Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q13158 (FADD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
Gene names
Name:FADD
Synonyms:MORT1
ORF Names:GIG3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length208 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.17 Ref.23 Ref.24 Ref.25

Subunit structure

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 LRDD. Interacts (via death domain) with FAS (via death domain). Interacts with CASP8. Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.17 Ref.23 Ref.24 Ref.25

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. Ref.24

The interaction between the FAS and FADD death domains is crucial for the formation of the death-inducing signaling complex (DISC). Ref.24

Involvement in 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).
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.17

Sequence similarities

Contains 1 death domain.

Contains 1 DED (death effector) domain.

Ontologies

Keywords
   Biological processApoptosis
Host-virus interaction
Immunity
Innate immunity
   DiseaseDisease mutation
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processT cell differentiation in thymus

Inferred from sequence or structural similarity. Source: UniProtKB

T cell homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

TRIF-dependent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

activation of cysteine-type endopeptidase activity involved in apoptotic process

Traceable author statement. Source: Reactome

cellular response to mechanical stimulus

Inferred from expression pattern PubMed 19593445. Source: UniProtKB

defense response to virus

Inferred from mutant phenotype Ref.17. Source: UniProtKB

extrinsic apoptotic signaling pathway in absence of ligand

Inferred from electronic annotation. Source: Ensembl

extrinsic apoptotic signaling pathway via death domain receptors

Traceable author statement Ref.1. Source: ProtInc

innate immune response

Traceable author statement. Source: Reactome

lymph node development

Inferred from sequence or structural similarity. Source: UniProtKB

motor neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

necrotic cell death

Inferred from mutant phenotype. Source: BHF-UCL

negative regulation of activation-induced cell death of T cells

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of CD8-positive, alpha-beta cytotoxic T cell extravasation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from expression pattern PubMed 12761501. Source: UniProtKB

positive regulation of T cell mediated cytotoxicity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of activated T cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of apoptotic process

Inferred from mutant phenotype Ref.25. Source: UniProtKB

positive regulation of extrinsic apoptotic signaling pathway

Inferred from mutant phenotype PubMed 21525013. Source: UniProtKB

positive regulation of extrinsic apoptotic signaling pathway via death domain receptors

Inferred from electronic annotation. Source: Ensembl

positive regulation of interferon-gamma production

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of interleukin-8 production

Inferred from direct assay Ref.14. Source: BHF-UCL

positive regulation of macrophage differentiation

Inferred from mutant phenotype PubMed 17047155. Source: UniProtKB

positive regulation of proteolysis

Inferred from direct assay PubMed 18387192. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.14. Source: BHF-UCL

positive regulation of tumor necrosis factor production

Inferred from direct assay Ref.14. Source: BHF-UCL

positive regulation of type I interferon-mediated signaling pathway

Inferred from mutant phenotype Ref.17. Source: UniProtKB

protein heterooligomerization

Inferred from electronic annotation. Source: Ensembl

regulation of extrinsic apoptotic signaling pathway in absence of ligand

Traceable author statement. Source: Reactome

spleen development

Inferred from sequence or structural similarity. Source: UniProtKB

thymus development

Inferred from sequence or structural similarity. Source: UniProtKB

toll-like receptor 3 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 4 signaling pathway

Traceable author statement. Source: Reactome

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentCD95 death-inducing signaling complex

Inferred from direct assay Ref.25. Source: UniProtKB

cell body

Inferred from electronic annotation. Source: Ensembl

cytosol

Traceable author statement. Source: Reactome

membrane raft

Inferred from electronic annotation. Source: Ensembl

neuron projection

Inferred from electronic annotation. Source: Ensembl

ripoptosome

Inferred from direct assay PubMed 21737330. Source: UniProtKB

   Molecular_functiondeath receptor binding

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 208208FAS-associated death domain protein
PRO_0000191279

Regions

Domain3 – 8179DED
Domain97 – 18185Death

Amino acid modifications

Modified residue1941Phosphoserine Ref.12 Ref.16 Ref.20

Natural variations

Natural variant1051C → W in IEHDCM; reduced folding stability as measured by differential scanning calorimetry of the mutant protein; impairs interaction with FAS. Ref.17
VAR_065124

