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Q13158

- FADD_HUMAN

UniProt

Q13158 - FADD_HUMAN

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Protein
FAS-associated death domain protein
Gene
FADD, MORT1, GIG3
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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

GO - Molecular functioni

  1. death effector domain binding Source: UniProtKB
  2. death receptor binding Source: ProtInc
  3. identical protein binding Source: IntAct
  4. protease binding Source: UniProtKB
  5. protein binding Source: UniProtKB
  6. receptor binding Source: UniProtKB
  7. tumor necrosis factor receptor superfamily binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. MyD88-independent toll-like receptor signaling pathway Source: Reactome
  2. T cell differentiation in thymus Source: UniProtKB
  3. T cell homeostasis Source: UniProtKB
  4. TRIF-dependent toll-like receptor signaling pathway Source: Reactome
  5. activation of cysteine-type endopeptidase activity Source: BHF-UCL
  6. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: Reactome
  7. apoptotic process Source: UniProtKB
  8. apoptotic signaling pathway Source: BHF-UCL
  9. cellular response to mechanical stimulus Source: UniProtKB
  10. defense response to virus Source: UniProtKB
  11. extrinsic apoptotic signaling pathway Source: UniProtKB
  12. extrinsic apoptotic signaling pathway in absence of ligand Source: Ensembl
  13. extrinsic apoptotic signaling pathway via death domain receptors Source: ProtInc
  14. innate immune response Source: Reactome
  15. lymph node development Source: UniProtKB
  16. motor neuron apoptotic process Source: Ensembl
  17. necroptotic signaling pathway Source: BHF-UCL
  18. negative regulation of activation-induced cell death of T cells Source: UniProtKB
  19. positive regulation of CD8-positive, alpha-beta cytotoxic T cell extravasation Source: UniProtKB
  20. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  21. positive regulation of T cell mediated cytotoxicity Source: UniProtKB
  22. positive regulation of activated T cell proliferation Source: UniProtKB
  23. positive regulation of adaptive immune response Source: UniProtKB
  24. positive regulation of apoptotic process Source: UniProtKB
  25. positive regulation of extrinsic apoptotic signaling pathway Source: UniProtKB
  26. positive regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: Ensembl
  27. positive regulation of interferon-gamma production Source: UniProtKB
  28. positive regulation of interleukin-8 production Source: BHF-UCL
  29. positive regulation of macrophage differentiation Source: UniProtKB
  30. positive regulation of proteolysis Source: BHF-UCL
  31. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  32. positive regulation of tumor necrosis factor production Source: BHF-UCL
  33. positive regulation of type I interferon-mediated signaling pathway Source: UniProtKB
  34. protein heterooligomerization Source: Ensembl
  35. regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: Reactome
  36. spleen development Source: UniProtKB
  37. thymus development Source: UniProtKB
  38. toll-like receptor 3 signaling pathway Source: Reactome
  39. toll-like receptor 4 signaling pathway Source: Reactome
  40. toll-like receptor signaling pathway Source: Reactome
  41. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Apoptosis, Host-virus interaction, Immunity, Innate immunity

Enzyme and pathway databases

ReactomeiREACT_1432. TNF signaling.
REACT_1503. Caspase-8 activation.
REACT_150361. TRIF-mediated programmed cell death.
REACT_164011. Regulation by c-FLIP.
REACT_25039. NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10.
REACT_402. TRAIL signaling.
REACT_832. Dimerization of procaspase-8.
REACT_900. FasL/ CD95L signaling.
SignaLinkiQ13158.

Names & Taxonomyi

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
Gene namesi
Name:FADD
Synonyms:MORT1
ORF Names:GIG3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:3573. FADD.

Subcellular locationi

GO - Cellular componenti

  1. CD95 death-inducing signaling complex Source: UniProtKB
  2. cell body Source: Ensembl
  3. cytosol Source: ParkinsonsUK-UCL
  4. death-inducing signaling complex Source: UniProtKB
  5. membrane raft Source: Ensembl
  6. neuron projection Source: Ensembl
  7. ripoptosome Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

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.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti105 – 1051C → W in IEHDCM; reduced folding stability as measured by differential scanning calorimetry of the mutant protein; impairs interaction with FAS. 1 Publication
VAR_065124

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi12 – 121S → R: Loss of interaction with CASP8. 1 Publication
Mutagenesisi25 – 251F → R: Loss of interaction with FAS. Loss of self-association. Abolishes induction of apoptosis. 1 Publication
Mutagenesisi33 – 331K → E: Loss of self-association. 1 Publication
Mutagenesisi38 – 381R → A: Loss of interaction with CASP8. 1 Publication
Mutagenesisi44 – 441D → R: Loss of interaction with CASP8. Abolishes induction of apoptosis. Decreased interaction with FAS. 1 Publication
Mutagenesisi51 – 511E → R: Loss of interaction with CASP8. 1 Publication
Mutagenesisi117 – 1171R → E: Loss of interaction with FAS. 1 Publication
Mutagenesisi121 – 1211V → N: Loss of interaction with FAS.
Mutagenesisi123 – 1231D → R: Strongly decreased interaction with FAS. 1 Publication
Mutagenesisi135 – 1351R → E: Strongly decreased interaction with FAS. 1 Publication
Mutagenesisi142 – 1421R → E: Decreased interaction with FAS. 1 Publication
Mutagenesisi172 – 1721L → A or E: Loss of interaction with FAS. 2 Publications
Mutagenesisi172 – 1721L → K: Strongly decreased interaction with FAS. 2 Publications
Mutagenesisi175 – 1751D → K: Strongly decreased interaction with FAS. 1 Publication
Mutagenesisi176 – 1761L → E: Decreased interaction with FAS. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi613759. phenotype.
Orphaneti306550. FADD-related immunodeficiency.
99806. Oculootodental syndrome.
PharmGKBiPA27972.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 208208FAS-associated death domain protein
PRO_0000191279Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei194 – 1941Phosphoserine3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ13158.
PaxDbiQ13158.
PeptideAtlasiQ13158.
PRIDEiQ13158.

PTM databases

PhosphoSiteiQ13158.

Expressioni

Tissue specificityi

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

Gene expression databases

ArrayExpressiQ13158.
BgeeiQ13158.
CleanExiHS_FADD.
GenevestigatoriQ13158.

Organism-specific databases

HPAiCAB010209.
HPA001464.

Interactioni

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 CASP8.9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-494804,EBI-494804
CASP8Q1479032EBI-494804,EBI-78060
CASP8Q14790-15EBI-494804,EBI-288309
CASP8Q14790-54EBI-494804,EBI-288326
FASP2544532EBI-494804,EBI-494743
FasP254465EBI-494804,EBI-296206From a different organism.
FASLGP480232EBI-494804,EBI-495538
LRRK2Q5S0074EBI-494804,EBI-5323863
MBD4O952436EBI-494804,EBI-348011
MYD88Q998363EBI-494804,EBI-447677
PARK7Q994979EBI-494804,EBI-1164361
PLK1P533509EBI-494804,EBI-476768
RIPK1Q135465EBI-494804,EBI-358507

Protein-protein interaction databases

BioGridi114302. 56 interactions.
DIPiDIP-286N.
IntActiQ13158. 27 interactions.
MINTiMINT-91814.
STRINGi9606.ENSP00000301838.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1311
Helixi16 – 3015
Helixi34 – 385
Beta strandi40 – 423
Helixi43 – 519
Helixi61 – 7010
Helixi74 – 829
Beta strandi88 – 914
Helixi94 – 10512
Beta strandi109 – 1113
Helixi112 – 1187
Helixi123 – 13210
Beta strandi133 – 1353
Helixi137 – 15115
Turni153 – 1553
Helixi158 – 16710
Helixi171 – 19020

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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. Positions 2-191.

Miscellaneous databases

EvolutionaryTraceiQ13158.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 8179DED
Add
BLAST
Domaini97 – 18185Death
Add
BLAST

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

Sequence similaritiesi

Contains 1 death domain.

Phylogenomic databases

eggNOGiNOG43830.
HOGENOMiHOG000112490.
HOVERGENiHBG000853.
InParanoidiQ13158.
KOiK02373.
OMAiCQMNLVA.
OrthoDBiEOG76X61Z.
PhylomeDBiQ13158.
TreeFamiTF102046.

Family and domain databases

Gene3Di1.10.533.10. 2 hits.
InterProiIPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR001875. DED.
IPR016729. FADD.
[Graphical view]
PfamiPF00531. Death. 1 hit.
PF01335. DED. 1 hit.
[Graphical view]
PIRSFiPIRSF018586. FADD. 1 hit.
SMARTiSM00005. DEATH. 1 hit.
SM00031. DED. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
PROSITEiPS50017. DEATH_DOMAIN. 1 hit.
PS50168. DED. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q13158-1 [UniParc]FASTAAdd to Basket

« Hide

MDPFLVLLHS VSSSLSSSEL TELKFLCLGR VGKRKLERVQ SGLDLFSMLL    50
EQNDLEPGHT ELLRELLASL RRHDLLRRVD DFEAGAAAGA APGEEDLCAA 100
FNVICDNVGK DWRRLARQLK VSDTKIDSIE DRYPRNLTER VRESLRIWKN 150
TEKENATVAH LVGALRSCQM NLVADLVQEV QQARDLQNRS GAMSPMSWNS 200
DASTSEAS 208
Length:208
Mass (Da):23,279
Last modified:November 1, 1997 - v1
Checksum:i0E65E2F852E83507
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti105 – 1051C → W in IEHDCM; reduced folding stability as measured by differential scanning calorimetry of the mutant protein; impairs interaction with FAS. 1 Publication
VAR_065124

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti32 – 321G → V in CAA59197. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.

Genome annotation databases

EnsembliENST00000301838; ENSP00000301838; ENSG00000168040.
GeneIDi8772.
KEGGihsa:8772.
UCSCiuc001opm.2. human.

Polymorphism databases

DMDMi2498355.

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS8196.1.
PIRi A56912.
RefSeqi NP_003815.1. NM_003824.3.
UniGenei Hs.86131.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1A1W NMR - A 1-83 [» ]
1A1Z NMR - A 1-83 [» ]
1E3Y NMR - A 93-192 [» ]
1E41 NMR - A 93-192 [» ]
2GF5 NMR - A 2-191 [» ]
3EZQ X-ray 2.73 B/D/F/H/J/L/N/P 93-208 [» ]
3OQ9 X-ray 6.80 H/I/J/K/L 93-184 [» ]
ProteinModelPortali Q13158.
SMRi Q13158. Positions 2-191.
ModBasei Search...

Protein-protein interaction databases

BioGridi 114302. 56 interactions.
DIPi DIP-286N.
IntActi Q13158. 27 interactions.
MINTi MINT-91814.
STRINGi 9606.ENSP00000301838.

PTM databases

PhosphoSitei Q13158.

Polymorphism databases

DMDMi 2498355.

Proteomic databases

MaxQBi Q13158.
PaxDbi Q13158.
PeptideAtlasi Q13158.
PRIDEi Q13158.

Protocols and materials databases

DNASUi 8772.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000301838 ; ENSP00000301838 ; ENSG00000168040 .
GeneIDi 8772.
KEGGi hsa:8772.
UCSCi uc001opm.2. human.

Organism-specific databases

CTDi 8772.
GeneCardsi GC11P070049.
HGNCi HGNC:3573. FADD.
HPAi CAB010209.
HPA001464.
MIMi 602457. gene.
613759. phenotype.
neXtProti NX_Q13158.
Orphaneti 306550. FADD-related immunodeficiency.
99806. Oculootodental syndrome.
PharmGKBi PA27972.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG43830.
HOGENOMi HOG000112490.
HOVERGENi HBG000853.
InParanoidi Q13158.
KOi K02373.
OMAi CQMNLVA.
OrthoDBi EOG76X61Z.
PhylomeDBi Q13158.
TreeFami TF102046.

Enzyme and pathway databases

Reactomei REACT_1432. TNF signaling.
REACT_1503. Caspase-8 activation.
REACT_150361. TRIF-mediated programmed cell death.
REACT_164011. Regulation by c-FLIP.
REACT_25039. NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10.
REACT_402. TRAIL signaling.
REACT_832. Dimerization of procaspase-8.
REACT_900. FasL/ CD95L signaling.
SignaLinki Q13158.

Miscellaneous databases

EvolutionaryTracei Q13158.
GeneWikii FADD.
GenomeRNAii 8772.
NextBioi 32890.
PROi Q13158.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q13158.
Bgeei Q13158.
CleanExi HS_FADD.
Genevestigatori Q13158.

Family and domain databases

Gene3Di 1.10.533.10. 2 hits.
InterProi IPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR001875. DED.
IPR016729. FADD.
[Graphical view ]
Pfami PF00531. Death. 1 hit.
PF01335. DED. 1 hit.
[Graphical view ]
PIRSFi PIRSF018586. FADD. 1 hit.
SMARTi SM00005. DEATH. 1 hit.
SM00031. DED. 1 hit.
[Graphical view ]
SUPFAMi SSF47986. SSF47986. 1 hit.
PROSITEi PS50017. DEATH_DOMAIN. 1 hit.
PS50168. DED. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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 PIDD1.
  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. 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. 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, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, MUTAGENESIS OF ARG-117; ASP-123; ARG-135; ARG-142; LEU-172 AND ASP-175.

Entry informationi

Entry nameiFADD_HUMAN
AccessioniPrimary (citable) accession number: Q13158
Secondary accession number(s): Q14866, Q6IBR4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: September 3, 2014
This is version 152 of the entry and version 1 of the sequence. [Complete history]
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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

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