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Protein

FAS-associated death domain protein

Gene

Fadd

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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 - Molecular functioni

GO - Biological processi

  • activation of cysteine-type endopeptidase activity Source: MGI
  • apoptotic process Source: UniProtKB
  • apoptotic signaling pathway Source: MGI
  • cardiac muscle tissue development Source: UniProtKB
  • cellular response to mechanical stimulus Source: Ensembl
  • defense response to virus Source: MGI
  • extrinsic apoptotic signaling pathway Source: MGI
  • extrinsic apoptotic signaling pathway in absence of ligand Source: MGI
  • innate immune response Source: UniProtKB
  • lymph node development Source: UniProtKB
  • motor neuron apoptotic process Source: MGI
  • necroptotic signaling pathway Source: MGI
  • negative regulation of activation-induced cell death of T cells Source: UniProtKB
  • negative regulation of necroptotic process Source: MGI
  • positive regulation of activated T cell proliferation Source: UniProtKB
  • positive regulation of adaptive immune response Source: UniProtKB
  • positive regulation of apoptotic process Source: MGI
  • positive regulation of CD8-positive, alpha-beta cytotoxic T cell extravasation Source: UniProtKB
  • positive regulation of extrinsic apoptotic signaling pathway Source: MGI
  • positive regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: MGI
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: Ensembl
  • positive regulation of interferon-gamma production Source: UniProtKB
  • positive regulation of interleukin-8 production Source: MGI
  • positive regulation of macrophage differentiation Source: MGI
  • positive regulation of proteolysis Source: MGI
  • positive regulation of T cell mediated cytotoxicity Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: MGI
  • positive regulation of tumor necrosis factor production Source: MGI
  • positive regulation of type I interferon-mediated signaling pathway Source: MGI
  • protein heterooligomerization Source: Ensembl
  • spleen development Source: UniProtKB
  • T cell differentiation Source: UniProtKB
  • T cell differentiation in thymus Source: UniProtKB
  • T cell homeostasis Source: UniProtKB
  • thymus development Source: UniProtKB
  • TRAIL-activated apoptotic signaling pathway Source: MGI
Complete GO annotation...

Keywords - Biological processi

Apoptosis, Immunity, Innate immunity

Enzyme and pathway databases

ReactomeiREACT_284272. TRIF-mediated programmed cell death.
REACT_284952. FasL/ CD95L signaling.
REACT_291404. TRAIL signaling.
REACT_301406. Dimerization of procaspase-8.
REACT_310781. Regulation by c-FLIP.
REACT_332213. NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10.
REACT_354529. Ligand-dependent caspase activation.
REACT_357294. TNFR1-mediated proapoptotic signaling.
REACT_362347. CASP8 activity is inhibited.
REACT_362359. RIPK1-mediated regulated necrosis.

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 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:109324. Fadd.

Subcellular locationi

GO - Cellular componenti

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.
GenevisibleiQ61160. MM.

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). Interacts directly (via DED domain) with NOL3 (via CARD domain); inhibits death-inducing signaling complex (DISC) assembly by inhibiting the increase in FAS-FADD binding induced by FAS activation.By similarity1 Publication

Binary interactionsi

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

Protein-protein interaction databases

BioGridi199586. 11 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 – 11825Combined sources
Helixi123 – 13210Combined sources
Helixi137 – 15216Combined sources
Helixi153 – 1564Combined sources
Helixi158 – 16811Combined sources
Helixi171 – 18111Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi199586. 11 interactions.
DIPiDIP-34771N.
IntActiQ61160. 12 interactions.
MINTiMINT-1514991.
STRINGi10090.ENSMUSP00000033394.

PTM databases

PhosphoSiteiQ61160.

Proteomic databases

MaxQBiQ61160.
PaxDbiQ61160.
PRIDEiQ61160.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi8772.
MGIiMGI:109324. Fadd.

Phylogenomic databases

eggNOGiNOG43830.
GeneTreeiENSGT00390000002105.
HOGENOMiHOG000112490.
HOVERGENiHBG000853.
InParanoidiQ61160.
KOiK02373.
OMAiCQMNLVA.
OrthoDBiEOG76X61Z.
PhylomeDBiQ61160.
TreeFamiTF102046.

Enzyme and pathway databases

ReactomeiREACT_284272. TRIF-mediated programmed cell death.
REACT_284952. FasL/ CD95L signaling.
REACT_291404. TRAIL signaling.
REACT_301406. Dimerization of procaspase-8.
REACT_310781. Regulation by c-FLIP.
REACT_332213. NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10.
REACT_354529. Ligand-dependent caspase activation.
REACT_357294. TNFR1-mediated proapoptotic signaling.
REACT_362347. CASP8 activity is inhibited.
REACT_362359. RIPK1-mediated regulated necrosis.

Miscellaneous databases

EvolutionaryTraceiQ61160.
NextBioi285096.
PROiQ61160.
SOURCEiSearch...

Gene expression databases

BgeeiQ61160.
CleanExiMM_FADD.
GenevisibleiQ61160. MM.

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]
ProtoNetiSearch...

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. "Inhibition of both the extrinsic and intrinsic death pathways through nonhomotypic death-fold interactions."
    Nam Y.J., Mani K., Ashton A.W., Peng C.F., Krishnamurthy B., Hayakawa Y., Lee P., Korsmeyer S.J., Kitsis R.N.
    Mol. Cell 15:901-912(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NOL3.
  6. "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: June 24, 2015
This is version 135 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.