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Q9UER7

- DAXX_HUMAN

UniProt

Q9UER7 - DAXX_HUMAN

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Protein

Death domain-associated protein 6

Gene
DAXX, BING2, DAP6
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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.12 Publications

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
Complete GO annotation...

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. 1 Publication
Mutagenesisi220 – 2201S → A: Abolishes interaction with histones H3 and H4. 1 Publication
Mutagenesisi222 – 2221Y → A or S: Abolishes interaction with histones H3 and H4. 2 Publications
Mutagenesisi222 – 2221Y → E: Abolishes interaction with histone H3.3. 2 Publications
Mutagenesisi225 – 2251E → L: Impairs interaction with histones H3 and H4. 1 Publication
Mutagenesisi229 – 2291K → A or L: Impairs interaction with histones H3 and H4. 1 Publication
Mutagenesisi251 – 2511R → A: Abolishes interaction with histones H3 and H4. 1 Publication
Mutagenesisi317 – 3171F → A: Abolishes interaction with histones H3 and H4. 1 Publication
Mutagenesisi328 – 3281R → A: Abolishes interaction with histones H3 and H4. 1 Publication
Mutagenesisi331 – 3311D → A: Abolishes interaction with histones H3 and H4. 1 Publication
Mutagenesisi630 – 6301K → A: Abolishes sumoylation; when associated with A-631. 1 Publication
Mutagenesisi631 – 6311K → A: Abolishes sumoylation; when associated with A-630. 1 Publication
Mutagenesisi668 – 6681S → A: No translocation to the cytosol upon glucose deprivation. 1 Publication
Mutagenesisi671 – 6711S → A: No effect on cytosol translocation. upon glucose deprivation. 1 Publication
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 – 4591Phosphothreonine By 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.3 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 UL123.27 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
FASP254452EBI-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.
HSPB1P047923EBI-77321,EBI-352682
HSPB1P159913EBI-77321,EBI-1559114From a different organism.
MAP3K5Q996836EBI-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
TP53P0463711EBI-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. 64 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.

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 – 21738 Reviewed predictionAdd
BLAST
Coiled coili358 – 39942 Reviewed predictionAdd
BLAST
Coiled coili430 – 48960 Reviewed predictionAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi391 – 3955Nuclear localization signal Reviewed prediction
Motifi628 – 6347Nuclear localization signal Reviewed prediction

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.

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7575Missing in isoform 3. VSP_045588Add
BLAST
Alternative sequencei696 – 74045SSLCI…LSDSD → PAKNLGRRRSKQDQG in isoform 2. VSP_001270Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti177 – 1771Q → R in AAB66585. 1 Publication
Sequence conflicti263 – 2631R → H in AAC72843. 1 Publication
Sequence conflicti323 – 3231R → W in AAB66585. 1 Publication
Sequence conflicti365 – 3651R → Q in AAB66585. 1 Publication
Sequence conflicti382 – 3821L → S in AAB66585. 1 Publication
Sequence conflicti505 – 5051E → G in BAG64795. 1 Publication
Sequence conflicti647 – 6471S → R in CAB09986. 1 Publication
Sequence conflicti647 – 6471S → R in CAB09989. 1 Publication
Sequence conflicti722 – 7221T → A in CAB09986. 1 Publication
Sequence conflicti722 – 7221T → A in CAB09989. 1 Publication
Sequence conflicti731 – 7322EE → KK in AAC72843. 1 Publication

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. 64 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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 143 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

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