Experimental info

Mutagenesis121S → R: Loss of interaction with CASP8. Ref.23
Mutagenesis251F → R: Loss of interaction with FAS. Loss of self-association. Abolishes induction of apoptosis. Ref.23
Mutagenesis331K → E: Loss of self-association. Ref.23
Mutagenesis381R → A: Loss of interaction with CASP8. Ref.23
Mutagenesis441D → R: Loss of interaction with CASP8. Abolishes induction of apoptosis. Decreased interaction with FAS. Ref.23
Mutagenesis511E → R: Loss of interaction with CASP8. Ref.23
Mutagenesis1171R → E: Loss of interaction with FAS. Ref.25
Mutagenesis1211V → N: Loss of interaction with FAS.
Mutagenesis1231D → R: Strongly decreased interaction with FAS. Ref.25
Mutagenesis1351R → E: Strongly decreased interaction with FAS. Ref.25
Mutagenesis1421R → E: Decreased interaction with FAS. Ref.25
Mutagenesis1721L → A or E: Loss of interaction with FAS. Ref.24 Ref.25
Mutagenesis1721L → K: Strongly decreased interaction with FAS. Ref.24 Ref.25
Mutagenesis1751D → K: Strongly decreased interaction with FAS. Ref.25
Mutagenesis1761L → E: Decreased interaction with FAS. Ref.24
Sequence conflict321G → V in CAA59197. Ref.2

Secondary structure

................................ 208
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q13158 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 0E65E2F852E83507

FASTA20823,279
        10         20         30         40         50         60 
MDPFLVLLHS VSSSLSSSEL TELKFLCLGR VGKRKLERVQ SGLDLFSMLL EQNDLEPGHT 

        70         80         90        100        110        120 
ELLRELLASL RRHDLLRRVD DFEAGAAAGA APGEEDLCAA FNVICDNVGK DWRRLARQLK 

       130        140        150        160        170        180 
VSDTKIDSIE DRYPRNLTER VRESLRIWKN TEKENATVAH LVGALRSCQM NLVADLVQEV 

       190        200 
QQARDLQNRS GAMSPMSWNS DASTSEAS 

« Hide

References

« Hide 'large scale' references
[1]"FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis."
Chinnaiyan A.M., O'Rourke K., Tewari M., Dixit V.M.
Cell 81:505-512(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS.
Tissue: Umbilical vein endothelial cell.
[2]"A novel protein that interacts with the death domain of Fas/APO1 contains a sequence motif related to the death domain."
Boldin M.P., Varfolomeev E.E., Pancer Z., Mett I.L., Camonis J.H., Wallach D.
J. Biol. Chem. 270:7795-7798(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Identification of a human growth inhibition gene 3 (GIG3)."
Kim J.W.
Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
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.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]NIEHS SNPs program
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[8]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung.
[10]"PED/PEA-15: an anti-apoptotic molecule that regulates FAS/TNFR1-induced apoptosis."
Condorelli G., Vigliotta G., Cafieri A., Trencia A., Andalo P., Oriente F., Miele C., Caruso M., Formisano P., Beguinot F.
Oncogene 18:4409-4415(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PEA15.
[11]"LRDD, a novel leucine rich repeat and death domain containing protein."
Telliez J.-B., Bean K.M., Lin L.-L.
Biochim. Biophys. Acta 1478:280-288(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LRDD.
[12]"FIST/HIPK3: a Fas/FADD-interacting serine/threonine kinase that induces FADD phosphorylation and inhibits Fas-mediated Jun NH2-terminal kinase activation."
Rochat-Steiner V., Becker K., Micheau O., Schneider P., Burns K., Tschopp J.
J. Exp. Med. 192:1165-1174(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH HIPK3 AND FAS, PHOSPHORYLATION AT SER-194.
[13]"Fas-associated death domain protein interacts with methyl-CpG binding domain protein 4: a potential link between genome surveillance and apoptosis."
Screaton R.A., Kiessling S., Sansom O.J., Millar C.B., Maddison K., Bird A., Clarke A.R., Frisch S.M.
Proc. Natl. Acad. Sci. U.S.A. 100:5211-5216(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MBD4.
[14]"IPS-1, an adaptor triggering RIG-I- and Mda5-mediated type I interferon induction."
Kawai T., Takahashi K., Sato S., Coban C., Kumar H., Kato H., Ishii K.J., Takeuchi O., Akira S.
Nat. Immunol. 6:981-988(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MAVS.
[15]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[17]"Whole-exome-sequencing-based discovery of human FADD deficiency."
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.
Am. J. Hum. Genet. 87:873-881(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN INTERFERON-MEDIATED IMMUNITY, INTERACTION WITH FAS, VARIANT IEHDCM TRP-105, CHARACTERIZATION OF VARIANT IEHDCM TRP-105.
[18]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
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.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"NMR structure and mutagenesis of the FADD (Mort1) death-effector domain."
Eberstadt M., Huang B., Chen Z., Meadows R.P., Ng S.C., Zheng L., Lenardo M.J., Fesik S.W.
Nature 392:941-945(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-83.
[22]"The three-dimensional solution structure and dynamic properties of the human FADD death domain."
Berglund H., Olerenshaw D., Sankar A., Federwisch M., McDonald N.Q., Driscoll P.C.
J. Mol. Biol. 302:171-188(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 93-192.
[23]"The structure of FADD and its mode of interaction with procaspase-8."
Carrington P.E., Sandu C., Wei Y., Hill J.M., Morisawa G., Huang T., Gavathiotis E., Wei Y., Werner M.H.
Mol. Cell 22:599-610(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 2-191, FUNCTION, INTERACTION WITH FAS AND CASP8, MUTAGENESIS OF SER-12; PHE-25; LYS-33; ARG-38; ASP-44 AND GLU-51.
[24]"The Fas-FADD death domain complex structure unravels signalling by receptor clustering."
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.
Nature 457:1019-1022(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.73 ANGSTROMS) OF 93-208 IN COMPLEX WITH FAS, FUNCTION, SUBUNIT, ELECTRON MICROSCOPY, DOMAIN, MUTAGENESIS OF LEU-172 AND LEU-176.
[25]"The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations."
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.
Nat. Struct. Mol. Biol. 17:1324-1329(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (6.80 ANGSTROMS) OF 93-184 IN COMPLEX WITH FAS, ELECTRON MICROSCOPY, FUNCTION, MASS SPECTROMETRY, SUBUNIT, MUTAGENESIS OF ARG-117; ASP-123; ARG-135; ARG-142; LEU-172 AND ASP-175.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA56912.
RefSeqNP_003815.1. NM_003824.3.
UniGeneHs.86131.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalQ13158.
SMRQ13158. Positions 2-191.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114302. 56 interactions.
DIPDIP-286N.
IntActQ13158. 27 interactions.
MINTMINT-91814.
STRING9606.ENSP00000301838.

