Q9UER7 (DAXX_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	DAXX
Synonyms:	BING2, DAP6

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	740 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Transcription corepressor known to repress transcriptional potential of several sumoylated transcription factors. 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. 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. Seems to regulate transcription in PML/POD/ND10 nuclear bodies together with PML and may influence TNFRSF6-dependent apoptosis thereby. Down-regulates basal and activated transcription. Seems to act as a transcriptional corepressor and inhibits PAX3 and ETS1 through direct protein-protein interaction. Modulates PAX5 activity. 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. Shows restriction activity towards human cytomegalovirus (HCMV). Ref.21 Ref.26 Ref.29 Ref.31 Ref.35
Subunit structure	Homomultimer. Binds to the TNFRSF6 death domain via its C-terminus and to PAX5. Binds to SLC2A4/GLUT4, MAP3K5, TGFBR2, phosphorylated dimeric HSPB1/HSP27, CENPC1, ETS1, sumoylated PML, UBE2I and MCRS1. Is part of a complex containing PAX5 and CREBBP. Interacts with HIPK2 and HIPK3 via its N-terminus. Interacts with HIPK1, which induces translocation from PML/POD/ND10 nuclear bodies to chromatin and enhances association with HDAC1 By similarity. The non-phosphorylated form binds to PAX3, PAX7, DEK, HDAC1, HDAC2, HDAC3, acetylated histone H4 and histones H2A, H2B, H3 and H4. Interacts with SPOP. Part of a complex consisting of DAXX, CUL3 and SPOP. 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 HCMV tegument phosphoprotein pp71. Part of a complex with MDM2, DAXX, RASSF1 and USP7. Part of a complex with DAXX, MDM2 and USP7. Interacts (via N-terminus) with RASSF1 (via C-terminus); the interaction is independent of MDM2 and TP53. Interacts with MDM2; the interaction is direct. Interacts with USP7; the interaction is direct and independent of MDM2 and TP53. Interacts with TP53. Interacts with human cytomegalovirus/HHV-5 protein UL123. Ref.3 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.28 Ref.29 Ref.31 Ref.32 Ref.33 Ref.36 Ref.41 Ref.45
Subcellular location	Cytoplasm. Nucleus › nucleoplasm. Nucleus › PML body. Nucleus › nucleolus. Chromosome › centromere. Note: Dispersed throughout the nucleoplasm, in PML/POD/ND10 nuclear bodies, and in nucleoli. Colocalizes with a subset of interphase centromeres, but is absent from mitotic centromeres. Detected in cytoplasmic punctate structures. Translocates from the nucleus to the cytoplasm upon glucose deprivation or oxidative stress. Colocalizes with RASSF1 in the nucleus. Colocalizes with USP7 in nucleoplasma with accumulation in speckled structures. Ref.2 Ref.3 Ref.14 Ref.16 Ref.19 Ref.23 Ref.29 Ref.31 Ref.33
Tissue specificity	Ubiquitous.
Induction	Upon mitogenic stimulation by concanavalin-A.
Domain	The Sumo interaction motif mediates Sumo binding, and is required both for sumoylation and binding to sumoylated targets.
Post-translational modification	Sumoylated with SUMO1 on multiple lysine residues. Ref.18 Ref.19 Ref.29 Phosphorylated by HIPK1 upon glucose deprivation. Ref.12 Ref.21 Ref.23 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. Ref.28 Ref.40
Sequence similarities	Belongs to the DAXX family.

