Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q13158

- FADD_HUMAN

UniProt

Q13158 - FADD_HUMAN

Protein

FAS-associated death domain protein

Gene

FADD

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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. tumor necrosis factor receptor superfamily binding Source: UniProtKB

    GO - Biological processi

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

    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

    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).1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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. 2 Publications
    Mutagenesisi25 – 251F → R: Loss of interaction with FAS. Loss of self-association. Abolishes induction of apoptosis. 2 Publications
    Mutagenesisi33 – 331K → E: Loss of self-association. 2 Publications
    Mutagenesisi38 – 381R → A: Loss of interaction with CASP8. 2 Publications
    Mutagenesisi44 – 441D → R: Loss of interaction with CASP8. Abolishes induction of apoptosis. Decreased interaction with FAS. 2 Publications
    Mutagenesisi51 – 511E → R: Loss of interaction with CASP8. 2 Publications
    Mutagenesisi117 – 1171R → E: Loss of interaction with FAS. 2 Publications
    Mutagenesisi121 – 1211V → N: Loss of interaction with FAS. 1 Publication
    Mutagenesisi123 – 1231D → R: Strongly decreased interaction with FAS. 2 Publications
    Mutagenesisi135 – 1351R → E: Strongly decreased interaction with FAS. 2 Publications
    Mutagenesisi142 – 1421R → E: Decreased interaction with FAS. 2 Publications
    Mutagenesisi172 – 1721L → A or E: Loss of interaction with FAS. 3 Publications
    Mutagenesisi172 – 1721L → K: Strongly decreased interaction with FAS. 3 Publications
    Mutagenesisi175 – 1751D → K: Strongly decreased interaction with FAS. 2 Publications
    Mutagenesisi176 – 1761L → E: Decreased interaction with FAS. 2 Publications

    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 proteinPRO_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
    FASP2544533EBI-494804,EBI-494743
    FasP254465EBI-494804,EBI-296206From a different organism.
    FASLGP480233EBI-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. 31 interactions.
    MINTiMINT-91814.
    STRINGi9606.ENSP00000301838.

    Structurei

    Secondary structure

    1
    208
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13158.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini3 – 8179DEDPROSITE-ProRule annotationAdd
    BLAST
    Domaini97 – 18185DeathPROSITE-ProRule annotationAdd
    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.PROSITE-ProRule annotation
    Contains 1 DED (death effector) domain.PROSITE-ProRule annotation

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti32 – 321G → V in CAA59197. (PubMed:7536190)Curated

    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 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...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114302. 56 interactions.
    DIPi DIP-286N.
    IntActi Q13158. 31 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

    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: October 1, 2014
    This is version 153 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