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Protein

Death domain-associated protein 6

Gene

DAXX

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 activation 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. Upon neuronal activation associates 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

  • androgen receptor binding Source: UniProtKB
  • enzyme binding Source: UniProtKB
  • heat shock protein binding Source: UniProtKB
  • histone binding Source: UniProtKB
  • p53 binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • protein kinase activator activity Source: ParkinsonsUK-UCL
  • protein kinase binding Source: ParkinsonsUK-UCL
  • protein N-terminus binding Source: UniProtKB
  • signal transducer activity, downstream of receptor Source: ProtInc
  • transcription corepressor activity Source: UniProtKB
  • transcription factor binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

  • activation of JUN kinase activity Source: ProtInc
  • androgen receptor signaling pathway Source: UniProtKB
  • apoptotic process Source: UniProtKB
  • chromatin modification Source: UniProtKB-KW
  • chromatin remodeling Source: UniProtKB
  • extrinsic apoptotic signaling pathway via death domain receptors Source: ProtInc
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • nucleosome assembly Source: UniProtKB
  • positive regulation of neuron death Source: ParkinsonsUK-UCL
  • positive regulation of protein kinase activity Source: ParkinsonsUK-UCL
  • positive regulation of protein phosphorylation Source: ParkinsonsUK-UCL
  • regulation of protein ubiquitination Source: UniProtKB
  • regulation of transcription, DNA-templated Source: MGI
  • transcription, DNA-templated Source: UniProtKB-KW
  • 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

BioCyciZFISH:ENSG00000007565-MONOMER.
BRENDAi2.7.7.19. 2681.
ReactomeiR-HSA-6804757. Regulation of TP53 Degradation.
SignaLinkiQ9UER7.
SIGNORiQ9UER7.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:2681. DAXX.

Subcellular locationi

Isoform beta :
Isoform gamma :

GO - Cellular componenti

  • chromosome, centromeric region Source: CACAO
  • cytoplasm Source: UniProtKB
  • cytosol Source: UniProtKB
  • nucleolus Source: UniProtKB-SubCell
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • PML body Source: UniProtKB
  • SWI/SNF superfamily-type complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi206Q → L: Impairs interaction with histones H3 and H4. 1 Publication1
Mutagenesisi220S → A: Abolishes interaction with histones H3 and H4. 1 Publication1
Mutagenesisi222Y → A or S: Abolishes interaction with histones H3 and H4. 2 Publications1
Mutagenesisi222Y → E: Abolishes interaction with histone H3.3. 2 Publications1
Mutagenesisi225E → L: Impairs interaction with histones H3 and H4. 1 Publication1
Mutagenesisi229K → A or L: Impairs interaction with histones H3 and H4. 1 Publication1
Mutagenesisi251R → A: Abolishes interaction with histones H3 and H4. 1 Publication1
Mutagenesisi317F → A: Abolishes interaction with histones H3 and H4. 1 Publication1
Mutagenesisi328R → A: Abolishes interaction with histones H3 and H4. 1 Publication1
Mutagenesisi331D → A: Abolishes interaction with histones H3 and H4. 1 Publication1
Mutagenesisi630K → A: Abolishes sumoylation; when associated with A-631. 1 Publication1
Mutagenesisi631K → A: Abolishes sumoylation; when associated with A-630. 1 Publication1
Mutagenesisi668S → A: No translocation to the cytosol upon glucose deprivation. 1 Publication1
Mutagenesisi671S → A: No effect on cytosol translocation. upon glucose deprivation. 1 Publication1
Mutagenesisi733 – 740Missing : Abolishes sumoylation. 1 Publication8

Organism-specific databases

DisGeNETi1616.
OpenTargetsiENSG00000204209.
ENSG00000206206.
ENSG00000206279.
ENSG00000227046.
ENSG00000231617.
PharmGKBiPA27148.

Polymorphism and mutation databases

BioMutaiDAXX.
DMDMi24636785.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001512581 – 740Death domain-associated protein 6Add BLAST740

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei25PhosphoserineCombined sources1
Modified residuei178PhosphoserineCombined sources1
Modified residuei213PhosphoserineCombined sources1
Modified residuei412PhosphoserineCombined sources1
Modified residuei424PhosphoserineCombined sources1
Modified residuei459PhosphothreonineBy similarity1
Modified residuei495PhosphoserineCombined sources1
Modified residuei498PhosphoserineBy similarity1
Modified residuei512N6-acetyllysineCombined sources1
Modified residuei561PhosphoserineBy similarity1
Modified residuei580PhosphoserineBy similarity1
Cross-linki630Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)1 Publication
Cross-linki631Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)1 Publication
Modified residuei668PhosphoserineCombined sources1 Publication1
Modified residuei671PhosphoserineCombined sources1
Modified residuei688PhosphoserineCombined sources1
Modified residuei702PhosphoserineCombined sources1
Modified residuei737PhosphoserineCombined sources1
Modified residuei739PhosphoserineCombined sources1

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

EPDiQ9UER7.
PaxDbiQ9UER7.
PeptideAtlasiQ9UER7.
PRIDEiQ9UER7.

PTM databases

iPTMnetiQ9UER7.
PhosphoSitePlusiQ9UER7.

Expressioni

Tissue specificityi

Ubiquitous.

Inductioni

Upon mitogenic stimulation by concanavalin-A.

Gene expression databases

BgeeiENSG00000204209.
CleanExiHS_DAXX.
ExpressionAtlasiQ9UER7. baseline and differential.
GenevisibleiQ9UER7. HS.

Organism-specific databases

HPAiCAB002224.
CAB025546.
HPA008736.
HPA065779.

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. Interacts with Epstein-Barr virus protein BNRF1. Interacts with human adenovirus 5 E1B-55K protein; this interaction might alterate the normal interactions of DAXX, PML, and TP53, which may contribute to cell transformation (PubMed:14557665).30 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P032434EBI-77321,EBI-1561361From a different organism.
AIREO439185EBI-77321,EBI-1753081
ARP102755EBI-77321,EBI-608057
ATRXP461007EBI-77321,EBI-396461
BNRF1P031795EBI-77321,EBI-9349301From a different organism.
CARD9Q9H2573EBI-77321,EBI-751319
CDCA7LQ96GN53EBI-77321,EBI-5278764
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
FAM9BQ8IZU03EBI-77321,EBI-10175124
FASP254453EBI-77321,EBI-494743
FasP254464EBI-77321,EBI-296206From a different organism.
FTH1P027945EBI-77321,EBI-713259
GOLGA2A0A0C4DGS54EBI-77321,EBI-11522202
GOLGA2Q083793EBI-77321,EBI-618309
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
NECAB2H3BTW25EBI-77321,EBI-10172876
PARK7Q994973EBI-77321,EBI-1164361
Pax5Q026504EBI-77321,EBI-296260From a different organism.
PBXIP1Q96AQ63EBI-77321,EBI-740845
PMLP295906EBI-77321,EBI-295890
PNMA1Q8ND904EBI-77321,EBI-302345
RASSF1Q9NS236EBI-77321,EBI-367363
RASSF1Q9NS23-45EBI-77321,EBI-438710
RELAQ042065EBI-77321,EBI-73886
Ripk3Q9QZL02EBI-77321,EBI-2367423From a different organism.
SPOPO437915EBI-77321,EBI-743549
SSX2IPQ9Y2D83EBI-77321,EBI-2212028
STAT3P407634EBI-77321,EBI-518675
SUMO1P631657EBI-77321,EBI-80140
TCF7L2Q9NQB05EBI-77321,EBI-924724
TGFBR2P371732EBI-77321,EBI-296151
TP53P0463712EBI-77321,EBI-366083
TSG101Q998164EBI-77321,EBI-346882
UBCP0CG482EBI-77321,EBI-3390054
UBE2IP632793EBI-77321,EBI-80168
USP7Q9300913EBI-77321,EBI-302474
WHSC1L1Q9BZ952EBI-77321,EBI-3390132

GO - Molecular functioni

  • androgen receptor binding Source: UniProtKB
  • enzyme binding Source: UniProtKB
  • heat shock protein binding Source: UniProtKB
  • histone binding Source: UniProtKB
  • p53 binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • protein kinase binding Source: ParkinsonsUK-UCL
  • protein N-terminus binding Source: UniProtKB
  • transcription factor binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi107985. 164 interactors.
DIPiDIP-27628N.
IntActiQ9UER7. 121 interactors.
MINTiMINT-122943.
STRINGi9606.ENSP00000266000.

