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Gene Ontology Classifications
Fas death domain-associated protein

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GO curators for mouse genes have assigned the following annotations to the gene product of Daxx. (This text reflects annotations as of Tuesday, May 26, 2015.)
Summary from NCBI RefSeq

[Summary is not available for the mouse gene. This summary is for the human ortholog.] This gene encodes a multifunctional protein that resides in multiple locations in the nucleus and in the cytoplasm. It interacts with a wide variety of proteins, such as apoptosis antigen Fas, centromere protein C, and transcription factor erythroblastosis virus E26 oncogene homolog 1. In the nucleus, the encoded protein functions as a potent transcription repressor that binds to sumoylated transcription factors. Its repression can be relieved by the sequestration of this protein into promyelocytic leukemia nuclear bodies or nucleoli. This protein also associates with centromeres in G2 phase. In the cytoplasm, the encoded protein may function to regulate apoptosis. The subcellular localization and function of this protein are modulated by post-translational modifications, including sumoylation, phosphorylation and polyubiquitination. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Nov 2008]
Summary text based on GO annotations supported by experimental evidence in mouse
Summary text based on GO annotations supported by experimental evidence in other organisms
Summary text for additional MGI annotations
  1. Drane P et al. (2010) The death-associated protein DAXX is a novel histone chaperone involved in the replication-independent deposition of H3.3. Genes Dev, 24:1253-65. (PubMed:20504901)
  2. Ecsedy JA et al. (2003) Homeodomain-interacting protein kinase 1 modulates daxx localization, phosphorylation, and transcriptional activity. Mol Cell Biol, 23:950-60. (PubMed:12529400)
  3. Emelyanov AV et al. (2002) The interaction of Pax5 (BSAP) with Daxx can result in transcriptional activation in B cells. J Biol Chem, 277:11156-64. (PubMed:11799127)
  4. Ishov AM et al. (2004) Heterochromatin and ND10 are cell-cycle regulated and phosphorylation-dependent alternate nuclear sites of the transcription repressor Daxx and SWI/SNF protein ATRX. J Cell Sci, 117:3807-20. (PubMed:15252119)
  5. Kawai T et al. (2003) ZIP kinase triggers apoptosis from nuclear PML oncogenic domains. Mol Cell Biol, 23:6174-86. (PubMed:12917339)
  6. Lewis PW et al. (2010) Daxx is an H3.3-specific histone chaperone and cooperates with ATRX in replication-independent chromatin assembly at telomeres. Proc Natl Acad Sci U S A, 107:14075-80. (PubMed:20651253)
  7. Lopez P et al. (2002) Gene control in germinal differentiation: RNF6, a transcription regulatory protein in the mouse sertoli cell. Mol Cell Biol, 22:3488-96. (PubMed:11971979)
  8. Michod D et al. (2012) Calcium-dependent dephosphorylation of the histone chaperone DAXX regulates H3.3 loading and transcription upon neuronal activation. Neuron, 74:122-35. (PubMed:22500635)
  9. Perlman R et al. (2001) TGF-beta-induced apoptosis is mediated by the adapter protein Daxx that facilitates JNK activation. Nat Cell Biol, 3:708-14. (PubMed:11483955)
  10. Tang J et al. (2005) The death domain-associated protein modulates activity of the transcription co-factor Skip/NcoA62. FEBS Lett, 579:2883-90. (PubMed:15878163)
  11. Yang X et al. (1997) Daxx, a novel Fas-binding protein that activates JNK and apoptosis. Cell, 89:1067-76. (PubMed:9215629)
  12. Zhong S et al. (2000) Promyelocytic leukemia protein (PML) and Daxx participate in a novel nuclear pathway for apoptosis. J Exp Med, 191:631-40. (PubMed:10684855)

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Gene Ontology Evidence Code Abbreviations:

  EXP Inferred from experiment
  IAS Inferred from ancestral sequence
  IBA Inferred from biological aspect of ancestor
  IBD Inferred from biological aspect of descendant
  IC Inferred by curator
  IDA Inferred from direct assay
  IEA Inferred from electronic annotation
  IGI Inferred from genetic interaction
  IKR Inferred from key residues
  IMP Inferred from mutant phenotype
  IMR Inferred from missing residues
  IPI Inferred from physical interaction
  IRD Inferred from rapid divergence
  ISS Inferred from sequence or structural similarity
  ISO Inferred from sequence orthology
  ISA Inferred from sequence alignment
  ISM Inferred from sequence model
  NAS Non-traceable author statement
  ND No biological data available
  RCA Reviewed computational analysis
  TAS Traceable author statement


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Mouse Genome Database (MGD), Gene Expression Database (GXD), Mouse Tumor Biology (MTB), Gene Ontology (GO), MouseCyc
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