DEDD

DEDD
Identifiers
Aliases	DEDD , CASP8IP1, DEDD1, DEFT, FLDED1, KE05, death effector domain containing
External IDs	OMIM: 606841; MGI: 1333874; HomoloGene: 7980; GeneCards: DEDD; OMA:DEDD - orthologs
Gene location (Human) Chr. Chromosome 1 (human) [1] Band 1q23.3 Start 161,120,974 bp [1] End 161,132,688 bp [1]
Gene location (Mouse) Chr. Chromosome 1 (mouse) [2] Band 1 H3|1 79.34 cM Start 171,156,713 bp [2] End 171,169,899 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in oocyte gastrocnemius muscle muscle of thigh gastric mucosa secondary oocyte gallbladder blood granulocyte right coronary artery biceps brachii Top expressed in primary oocyte neural layer of retina spermatid zygote yolk sac fossa condyle secondary oocyte seminiferous tubule muscle of thigh More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein binding DNA binding Cellular component cytoplasm nucleus nucleolus Biological process regulation of apoptotic process regulation of transcription, DNA-templated transcription, DNA-templated apoptotic process spermatogenesis extrinsic apoptotic signaling pathway via death domain receptors negative regulation of protein catabolic process decidualization negative regulation of transcription of nucleolar large rRNA by RNA polymerase I Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 9191 21945 Ensembl ENSG00000158796 ENSMUSG00000013973 UniProt O75618 Q9Z1L3 RefSeq (mRNA) NM_001039711 NM_001039712 NM_004216 NM_032998 NM_001330765 NM_001128609 NM_011615 NM_001357550 NM_001357551 NM_001357552 NM_001357553 RefSeq (protein) NP_001034800 NP_001034801 NP_001317694 NP_127491 NP_001122081 NP_035745 NP_001344479 NP_001344480 NP_001344481 NP_001344482 Location (UCSC) Chr 1: 161.12 – 161.13 Mb Chr 1: 171.16 – 171.17 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Death effector domain containing protein is a protein that in humans is encoded by the DEDD gene. ^{[5] [6] [7]}

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. ^[7]

Interactions

DEDD has been shown to interact with:

• CFLAR, ^{[8] [9]}
• Caspase 8, ^{[8] [10] [11]} and
• FADD. ^{[5] [9]}

References

1. GRCh38: Ensembl release 89: ENSG00000158796 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000013973 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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.
6. 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/endo.139.12.6335 . PMID   9832420.
7. "Entrez Gene: DEDD death effector domain containing".
8. 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.
9. 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.
10. 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.
11. 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

• Park MY, Ryu SW, Kim KD, Lim JS, Lee ZW, Kim E (2005). "Fas-associated factor-1 mediates chemotherapeutic-induced apoptosis via death effector filament formation". Int. J. Cancer. 115 (3): 412–8. doi: 10.1002/ijc.20857 . PMID   15688372.
• Alcivar A, Hu S, Tang J, Yang X (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.
• Lee JC, Schickling O, Stegh AH, Oshima RG, Dinsdale D, Cohen GM, Peter ME (2002). "DEDD regulates degradation of intermediate filaments during apoptosis". J. Cell Biol. 158 (6): 1051–66. doi:10.1083/jcb.200112124. PMC   2173221 . PMID   12235123.
• Zhan Y, Hegde R, Srinivasula SM, Fernandes-Alnemri T, Alnemri ES (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.
• Schickling O, Stegh AH, Byrd J, Peter ME (2002). "Nuclear localization of DEDD leads to caspase-6 activation through its death effector domain and inhibition of RNA polymerase I dependent transcription". Cell Death Differ. 8 (12): 1157–68. doi: 10.1038/sj.cdd.4400928 . PMID   11753564.
• Roth W, Stenner-Liewen F, Pawlowski K, Godzik A, Reed JC (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.