Structurei

Secondary structure

1740
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi60 – 77Combined sources18
Turni78 – 80Combined sources3
Helixi84 – 93Combined sources10
Helixi97 – 100Combined sources4
Helixi103 – 118Combined sources16
Helixi120 – 122Combined sources3
Helixi123 – 136Combined sources14
Beta strandi138 – 140Combined sources3
Helixi185 – 206Combined sources22
Helixi214 – 216Combined sources3
Helixi221 – 242Combined sources22
Helixi252 – 254Combined sources3
Helixi265 – 275Combined sources11
Beta strandi278 – 280Combined sources3
Helixi286 – 299Combined sources14
Helixi306 – 333Combined sources28
Helixi339 – 341Combined sources3
Helixi346 – 348Combined sources3
Helixi350 – 353Combined sources4
Helixi355 – 384Combined sources30

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5KDMX-ray3.50C178-389[»]
DisProtiDP00707.
ProteinModelPortaliQ9UER7.
SMRiQ9UER7.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UER7.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 160Necessary for interaction with USP7 and ATRXAdd BLAST160
Regioni183 – 417Interaction with histone H3.3Add BLAST235
Regioni347 – 570Necessary for interaction with USP7Add BLAST224
Regioni501 – 625Interaction with MAP3K5Add BLAST125
Regioni626 – 740Interaction with SPOP1 PublicationAdd BLAST115
Regioni733 – 740Sumo interaction motif (SIM)8

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili180 – 217Sequence analysisAdd BLAST38
Coiled coili358 – 399Sequence analysisAdd BLAST42
Coiled coili430 – 489Sequence analysisAdd BLAST60

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi391 – 395Nuclear localization signalSequence analysis5
Motifi628 – 634Nuclear localization signalSequence analysis7

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi11 – 16Poly-Asp6
Compositional biasi434 – 572Asp/Glu-rich (acidic)Add BLAST139

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

eggNOGiENOG410IGIP. Eukaryota.
ENOG4111K0B. LUCA.
GeneTreeiENSGT00390000009448.
HOGENOMiHOG000112148.
HOVERGENiHBG031495.
InParanoidiQ9UER7.
KOiK02308.
OMAiLCKTQTA.
OrthoDBiEOG091G0JSL.
PhylomeDBiQ9UER7.
TreeFamiTF325803.

Family and domain databases

CDDicd13151. DAXX_helical_bundle. 1 hit.
InterProiIPR005012. Daxx.
IPR031333. Daxx_N.
[Graphical view]
PANTHERiPTHR12766. PTHR12766. 1 hit.
PfamiPF03344. Daxx. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

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

        10         20         30         40         50
MATANSIIVL DDDDEDEAAA QPGPSHPLPN AASPGAEAPS SSEPHGARGS
60 70 80 90 100
SSSGGKKCYK LENEKLFEEF LELCKMQTAD HPEVVPFLYN RQQRAHSLFL
110 120 130 140 150
ASAEFCNILS RVLSRARSRP AKLYVYINEL CTVLKAHSAK KKLNLAPAAT
160 170 180 190 200
TSNEPSGNNP PTHLSLDPTN AENTASQSPR TRGSRRQIQR LEQLLALYVA
210 220 230 240 250
EIRRLQEKEL DLSELDDPDS AYLQEARLKR KLIRLFGRLC ELKDCSSLTG
260 270 280 290 300
RVIEQRIPYR GTRYPEVNRR IERLINKPGP DTFPDYGDVL RAVEKAAARH
310 320 330 340 350
SLGLPRQQLQ LMAQDAFRDV GIRLQERRHL DLIYNFGCHL TDDYRPGVDP
360 370 380 390 400
ALSDPVLARR LRENRSLAMS RLDEVISKYA MLQDKSEEGE RKKRRARLQG
410 420 430 440 450
TSSHSADTPE ASLDSGEGPS GMASQGCPSA SRAETDDEDD EESDEEEEEE
460 470 480 490 500
EEEEEEEATD SEEEEDLEQM QEGQEDDEEE DEEEEAAAGK DGDKSPMSSL
510 520 530 540 550
QISNEKNLEP GKQISRSSGE QQNKGRIVSP SLLSEEPLAP SSIDAESNGE
560 570 580 590 600
QPEELTLEEE SPVSQLFELE IEALPLDTPS SVETDISSSR KQSEEPFTTV
610 620 630 640 650
LENGAGMVSS TSFNGGVSPH NWGDSGPPCK KSRKEKKQTG SGPLGNSYVE
660 670 680 690 700
RQRSVHEKNG KKICTLPSPP SPLASLAPVA DSSTRVDSPS HGLVTSSLCI
710 720 730 740
PSPARLSQTP HSQPPRPGTC KTSVATQCDP EEIIVLSDSD
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
Isoform beta (identifier: Q9UER7-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     653-688: RSVHEKNGKKICTLPSPPSPLASLAPVADSSTRVDS → SPAVPNPPFTASSAWYLQDKCGHTMRSRRDHRALRL
     689-740: Missing.

Note: Markedly decreased affinity for PML and TP53/p53, unable to repress p53-mediated transcription.1 Publication
Show »
Length:688
Mass (Da):76,326
Checksum:i3835917DA2147821
GO
Isoform gamma (identifier: Q9UER7-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     648-682: YVERQRSVHEKNGKKICTLPSPPSPLASLAPVADS → PAVPNPPFTASSAWYLQDKCGHTMRSRRDHRALRL
     683-740: Missing.

Note: Markedly decreased affinity for PML and TP53/p53, unable to repress p53-mediated transcription.1 Publication
Show »
Length:682
Mass (Da):75,563
Checksum:i080438D150FCEF3A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti177Q → R in AAB66585 (PubMed:9407001).Curated1
Sequence conflicti263R → H in AAC72843 (PubMed:10698492).Curated1
Sequence conflicti323R → W in AAB66585 (PubMed:9407001).Curated1
Sequence conflicti365R → Q in AAB66585 (PubMed:9407001).Curated1
Sequence conflicti382L → S in AAB66585 (PubMed:9407001).Curated1
Sequence conflicti505E → G in BAG64795 (PubMed:14702039).Curated1
Sequence conflicti647S → R in CAB09986 (PubMed:14574404).Curated1
Sequence conflicti647S → R in CAB09989 (PubMed:14574404).Curated1
Sequence conflicti722T → A in CAB09986 (PubMed:14574404).Curated1
Sequence conflicti722T → A in CAB09989 (PubMed:14574404).Curated1
Sequence conflicti731 – 732EE → KK in AAC72843 (PubMed:10698492).Curated2

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0455881 – 75Missing in isoform 3. 1 PublicationAdd BLAST75
Alternative sequenceiVSP_057437648 – 682YVERQ…PVADS → PAVPNPPFTASSAWYLQDKC GHTMRSRRDHRALRL in isoform gamma. 1 PublicationAdd BLAST35
Alternative sequenceiVSP_057438653 – 688RSVHE…TRVDS → SPAVPNPPFTASSAWYLQDK CGHTMRSRRDHRALRL in isoform beta. 1 PublicationAdd BLAST36
Alternative sequenceiVSP_057439683 – 740Missing in isoform gamma. 1 PublicationAdd BLAST58
Alternative sequenceiVSP_057440689 – 740Missing in isoform beta. 1 PublicationAdd BLAST52
Alternative sequenceiVSP_001270696 – 740SSLCI…LSDSD → PAKNLGRRRSKQDQG in isoform 2. 1 PublicationAdd BLAST45

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
HQ436528 mRNA. Translation: AEC33235.1.
HQ436529 mRNA. Translation: AEC33236.1.
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]
ENST00000612868; ENSP00000479172; ENSG00000227046. [Q9UER7-3]
ENST00000612888; ENSP00000483394; ENSG00000206206. [Q9UER7-3]
ENST00000613912; ENSP00000477633; ENSG00000206206. [Q9UER7-4]
ENST00000616312; ENSP00000483517; ENSG00000227046. [Q9UER7-4]
ENST00000617660; ENSP00000480448; ENSG00000206279. [Q9UER7-3]
ENST00000619421; ENSP00000478810; ENSG00000206279. [Q9UER7-4]
ENST00000620164; ENSP00000482399; ENSG00000204209. [Q9UER7-4]
ENST00000622655; ENSP00000484830; ENSG00000231617. [Q9UER7-4]
GeneIDi1616.
KEGGihsa:1616.
UCSCiuc003oec.4. human. [Q9UER7-1]
uc063nwl.1. human.

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:
EMBLi
GenBanki
DDBJi
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.
HQ436528 mRNA. Translation: AEC33235.1.
HQ436529 mRNA. Translation: AEC33236.1.
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5KDMX-ray3.50C178-389[»]
DisProtiDP00707.
ProteinModelPortaliQ9UER7.
SMRiQ9UER7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107985. 164 interactors.
DIPiDIP-27628N.
IntActiQ9UER7. 121 interactors.
MINTiMINT-122943.
STRINGi9606.ENSP00000266000.

PTM databases

iPTMnetiQ9UER7.
PhosphoSitePlusiQ9UER7.

Polymorphism and mutation databases

BioMutaiDAXX.
DMDMi24636785.

Proteomic databases

EPDiQ9UER7.
PaxDbiQ9UER7.
PeptideAtlasiQ9UER7.
PRIDEiQ9UER7.

Protocols and materials databases

DNASUi1616.
Structural Biology KnowledgebaseSearch...

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]
ENST00000612868; ENSP00000479172; ENSG00000227046. [Q9UER7-3]
ENST00000612888; ENSP00000483394; ENSG00000206206. [Q9UER7-3]
ENST00000613912; ENSP00000477633; ENSG00000206206. [Q9UER7-4]
ENST00000616312; ENSP00000483517; ENSG00000227046. [Q9UER7-4]
ENST00000617660; ENSP00000480448; ENSG00000206279. [Q9UER7-3]
ENST00000619421; ENSP00000478810; ENSG00000206279. [Q9UER7-4]
ENST00000620164; ENSP00000482399; ENSG00000204209. [Q9UER7-4]
ENST00000622655; ENSP00000484830; ENSG00000231617. [Q9UER7-4]
GeneIDi1616.
KEGGihsa:1616.
UCSCiuc003oec.4. human. [Q9UER7-1]
uc063nwl.1. human.

Organism-specific databases

CTDi1616.
DisGeNETi1616.
GeneCardsiDAXX.
HGNCiHGNC:2681. DAXX.
HPAiCAB002224.
CAB025546.
HPA008736.
HPA065779.
MIMi603186. gene.
neXtProtiNX_Q9UER7.
OpenTargetsiENSG00000204209.
ENSG00000206206.
ENSG00000206279.
ENSG00000227046.
ENSG00000231617.
PharmGKBiPA27148.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IGIP. Eukaryota.
ENOG4111K0B. LUCA.
GeneTreeiENSGT00390000009448.
HOGENOMiHOG000112148.
HOVERGENiHBG031495.
InParanoidiQ9UER7.
KOiK02308.
OMAiLCKTQTA.
OrthoDBiEOG091G0JSL.
PhylomeDBiQ9UER7.
TreeFamiTF325803.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000007565-MONOMER.
BRENDAi2.7.7.19. 2681.
ReactomeiR-HSA-6804757. Regulation of TP53 Degradation.
SignaLinkiQ9UER7.
SIGNORiQ9UER7.

Miscellaneous databases

ChiTaRSiDAXX. human.
EvolutionaryTraceiQ9UER7.
GeneWikiiDeath-associated_protein_6.
GenomeRNAii1616.
PROiQ9UER7.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000204209.
CleanExiHS_DAXX.
ExpressionAtlasiQ9UER7. baseline and differential.
GenevisibleiQ9UER7. HS.

Family and domain databases

CDDicd13151. DAXX_helical_bundle. 1 hit.
InterProiIPR005012. Daxx.
IPR031333. Daxx_N.
[Graphical view]
PANTHERiPTHR12766. PTHR12766. 1 hit.
PfamiPF03344. Daxx. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDAXX_HUMAN
AccessioniPrimary (citable) accession number: Q9UER7
Secondary accession number(s): B4E1I3
, F5ANJ6, F5ANJ7, F5H082, O14747, O15141, O15208, Q5STK9, Q9BWI3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: November 1, 2002
Last modified: November 30, 2016
This is version 168 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.