Ontologies

Keywords
Biological process	Apoptosis Host-virus interaction Transcription Transcription regulation
Cellular component	Centromere Chromosome Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Domain	Coiled coil
Molecular function	Repressor
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	activation of JUN kinase activity Traceable author statement Ref.1. Source: ProtInc androgen receptor signaling pathway Inferred from direct assay PubMed 15572661. Source: UniProtKB cytokinesis after mitosis Inferred from electronic annotation. Source: Compara extrinsic apoptotic signaling pathway via death domain receptors Traceable author statement Ref.1. Source: ProtInc induction of apoptosis Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of transcription, DNA-dependent Inferred from direct assay PubMed 15572661Ref.5. Source: UniProtKB regulation of protein ubiquitination Inferred from direct assay Ref.33. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	PML body Inferred from direct assay Ref.33Ref.14. Source: UniProtKB chromosome, centromeric region Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Inferred from sequence or structural similarity. Source: UniProtKB heterochromatin Inferred from electronic annotation. Source: Compara nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	heat shock protein binding Traceable author statement PubMed 15572661. Source: UniProtKB protein homodimerization activity Inferred from direct assay Ref.5. Source: UniProtKB receptor signaling protein activity Traceable author statement Ref.1. Source: ProtInc transcription factor binding Inferred from direct assay Ref.5. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	P03243	4	EBI-77321,EBI-1561361	From a different organism.
AIRE	O43918	5	EBI-77321,EBI-1753081
AR	P10275	5	EBI-77321,EBI-608057
ATRX	P46100	3	EBI-77321,EBI-396461
CDKN2A	Q8N726	8	EBI-77321,EBI-625922
CREBBP	Q92793	2	EBI-77321,EBI-81215
E1B	P03244	4	EBI-77321,EBI-1561155	From a different organism.
ETS1	P14921-1	3	EBI-287635,EBI-913224
ETS1	P14921-2	2	EBI-287635,EBI-913228
FAS	P25445	2	EBI-77321,EBI-494743
Fas	P25446	4	EBI-77321,EBI-296206	From a different organism.
FTH1	P02794	5	EBI-77321,EBI-713259
HDAC1	Q13547	2	EBI-77321,EBI-301834
HDAC2	Q92769	2	EBI-77321,EBI-301821
Hipk1	O88904	3	EBI-77321,EBI-692945	From a different organism.
HSPB1	P04792	3	EBI-77321,EBI-352682
HSPB1	P15991	3	EBI-77321,EBI-1559114	From a different organism.
MAP3K5	Q99683	6	EBI-77321,EBI-476263
MCRS1	Q96EZ8	7	EBI-77321,EBI-348259
MDM2	Q00987	14	EBI-77321,EBI-389668
PARK7	Q99497	3	EBI-77321,EBI-1164361
Pax5	Q02650	4	EBI-77321,EBI-296260	From a different organism.
PML	P29590	6	EBI-77321,EBI-295890
SLC2A4	P14672	7	EBI-77321,EBI-367146
SPOP	O43791	5	EBI-77321,EBI-743549
STAT3	P40763	4	EBI-77321,EBI-518675
SUMO1	P63165	5	EBI-77321,EBI-80140
TCF7L2	Q9NQB0	5	EBI-77321,EBI-924724
TGFBR2	P37173	2	EBI-77321,EBI-296151
TP53	P04637	11	EBI-77321,EBI-366083
TSG101	Q99816	4	EBI-77321,EBI-346882
USP7	Q93009	10	EBI-77321,EBI-302474

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9UER7-1)

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.

Isoform 2 (identifier: Q9UER7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     696-740: SSLCIPSPARLSQTPHSQPPRPGTCKTSVATQCDPEEIIVLSDSD → PAKNLGRRRSKQDQG

Note: No experimental confirmation available.

Isoform 3 (identifier: Q9UER7-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-75: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 740

740

Death domain-associated protein 6

PRO_0000151258

Regions

Region

1 – 160

160

Necessary for interaction with USP7

Region

347 – 570

224

Necessary for interaction with USP7

Region

501 – 625

125

Interaction with MAP3K5

Region

626 – 740

115

Interaction with SPOP

Region

733 – 740

8

Sumo interaction motif (SIM)

