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Search results 201 to 237 out of 237 for Daxx

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Type Details Score
Publication
28358373 | -
First Author: Salsman J
Year: 2017
Journal: Cell Death Dis
Title: Myogenic differentiation triggers PML nuclear body loss and DAXX relocalization to chromocentres.
Volume: 8
Issue: 3
Pages: e2724
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GXD Expression
GXD Expression
 
Probe: MGI:7384879
Assay Type: Immunohistochemistry
Annotation Date: 2022-11-18
Strength: Present
Sex: Not Specified
Emaps: EMAPS:160362
Pattern: Regionally restricted
Stage: TS02
Assay Id: MGI:7384974
Age: embryonic day 1.0
Note: Daxx gold particles and Atrx gold particles were noted in a single structure in close proximity to the surface of interchromatin granule cluster.
Specimen Label: 2d
Detected: true
Specimen Num: 2
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Publication
18480450 | -
First Author: Ullman AJ
Year: 2008
Journal: J Virol
Title: Cellular proteins PML and Daxx mediate an innate antiviral defense antagonized by the adenovirus E4 ORF3 protein.
Volume: 82
Issue: 15
Pages: 7325-35
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Publication
16524876 | -
First Author: Kwon JE
Year: 2006
Journal: J Biol Chem
Title: BTB domain-containing speckle-type POZ protein (SPOP) serves as an adaptor of Daxx for ubiquitination by Cul3-based ubiquitin ligase.
Volume: 281
Issue: 18
Pages: 12664-72
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Protein
G3UWI4
Organism: Mus musculus/domesticus
Length: 166  
Fragment?: true
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Protein
G3UWJ9
Organism: Mus musculus/domesticus
Length: 137  
Fragment?: true
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Protein
G3UX50
Organism: Mus musculus/domesticus
Length: 206  
Fragment?: true
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Protein Domain
IPR031333 | Daxx_N
Type: Domain
Description: The Daxx protein (also known as death domain-associated protein 6) is thought to play a role in apoptosis. Daxx forms a complex with Axin []. Daxx is a scaffold protein shown to play diverse roles in transcription and cell cycle regulation. This N-terminal domain folds into a left-handed four-helix bundle (H1, H2, H4, H5) that binds to the N-terminal residues of the tumour-suppressor Rassf1C [].
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Protein Domain
IPR038298 | Daxx_N_sf
Type: Homologous_superfamily
Description: The Daxx protein (also known as death domain-associated protein 6) is thought to play a role in apoptosis. Daxx forms a complex with Axin []. Daxx is a scaffold protein shown to play diverse roles in transcription and cell cycle regulation. This N-terminal domain folds into a left-handed four-helix bundle (H1, H2, H4, H5) that binds to the N-terminal residues of the tumour-suppressor Rassf1C [].
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Protein
Q5XW58
Organism: Mus musculus/domesticus
Length: 119  
Fragment?: true
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Protein Domain
IPR046378 | DAXX_histone-bd
Type: Domain
Description: Daxx (also known as death domain-associated protein 6) is a nuclear protein that modulates transcription of various genes and is involved in cell death and/or the suppression of growth. Daxx is also a histone chaperone conserved in metazoa that acts specifically on histone H3.3. This entry represents the histone-binding domain of Daxx that interacts with the histone H3.3-H4 dimer, and in doing so competes with DNA binding and interactions between the histone chaperone ASF1/CIA and the H3-H4 dimer [, , , , , ].
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Protein Domain
IPR046426 | DAXX_histone-bd_sf
Type: Homologous_superfamily
Description: Daxx (also known as death domain-associated protein 6) is a nuclear protein that modulates transcription of various genes and is involved in cell death and/or the suppression of growth. Daxx is also a histone chaperone conserved in metazoa that acts specifically on histone H3.3. This entry represents the histone-binding domain of Daxx that interacts with the histone H3.3-H4 dimer, and in doing so competes with DNA binding and interactions between the histone chaperone ASF1/CIA and the H3-H4 dimer [, , , , , ].
