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UniProtKB - Q9UER7 (DAXX_HUMAN)

Protein

Death domain-associated protein 6

Gene

DAXX

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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). Plays a role as a positive regulator of the heat shock transcription factor HSF1 activity during the stress protein response (PubMed:15016915).12 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 heterodimerization activity Source: CAFA
  • protein homodimerization activity Source: UniProtKB
  • protein kinase activator activity Source: ParkinsonsUK-UCL
  • protein kinase binding Source: ParkinsonsUK-UCL
  • protein N-terminus binding Source: UniProtKB
  • SUMO binding Source: CAFA
  • transcription coactivator activity Source: UniProtKB
  • transcription corepressor activity Source: UniProtKB
  • transcription factor binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionChaperone, Chromatin regulator, Repressor
Biological processApoptosis, Host-virus interaction, Transcription, Transcription regulation

Enzyme and pathway databases

BRENDAi2.7.7.19 2681
ReactomeiR-HSA-3899300 SUMOylation of transcription cofactors
R-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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

EuPathDBiHostDB:ENSG00000204209.10
HGNCiHGNC:2681 DAXX
MIMi603186 gene
neXtProtiNX_Q9UER7

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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
MalaCardsiDAXX
OpenTargetsiENSG00000204209
Orphaneti100075 Neuroendocrine tumor of stomach
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
Cross-linki142Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
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
ProteomicsDBi84150
84151 [Q9UER7-2]

PTM databases

iPTMnetiQ9UER7
PhosphoSitePlusiQ9UER7

Expressioni

Tissue specificityi

Ubiquitous.

Inductioni

Upon mitogenic stimulation by concanavalin-A.

Gene expression databases

BgeeiENSG00000204209 Expressed in 223 organ(s), highest expression level in testis
CleanExiHS_DAXX
ExpressionAtlasiQ9UER7 baseline and differential
GenevisibleiQ9UER7 HS

Organism-specific databases

HPAiCAB002224
CAB025546
HPA008736
HPA008797
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 HSF1 (via homotrimeric form preferentially); this interaction relieves homotrimeric HSF1 from repression of its transcriptional activity by HSP90-dependent multichaperone complex upon heat shock (PubMed:15016915). Interacts with SUMO1P1/SUMO5 (PubMed:27211601).29 Publications
(Microbial infection) Interacts with human cytomegalovirus/HHV-5 tegument phosphoprotein pp71 and protein UL123.1 Publication
(Microbial infection) Interacts with Epstein-Barr virus protein BNRF1.1 Publication
(Microbial infection) 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.1 Publication

Binary interactionsi

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi107985, 238 interactors
CORUMiQ9UER7
DIPiDIP-27628N
IntActiQ9UER7, 128 interactors
MINTiQ9UER7
STRINGi9606.ENSP00000266000

Structurei

Secondary structure

1740
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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
OrthoDBiEOG09370P3D
PhylomeDBiQ9UER7
TreeFamiTF325803

Family and domain databases

CDDicd13151 DAXX_helical_bundle, 1 hit
Gene3Di1.10.8.810, 1 hit
InterProiView protein in InterPro
IPR005012 Daxx
IPR031333 Daxx_N
IPR038298 Daxx_N_sf
PANTHERiPTHR12766 PTHR12766, 1 hit
PfamiView protein in Pfam
PF03344 Daxx, 1 hit

Sequences (5+)i

Sequence statusi: Complete.

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

This entry has 5 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

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.
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.
Show »
Length:682
Mass (Da):75,563
Checksum:i080438D150FCEF3A
GO

Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q4VX54Q4VX54_HUMAN
Death domain-associated protein 6
DAXX
178Annotation score:
A2AB94A2AB94_HUMAN
Death domain-associated protein 6
DAXX
48Annotation score:
A0A0G2JJZ4A0A0G2JJZ4_HUMAN
Death domain-associated protein 6
DAXX
129Annotation score:

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

Similar proteinsi

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[»]
5GRQX-ray1.58A55-144[»]
B55-143[»]
5KDMX-ray3.50C178-389[»]
5Y18X-ray2.20A55-144[»]
5Y6OX-ray3.10A/B/C/D/E/F/G/H/I50-144[»]
DisProtiDP00707
ProteinModelPortaliQ9UER7
SMRiQ9UER7
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107985, 238 interactors
CORUMiQ9UER7
DIPiDIP-27628N
IntActiQ9UER7, 128 interactors
MINTiQ9UER7
STRINGi9606.ENSP00000266000

PTM databases

iPTMnetiQ9UER7
PhosphoSitePlusiQ9UER7

Polymorphism and mutation databases

BioMutaiDAXX
DMDMi24636785

Proteomic databases

EPDiQ9UER7
PaxDbiQ9UER7
PeptideAtlasiQ9UER7
PRIDEiQ9UER7
ProteomicsDBi84150
84151 [Q9UER7-2]

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
EuPathDBiHostDB:ENSG00000204209.10
GeneCardsiDAXX
HGNCiHGNC:2681 DAXX
HPAiCAB002224
CAB025546
HPA008736
HPA008797
HPA065779
MalaCardsiDAXX
MIMi603186 gene
neXtProtiNX_Q9UER7
OpenTargetsiENSG00000204209
Orphaneti100075 Neuroendocrine tumor of stomach
PharmGKBiPA27148
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IGIP Eukaryota
ENOG4111K0B LUCA
GeneTreeiENSGT00390000009448
HOGENOMiHOG000112148
HOVERGENiHBG031495
InParanoidiQ9UER7
KOiK02308
OMAiLCKTQTA
OrthoDBiEOG09370P3D
PhylomeDBiQ9UER7
TreeFamiTF325803

Enzyme and pathway databases

BRENDAi2.7.7.19 2681
ReactomeiR-HSA-3899300 SUMOylation of transcription cofactors
R-HSA-6804757 Regulation of TP53 Degradation
SignaLinkiQ9UER7
SIGNORiQ9UER7

Miscellaneous databases

ChiTaRSiDAXX human
EvolutionaryTraceiQ9UER7
GeneWikiiDeath-associated_protein_6
GenomeRNAii1616
PROiPR:Q9UER7
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000204209 Expressed in 223 organ(s), highest expression level in testis
CleanExiHS_DAXX
ExpressionAtlasiQ9UER7 baseline and differential
GenevisibleiQ9UER7 HS

Family and domain databases

CDDicd13151 DAXX_helical_bundle, 1 hit
Gene3Di1.10.8.810, 1 hit
InterProiView protein in InterPro
IPR005012 Daxx
IPR031333 Daxx_N
IPR038298 Daxx_N_sf
PANTHERiPTHR12766 PTHR12766, 1 hit
PfamiView protein in Pfam
PF03344 Daxx, 1 hit
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 historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: November 1, 2002
Last modified: November 7, 2018
This is version 187 of the entry and version 2 of the sequence. See 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. SIMILARITY comments
    Index of protein domains and families
  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. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
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