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{{Infobox_gene}}
{{PBB_Controls
'''Death effector domain containing protein''' is a [[protein]] that in humans is encoded by the ''DEDD'' [[gene]].<ref name="pmid9774341">{{cite journal | vauthors = Stegh AH, Schickling O, Ehret A, Scaffidi C, Peterhänsel C, Hofmann TG, Grummt I, Krammer PH, Peter ME | title = DEDD, a novel death effector domain-containing protein, targeted to the nucleolus | journal = EMBO J | volume = 17 | issue = 20 | pages = 5974–86 | date = Dec 1998 | pmid = 9774341 | pmc = 1170924 | doi = 10.1093/emboj/17.20.5974 }}</ref><ref name="pmid9832420">{{cite journal | vauthors = Leo CP, Hsu SY, McGee EA, Salanova M, Hsueh AJ | title = DEFT, a novel death effector domain-containing molecule predominantly expressed in testicular germ cells | journal = Endocrinology | volume = 139 | issue = 12 | pages = 4839–48 | date = Dec 1998 | pmid = 9832420 | pmc = | doi = 10.1210/en.139.12.4839 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: DEDD death effector domain containing| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9191| accessdate = }}</ref>
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Death effector domain containing
| HGNCid = 2755
| Symbol = DEDD
| AltSymbols =; CASP8IP1; DEDD1; DEFT; FLDED1; KE05
| OMIM = 606841
| ECnumber = 
| Homologene = 7980
| MGIid = 1333874
| GeneAtlas_image1 = PBB_GE_DEDD_215158_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_DEDD_202480_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_DEDD_211255_x_at_tn.png
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005730 |text = nucleolus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006917 |text = induction of apoptosis}} {{GNF_GO|id=GO:0007283 |text = spermatogenesis}} {{GNF_GO|id=GO:0008625 |text = induction of apoptosis via death domain receptors}} {{GNF_GO|id=GO:0016481 |text = negative regulation of transcription}} {{GNF_GO|id=GO:0042981 |text = regulation of apoptosis}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 9191
    | Hs_Ensembl = ENSG00000158796
    | Hs_RefseqProtein = NP_001034800
    | Hs_RefseqmRNA = NM_001039711
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 159357388
    | Hs_GenLoc_end = 159369082
    | Hs_Uniprot = O75618
    | Mm_EntrezGene = 21945
    | Mm_Ensembl = ENSMUSG00000013973
    | Mm_RefseqmRNA = NM_011615
    | Mm_RefseqProtein = NP_035745
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 1
    | Mm_GenLoc_start = 173167928
    | Mm_GenLoc_end = 173178291
    | Mm_Uniprot = Q3U001
  }}
}}
'''Death effector domain containing''', also known as '''DEDD''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DEDD death effector domain containing| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9191| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
This gene encodes a protein that contains a death effector [[protein domain|domain]] (DED). DED is a [[protein–protein interaction]] domain shared by adaptors, regulators and executors of the [[programmed cell death]] pathway. [[Gene expression|Overexpression]] of this gene was shown to induce weak [[apoptosis]]. Upon stimulation, this protein was found to [[protein targeting#Protein translocation|translocate]] from cytoplasm to nucleus and colocalize with [[UBTF]], a basal factor required for [[RNA polymerase I]] transcription, in the [[nucleolus]]. At least three transcript variants encoding the same protein have been found for this gene.<ref name="entrez"/>
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a protein that contains a death effector domain (DED). DED is a protein-protein interaction domain shared by adaptors, regulators and executors of the programmed cell death pathway. Overexpression of this gene was shown to induce weak apoptosis. Upon stimulation, this protein was found to translocate from cytoplasm to nucleus and colocalize with UBTF, a basal factor required for RNA polymerase I transcription, in the nucleolus. At least three transcript variants encoding the same protein have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: DEDD death effector domain containing| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9191| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal  | author=Ewing RM, Chu P, Elisma F, ''et al.'' |title=Large-scale mapping of human protein-protein interactions by mass spectrometry. |journal=Mol. Syst. Biol. |volume=3 |issue=  |pages= 89 |year= 2007 |pmid= 17353931 |doi= 10.1038/msb4100134 }}
*{{cite journal  | author=Gregory SG, Barlow KF, McLay KE, ''et al.'' |title=The DNA sequence and biological annotation of human chromosome 1. |journal=Nature |volume=441 |issue= 7091 |pages= 315-21 |year= 2006 |pmid= 16710414 |doi= 10.1038/nature04727 }}
*{{cite journal  | author=Rual JF, Venkatesan K, Hao T, ''et al.'' |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173-8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 }}
*{{cite journal  | author=Park MY, Ryu SW, Kim KD, ''et al.'' |title=Fas-associated factor-1 mediates chemotherapeutic-induced apoptosis via death effector filament formation. |journal=Int. J. Cancer |volume=115 |issue= 3 |pages= 412-8 |year= 2005 |pmid= 15688372 |doi= 10.1002/ijc.20857 }}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  | author=Alcivar A, Hu S, Tang J, Yang X |title=DEDD and DEDD2 associate with caspase-8/10 and signal cell death. |journal=Oncogene |volume=22 |issue= 2 |pages= 291-7 |year= 2003 |pmid= 12527898 |doi= 10.1038/sj.onc.1206099 }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | author=Lee JC, Schickling O, Stegh AH, ''et al.'' |title=DEDD regulates degradation of intermediate filaments during apoptosis. |journal=J. Cell Biol. |volume=158 |issue= 6 |pages= 1051-66 |year= 2002 |pmid= 12235123 |doi= 10.1083/jcb.200112124 }}
*{{cite journal  | author=Zhan Y, Hegde R, Srinivasula SM, ''et al.'' |title=Death effector domain-containing proteins DEDD and FLAME-3 form nuclear complexes with the TFIIIC102 subunit of human transcription factor IIIC. |journal=Cell Death Differ. |volume=9 |issue= 4 |pages= 439-47 |year= 2002 |pmid= 11965497 |doi= 10.1038/sj/cdd/4401038 }}
*{{cite journal  | author=Schickling O, Stegh AH, Byrd J, Peter ME |title=Nuclear localization of DEDD leads to caspase-6 activation through its death effector domain and inhibition of RNA polymerase I dependent transcription. |journal=Cell Death Differ. |volume=8 |issue= 12 |pages= 1157-68 |year= 2002 |pmid= 11753564 |doi= 10.1038/sj/cdd/4400928 }}
*{{cite journal  | author=Roth W, Stenner-Liewen F, Pawlowski K, ''et al.'' |title=Identification and characterization of DEDD2, a death effector domain-containing protein. |journal=J. Biol. Chem. |volume=277 |issue= 9 |pages= 7501-8 |year= 2002 |pmid= 11741985 |doi= 10.1074/jbc.M110749200 }}
*{{cite journal  | author=Leo CP, Hsu SY, McGee EA, ''et al.'' |title=DEFT, a novel death effector domain-containing molecule predominantly expressed in testicular germ cells. |journal=Endocrinology |volume=139 |issue= 12 |pages= 4839-48 |year= 1998 |pmid= 9832420 |doi=  }}
*{{cite journal  | author=Stegh AH, Schickling O, Ehret A, ''et al.'' |title=DEDD, a novel death effector domain-containing protein, targeted to the nucleolus. |journal=EMBO J. |volume=17 |issue= 20 |pages= 5974-86 |year= 1998 |pmid= 9774341 |doi= 10.1093/emboj/17.20.5974 }}
}}
{{refend}}


