DAXX_HUMAN
ID DAXX_HUMAN Reviewed; 740 AA.
AC Q9UER7; B4E1I3; F5ANJ6; F5ANJ7; F5H082; O14747; O15141; O15208; Q5STK9;
AC Q9BWI3;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 212.
DE RecName: Full=Death domain-associated protein 6;
DE AltName: Full=Daxx;
DE Short=hDaxx;
DE AltName: Full=ETS1-associated protein 1;
DE Short=EAP1;
DE AltName: Full=Fas death domain-associated protein;
GN Name=DAXX; Synonyms=BING2, DAP6;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9215629; DOI=10.1016/s0092-8674(00)80294-9;
RA Yang X., Khosravi-Far R., Chang H.Y., Baltimore D.;
RT "Daxx, a novel Fas-binding protein that activates JNK and apoptosis.";
RL Cell 89:1067-1076(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBCELLULAR LOCATION.
RC TISSUE=Placenta;
RX PubMed=9407001; DOI=10.1089/dna.1997.16.1289;
RA Kiriakidou M., Driscoll D.A., Lopez-Guisa J.M., Strauss J.F. III;
RT "Cloning and expression of primate Daxx cDNAs and mapping of the human gene
RT to chromosome 6p21.3 in the MHC region.";
RL DNA Cell Biol. 16:1289-1298(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH CENPC, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Cervix carcinoma;
RX PubMed=9645950; DOI=10.1242/jcs.111.14.2029;
RA Pluta A.F., Earnshaw W.C., Goldberg I.G.;
RT "Interphase-specific association of intrinsic centromere protein CENP-C
RT with HDaxx, a death domain-binding protein implicated in Fas-mediated cell
RT death.";
RL J. Cell Sci. 111:2029-2041(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX PubMed=9545376; DOI=10.1006/jmbi.1998.1637;
RA Herberg J.A., Beck S., Trowsdale J.;
RT "TAPASIN, DAXX, RGL2, HKE2 and four new genes (BING 1, 3 to 5) form a dense
RT cluster at the centromeric end of the MHC.";
RL J. Mol. Biol. 277:839-857(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=T-cell;
RX PubMed=10698492; DOI=10.1038/sj.onc.1203385;
RA Li R., Pei H., Watson D.K., Papas T.S.;
RT "EAP1/Daxx interacts with ETS1 and represses transcriptional activation of
RT ETS1 target genes.";
RL Oncogene 19:745-753(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BETA AND GAMMA), SUBCELLULAR LOCATION
RP (ISOFORMS BETA AND GAMMA), AND ALTERNATIVE SPLICING.
RC TISSUE=Renal cell carcinoma;
RX PubMed=21482821; DOI=10.1074/jbc.m110.196311;
RA Wethkamp N., Hanenberg H., Funke S., Suschek C.V., Wetzel W., Heikaus S.,
RA Grinstein E., Ramp U., Engers R., Gabbert H.E., Mahotka C.;
RT "Daxx-beta and Daxx-gamma, two novel splice variants of the transcriptional
RT co-repressor Daxx.";
RL J. Biol. Chem. 286:19576-19588(2011).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Usui T.;
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 334-740 (ISOFORM 2).
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [13]
RP INTERACTION WITH PAX3 AND PAX7, AND PHOSPHORYLATION.
RX PubMed=10393185; DOI=10.1093/emboj/18.13.3702;
RA Hollenbach A.D., Sublett J.E., McPherson C.J., Grosveld G.;
RT "The Pax3-FKHR oncoprotein is unresponsive to the Pax3-associated repressor
RT hDaxx.";
RL EMBO J. 18:3702-3711(1999).
RN [14]
RP INTERACTION WITH PML.
RX PubMed=10684855; DOI=10.1084/jem.191.4.631;
RA Zhong S., Salomoni P., Ronchetti S., Guo A., Ruggero D., Pandolfi P.P.;
RT "Promyelocytic leukemia protein (PML) and Daxx participate in a novel
RT nuclear pathway for apoptosis.";
RL J. Exp. Med. 191:631-640(2000).
RN [15]
RP INTERACTION WITH SUMOYLATED PML; HDAC1; HDAC2 AND HDAC3, AND SUBCELLULAR
RP LOCATION.
RX PubMed=10669754; DOI=10.1128/mcb.20.5.1784-1796.2000;
RA Li H., Leo C., Zhu J., Wu X., O'Neil J., Park E.-J., Chen J.D.;
RT "Sequestration and inhibition of Daxx-mediated transcriptional repression
RT by PML.";
RL Mol. Cell. Biol. 20:1784-1796(2000).
RN [16]
RP INTERACTION WITH HSPB1.
RX PubMed=11003656; DOI=10.1128/mcb.20.20.7602-7612.2000;
RA Charette S.J., Lavoie J.N., Lambert H., Landry J.;
RT "Inhibition of Daxx-mediated apoptosis by heat shock protein 27.";
RL Mol. Cell. Biol. 20:7602-7612(2000).
RN [17]
RP INTERACTION WITH MAP3K5, AND SUBCELLULAR LOCATION.
RX PubMed=11495919; DOI=10.1074/jbc.m105928200;
RA Ko Y.-G., Kang Y.-S., Park H., Seol W., Kim J., Kim T., Park H.-S.,
RA Choi E.-J., Kim S.;
RT "Apoptosis signal-regulating kinase 1 controls the proapoptotic function of
RT death-associated protein (Daxx) in the cytoplasm.";
RL J. Biol. Chem. 276:39103-39106(2001).
RN [18]
RP INTERACTION WITH TGFBR2.
RX PubMed=11483955; DOI=10.1038/35087019;
RA Perlman R., Schiemann W.P., Brooks M.W., Lodish H.F., Weinberg R.A.;
RT "TGF-beta-induced apoptosis is mediated by the adapter protein Daxx that
RT facilitates JNK activation.";
RL Nat. Cell Biol. 3:708-714(2001).
RN [19]
RP SUMOYLATION AT LYS-630 AND LYS-631, AND MUTAGENESIS OF LYS-630 AND LYS-631.
RX PubMed=12150977; DOI=10.1016/s0006-291x(02)00699-x;
RA Jang M.-S., Ryu S.-W., Kim E.;
RT "Modification of Daxx by small ubiquitin-related modifier-1.";
RL Biochem. Biophys. Res. Commun. 295:495-500(2002).
RN [20]
RP INTERACTION WITH SLC2A4 AND UBE2I, SUMOYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=11842083; DOI=10.1074/jbc.m110294200;
RA Lalioti V.S., Vergarajauregui S., Pulido D., Sandoval I.V.;
RT "The insulin-sensitive glucose transporter, GLUT4, interacts physically
RT with Daxx. Two proteins with capacity to bind Ubc9 and conjugated to
RT SUMO1.";
RL J. Biol. Chem. 277:19783-19791(2002).
RN [21]
RP INTERACTION WITH MCRS1.
RX PubMed=11948183; DOI=10.1074/jbc.m200633200;
RA Lin D.-Y., Shih H.-M.;
RT "Essential role of the 58-kDa microspherule protein in the modulation of
RT Daxx-dependent transcriptional repression as revealed by nucleolar
RT sequestration.";
RL J. Biol. Chem. 277:25446-25456(2002).
RN [22]
RP FUNCTION, PHOSPHORYLATION, AND INTERACTION WITH HDAC2; HISTONES AND DEK.
RX PubMed=12140263; DOI=10.1242/jcs.115.16.3319;
RA Hollenbach A.D., McPherson C.J., Mientjes E.J., Iyengar R., Grosveld G.;
RT "Daxx and histone deacetylase II associate with chromatin through an
RT interaction with core histones and the chromatin-associated protein Dek.";
RL J. Cell Sci. 115:3319-3330(2002).
RN [23]
RP INTERACTION WITH PUUMALA HANTAVIRUS NUCLEOPROTEIN (MICROBIAL INFECTION).
RX PubMed=11907324; DOI=10.1099/0022-1317-83-4-759;
RA Li X.D., Maekelae T.P., Guo D., Soliymani R., Koistinen V., Vapalahti O.,
RA Vaheri A., Lankinen H.;
RT "Hantavirus nucleocapsid protein interacts with the Fas-mediated apoptosis
RT enhancer Daxx.";
RL J. Gen. Virol. 83:759-766(2002).
RN [24]
RP INTERACTION WITH HIPK2.
RX PubMed=14678985;
RA Hofmann T.G., Stollberg N., Schmitz M.L., Will H.;
RT "HIPK2 regulates transforming growth factor-beta-induced c-Jun NH(2)-
RT terminal kinase activation and apoptosis in human hepatoma cells.";
RL Cancer Res. 63:8271-8277(2003).
RN [25]
RP OLIGOMERIZATION, SUBCELLULAR LOCATION, INTERACTION WITH MAP3K5, MUTAGENESIS
RP OF SER-668 AND SER-671, AND PHOSPHORYLATION AT SER-668.
RX PubMed=12968034; DOI=10.1074/jbc.m213201200;
RA Song J.J., Lee Y.J.;
RT "Role of the ASK1-SEK1-JNK1-HIPK1 signal in Daxx trafficking and ASK1
RT oligomerization.";
RL J. Biol. Chem. 278:47245-47252(2003).
RN [26]
RP INTERACTION WITH HIPK1.
RX PubMed=12529400; DOI=10.1128/mcb.23.3.950-960.2003;
RA Ecsedy J.A., Michaelson J.S., Leder P.;
RT "Homeodomain-interacting protein kinase 1 modulates Daxx localization,
RT phosphorylation, and transcriptional activity.";
RL Mol. Cell. Biol. 23:950-960(2003).
RN [27]
RP INTERACTION WITH ATRX, AND SUBCELLULAR LOCATION.
RX PubMed=12953102; DOI=10.1073/pnas.1937626100;
RA Xue Y., Gibbons R., Yan Z., Yang D., McDowell T.L., Sechi S., Qin J.,
RA Zhou S., Higgs D., Wang W.;
RT "The ATRX syndrome protein forms a chromatin-remodeling complex with Daxx
RT and localizes in promyelocytic leukemia nuclear bodies.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10635-10640(2003).
RN [28]
RP INTERACTION WITH HADV5 E1B-55K (MICROBIAL INFECTION).
RX PubMed=14557665; DOI=10.1128/jvi.77.21.11809-11821.2003;
RA Zhao L.Y., Colosimo A.L., Liu Y., Wan Y., Liao D.;
RT "Adenovirus E1B 55-kilodalton oncoprotein binds to Daxx and eliminates
RT enhancement of p53-dependent transcription by DAXX.";
RL J. Virol. 77:11809-11821(2003).
RN [29]
RP INTERACTION WITH SPOP.
RX PubMed=15240113; DOI=10.1016/j.bbrc.2004.06.022;
RA La M., Kim K., Park J., Won J., Lee J.-H., Fu Y.M., Meadows G.G., Joe C.O.;
RT "Daxx-mediated transcriptional repression of MMP1 gene is reversed by
RT SPOP.";
RL Biochem. Biophys. Res. Commun. 320:760-765(2004).