Coiled coil

180 – 217

38

Potential

Coiled coil

358 – 399

42

Potential

Coiled coil

430 – 489

60

Potential

Motif

391 – 395

5

Nuclear localization signal Potential

Motif

628 – 634

7

Nuclear localization signal Potential

Compositional bias

11 – 16

6

Poly-Asp

Compositional bias

434 – 572

139

Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue

178

1

Phosphoserine Ref.37

Modified residue

213

1

Phosphoserine Ref.37

Modified residue

459

1

Phosphothreonine By similarity

Modified residue

495

1

Phosphoserine Ref.37 Ref.42 Ref.44

Modified residue

512

1

N6-acetyllysine Ref.39

Modified residue

668

1

Phosphoserine Ref.23 Ref.37

Modified residue

671

1

Phosphoserine Ref.34 Ref.37

Modified residue

688

1

Phosphoserine Ref.37

Modified residue

702

1

Phosphoserine Ref.30 Ref.34 Ref.37 Ref.38 Ref.42 Ref.44

Modified residue

737

1

Phosphoserine Ref.37 Ref.38 Ref.42

Modified residue

739

1

Phosphoserine Ref.37 Ref.38 Ref.42

Cross-link

630

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)

Cross-link

631

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)

Natural variations

Alternative sequence

1 – 75

75

Missing in isoform 3.

VSP_045588

Alternative sequence

696 – 740

45

SSLCI…LSDSD → PAKNLGRRRSKQDQG in isoform 2.

VSP_001270

Experimental info

Mutagenesis

630

1

K → A: Abolishes sumoylation; when associated with A-631. Ref.18

Mutagenesis

631

1

K → A: Abolishes sumoylation; when associated with A-630. Ref.18

Mutagenesis

668

1

S → A: No translocation to the cytosol upon glucose deprivation. Ref.23

Mutagenesis

671

1

S → A: No effect on cytosol translocation. upon glucose deprivation. Ref.23

Mutagenesis

733 – 740

8

Missing: Abolishes sumoylation. Ref.29

Sequence conflict

177

1

Q → R in AAB66585. Ref.2

Sequence conflict

263

1

R → H in AAC72843. Ref.5

Sequence conflict

323

1

R → W in AAB66585. Ref.2

Sequence conflict

365

1

R → Q in AAB66585. Ref.2

Sequence conflict

382

1

L → S in AAB66585. Ref.2

Sequence conflict

505

1

E → G in BAG64795. Ref.7

Sequence conflict

647

1

S → R in CAB09986. Ref.9

Sequence conflict

647

1

S → R in CAB09989. Ref.9

Sequence conflict

722

1

T → A in CAB09986. Ref.9

Sequence conflict

722

1

T → A in CAB09989. Ref.9

Sequence conflict

731 – 732

2

EE → KK in AAC72843. Ref.5

Secondary structure

1

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740

Helix Strand Turn

Details...