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Publication
21474063 | -
First Author: Mukhopadhyay D
Year: 2011
Journal: Mol Cell
Title: SUMmOning Daxx-mediated repression.
Volume: 42
Issue: 1
Pages: 4-5
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Publication
23023413 | -
First Author: Muromoto R
Year: 2012
Journal: Yakugaku Zasshi
Title: [Death domain-associated protein (DAXX)-mediated regulation of transcription and cell death].
Volume: 132
Issue: 9
Pages: 979-84
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GXD Expression
GXD Expression
 
Probe: MGI:7384879
Assay Type: Immunohistochemistry
Annotation Date: 2022-11-18
Strength: Present
Sex: Not Specified
Emaps: EMAPS:160362
Pattern: Regionally restricted
Stage: TS02
Assay Id: MGI:7384973
Age: embryonic day 1.0
Note: At late two-cell stage, colocalization of Daxx and ATRX was detectable both in the ring-shaped heterochromatin zones associated with the nucleolus precursor body (NPB) periphery and in NPB-unassociated heterochromatin patches. Some zones of Daxx localization did not overlap with ATRX (and vise versa). ATRX was found in 60% Daxx-positive heterochromatin areas associated with NPBs and in 80% Daxx-positive heterochromatin clumps located outside the NPBs.
Specimen Label: 4b
Detected: true
Specimen Num: 2
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Publication
11948183 | -
First Author: Lin DY
Year: 2002
Journal: J Biol Chem
Title: Essential role of the 58-kDa microspherule protein in the modulation of Daxx-dependent transcriptional repression as revealed by nucleolar sequestration.
Volume: 277
Issue: 28
Pages: 25446-56
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Publication
16571602 | -
First Author: Davidovic L
Year: 2006
Journal: Hum Mol Genet
Title: The nuclear microspherule protein 58 is a novel RNA-binding protein that interacts with fragile X mental retardation protein in polyribosomal mRNPs from neurons.
Volume: 15
Issue: 9
Pages: 1525-38
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Publication
15044100 | -
First Author: Song H
Year: 2004
Journal: Biochem Biophys Res Commun
Title: Human MCRS2, a cell-cycle-dependent protein, associates with LPTS/PinX1 and reduces the telomere length.
Volume: 316
Issue: 4
Pages: 1116-23
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Protein Domain
IPR037912 | MCRS1
Type: Family
Description: Microspherule protein 1 (MCRS1 or MSP58) is an RNA-binding protein that interacts with Daxx transcriptional regulator, relieving its repressor activity. Overexpression of MCRS1 leads to translocation of Daxx to the enlarged nucleoli in COS-1 or 293 cells []. It also interacts with fragile X messenger ribonucleoprotein 1 (FMRP), which represses specific mRNAs being transported as silent ribonucleoparticles from the cell body of a neuron to the distant synapse. MCRS1 binds to the G-quadruplex structures of the mRNA []. MCRS1 is a component of the NSL complex [], the MLL1/MLL complex [], and is a putative regulatory component in the chromatin remodeling INO80 complex []. The isoform MCRS2 is a cell-cycle-dependent protein which accumulates in the early S phase, and interacts with the telomerase-inhibitory protein LPTS/PinX1 [].
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Publication
16973549 | -
First Author: Feederle R
Year: 2006
Journal: J Virol
Title: Epstein-Barr virus BNRF1 protein allows efficient transfer from the endosomal compartment to the nucleus of primary B lymphocytes.
Volume: 80
Issue: 19
Pages: 9435-43
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Publication
22102817 | -
First Author: Tsai K
Year: 2011
Journal: PLoS Pathog
Title: EBV tegument protein BNRF1 disrupts DAXX-ATRX to activate viral early gene transcription.
