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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.
26-FEB-2020, entry version 205.
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 MOLLUSCUM CONTAGIOSUM VIRUS PROTEIN MC159L AND MC160L
(MICROBIAL INFECTION).
PubMed=11259186; DOI=10.1006/viro.2001.0834;
Shisler J.L., Moss B.;
"Molluscum contagiosum virus inhibitors of apoptosis: The MC159 v-FLIP
protein blocks Fas-induced activation of procaspases and degradation of the
related MC160 protein.";
Virology 282:14-25(2001).
[14]
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).
[15]
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).
[16]
INTERACTION WITH TNFRSF10B.
PubMed=18846110; DOI=10.1038/cdd.2008.124;
Sun M., Song L., Li Y., Zhou T., Jope R.S.;
"Identification of an antiapoptotic protein complex at death receptors.";
Cell Death Differ. 15:1887-1900(2008).
[17]
INTERACTION WITH HUMAN PAPILLOMAVIRUS 16/HPV16 PROTEIN E6 (MICROBIAL
INFECTION).
PubMed=18632871; DOI=10.1128/jvi.00538-08;
Tungteakkhun S.S., Filippova M., Neidigh J.W., Fodor N.,
Duerksen-Hughes P.J.;
"The interaction between human papillomavirus type 16 and FADD is mediated
by a novel E6 binding domain.";
J. Virol. 82:9600-9614(2008).
[18]
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).
[19]
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).
[20]
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).
[21]
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).
[22]
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).
[23]
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).
[24]
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).
[25]
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).
[26]
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).
[27]
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).
[28]
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).
[29]
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). Interacts with RIPK1, TRADD and CASP8 (By similarity).
Interacts with stimulated TNFRSF10B (PubMed:18846110).
{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:18846110,
ECO:0000269|PubMed:19118384, ECO:0000269|PubMed:20935634,
ECO:0000269|PubMed:21109225}.
-!- SUBUNIT: (Microbial infection) Interacts with human papillomavirus
16/HPV16 protein E6. {ECO:0000269|PubMed:18632871}.
-!- SUBUNIT: (Microbial infection) Interacts with molluscum contagiosum
virus proteins MC159L/v-CFLAR and MC160L.
{ECO:0000269|PubMed:11259186}.
-!- INTERACTION:
Self; NbExp=7; IntAct=EBI-494804, EBI-494804;
Q14790:CASP8; NbExp=44; 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.
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.
PDB; 6ACI; X-ray; 1.87 A; H=93-184.
PDBsum; 1A1W; -.
PDBsum; 1A1Z; -.
PDBsum; 1E3Y; -.
PDBsum; 1E41; -.
PDBsum; 2GF5; -.
PDBsum; 3EZQ; -.
PDBsum; 3OQ9; -.
PDBsum; 6ACI; -.
SMR; Q13158; -.
BioGrid; 114302; 95.
ComplexPortal; CPX-1907; Ripoptosome.
CORUM; Q13158; -.
DIP; DIP-286N; -.
IntAct; Q13158; 75.
MINT; Q13158; -.
STRING; 9606.ENSP00000301838; -.
iPTMnet; Q13158; -.
PhosphoSitePlus; Q13158; -.
BioMuta; FADD; -.
DMDM; 2498355; -.
EPD; Q13158; -.
jPOST; Q13158; -.
MassIVE; Q13158; -.
MaxQB; Q13158; -.
PaxDb; Q13158; -.
PeptideAtlas; Q13158; -.
PRIDE; Q13158; -.
ProteomicsDB; 59197; -.
DNASU; 8772; -.
Ensembl; ENST00000301838; ENSP00000301838; ENSG00000168040.
GeneID; 8772; -.
KEGG; hsa:8772; -.
UCSC; uc001opm.3; human.
CTD; 8772; -.
DisGeNET; 8772; -.
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; CLU_087961_0_0_1; -.
InParanoid; Q13158; -.
KO; K02373; -.
OMA; ELKFLCR; -.
OrthoDB; 1619689at2759; -.
PhylomeDB; Q13158; -.
TreeFam; TF102046; -.
Reactome; R-HSA-140534; Caspase activation via Death Receptors in the presence of ligand.
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-9013957; TLR3-mediated TICAM1-dependent programmed cell death.
Reactome; R-HSA-933543; NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10.
SignaLink; Q13158; -.
SIGNOR; Q13158; -.
ChiTaRS; FADD; human.
EvolutionaryTrace; Q13158; -.
GeneWiki; FADD; -.
GenomeRNAi; 8772; -.
Pharos; Q13158; Tbio.
PRO; PR:Q13158; -.
Proteomes; UP000005640; Chromosome 11.
RNAct; Q13158; protein.
Bgee; ENSG00000168040; Expressed in blood and 210 other tissues.
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; IBA:GO_Central.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0002020; F:protease binding; IPI:UniProtKB.
GO; GO:0044877; F:protein-containing 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: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:0001822; P:kidney development; IEA:Ensembl.
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: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 by RNA polymerase II; 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:0034138; P:toll-like receptor 3 signaling pathway; TAS:Reactome.
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_sf.
InterPro; IPR000488; Death_domain.
InterPro; IPR001875; DED_dom.
InterPro; IPR016729; FADD.
PANTHER; PTHR15077; PTHR15077; 1.
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; Disease mutation; Host-virus interaction;
Immunity; Innate immunity; Phosphoprotein; Reference proteome.
CHAIN 1..208
/note="FAS-associated death domain protein"
/id="PRO_0000191279"
DOMAIN 3..81
/note="DED"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00065"
DOMAIN 97..181
/note="Death"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00064"
MOD_RES 194
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692, ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:11034606"
VARIANT 105
/note="C -> W (in IEHDCM; reduced folding stability as
measured by differential scanning calorimetry of the mutant
protein; impairs interaction with FAS; dbSNP:rs387906839)"
/evidence="ECO:0000269|PubMed:21109225"
/id="VAR_065124"
MUTAGEN 12
/note="S->R: Loss of interaction with CASP8."
/evidence="ECO:0000269|PubMed:16762833"
MUTAGEN 25
/note="F->R: Loss of interaction with FAS. Loss of self-
association. Abolishes induction of apoptosis."
/evidence="ECO:0000269|PubMed:16762833"
MUTAGEN 33
/note="K->E: Loss of self-association."
/evidence="ECO:0000269|PubMed:16762833"
MUTAGEN 38
/note="R->A: Loss of interaction with CASP8."
/evidence="ECO:0000269|PubMed:16762833"
MUTAGEN 44
/note="D->R: Loss of interaction with CASP8. Abolishes
induction of apoptosis. Decreased interaction with FAS."
/evidence="ECO:0000269|PubMed:16762833"
MUTAGEN 51
/note="E->R: Loss of interaction with CASP8."
/evidence="ECO:0000269|PubMed:16762833"
MUTAGEN 117
/note="R->E: Loss of interaction with FAS."
/evidence="ECO:0000269|PubMed:20935634"
MUTAGEN 121
/note="V->N: Loss of interaction with FAS."
/evidence="ECO:0000269|PubMed:7538907"
MUTAGEN 123
/note="D->R: Strongly decreased interaction with FAS."
/evidence="ECO:0000269|PubMed:20935634"
MUTAGEN 135
/note="R->E: Strongly decreased interaction with FAS."
/evidence="ECO:0000269|PubMed:20935634"
MUTAGEN 142
/note="R->E: Decreased interaction with FAS."
/evidence="ECO:0000269|PubMed:20935634"
MUTAGEN 172
/note="L->A,E: Loss of interaction with FAS."
/evidence="ECO:0000269|PubMed:19118384,
ECO:0000269|PubMed:20935634"
MUTAGEN 172
/note="L->K: Strongly decreased interaction with FAS."
/evidence="ECO:0000269|PubMed:19118384,
ECO:0000269|PubMed:20935634"
MUTAGEN 175
/note="D->K: Strongly decreased interaction with FAS."
/evidence="ECO:0000269|PubMed:20935634"
MUTAGEN 176
/note="L->E: Decreased interaction with FAS."
/evidence="ECO:0000269|PubMed:19118384"
CONFLICT 32
/note="G -> V (in Ref. 2; CAA59197)"
/evidence="ECO:0000305"
HELIX 3..13
/evidence="ECO:0000244|PDB:1A1W"
HELIX 16..30
/evidence="ECO:0000244|PDB:1A1W"
HELIX 34..38
/evidence="ECO:0000244|PDB:1A1W"
STRAND 40..42
/evidence="ECO:0000244|PDB:1A1W"
HELIX 43..51
/evidence="ECO:0000244|PDB:1A1W"
HELIX 61..70
/evidence="ECO:0000244|PDB:1A1W"
HELIX 74..82
/evidence="ECO:0000244|PDB:1A1W"
STRAND 91..93
/evidence="ECO:0000244|PDB:1E3Y"
HELIX 97..107
/evidence="ECO:0000244|PDB:6ACI"
STRAND 109..111
/evidence="ECO:0000244|PDB:1E41"
HELIX 112..118
/evidence="ECO:0000244|PDB:6ACI"
HELIX 123..132
/evidence="ECO:0000244|PDB:6ACI"
STRAND 133..135
/evidence="ECO:0000244|PDB:2GF5"
HELIX 137..152
/evidence="ECO:0000244|PDB:6ACI"
HELIX 153..155
/evidence="ECO:0000244|PDB:6ACI"
HELIX 158..167
/evidence="ECO:0000244|PDB:6ACI"
HELIX 171..181
/evidence="ECO:0000244|PDB:6ACI"
TURN 186..189
/evidence="ECO:0000244|PDB:1E41"
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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Pathways :
WP1689: Porphyrin and chlorophyll metabolism
WP2292: Chemokine signaling pathway
WP2272: Pathogenic Escherichia coli infection
WP211: BMP signaling pathway
WP1625: Base excision repair
WP1892: Protein folding
WP1693: Purine metabolism
WP1654: gamma-Hexachlorocyclohexane degradation
WP35: G Protein Signaling Pathways
WP1939: Unfolded Protein Response
WP1713: Two-component system
WP2203: TSLP Signaling Pathway
WP525: Mitochondrial Unfolded-Protein Response
WP1502: Mitochondrial biogenesis
WP1665: Limonene and pinene degradation
WP1675: Nitrogen metabolism
WP1566: Citrate cycle (TCA cycle)
WP1624: Bacterial secretion system
WP1888: Post-translational protein modification
WP1685: Peptidoglycan biosynthesis
WP210: Cytoplasmic Ribosomal Proteins
WP1692: Protein export
WP731: Sterol regulatory element binding protein related
WP1650: Fluorobenzoate degradation
WP931: G Protein Signaling Pathways

Related Genes :
[FADD MORT1 GIG3] FAS-associated death domain protein (FAS-associating death domain-containing protein) (Growth-inhibiting gene 3 protein) (Mediator of receptor induced toxicity) (Protein FADD)
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[Fadd fadd rCG_48606] FAS-associated death domain protein (FAS-associating death domain-containing protein) (Protein FADD)
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[FADD] FAS-associated death domain protein (FAS-associating death domain-containing protein) (Protein FADD)
[FADD] FAS-associated death domain protein (FAS-associating death domain-containing protein) (Protein FADD)
[FADD] FAS-associated death domain protein (FAS-associating death domain-containing protein) (Protein FADD)
[FADD] FAS-associated death domain protein (FAS-associating death domain-containing protein) (Protein FADD)
[FADD] FAS-associated death domain protein (FAS-associating death domain-containing protein) (Protein FADD)
[FADD] FAS-associated death domain protein (FAS-associating death domain-containing protein) (Protein FADD)
[FADD] FAS-associated death domain protein (FAS-associating death domain-containing protein) (Protein FADD)
[FADD] FAS-associated death domain protein (FAS-associating death domain-containing protein) (Protein FADD)
[FADD] FAS-associated death domain protein (FAS-associating death domain-containing protein) (Protein FADD)
[FADD] FAS-associated death domain protein (FAS-associating death domain-containing protein) (Protein FADD)
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Bibliography :