Helix

60 – 77

18

Turn

78 – 80

3

Helix

84 – 93

10

Helix

97 – 100

4

Helix

103 – 118

16

Helix

120 – 122

3

Helix

123 – 136

14

Beta strand

138 – 140

3

Helix

185 – 206

22

Helix

214 – 216

3

Helix

221 – 242

22

Helix

252 – 254

3

Helix

265 – 275

11

Beta strand

278 – 280

3

Helix

286 – 299

14

Helix

306 – 333

28

Helix

339 – 341

3

Helix

346 – 348

3

Helix

350 – 353

4

Helix

355 – 384

30

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 2002. Version 2. Checksum: 1B309ADDAA878040	FASTA	740	81,373
	10 20 30 40 50 60 MATANSIIVL DDDDEDEAAA QPGPSHPLPN AASPGAEAPS SSEPHGARGS SSSGGKKCYK 70 80 90 100 110 120 LENEKLFEEF LELCKMQTAD HPEVVPFLYN RQQRAHSLFL ASAEFCNILS RVLSRARSRP 130 140 150 160 170 180 AKLYVYINEL CTVLKAHSAK KKLNLAPAAT TSNEPSGNNP PTHLSLDPTN AENTASQSPR 190 200 210 220 230 240 TRGSRRQIQR LEQLLALYVA EIRRLQEKEL DLSELDDPDS AYLQEARLKR KLIRLFGRLC 250 260 270 280 290 300 ELKDCSSLTG RVIEQRIPYR GTRYPEVNRR IERLINKPGP DTFPDYGDVL RAVEKAAARH 310 320 330 340 350 360 SLGLPRQQLQ LMAQDAFRDV GIRLQERRHL DLIYNFGCHL TDDYRPGVDP ALSDPVLARR 370 380 390 400 410 420 LRENRSLAMS RLDEVISKYA MLQDKSEEGE RKKRRARLQG TSSHSADTPE ASLDSGEGPS 430 440 450 460 470 480 GMASQGCPSA SRAETDDEDD EESDEEEEEE EEEEEEEATD SEEEEDLEQM QEGQEDDEEE 490 500 510 520 530 540 DEEEEAAAGK DGDKSPMSSL QISNEKNLEP GKQISRSSGE QQNKGRIVSP SLLSEEPLAP 550 560 570 580 590 600 SSIDAESNGE QPEELTLEEE SPVSQLFELE IEALPLDTPS SVETDISSSR KQSEEPFTTV 610 620 630 640 650 660 LENGAGMVSS TSFNGGVSPH NWGDSGPPCK KSRKEKKQTG SGPLGNSYVE RQRSVHEKNG 670 680 690 700 710 720 KKICTLPSPP SPLASLAPVA DSSTRVDSPS HGLVTSSLCI PSPARLSQTP HSQPPRPGTC 730 740 KTSVATQCDP EEIIVLSDSD
	Isoform 2 [UniParc]. Checksum: 47E099676EB7315C	FASTA	710	78,333
	10 20 30 40 50 60 MATANSIIVL DDDDEDEAAA QPGPSHPLPN AASPGAEAPS SSEPHGARGS SSSGGKKCYK 70 80 90 100 110 120 LENEKLFEEF LELCKMQTAD HPEVVPFLYN RQQRAHSLFL ASAEFCNILS RVLSRARSRP 130 140 150 160 170 180 AKLYVYINEL CTVLKAHSAK KKLNLAPAAT TSNEPSGNNP PTHLSLDPTN AENTASQSPR 190 200 210 220 230 240 TRGSRRQIQR LEQLLALYVA EIRRLQEKEL DLSELDDPDS AYLQEARLKR KLIRLFGRLC 250 260 270 280 290 300 ELKDCSSLTG RVIEQRIPYR GTRYPEVNRR IERLINKPGP DTFPDYGDVL RAVEKAAARH 310 320 330 340 350 360 SLGLPRQQLQ LMAQDAFRDV GIRLQERRHL DLIYNFGCHL TDDYRPGVDP ALSDPVLARR 370 380 390 400 410 420 LRENRSLAMS RLDEVISKYA MLQDKSEEGE RKKRRARLQG TSSHSADTPE ASLDSGEGPS 430 440 450 460 470 480 GMASQGCPSA SRAETDDEDD EESDEEEEEE EEEEEEEATD SEEEEDLEQM QEGQEDDEEE 490 500 510 520 530 540 DEEEEAAAGK DGDKSPMSSL QISNEKNLEP GKQISRSSGE QQNKGRIVSP SLLSEEPLAP 550 560 570 580 590 600 SSIDAESNGE QPEELTLEEE SPVSQLFELE IEALPLDTPS SVETDISSSR KQSEEPFTTV 610 620 630 640 650 660 LENGAGMVSS TSFNGGVSPH NWGDSGPPCK KSRKEKKQTG SGPLGNSYVE RQRSVHEKNG 670 680 690 700 710 KKICTLPSPP SPLASLAPVA DSSTRVDSPS HGLVTPAKNL GRRRSKQDQG
	Isoform 3 [UniParc]. Checksum: 11AF08F83A462073	FASTA	665	73,589
	10 20 30 40 50 60 MQTADHPEVV PFLYNRQQRA HSLFLASAEF CNILSRVLSR ARSRPAKLYV YINELCTVLK 70 80 90 100 110 120 AHSAKKKLNL APAATTSNEP SGNNPPTHLS LDPTNAENTA SQSPRTRGSR RQIQRLEQLL 130 140 150 160 170 180 ALYVAEIRRL QEKELDLSEL DDPDSAYLQE ARLKRKLIRL FGRLCELKDC SSLTGRVIEQ 190 200 210 220 230 240 RIPYRGTRYP EVNRRIERLI NKPGPDTFPD YGDVLRAVEK AAARHSLGLP RQQLQLMAQD 250 260 270 280 290 300 AFRDVGIRLQ ERRHLDLIYN FGCHLTDDYR PGVDPALSDP VLARRLRENR SLAMSRLDEV 310 320 330 340 350 360 ISKYAMLQDK SEEGERKKRR ARLQGTSSHS ADTPEASLDS GEGPSGMASQ GCPSASRAET 370 380 390 400 410 420 DDEDDEESDE EEEEEEEEEE EEATDSEEEE DLEQMQEGQE DDEEEDEEEE AAAGKDGDKS 430 440 450 460 470 480 PMSSLQISNE KNLEPGKQIS RSSGEQQNKG RIVSPSLLSE EPLAPSSIDA