RN [30]
RP FUNCTION, INTERACTION WITH ATRX, AND SUBCELLULAR LOCATION.
RX PubMed=14990586; DOI=10.1074/jbc.m401321200;
RA Tang J., Wu S., Liu H., Stratt R., Barak O.G., Shiekhattar R.,
RA Picketts D.J., Yang X.;
RT "A novel transcription regulatory complex containing death domain-
RT associated protein and the ATR-X syndrome protein.";
RL J. Biol. Chem. 279:20369-20377(2004).
RN [31]
RP FUNCTION, AND INTERACTION WITH MDM2 AND TP53.
RX PubMed=15364927; DOI=10.1074/jbc.m406743200;
RA Zhao L.Y., Liu J., Sidhu G.S., Niu Y., Liu Y., Wang R., Liao D.;
RT "Negative regulation of p53 functions by Daxx and the involvement of
RT MDM2.";
RL J. Biol. Chem. 279:50566-50579(2004).
RN [32]
RP FUNCTION, AND INTERACTION WITH HSF1.
RX PubMed=15016915; DOI=10.1073/pnas.0304768101;
RA Boellmann F., Guettouche T., Guo Y., Fenna M., Mnayer L., Voellmy R.;
RT "DAXX interacts with heat shock factor 1 during stress activation and
RT enhances its transcriptional activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:4100-4105(2004).
RN [33]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [34]
RP IDENTIFICATION IN A COMPLEX WITH CUL3 AND SPOP, AND UBIQUITINATION.
RX PubMed=16524876; DOI=10.1074/jbc.m600204200;
RA Kwon J.E., La M., Oh K.H., Oh Y.M., Kim G.R., Seol J.H., Baek S.H.,
RA Chiba T., Tanaka K., Bang O.S., Joe C.O., Chung C.H.;
RT "BTB domain-containing speckle-type POZ protein (SPOP) serves as an adaptor
RT of Daxx for ubiquitination by Cul3-based ubiquitin ligase.";
RL J. Biol. Chem. 281:12664-12672(2006).
RN [35]
RP FUNCTION, SUBCELLULAR LOCATION, SUMOYLATION, SUMO INTERACTION MOTIF, AND
RP MUTAGENESIS OF 733-ILE--ASP-740.
RX PubMed=17081986; DOI=10.1016/j.molcel.2006.10.019;
RA Lin D.Y., Huang Y.S., Jeng J.C., Kuo H.Y., Chang C.C., Chao T.T., Ho C.C.,
RA Chen Y.C., Lin T.P., Fang H.I., Hung C.C., Suen C.S., Hwang M.J.,
RA Chang K.S., Maul G.G., Shih H.M.;
RT "Role of SUMO-interacting motif in Daxx SUMO modification, subnuclear
RT localization, and repression of sumoylated transcription factors.";
RL Mol. Cell 24:341-354(2006).
RN [36]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-702, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [37]
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH MDM2 AND USP7, INTERACTION WITH
RP MDM2; TP53 AND USP7, AND SUBCELLULAR LOCATION.
RX PubMed=16845383; DOI=10.1038/ncb1442;
RA Tang J., Qu L.K., Zhang J., Wang W., Michaelson J.S., Degenhardt Y.Y.,
RA El-Deiry W.S., Yang X.;
RT "Critical role for Daxx in regulating Mdm2.";
RL Nat. Cell Biol. 8:855-862(2006).
RN [38]
RP INTERACTION WITH AXIN1.
RX PubMed=17210684; DOI=10.1158/0008-5472.can-06-1671;
RA Li Q., Wang X., Wu X., Rui Y., Liu W., Wang J., Wang X., Liou Y.C., Ye Z.,
RA Lin S.C.;
RT "Daxx cooperates with the Axin/HIPK2/p53 complex to induce cell death.";
RL Cancer Res. 67:66-74(2007).
RN [39]
RP IDENTIFICATION IN A COMPLEX WITH MDM2; RASSF1 AND USP7, INTERACTION WITH
RP RASSF1; USP7 AND MDM2, AND SUBCELLULAR LOCATION.
RX PubMed=18566590; DOI=10.1038/emboj.2008.115;
RA Song M.S., Song S.J., Kim S.Y., Oh H.J., Lim D.S.;
RT "The tumour suppressor RASSF1A promotes MDM2 self-ubiquitination by
RT disrupting the MDM2-DAXX-HAUSP complex.";
RL EMBO J. 27:1863-1874(2008).
RN [40]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-671 AND SER-702, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [41]
RP FUNCTION IN HCMV RESTRICTION.
RX PubMed=17942542; DOI=10.1128/jvi.01685-07;
RA Tavalai N., Papior P., Rechter S., Stamminger T.;
RT "Nuclear domain 10 components promyelocytic leukemia protein and hDaxx
RT independently contribute to an intrinsic antiviral defense against human
RT cytomegalovirus infection.";
RL J. Virol. 82:126-137(2008).
RN [42]
RP INTERACTION WITH HCMV PP71 (MICROBIAL INFECTION).
RX PubMed=18922870; DOI=10.1128/jvi.01215-08;
RA Lukashchuk V., McFarlane S., Everett R.D., Preston C.M.;
RT "Human cytomegalovirus protein pp71 displaces the chromatin-associated
RT factor ATRX from nuclear domain 10 at early stages of infection.";
RL J. Virol. 82:12543-12554(2008).