PTM databases

PhosphoSiteQ13158.

Polymorphism databases

DMDM2498355.

Proteomic databases

PaxDbQ13158.
PeptideAtlasQ13158.
PRIDEQ13158.

Protocols and materials databases

DNASU8772.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000301838; ENSP00000301838; ENSG00000168040.
GeneID8772.
KEGGhsa:8772.
UCSCuc001opm.2. human.

Organism-specific databases

CTD8772.
GeneCardsGC11P070049.
HGNCHGNC:3573. FADD.
HPACAB010209.
HPA001464.
MIM602457. gene.
613759. phenotype.
neXtProtNX_Q13158.
Orphanet306550. FADD-related immunodeficiency.
99806. Oculootodental syndrome.
PharmGKBPA27972.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG43830.
HOGENOMHOG000112490.
HOVERGENHBG000853.
InParanoidQ13158.
KOK02373.
OMACQMNLVA.
OrthoDBEOG76X61Z.
PhylomeDBQ13158.
TreeFamTF102046.

Enzyme and pathway databases

ReactomeREACT_578. Apoptosis.
REACT_6900. Immune System.
SignaLinkQ13158.

Gene expression databases

ArrayExpressQ13158.
BgeeQ13158.
CleanExHS_FADD.
GenevestigatorQ13158.

Family and domain databases

Gene3D1.10.533.10. 2 hits.
InterProIPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR001875. DED.
IPR016729. FADD.
[Graphical view]
PfamPF00531. Death. 1 hit.
PF01335. DED. 1 hit.
[Graphical view]
PIRSFPIRSF018586. FADD. 1 hit.
SMARTSM00005. DEATH. 1 hit.
SM00031. DED. 1 hit.
[Graphical view]
SUPFAMSSF47986. SSF47986. 1 hit.
PROSITEPS50017. DEATH_DOMAIN. 1 hit.
PS50168. DED. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ13158.
GeneWikiFADD.
GenomeRNAi8772.
NextBio32890.
PROQ13158.
SOURCESearch...

Entry information

Entry nameFADD_HUMAN
AccessionPrimary (citable) accession number: Q13158
Secondary accession number(s): Q14866, Q6IBR4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: March 19, 2014
This is version 147 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM