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Q9UER7

- DAXX_HUMAN

UniProt

Q9UER7 - DAXX_HUMAN

Protein

Death domain-associated protein 6

Gene

DAXX

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 2 (01 Nov 2002)
      Previous versions | rss
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    Functioni

    Transcription corepressor known to repress transcriptional potential of several sumoylated transcription factors. Down-regulates basal and activated transcription. Its transcription repressor activity is modulated by recruiting it to subnuclear compartments like the nucleolus or PML/POD/ND10 nuclear bodies through interactions with MCSR1 and PML, respectively. Seems to regulate transcription in PML/POD/ND10 nuclear bodies together with PML and may influence TNFRSF6-dependent apoptosis thereby. Inhibits transcriptional activatiopn of PAX3 and ETS1 through direct protein-protein interactions. Modulates PAX5 activity; the function seems to involve CREBBP. Acts as an adapter protein in a MDM2-DAXX-USP7 complex by regulating the RING-finger E3 ligase MDM2 ubiquitination activity. Under non-stress condition, in association with the deubiquitinating USP7, prevents MDM2 self-ubiquitination and enhances the intrinsic E3 ligase activity of MDM2 towards TP53, thereby promoting TP53 ubiquitination and subsequent proteasomal degradation. Upon DNA damage, its association with MDM2 and USP7 is disrupted, resulting in increased MDM2 autoubiquitination and consequently, MDM2 degradation, which leads to TP53 stabilization. Acts as histone chaperone that facilitates deposition of histone H3.3. Acts as targeting component of the chromatin remodeling complex ATRX:DAXX which has ATP-dependent DNA translocase activity and catalyzes the replication-independent deposition of histone H3.3 in pericentric DNA repeats outside S-phase and telomeres, and the in vitro remodeling of H3.3-containing nucleosomes. Does not affect the ATPase activity of ATRX but alleviates its transcription repression activity. Upopn neuronal activation asociates with regulatory elements of selected immediate early genes where it promotes deposition of histone H3.3 which may be linked to transcriptional induction of these genes. Required for the recruitment of histone H3.3:H4 dimers to PML-nuclear bodies (PML-NBs); the process is independent of ATRX and facilitated by ASF1A; PML-NBs are suggested to function as regulatory sites for the incorporation of newly synthesized histone H3.3 into chromatin. In case of overexpression of centromeric histone variant CENPA (as found in various tumors) is involved in its mislocalization to chromosomes; the ectopic localization involves a heterotypic tetramer containing CENPA, and histones H3.3 and H4 and decreases binding of CTCF to chromatin. Proposed to mediate activation of the JNK pathway and apoptosis via MAP3K5 in response to signaling from TNFRSF6 and TGFBR2. Interaction with HSPB1/HSP27 may prevent interaction with TNFRSF6 and MAP3K5 and block DAXX-mediated apoptosis. In contrast, in lymphoid cells JNC activation and TNFRSF6-mediated apoptosis may not involve DAXX. Shows restriction activity towards human cytomegalovirus (HCMV).11 Publications

    GO - Molecular functioni

    1. androgen receptor binding Source: UniProtKB
    2. enzyme binding Source: UniProtKB
    3. heat shock protein binding Source: UniProtKB
    4. histone binding Source: UniProtKB
    5. p53 binding Source: UniProtKB
    6. protein binding Source: UniProtKB
    7. protein homodimerization activity Source: UniProtKB
    8. protein kinase activator activity Source: ParkinsonsUK-UCL
    9. protein kinase binding Source: ParkinsonsUK-UCL
    10. protein N-terminus binding Source: UniProtKB
    11. receptor signaling protein activity Source: ProtInc
    12. transcription corepressor activity Source: UniProtKB
    13. transcription factor binding Source: UniProtKB
    14. ubiquitin protein ligase binding Source: UniProtKB

    GO - Biological processi

    1. activation of JUN kinase activity Source: ProtInc
    2. androgen receptor signaling pathway Source: UniProtKB
    3. apoptotic process Source: UniProtKB
    4. chromatin remodeling Source: UniProtKB
    5. extrinsic apoptotic signaling pathway via death domain receptors Source: ProtInc
    6. mitotic cytokinesis Source: Ensembl
    7. negative regulation of transcription, DNA-templated Source: UniProtKB
    8. nucleosome assembly Source: UniProtKB
    9. positive regulation of apoptotic signaling pathway Source: Ensembl
    10. positive regulation of neuron death Source: ParkinsonsUK-UCL
    11. positive regulation of protein kinase activity Source: ParkinsonsUK-UCL
    12. positive regulation of protein phosphorylation Source: ParkinsonsUK-UCL
    13. regulation of protein ubiquitination Source: UniProtKB
    14. regulation of transcription, DNA-templated Source: MGI
    15. transcription, DNA-templated Source: UniProtKB-KW
    16. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chaperone, Chromatin regulator, Repressor

    Keywords - Biological processi

    Apoptosis, Host-virus interaction, Transcription, Transcription regulation

    Enzyme and pathway databases

    SignaLinkiQ9UER7.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Death domain-associated protein 6
    Alternative name(s):
    Daxx
    Short name:
    hDaxx
    ETS1-associated protein 1
    Short name:
    EAP1
    Fas death domain-associated protein
    Gene namesi
    Name:DAXX
    Synonyms:BING2, DAP6
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:2681. DAXX.

    Subcellular locationi

    Cytoplasm. Nucleusnucleoplasm. NucleusPML body. Nucleusnucleolus. Chromosomecentromere
    Note: Dispersed throughout the nucleoplasm, in PML/POD/ND10 nuclear bodies, and in nucleoli. Colocalizes with histone H3.3, ATRX, HIRA and ASF1A at PML-nuclear bodies. Colocalizes with a subset of interphase centromeres, but is absent from mitotic centromeres. Detected in cytoplasmic punctate structures. Translocates from the nucleus to the cytoplasm upon glucose deprivation or oxidative stress. Colocalizes with RASSF1 in the nucleus. Colocalizes with USP7 in nucleoplasma with accumulation in speckled structures.

    GO - Cellular componenti

    1. chromosome, centromeric region Source: UniProtKB-SubCell
    2. cytoplasm Source: UniProtKB
    3. cytosol Source: UniProtKB
    4. heterochromatin Source: Ensembl
    5. nucleolus Source: UniProtKB-SubCell
    6. nucleus Source: UniProtKB
    7. PML body Source: UniProtKB
    8. SWI/SNF superfamily-type complex Source: UniProtKB

    Keywords - Cellular componenti

    Centromere, Chromosome, Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi206 – 2061Q → L: Impairs interaction with histones H3 and H4. 2 Publications
    Mutagenesisi220 – 2201S → A: Abolishes interaction with histones H3 and H4. 2 Publications
    Mutagenesisi222 – 2221Y → A or S: Abolishes interaction with histones H3 and H4. 3 Publications
    Mutagenesisi222 – 2221Y → E: Abolishes interaction with histone H3.3. 3 Publications
    Mutagenesisi225 – 2251E → L: Impairs interaction with histones H3 and H4. 2 Publications
    Mutagenesisi229 – 2291K → A or L: Impairs interaction with histones H3 and H4. 2 Publications
    Mutagenesisi251 – 2511R → A: Abolishes interaction with histones H3 and H4. 2 Publications
    Mutagenesisi317 – 3171F → A: Abolishes interaction with histones H3 and H4. 2 Publications
    Mutagenesisi328 – 3281R → A: Abolishes interaction with histones H3 and H4. 2 Publications
    Mutagenesisi331 – 3311D → A: Abolishes interaction with histones H3 and H4. 2 Publications
    Mutagenesisi630 – 6301K → A: Abolishes sumoylation; when associated with A-631. 2 Publications
    Mutagenesisi631 – 6311K → A: Abolishes sumoylation; when associated with A-630. 2 Publications
    Mutagenesisi668 – 6681S → A: No translocation to the cytosol upon glucose deprivation. 2 Publications
    Mutagenesisi671 – 6711S → A: No effect on cytosol translocation. upon glucose deprivation. 2 Publications
    Mutagenesisi733 – 7408Missing: Abolishes sumoylation. 1 Publication

    Organism-specific databases

    PharmGKBiPA27148.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 740740Death domain-associated protein 6PRO_0000151258Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei178 – 1781Phosphoserine1 Publication
    Modified residuei213 – 2131Phosphoserine1 Publication
    Modified residuei459 – 4591PhosphothreonineBy similarity
    Modified residuei495 – 4951Phosphoserine3 Publications
    Modified residuei512 – 5121N6-acetyllysine1 Publication
    Cross-linki630 – 630Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)
    Cross-linki631 – 631Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)
    Modified residuei668 – 6681Phosphoserine2 Publications
    Modified residuei671 – 6711Phosphoserine2 Publications
    Modified residuei688 – 6881Phosphoserine1 Publication
    Modified residuei702 – 7021Phosphoserine6 Publications
    Modified residuei737 – 7371Phosphoserine3 Publications
    Modified residuei739 – 7391Phosphoserine3 Publications

    Post-translational modificationi

    Sumoylated with SUMO1 on multiple lysine residues.3 Publications
    Phosphorylated by HIPK1 upon glucose deprivation.9 Publications
    Polyubiquitinated; which is promoted by CUL3 and SPOP and results in proteasomal degradation. Ubiquitinated by MDM2; inducing its degradation. Deubiquitinated by USP7; leading to stabilize it.2 Publications

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9UER7.
    PaxDbiQ9UER7.
    PeptideAtlasiQ9UER7.
    PRIDEiQ9UER7.

    PTM databases

    PhosphoSiteiQ9UER7.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Inductioni

    Upon mitogenic stimulation by concanavalin-A.

    Gene expression databases

    ArrayExpressiQ9UER7.
    BgeeiQ9UER7.
    CleanExiHS_DAXX.
    GenevestigatoriQ9UER7.

    Organism-specific databases

    HPAiCAB002224.
    CAB025546.
    HPA008736.
    HPA008797.

    Interactioni

    Subunit structurei

    Homomultimer. Interacts (via C-terminus) with TNFRSF6 (via death domain). Interacts with PAX5, SLC2A4/GLUT4, MAP3K5, TGFBR2, phosphorylated dimeric HSPB1/HSP27, CENPC, ETS1, sumoylated PML, UBE2I, MCRS1 and TP53. Interacts (via N-terminus) with HIPK2 and HIPK3. Interacts with HIPK1, which induces translocation from PML/POD/ND10 nuclear bodies to chromatin and enhances association with HDAC1. Interacts (non-phosphorylated) with PAX3, PAX7, DEK, HDAC1, HDAC2, HDAC3, acetylated histone H4 and histones H2A, H2B, H3, H3.3 and H4. Interacts with SPOP; mediating CUL3-dependent proteosomal degradation. Interacts with CBP; the interaction is dependent the sumoylation of CBP and suppresses CBP transcriptional activity via recruitment of HDAC2 directly in the complex with TP53 and HIPK2. Interacts with AXIN1; the interaction stimulates the interaction of DAXX with TP53, stimulates 'Ser-46' phosphorylation of TP53 on and induces cell death on UV irradiation. Interacts with MDM2; the interaction is direct. Interacts with USP7; the interaction is direct and independent of MDM2 and TP53. Part of a complex with DAXX, MDM2 and USP7 under non-stress conditions. Interacts (via N-terminus) with RASSF1 (via C-terminus); the interaction is independent of MDM2 and TP53; RASSF1 isoform A disrupts interactions among MDM2, DAXX and USP7, thus contributing to the efficient activation of TP53 by promoting MDM2 self-ubiquitination in cell-cycle checkpoint control in response to DNA damage. Interacts with ATRX to form the chromatin remodeling complex ATRX:DAXX. Interacts with human cytomegalovirus/HHV-5 tegument phosphoprotein pp71 and protein UL123.28 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    P032434EBI-77321,EBI-1561361From a different organism.
    AIREO439185EBI-77321,EBI-1753081
    ARP102755EBI-77321,EBI-608057
    ATRXP461005EBI-77321,EBI-396461
    CDKN2AQ8N7268EBI-77321,EBI-625922
    CREBBPQ927932EBI-77321,EBI-81215
    E1BP032444EBI-77321,EBI-1561155From a different organism.
    ETS1P14921-13EBI-287635,EBI-913224
    ETS1P14921-22EBI-287635,EBI-913228
    FASP254453EBI-77321,EBI-494743
    FasP254464EBI-77321,EBI-296206From a different organism.
    FTH1P027945EBI-77321,EBI-713259
    HDAC1Q135472EBI-77321,EBI-301834
    HDAC2Q927692EBI-77321,EBI-301821
    Hipk1O889043EBI-77321,EBI-692945From a different organism.
    HSPB1P047924EBI-77321,EBI-352682
    HSPB1P159913EBI-77321,EBI-1559114From a different organism.
    MAP3K5Q996837EBI-77321,EBI-476263
    MCRS1Q96EZ88EBI-77321,EBI-348259
    MDM2Q0098718EBI-77321,EBI-389668
    PARK7Q994973EBI-77321,EBI-1164361
    Pax5Q026504EBI-77321,EBI-296260From a different organism.
    PMLP295906EBI-77321,EBI-295890
    RASSF1Q9NS236EBI-77321,EBI-367363
    RASSF1Q9NS23-45EBI-77321,EBI-438710
    Ripk3Q9QZL02EBI-77321,EBI-2367423From a different organism.
    SPOPO437915EBI-77321,EBI-743549
    STAT3P407634EBI-77321,EBI-518675
    SUMO1P631655EBI-77321,EBI-80140
    TCF7L2Q9NQB05EBI-77321,EBI-924724
    TGFBR2P371732EBI-77321,EBI-296151
    TP53P0463712EBI-77321,EBI-366083
    TSG101Q998164EBI-77321,EBI-346882
    UBCP0CG482EBI-77321,EBI-3390054
    USP7Q9300913EBI-77321,EBI-302474
    WHSC1L1Q9BZ952EBI-77321,EBI-3390132

    Protein-protein interaction databases

    BioGridi107985. 103 interactions.
    DIPiDIP-27628N.
    IntActiQ9UER7. 65 interactions.
    MINTiMINT-122943.
    STRINGi9606.ENSP00000266000.

    Structurei

    Secondary structure

    1
    740
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi60 – 7718
    Turni78 – 803
    Helixi84 – 9310
    Helixi97 – 1004
    Helixi103 – 11816
    Helixi120 – 1223
    Helixi123 – 13614
    Beta strandi138 – 1403
    Helixi185 – 20622
    Helixi214 – 2163
    Helixi221 – 24222
    Helixi252 – 2543
    Helixi265 – 27511
    Beta strandi278 – 2803
    Helixi286 – 29914
    Helixi306 – 33328
    Helixi339 – 3413
    Helixi346 – 3483
    Helixi350 – 3534
    Helixi355 – 38430

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2KQSNMR-B721-740[»]
    2KZSNMR-A55-144[»]
    2KZUNMR-A55-144[»]
    4H9NX-ray1.95C178-389[»]
    4H9OX-ray2.05C178-389[»]
    4H9PX-ray2.20C178-389[»]
    4H9QX-ray1.95C178-389[»]
    4H9RX-ray2.20C178-389[»]
    4H9SX-ray2.60E/F183-398[»]
    4HGAX-ray2.80A184-390[»]
    DisProtiDP00707.
    ProteinModelPortaliQ9UER7.
    SMRiQ9UER7. Positions 52-144, 182-386.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UER7.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 160160Necessary for interaction with USP7 and ATRXAdd
    BLAST
    Regioni183 – 417235Interaction with histone H3.3Add
    BLAST
    Regioni347 – 570224Necessary for interaction with USP7Add
    BLAST
    Regioni501 – 625125Interaction with MAP3K5Add
    BLAST
    Regioni626 – 740115Interaction with SPOPAdd
    BLAST
    Regioni733 – 7408Sumo interaction motif (SIM)

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili180 – 21738Sequence AnalysisAdd
    BLAST
    Coiled coili358 – 39942Sequence AnalysisAdd
    BLAST
    Coiled coili430 – 48960Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi391 – 3955Nuclear localization signalSequence Analysis
    Motifi628 – 6347Nuclear localization signalSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi11 – 166Poly-Asp
    Compositional biasi434 – 572139Asp/Glu-rich (acidic)Add
    BLAST

    Domaini

    The Sumo interaction motif mediates Sumo binding, and is required both for sumoylation and binding to sumoylated targets.

    Sequence similaritiesi

    Belongs to the DAXX family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG39676.
    HOGENOMiHOG000112148.
    HOVERGENiHBG031495.
    InParanoidiQ9UER7.
    KOiK02308.
    OMAiELCKTQT.
    PhylomeDBiQ9UER7.
    TreeFamiTF325803.

    Family and domain databases

    InterProiIPR005012. Daxx.
    [Graphical view]
    PANTHERiPTHR12766. PTHR12766. 1 hit.
    PfamiPF03344. Daxx. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UER7-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MATANSIIVL DDDDEDEAAA QPGPSHPLPN AASPGAEAPS SSEPHGARGS    50
    SSSGGKKCYK LENEKLFEEF LELCKMQTAD HPEVVPFLYN RQQRAHSLFL 100
    ASAEFCNILS RVLSRARSRP AKLYVYINEL CTVLKAHSAK KKLNLAPAAT 150
    TSNEPSGNNP PTHLSLDPTN AENTASQSPR TRGSRRQIQR LEQLLALYVA 200
    EIRRLQEKEL DLSELDDPDS AYLQEARLKR KLIRLFGRLC ELKDCSSLTG 250
    RVIEQRIPYR GTRYPEVNRR IERLINKPGP DTFPDYGDVL RAVEKAAARH 300
    SLGLPRQQLQ LMAQDAFRDV GIRLQERRHL DLIYNFGCHL TDDYRPGVDP 350
    ALSDPVLARR LRENRSLAMS RLDEVISKYA MLQDKSEEGE RKKRRARLQG 400
    TSSHSADTPE ASLDSGEGPS GMASQGCPSA SRAETDDEDD EESDEEEEEE 450
    EEEEEEEATD SEEEEDLEQM QEGQEDDEEE DEEEEAAAGK DGDKSPMSSL 500
    QISNEKNLEP GKQISRSSGE QQNKGRIVSP SLLSEEPLAP SSIDAESNGE 550
    QPEELTLEEE SPVSQLFELE IEALPLDTPS SVETDISSSR KQSEEPFTTV 600
    LENGAGMVSS TSFNGGVSPH NWGDSGPPCK KSRKEKKQTG SGPLGNSYVE 650
    RQRSVHEKNG KKICTLPSPP SPLASLAPVA DSSTRVDSPS HGLVTSSLCI 700
    PSPARLSQTP HSQPPRPGTC KTSVATQCDP EEIIVLSDSD 740
    Length:740
    Mass (Da):81,373
    Last modified:November 1, 2002 - v2
    Checksum:i1B309ADDAA878040
    GO
    Isoform 2 (identifier: Q9UER7-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         696-740: SSLCIPSPARLSQTPHSQPPRPGTCKTSVATQCDPEEIIVLSDSD → PAKNLGRRRSKQDQG

    Note: No experimental confirmation available.

    Show »
    Length:710
    Mass (Da):78,333
    Checksum:i47E099676EB7315C
    GO
    Isoform 3 (identifier: Q9UER7-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-75: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:665
    Mass (Da):73,589
    Checksum:i11AF08F83A462073
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti177 – 1771Q → R in AAB66585. (PubMed:9407001)Curated
    Sequence conflicti263 – 2631R → H in AAC72843. (PubMed:10698492)Curated
    Sequence conflicti323 – 3231R → W in AAB66585. (PubMed:9407001)Curated
    Sequence conflicti365 – 3651R → Q in AAB66585. (PubMed:9407001)Curated
    Sequence conflicti382 – 3821L → S in AAB66585. (PubMed:9407001)Curated
    Sequence conflicti505 – 5051E → G in BAG64795. (PubMed:14702039)Curated
    Sequence conflicti647 – 6471S → R in CAB09986. (PubMed:14574404)Curated
    Sequence conflicti647 – 6471S → R in CAB09989. (PubMed:14574404)Curated
    Sequence conflicti722 – 7221T → A in CAB09986. (PubMed:14574404)Curated
    Sequence conflicti722 – 7221T → A in CAB09989. (PubMed:14574404)Curated
    Sequence conflicti731 – 7322EE → KK in AAC72843. (PubMed:10698492)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 7575Missing in isoform 3. 1 PublicationVSP_045588Add
    BLAST
    Alternative sequencei696 – 74045SSLCI…LSDSD → PAKNLGRRRSKQDQG in isoform 2. 1 PublicationVSP_001270Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF039136 mRNA. Translation: AAB92671.1.
    AF006041 mRNA. Translation: AAB63043.1.
    AF015956 mRNA. Translation: AAB66585.2.
    AF050179 mRNA. Translation: AAC39853.1.
    AF097742 mRNA. Translation: AAC72843.1.
    AB015051 mRNA. Translation: BAA34295.1.
    AK303854 mRNA. Translation: BAG64795.1.
    CR457085 mRNA. Translation: CAG33366.1.
    AL662827 Genomic DNA. Translation: CAI17527.1.
    AL662820 Genomic DNA. Translation: CAI18124.1.
    BX248088 Genomic DNA. Translation: CAI41788.1.
    CR759793 Genomic DNA. No translation available.
    CR759817 Genomic DNA. Translation: CAQ08035.1.
    CR759786 Genomic DNA. Translation: CAQ08265.1.
    Z97183, Z97184 Genomic DNA. Translation: CAB09986.2.
    Z97184, Z97183 Genomic DNA. Translation: CAB09989.2.
    CH471081 Genomic DNA. Translation: EAX03722.1.
    BC000220 mRNA. Translation: AAH00220.1.
    BC109073 mRNA. Translation: AAI09074.1.
    BC109074 mRNA. Translation: AAI09075.1.
    CCDSiCCDS4776.1. [Q9UER7-1]
    CCDS59008.1. [Q9UER7-3]
    PIRiT03847.
    RefSeqiNP_001135441.1. NM_001141969.1. [Q9UER7-1]
    NP_001241646.1. NM_001254717.1. [Q9UER7-3]
    NP_001341.1. NM_001350.4. [Q9UER7-1]
    UniGeneiHs.336916.

    Genome annotation databases

    EnsembliENST00000266000; ENSP00000266000; ENSG00000204209. [Q9UER7-1]
    ENST00000374542; ENSP00000363668; ENSG00000204209. [Q9UER7-1]
    ENST00000383062; ENSP00000372539; ENSG00000206206. [Q9UER7-1]
    ENST00000383194; ENSP00000372681; ENSG00000206279. [Q9UER7-1]
    ENST00000399060; ENSP00000382014; ENSG00000206206. [Q9UER7-1]
    ENST00000399344; ENSP00000382281; ENSG00000206279. [Q9UER7-1]
    ENST00000414083; ENSP00000396876; ENSG00000204209. [Q9UER7-3]
    ENST00000433482; ENSP00000404623; ENSG00000231617. [Q9UER7-1]
    ENST00000436311; ENSP00000404376; ENSG00000227046. [Q9UER7-1]
    ENST00000445009; ENSP00000394108; ENSG00000231617. [Q9UER7-1]
    ENST00000455860; ENSP00000410772; ENSG00000227046. [Q9UER7-1]
    GeneIDi1616.
    KEGGihsa:1616.
    UCSCiuc003oec.3. human. [Q9UER7-1]

    Polymorphism databases

    DMDMi24636785.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF039136 mRNA. Translation: AAB92671.1 .
    AF006041 mRNA. Translation: AAB63043.1 .
    AF015956 mRNA. Translation: AAB66585.2 .
    AF050179 mRNA. Translation: AAC39853.1 .
    AF097742 mRNA. Translation: AAC72843.1 .
    AB015051 mRNA. Translation: BAA34295.1 .
    AK303854 mRNA. Translation: BAG64795.1 .
    CR457085 mRNA. Translation: CAG33366.1 .
    AL662827 Genomic DNA. Translation: CAI17527.1 .
    AL662820 Genomic DNA. Translation: CAI18124.1 .
    BX248088 Genomic DNA. Translation: CAI41788.1 .
    CR759793 Genomic DNA. No translation available.
    CR759817 Genomic DNA. Translation: CAQ08035.1 .
    CR759786 Genomic DNA. Translation: CAQ08265.1 .
    Z97183 , Z97184 Genomic DNA. Translation: CAB09986.2 .
    Z97184 , Z97183 Genomic DNA. Translation: CAB09989.2 .
    CH471081 Genomic DNA. Translation: EAX03722.1 .
    BC000220 mRNA. Translation: AAH00220.1 .
    BC109073 mRNA. Translation: AAI09074.1 .
    BC109074 mRNA. Translation: AAI09075.1 .
    CCDSi CCDS4776.1. [Q9UER7-1 ]
    CCDS59008.1. [Q9UER7-3 ]
    PIRi T03847.
    RefSeqi NP_001135441.1. NM_001141969.1. [Q9UER7-1 ]
    NP_001241646.1. NM_001254717.1. [Q9UER7-3 ]
    NP_001341.1. NM_001350.4. [Q9UER7-1 ]
    UniGenei Hs.336916.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2KQS NMR - B 721-740 [» ]
    2KZS NMR - A 55-144 [» ]
    2KZU NMR - A 55-144 [» ]
    4H9N X-ray 1.95 C 178-389 [» ]
    4H9O X-ray 2.05 C 178-389 [» ]
    4H9P X-ray 2.20 C 178-389 [» ]
    4H9Q X-ray 1.95 C 178-389 [» ]
    4H9R X-ray 2.20 C 178-389 [» ]
    4H9S X-ray 2.60 E/F 183-398 [» ]
    4HGA X-ray 2.80 A 184-390 [» ]
    DisProti DP00707.
    ProteinModelPortali Q9UER7.
    SMRi Q9UER7. Positions 52-144, 182-386.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107985. 103 interactions.
    DIPi DIP-27628N.
    IntActi Q9UER7. 65 interactions.
    MINTi MINT-122943.
    STRINGi 9606.ENSP00000266000.

    PTM databases

    PhosphoSitei Q9UER7.

    Polymorphism databases

    DMDMi 24636785.

    Proteomic databases

    MaxQBi Q9UER7.
    PaxDbi Q9UER7.
    PeptideAtlasi Q9UER7.
    PRIDEi Q9UER7.

    Protocols and materials databases

    DNASUi 1616.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000266000 ; ENSP00000266000 ; ENSG00000204209 . [Q9UER7-1 ]
    ENST00000374542 ; ENSP00000363668 ; ENSG00000204209 . [Q9UER7-1 ]
    ENST00000383062 ; ENSP00000372539 ; ENSG00000206206 . [Q9UER7-1 ]
    ENST00000383194 ; ENSP00000372681 ; ENSG00000206279 . [Q9UER7-1 ]
    ENST00000399060 ; ENSP00000382014 ; ENSG00000206206 . [Q9UER7-1 ]
    ENST00000399344 ; ENSP00000382281 ; ENSG00000206279 . [Q9UER7-1 ]
    ENST00000414083 ; ENSP00000396876 ; ENSG00000204209 . [Q9UER7-3 ]
    ENST00000433482 ; ENSP00000404623 ; ENSG00000231617 . [Q9UER7-1 ]
    ENST00000436311 ; ENSP00000404376 ; ENSG00000227046 . [Q9UER7-1 ]
    ENST00000445009 ; ENSP00000394108 ; ENSG00000231617 . [Q9UER7-1 ]
    ENST00000455860 ; ENSP00000410772 ; ENSG00000227046 . [Q9UER7-1 ]
    GeneIDi 1616.
    KEGGi hsa:1616.
    UCSCi uc003oec.3. human. [Q9UER7-1 ]

    Organism-specific databases

    CTDi 1616.
    GeneCardsi GC06M033286.
    GC06Mj33207.
    GC06Mk33264.
    GC06Mm33456.
    GC06Mn33215.
    HGNCi HGNC:2681. DAXX.
    HPAi CAB002224.
    CAB025546.
    HPA008736.
    HPA008797.
    MIMi 603186. gene.
    neXtProti NX_Q9UER7.
    PharmGKBi PA27148.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG39676.
    HOGENOMi HOG000112148.
    HOVERGENi HBG031495.
    InParanoidi Q9UER7.
    KOi K02308.
    OMAi ELCKTQT.
    PhylomeDBi Q9UER7.
    TreeFami TF325803.

    Enzyme and pathway databases

    SignaLinki Q9UER7.

    Miscellaneous databases

    ChiTaRSi DAXX. human.
    EvolutionaryTracei Q9UER7.
    GeneWikii Death-associated_protein_6.
    GenomeRNAii 1616.
    NextBioi 6638.
    PROi Q9UER7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UER7.
    Bgeei Q9UER7.
    CleanExi HS_DAXX.
    Genevestigatori Q9UER7.

    Family and domain databases

    InterProi IPR005012. Daxx.
    [Graphical view ]
    PANTHERi PTHR12766. PTHR12766. 1 hit.
    Pfami PF03344. Daxx. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Daxx, a novel Fas-binding protein that activates JNK and apoptosis."
      Yang X., Khosravi-Far R., Chang H.Y., Baltimore D.
      Cell 89:1067-1076(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Cloning and expression of primate Daxx cDNAs and mapping of the human gene to chromosome 6p21.3 in the MHC region."
      Kiriakidou M., Driscoll D.A., Lopez-Guisa J.M., Strauss J.F. III
      DNA Cell Biol. 16:1289-1298(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION.
      Tissue: Placenta.
    3. "Interphase-specific association of intrinsic centromere protein CENP-C with HDaxx, a death domain-binding protein implicated in Fas-mediated cell death."
      Pluta A.F., Earnshaw W.C., Goldberg I.G.
      J. Cell Sci. 111:2029-2041(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH CENPC, SUBCELLULAR LOCATION.
      Tissue: Cervix carcinoma.
    4. "TAPASIN, DAXX, RGL2, HKE2 and four new genes (BING 1, 3 to 5) form a dense cluster at the centromeric end of the MHC."
      Herberg J.A., Beck S., Trowsdale J.
      J. Mol. Biol. 277:839-857(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
    5. "EAP1/Daxx interacts with ETS1 and represses transcriptional activation of ETS1 target genes."
      Li R., Pei H., Watson D.K., Papas T.S.
      Oncogene 19:745-753(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: T-cell.
    6. Usui T.
      Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    7. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Trachea.
    8. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    9. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    11. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 334-740 (ISOFORM 2).
      Tissue: Eye.
    12. "The Pax3-FKHR oncoprotein is unresponsive to the Pax3-associated repressor hDaxx."
      Hollenbach A.D., Sublett J.E., McPherson C.J., Grosveld G.
      EMBO J. 18:3702-3711(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PAX3 AND PAX7, PHOSPHORYLATION.
    13. "Promyelocytic leukemia protein (PML) and Daxx participate in a novel nuclear pathway for apoptosis."
      Zhong S., Salomoni P., Ronchetti S., Guo A., Ruggero D., Pandolfi P.P.
      J. Exp. Med. 191:631-640(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PML.
    14. "Sequestration and inhibition of Daxx-mediated transcriptional repression by PML."
      Li H., Leo C., Zhu J., Wu X., O'Neil J., Park E.-J., Chen J.D.
      Mol. Cell. Biol. 20:1784-1796(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SUMOYLATED PML; HDAC1; HDAC2 AND HDAC3, SUBCELLULAR LOCATION.
    15. "Inhibition of Daxx-mediated apoptosis by heat shock protein 27."
      Charette S.J., Lavoie J.N., Lambert H., Landry J.
      Mol. Cell. Biol. 20:7602-7612(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HSPB1.
    16. "Apoptosis signal-regulating kinase 1 controls the proapoptotic function of death-associated protein (Daxx) in the cytoplasm."
      Ko Y.-G., Kang Y.-S., Park H., Seol W., Kim J., Kim T., Park H.-S., Choi E.-J., Kim S.
      J. Biol. Chem. 276:39103-39106(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAP3K5, SUBCELLULAR LOCATION.
    17. "TGF-beta-induced apoptosis is mediated by the adapter protein Daxx that facilitates JNK activation."
      Perlman R., Schiemann W.P., Brooks M.W., Lodish H.F., Weinberg R.A.
      Nat. Cell Biol. 3:708-714(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TGFBR2.
    18. "Modification of Daxx by small ubiquitin-related modifier-1."
      Jang M.-S., Ryu S.-W., Kim E.
      Biochem. Biophys. Res. Commun. 295:495-500(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION, MUTAGENESIS OF LYS-630 AND LYS-631.
    19. "The insulin-sensitive glucose transporter, GLUT4, interacts physically with Daxx. Two proteins with capacity to bind Ubc9 and conjugated to SUMO1."
      Lalioti V.S., Vergarajauregui S., Pulido D., Sandoval I.V.
      J. Biol. Chem. 277:19783-19791(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SLC2A4 AND UBE2I, SUMOYLATION, SUBCELLULAR LOCATION.
    20. "Essential role of the 58-kDa microspherule protein in the modulation of Daxx-dependent transcriptional repression as revealed by nucleolar sequestration."
      Lin D.-Y., Shih H.-M.
      J. Biol. Chem. 277:25446-25456(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MCRS1.
    21. "Daxx and histone deacetylase II associate with chromatin through an interaction with core histones and the chromatin-associated protein Dek."
      Hollenbach A.D., McPherson C.J., Mientjes E.J., Iyengar R., Grosveld G.
      J. Cell Sci. 115:3319-3330(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION, INTERACTION WITH HDAC2; HISTONES AND DEK.
    22. "HIPK2 regulates transforming growth factor-beta-induced c-Jun NH(2)-terminal kinase activation and apoptosis in human hepatoma cells."
      Hofmann T.G., Stollberg N., Schmitz M.L., Will H.
      Cancer Res. 63:8271-8277(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HIPK2.
    23. "Role of the ASK1-SEK1-JNK1-HIPK1 signal in Daxx trafficking and ASK1 oligomerization."
      Song J.J., Lee Y.J.
      J. Biol. Chem. 278:47245-47252(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: OLIGOMERIZATION, SUBCELLULAR LOCATION, INTERACTION WITH MAP3K5, MUTAGENESIS OF SER-668 AND SER-671, PHOSPHORYLATION AT SER-668.
    24. "Homeodomain-interacting protein kinase 1 modulates Daxx localization, phosphorylation, and transcriptional activity."
      Ecsedy J.A., Michaelson J.S., Leder P.
      Mol. Cell. Biol. 23:950-960(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HIPK1.
    25. "The ATRX syndrome protein forms a chromatin-remodeling complex with Daxx and localizes in promyelocytic leukemia nuclear bodies."
      Xue Y., Gibbons R., Yan Z., Yang D., McDowell T.L., Sechi S., Qin J., Zhou S., Higgs D., Wang W.
      Proc. Natl. Acad. Sci. U.S.A. 100:10635-10640(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ATRX, SUBCELLULAR LOCATION.
    26. "Daxx-mediated transcriptional repression of MMP1 gene is reversed by SPOP."
      La M., Kim K., Park J., Won J., Lee J.-H., Fu Y.M., Meadows G.G., Joe C.O.
      Biochem. Biophys. Res. Commun. 320:760-765(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SPOP.
    27. "A novel transcription regulatory complex containing death domain-associated protein and the ATR-X syndrome protein."
      Tang J., Wu S., Liu H., Stratt R., Barak O.G., Shiekhattar R., Picketts D.J., Yang X.
      J. Biol. Chem. 279:20369-20377(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ATRX, SUBCELLULAR LOCATION.
    28. "Negative regulation of p53 functions by Daxx and the involvement of MDM2."
      Zhao L.Y., Liu J., Sidhu G.S., Niu Y., Liu Y., Wang R., Liao D.
      J. Biol. Chem. 279:50566-50579(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MDM2 AND TP53.
    29. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    30. "BTB domain-containing speckle-type POZ protein (SPOP) serves as an adaptor of Daxx for ubiquitination by Cul3-based ubiquitin ligase."
