Details for: DAXX
Associated with
Other Information
Genular Protein ID: 655863942
Symbol: DAXX_HUMAN
Name: Death domain-associated protein 6
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 9215629
Title: Daxx, a novel Fas-binding protein that activates JNK and apoptosis.
PubMed ID: 9215629
PubMed ID: 9407001
Title: Cloning and expression of primate Daxx cDNAs and mapping of the human gene to chromosome 6p21.3 in the MHC region.
PubMed ID: 9407001
PubMed ID: 9645950
Title: Interphase-specific association of intrinsic centromere protein CENP-C with HDaxx, a death domain-binding protein implicated in Fas-mediated cell death.
PubMed ID: 9645950
PubMed ID: 9545376
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.
PubMed ID: 9545376
PubMed ID: 10698492
Title: EAP1/Daxx interacts with ETS1 and represses transcriptional activation of ETS1 target genes.
PubMed ID: 10698492
PubMed ID: 21482821
Title: Daxx-beta and Daxx-gamma, two novel splice variants of the transcriptional co-repressor Daxx.
PubMed ID: 21482821
PubMed ID: 14702039
Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.
PubMed ID: 14702039
DOI: 10.1038/ng1285
PubMed ID: 14574404
Title: The DNA sequence and analysis of human chromosome 6.
PubMed ID: 14574404
DOI: 10.1038/nature02055
PubMed ID: 15489334
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
PubMed ID: 15489334
DOI: 10.1101/gr.2596504
PubMed ID: 10393185
Title: The Pax3-FKHR oncoprotein is unresponsive to the Pax3-associated repressor hDaxx.
PubMed ID: 10393185
PubMed ID: 10684855
Title: Promyelocytic leukemia protein (PML) and Daxx participate in a novel nuclear pathway for apoptosis.
PubMed ID: 10684855
PubMed ID: 10669754
Title: Sequestration and inhibition of Daxx-mediated transcriptional repression by PML.
PubMed ID: 10669754
PubMed ID: 11003656
Title: Inhibition of Daxx-mediated apoptosis by heat shock protein 27.
PubMed ID: 11003656
PubMed ID: 11495919
Title: Apoptosis signal-regulating kinase 1 controls the proapoptotic function of death-associated protein (Daxx) in the cytoplasm.
PubMed ID: 11495919
PubMed ID: 11483955
Title: TGF-beta-induced apoptosis is mediated by the adapter protein Daxx that facilitates JNK activation.
PubMed ID: 11483955
DOI: 10.1038/35087019
PubMed ID: 12150977
Title: Modification of Daxx by small ubiquitin-related modifier-1.
PubMed ID: 12150977
PubMed ID: 11842083
Title: The insulin-sensitive glucose transporter, GLUT4, interacts physically with Daxx. Two proteins with capacity to bind Ubc9 and conjugated to SUMO1.
PubMed ID: 11842083
PubMed ID: 11948183
Title: Essential role of the 58-kDa microspherule protein in the modulation of Daxx-dependent transcriptional repression as revealed by nucleolar sequestration.
PubMed ID: 11948183
PubMed ID: 12140263
Title: Daxx and histone deacetylase II associate with chromatin through an interaction with core histones and the chromatin-associated protein Dek.
PubMed ID: 12140263
PubMed ID: 11907324
Title: Hantavirus nucleocapsid protein interacts with the Fas-mediated apoptosis enhancer Daxx.
PubMed ID: 11907324
PubMed ID: 14678985
Title: HIPK2 regulates transforming growth factor-beta-induced c-Jun NH(2)-terminal kinase activation and apoptosis in human hepatoma cells.
PubMed ID: 14678985
PubMed ID: 12968034
Title: Role of the ASK1-SEK1-JNK1-HIPK1 signal in Daxx trafficking and ASK1 oligomerization.
PubMed ID: 12968034
PubMed ID: 12529400
Title: Homeodomain-interacting protein kinase 1 modulates Daxx localization, phosphorylation, and transcriptional activity.
PubMed ID: 12529400
PubMed ID: 12953102
Title: The ATRX syndrome protein forms a chromatin-remodeling complex with Daxx and localizes in promyelocytic leukemia nuclear bodies.