ESNGEQPEEL 490 500 510 520 530 540 TLEEESPVSQ LFELEIEALP LDTPSSVETD ISSSRKQSEE PFTTVLENGA GMVSSTSFNG 550 560 570 580 590 600 GVSPHNWGDS GPPCKKSRKE KKQTGSGPLG NSYVERQRSV HEKNGKKICT LPSPPSPLAS 610 620 630 640 650 660 LAPVADSSTR VDSPSHGLVT SSLCIPSPAR LSQTPHSQPP RPGTCKTSVA TQCDPEEIIV LSDSD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Daxx, a novel Fas-binding protein that activates JNK and apoptosis." Yang X., Khosravi-Far R., Chang H.Y., Baltimore D. Cell 89:1067-1076(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Cloning and expression of primate Daxx cDNAs and mapping of the human gene to chromosome 6p21.3 in the MHC region." Kiriakidou M., Driscoll D.A., Lopez-Guisa J.M., Strauss J.F. III DNA Cell Biol. 16:1289-1298(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION. Tissue: Placenta.
[3]	"Interphase-specific association of intrinsic centromere protein CENP-C with HDaxx, a death domain-binding protein implicated in Fas-mediated cell death." Pluta A.F., Earnshaw W.C., Goldberg I.G. J. Cell Sci. 111:2029-2041(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH CENPC1, SUBCELLULAR LOCATION. Tissue: Cervix carcinoma.
[4]	"TAPASIN, DAXX, RGL2, HKE2 and four new genes (BING 1, 3 to 5) form a dense cluster at the centromeric end of the MHC." Herberg J.A., Beck S., Trowsdale J. J. Mol. Biol. 277:839-857(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
[5]	"EAP1/Daxx interacts with ETS1 and represses transcriptional activation of ETS1 target genes." Li R., Pei H., Watson D.K., Papas T.S. Oncogene 19:745-753(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: T-cell.
[6]	Usui T. Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[7]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Trachea.
[8]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[9]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 334-740 (ISOFORM 2). Tissue: Eye.
[12]	"The Pax3-FKHR oncoprotein is unresponsive to the Pax3-associated repressor hDaxx." Hollenbach A.D., Sublett J.E., McPherson C.J., Grosveld G. EMBO J. 18:3702-3711(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PAX3 AND PAX7, PHOSPHORYLATION.
[13]	"Promyelocytic leukemia protein (PML) and Daxx participate in a novel nuclear pathway for apoptosis." Zhong S., Salomoni P., Ronchetti S., Guo A., Ruggero D., Pandolfi P.P. J. Exp. Med. 191:631-640(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PML.
[14]	"Sequestration and inhibition of Daxx-mediated transcriptional repression by PML." Li H., Leo C., Zhu J., Wu X., O'Neil J., Park E.-J., Chen J.D. Mol. Cell. Biol. 20:1784-1796(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SUMOYLATED PML; HDAC1; HDAC2 AND HDAC3, SUBCELLULAR LOCATION.
[15]	"Inhibition of Daxx-mediated apoptosis by heat shock protein 27." Charette S.J., Lavoie J.N., Lambert H., Landry J. Mol. Cell. Biol. 20:7602-7612(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HSPB1.
[16]	"Apoptosis signal-regulating kinase 1 controls the proapoptotic function of death-associated protein (Daxx) in the cytoplasm." Ko Y.-G., Kang Y.-S., Park H., Seol W., Kim J., Kim T., Park H.-S., Choi E.-J., Kim S. J. Biol. Chem. 276:39103-39106(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MAP3K5, SUBCELLULAR LOCATION.
[17]	"TGF-beta-induced apoptosis is mediated by the adapter protein Daxx that facilitates JNK activation." Perlman R., Schiemann W.P., Brooks M.W., Lodish H.F., Weinberg R.A. Nat. Cell Biol. 3:708-714(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TGFBR2.
