DAXX
entrez
1616
canonical
uniprot
Q9UER7
canonical
ensembl
ENSG00000204209
resolver
ensembl
ENSG00000206206
resolver
ensembl
ENSG00000206279
resolver
ensembl
ENSG00000227046
resolver
ensembl
ENSG00000231617
resolver
ensp
ENSP00000266000
resolver
ensp
ENSP00000363668
resolver
ensp
ENSP00000396876
resolver
ensp
ENSP00000516212
resolver
enst
ENST00000706094
resolver
genesymbol
DAXX
resolver
genesymbol_syn
BING2
resolver
genesymbol_syn
DAP6
resolver
hgnc
HGNC:2681
resolver
uniprot
A0A994J5B3
resolver
uniprot
B4E1C1
resolver
uniprot
B4E1I3
resolver
uniprot
F5ANJ6
resolver
uniprot
F5ANJ7
resolver
uniprot
F5H082
resolver
uniprot
O14747
resolver
uniprot
O15141
resolver
uniprot
O15208
resolver
uniprot
Q53F85
resolver
uniprot
Q5STK9
resolver
uniprot
Q9BWI3
resolver
uniprot_entry
A0A994J5B3_HUMAN
resolver
uniprot_entry
B4E1C1_HUMAN
resolver
uniprot_entry
DAXX_HUMAN
resolver
uniprot_entry
Q53F85_HUMAN
resolver
uniprot_sec
B4E1I3
resolver
uniprot_sec
F5ANJ6
resolver
uniprot_sec
F5ANJ7
resolver
uniprot_sec
F5H082
resolver
uniprot_sec
O14747
resolver
uniprot_sec
O15141
resolver
uniprot_sec
O15208
resolver
uniprot_sec
Q5STK9
resolver
uniprot_sec
Q9BWI3
resolver
amino_acid_sequence
MATANSIIVLDDDDEDEAAAQPGPSHPLPNAASPGAEAPSSSEPHGARGSSSSGGKKCYKLENEKLFEEFLELCKMQTADHPEVVPFLYNRQQRAHSLFLASAEFCNILSRVLSRARSRPAKLYVYINELCTVLKAHSAKKKLNLAPAATTSNEPSGNNPPTHLSLDPTNAENTASQSPRTRGSRRQIQRLEQLLALYVAEIRRLQEKELDLSELDDPDSAYLQEARLKRKLIRLFGRLCELKDCSSLTGRVIEQRIPYRGTRYPEVNRRIERLINKPGPDTFPDYGDVLRAVEKAAARHSLGLPRQQLQLMAQDAFRDVGIRLQERRHLDLIYNFGCHLTDDYRPGVDPALSDPVLARRLRENRSLAMSRLDEVISKYAMLQDKSEEGERKKRRARLQGTSSHSADTPEASLDSGEGPSGMASQGCPSASRAETDDEDDEESDEEEEEEEEEEEEEATDSEEEEDLEQMQEGQEDDEEEDEEEEAAAGKDGDKSPMSSLQISNEKNLEPGKQISRSSGEQQNKGRIVSPSLLSEEPLAPSSIDAESNGEQPEELTLEEESPVSQLFELEIEALPLDTPSSVETDISSSRKQSEEPFTTVLENGAGMVSSTSFNGGVSPHNWGDSGPPCKKSRKEKKQTGSGPLGNSYVERQRSVHEKNGKKICTLPSPPSPLASLAPVADSSTRVDSPSHGLVTSSLCIPSPARLSQTPHSQPPRPGTCKTSVATQCDPEEIIVLSDSD
uniprot
proteins
function
FUNCTION: 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 a histone chaperone that facilitates deposition of histone H3.3. Acts as a 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). {ECO:0000269|PubMed:12140263, ECO:0000269|PubMed:14990586, ECO:0000269|PubMed:15016915, ECO:0000269|PubMed:15364927, ECO:0000269|PubMed:16845383, ECO:0000269|PubMed:17081986, ECO:0000269|PubMed:17942542, ECO:0000269|PubMed:20504901, ECO:0000269|PubMed:20651253, ECO:0000269|PubMed:23222847, ECO:0000269|PubMed:24200965, ECO:0000269|PubMed:24530302}.
uniprot
proteins
mass_dalton
81373
uniprot
proteins
mutagenesis
MUTAGEN 206; /note="Q->L: Impairs interaction with histones H3 and H4."; /evidence="ECO:0000269|PubMed:23075851"; MUTAGEN 220; /note="S->A: Abolishes interaction with histones H3 and H4."; /evidence="ECO:0000269|PubMed:23075851"; MUTAGEN 222; /note="Y->A,S: Abolishes interaction with histones H3 and H4."; /evidence="ECO:0000269|PubMed:23075851, ECO:0000269|PubMed:23142979"; MUTAGEN 222; /note="Y->E: Abolishes interaction with histone H3.3."; /evidence="ECO:0000269|PubMed:23075851, ECO:0000269|PubMed:23142979"; MUTAGEN 225; /note="E->L: Impairs interaction with histones H3 and H4."; /evidence="ECO:0000269|PubMed:23075851"; MUTAGEN 229; /note="K->A,L: Impairs interaction with histones H3 and H4."; /evidence="ECO:0000269|PubMed:23075851"; MUTAGEN 251; /note="R->A: Abolishes interaction with histones H3 and H4."; /evidence="ECO:0000269|PubMed:23075851"; MUTAGEN 317; /note="F->A: Abolishes interaction with histones H3 and H4."; /evidence="ECO:0000269|PubMed:23075851"; MUTAGEN 328; /note="R->A: Abolishes interaction with histones H3 and H4."; /evidence="ECO:0000269|PubMed:23075851"; MUTAGEN 331; /note="D->A: Abolishes interaction with histones H3 and H4."; /evidence="ECO:0000269|PubMed:23075851"; MUTAGEN 630; /note="K->A: Abolishes sumoylation; when associated with A-631."; /evidence="ECO:0000269|PubMed:12150977"; MUTAGEN 631; /note="K->A: Abolishes sumoylation; when associated with A-630."; /evidence="ECO:0000269|PubMed:12150977"; MUTAGEN 668; /note="S->A: No translocation to the cytosol upon glucose deprivation."; /evidence="ECO:0000269|PubMed:12968034"; MUTAGEN 671; /note="S->A: No effect on cytosol translocation. upon glucose deprivation."; /evidence="ECO:0000269|PubMed:12968034"; MUTAGEN 733..740; /note="Missing: Abolishes sumoylation."; /evidence="ECO:0000269|PubMed:17081986
uniprot
proteins
post_translational_modification
PTM: Sumoylated with SUMO1 on multiple lysine residues. {ECO:0000269|PubMed:11842083, ECO:0000269|PubMed:12150977, ECO:0000269|PubMed:17081986}.; PTM: Phosphorylated by HIPK1 upon glucose deprivation. {ECO:0000269|PubMed:10393185, ECO:0000269|PubMed:12140263, ECO:0000269|PubMed:12968034}.; PTM: 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. {ECO:0000269|PubMed:16524876, ECO:0000269|PubMed:20153724}.
uniprot
proteins
protein_family
DAXX family
uniprot
proteins
pubmed
10393185
uniprot
proteins
pubmed
10669754
uniprot
proteins
pubmed
10684855
uniprot
proteins
pubmed
10698492
uniprot
proteins
pubmed
11003656
uniprot
proteins
pubmed
11483955
uniprot
proteins
pubmed
11495919
uniprot
proteins
pubmed
11842083
uniprot
proteins
pubmed
11907324
uniprot
proteins
pubmed
11948183
uniprot
proteins
pubmed
12140263
uniprot
proteins
pubmed
12150977
uniprot
proteins
pubmed
12529400
uniprot
proteins
pubmed
12953102
uniprot
proteins
pubmed
12968034
uniprot
proteins
pubmed
14557665
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
14678985
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14990586
uniprot
proteins
pubmed
15016915
uniprot
proteins
pubmed
15240113
uniprot
proteins
pubmed
15364927
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16524876
uniprot
proteins
pubmed
16845383
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17081986
uniprot
proteins
pubmed
17210684
uniprot
proteins
pubmed
17942542
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18566590
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18922870
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20153724
uniprot
proteins
pubmed
20444888
uniprot
proteins
pubmed
20504901
uniprot
proteins
pubmed
20651253
uniprot
proteins
pubmed
20927612
uniprot
proteins
pubmed
21134643
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21482821
uniprot
proteins
pubmed
23075851
uniprot
proteins
pubmed
23142979
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23222847
uniprot
proteins
pubmed
24200965
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24530302
uniprot
proteins
pubmed
25275136
uniprot
proteins
pubmed
27211601
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
9215629
uniprot
proteins
pubmed
9407001
uniprot
proteins
pubmed
9545376
uniprot
proteins
pubmed
9645950
uniprot
proteins
sequence_length
740
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11495919, ECO:0000269|PubMed:11842083, ECO:0000269|PubMed:12968034, ECO:0000269|PubMed:9407001}. Nucleus, nucleoplasm {ECO:0000269|PubMed:10669754, ECO:0000269|PubMed:16845383, ECO:0000269|PubMed:18566590, ECO:0000269|PubMed:23222847, ECO:0000269|PubMed:9407001}. Nucleus, PML body {ECO:0000269|PubMed:10669754, ECO:0000269|PubMed:11842083, ECO:0000269|PubMed:14990586, ECO:0000269|PubMed:17081986, ECO:0000269|PubMed:21482821, ECO:0000269|PubMed:23222847, ECO:0000269|PubMed:24200965, ECO:0000269|PubMed:25275136}. Nucleus, nucleolus {ECO:0000269|PubMed:23222847}. Chromosome, centromere {ECO:0000269|PubMed:24200965, ECO:0000269|PubMed:9645950}. Note=Dispersed throughout the nucleoplasm, in PML/POD/ND10 nuclear bodies, and in nucleoli (Probable). Colocalizes with histone H3.3, ATRX, HIRA and ASF1A at PML-nuclear bodies (PubMed:12953102, PubMed:14990586, PubMed:23222847, PubMed:24200965). Colocalizes with a subset of interphase centromeres, but is absent from mitotic centromeres (PubMed:9645950). Detected in cytoplasmic punctate structures (PubMed:11842083). Translocates from the nucleus to the cytoplasm upon glucose deprivation or oxidative stress (PubMed:12968034). Colocalizes with RASSF1 in the nucleus (PubMed:18566590). Colocalizes with USP7 in nucleoplasma with accumulation in speckled structures (PubMed:16845383). {ECO:0000269|PubMed:11842083, ECO:0000269|PubMed:12953102, ECO:0000269|PubMed:12968034, ECO:0000269|PubMed:14990586, ECO:0000269|PubMed:16845383, ECO:0000269|PubMed:18566590, ECO:0000269|PubMed:23222847, ECO:0000269|PubMed:24200965, ECO:0000269|PubMed:9645950, ECO:0000305|PubMed:10669754}.; SUBCELLULAR LOCATION: [Isoform beta]: Nucleus {ECO:0000269|PubMed:21482821}. Note=Diffuse nuclear distribution pattern and no comparable dot-like accumulation of isoform 1. {ECO:0000269|PubMed:21482821}.; SUBCELLULAR LOCATION: [Isoform gamma]: Nucleus {ECO:0000269|PubMed:21482821}. Note=Diffuse nuclear distribution pattern and no comparable dot-like accumulation of isoform 1. {ECO:0000269|PubMed:21482821}.
uniprot
proteins