{{protein-stub}}
DEDD has been shown to [[Protein-protein interaction|interact]] with:
{{WikiDoc Sources}}
* [[CFLAR]],<ref name = pmid11965497/><ref name = pmid11741985/>
* [[Caspase 8]],<ref name = pmid11965497>{{cite journal | vauthors = Zhan Y, Hegde R, Srinivasula SM, Fernandes-Alnemri T, Alnemri ES | title = Death effector domain-containing proteins DEDD and FLAME-3 form nuclear complexes with the TFIIIC102 subunit of human transcription factor IIIC | journal = Cell Death Differ. | volume = 9 | issue = 4 | pages = 439–47 | date = Apr 2002 | pmid = 11965497 | doi = 10.1038/sj/cdd/4401038 }}</ref><ref name = autogenerated1>{{cite journal | vauthors = Stegh AH, Schickling O, Ehret A, Scaffidi C, Peterhänsel C, Hofmann TG, Grummt I, Krammer PH, Peter ME | title = DEDD, a novel death effector domain-containing protein, targeted to the nucleolus | journal = EMBO J. | volume = 17 | issue = 20 | pages = 5974–86 | date = Oct 1998 | pmid = 9774341 | pmc = 1170924 | doi = 10.1093/emboj/17.20.5974 }}</ref><ref name = pmid12527898>{{cite journal | vauthors = Alcivar A, Hu S, Tang J, Yang X | title = DEDD and DEDD2 associate with caspase-8/10 and signal cell death | journal = Oncogene | volume = 22 | issue = 2 | pages = 291–7 | date = Jan 2003 | pmid = 12527898 | doi = 10.1038/sj.onc.1206099 }}</ref>  and
* [[FADD]].<ref name = pmid9774341/><ref name = pmid11741985>{{cite journal | vauthors = Roth W, Stenner-Liewen F, Pawlowski K, Godzik A, Reed JC | title = Identification and characterization of DEDD2, a death effector domain-containing protein | journal = J. Biol. Chem. | volume = 277 | issue = 9 | pages = 7501–8 | date = Mar 2002 | pmid = 11741985 | doi = 10.1074/jbc.M110749200 }}</ref>
 