[18]	"Modification of Daxx by small ubiquitin-related modifier-1." Jang M.-S., Ryu S.-W., Kim E. Biochem. Biophys. Res. Commun. 295:495-500(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SUMOYLATION, MUTAGENESIS OF LYS-630 AND LYS-631.
[19]	"The insulin-sensitive glucose transporter, GLUT4, interacts physically with Daxx. Two proteins with capacity to bind Ubc9 and conjugated to SUMO1." Lalioti V.S., Vergarajauregui S., Pulido D., Sandoval I.V. J. Biol. Chem. 277:19783-19791(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SLC2A4 AND UBE2I, SUMOYLATION, SUBCELLULAR LOCATION.
[20]	"Essential role of the 58-kDa microspherule protein in the modulation of Daxx-dependent transcriptional repression as revealed by nucleolar sequestration." Lin D.-Y., Shih H.-M. J. Biol. Chem. 277:25446-25456(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MCRS1.
[21]	"Daxx and histone deacetylase II associate with chromatin through an interaction with core histones and the chromatin-associated protein Dek." Hollenbach A.D., McPherson C.J., Mientjes E.J., Iyengar R., Grosveld G. J. Cell Sci. 115:3319-3330(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION, INTERACTION WITH HDAC2; HISTONES AND DEK.
[22]	"HIPK2 regulates transforming growth factor-beta-induced c-Jun NH(2)-terminal kinase activation and apoptosis in human hepatoma cells." Hofmann T.G., Stollberg N., Schmitz M.L., Will H. Cancer Res. 63:8271-8277(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HIPK2.
[23]	"Role of the ASK1-SEK1-JNK1-HIPK1 signal in Daxx trafficking and ASK1 oligomerization." Song J.J., Lee Y.J. J. Biol. Chem. 278:47245-47252(2003) [PubMed] [Europe PMC] [Abstract] Cited for: OLIGOMERIZATION, SUBCELLULAR LOCATION, INTERACTION WITH MAP3K5, MUTAGENESIS OF SER-668 AND SER-671, PHOSPHORYLATION AT SER-668.
[24]	"Homeodomain-interacting protein kinase 1 modulates Daxx localization, phosphorylation, and transcriptional activity." Ecsedy J.A., Michaelson J.S., Leder P. Mol. Cell. Biol. 23:950-960(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HIPK1.
[25]	"Daxx-mediated transcriptional repression of MMP1 gene is reversed by SPOP." La M., Kim K., Park J., Won J., Lee J.-H., Fu Y.M., Meadows G.G., Joe C.O. Biochem. Biophys. Res. Commun. 320:760-765(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SPOP.
[26]	"Negative regulation of p53 functions by Daxx and the involvement of MDM2." Zhao L.Y., Liu J., Sidhu G.S., Niu Y., Liu Y., Wang R., Liao D. J. Biol. Chem. 279:50566-50579(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH MDM2 AND TP53.
[27]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[28]	"BTB domain-containing speckle-type POZ protein (SPOP) serves as an adaptor of Daxx for ubiquitination by Cul3-based ubiquitin ligase." Kwon J.E., La M., Oh K.H., Oh Y.M., Kim G.R., Seol J.H., Baek S.H., Chiba T., Tanaka K., Bang O.S., Joe C.O., Chung C.H. J. Biol. Chem. 281:12664-12672(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH CUL3 AND SPOP, UBIQUITINATION.
[29]	"Role of SUMO-interacting motif in Daxx SUMO modification, subnuclear localization, and repression of sumoylated transcription factors." Lin D.Y., Huang Y.S., Jeng J.C., Kuo H.Y., Chang C.C., Chao T.T., Ho C.C., Chen Y.C., Lin T.P., Fang H.I., Hung C.C., Suen C.S., Hwang M.J., Chang K.S., Maul G.G., Shih H.M. Mol. Cell 24:341-354(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, SUMOYLATION, SUMO INTERACTION MOTIF, MUTAGENESIS OF 733-ILE--ASP-740.
