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UniProtKB/Swiss-Prot entry Q61160


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name FADD_MOUSE
Primary accession number Q61160
Secondary accession numbers Q3TC37 Q61082
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on November 1, 1997 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 82)
Name and origin of the protein
Protein name Protein FADD
Synonyms FAS-associated death domain protein
FAS-associating death domain-containing protein
Mediator of receptor induced toxicity
Gene name
Name: Fadd
Synonyms: Mort1
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8649383 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang J., Winoto A.;
"A mouse Fas-associated protein with homology to the human Mort1/FADD protein is essential for Fas-induced apoptosis.";
Mol. Cell. Biol. 16:2756-2763(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1016/S0092-8674(00)80984-8; PubMed=8565075 [NCBI, ExPASy, EBI, Israel, Japan]
Hsu H., Shu H.-B., Pan M.G., Goeddel D.V.;
"TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways.";
Cell 84:299-308(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD;
TISSUE=Heart, and Thymus;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Czech II;
TISSUE=Mammary gland, and Salivary gland;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
STRUCTURE BY NMR OF 89-183.
DOI=10.1074/jbc.274.23.16337; PubMed=10347191 [NCBI, ExPASy, EBI, Israel, Japan]
Jeong E.-J., Bang S., Lee T.H., Park Y.-I., Sim W.-S., Kim K.-S.;
"The solution structure of FADD death domain. Structural basis of death domain interactions of Fas and FADD.";
J. Biol. Chem. 274:16337-16342(1999).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U50406; AAB07789.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U43184; AAA97876.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK084808; BAC39283.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK169798; BAE41374.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK170927; BAE42120.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC004584; AAH04584.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC021400; AAH21400.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00117888; -.
RefSeq NP_034305.1; -.
UniGene Mm.5126
3D structure databases
PDB
1FAD; NMR; -; A=89-183.[ExPASy / RCSB / EBI]
PDBsum 1FAD; -.
SMR Q61160; 2-183.
ModBase Q61160.
Protein-protein interaction databases
IntAct Q61160; 5.
PTM databases
PhosphoSite Q61160; -.
Organism-specific databases
MGI MGI:109324; Fadd.
Gene expression databases
ArrayExpress Q61160; -.
Bgee Q61160; -.
CleanEx MM_FADD; -.
GermOnline ENSMUSG00000031077; Mus musculus.
Ontologies
GO
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006915; Biological process: apoptosis (inferred from direct assay from MGI).
GO:0042981; Biological process: regulation of apoptosis (inferred from mutant phenotype from MGI).
GO:0007165; Biological process: signal transduction (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR000488; Death.
IPR011029; DEATH-like.
IPR001875; DED.
IPR016729; FADD.
Graphical view of domain structure.
Gene3D G3DSA:1.10.533.10; DEATH_like; 1.
Pfam PF00531; Death; 1.
PF01335; DED; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF018586; FADD; 1.
SMART SM00005; DEATH; 1.
SM00031; DED; 1.
SMART graphical view of domain structure.
PROSITE PS50017; DEATH_DOMAIN; 1.
PS50168; DED; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE Q61160; -.
Genome annotation databases
Ensembl ENSMUSG00000031077; Mus musculus. [Contig view]
GeneID 14082; -.
KEGG mmu:14082; -.
Phylogenomic databases
HOGENOM Q61160; -.
HOVERGEN Q61160; -.
OMA Q61160; LEQNDLE.
Other
NextBio 285096; -.
SOURCE Fadd; Mus musculus.
ProtoNet Q61160.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Apoptosis; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   205  205     Protein FADD. PRO_0000191280
DOMAIN   3    81  79     DED. 
DOMAIN   97   181  85     Death. 
MOD_RES   191   191        Phosphoserine (By similarity). 
CONFLICT   168   168        C -> F (in Ref. 2; AAA97876). 
HELIX   94   118  25      
HELIX   123   132  10      
HELIX   137   152  16      
HELIX   153   156  4      
HELIX   158   168  11      
HELIX   171   181  11      
Sequence information
Length: 205 AA [This is the length of the unprocessed precursor] Molecular weight: 22960 Da [This is the MW of the unprocessed precursor] CRC64: 4BC8D86B33A58783 [This is a checksum on the sequence]
        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 

Q61160 in FASTA format

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