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Q9UER7 (DAXX_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length740 AA.
Sequence statusComplete.
Protein existenceEvidence 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, CENPC, 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.42 Ref.46

Subcellular location

Cytoplasm. Nucleusnucleoplasm. NucleusPML body. Nucleusnucleolus. Chromosomecentromere. 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.41

Sequence similarities

Belongs to the DAXX family.

Ontologies

Keywords
   Biological processApoptosis
Host-virus interaction
Transcription
Transcription regulation
   Cellular componentCentromere
Chromosome
Cytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
   Molecular functionRepressor
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of JUN kinase activity

Traceable author statement Ref.1. Source: ProtInc

androgen receptor signaling pathway

Inferred from direct assay PubMed 15572661. Source: UniProtKB

apoptotic process

Traceable author statement PubMed 15572661. Source: UniProtKB

extrinsic apoptotic signaling pathway via death domain receptors

Traceable author statement Ref.1. Source: ProtInc

mitotic cytokinesis

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 15572661Ref.5. Source: UniProtKB

positive regulation of apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

regulation of protein ubiquitination

Inferred from direct assay Ref.33. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from direct assay PubMed 15878163. Source: MGI

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentPML body

Inferred from direct assay Ref.33Ref.14. Source: UniProtKB

chromosome, centromeric region

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Traceable author statement PubMed 15572661. Source: UniProtKB

cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

heterochromatin

Inferred from electronic annotation. Source: Ensembl

nucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay PubMed 15572661. Source: UniProtKB

   Molecular_functionandrogen receptor binding

Inferred from physical interaction PubMed 15572661. Source: UniProtKB

enzyme binding

Inferred from physical interaction Ref.31. Source: UniProtKB

heat shock protein binding

Traceable author statement PubMed 15572661. Source: UniProtKB

p53 binding

Inferred from physical interaction Ref.31. Source: UniProtKB

protein N-terminus binding

Inferred from physical interaction PubMed 15572661Ref.33. 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

ubiquitin protein ligase binding

Inferred from physical interaction Ref.31. Source: UniProtKB

Complete GO annotation...

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 740740Death domain-associated protein 6
PRO_0000151258

Regions

Region1 – 160160Necessary for interaction with USP7
Region347 – 570224Necessary for interaction with USP7
Region501 – 625125Interaction with MAP3K5
Region626 – 740115Interaction with SPOP
Region733 – 7408Sumo interaction motif (SIM)
Coiled coil180 – 21738 Potential
Coiled coil358 – 39942 Potential
Coiled coil430 – 48960 Potential
Motif391 – 3955Nuclear localization signal Potential
Motif628 – 6347Nuclear localization signal Potential
Compositional bias11 – 166Poly-Asp
Compositional bias434 – 572139Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue1781Phosphoserine Ref.37
Modified residue2131Phosphoserine Ref.37
Modified residue4591Phosphothreonine By similarity
Modified residue4951Phosphoserine Ref.37 Ref.43 Ref.45
Modified residue5121N6-acetyllysine Ref.40
Modified residue6681Phosphoserine Ref.23 Ref.37
Modified residue6711Phosphoserine Ref.34 Ref.37
Modified residue6881Phosphoserine Ref.37
Modified residue7021Phosphoserine Ref.30 Ref.34 Ref.37 Ref.39 Ref.43 Ref.45
Modified residue7371Phosphoserine Ref.37 Ref.39 Ref.43
Modified residue7391Phosphoserine Ref.37 Ref.39 Ref.43
Cross-link630Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)
Cross-link631Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)

Natural variations

Alternative sequence1 – 7575Missing in isoform 3.
VSP_045588
Alternative sequence696 – 74045SSLCI…LSDSD → PAKNLGRRRSKQDQG in isoform 2.
VSP_001270