RN [43]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178; SER-213; SER-495;
RP SER-668; SER-671; SER-688; SER-702; SER-737 AND SER-739, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [44]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [45]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-702; SER-737 AND SER-739, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [46]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-512, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [47]
RP UBIQUITINATION, AND DEUBIQUITINATION BY USP7.
RX PubMed=20153724; DOI=10.1016/j.bbrc.2010.02.051;
RA Tang J., Qu L., Pang M., Yang X.;
RT "Daxx is reciprocally regulated by Mdm2 and Hausp.";
RL Biochem. Biophys. Res. Commun. 393:542-545(2010).
RN [48]
RP FUNCTION AS HISTONE CHAPERONE, FUNCTION OF THE ATRX:DAXX COMPLEX, AND
RP INTERACTION WITH HISTONE H3.3.
RX PubMed=20504901; DOI=10.1101/gad.566910;
RA Drane P., Ouararhni K., Depaux A., Shuaib M., Hamiche A.;
RT "The death-associated protein DAXX is a novel histone chaperone involved in
RT the replication-independent deposition of H3.3.";
RL Genes Dev. 24:1253-1265(2010).
RN [49]
RP INTERACTION WITH HHV-5 PROTEIN UL123.
RX PubMed=20444888; DOI=10.1128/jvi.02231-09;
RA Reeves M., Woodhall D., Compton T., Sinclair J.;
RT "Human cytomegalovirus IE72 protein interacts with the transcriptional
RT repressor hDaxx to regulate LUNA gene expression during lytic infection.";
RL J. Virol. 84:7185-7194(2010).
RN [50]
RP FUNCTION AS HISTONE H3.3 CHAPERONE, AND INTERACTION WITH HISTONE H3.3.
RX PubMed=20651253; DOI=10.1073/pnas.1008850107;
RA Lewis P.W., Elsaesser S.J., Noh K.M., Stadler S.C., Allis C.D.;
RT "Daxx is an H3.3-specific histone chaperone and cooperates with ATRX in
RT replication-independent chromatin assembly at telomeres.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:14075-14080(2010).
RN [51]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495; SER-702; SER-737 AND
RP SER-739, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [52]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [53]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495 AND SER-702, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [54]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23222847; DOI=10.1101/gr.142703.112;
RA Delbarre E., Ivanauskiene K., Kuntziger T., Collas P.;
RT "DAXX-dependent supply of soluble (H3.3-H4) dimers to PML bodies pending
RT deposition into chromatin.";
RL Genome Res. 23:440-451(2013).
RN [55]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178; SER-412; SER-424;
RP SER-495; SER-671; SER-688 AND SER-702, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [56]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24200965; DOI=10.4161/cc.26988;
RA Corpet A., Olbrich T., Gwerder M., Fink D., Stucki M.;
RT "Dynamics of histone H3.3 deposition in proliferating and senescent cells
RT reveals a DAXX-dependent targeting to PML-NBs important for pericentromeric
RT heterochromatin organization.";
RL Cell Cycle 13:249-267(2014).
RN [57]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [58]
RP INTERACTION WITH EPSTEIN-BARR VIRUS PROTEIN BNRF1 (MICROBIAL INFECTION),
RP AND SUBCELLULAR LOCATION.
RX PubMed=25275136; DOI=10.1128/jvi.01895-14;
RA Tsai K., Chan L., Gibeault R., Conn K., Dheekollu J., Domsic J.,
RA Marmorstein R., Schang L.M., Lieberman P.M.;
RT "Viral reprogramming of the Daxx histone H3.3 chaperone during early
RT Epstein-Barr virus infection.";
RL J. Virol. 88:14350-14363(2014).
RN [59]
RP FUNCTION.
RX PubMed=24530302; DOI=10.1016/j.molcel.2014.01.018;
RA Lacoste N., Woolfe A., Tachiwana H., Garea A.V., Barth T., Cantaloube S.,
RA Kurumizaka H., Imhof A., Almouzni G.;
RT "Mislocalization of the centromeric histone variant CenH3/CENP-A in human
RT cells depends on the chaperone DAXX.";
RL Mol. Cell 53:631-644(2014).
RN [60]
RP INTERACTION WITH SUMO1P1/SUMO5.
RX PubMed=27211601; DOI=10.1038/srep26509;
RA Liang Y.C., Lee C.C., Yao Y.L., Lai C.C., Schmitz M.L., Yang W.M.;
RT "SUMO5, a novel poly-sumo isoform, regulates pml nuclear bodies.";
RL Sci. Rep. 6:26509-26509(2016).
RN [61]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-142, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [62]
RP STRUCTURE BY NMR OF 55-144 IN COMPLEX WITH RASSF1, AND INTERACTION WITH
RP RASSF1.
RX PubMed=21134643; DOI=10.1016/j.str.2010.09.016;
RA Escobar-Cabrera E., Lau D.K., Giovinazzi S., Ishov A.M., McIntosh L.P.;
RT "Structural characterization of the DAXX N-terminal helical bundle domain
RT and its complex with Rassf1C.";
RL Structure 18:1642-1653(2010).
RN [63]
RP STRUCTURE BY NMR OF 721-740.
RX PubMed=20927612; DOI=10.1007/s12104-010-9271-4;
RA Naik M.T., Chang C.C., Naik N.M., Kung C.C., Shih H.M., Huang T.H.;
RT "NMR chemical shift assignments of a complex between SUMO-1 and SIM peptide
RT derived from the C-terminus of Daxx.";
RL Biomol. NMR. Assign. 5:75-77(2011).