== References ==
{{Reflist}}
{{Clear}}
 
== Further reading ==
{{Refbegin| 2}}
* {{cite journal | vauthors = Park MY, Ryu SW, Kim KD, Lim JS, Lee ZW, Kim E | title = Fas-associated factor-1 mediates chemotherapeutic-induced apoptosis via death effector filament formation | journal = Int. J. Cancer | volume = 115 | issue = 3 | pages = 412–8 | year = 2005 | pmid = 15688372 | doi = 10.1002/ijc.20857 }}
* {{cite journal | vauthors = Alcivar A, Hu S, Tang J, Yang X | title = DEDD and DEDD2 associate with caspase-8/10 and signal cell death | journal = Oncogene | volume = 22 | issue = 2 | pages = 291–7 | year = 2003 | pmid = 12527898 | doi = 10.1038/sj.onc.1206099 }}
* {{cite journal | vauthors = Lee JC, Schickling O, Stegh AH, Oshima RG, Dinsdale D, Cohen GM, Peter ME | title = DEDD regulates degradation of intermediate filaments during apoptosis | journal = J. Cell Biol. | volume = 158 | issue = 6 | pages = 1051–66 | year = 2002 | pmid = 12235123 | pmc = 2173221 | doi = 10.1083/jcb.200112124 }}
* {{cite journal | vauthors = Zhan Y, Hegde R, Srinivasula SM, Fernandes-Alnemri T, Alnemri ES | title = Death effector domain-containing proteins DEDD and FLAME-3 form nuclear complexes with the TFIIIC102 subunit of human transcription factor IIIC | journal = Cell Death Differ. | volume = 9 | issue = 4 | pages = 439–47 | year = 2002 | pmid = 11965497 | doi = 10.1038/sj/cdd/4401038 }}
* {{cite journal | vauthors = Schickling O, Stegh AH, Byrd J, Peter ME | title = Nuclear localization of DEDD leads to caspase-6 activation through its death effector domain and inhibition of RNA polymerase I dependent transcription | journal = Cell Death Differ. | volume = 8 | issue = 12 | pages = 1157–68 | year = 2002 | pmid = 11753564 | doi = 10.1038/sj.cdd.4400928 }}
* {{cite journal | vauthors = Roth W, Stenner-Liewen F, Pawlowski K, Godzik A, Reed JC | title = Identification and characterization of DEDD2, a death effector domain-containing protein | journal = J. Biol. Chem. | volume = 277 | issue = 9 | pages = 7501–8 | year = 2002 | pmid = 11741985 | doi = 10.1074/jbc.M110749200 }}
{{Refend}}
 
 
{{Gene-1-stub}}

Latest revision as of 18:21, 30 August 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Death effector domain containing protein is a protein that in humans is encoded by the DEDD gene.[1][2][3]

Function

This gene encodes a protein that contains a death effector domain (DED). DED is a protein–protein interaction domain shared by adaptors, regulators and executors of the programmed cell death pathway. Overexpression of this gene was shown to induce weak apoptosis. Upon stimulation, this protein was found to translocate from cytoplasm to nucleus and colocalize with UBTF, a basal factor required for RNA polymerase I transcription, in the nucleolus. At least three transcript variants encoding the same protein have been found for this gene.[3]

Interactions

DEDD has been shown to interact with:

References

  1. ↑ 1.0 1.1 Stegh AH, Schickling O, Ehret A, Scaffidi C, Peterhänsel C, Hofmann TG, Grummt I, Krammer PH, Peter ME (Dec 1998). "DEDD, a novel death effector domain-containing protein, targeted to the nucleolus". EMBO J. 17 (20): 5974–86. doi:10.1093/emboj/17.20.5974. PMC 1170924. PMID 9774341.
  2. ↑ Leo CP, Hsu SY, McGee EA, Salanova M, Hsueh AJ (Dec 1998). "DEFT, a novel death effector domain-containing molecule predominantly expressed in testicular germ cells". Endocrinology. 139 (12): 4839–48. doi:10.1210/en.139.12.4839. PMID 9832420.
  3. ↑ 3.0 3.1 "Entrez Gene: DEDD death effector domain containing".
  4. ↑ 4.0 4.1 Zhan Y, Hegde R, Srinivasula SM, Fernandes-Alnemri T, Alnemri ES (Apr 2002). "Death effector domain-containing proteins DEDD and FLAME-3 form nuclear complexes with the TFIIIC102 subunit of human transcription factor IIIC". Cell Death Differ. 9 (4): 439–47. doi:10.1038/sj/cdd/4401038. PMID 11965497.
  5. ↑ 5.0 5.1 Roth W, Stenner-Liewen F, Pawlowski K, Godzik A, Reed JC (Mar 2002). "Identification and characterization of DEDD2, a death effector domain-containing protein". J. Biol. Chem. 277 (9): 7501–8. doi:10.1074/jbc.M110749200. PMID 11741985.
  6. ↑ Stegh AH, Schickling O, Ehret A, Scaffidi C, Peterhänsel C, Hofmann TG, Grummt I, Krammer PH, Peter ME (Oct 1998). "DEDD, a novel death effector domain-containing protein, targeted to the nucleolus". EMBO J. 17 (20): 5974–86. doi:10.1093/emboj/17.20.5974. PMC 1170924. PMID 9774341.
  7. ↑ Alcivar A, Hu S, Tang J, Yang X (Jan 2003). "DEDD and DEDD2 associate with caspase-8/10 and signal cell death". Oncogene. 22 (2): 291–7. doi:10.1038/sj.onc.1206099. PMID 12527898.

Further reading


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