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Q61160 (FADD_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
FAS-associated death domain protein
Alternative name(s):
FAS-associating death domain-containing protein
Mediator of receptor induced toxicity
Protein FADD
Gene names
Name:Fadd
Synonyms:Mort1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length205 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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

Domain

Contains a death domain involved in the binding of the corresponding domain within Fas receptor.

Post-translational modification

Phosphorylated.

Sequence similarities

Contains 1 death domain.

Contains 1 DED (death effector) domain.

Ontologies

Keywords
   Biological processApoptosis
Immunity
Innate immunity
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processT cell differentiation

Traceable author statement PubMed 18309324. Source: UniProtKB

T cell differentiation in thymus

Inferred from mutant phenotype PubMed 21876153. Source: UniProtKB

T cell homeostasis

Inferred from mutant phenotype PubMed 21876153. Source: UniProtKB

activation of cysteine-type endopeptidase activity

Inferred from electronic annotation. Source: Ensembl

apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

cardiac muscle tissue development

Traceable author statement PubMed 18309324. Source: UniProtKB

cellular response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

defense response to virus

Inferred from electronic annotation. Source: Ensembl

extrinsic apoptotic signaling pathway

Inferred from direct assay PubMed 10588860. Source: MGI

extrinsic apoptotic signaling pathway in absence of ligand

Inferred from mutant phenotype PubMed 13679421. Source: MGI

innate immune response

Traceable author statement PubMed 18309324. Source: UniProtKB

lymph node development

Inferred from genetic interaction PubMed 21876153. Source: UniProtKB

motor neuron apoptotic process

Inferred from mutant phenotype PubMed 13679421. Source: MGI

necrotic cell death

Inferred from electronic annotation. Source: Ensembl

negative regulation of activation-induced cell death of T cells

Inferred from mutant phenotype PubMed 21876153. Source: UniProtKB

negative regulation of necroptotic process

Inferred from genetic interaction PubMed 22089168PubMed 22675671. Source: MGI

positive regulation of CD8-positive, alpha-beta cytotoxic T cell extravasation

Inferred from mutant phenotype PubMed 21876153. Source: UniProtKB

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from electronic annotation. Source: Ensembl

positive regulation of T cell mediated cytotoxicity

Inferred from mutant phenotype PubMed 21876153. Source: UniProtKB

positive regulation of activated T cell proliferation

Inferred from mutant phenotype PubMed 21876153. Source: UniProtKB

positive regulation of adaptive immune response

Inferred from mutant phenotype PubMed 21876153. Source: UniProtKB

positive regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of extrinsic apoptotic signaling pathway

Inferred from genetic interaction PubMed 22675671. Source: MGI

positive regulation of extrinsic apoptotic signaling pathway via death domain receptors

Inferred from genetic interaction PubMed 16183742. Source: MGI

positive regulation of interferon-gamma production

Inferred from mutant phenotype PubMed 21876153. Source: UniProtKB

positive regulation of interleukin-8 production

Inferred from electronic annotation. Source: Ensembl

positive regulation of proteolysis

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

positive regulation of tumor necrosis factor production

Inferred from electronic annotation. Source: Ensembl

positive regulation of type I interferon-mediated signaling pathway

Inferred from electronic annotation. Source: Ensembl

protein heterooligomerization

Inferred from electronic annotation. Source: Ensembl

spleen development

Inferred from genetic interaction PubMed 21876153. Source: UniProtKB

thymus development

Inferred from genetic interaction PubMed 21876153. Source: UniProtKB

   Cellular_componentCD95 death-inducing signaling complex

Inferred from electronic annotation. Source: Ensembl

cell body

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from electronic annotation. Source: Ensembl

membrane raft

Inferred from electronic annotation. Source: Ensembl

neuron projection

Inferred from electronic annotation. Source: Ensembl

ripoptosome

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

FasP254463EBI-524415,EBI-296206

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 205205FAS-associated death domain protein
PRO_0000191280

Regions

Domain3 – 8179DED
Domain97 – 18185Death

Amino acid modifications

Modified residue1911Phosphoserine By similarity

Experimental info

Sequence conflict1681C → F in AAA97876. Ref.2

Secondary structure

............ 205
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q61160 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 4BC8D86B33A58783

FASTA20522,960
        10         20         30         40         50         60 
MDPFLVLLHS LSGSLSGNDL MELKFLCRER VSKRKLERVQ SGLDLFTVLL EQNDLERGHT 

        70         80         90        100        110        120 
GLLRELLASL RRHDLLQRLD DFEAGTATAA PPGEADLQVA FDIVCDNVGR DWKRLARELK 

       130        140        150        160        170        180 
VSEAKMDGIE EKYPRSLSER VRESLKVWKN AEKKNASVAG LVKALRTCRL NLVADLVEEA 

       190        200 
QESVSKSENM SPVLRDSTVS SSETP 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_034305.1. NM_010175.5.
UniGeneMm.5126.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FADNMR-A89-183[»]
ProteinModelPortalQ61160.
SMRQ61160. Positions 1-183.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199586. 7 interactions.
DIPDIP-34771N.
IntActQ61160. 12 interactions.
MINTMINT-1514991.
STRING10090.ENSMUSP00000033394.

PTM databases

PhosphoSiteQ61160.

Proteomic databases

PaxDbQ61160.
PRIDEQ61160.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000033394; ENSMUSP00000033394; ENSMUSG00000031077.
GeneID14082.
KEGGmmu:14082.
UCSCuc009kql.1. mouse.

Organism-specific databases

CTD8772.
MGIMGI:109324. Fadd.

Phylogenomic databases

eggNOGNOG43830.
GeneTreeENSGT00390000002105.
HOGENOMHOG000112490.
HOVERGENHBG000853.
InParanoidQ61160.
KOK02373.
OMACQMNLVA.
OrthoDBEOG76X61Z.
PhylomeDBQ61160.
TreeFamTF102046.

Gene expression databases

BgeeQ61160.
CleanExMM_FADD.
GenevestigatorQ61160.

Family and domain databases

Gene3D1.10.533.10. 2 hits.
InterProIPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR001875. DED.
IPR016729. FADD.
[Graphical view]
PfamPF00531. Death. 1 hit.
PF01335. DED. 1 hit.
[Graphical view]
PIRSFPIRSF018586. FADD. 1 hit.
SMARTSM00005. DEATH. 1 hit.
SM00031. DED. 1 hit.
[Graphical view]
SUPFAMSSF47986. SSF47986. 1 hit.
PROSITEPS50017. DEATH_DOMAIN. 1 hit.
PS50168. DED. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ61160.
NextBio285096.
PROQ61160.
SOURCESearch...

Entry information

Entry nameFADD_MOUSE
AccessionPrimary (citable) accession number: Q61160
Secondary accession number(s): Q3TC37, Q61082
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: April 16, 2014
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot