DEDD

Protein-coding gene in humans
DEDD
Identifiers
AliasesDEDD, CASP8IP1, DEDD1, DEFT, FLDED1, KE05, death effector domain containing
External IDsOMIM: 606841; MGI: 1333874; HomoloGene: 7980; GeneCards: DEDD; OMA:DEDD - orthologs
Gene location (Human)
Chromosome 1 (human)
Chr.Chromosome 1 (human)[1]
Chromosome 1 (human)
Genomic location for DEDD
Genomic location for DEDD
Band1q23.3Start161,120,974 bp[1]
End161,132,688 bp[1]
Gene location (Mouse)
Chromosome 1 (mouse)
Chr.Chromosome 1 (mouse)[2]
Chromosome 1 (mouse)
Genomic location for DEDD
Genomic location for DEDD
Band1 H3|1 79.34 cMStart171,156,713 bp[2]
End171,169,899 bp[2]
RNA expression pattern
Bgee
HumanMouse (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
SpeciesHumanMouse
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 MbChr 1: 171.16 – 171.17 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/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:

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000158796 – Ensembl, May 2017
  2. ^ a b c 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. ^ a b 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. ^ a b "Entrez Gene: DEDD death effector domain containing".
  8. ^ a b 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. ^ a b 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.


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