[30]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-702, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[31]	"Critical role for Daxx in regulating Mdm2." Tang J., Qu L.K., Zhang J., Wang W., Michaelson J.S., Degenhardt Y.Y., El-Deiry W.S., Yang X. Nat. Cell Biol. 8:855-862(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH MDM2 AND USP7, INTERACTION WITH MDM2; TP53 AND USP7, SUBCELLULAR LOCATION.
[32]	"Daxx cooperates with the Axin/HIPK2/p53 complex to induce cell death." Li Q., Wang X., Wu X., Rui Y., Liu W., Wang J., Wang X., Liou Y.C., Ye Z., Lin S.C. Cancer Res. 67:66-74(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH AXIN1.
[33]	"The tumour suppressor RASSF1A promotes MDM2 self-ubiquitination by disrupting the MDM2-DAXX-HAUSP complex." Song M.S., Song S.J., Kim S.Y., Oh H.J., Lim D.S. EMBO J. 27:1863-1874(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH MDM2; RASSF1 AND USP7, INTERACTION WITH RASSF1; USP7 AND MDM2, SUBCELLULAR LOCATION.
[34]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-671 AND SER-702, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[35]	"Nuclear domain 10 components promyelocytic leukemia protein and hDaxx independently contribute to an intrinsic antiviral defense against human cytomegalovirus infection." Tavalai N., Papior P., Rechter S., Stamminger T. J. Virol. 82:126-137(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN HCMV RESTRICTION.
[36]	"Human cytomegalovirus protein pp71 displaces the chromatin-associated factor ATRX from nuclear domain 10 at early stages of infection." Lukashchuk V., McFarlane S., Everett R.D., Preston C.M. J. Virol. 82:12543-12554(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HCMV PP71.
[37]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178; SER-213; SER-495; SER-668; SER-671; SER-688; SER-702; SER-737 AND SER-739, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[38]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-702; SER-737 AND SER-739, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[39]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-512, MASS SPECTROMETRY.
[40]	"Daxx is reciprocally regulated by Mdm2 and Hausp." Tang J., Qu L., Pang M., Yang X. Biochem. Biophys. Res. Commun. 393:542-545(2010) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION, DEUBIQUITINATION BY USP7.
[41]	"Human cytomegalovirus IE72 protein interacts with the transcriptional repressor hDaxx to regulate LUNA gene expression during lytic infection." Reeves M., Woodhall D., Compton T., Sinclair J. J. Virol. 84:7185-7194(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HHV-5 PROTEIN UL123.
[42]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495; SER-702; SER-737 AND SER-739, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[43]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[44]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495 AND SER-702, MASS SPECTROMETRY.
[45]	"Structural characterization of the DAXX N-terminal helical bundle domain and its complex with Rassf1C." Escobar-Cabrera E., Lau D.K., Giovinazzi S., Ishov A.M., McIntosh L.P. Structure 18:1642-1653(2010) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 55-144 IN COMPLEX WITH RASSF1, INTERACTION WITH RASSF1.
[46]	"NMR chemical shift assignments of a complex between SUMO-1 and SIM peptide derived from the C-terminus of Daxx." Naik M.T., Chang C.C., Naik N.M., Kung C.C., Shih H.M., Huang T.H. Biomol. NMR. Assign. 5:75-77(2011) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 721-740.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.
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.