PubMed ID: 12953102
PubMed ID: 14557665
Title: Adenovirus E1B 55-kilodalton oncoprotein binds to Daxx and eliminates enhancement of p53-dependent transcription by DAXX.
PubMed ID: 14557665
PubMed ID: 15240113
Title: Daxx-mediated transcriptional repression of MMP1 gene is reversed by SPOP.
PubMed ID: 15240113
PubMed ID: 14990586
Title: A novel transcription regulatory complex containing death domain-associated protein and the ATR-X syndrome protein.
PubMed ID: 14990586
PubMed ID: 15364927
Title: Negative regulation of p53 functions by Daxx and the involvement of MDM2.
PubMed ID: 15364927
PubMed ID: 15016915
Title: DAXX interacts with heat shock factor 1 during stress activation and enhances its transcriptional activity.
PubMed ID: 15016915
PubMed ID: 17081983
Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.
PubMed ID: 17081983
PubMed ID: 16524876
Title: BTB domain-containing speckle-type POZ protein (SPOP) serves as an adaptor of Daxx for ubiquitination by Cul3-based ubiquitin ligase.
PubMed ID: 16524876
PubMed ID: 17081986
Title: Role of SUMO-interacting motif in Daxx SUMO modification, subnuclear localization, and repression of sumoylated transcription factors.
PubMed ID: 17081986
PubMed ID: 16964243
Title: A probability-based approach for high-throughput protein phosphorylation analysis and site localization.
PubMed ID: 16964243
DOI: 10.1038/nbt1240
PubMed ID: 16845383
PubMed ID: 17210684
Title: Daxx cooperates with the Axin/HIPK2/p53 complex to induce cell death.
PubMed ID: 17210684
PubMed ID: 18566590
Title: The tumour suppressor RASSF1A promotes MDM2 self-ubiquitination by disrupting the MDM2-DAXX-HAUSP complex.
PubMed ID: 18566590
PubMed ID: 18220336
Title: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.
PubMed ID: 18220336
DOI: 10.1021/pr0705441
PubMed ID: 17942542
Title: Nuclear domain 10 components promyelocytic leukemia protein and hDaxx independently contribute to an intrinsic antiviral defense against human cytomegalovirus infection.
PubMed ID: 17942542
DOI: 10.1128/jvi.01685-07
PubMed ID: 18922870
Title: Human cytomegalovirus protein pp71 displaces the chromatin-associated factor ATRX from nuclear domain 10 at early stages of infection.
PubMed ID: 18922870
DOI: 10.1128/jvi.01215-08
PubMed ID: 18669648
Title: A quantitative atlas of mitotic phosphorylation.
PubMed ID: 18669648
PubMed ID: 19413330
Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.
PubMed ID: 19413330
DOI: 10.1021/ac9004309
PubMed ID: 19690332
Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.
PubMed ID: 19690332
PubMed ID: 19608861
Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.
PubMed ID: 19608861
PubMed ID: 20153724
Title: Daxx is reciprocally regulated by Mdm2 and Hausp.
PubMed ID: 20153724
PubMed ID: 20504901
Title: The death-associated protein DAXX is a novel histone chaperone involved in the replication-independent deposition of H3.3.
PubMed ID: 20504901
DOI: 10.1101/gad.566910
PubMed ID: 20444888
Title: Human cytomegalovirus IE72 protein interacts with the transcriptional repressor hDaxx to regulate LUNA gene expression during lytic infection.
PubMed ID: 20444888
DOI: 10.1128/jvi.02231-09
PubMed ID: 20651253
Title: Daxx is an H3.3-specific histone chaperone and cooperates with ATRX in replication-independent chromatin assembly at telomeres.
PubMed ID: 20651253
PubMed ID: 20068231
Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.
PubMed ID: 20068231
PubMed ID: 21269460
Title: Initial characterization of the human central proteome.
PubMed ID: 21269460
PubMed ID: 21406692
Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.
PubMed ID: 21406692
PubMed ID: 23222847
Title: DAXX-dependent supply of soluble (H3.3-H4) dimers to PML bodies pending deposition into chromatin.
PubMed ID: 23222847
PubMed ID: 23186163
Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.
PubMed ID: 23186163
DOI: 10.1021/pr300630k
PubMed ID: 24200965
Title: Dynamics of histone H3.3 deposition in proliferating and senescent cells reveals a DAXX-dependent targeting to PML-NBs important for pericentromeric heterochromatin organization.
PubMed ID: 24200965
DOI: 10.4161/cc.26988
PubMed ID: 24275569
Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
PubMed ID: 24275569
PubMed ID: 25275136
Title: Viral reprogramming of the Daxx histone H3.3 chaperone during early Epstein-Barr virus infection.
PubMed ID: 25275136
DOI: 10.1128/jvi.01895-14
PubMed ID: 24530302
Title: Mislocalization of the centromeric histone variant CenH3/CENP-A in human cells depends on the chaperone DAXX.
PubMed ID: 24530302
PubMed ID: 27211601
Title: SUMO5, a novel poly-sumo isoform, regulates pml nuclear bodies.
PubMed ID: 27211601
DOI: 10.1038/srep26509
PubMed ID: 28112733
Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.
PubMed ID: 28112733
DOI: 10.1038/nsmb.3366
PubMed ID: 21134643
Title: Structural characterization of the DAXX N-terminal helical bundle domain and its complex with Rassf1C.
PubMed ID: 21134643
PubMed ID: 20927612
Title: NMR chemical shift assignments of a complex between SUMO-1 and SIM peptide derived from the C-terminus of Daxx.
PubMed ID: 20927612
PubMed ID: 23142979
Title: Structure of the variant histone H3.3-H4 heterodimer in complex with its chaperone DAXX.
PubMed ID: 23142979
DOI: 10.1038/nsmb.2439
PubMed ID: 23075851
Title: DAXX envelops a histone H3.3-H4 dimer for H3.3-specific recognition.
PubMed ID: 23075851
DOI: 10.1038/nature11608
Sequence Information:
- Length: 740
- Mass: 81373
- Checksum: 1B309ADDAA878040
- Sequence:
MATANSIIVL DDDDEDEAAA QPGPSHPLPN AASPGAEAPS SSEPHGARGS SSSGGKKCYK LENEKLFEEF LELCKMQTAD HPEVVPFLYN RQQRAHSLFL ASAEFCNILS RVLSRARSRP AKLYVYINEL CTVLKAHSAK KKLNLAPAAT TSNEPSGNNP PTHLSLDPTN AENTASQSPR TRGSRRQIQR LEQLLALYVA EIRRLQEKEL DLSELDDPDS AYLQEARLKR KLIRLFGRLC ELKDCSSLTG RVIEQRIPYR GTRYPEVNRR IERLINKPGP DTFPDYGDVL RAVEKAAARH SLGLPRQQLQ LMAQDAFRDV GIRLQERRHL DLIYNFGCHL TDDYRPGVDP ALSDPVLARR LRENRSLAMS RLDEVISKYA MLQDKSEEGE RKKRRARLQG TSSHSADTPE ASLDSGEGPS GMASQGCPSA SRAETDDEDD EESDEEEEEE EEEEEEEATD SEEEEDLEQM QEGQEDDEEE DEEEEAAAGK DGDKSPMSSL QISNEKNLEP GKQISRSSGE QQNKGRIVSP SLLSEEPLAP SSIDAESNGE QPEELTLEEE SPVSQLFELE IEALPLDTPS SVETDISSSR KQSEEPFTTV LENGAGMVSS TSFNGGVSPH NWGDSGPPCK KSRKEKKQTG SGPLGNSYVE RQRSVHEKNG KKICTLPSPP SPLASLAPVA DSSTRVDSPS HGLVTSSLCI PSPARLSQTP HSQPPRPGTC KTSVATQCDP EEIIVLSDSD
Genular Protein ID: 646257007
Symbol: B4E1C1_HUMAN
Name: N/A
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 14574404
Title: The DNA sequence and analysis of human chromosome 6.