RN [64]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 184-390 IN COMPLEX WITH HISTONE
RP H3.3/H4 DIMER, AND MUTAGENESIS OF TYR-222.
RX PubMed=23142979; DOI=10.1038/nsmb.2439;
RA Liu C.P., Xiong C., Wang M., Yu Z., Yang N., Chen P., Zhang Z., Li G.,
RA Xu R.M.;
RT "Structure of the variant histone H3.3-H4 heterodimer in complex with its
RT chaperone DAXX.";
RL Nat. Struct. Mol. Biol. 19:1287-1292(2012).
RN [65]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 178-389 IN COMPLEX WITH HISTONE
RP H3.3/H4 DIMER, AND MUTAGENESIS OF GLN-206; SER-220; TYR-222; GLU-225;
RP LYS-229; ARG-251; PHE-317; ARG-328 AND ASP-331.
RX PubMed=23075851; DOI=10.1038/nature11608;
RA Elsasser S.J., Huang H., Lewis P.W., Chin J.W., Allis C.D., Patel D.J.;
RT "DAXX envelops a histone H3.3-H4 dimer for H3.3-specific recognition.";
RL Nature 491:560-565(2012).
CC -!- FUNCTION: Transcription corepressor known to repress transcriptional
CC potential of several sumoylated transcription factors. Down-regulates
CC basal and activated transcription. Its transcription repressor activity
CC is modulated by recruiting it to subnuclear compartments like the
CC nucleolus or PML/POD/ND10 nuclear bodies through interactions with
CC MCSR1 and PML, respectively. Seems to regulate transcription in
CC PML/POD/ND10 nuclear bodies together with PML and may influence
CC TNFRSF6-dependent apoptosis thereby. Inhibits transcriptional
CC activation of PAX3 and ETS1 through direct protein-protein
CC interactions. Modulates PAX5 activity; the function seems to involve
CC CREBBP. Acts as an adapter protein in a MDM2-DAXX-USP7 complex by
CC regulating the RING-finger E3 ligase MDM2 ubiquitination activity.
CC Under non-stress condition, in association with the deubiquitinating
CC USP7, prevents MDM2 self-ubiquitination and enhances the intrinsic E3
CC ligase activity of MDM2 towards TP53, thereby promoting TP53
CC ubiquitination and subsequent proteasomal degradation. Upon DNA damage,
CC its association with MDM2 and USP7 is disrupted, resulting in increased
CC MDM2 autoubiquitination and consequently, MDM2 degradation, which leads
CC to TP53 stabilization. Acts as histone chaperone that facilitates
CC deposition of histone H3.3. Acts as targeting component of the
CC chromatin remodeling complex ATRX:DAXX which has ATP-dependent DNA
CC translocase activity and catalyzes the replication-independent
CC deposition of histone H3.3 in pericentric DNA repeats outside S-phase
CC and telomeres, and the in vitro remodeling of H3.3-containing
CC nucleosomes. Does not affect the ATPase activity of ATRX but alleviates
CC its transcription repression activity. Upon neuronal activation
CC associates with regulatory elements of selected immediate early genes
CC where it promotes deposition of histone H3.3 which may be linked to
CC transcriptional induction of these genes. Required for the recruitment
CC of histone H3.3:H4 dimers to PML-nuclear bodies (PML-NBs); the process
CC is independent of ATRX and facilitated by ASF1A; PML-NBs are suggested
CC to function as regulatory sites for the incorporation of newly
CC synthesized histone H3.3 into chromatin. In case of overexpression of
CC centromeric histone variant CENPA (as found in various tumors) is
CC involved in its mislocalization to chromosomes; the ectopic
CC localization involves a heterotypic tetramer containing CENPA, and
CC histones H3.3 and H4 and decreases binding of CTCF to chromatin.
CC Proposed to mediate activation of the JNK pathway and apoptosis via
CC MAP3K5 in response to signaling from TNFRSF6 and TGFBR2. Interaction
CC with HSPB1/HSP27 may prevent interaction with TNFRSF6 and MAP3K5 and
CC block DAXX-mediated apoptosis. In contrast, in lymphoid cells JNC
CC activation and TNFRSF6-mediated apoptosis may not involve DAXX. Shows
CC restriction activity towards human cytomegalovirus (HCMV). Plays a role
CC as a positive regulator of the heat shock transcription factor HSF1
CC activity during the stress protein response (PubMed:15016915).
CC {ECO:0000269|PubMed:12140263, ECO:0000269|PubMed:14990586,
CC ECO:0000269|PubMed:15016915, ECO:0000269|PubMed:15364927,
CC ECO:0000269|PubMed:16845383, ECO:0000269|PubMed:17081986,
CC ECO:0000269|PubMed:17942542, ECO:0000269|PubMed:20504901,
CC ECO:0000269|PubMed:20651253, ECO:0000269|PubMed:23222847,
CC ECO:0000269|PubMed:24200965, ECO:0000269|PubMed:24530302}.
CC -!- SUBUNIT: Homomultimer. Interacts (via C-terminus) with TNFRSF6 (via
CC death domain). Interacts with PAX5, SLC2A4/GLUT4, MAP3K5, TGFBR2,
CC phosphorylated dimeric HSPB1/HSP27, CENPC, ETS1, sumoylated PML, UBE2I,
CC MCRS1 and TP53. Interacts (via N-terminus) with HIPK2 and HIPK3.
CC Interacts with HIPK1, which induces translocation from PML/POD/ND10
CC nuclear bodies to chromatin and enhances association with HDAC1.
CC Interacts (non-phosphorylated) with PAX3, PAX7, DEK, HDAC1, HDAC2,
CC HDAC3, acetylated histone H4 and histones H2A, H2B, H3, H3.3 and H4.
CC Interacts with SPOP; mediating CUL3-dependent proteosomal degradation.
CC Interacts with CBP; the interaction is dependent the sumoylation of CBP
CC and suppresses CBP transcriptional activity via recruitment of HDAC2
CC directly in the complex with TP53 and HIPK2. Interacts with AXIN1; the
CC interaction stimulates the interaction of DAXX with TP53, stimulates
CC 'Ser-46' phosphorylation of TP53 on and induces cell death on UV
CC irradiation. Interacts with MDM2; the interaction is direct. Interacts
CC with USP7; the interaction is direct and independent of MDM2 and TP53.
CC Part of a complex with DAXX, MDM2 and USP7 under non-stress conditions.
CC Interacts (via N-terminus) with RASSF1 (via C-terminus); the
CC interaction is independent of MDM2 and TP53; RASSF1 isoform A disrupts
CC interactions among MDM2, DAXX and USP7, thus contributing to the
CC efficient activation of TP53 by promoting MDM2 self-ubiquitination in
CC cell-cycle checkpoint control in response to DNA damage. Interacts with
CC ATRX to form the chromatin remodeling complex ATRX:DAXX. Interacts with
CC HSF1 (via homotrimeric form preferentially); this interaction relieves
CC homotrimeric HSF1 from repression of its transcriptional activity by
CC HSP90-dependent multichaperone complex upon heat shock
CC (PubMed:15016915). Interacts with SUMO1P1/SUMO5 (PubMed:27211601).
CC {ECO:0000269|PubMed:10393185, ECO:0000269|PubMed:10669754,
CC ECO:0000269|PubMed:10684855, ECO:0000269|PubMed:11003656,
CC ECO:0000269|PubMed:11483955, ECO:0000269|PubMed:11495919,
CC ECO:0000269|PubMed:11842083, ECO:0000269|PubMed:11948183,
CC ECO:0000269|PubMed:12140263, ECO:0000269|PubMed:12529400,
CC ECO:0000269|PubMed:12953102, ECO:0000269|PubMed:12968034,
CC ECO:0000269|PubMed:14678985, ECO:0000269|PubMed:14990586,
CC ECO:0000269|PubMed:15016915, ECO:0000269|PubMed:15240113,
CC ECO:0000269|PubMed:15364927, ECO:0000269|PubMed:16524876,
CC ECO:0000269|PubMed:16845383, ECO:0000269|PubMed:17210684,
CC ECO:0000269|PubMed:18566590, ECO:0000269|PubMed:20444888,
CC ECO:0000269|PubMed:20504901, ECO:0000269|PubMed:20651253,
CC ECO:0000269|PubMed:21134643, ECO:0000269|PubMed:23075851,
CC ECO:0000269|PubMed:23142979, ECO:0000269|PubMed:27211601,
CC ECO:0000269|PubMed:9645950}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human
CC cytomegalovirus/HHV-5 tegument phosphoprotein pp71 and protein UL123.
CC {ECO:0000269|PubMed:18922870}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Epstein-Barr virus
CC protein BNRF1. {ECO:0000269|PubMed:25275136}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human adenovirus 5 E1B-
CC 55K protein; this interaction might alterate the normal interactions of
CC DAXX, PML, and TP53, which may contribute to cell transformation.
CC {ECO:0000269|PubMed:14557665}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Puumala hantavirus
CC nucleoprotein. {ECO:0000269|PubMed:11907324}.
CC -!- INTERACTION:
CC Q9UER7; O43918: AIRE; NbExp=5; IntAct=EBI-77321, EBI-1753081;
CC Q9UER7; Q9Y2J4: AMOTL2; NbExp=3; IntAct=EBI-77321, EBI-746752;
CC Q9UER7; Q92870-2: APBB2; NbExp=3; IntAct=EBI-77321, EBI-21535880;
CC Q9UER7; P10275: AR; NbExp=5; IntAct=EBI-77321, EBI-608057;
CC Q9UER7; P46100: ATRX; NbExp=8; IntAct=EBI-77321, EBI-396461;
CC Q9UER7; Q9H257: CARD9; NbExp=3; IntAct=EBI-77321, EBI-751319;
CC Q9UER7; Q96GN5: CDCA7L; NbExp=3; IntAct=EBI-77321, EBI-5278764;
CC Q9UER7; Q8N726: CDKN2A; NbExp=8; IntAct=EBI-77321, EBI-625922;
CC Q9UER7; Q96MT8-3: CEP63; NbExp=3; IntAct=EBI-77321, EBI-11522539;
CC Q9UER7; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-77321, EBI-739624;
