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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
  • receptor signaling protein activity 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
  • cellular response to anoxia Source: Ensembl
  • cellular response to tumor necrosis factor Source: Ensembl
  • chromatin remodeling Source: UniProtKB
  • extrinsic apoptotic signaling pathway via death domain receptors Source: ProtInc
  • negative regulation of myotube differentiation Source: Ensembl
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  • nucleosome assembly Source: UniProtKB
  • PML body organization Source: Ensembl
  • positive regulation of apoptotic process Source: Ensembl
  • positive regulation of histone phosphorylation Source: Ensembl
  • 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
  • response to metal ion Source: Ensembl
  • 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

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

  • cell body Source: Ensembl
  • cell cortex Source: Ensembl
  • chromosome, centromeric region Source: CACAO
  • cytoplasm Source: UniProtKB
  • cytosol Source: UniProtKB
  • microtubule Source: Ensembl
  • neuron projection Source: Ensembl
  • nucleolus Source: UniProtKB-SubCell
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • PML body Source: UniProtKB
  • SWI/SNF superfamily-type complex Source: UniProtKB
  • XY body Source: Ensembl
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.

Polymorphism and mutation databases

BioMutaiDAXX.
DMDMi24636785.

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 residuei25 – 251PhosphoserineCombined sources
Modified residuei178 – 1781PhosphoserineCombined sources
Modified residuei213 – 2131PhosphoserineCombined sources
Modified residuei412 – 4121PhosphoserineCombined sources
Modified residuei424 – 4241PhosphoserineCombined sources
Modified residuei459 – 4591PhosphothreonineBy similarity
Modified residuei495 – 4951PhosphoserineCombined sources
Modified residuei498 – 4981PhosphoserineBy similarity
Modified residuei512 – 5121N6-acetyllysineCombined sources
Modified residuei561 – 5611PhosphoserineBy similarity
Modified residuei580 – 5801PhosphoserineBy similarity
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 – 6681PhosphoserineCombined sources1 Publication
Modified residuei671 – 6711PhosphoserineCombined sources
Modified residuei688 – 6881PhosphoserineCombined sources
Modified residuei702 – 7021PhosphoserineCombined sources
Modified residuei737 – 7371PhosphoserineCombined sources
Modified residuei739 – 7391PhosphoserineCombined sources

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.
MaxQBiQ9UER7.
PaxDbiQ9UER7.
PeptideAtlasiQ9UER7.
PRIDEiQ9UER7.

PTM databases

iPTMnetiQ9UER7.
PhosphoSiteiQ9UER7.

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
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
NECAB2H3BTW23EBI-77321,EBI-10172876
PARK7Q994973EBI-77321,EBI-1164361
Pax5Q026504EBI-77321,EBI-296260From a different organism.
PBXIP1Q96AQ63EBI-77321,EBI-740845
PMLP295906EBI-77321,EBI-295890
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. 151 interactions.
DIPiDIP-27628N.
IntActiQ9UER7. 105 interactions.
MINTiMINT-122943.
STRINGi9606.ENSP00000266000.

Structurei

Secondary structure

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

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ9UER7.

Family & Domainsi

Region

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

Coiled coil

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

Motif

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

Compositional bias

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

Domaini

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

Sequence similaritiesi

Belongs to the DAXX family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7575Missing in isoform 3. 1 PublicationVSP_045588Add
BLAST
Alternative sequencei648 – 68235YVERQ…PVADS → PAVPNPPFTASSAWYLQDKC GHTMRSRRDHRALRL in isoform gamma. 1 PublicationVSP_057437Add
BLAST
Alternative sequencei653 – 68836RSVHE…TRVDS → SPAVPNPPFTASSAWYLQDK CGHTMRSRRDHRALRL in isoform beta. 1 PublicationVSP_057438Add
BLAST
Alternative sequencei683 – 74058Missing in isoform gamma. 1 PublicationVSP_057439Add
BLAST
Alternative sequencei689 – 74052Missing in isoform beta. 1 PublicationVSP_057440Add
BLAST
Alternative sequencei696 – 74045SSLCI…LSDSD → PAKNLGRRRSKQDQG in isoform 2. 1 PublicationVSP_001270Add
BLAST

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

Protein-protein interaction databases

BioGridi107985. 151 interactions.
DIPiDIP-27628N.
IntActiQ9UER7. 105 interactions.
MINTiMINT-122943.
STRINGi9606.ENSP00000266000.

PTM databases

iPTMnetiQ9UER7.
PhosphoSiteiQ9UER7.

Polymorphism and mutation databases

BioMutaiDAXX.
DMDMi24636785.

Proteomic databases

EPDiQ9UER7.
MaxQBiQ9UER7.
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.
GeneCardsiDAXX.
HGNCiHGNC:2681. DAXX.
HPAiCAB002224.
CAB025546.
HPA008736.
HPA065779.
MIMi603186. gene.
neXtProtiNX_Q9UER7.
PharmGKBiPA27148.
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

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: September 7, 2016
This is version 165 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.