Experimental info

Mutagenesis6301K → A: Abolishes sumoylation; when associated with A-631. Ref.18
Mutagenesis6311K → A: Abolishes sumoylation; when associated with A-630. Ref.18
Mutagenesis6681S → A: No translocation to the cytosol upon glucose deprivation. Ref.23
Mutagenesis6711S → A: No effect on cytosol translocation. upon glucose deprivation. Ref.23
Mutagenesis733 – 7408Missing: Abolishes sumoylation. Ref.29
Sequence conflict1771Q → R in AAB66585. Ref.2
Sequence conflict2631R → H in AAC72843. Ref.5
Sequence conflict3231R → W in AAB66585. Ref.2
Sequence conflict3651R → Q in AAB66585. Ref.2
Sequence conflict3821L → S in AAB66585. Ref.2
Sequence conflict5051E → G in BAG64795. Ref.7
Sequence conflict6471S → R in CAB09986. Ref.9
Sequence conflict6471S → R in CAB09989. Ref.9
Sequence conflict7221T → A in CAB09986. Ref.9
Sequence conflict7221T → A in CAB09989. Ref.9
Sequence conflict731 – 7322EE → KK in AAC72843. Ref.5

Secondary structure

....................................... 740
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 2002. Version 2.
Checksum: 1B309ADDAA878040

FASTA74081,373
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 47E099676EB7315C
Show »

FASTA71078,333
Isoform 3 [UniParc].

Checksum: 11AF08F83A462073
Show »

FASTA66573,589

References

« Hide '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 CENPC, 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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[38]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[39]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[40]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[41]"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.
[42]"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.
[43]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[44]"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].
[45]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[46]"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.
[47]"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.

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.
PIRT03847.
RefSeqNP_001135441.1. NM_001141969.1.
NP_001241646.1. NM_001254717.1.
NP_001341.1. NM_001350.4.
UniGeneHs.336916.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
DisProtDP00707.
ProteinModelPortalQ9UER7.
SMRQ9UER7. Positions 52-144, 182-386.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107985. 103 interactions.
DIPDIP-27628N.
IntActQ9UER7. 60 interactions.
MINTMINT-122943.
STRING9606.ENSP00000266000.

PTM databases

PhosphoSiteQ9UER7.

Polymorphism databases

DMDM24636785.

Proteomic databases

PaxDbQ9UER7.
PeptideAtlasQ9UER7.
PRIDEQ9UER7.

Protocols and materials databases

DNASU1616.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000266000; 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]
GeneID1616.
KEGGhsa:1616.
UCSCuc003oec.3. human. [Q9UER7-1]

Organism-specific databases

CTD1616.
GeneCardsGC06M033286.
GC06Mj33207.
GC06Mk33264.
GC06Mm33456.
GC06Mn33215.
HGNCHGNC:2681. DAXX.
HPACAB002224.
CAB025546.
HPA008736.
HPA008797.
MIM603186. gene.
neXtProtNX_Q9UER7.
PharmGKBPA27148.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG39676.
HOGENOMHOG000112148.
HOVERGENHBG031495.
InParanoidQ9UER7.
KOK02308.
OMAEQMQEGQ.
PhylomeDBQ9UER7.
TreeFamTF325803.

Enzyme and pathway databases

SignaLinkQ9UER7.

Gene expression databases

ArrayExpressQ9UER7.
BgeeQ9UER7.
CleanExHS_DAXX.
GenevestigatorQ9UER7.

Family and domain databases

InterProIPR005012. Daxx.
[Graphical view]
PANTHERPTHR12766. PTHR12766. 1 hit.
PfamPF03344. Daxx. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDAXX. human.
EvolutionaryTraceQ9UER7.
GeneWikiDeath-associated_protein_6.
GenomeRNAi1616.
NextBio6638.
PROQ9UER7.
SOURCESearch...

Entry information

Entry nameDAXX_HUMAN
AccessionPrimary (citable) accession number: Q9UER7
Secondary accession number(s): B4E1I3 expand/collapse secondary AC list , F5H082, O14747, O15141, O15208, Q5STK9, Q9BWI3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: November 1, 2002
Last modified: April 16, 2014
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM