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Q61160

- FADD_MOUSE

UniProt

Q61160 - FADD_MOUSE

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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

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 - 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. necroptotic signaling pathway 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
Complete GO annotation...

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
Complete GO annotation...

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

        10         20         30         40         50
MDPFLVLLHS LSGSLSGNDL MELKFLCRER VSKRKLERVQ SGLDLFTVLL
60 70 80 90 100
EQNDLERGHT GLLRELLASL RRHDLLQRLD DFEAGTATAA PPGEADLQVA
110 120 130 140 150
FDIVCDNVGR DWKRLARELK VSEAKMDGIE EKYPRSLSER VRESLKVWKN
160 170 180 190 200
AEKKNASVAG LVKALRTCRL NLVADLVEEA QESVSKSENM SPVLRDSTVS

SSETP
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

« Hide 'large scale' publications
  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 29, 2014
This is version 128 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