PubMed ID: 14574404
DOI: 10.1038/nature02055
Sequence Information:
- Length: 752
- Mass: 82876
- Checksum: 564F283805B26479
- Sequence:
MRGSENCGEG RLERRFLSII VLDDDDEDEA AAQPGPSHPL PNAASPGAEA PSSSEPHGAR GSSSSGGKKC YKLENEKLFE EFLELCKMQT ADHPEVVPFL YNRQQRAHSL FLASAEFCNI LSRVLSRARS RPAKLYVYIN ELCTVLKAHS AKKKLNLAPA ATTSNEPSGN NPPTHLSLDP TNAENTASQS PRTRGSRRQI QRLEQLLALY VAEIRRLQEK ELDLSELDDP DSAYLQEARL KRKLIRLFGR LCELKDCSSL TGRVIEQRIP YRGTRYPEVN RRIERLINKP GPDTFPDYGD VLRAVEKAAA RHSLGLPRQQ LQLMAQDAFR DVGIRLQERR HLDLIYNFGC HLTDDYRPGV DPALSDPVLA RRLRENRSLA MSRLDEVISK YAMLQDKSEE GERKKRRARL QGTSSHSADT PEASLDSGEG PSGMASQGCP SASRAETDDE DDEESDEEEE EEEEEEEEEA TDSEEEEDLE QMQEGQEDDE EEDEEEEAAA GKDGDKSPMS SLQISNEKNL EPGKQISRSS GEQQNKGRIV SPSLLSEEPL APSSIDAESN GEQPEELTLE EESPVSQLFE LEIEALPLDT PSSVETDISS SRKQSEEPFT TVLENGAGMV SSTSFNGGVS PHNWGDSGPP CKKSRKEKKQ TGSGPLGNSY VERQRSVHEK NGKKICTLPS PPSPLASLAP VADSSTRVDS PSHGLVTSSL CIPSPARLSQ TPHSQPPRPG TCKTSVATQC DPEEIIVLSD SD
Genular Protein ID: 35241425
Symbol: Q53F85_HUMAN
Name: N/A
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 8125298
Title: Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.
PubMed ID: 8125298
PubMed ID: 9373149
Title: Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.
PubMed ID: 9373149
Sequence Information:
- Length: 740
- Mass: 81228
- Checksum: 046B3A2A3BAC65E7
- Sequence:
MATANSIIVL DDDDEDEAAA QPGPSHPLPN AASPGAEAPS SSEPHGARGS SSSGGKKCYK LENEKLCEEF LGLCKMQTAD HPEVVPFLYN RQQRAHSLFL ASAEFCNILS RVLSRARSRP AKLYVYINEL CTVLKAHSAK KKLNLAPAAT TSNEPSGNNP PTHLSLDPTN AENTASQSPR TRGSRRQIQR LEQLLALYVA EIRRLQEKEL DLSELDDPDS AYLQEARLKR KLIRLFGRLC ELKDCSSLTG RVIEQRIPYR GTRYPEVNRR IERLINKPGP DTFPDYGDVL RAVEKAAARH SLGLPRQQLQ LMAQDAFRDA GIRLQERRHL DLIYNFGCHL TDDYRPGVDP ALSDPVLARR LRENRSLAMS RLDEVISKYA MLQDKSEEGE RKKRRARLQG TSSHSADTPE ASLDSGEGPS GMASQGCPSA SRAETDDEDD EESDEEEEEE EEEEEEEATD SEEEEDLEQM QEGQEDDEEE DEEEEAAAGK DGDKSPMSSL QISNEKNLEP GKQISRSSGE QQNKGRIVSP SLLSEEPLAP SSIDAESNGE QPEELTLEEE SPVSQLFELE IEALPLDTPS SVETDISSSR KQSEEPFTTV LENGAGMVSS TSFNGGVSPH NWGDSGPPCK KSRKEKKQTG SGPLGNSYVE RQRSVHEKNG KKICTLPSPP SPLASLAPVA DSSTRVDSPS HGLVTSSLCI PSPARLSQTP HSQPPRPGTC KTSVATQCDP EEIIVLSDSD
Database document:
This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.