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Protein
Submitted name:

FADD/MORT1 protein with death effector domain

Gene

Fadd

Organism
Rattus norvegicus (Rat)
Status
Unreviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  • death receptor binding Source: RGD
  • protease binding Source: RGD
  • protein complex binding Source: RGD
  • tumor necrosis factor receptor binding Source: RGD

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-RNO-3371378. Regulation by c-FLIP.
R-RNO-5213460. RIPK1-mediated regulated necrosis.
R-RNO-5218900. CASP8 activity is inhibited.
R-RNO-5357786. TNFR1-induced proapoptotic signaling.
R-RNO-69416. Dimerization of procaspase-8.
R-RNO-75157. FasL/ CD95L signaling.
R-RNO-75158. TRAIL signaling.

Names & Taxonomyi

Protein namesi
Submitted name:
FADD/MORT1 protein with death effector domainImported
Submitted name:
Fas (TNFRSF6)-associated via death domainImported
Submitted name:
Fas death domain associated proteinImported
Submitted name:
Protein FaddImported
Gene namesi
Name:FaddImported
Synonyms:faddImported
ORF Names:rCG_48606Imported
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi628700. Fadd.

Subcellular locationi

GO - Cellular componenti

  • CD95 death-inducing signaling complex Source: RGD
  • cell body Source: RGD
  • cytoplasm Source: RGD
  • death-inducing signaling complex Source: RGD
  • membrane raft Source: RGD
  • neuron projection Source: RGD
  • protein complex Source: RGD
  • ripoptosome Source: UniProtKB
Complete GO annotation...

PTM / Processingi

PTM databases

iPTMnetiQ8R2E7.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
Casp8Q9JHX42EBI-4326723,EBI-4326675

GO - Molecular functioni

  • death receptor binding Source: RGD
  • protease binding Source: RGD
  • protein complex binding Source: RGD
  • tumor necrosis factor receptor binding Source: RGD

Protein-protein interaction databases

IntActiQ8R2E7. 2 interactions.
STRINGi10116.ENSRNOP00000066289.

Structurei

3D structure databases

SMRiQ8R2E7. Positions 2-190.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 8179DED (death effector)InterPro annotationAdd
BLAST
Domaini97 – 18185DeathInterPro annotationAdd
BLAST

Phylogenomic databases

eggNOGiENOG410J0KM. Eukaryota.
ENOG41122TX. LUCA.
GeneTreeiENSGT00390000002105.
HOGENOMiHOG000112490.
HOVERGENiHBG000853.
KOiK02373.
OMAiCQMNLVA.
OrthoDBiEOG76X61Z.
PhylomeDBiQ8R2E7.
TreeFamiTF102046.

Family and domain databases

Gene3Di1.10.533.10. 2 hits.
InterProiIPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR001875. DED_dom.
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.

Q8R2E7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDPFLVLLHS LSSSLSGNDL TDLKFLCRER VSKRKLERVQ SGLDLFSVLL
60 70 80 90 100
EQNDLERGHT GLLRELLASL GRHDLLQRLD DFEAGATTAA TPGEADLRVA
110 120 130 140 150
FDIVCDNVGR DWKRLARELK VSEAKIDGIE ERYPRSLSDR VRETLRVWKN
160 170 180 190 200
VEKENASVAG LVKALRACRL NLVADLVEEA LMAQGSVSKS DDTSSALRDS

TVSFSETP
Length:208
Mass (Da):23,124
Last modified:June 1, 2002 - v1
Checksum:iABA3305406137CDB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC110851 Genomic DNA. No translation available.
AF406779 mRNA. Translation: AAN01113.1.
AJ441127 mRNA. Translation: CAD29628.1.
CH473953 Genomic DNA. Translation: EDM12244.1.
RefSeqiNP_690920.1. NM_152937.2.
UniGeneiRn.16183.

Genome annotation databases

EnsembliENSRNOT00000075089; ENSRNOP00000066289; ENSRNOG00000047035.
GeneIDi266610.
KEGGirno:266610.
UCSCiRGD:628700. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC110851 Genomic DNA. No translation available.
AF406779 mRNA. Translation: AAN01113.1.
AJ441127 mRNA. Translation: CAD29628.1.
CH473953 Genomic DNA. Translation: EDM12244.1.
RefSeqiNP_690920.1. NM_152937.2.
UniGeneiRn.16183.

3D structure databases

SMRiQ8R2E7. Positions 2-190.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8R2E7. 2 interactions.
STRINGi10116.ENSRNOP00000066289.

PTM databases

iPTMnetiQ8R2E7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000075089; ENSRNOP00000066289; ENSRNOG00000047035.
GeneIDi266610.
KEGGirno:266610.
UCSCiRGD:628700. rat.

Organism-specific databases

CTDi8772.
RGDi628700. Fadd.

Phylogenomic databases

eggNOGiENOG410J0KM. Eukaryota.
ENOG41122TX. LUCA.
GeneTreeiENSGT00390000002105.
HOGENOMiHOG000112490.
HOVERGENiHBG000853.
KOiK02373.
OMAiCQMNLVA.
OrthoDBiEOG76X61Z.
PhylomeDBiQ8R2E7.
TreeFamiTF102046.

Enzyme and pathway databases

ReactomeiR-RNO-3371378. Regulation by c-FLIP.
R-RNO-5213460. RIPK1-mediated regulated necrosis.
R-RNO-5218900. CASP8 activity is inhibited.
R-RNO-5357786. TNFR1-induced proapoptotic signaling.
R-RNO-69416. Dimerization of procaspase-8.
R-RNO-75157. FasL/ CD95L signaling.
R-RNO-75158. TRAIL signaling.

Family and domain databases

Gene3Di1.10.533.10. 2 hits.
InterProiIPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR001875. DED_dom.
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. "Identification of neuronal caspases and involvement of death domain proteins in neuronal apoptosis."
    Spadoni C.G.
    Thesis (2001), University of London, London, United Kingdom
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: Sprague-DawleyImported.
    Tissue: Ischemic brainImported.
  2. Kim P.K., Billiar T.R.
    Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: Sprague-DawleyImported.
    Tissue: LiverImported.
  3. "Hepatocyte Fas-associating death domain protein/mediator of receptor-induced toxicity (FADD/MORT1) levels increase in response to pro-apoptotic stimuli."
    Kim P.K., Wang Y., Gambotto A., Kim Y.M., Weller R., Zuckerbraun B.S., Hua Y., Watkins S.C., Billiar T.R.
    J. Biol. Chem. 277:38855-38862(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: Sprague-DawleyImported.
    Tissue: LiverImported.
  4. Neame S.
    Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: Sprague-DawleyImported.
    Tissue: Ischemic brainImported.
  5. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Rat Genome Sequencing Project Consortium
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown NorwayImported.
  6. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  7. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  8. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Ensembl
    Submitted (FEB-2013) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: Brown NorwayImported.

Entry informationi

Entry nameiQ8R2E7_RAT
AccessioniPrimary (citable) accession number: Q8R2E7
Entry historyi
Integrated into UniProtKB/TrEMBL: June 1, 2002
Last sequence update: June 1, 2002
Last modified: June 8, 2016
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Proteomics identificationCombined sources, Reference proteomeImported

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 one 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.