd></dl>
<dl><dt><i>Anti-apoptotic:</i></dt>
<dd><a href="Bcl-2" title="Bcl-2">Bcl-2</a></dd>
<dd><a href="Bcl-xL" title="Bcl-xL">Bcl-xL</a></dd></dl>
</div></td></tr></tbody></table><div></div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%;background-color: AntiqueWhite"><a href="Apoptosis#TNF_path" title="Apoptosis">TNF path</a></th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%;background-color: AntiqueWhite"><a href="Ligand_(biochemistry)" title="Ligand (biochemistry)">Ligand</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em">
<ul><li><a href="Tumor_necrosis_factor_alpha" class="mw-redirect" title="Tumor necrosis factor alpha">Tumor necrosis factor alpha</a></li></ul>
</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%;background-color: AntiqueWhite"><a href="Receptor_(biochemistry)" title="Receptor (biochemistry)">Receptor</a></th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em">
<ul><li><a href="Tumor_necrosis_factor_receptor_1" title="Tumor necrosis factor receptor 1">Tumor necrosis factor receptor 1</a></li>
<li><a href="Tumor_necrosis_factor_receptor_2" title="Tumor necrosis factor receptor 2">Tumor necrosis factor receptor 2</a></li></ul>
</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%;background-color: AntiqueWhite"><a href="Intracellular_signaling_peptides_and_proteins" class="mw-redirect" title="Intracellular signaling peptides and proteins">Intracellular</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em">
<ul><li><a href="TRADD" title="TRADD">TRADD</a></li></ul>
<ul>
<li><a href="Caspase_8" title="Caspase 8">Caspase 8</a></li>
<li><a href="Caspase_3" title="Caspase 3">Caspase 3</a></li>
<li><a href="BH3_interacting_domain_death_agonist" class="mw-redirect" title="BH3 interacting domain death agonist">BID</a></li></ul>
<ul><li><a href="TRAF2" title="TRAF2">TRAF2</a></li>
<li><a href="ASK1" title="ASK1">ASK-1</a></li>
<li><a href="MAP3K1" title="MAP3K1">MEKK1</a></li>
<li><a href="I%CE%BAB_kinase" title="IκB kinase">IKK</a></li>
<li><a href="I%CE%BAB%CE%B1" title="IκBα">IκBα</a></li>
<li><a href="MAP2K7" title="MAP2K7">MKK7</a></li>
<li><a href="C-Jun_N-terminal_kinases" title="C-Jun N-terminal kinases">JNK</a></li>
<li><a href="NF-%CE%BAB" title="NF-κB">NF-κB</a></li></ul>
</div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%;background-color: AntiqueWhite">Other</th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th id="Intracellular63" scope="row" class="navbox-group" style="width:1%;background-color: AntiqueWhite; text-align:center; padding-left:3.6em;"><a href="Intracellular_signaling_peptides_and_proteins" class="mw-redirect" title="Intracellular signaling peptides and proteins">Intracellular</a></th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em">
<dl><dt><a href="Inhibitor_of_apoptosis" title="Inhibitor of apoptosis">IAPs</a></dt>
<dd><a href="XIAP" title="XIAP">XIAP</a></dd>
<dd><a href="NAIP_(gene)" title="NAIP (gene)">NAIP</a></dd>
<dd><a href="Survivin" title="Survivin">Survivin</a></dd>
<dd><a href="BIRC2" class="mw-redirect" title="BIRC2">c-IAP-1</a></dd>
<dd><a href="BIRC3" class="mw-redirect" title="BIRC3">c-IAP-2</a></dd></dl>
<ul><li><a href="Apoptosis-inducing_factor" title="Apoptosis-inducing factor">Apoptosis-inducing factor</a></li></ul>
</div></td></tr></tbody></table><div></div></td></tr></tbody></table></div></div><!--htdig_noindex--><div><div class="zim-footer">
This article is issued from <a class="external text" title="Last edited on 2025-06-02" href="https://en.wikipedia.org/wiki/?title=FADD&amp;oldid=1293533238">Wikipedia</a>. The text is available under <a class="external text" href="https://creativecommons.org/licenses/by-sa/4.0/deed.en">Creative Commons Attribution-Share Alike 4.0</a> unless otherwise noted. Additional terms may apply for the media files.
</div>
</div><!--/htdig_noindex--></div>
</div>
</main>
</div>
</div>
</div>

</body></html>