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)

Q61160

- FADD_MOUSE

UniProt

Q61160 - FADD_MOUSE

Protein

FAS-associated death domain protein

Gene

Fadd

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 127 (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 By similarity. Involved in interferon-mediated antiviral immune response, playing a role in the positive regulation of interferon signaling By similarity.By similarity

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

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

    Keywords - Biological processi

    Apoptosis, Immunity, Innate immunity

    Enzyme and pathway databases

    ReactomeiREACT_196636. TRIF-mediated programmed cell death.
    REACT_205717. NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10.
    REACT_215122. Regulation by c-FLIP.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    FAS-associated death domain protein
    Alternative name(s):
    FAS-associating death domain-containing protein
    Mediator of receptor induced toxicity
    Protein FADD
    Gene namesi
    Name:Fadd
    Synonyms:Mort1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:109324. Fadd.

    Subcellular locationi

    GO - Cellular componenti

    1. CD95 death-inducing signaling complex Source: Ensembl
    2. cell body Source: Ensembl
    3. membrane raft Source: Ensembl
    4. neuron projection Source: Ensembl
    5. ripoptosome Source: UniProtKB

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 205205FAS-associated death domain proteinPRO_0000191280Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei191 – 1911PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated.

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ61160.
    PaxDbiQ61160.
    PRIDEiQ61160.

    PTM databases

    PhosphoSiteiQ61160.

    Expressioni

    Gene expression databases

    BgeeiQ61160.
    CleanExiMM_FADD.
    GenevestigatoriQ61160.

    Interactioni

    Subunit structurei

    Interacts with CFLAR, PEA15 and MBD4. When phosphorylated, part of a complex containing HIPK3 and FAS. May interact with MAVS/IPS1. Interacts with PIDD1 By similarity. Interacts with FAS By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FasP254463EBI-524415,EBI-296206

    Protein-protein interaction databases

    BioGridi199586. 7 interactions.
    DIPiDIP-34771N.
    IntActiQ61160. 12 interactions.
    MINTiMINT-1514991.
    STRINGi10090.ENSMUSP00000033394.

    Structurei

    Secondary structure

    1
    205
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi94 – 11825
    Helixi123 – 13210
    Helixi137 – 15216
    Helixi153 – 1564
    Helixi158 – 16811
    Helixi171 – 18111

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FADNMR-A89-183[»]
    ProteinModelPortaliQ61160.
    SMRiQ61160. Positions 1-183.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ61160.

    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.

    Sequence similaritiesi

    Contains 1 death domain.PROSITE-ProRule annotation
    Contains 1 DED (death effector) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG43830.
    GeneTreeiENSGT00390000002105.
    HOGENOMiHOG000112490.
    HOVERGENiHBG000853.
    InParanoidiQ61160.
    KOiK02373.
    OMAiCQMNLVA.
    OrthoDBiEOG76X61Z.
    PhylomeDBiQ61160.
    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.

    Q61160-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDPFLVLLHS LSGSLSGNDL MELKFLCRER VSKRKLERVQ SGLDLFTVLL    50
    EQNDLERGHT GLLRELLASL RRHDLLQRLD DFEAGTATAA PPGEADLQVA 100
    FDIVCDNVGR DWKRLARELK VSEAKMDGIE EKYPRSLSER VRESLKVWKN 150
    AEKKNASVAG LVKALRTCRL NLVADLVEEA QESVSKSENM SPVLRDSTVS 200
    SSETP 205
    Length:205
    Mass (Da):22,960
    Last modified:November 1, 1997 - v1
    Checksum:i4BC8D86B33A58783
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti168 – 1681C → F in AAA97876. (PubMed:8565075)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U50406 mRNA. Translation: AAB07789.1.
    U43184 mRNA. Translation: AAA97876.1.
    AK084808 mRNA. Translation: BAC39283.1.
    AK169798 mRNA. Translation: BAE41374.1.
    AK170927 mRNA. Translation: BAE42120.1.
    BC004584 mRNA. Translation: AAH04584.1.
    BC021400 mRNA. Translation: AAH21400.1.
    CCDSiCCDS22050.1.
    RefSeqiNP_034305.1. NM_010175.5.
    UniGeneiMm.5126.

    Genome annotation databases

    EnsembliENSMUST00000033394; ENSMUSP00000033394; ENSMUSG00000031077.
    GeneIDi14082.
    KEGGimmu:14082.
    UCSCiuc009kql.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U50406 mRNA. Translation: AAB07789.1 .
    U43184 mRNA. Translation: AAA97876.1 .
    AK084808 mRNA. Translation: BAC39283.1 .
    AK169798 mRNA. Translation: BAE41374.1 .
    AK170927 mRNA. Translation: BAE42120.1 .
    BC004584 mRNA. Translation: AAH04584.1 .
    BC021400 mRNA. Translation: AAH21400.1 .
    CCDSi CCDS22050.1.
    RefSeqi NP_034305.1. NM_010175.5.
    UniGenei Mm.5126.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FAD NMR - A 89-183 [» ]
    ProteinModelPortali Q61160.
    SMRi Q61160. Positions 1-183.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199586. 7 interactions.
    DIPi DIP-34771N.
    IntActi Q61160. 12 interactions.
    MINTi MINT-1514991.
    STRINGi 10090.ENSMUSP00000033394.

    PTM databases

    PhosphoSitei Q61160.

    Proteomic databases

    MaxQBi Q61160.
    PaxDbi Q61160.
    PRIDEi Q61160.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000033394 ; ENSMUSP00000033394 ; ENSMUSG00000031077 .
    GeneIDi 14082.
    KEGGi mmu:14082.
    UCSCi uc009kql.1. mouse.

    Organism-specific databases

    CTDi 8772.
    MGIi MGI:109324. Fadd.

    Phylogenomic databases

    eggNOGi NOG43830.
    GeneTreei ENSGT00390000002105.
    HOGENOMi HOG000112490.
    HOVERGENi HBG000853.
    InParanoidi Q61160.
    KOi K02373.
    OMAi CQMNLVA.
    OrthoDBi EOG76X61Z.
    PhylomeDBi Q61160.
    TreeFami TF102046.

    Enzyme and pathway databases

    Reactomei REACT_196636. TRIF-mediated programmed cell death.
    REACT_205717. NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10.
    REACT_215122. Regulation by c-FLIP.

    Miscellaneous databases

    EvolutionaryTracei Q61160.
    NextBioi 285096.
    PROi Q61160.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q61160.
    CleanExi MM_FADD.
    Genevestigatori Q61160.

    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. "A mouse Fas-associated protein with homology to the human Mort1/FADD protein is essential for Fas-induced apoptosis."
      Zhang J., Winoto A.
      Mol. Cell. Biol. 16:2756-2763(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways."
      Hsu H., Shu H.-B., Pan M.G., Goeddel D.V.
      Cell 84:299-308(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J and NOD.
      Tissue: Heart and Thymus.
    4. "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].
      Strain: Czech II.
      Tissue: Mammary gland and Salivary gland.
    5. "The solution structure of FADD death domain. Structural basis of death domain interactions of Fas and FADD."
      Jeong E.-J., Bang S., Lee T.H., Park Y.-I., Sim W.-S., Kim K.-S.
      J. Biol. Chem. 274:16337-16342(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 89-183.

    Entry informationi

    Entry nameiFADD_MOUSE
    AccessioniPrimary (citable) accession number: Q61160
    Secondary accession number(s): Q3TC37, Q61082
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 127 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3