Volume: 7
Issue: 11
Pages: e1002376
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Protein Domain
IPR010077 | Herpes_virus_tegument
Type: Family
Description: This is a family of major tegument proteins from Herpesviruses. Herpesvirus tegument proteins counteract the intrinsic anti-viral defenses and support the early steps of infection. BNRF1 is the Epstein-Barr virus (EBV) major tegument protein and plays an important role in viral transport from the endosomes to the nucleus []. Furthermore, it supports EBV early infection by interacting with host nuclear protein Daxx and disrupting the formation of the Daxx-ATRX chromatin remodeling complex [].
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Protein
A0A2R8VJX8
Organism: Mus musculus/domesticus
Length: 88  
Fragment?: true
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Publication
15710327 | J:95945
First Author: Zhu J
Year: 2005
Journal: Cancer Cell
Title: A sumoylation site in PML/RARA is essential for leukemic transformation.
Volume: 7
Issue: 2
Pages: 143-53
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Publication
9545376 | J:47809
First Author: Herberg JA
Year: 1998
Journal: J Mol Biol
Title: TAPASIN, DAXX, RGL2, HKE2 and four new genes (BING 1, 3 to 5) form a dense cluster at the centromeric end of the MHC.
Volume: 277
Issue: 4
Pages: 839-57
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Publication
18716620 | J:141030
First Author: Song MS
Year: 2008
Journal: Nature
Title: The deubiquitinylation and localization of PTEN are regulated by a HAUSP-PML network.
Volume: 455
Issue: 7214
Pages: 813-7
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Publication
9645950 | J:49095
 
First Author: Pluta AF
Year: 1998
Journal: J Cell Sci
Title: Interphase-specific association of intrinsic centromere protein CENP-C with HDaxx, a death domain-binding protein implicated in Fas-mediated cell death.
Volume: 111 ( Pt 14)
Pages: 2029-41
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Publication
20885787 | J:165659
First Author: Baumann C
Year: 2010
Journal: PLoS Genet
Title: Loss of maternal ATRX results in centromere instability and aneuploidy in the mammalian oocyte and pre-implantation embryo.
Volume: 6
Issue: 9
Pages: e1001137
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Publication
30251683 | J:270470
First Author: Hu J
Year: 2018
Journal: Biochim Biophys Acta Mol Basis Dis
Title: Exosomal Mst1 transfer from cardiac microvascular endothelial cells to cardiomyocytes deteriorates diabetic cardiomyopathy.
Volume: 1864
Issue: 11
Pages: 3639-3649
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Protein
Q99L90
Organism: Mus musculus/domesticus
Length: 462  
Fragment?: false
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Protein
Q3TJY1
Organism: Mus musculus/domesticus
Length: 449  
Fragment?: false
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Protein
Q3TYU7
Organism: Mus musculus/domesticus
Length: 462  
Fragment?: false
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Publication
21303910 | -
First Author: Chen L
Year: 2011
Journal: J Biol Chem
Title: Subunit organization of the human INO80 chromatin remodeling complex: an evolutionarily conserved core complex catalyzes ATP-dependent nucleosome remodeling.
Volume: 286
Issue: 13
Pages: 11283-9
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Publication
22106414 | J:198902
First Author: Vincent A
Year: 2012
Journal: Cardiovasc Res
Title: Down-regulation of the transcription factor ZAC1 upon pre- and postconditioning protects against I/R injury in the mouse myocardium.
Volume: 94
Issue: 2
Pages: 351-8
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Publication
27626385 | J:238814
First Author: Wang D
Year: 2016
Journal: Nature
Title: Acetylation-regulated interaction between p53 and SET reveals a widespread regulatory mode.
Volume: 538
Issue: 7623
Pages: 118-122
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Publication
20018852 | -
First Author: Cai Y
Year: 2010
Journal: J Biol Chem
Title: Subunit composition and substrate specificity of a MOF-containing histone acetyltransferase distinct from the male-specific lethal (MSL) complex.
Volume: 285
Issue: 7
Pages: 4268-72
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Publication
15960975 | J:156231
First Author: Dou Y
Year: 2005
Journal: Cell
Title: Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF.
Volume: 121
Issue: 6
Pages: 873-85
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