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Entry version 197 (13 Feb 2019)
Sequence version 1 (01 Nov 1997)
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Protein

FAS-associated death domain protein

Gene

FADD

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

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

Apoptotic adaptor molecule that recruits caspase-8 or caspase-10 to the activated Fas (CD95) or TNFR-1 receptors. The resulting aggregate called the death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation. Active caspase-8 initiates the subsequent cascade of caspases mediating apoptosis. Involved in interferon-mediated antiviral immune response, playing a role in the positive regulation of interferon signaling.4 Publications

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

GO - Biological processi

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

Biological processApoptosis, Host-virus interaction, Immunity, Innate immunity

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-140534 Caspase activation via Death Receptors in the presence of ligand
R-HSA-2562578 TRIF-mediated programmed cell death
R-HSA-3371378 Regulation by c-FLIP
R-HSA-5213460 RIPK1-mediated regulated necrosis
R-HSA-5218900 CASP8 activity is inhibited
R-HSA-5357786 TNFR1-induced proapoptotic signaling
R-HSA-69416 Dimerization of procaspase-8
R-HSA-75157 FasL/ CD95L signaling
R-HSA-75158 TRAIL signaling
R-HSA-9013957 TLR3-mediated TICAM1-dependent programmed cell death
R-HSA-933543 NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
Q13158

SIGNOR Signaling Network Open Resource

More...
SIGNORi
Q13158

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

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
FAS-associated death domain protein
Alternative name(s):
FAS-associating death domain-containing protein
Growth-inhibiting gene 3 protein
Mediator of receptor induced toxicity
Protein FADD
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:FADD
Synonyms:MORT1
ORF Names:GIG3
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 11

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000168040.4

Human Gene Nomenclature Database

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HGNCi
HGNC:3573 FADD

Online Mendelian Inheritance in Man (OMIM)

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MIMi
602457 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_Q13158

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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

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

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Infections, recurrent, associated with encephalopathy, hepatic dysfunction and cardiovascular malformations (IEHDCM)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA condition with biological features of autoimmune lymphoproliferative syndrome such as high-circulating CD4(-)CD8(-)TCR-alpha-beta(+) T-cell counts, and elevated IL10 and FASL levels. Affected individuals suffer from recurrent, stereotypical episodes of fever, encephalopathy, and mild liver dysfunction sometimes accompanied by generalized seizures. The episodes can be triggered by varicella zoster virus (VZV), measles mumps rubella (MMR) attenuated vaccine, parainfluenza virus, and Epstein-Barr virus (EBV).
See also OMIM:613759
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_065124105C → W in IEHDCM; reduced folding stability as measured by differential scanning calorimetry of the mutant protein; impairs interaction with FAS. 1 PublicationCorresponds to variant dbSNP:rs387906839EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi12S → R: Loss of interaction with CASP8. 1 Publication1
Mutagenesisi25F → R: Loss of interaction with FAS. Loss of self-association. Abolishes induction of apoptosis. 1 Publication1
Mutagenesisi33K → E: Loss of self-association. 1 Publication1
Mutagenesisi38R → A: Loss of interaction with CASP8. 1 Publication1
Mutagenesisi44D → R: Loss of interaction with CASP8. Abolishes induction of apoptosis. Decreased interaction with FAS. 1 Publication1
Mutagenesisi51E → R: Loss of interaction with CASP8. 1 Publication1
Mutagenesisi117R → E: Loss of interaction with FAS. 1 Publication1
Mutagenesisi121V → N: Loss of interaction with FAS. 1 Publication1
Mutagenesisi123D → R: Strongly decreased interaction with FAS. 1 Publication1
Mutagenesisi135R → E: Strongly decreased interaction with FAS. 1 Publication1
Mutagenesisi142R → E: Decreased interaction with FAS. 1 Publication1
Mutagenesisi172L → A or E: Loss of interaction with FAS. 2 Publications1
Mutagenesisi172L → K: Strongly decreased interaction with FAS. 2 Publications1
Mutagenesisi175D → K: Strongly decreased interaction with FAS. 1 Publication1
Mutagenesisi176L → E: Decreased interaction with FAS. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

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DisGeNETi
8772

MalaCards human disease database

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MalaCardsi
FADD
MIMi613759 phenotype

Open Targets

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OpenTargetsi
ENSG00000168040

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
306550 FADD-related immunodeficiency
99806 Oculootodental syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA27972

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
FADD

Domain mapping of disease mutations (DMDM)

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DMDMi
2498355

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001912791 – 208FAS-associated death domain proteinAdd BLAST208

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei194PhosphoserineCombined sources1 Publication1

Keywords - PTMi

Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q13158

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q13158

MaxQB - The MaxQuant DataBase

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MaxQBi
Q13158

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q13158

PeptideAtlas

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PeptideAtlasi
Q13158

PRoteomics IDEntifications database

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PRIDEi
Q13158

ProteomicsDB human proteome resource

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ProteomicsDBi
59197

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q13158

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
Q13158

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

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

Expressed in a wide variety of tissues, except for peripheral blood mononuclear leukocytes.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000168040 Expressed in 211 organ(s), highest expression level in blood

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q13158 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB010209
HPA001464

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

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

Can self-associate. Interacts with CFLAR, PEA15 and MBD4. When phosphorylated, part of a complex containing HIPK3 and FAS. May interact with MAVS/IPS1. Interacts with MOCV v-CFLAR protein and PIDD1. Interacts (via death domain) with FAS (via death domain). Interacts with CASP8. Interacts directly (via DED domain) with NOL3 (via CARD domain); inhibits death-inducing signaling complex (DISC) assembly by inhibiting the increase in FAS-FADD binding induced by FAS activation (By similarity).By similarity9 Publications
(Microbial infection) Interacts with human papillomavirus 16/HPV16 protein E6.1 Publication
(Microbial infection) Interacts with molluscum contagiosum virus proteins MC159L/v-CFLAR and MC160L.1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
114302, 68 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-1907 Ripoptosome

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q13158

Database of interacting proteins

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DIPi
DIP-286N

Protein interaction database and analysis system

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IntActi
Q13158, 72 interactors

Molecular INTeraction database

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MINTi
Q13158

STRING: functional protein association networks

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STRINGi
9606.ENSP00000301838

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

Secondary structure

1208
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A1WNMR-A1-83[»]
1A1ZNMR-A1-83[»]
1E3YNMR-A93-192[»]
1E41NMR-A93-192[»]
2GF5NMR-A2-191[»]
3EZQX-ray2.73B/D/F/H/J/L/N/P93-208[»]
3OQ9X-ray6.80H/I/J/K/L93-184[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q13158

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q13158

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
Q13158

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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini3 – 81DEDPROSITE-ProRule annotationAdd BLAST79
Domaini97 – 181DeathPROSITE-ProRule annotationAdd BLAST85

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

Contains a death domain involved in the binding of the corresponding domain within Fas receptor.1 Publication
The interaction between the FAS and FADD death domains is crucial for the formation of the death-inducing signaling complex (DISC).1 Publication

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
ENOG410J0KM Eukaryota
ENOG41122TX LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00390000002105

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000112490

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG000853

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q13158

KEGG Orthology (KO)

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KOi
K02373

Identification of Orthologs from Complete Genome Data

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OMAi
ELKFLCR

Database of Orthologous Groups

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OrthoDBi
1619689at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q13158

TreeFam database of animal gene trees

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TreeFami
TF102046

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR011029 DEATH-like_dom_sf
IPR000488 Death_domain
IPR001875 DED_dom
IPR016729 FADD

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00531 Death, 1 hit
PF01335 DED, 1 hit

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF018586 FADD, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00005 DEATH, 1 hit
SM00031 DED, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF47986 SSF47986, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS50017 DEATH_DOMAIN, 1 hit
PS50168 DED, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

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

Q13158-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDPFLVLLHS VSSSLSSSEL TELKFLCLGR VGKRKLERVQ SGLDLFSMLL
60 70 80 90 100
EQNDLEPGHT ELLRELLASL RRHDLLRRVD DFEAGAAAGA APGEEDLCAA
110 120 130 140 150
FNVICDNVGK DWRRLARQLK VSDTKIDSIE DRYPRNLTER VRESLRIWKN
160 170 180 190 200
TEKENATVAH LVGALRSCQM NLVADLVQEV QQARDLQNRS GAMSPMSWNS

DASTSEAS
Length:208
Mass (Da):23,279
Last modified:November 1, 1997 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i0E65E2F852E83507
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti32G → V in CAA59197 (PubMed:7536190).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_065124105C → W in IEHDCM; reduced folding stability as measured by differential scanning calorimetry of the mutant protein; impairs interaction with FAS. 1 PublicationCorresponds to variant dbSNP:rs387906839EnsemblClinVar.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U24231 mRNA Translation: AAA86517.1
X84709 mRNA Translation: CAA59197.1
AY423721 mRNA Translation: AAS00484.1
AK291005 mRNA Translation: BAF83694.1
BT006927 mRNA Translation: AAP35573.1
CR456738 mRNA Translation: CAG33019.1
DQ449938 Genomic DNA Translation: ABD96828.1
CH471076 Genomic DNA Translation: EAW74761.1
BC000334 mRNA Translation: AAH00334.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS8196.1

Protein sequence database of the Protein Information Resource

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PIRi
A56912

NCBI Reference Sequences

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RefSeqi
NP_003815.1, NM_003824.3

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.86131

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000301838; ENSP00000301838; ENSG00000168040

Database of genes from NCBI RefSeq genomes

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GeneIDi
8772

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:8772

UCSC genome browser

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UCSCi
uc001opm.3 human

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

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

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

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U24231 mRNA Translation: AAA86517.1
X84709 mRNA Translation: CAA59197.1
AY423721 mRNA Translation: AAS00484.1
AK291005 mRNA Translation: BAF83694.1
BT006927 mRNA Translation: AAP35573.1
CR456738 mRNA Translation: CAG33019.1
DQ449938 Genomic DNA Translation: ABD96828.1
CH471076 Genomic DNA Translation: EAW74761.1
BC000334 mRNA Translation: AAH00334.1
CCDSiCCDS8196.1
PIRiA56912
RefSeqiNP_003815.1, NM_003824.3
UniGeneiHs.86131

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A1WNMR-A1-83[»]
1A1ZNMR-A1-83[»]
1E3YNMR-A93-192[»]
1E41NMR-A93-192[»]
2GF5NMR-A2-191[»]
3EZQX-ray2.73B/D/F/H/J/L/N/P93-208[»]
3OQ9X-ray6.80H/I/J/K/L93-184[»]
ProteinModelPortaliQ13158
SMRiQ13158
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114302, 68 interactors
ComplexPortaliCPX-1907 Ripoptosome
CORUMiQ13158
DIPiDIP-286N
IntActiQ13158, 72 interactors
MINTiQ13158
STRINGi9606.ENSP00000301838

PTM databases

iPTMnetiQ13158
PhosphoSitePlusiQ13158

Polymorphism and mutation databases

BioMutaiFADD
DMDMi2498355

Proteomic databases

EPDiQ13158
jPOSTiQ13158
MaxQBiQ13158
PaxDbiQ13158
PeptideAtlasiQ13158
PRIDEiQ13158
ProteomicsDBi59197

Protocols and materials databases

The DNASU plasmid repository

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DNASUi
8772
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000301838; ENSP00000301838; ENSG00000168040
GeneIDi8772
KEGGihsa:8772
UCSCiuc001opm.3 human

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
8772
DisGeNETi8772
EuPathDBiHostDB:ENSG00000168040.4

GeneCards: human genes, protein and diseases

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GeneCardsi
FADD
HGNCiHGNC:3573 FADD
HPAiCAB010209
HPA001464
MalaCardsiFADD
MIMi602457 gene
613759 phenotype
neXtProtiNX_Q13158
OpenTargetsiENSG00000168040
Orphaneti306550 FADD-related immunodeficiency
99806 Oculootodental syndrome
PharmGKBiPA27972

GenAtlas: human gene database

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GenAtlasi
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Phylogenomic databases

eggNOGiENOG410J0KM Eukaryota
ENOG41122TX LUCA
GeneTreeiENSGT00390000002105
HOGENOMiHOG000112490
HOVERGENiHBG000853
InParanoidiQ13158
KOiK02373
OMAiELKFLCR
OrthoDBi1619689at2759
PhylomeDBiQ13158
TreeFamiTF102046

Enzyme and pathway databases

ReactomeiR-HSA-140534 Caspase activation via Death Receptors in the presence of ligand
R-HSA-2562578 TRIF-mediated programmed cell death
R-HSA-3371378 Regulation by c-FLIP
R-HSA-5213460 RIPK1-mediated regulated necrosis
R-HSA-5218900 CASP8 activity is inhibited
R-HSA-5357786 TNFR1-induced proapoptotic signaling
R-HSA-69416 Dimerization of procaspase-8
R-HSA-75157 FasL/ CD95L signaling
R-HSA-75158 TRAIL signaling
R-HSA-9013957 TLR3-mediated TICAM1-dependent programmed cell death
R-HSA-933543 NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10
SignaLinkiQ13158
SIGNORiQ13158

Miscellaneous databases

EvolutionaryTraceiQ13158

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
FADD

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
8772

Protein Ontology

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PROi
PR:Q13158

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000168040 Expressed in 211 organ(s), highest expression level in blood
GenevisibleiQ13158 HS

Family and domain databases

InterProiView protein in InterPro
IPR011029 DEATH-like_dom_sf
IPR000488 Death_domain
IPR001875 DED_dom
IPR016729 FADD
PfamiView protein in Pfam
PF00531 Death, 1 hit
PF01335 DED, 1 hit
PIRSFiPIRSF018586 FADD, 1 hit
SMARTiView protein in SMART
SM00005 DEATH, 1 hit
SM00031 DED, 1 hit
SUPFAMiSSF47986 SSF47986, 1 hit
PROSITEiView protein in PROSITE
PS50017 DEATH_DOMAIN, 1 hit
PS50168 DED, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

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

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiFADD_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q13158
Secondary accession number(s): Q14866, Q6IBR4
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: February 13, 2019
This is version 197 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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