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UniProtKB/Swiss-Prot entry Q13158


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name FADD_HUMAN
Primary accession number Q13158
Secondary accession number Q14866
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on November 1, 1997 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 87)
Name and origin of the protein
Protein name Protein FADD
Synonyms FAS-associated death domain protein
FAS-associating death domain-containing protein
Mediator of receptor induced toxicity
Gene name
Name: FADD
Synonyms: MORT1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND MUTAGENESIS.
TISSUE=Umbilical vein endothelial cell;
DOI=10.1016/0092-8674(95)90071-3; PubMed=7538907 [NCBI, ExPASy, EBI, Israel, Japan]
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].
DOI=10.1074/jbc.270.14.7795; PubMed=7536190 [NCBI, ExPASy, EBI, Israel, Japan]
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].
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.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[5]
INTERACTION WITH PEA15.
DOI=10.1038/sj.onc.1202831; PubMed=10442631 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[6]
INTERACTION WITH LRDD.
DOI=10.1016/S0167-4838(00)00029-7; PubMed=10825539 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[7]
IDENTIFICATION IN A COMPLEX WITH HIPK3 AND FAS, AND PHOSPHORYLATION AT SER-194.
DOI=10.1084/jem.192.8.1165; PubMed=11034606 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[8]
INTERACTION WITH MBD4.
DOI=10.1073/pnas.0431215100; PubMed=12702765 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[9]
INTERACTION WITH MAVS.
DOI=10.1038/ni1243; PubMed=16127453 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[10]
STRUCTURE BY NMR OF 1-83.
DOI=10.1038/31972; PubMed=9582077 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U24231; AAA86517.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X84709; CAA59197.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT006927; AAP35573.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC000334; AAH00334.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A56912; A56912.
RefSeq NP_003815.1; -.
UniGene Hs.86131
3D structure databases
PDB
1A1W; NMR; -; A=1-83.[ExPASy / RCSB / EBI]
1A1Z; NMR; -; A=1-83.[ExPASy / RCSB / EBI]
1E3Y; NMR; -; A=93-192.[ExPASy / RCSB / EBI]
1E41; NMR; -; A=93-192.[ExPASy / RCSB / EBI]
2GF5; NMR; -; A=2-191.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1A1W; -.
1A1Z; -.
1E3Y; -.
1E41; -.
2GF5; -.
ModBase Q13158.
Protein-protein interaction databases
DIP DIP:286N; -.
IntAct Q13158; -.
PTM databases
PhosphoSite Q13158; -.
Enzyme and pathway databases
Reactome REACT_578; Apoptosis.
Organism-specific databases
H-InvDB HIX0009893; -.
HGNC HGNC:3573; FADD.
GenAtlas FADD.
HPA CAB010209; -.
HPA001464; -.
MIM 602457; gene. [NCBI / EBI]
PharmGKB PA27972; -.
GeneCards Q13158.
Gene expression databases
ArrayExpress Q13158; -.
CleanEx HS_FADD; -.
GermOnline ENSG00000168040; Homo sapiens.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from experiment from Reactome).
GO:0005794; Cellular component: Golgi apparatus (inferred from direct assay from HPA).
GO:0005634; Cellular component: nucleus (inferred from direct assay from HPA).
GO:0005123; Molecular function: death receptor binding (traceable author statement from ProtInc).
GO:0042802; Molecular function: identical protein binding (inferred from physical interaction from IntAct).
GO:0008633; Biological process: activation of pro-apoptotic gene products (inferred from experiment from Reactome).
GO:0008625; Biological process: induction of apoptosis via death domain receptors (traceable author statement from ProtInc).
GO:0044419; Biological process: interspecies interaction between organisms (inferred from electronic annotation from UniProtKB-KW).
GO:0043123; Biological process: positive regulation of I-kappaB kinase/NF-kappaB cascade (inferred from expression pattern from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR000488; Death.
IPR011029; DEATH_like.
IPR001875; DED.
IPR016729; FADD.
Graphical view of domain structure.
Gene3D G3DSA:1.10.533.10; DEATH_like; 1.
Pfam PF00531; Death; 1.
PF01335; DED; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF018586; FADD; 1.
SMART SM00005; DEATH; 1.
SM00031; DED; 1.
SMART graphical view of domain structure.
PROSITE PS50017; DEATH_DOMAIN; 1.
PS50168; DED; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet Q13158.
Proteomic databases
PeptideAtlas Q13158; -.
Genome annotation databases
Ensembl ENSG00000168040; Homo sapiens. [Contig view]
GeneID 8772; -.
KEGG hsa:8772; -.
Phylogenomic databases
HOGENOM Q13158; -.
HOVERGEN Q13158; -.
Other
LinkHub Q13158; -.
NextBio 32890; -.
SOURCE FADD; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Apoptosis; Host-virus interaction; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   208  208     Protein FADD. PRO_0000191279
DOMAIN   3    81  79     DED. 
DOMAIN   97   181  85     Death. 
MOD_RES   194   194        Phosphoserine (Probable). 
MUTAGEN   121   121        V->N: No interaction with Fas receptor. 
CONFLICT   32    32        G -> V (in Ref. 2; CAA59197). 
HELIX   3    13  11      
HELIX   16    30  15      
HELIX   34    38  5      
STRAND   40    42  3      
HELIX   43    51  9      
HELIX   61    70  10      
HELIX   74    82  9      
STRAND   88    91  4      
HELIX   97   106  10      
HELIX   112   120  9      
HELIX   123   132  10      
HELIX   137   152  16      
TURN   153   155  3      
HELIX   158   167  10      
HELIX   171   187  17      
Sequence information
Length: 208 AA [This is the length of the unprocessed precursor] Molecular weight: 23279 Da [This is the MW of the unprocessed precursor] CRC64: 0E65E2F852E83507 [This is a checksum on the sequence]
        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 

Q13158 in FASTA format

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