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UniProtKB - Q9UER7 (DAXX_HUMAN)

Entry version 207 (07 Apr 2021)
Sequence version 2 (01 Nov 2002)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

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

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.7.7.19, 2681

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		Q9UER7

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-3899300, SUMOylation of transcription cofactors
R-HSA-6804757, Regulation of TP53 Degradation
R-HSA-9609690, HCMV Early Events
R-HSA-9670095, Inhibition of DNA recombination at telomere
R-HSA-9670613, Defective Inhibition of DNA Recombination at Telomere Due to DAXX Mutations
R-HSA-9670615, Defective Inhibition of DNA Recombination at Telomere Due to ATRX Mutations

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...SignaLinki		Q9UER7

SIGNOR Signaling Network Open Resource

More...SIGNORi		Q9UER7

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:DAXX
Synonyms:BING2, DAP6
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 6

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:2681, DAXX

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		603186, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q9UER7

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000204209.10

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

DisGeNET

More...DisGeNETi		1616

MalaCards human disease database

More...MalaCardsi		DAXX

Open Targets

More...OpenTargetsi		ENSG00000204209

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		100075, Neuroendocrine tumor of stomach

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA27148

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		Q9UER7, Tbio

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		DAXX

Domain mapping of disease mutations (DMDM)

More...DMDMi		24636785

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001512581 – 740Death domain-associated protein 6Add BLAST740

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei25PhosphoserineCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

Encyclopedia of Proteome Dynamics

More...EPDi		Q9UER7

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q9UER7

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		Q9UER7

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		Q9UER7

PeptideAtlas

More...PeptideAtlasi		Q9UER7

PRoteomics IDEntifications database

More...PRIDEi		Q9UER7

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		25260
84150 [Q9UER7-1]
84151 [Q9UER7-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q9UER7

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		Q9UER7

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Ubiquitous.

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Upon mitogenic stimulation by concanavalin-A.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000204209, Expressed in granulocyte and 234 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q9UER7, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q9UER7, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000204209, Low tissue specificity

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Q9UER7
With#Exp.IntAct
AIRE [O43918]5EBI-77321,EBI-1753081
AMOTL2 [Q9Y2J4]3EBI-77321,EBI-746752
APBB2 - isoform 2 [Q92870-2]3EBI-77321,EBI-21535880
AR [P10275]5EBI-77321,EBI-608057
ATRX [P46100]8EBI-77321,EBI-396461
CARD9 [Q9H257]3EBI-77321,EBI-751319
CDCA7L [Q96GN5]3EBI-77321,EBI-5278764
CDKN2A [Q8N726]8EBI-77321,EBI-625922
CEP63 - isoform 3 [Q96MT8-3]3EBI-77321,EBI-11522539
CEP70 [Q8NHQ1]3EBI-77321,EBI-739624
CREBBP [Q92793]2EBI-77321,EBI-81215
DMAP1 [Q9NPF5]3EBI-77321,EBI-399105
DMWD [G5E9A7]3EBI-77321,EBI-10976677
FAM9B [Q8IZU0]4EBI-77321,EBI-10175124
FAS [P25445]3EBI-77321,EBI-494743
FTH1 [P02794]5EBI-77321,EBI-713259
GAS8 [O95995]5EBI-77321,EBI-1052570
GLE1 [Q53GS7]3EBI-77321,EBI-1955541
GMCL1 [Q96IK5]3EBI-77321,EBI-2548508
GOLGA2 [Q08379]8EBI-77321,EBI-618309
GOLGA6L9 [A6NEM1]3EBI-77321,EBI-5916454
GRIPAP1 [Q4V328]3EBI-77321,EBI-717919
H3-3B [P84243]6EBI-77321,EBI-120658
H3-5 [Q6NXT2]3EBI-77321,EBI-2868501
HDAC1 [Q13547]2EBI-77321,EBI-301834
HDAC2 [Q92769]2EBI-77321,EBI-301821
HSPB1 [P04792]4EBI-77321,EBI-352682
HTT [P42858]15EBI-77321,EBI-466029
KCTD4 [Q8WVF5]3EBI-77321,EBI-741463
KLHL8 - isoform 2 [Q9P2G9-2]3EBI-77321,EBI-11959635
MAP3K5 [Q99683]7EBI-77321,EBI-476263
MCRS1 [Q96EZ8]11EBI-77321,EBI-348259
MDM2 [Q00987]18EBI-77321,EBI-389668
MIPOL1 [Q8TD10]3EBI-77321,EBI-2548751
MKRN1 [Q9UHC7]3EBI-77321,EBI-373524
MSANTD4 [Q8NCY6]3EBI-77321,EBI-7850168
NECAB2 - isoform 2 [Q7Z6G3-2]6EBI-77321,EBI-10172876
NSD3 [Q9BZ95]2EBI-77321,EBI-3390132
PARK7 [Q99497]6EBI-77321,EBI-1164361
PBXIP1 [Q96AQ6]3EBI-77321,EBI-740845
PEX26 [Q7Z412]3EBI-77321,EBI-752057
PIBF1 [Q4G0R1]3EBI-77321,EBI-14066006
PML [P29590]6EBI-77321,EBI-295890
PMP22 [D3DTS7]3EBI-77321,EBI-25882629
PNMA1 [Q8ND90]5EBI-77321,EBI-302345
RASSF1 [Q9NS23]6EBI-77321,EBI-367363
RASSF1 - isoform C [Q9NS23-4]5EBI-77321,EBI-438710
RASSF3 [Q86WH2]3EBI-77321,EBI-2845202
RELA [Q04206]5EBI-77321,EBI-73886
RNF4 [P78317]3EBI-77321,EBI-2340927
SERTAD3 [Q9UJW9]3EBI-77321,EBI-748621
SPOP [O43791]5EBI-77321,EBI-743549
SPRED1 [Q7Z699]3EBI-77321,EBI-5235340
SSX2IP [Q9Y2D8]3EBI-77321,EBI-2212028
STAT3 [P40763]4EBI-77321,EBI-518675
SUMO1 [P63165]7EBI-77321,EBI-80140
TAX1BP1 [Q86VP1]3EBI-77321,EBI-529518
TCF7L2 [Q9NQB0]5EBI-77321,EBI-924724
TFIP11 [Q9UBB9]3EBI-77321,EBI-1105213
TGFBR2 [P37173]2EBI-77321,EBI-296151
TP53 [P04637]12EBI-77321,EBI-366083
TSG101 [Q99816]4EBI-77321,EBI-346882
UBC [P0CG48]2EBI-77321,EBI-3390054
UBE2I [P63279]3EBI-77321,EBI-80168
USH1G [Q495M9]3EBI-77321,EBI-8601749
USP7 [Q93009]14EBI-77321,EBI-302474
ZBTB2 [Q8N680]3EBI-77321,EBI-2515601
ZBTB26 [Q9HCK0]3EBI-77321,EBI-3918996
BNRF1 [P03179] from Epstein-Barr virus (strain B95-8).5EBI-77321,EBI-9349301
E1B [P03244] from Human adenovirus C serotype 2.4EBI-77321,EBI-1561155
Fas [P25446] from Mus musculus.4EBI-77321,EBI-296206
Hipk1 [O88904] from Mus musculus.3EBI-77321,EBI-692945
HSPB1 [P15991] from Cricetulus longicaudatus.3EBI-77321,EBI-1559114
Pax5 [Q02650] from Mus musculus.4EBI-77321,EBI-296260
Ripk3 [Q9QZL0] from Mus musculus.2EBI-77321,EBI-2367423
P03243 from Human adenovirus C serotype 5.4EBI-77321,EBI-1561361
Isoform 1 [Q9UER7-1]
With#Exp.IntAct
ETS1 - isoform c-ETS-1A [P14921-1]3EBI-287635,EBI-913224
ETS1 - isoform c-ETS-1B [P14921-2]2EBI-287635,EBI-913228
H3-3B [P84243]21EBI-287635,EBI-120658
H3C12 [P68431]6EBI-287635,EBI-79722
H3C15 [Q71DI3]5EBI-287635,EBI-750650

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		107985, 276 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		Q9UER7

Database of interacting proteins

More...DIPi		DIP-27628N

Protein interaction database and analysis system

More...IntActi		Q9UER7, 162 interactors

Molecular INTeraction database

More...MINTi		Q9UER7

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000363668

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q9UER7, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

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

3D structure databases

Biological Magnetic Resonance Data Bank

More...BMRBi		Q9UER7

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		Q9UER7

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		Q9UER7

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>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
<p>This subsection of the 'Family and domains' section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili180 – 217Sequence analysisAdd BLAST38
Coiled coili358 – 399Sequence analysisAdd BLAST42
Coiled coili430 – 489Sequence analysisAdd BLAST60

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi391 – 395Nuclear localization signalSequence analysis5
Motifi628 – 634Nuclear localization signalSequence analysis7

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi11 – 16Poly-Asp6
Compositional biasi434 – 572Asp/Glu-rich (acidic)Add BLAST139

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

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

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the DAXX family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG502QRS6, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00390000009448

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_022811_1_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q9UER7

Identification of Orthologs from Complete Genome Data

More...OMAi		AMMQDKS

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q9UER7

TreeFam database of animal gene trees

More...TreeFami		TF325803

Family and domain databases

Conserved Domains Database

More...CDDi		cd13151, DAXX_helical_bundle, 1 hit

Database of protein disorder

More...DisProti		DP00707

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.8.810, 1 hit

Intrinsically Disordered proteins with Extensive Annotations and Literature

More...IDEALi		IID00398

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR005012, Daxx
IPR031333, Daxx_N
IPR038298, Daxx_N_sf

The PANTHER Classification System

More...PANTHERi		PTHR12766:SF7, PTHR12766:SF7, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF03344, Daxx, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (5+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 5 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> 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 <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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

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.

