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FAS-associated death domain protein (FAS-associating death domain-containing protein) (Growth-inhibiting gene 3 protein) (Mediator of receptor induced toxicity) (Protein FADD)

 FADD_HUMAN              Reviewed;         208 AA.
Q13158; Q14866; Q6IBR4;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 1.
25-OCT-2017, entry version 184.
RecName: Full=FAS-associated death domain protein;
AltName: Full=FAS-associating death domain-containing protein;
AltName: Full=Growth-inhibiting gene 3 protein;
AltName: Full=Mediator of receptor induced toxicity;
AltName: Full=Protein FADD;
Name=FADD; Synonyms=MORT1; ORFNames=GIG3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND MUTAGENESIS.
TISSUE=Umbilical vein endothelial cell;
PubMed=7538907; DOI=10.1016/0092-8674(95)90071-3;
Chinnaiyan A.M., O'Rourke K., Tewari M., Dixit V.M.;
"FADD, a novel death domain-containing protein, interacts with the
death domain of Fas and initiates apoptosis.";
Cell 81:505-512(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7536190; DOI=10.1074/jbc.270.14.7795;
Boldin M.P., Varfolomeev E.E., Pancer Z., Mett I.L., Camonis J.H.,
Wallach D.;
"A novel protein that interacts with the death domain of Fas/APO1
contains a sequence motif related to the death domain.";
J. Biol. Chem. 270:7795-7798(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kim J.W.;
"Identification of a human growth inhibition gene 3 (GIG3).";
Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
INTERACTION WITH PEA15.
PubMed=10442631; DOI=10.1038/sj.onc.1202831;
Condorelli G., Vigliotta G., Cafieri A., Trencia A., Andalo P.,
Oriente F., Miele C., Caruso M., Formisano P., Beguinot F.;
"PED/PEA-15: an anti-apoptotic molecule that regulates FAS/TNFR1-
induced apoptosis.";
Oncogene 18:4409-4415(1999).
[11]
INTERACTION WITH PIDD1.
PubMed=10825539; DOI=10.1016/S0167-4838(00)00029-7;
Telliez J.-B., Bean K.M., Lin L.-L.;
"LRDD, a novel leucine rich repeat and death domain containing
protein.";
Biochim. Biophys. Acta 1478:280-288(2000).
[12]
IDENTIFICATION IN A COMPLEX WITH HIPK3 AND FAS, AND PHOSPHORYLATION AT
SER-194.
PubMed=11034606; DOI=10.1084/jem.192.8.1165;
Rochat-Steiner V., Becker K., Micheau O., Schneider P., Burns K.,
Tschopp J.;
"FIST/HIPK3: a Fas/FADD-interacting serine/threonine kinase that
induces FADD phosphorylation and inhibits Fas-mediated Jun NH2-
terminal kinase activation.";
J. Exp. Med. 192:1165-1174(2000).
[13]
INTERACTION WITH MBD4.
PubMed=12702765; DOI=10.1073/pnas.0431215100;
Screaton R.A., Kiessling S., Sansom O.J., Millar C.B., Maddison K.,
Bird A., Clarke A.R., Frisch S.M.;
"Fas-associated death domain protein interacts with methyl-CpG binding
domain protein 4: a potential link between genome surveillance and
apoptosis.";
Proc. Natl. Acad. Sci. U.S.A. 100:5211-5216(2003).
[14]
INTERACTION WITH MAVS.
PubMed=16127453; DOI=10.1038/ni1243;
Kawai T., Takahashi K., Sato S., Coban C., Kumar H., Kato H.,
Ishii K.J., Takeuchi O., Akira S.;
"IPS-1, an adaptor triggering RIG-I- and Mda5-mediated type I
interferon induction.";
Nat. Immunol. 6:981-988(2005).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[17]
FUNCTION IN INTERFERON-MEDIATED IMMUNITY, INTERACTION WITH FAS,
VARIANT IEHDCM TRP-105, AND CHARACTERIZATION OF VARIANT IEHDCM
TRP-105.