IPI

IPI00170867.
IPI00220885.
IPI01009417.

PIR

T03847.

RefSeq

NP_001135441.1. NM_001141969.1.
NP_001241646.1. NM_001254717.1.
NP_001341.1. NM_001350.4.

UniGene

Hs.336916.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2KQS	NMR	-	B	721-740	[»]
2KZS	NMR	-	A	55-144	[»]
2KZU	NMR	-	A	55-144	[»]
4H9N	X-ray	1.95	C	178-389	[»]
4H9O	X-ray	2.05	C	178-389	[»]
4H9P	X-ray	2.20	C	178-389	[»]
4H9Q	X-ray	1.95	C	178-389	[»]
4H9R	X-ray	2.20	C	178-389	[»]
4H9S	X-ray	2.60	E/F	183-398	[»]
4HGA	X-ray	2.80	A	184-390	[»]

ProteinModelPortal

Q9UER7.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-27628N.

IntAct

Q9UER7. 50 interactions.

MINT

MINT-122943.

STRING

9606.ENSP00000266000.

PTM databases

PhosphoSite

Q9UER7.

Polymorphism databases

DMDM

24636785.

Proteomic databases

PaxDb

Q9UER7.

PeptideAtlas

Q9UER7.

PRIDE

Q9UER7.

Protocols and materials databases

DNASU

1616.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000266000; ENSP00000266000; ENSG00000204209.
ENST00000374542; ENSP00000363668; ENSG00000204209.
ENST00000383062; ENSP00000372539; ENSG00000206206.
ENST00000383194; ENSP00000372681; ENSG00000206279.
ENST00000399060; ENSP00000382014; ENSG00000206206.
ENST00000399344; ENSP00000382281; ENSG00000206279.
ENST00000414083; ENSP00000396876; ENSG00000204209.
ENST00000433482; ENSP00000404623; ENSG00000231617.
ENST00000436311; ENSP00000404376; ENSG00000227046.
ENST00000445009; ENSP00000394108; ENSG00000231617.
ENST00000455860; ENSP00000410772; ENSG00000227046.
ENST00000547663; ENSP00000447115; ENSG00000206279.
ENST00000548604; ENSP00000448337; ENSG00000231617.
ENST00000550822; ENSP00000447861; ENSG00000206206.
ENST00000552944; ENSP00000447833; ENSG00000227046.

GeneID

1616.

KEGG

hsa:1616.

UCSC

uc003oec.3. human.

Organism-specific databases

CTD

1616.

GeneCards

GC06M033286.

HGNC

HGNC:2681. DAXX.

HPA

CAB002224.
CAB025546.
HPA008736.

MIM

603186. gene.

neXtProt

NX_Q9UER7.

PharmGKB

PA27148.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG39676.

HOGENOM

HOG000112148.

HOVERGEN

HBG031495.

InParanoid

Q9UER7.

KO

K02308.

OMA

EQMQEGQ.

OrthoDB

EOG41NTMN.

PhylomeDB

Q9UER7.

Enzyme and pathway databases

Pathway_Interaction_DB

hivnefpathway. HIV-1 Nef: Negative effector of Fas and TNF-alpha.
tgfbrpathway. TGF-beta receptor signaling.

Gene expression databases

ArrayExpress

Q9UER7.

Bgee

Q9UER7.

CleanEx

HS_DAXX.

Genevestigator

Q9UER7.

GermOnline

ENSG00000204209. Homo sapiens.

Family and domain databases

InterPro

IPR005012. Daxx.
[Graphical view]

PANTHER

PTHR12766. PTHR12766. 1 hit.

Pfam

PF03344. Daxx. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

DAXX. human.

EvolutionaryTrace

Q9UER7.

GenomeRNAi

1616.

NextBio

6638.

SOURCE

Search...

Entry information

Entry name

DAXX_HUMAN

Accession

Primary (citable) accession number: Q9UER7
Secondary accession number(s): B4E1I3 , F5H082, O14747, O15141, O15208, Q5STK9, Q9BWI3

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 2002
Last sequence update:	November 1, 2002
Last modified:	May 1, 2013
This is version 129 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.