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

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>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:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A2AB94A2AB94_HUMAN
Death domain-associated protein 6
DAXX
48Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A0G2JJZ4A0A0G2JJZ4_HUMAN
Death domain-associated protein 6
DAXX
129Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>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
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>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:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...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
AL662820 Genomic DNA No translation available.
AL662827 Genomic DNA No translation available.
BX248088 Genomic DNA No translation available.
CR759793 Genomic DNA No translation available.
CR759786 Genomic DNA No translation available.
CR759817 Genomic DNA No translation available.
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

The Consensus CDS (CCDS) project

More...CCDSi		CCDS4776.1 [Q9UER7-1]
CCDS59008.1 [Q9UER7-3]

Protein sequence database of the Protein Information Resource

More...PIRi		T03847

NCBI Reference Sequences

More...RefSeqi		NP_001135441.1, NM_001141969.1 [Q9UER7-1]
NP_001241646.1, NM_001254717.1 [Q9UER7-3]
NP_001341.1, NM_001350.4 [Q9UER7-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

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

Database of genes from NCBI RefSeq genomes

More...GeneIDi		1616

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:1616

UCSC genome browser

More...UCSCi		uc003oec.4, human [Q9UER7-1]
uc063nwl.1, human

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>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
AL662820 Genomic DNA No translation available.
AL662827 Genomic DNA No translation available.
BX248088 Genomic DNA No translation available.
CR759793 Genomic DNA No translation available.
CR759786 Genomic DNA No translation available.
CR759817 Genomic DNA No translation available.
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]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...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[»]
BMRBiQ9UER7
SMRiQ9UER7
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi107985, 276 interactors
CORUMiQ9UER7
DIPiDIP-27628N
IntActiQ9UER7, 162 interactors
MINTiQ9UER7
STRINGi9606.ENSP00000363668

PTM databases

iPTMnetiQ9UER7
PhosphoSitePlusiQ9UER7

Genetic variation databases

BioMutaiDAXX
DMDMi24636785

Proteomic databases

EPDiQ9UER7
jPOSTiQ9UER7
MassIVEiQ9UER7
PaxDbiQ9UER7
PeptideAtlasiQ9UER7
PRIDEiQ9UER7
ProteomicsDBi25260
84150 [Q9UER7-1]
84151 [Q9UER7-2]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		1411, 993 antibodies

The DNASU plasmid repository

More...DNASUi		1616

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

Comparative Toxicogenomics Database

More...CTDi		1616
DisGeNETi1616

GeneCards: human genes, protein and diseases

More...GeneCardsi		DAXX
HGNCiHGNC:2681, DAXX
HPAiENSG00000204209, Low tissue specificity
MalaCardsiDAXX
MIMi603186, gene
neXtProtiNX_Q9UER7
OpenTargetsiENSG00000204209
Orphaneti100075, Neuroendocrine tumor of stomach
PharmGKBiPA27148
VEuPathDBiHostDB:ENSG00000204209.10

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiENOG502QRS6, Eukaryota
GeneTreeiENSGT00390000009448
HOGENOMiCLU_022811_1_0_1
InParanoidiQ9UER7
OMAiAMMQDKS
PhylomeDBiQ9UER7
TreeFamiTF325803

Enzyme and pathway databases

BRENDAi2.7.7.19, 2681
PathwayCommonsiQ9UER7
ReactomeiR-HSA-3899300, SUMOylation of transcription cofactors
R-HSA-6804757, Regulation of TP53 Degradation
R-HSA-9609690, HCMV Early Events
R-HSA-9670095, Inhibition of DNA recombination at telomere
R-HSA-9670613, Defective Inhibition of DNA Recombination at Telomere Due to DAXX Mutations
R-HSA-9670615, Defective Inhibition of DNA Recombination at Telomere Due to ATRX Mutations
SignaLinkiQ9UER7
SIGNORiQ9UER7

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		1616, 110 hits in 995 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		DAXX, human
EvolutionaryTraceiQ9UER7

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		Death-associated_protein_6

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		1616
PharosiQ9UER7, Tbio

Protein Ontology

More...PROi		PR:Q9UER7
RNActiQ9UER7, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000204209, Expressed in granulocyte and 234 other tissues
ExpressionAtlasiQ9UER7, baseline and differential
GenevisibleiQ9UER7, HS

Family and domain databases

CDDicd13151, DAXX_helical_bundle, 1 hit
DisProtiDP00707
Gene3Di1.10.8.810, 1 hit
IDEALiIID00398
InterProiView protein in InterPro
IPR005012, Daxx
IPR031333, Daxx_N
IPR038298, Daxx_N_sf
PANTHERiPTHR12766:SF7, PTHR12766:SF7, 1 hit
PfamiView protein in Pfam
PF03344, Daxx, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiDAXX_HUMAN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9UER7
Secondary accession number(s): B4E1I3
, F5ANJ6, F5ANJ7, F5H082, O14747, O15141, O15208, Q5STK9, Q9BWI3
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: November 1, 2002
Last modified: April 7, 2021
This is version 207 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, 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
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