PubMed=21109225; DOI=10.1016/j.ajhg.2010.10.028;
Bolze A., Byun M., McDonald D., Morgan N.V., Abhyankar A.,
Premkumar L., Puel A., Bacon C.M., Rieux-Laucat F., Pang K.,
Britland A., Abel L., Cant A., Maher E.R., Riedl S.J., Hambleton S.,
Casanova J.L.;
"Whole-exome-sequencing-based discovery of human FADD deficiency.";
Am. J. Hum. Genet. 87:873-881(2010).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[22]
STRUCTURE BY NMR OF 1-83.
PubMed=9582077; DOI=10.1038/31972;
Eberstadt M., Huang B., Chen Z., Meadows R.P., Ng S.C., Zheng L.,
Lenardo M.J., Fesik S.W.;
"NMR structure and mutagenesis of the FADD (Mort1) death-effector
domain.";
Nature 392:941-945(1998).
[23]
STRUCTURE BY NMR OF 93-192.
PubMed=10964568; DOI=10.1006/jmbi.2000.4011;
Berglund H., Olerenshaw D., Sankar A., Federwisch M., McDonald N.Q.,
Driscoll P.C.;
"The three-dimensional solution structure and dynamic properties of
the human FADD death domain.";
J. Mol. Biol. 302:171-188(2000).
[24]
STRUCTURE BY NMR OF 2-191, FUNCTION, INTERACTION WITH FAS AND CASP8,
AND MUTAGENESIS OF SER-12; PHE-25; LYS-33; ARG-38; ASP-44 AND GLU-51.
PubMed=16762833; DOI=10.1016/j.molcel.2006.04.018;
Carrington P.E., Sandu C., Wei Y., Hill J.M., Morisawa G., Huang T.,
Gavathiotis E., Wei Y., Werner M.H.;
"The structure of FADD and its mode of interaction with procaspase-
8.";
Mol. Cell 22:599-610(2006).
[25]
X-RAY CRYSTALLOGRAPHY (2.73 ANGSTROMS) OF 93-208 IN COMPLEX WITH FAS,
FUNCTION, SUBUNIT, ELECTRON MICROSCOPY, DOMAIN, AND MUTAGENESIS OF
LEU-172 AND LEU-176.
PubMed=19118384; DOI=10.1038/nature07606;
Scott F.L., Stec B., Pop C., Dobaczewska M.K., Lee J.J., Monosov E.,
Robinson H., Salvesen G.S., Schwarzenbacher R., Riedl S.J.;
"The Fas-FADD death domain complex structure unravels signalling by
receptor clustering.";
Nature 457:1019-1022(2009).
[26]
X-RAY CRYSTALLOGRAPHY (6.80 ANGSTROMS) OF 93-184 IN COMPLEX WITH FAS,
ELECTRON MICROSCOPY, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY,
SUBUNIT, AND MUTAGENESIS OF ARG-117; ASP-123; ARG-135; ARG-142;
LEU-172 AND ASP-175.
PubMed=20935634; DOI=10.1038/nsmb.1920;
Wang L., Yang J.K., Kabaleeswaran V., Rice A.J., Cruz A.C., Park A.Y.,
Yin Q., Damko E., Jang S.B., Raunser S., Robinson C.V., Siegel R.M.,
Walz T., Wu H.;
"The Fas-FADD death domain complex structure reveals the basis of DISC
assembly and disease mutations.";
Nat. Struct. Mol. Biol. 17:1324-1329(2010).
-!- FUNCTION: 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.
{ECO:0000269|PubMed:16762833, ECO:0000269|PubMed:19118384,
ECO:0000269|PubMed:20935634, ECO:0000269|PubMed:21109225}.
-!- SUBUNIT: 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).
{ECO:0000250|UniProtKB:Q61160, ECO:0000269|PubMed:10442631,
ECO:0000269|PubMed:10825539, ECO:0000269|PubMed:11034606,
ECO:0000269|PubMed:12702765, ECO:0000269|PubMed:16127453,
ECO:0000269|PubMed:16762833, ECO:0000269|PubMed:19118384,
ECO:0000269|PubMed:20935634, ECO:0000269|PubMed:21109225}.