      Kwon J.E., La M., Oh K.H., Oh Y.M., Kim G.R., Seol J.H., Baek S.H., Chiba T., Tanaka K., Bang O.S., Joe C.O., Chung C.H.
      J. Biol. Chem. 281:12664-12672(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH CUL3 AND SPOP, UBIQUITINATION.
    31. "Role of SUMO-interacting motif in Daxx SUMO modification, subnuclear localization, and repression of sumoylated transcription factors."
      Lin D.Y., Huang Y.S., Jeng J.C., Kuo H.Y., Chang C.C., Chao T.T., Ho C.C., Chen Y.C., Lin T.P., Fang H.I., Hung C.C., Suen C.S., Hwang M.J., Chang K.S., Maul G.G., Shih H.M.
      Mol. Cell 24:341-354(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, SUMOYLATION, SUMO INTERACTION MOTIF, MUTAGENESIS OF 733-ILE--ASP-740.
    32. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-702, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    33. Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH MDM2 AND USP7, INTERACTION WITH MDM2; TP53 AND USP7, SUBCELLULAR LOCATION.
    34. "Daxx cooperates with the Axin/HIPK2/p53 complex to induce cell death."
      Li Q., Wang X., Wu X., Rui Y., Liu W., Wang J., Wang X., Liou Y.C., Ye Z., Lin S.C.
      Cancer Res. 67:66-74(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AXIN1.
    35. "The tumour suppressor RASSF1A promotes MDM2 self-ubiquitination by disrupting the MDM2-DAXX-HAUSP complex."
      Song M.S., Song S.J., Kim S.Y., Oh H.J., Lim D.S.
      EMBO J. 27:1863-1874(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH MDM2; RASSF1 AND USP7, INTERACTION WITH RASSF1; USP7 AND MDM2, SUBCELLULAR LOCATION.
    36. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-671 AND SER-702, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    37. "Nuclear domain 10 components promyelocytic leukemia protein and hDaxx independently contribute to an intrinsic antiviral defense against human cytomegalovirus infection."
      Tavalai N., Papior P., Rechter S., Stamminger T.
      J. Virol. 82:126-137(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN HCMV RESTRICTION.
    38. "Human cytomegalovirus protein pp71 displaces the chromatin-associated factor ATRX from nuclear domain 10 at early stages of infection."
      Lukashchuk V., McFarlane S., Everett R.D., Preston C.M.
      J. Virol. 82:12543-12554(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HCMV PP71.
    39. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178; SER-213; SER-495; SER-668; SER-671; SER-688; SER-702; SER-737 AND SER-739, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    40. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    41. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-702; SER-737 AND SER-739, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    42. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-512, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    43. "Daxx is reciprocally regulated by Mdm2 and Hausp."
      Tang J., Qu L., Pang M., Yang X.
      Biochem. Biophys. Res. Commun. 393:542-545(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION, DEUBIQUITINATION BY USP7.
    44. "The death-associated protein DAXX is a novel histone chaperone involved in the replication-independent deposition of H3.3."
      Drane P., Ouararhni K., Depaux A., Shuaib M., Hamiche A.
      Genes Dev. 24:1253-1265(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS HISTONE CHAPERONE, FUNCTION OF THE ATRX:DAXX COMPLEX, INTERACTION WITH HISTONE H3.3.
    45. "Human cytomegalovirus IE72 protein interacts with the transcriptional repressor hDaxx to regulate LUNA gene expression during lytic infection."
      Reeves M., Woodhall D., Compton T., Sinclair J.
      J. Virol. 84:7185-7194(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HHV-5 PROTEIN UL123.
    46. "Daxx is an H3.3-specific histone chaperone and cooperates with ATRX in replication-independent chromatin assembly at telomeres."
      Lewis P.W., Elsaesser S.J., Noh K.M., Stadler S.C., Allis C.D.
      Proc. Natl. Acad. Sci. U.S.A. 107:14075-14080(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS HISTONE H3.3 CHAPERONE, INTERACTION WITH HISTONE H3.3.
    47. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495; SER-702; SER-737 AND SER-739, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    48. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    49. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495 AND SER-702, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    50. "DAXX-dependent supply of soluble (H3.3-H4) dimers to PML bodies pending deposition into chromatin."
      Delbarre E., Ivanauskiene K., Kuntziger T., Collas P.
      Genome Res. 23:440-451(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELULAR LOCATION.
    51. "Dynamics of histone H3.3 deposition in proliferating and senescent cells reveals a DAXX-dependent targeting to PML-NBs important for pericentromeric heterochromatin organization."
      Corpet A., Olbrich T., Gwerder M., Fink D., Stucki M.
      Cell Cycle 13:249-267(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    52. "Mislocalization of the centromeric histone variant CenH3/CENP-A in human cells depends on the chaperone DAXX."
      Lacoste N., Woolfe A., Tachiwana H., Garea A.V., Barth T., Cantaloube S., Kurumizaka H., Imhof A., Almouzni G.
      Mol. Cell 53:631-644(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    53. "Structural characterization of the DAXX N-terminal helical bundle domain and its complex with Rassf1C."
      Escobar-Cabrera E., Lau D.K., Giovinazzi S., Ishov A.M., McIntosh L.P.
      Structure 18:1642-1653(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 55-144 IN COMPLEX WITH RASSF1, INTERACTION WITH RASSF1.
    54. "NMR chemical shift assignments of a complex between SUMO-1 and SIM peptide derived from the C-terminus of Daxx."
      Naik M.T., Chang C.C., Naik N.M., Kung C.C., Shih H.M., Huang T.H.
      Biomol. NMR. Assign. 5:75-77(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 721-740.
    55. "Structure of the variant histone H3.3-H4 heterodimer in complex with its chaperone DAXX."
      Liu C.P., Xiong C., Wang M., Yu Z., Yang N., Chen P., Zhang Z., Li G., Xu R.M.
      Nat. Struct. Mol. Biol. 19:1287-1292(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 184-390 IN COMPLEX WITH HISTONE H3.3/H4 DIMER, MUTAGENESIS OF TYR-222.
    56. "DAXX envelops a histone H3.3-H4 dimer for H3.3-specific recognition."
      Elsasser S.J., Huang H., Lewis P.W., Chin J.W., Allis C.D., Patel D.J.
      Nature 491:560-565(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 178-389 IN COMPLEX WITH HISTONE H3.3/H4 DIMER, MUTAGENESIS OF GLN-206; SER-220; TYR-222; GLU-225; LYS-229; ARG-251; PHE-317; ARG-328 AND ASP-331.

    Entry informationi

    Entry nameiDAXX_HUMAN
    AccessioniPrimary (citable) accession number: Q9UER7
    Secondary accession number(s): B4E1I3
    , F5H082, O14747, O15141, O15208, Q5STK9, Q9BWI3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 2002
    Last sequence update: November 1, 2002
    Last modified: October 1, 2014
    This is version 144 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3