-!- INTERACTION:
Self; NbExp=7; IntAct=EBI-494804, EBI-494804;
Q14790:CASP8; NbExp=42; IntAct=EBI-494804, EBI-78060;
Q14790-1:CASP8; NbExp=5; IntAct=EBI-494804, EBI-288309;
Q14790-5:CASP8; NbExp=4; IntAct=EBI-494804, EBI-288326;
B7UI21:E2348C_3231 (xeno); NbExp=7; IntAct=EBI-494804, EBI-16070376;
P25445:FAS; NbExp=21; IntAct=EBI-494804, EBI-494743;
P25445-1:FAS; NbExp=17; IntAct=EBI-494804, EBI-15749113;
P25446:Fas (xeno); NbExp=8; IntAct=EBI-494804, EBI-296206;
P48023:FASLG; NbExp=4; IntAct=EBI-494804, EBI-495538;
Q5S007:LRRK2; NbExp=4; IntAct=EBI-494804, EBI-5323863;
O95243:MBD4; NbExp=6; IntAct=EBI-494804, EBI-348011;
Q99836:MYD88; NbExp=3; IntAct=EBI-494804, EBI-447677;
Q99497:PARK7; NbExp=9; IntAct=EBI-494804, EBI-1164361;
P53350:PLK1; NbExp=9; IntAct=EBI-494804, EBI-476768;
Q13546:RIPK1; NbExp=11; IntAct=EBI-494804, EBI-358507;
O00560:SDCBP; NbExp=4; IntAct=EBI-494804, EBI-727004;
Q15628:TRADD; NbExp=6; IntAct=EBI-494804, EBI-359215;
-!- TISSUE SPECIFICITY: Expressed in a wide variety of tissues, except
for peripheral blood mononuclear leukocytes.
-!- DOMAIN: Contains a death domain involved in the binding of the
corresponding domain within Fas receptor.
{ECO:0000269|PubMed:19118384}.
-!- DOMAIN: The interaction between the FAS and FADD death domains is
crucial for the formation of the death-inducing signaling complex
(DISC). {ECO:0000269|PubMed:19118384}.
-!- DISEASE: Infections, recurrent, associated with encephalopathy,
hepatic dysfunction and cardiovascular malformations (IEHDCM)
[MIM:613759]: A 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). {ECO:0000269|PubMed:21109225}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/fadd/";
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EMBL; U24231; AAA86517.1; -; mRNA.
EMBL; X84709; CAA59197.1; -; mRNA.
EMBL; AY423721; AAS00484.1; -; mRNA.
EMBL; AK291005; BAF83694.1; -; mRNA.
EMBL; BT006927; AAP35573.1; -; mRNA.
EMBL; CR456738; CAG33019.1; -; mRNA.
EMBL; DQ449938; ABD96828.1; -; Genomic_DNA.
EMBL; CH471076; EAW74761.1; -; Genomic_DNA.
EMBL; BC000334; AAH00334.1; -; mRNA.
CCDS; CCDS8196.1; -.
PIR; A56912; A56912.
RefSeq; NP_003815.1; NM_003824.3.
UniGene; Hs.86131; -.
PDB; 1A1W; NMR; -; A=1-83.
PDB; 1A1Z; NMR; -; A=1-83.
PDB; 1E3Y; NMR; -; A=93-192.
PDB; 1E41; NMR; -; A=93-192.
PDB; 2GF5; NMR; -; A=2-191.
PDB; 3EZQ; X-ray; 2.73 A; B/D/F/H/J/L/N/P=93-208.
PDB; 3OQ9; X-ray; 6.80 A; H/I/J/K/L=93-184.
PDBsum; 1A1W; -.
PDBsum; 1A1Z; -.
PDBsum; 1E3Y; -.
PDBsum; 1E41; -.
PDBsum; 2GF5; -.
PDBsum; 3EZQ; -.
PDBsum; 3OQ9; -.
ProteinModelPortal; Q13158; -.
SMR; Q13158; -.
BioGrid; 114302; 67.
CORUM; Q13158; -.
DIP; DIP-286N; -.
IntAct; Q13158; 42.
MINT; MINT-91814; -.
STRING; 9606.ENSP00000301838; -.
iPTMnet; Q13158; -.
PhosphoSitePlus; Q13158; -.
BioMuta; FADD; -.
DMDM; 2498355; -.
EPD; Q13158; -.
MaxQB; Q13158; -.
PaxDb; Q13158; -.
PeptideAtlas; Q13158; -.
PRIDE; Q13158; -.
DNASU; 8772; -.
Ensembl; ENST00000301838; ENSP00000301838; ENSG00000168040.
GeneID; 8772; -.
KEGG; hsa:8772; -.
UCSC; uc001opm.3; human.
CTD; 8772; -.
DisGeNET; 8772; -.
EuPathDB; HostDB:ENSG00000168040.4; -.
GeneCards; FADD; -.
HGNC; HGNC:3573; FADD.
HPA; CAB010209; -.
HPA; HPA001464; -.
MalaCards; FADD; -.
MIM; 602457; gene.
MIM; 613759; phenotype.
neXtProt; NX_Q13158; -.
OpenTargets; ENSG00000168040; -.
Orphanet; 306550; FADD-related immunodeficiency.
Orphanet; 99806; Oculootodental syndrome.
PharmGKB; PA27972; -.
eggNOG; ENOG410J0KM; Eukaryota.
eggNOG; ENOG41122TX; LUCA.
GeneTree; ENSGT00390000002105; -.
HOGENOM; HOG000112490; -.
HOVERGEN; HBG000853; -.
InParanoid; Q13158; -.
KO; K02373; -.
OMA; CQMNLVA; -.
OrthoDB; EOG091G0SHT; -.
PhylomeDB; Q13158; -.
TreeFam; TF102046; -.
Reactome; R-HSA-140534; Ligand-dependent caspase activation.
Reactome; R-HSA-2562578; TRIF-mediated programmed cell death.
Reactome; R-HSA-3371378; Regulation by c-FLIP.
Reactome; R-HSA-5213460; RIPK1-mediated regulated necrosis.
Reactome; R-HSA-5218900; CASP8 activity is inhibited.
Reactome; R-HSA-5357786; TNFR1-induced proapoptotic signaling.
Reactome; R-HSA-69416; Dimerization of procaspase-8.
Reactome; R-HSA-75157; FasL/ CD95L signaling.
Reactome; R-HSA-75158; TRAIL signaling.
Reactome; R-HSA-933543; NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10.
SignaLink; Q13158; -.
SIGNOR; Q13158; -.
EvolutionaryTrace; Q13158; -.
GeneWiki; FADD; -.
GenomeRNAi; 8772; -.
PRO; PR:Q13158; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000168040; -.
CleanEx; HS_FADD; -.
Genevisible; Q13158; HS.
GO; GO:0031265; C:CD95 death-inducing signaling complex; IDA:UniProtKB.
GO; GO:0044297; C:cell body; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:ParkinsonsUK-UCL.
GO; GO:0031264; C:death-inducing signaling complex; IDA:UniProtKB.
GO; GO:0045121; C:membrane raft; IEA:Ensembl.
GO; GO:0043005; C:neuron projection; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0097342; C:ripoptosome; IDA:UniProtKB.
GO; GO:0089720; F:caspase binding; IPI:AgBase.
GO; GO:0035877; F:death effector domain binding; IPI:UniProtKB.
GO; GO:0005123; F:death receptor binding; TAS:ProtInc.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0002020; F:protease binding; IPI:UniProtKB.
GO; GO:0032403; F:protein complex binding; IEA:Ensembl.
GO; GO:0033612; F:receptor serine/threonine kinase binding; IEA:Ensembl.
GO; GO:0005164; F:tumor necrosis factor receptor binding; IEA:Ensembl.
GO; GO:0032813; F:tumor necrosis factor receptor superfamily binding; IPI:UniProtKB.
GO; GO:0097202; P:activation of cysteine-type endopeptidase activity; IDA:BHF-UCL.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; TAS:Reactome.
GO; GO:0097296; P:activation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; TAS:Reactome.
GO; GO:0006915; P:apoptotic process; IMP:UniProtKB.
GO; GO:0097190; P:apoptotic signaling pathway; IDA:BHF-UCL.
GO; GO:0048148; P:behavioral response to cocaine; IEA:Ensembl.
GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:Reactome.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:UniProtKB.
GO; GO:0071550; P:death-inducing signaling complex assembly; TAS:Reactome.
GO; GO:0051607; P:defense response to virus; IMP:UniProtKB.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IDA:UniProtKB.
GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; TAS:ProtInc.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0048535; P:lymph node development; ISS:UniProtKB.
GO; GO:0097049; P:motor neuron apoptotic process; IEA:Ensembl.
GO; GO:0097527; P:necroptotic signaling pathway; IMP:BHF-UCL.
GO; GO:0070236; P:negative regulation of activation-induced cell death of T cells; ISS:UniProtKB.
GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; TAS:Reactome.
GO; GO:0060546; P:negative regulation of necroptotic process; IEA:Ensembl.
GO; GO:0042104; P:positive regulation of activated T cell proliferation; ISS:UniProtKB.
GO; GO:0002821; P:positive regulation of adaptive immune response; ISS:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
GO; GO:2000454; P:positive regulation of CD8-positive, alpha-beta cytotoxic T cell extravasation; ISS:UniProtKB.
GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IMP:UniProtKB.
GO; GO:1902043; P:positive regulation of extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEP:UniProtKB.
GO; GO:0032729; P:positive regulation of interferon-gamma production; ISS:UniProtKB.
GO; GO:0032757; P:positive regulation of interleukin-8 production; IDA:BHF-UCL.
GO; GO:0045651; P:positive regulation of macrophage differentiation; IMP:UniProtKB.
GO; GO:0045862; P:positive regulation of proteolysis; IDA:BHF-UCL.
GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IDA:BHF-UCL.
GO; GO:0060340; P:positive regulation of type I interferon-mediated signaling pathway; IMP:UniProtKB.
GO; GO:1902041; P:regulation of extrinsic apoptotic signaling pathway via death domain receptors; TAS:Reactome.
GO; GO:0043278; P:response to morphine; IEA:Ensembl.
GO; GO:0048536; P:spleen development; ISS:UniProtKB.
GO; GO:0033077; P:T cell differentiation in thymus; ISS:UniProtKB.
GO; GO:0043029; P:T cell homeostasis; ISS:UniProtKB.
GO; GO:0048538; P:thymus development; ISS:UniProtKB.
GO; GO:0036462; P:TRAIL-activated apoptotic signaling pathway; IDA:ParkinsonsUK-UCL.
GO; GO:0035666; P:TRIF-dependent toll-like receptor signaling pathway; TAS:Reactome.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
InterPro; IPR011029; DEATH-like_dom.
InterPro; IPR000488; Death_domain.
InterPro; IPR001875; DED_dom.
InterPro; IPR016729; FADD.
Pfam; PF00531; Death; 1.
Pfam; PF01335; DED; 1.
PIRSF; PIRSF018586; FADD; 1.
SMART; SM00005; DEATH; 1.
SMART; SM00031; DED; 1.
SUPFAM; SSF47986; SSF47986; 1.
PROSITE; PS50017; DEATH_DOMAIN; 1.
PROSITE; PS50168; DED; 1.
1: Evidence at protein level;
3D-structure; Apoptosis; Complete proteome; Disease mutation;
Host-virus interaction; Immunity; Innate immunity; Phosphoprotein;
Reference proteome.
CHAIN 1 208 FAS-associated death domain protein.
/FTId=PRO_0000191279.
DOMAIN 3 81 DED. {ECO:0000255|PROSITE-
ProRule:PRU00065}.
DOMAIN 97 181 Death. {ECO:0000255|PROSITE-
ProRule:PRU00064}.
MOD_RES 194 194 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:11034606}.
VARIANT 105 105 C -> W (in IEHDCM; reduced folding
stability as measured by differential
scanning calorimetry of the mutant
protein; impairs interaction with FAS;
dbSNP:rs387906839).
{ECO:0000269|PubMed:21109225}.
/FTId=VAR_065124.
MUTAGEN 12 12 S->R: Loss of interaction with CASP8.
{ECO:0000269|PubMed:16762833}.
MUTAGEN 25 25 F->R: Loss of interaction with FAS. Loss
of self-association. Abolishes induction
of apoptosis.
{ECO:0000269|PubMed:16762833}.
MUTAGEN 33 33 K->E: Loss of self-association.
{ECO:0000269|PubMed:16762833}.
MUTAGEN 38 38 R->A: Loss of interaction with CASP8.
{ECO:0000269|PubMed:16762833}.
MUTAGEN 44 44 D->R: Loss of interaction with CASP8.
Abolishes induction of apoptosis.
Decreased interaction with FAS.
{ECO:0000269|PubMed:16762833}.
MUTAGEN 51 51 E->R: Loss of interaction with CASP8.
{ECO:0000269|PubMed:16762833}.
MUTAGEN 117 117 R->E: Loss of interaction with FAS.
{ECO:0000269|PubMed:20935634}.
MUTAGEN 121 121 V->N: Loss of interaction with FAS.
{ECO:0000269|PubMed:7538907}.
MUTAGEN 123 123 D->R: Strongly decreased interaction with
FAS. {ECO:0000269|PubMed:20935634}.
MUTAGEN 135 135 R->E: Strongly decreased interaction with
FAS. {ECO:0000269|PubMed:20935634}.
MUTAGEN 142 142 R->E: Decreased interaction with FAS.
{ECO:0000269|PubMed:20935634}.
MUTAGEN 172 172 L->A,E: Loss of interaction with FAS.
{ECO:0000269|PubMed:19118384,
ECO:0000269|PubMed:20935634}.
MUTAGEN 172 172 L->K: Strongly decreased interaction with
FAS. {ECO:0000269|PubMed:19118384,
ECO:0000269|PubMed:20935634}.
MUTAGEN 175 175 D->K: Strongly decreased interaction with
FAS. {ECO:0000269|PubMed:20935634}.
MUTAGEN 176 176 L->E: Decreased interaction with FAS.
{ECO:0000269|PubMed:19118384}.
CONFLICT 32 32 G -> V (in Ref. 2; CAA59197).
{ECO:0000305}.
HELIX 3 13 {ECO:0000244|PDB:1A1W}.
HELIX 16 30 {ECO:0000244|PDB:1A1W}.
HELIX 34 38 {ECO:0000244|PDB:1A1W}.
STRAND 40 42 {ECO:0000244|PDB:1A1W}.
HELIX 43 51 {ECO:0000244|PDB:1A1W}.
HELIX 61 70 {ECO:0000244|PDB:1A1W}.
HELIX 74 82 {ECO:0000244|PDB:1A1W}.
STRAND 88 91 {ECO:0000244|PDB:2GF5}.
HELIX 94 105 {ECO:0000244|PDB:3EZQ}.
STRAND 109 111 {ECO:0000244|PDB:1E41}.
HELIX 112 118 {ECO:0000244|PDB:3EZQ}.
HELIX 123 132 {ECO:0000244|PDB:3EZQ}.
STRAND 133 135 {ECO:0000244|PDB:2GF5}.
HELIX 137 151 {ECO:0000244|PDB:3EZQ}.
TURN 153 155 {ECO:0000244|PDB:3EZQ}.
HELIX 158 167 {ECO:0000244|PDB:3EZQ}.
HELIX 171 190 {ECO:0000244|PDB:3EZQ}.
SEQUENCE 208 AA; 23279 MW; 0E65E2F852E83507 CRC64;
MDPFLVLLHS VSSSLSSSEL TELKFLCLGR VGKRKLERVQ SGLDLFSMLL EQNDLEPGHT
ELLRELLASL RRHDLLRRVD DFEAGAAAGA APGEEDLCAA FNVICDNVGK DWRRLARQLK
VSDTKIDSIE DRYPRNLTER VRESLRIWKN TEKENATVAH LVGALRSCQM NLVADLVQEV
QQARDLQNRS GAMSPMSWNS DASTSEAS


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