CC Q9UER7; Q92793: CREBBP; NbExp=2; IntAct=EBI-77321, EBI-81215;
CC Q9UER7; Q9NPF5: DMAP1; NbExp=3; IntAct=EBI-77321, EBI-399105;
CC Q9UER7; G5E9A7: DMWD; NbExp=3; IntAct=EBI-77321, EBI-10976677;
CC Q9UER7; Q8IZU0: FAM9B; NbExp=4; IntAct=EBI-77321, EBI-10175124;
CC Q9UER7; P25445: FAS; NbExp=3; IntAct=EBI-77321, EBI-494743;
CC Q9UER7; P02794: FTH1; NbExp=5; IntAct=EBI-77321, EBI-713259;
CC Q9UER7; O95995: GAS8; NbExp=5; IntAct=EBI-77321, EBI-1052570;
CC Q9UER7; Q53GS7: GLE1; NbExp=3; IntAct=EBI-77321, EBI-1955541;
CC Q9UER7; Q96IK5: GMCL1; NbExp=3; IntAct=EBI-77321, EBI-2548508;
CC Q9UER7; Q08379: GOLGA2; NbExp=8; IntAct=EBI-77321, EBI-618309;
CC Q9UER7; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-77321, EBI-5916454;
CC Q9UER7; Q4V328: GRIPAP1; NbExp=3; IntAct=EBI-77321, EBI-717919;
CC Q9UER7; P84243: H3-3B; NbExp=6; IntAct=EBI-77321, EBI-120658;
CC Q9UER7; Q6NXT2: H3-5; NbExp=3; IntAct=EBI-77321, EBI-2868501;
CC Q9UER7; Q13547: HDAC1; NbExp=2; IntAct=EBI-77321, EBI-301834;
CC Q9UER7; Q92769: HDAC2; NbExp=2; IntAct=EBI-77321, EBI-301821;
CC Q9UER7; P04792: HSPB1; NbExp=4; IntAct=EBI-77321, EBI-352682;
CC Q9UER7; P42858: HTT; NbExp=15; IntAct=EBI-77321, EBI-466029;
CC Q9UER7; Q8WVF5: KCTD4; NbExp=3; IntAct=EBI-77321, EBI-741463;
CC Q9UER7; Q9P2G9-2: KLHL8; NbExp=3; IntAct=EBI-77321, EBI-11959635;
CC Q9UER7; Q99683: MAP3K5; NbExp=7; IntAct=EBI-77321, EBI-476263;
CC Q9UER7; Q96EZ8: MCRS1; NbExp=11; IntAct=EBI-77321, EBI-348259;
CC Q9UER7; Q00987: MDM2; NbExp=18; IntAct=EBI-77321, EBI-389668;
CC Q9UER7; Q8TD10: MIPOL1; NbExp=3; IntAct=EBI-77321, EBI-2548751;
CC Q9UER7; Q9UHC7: MKRN1; NbExp=3; IntAct=EBI-77321, EBI-373524;
CC Q9UER7; Q8NCY6: MSANTD4; NbExp=3; IntAct=EBI-77321, EBI-7850168;
CC Q9UER7; Q7Z6G3-2: NECAB2; NbExp=6; IntAct=EBI-77321, EBI-10172876;
CC Q9UER7; Q9BZ95: NSD3; NbExp=2; IntAct=EBI-77321, EBI-3390132;
CC Q9UER7; Q99497: PARK7; NbExp=6; IntAct=EBI-77321, EBI-1164361;
CC Q9UER7; Q96AQ6: PBXIP1; NbExp=3; IntAct=EBI-77321, EBI-740845;
CC Q9UER7; Q7Z412: PEX26; NbExp=3; IntAct=EBI-77321, EBI-752057;
CC Q9UER7; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-77321, EBI-14066006;
CC Q9UER7; P29590: PML; NbExp=6; IntAct=EBI-77321, EBI-295890;
CC Q9UER7; D3DTS7: PMP22; NbExp=3; IntAct=EBI-77321, EBI-25882629;
CC Q9UER7; Q8ND90: PNMA1; NbExp=5; IntAct=EBI-77321, EBI-302345;
CC Q9UER7; Q9NS23: RASSF1; NbExp=6; IntAct=EBI-77321, EBI-367363;
CC Q9UER7; Q9NS23-4: RASSF1; NbExp=5; IntAct=EBI-77321, EBI-438710;
CC Q9UER7; Q86WH2: RASSF3; NbExp=3; IntAct=EBI-77321, EBI-2845202;
CC Q9UER7; Q04206: RELA; NbExp=5; IntAct=EBI-77321, EBI-73886;
CC Q9UER7; P78317: RNF4; NbExp=3; IntAct=EBI-77321, EBI-2340927;
CC Q9UER7; Q9UJW9: SERTAD3; NbExp=3; IntAct=EBI-77321, EBI-748621;
CC Q9UER7; O43791: SPOP; NbExp=5; IntAct=EBI-77321, EBI-743549;
CC Q9UER7; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-77321, EBI-5235340;
CC Q9UER7; Q9Y2D8: SSX2IP; NbExp=3; IntAct=EBI-77321, EBI-2212028;
CC Q9UER7; P40763: STAT3; NbExp=4; IntAct=EBI-77321, EBI-518675;
CC Q9UER7; P63165: SUMO1; NbExp=7; IntAct=EBI-77321, EBI-80140;
CC Q9UER7; Q86VP1: TAX1BP1; NbExp=3; IntAct=EBI-77321, EBI-529518;
CC Q9UER7; Q9NQB0: TCF7L2; NbExp=5; IntAct=EBI-77321, EBI-924724;
CC Q9UER7; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-77321, EBI-1105213;
CC Q9UER7; P37173: TGFBR2; NbExp=2; IntAct=EBI-77321, EBI-296151;
CC Q9UER7; P04637: TP53; NbExp=12; IntAct=EBI-77321, EBI-366083;
CC Q9UER7; Q99816: TSG101; NbExp=4; IntAct=EBI-77321, EBI-346882;
CC Q9UER7; P0CG48: UBC; NbExp=2; IntAct=EBI-77321, EBI-3390054;
CC Q9UER7; P63279: UBE2I; NbExp=3; IntAct=EBI-77321, EBI-80168;
CC Q9UER7; Q495M9: USH1G; NbExp=3; IntAct=EBI-77321, EBI-8601749;
CC Q9UER7; Q93009: USP7; NbExp=14; IntAct=EBI-77321, EBI-302474;
CC Q9UER7; Q8N680: ZBTB2; NbExp=3; IntAct=EBI-77321, EBI-2515601;
CC Q9UER7; Q9HCK0: ZBTB26; NbExp=3; IntAct=EBI-77321, EBI-3918996;
CC Q9UER7; P03179: BNRF1; Xeno; NbExp=5; IntAct=EBI-77321, EBI-9349301;
CC Q9UER7; P03244: E1B; Xeno; NbExp=4; IntAct=EBI-77321, EBI-1561155;
CC Q9UER7; P25446: Fas; Xeno; NbExp=4; IntAct=EBI-77321, EBI-296206;
CC Q9UER7; O88904: Hipk1; Xeno; NbExp=3; IntAct=EBI-77321, EBI-692945;
CC Q9UER7; P15991: HSPB1; Xeno; NbExp=3; IntAct=EBI-77321, EBI-1559114;
CC Q9UER7; Q02650: Pax5; Xeno; NbExp=4; IntAct=EBI-77321, EBI-296260;
CC Q9UER7; Q9QZL0: Ripk3; Xeno; NbExp=2; IntAct=EBI-77321, EBI-2367423;
CC Q9UER7; P03243; Xeno; NbExp=4; IntAct=EBI-77321, EBI-1561361;
CC Q9UER7-1; P14921-1: ETS1; NbExp=3; IntAct=EBI-287635, EBI-913224;
CC Q9UER7-1; P14921-2: ETS1; NbExp=2; IntAct=EBI-287635, EBI-913228;
CC Q9UER7-1; P84243: H3-3B; NbExp=21; IntAct=EBI-287635, EBI-120658;
CC Q9UER7-1; P68431: H3C12; NbExp=6; IntAct=EBI-287635, EBI-79722;
CC Q9UER7-1; Q71DI3: H3C15; NbExp=5; IntAct=EBI-287635, EBI-750650;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11495919,
CC ECO:0000269|PubMed:11842083, ECO:0000269|PubMed:12968034,
CC ECO:0000269|PubMed:9407001}. Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:10669754, ECO:0000269|PubMed:16845383,
CC ECO:0000269|PubMed:18566590, ECO:0000269|PubMed:23222847,
CC ECO:0000269|PubMed:9407001}. Nucleus, PML body
CC {ECO:0000269|PubMed:10669754, ECO:0000269|PubMed:11842083,
CC ECO:0000269|PubMed:14990586, ECO:0000269|PubMed:17081986,
CC ECO:0000269|PubMed:21482821, ECO:0000269|PubMed:23222847,
CC ECO:0000269|PubMed:24200965, ECO:0000269|PubMed:25275136}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:23222847}. Chromosome, centromere
CC {ECO:0000269|PubMed:24200965, ECO:0000269|PubMed:9645950}.
CC Note=Dispersed throughout the nucleoplasm, in PML/POD/ND10 nuclear
CC bodies, and in nucleoli (Probable). Colocalizes with histone H3.3,
CC ATRX, HIRA and ASF1A at PML-nuclear bodies (PubMed:12953102,
CC PubMed:14990586, PubMed:23222847, PubMed:24200965). Colocalizes with a
CC subset of interphase centromeres, but is absent from mitotic
CC centromeres (PubMed:9645950). Detected in cytoplasmic punctate
CC structures (PubMed:11842083). Translocates from the nucleus to the
CC cytoplasm upon glucose deprivation or oxidative stress
CC (PubMed:12968034). Colocalizes with RASSF1 in the nucleus
CC (PubMed:18566590). Colocalizes with USP7 in nucleoplasma with
CC accumulation in speckled structures (PubMed:16845383).
CC {ECO:0000269|PubMed:11842083, ECO:0000269|PubMed:12953102,
CC ECO:0000269|PubMed:12968034, ECO:0000269|PubMed:14990586,
CC ECO:0000269|PubMed:16845383, ECO:0000269|PubMed:18566590,
CC ECO:0000269|PubMed:23222847, ECO:0000269|PubMed:24200965,
CC ECO:0000269|PubMed:9645950, ECO:0000305|PubMed:10669754}.
CC -!- SUBCELLULAR LOCATION: [Isoform beta]: Nucleus
CC {ECO:0000269|PubMed:21482821}. Note=Diffuse nuclear distribution
CC pattern and no comparable dot-like accumulation of isoform 1.
CC {ECO:0000269|PubMed:21482821}.
CC -!- SUBCELLULAR LOCATION: [Isoform gamma]: Nucleus
CC {ECO:0000269|PubMed:21482821}. Note=Diffuse nuclear distribution
CC pattern and no comparable dot-like accumulation of isoform 1.
CC {ECO:0000269|PubMed:21482821}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q9UER7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UER7-2; Sequence=VSP_001270;
CC Name=3;
CC IsoId=Q9UER7-3; Sequence=VSP_045588;
CC Name=beta;
CC IsoId=Q9UER7-4; Sequence=VSP_057438, VSP_057440;
CC Name=gamma;
CC IsoId=Q9UER7-5; Sequence=VSP_057437, VSP_057439;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- INDUCTION: Upon mitogenic stimulation by concanavalin-A.
CC -!- DOMAIN: The Sumo interaction motif mediates Sumo binding, and is
CC required both for sumoylation and binding to sumoylated targets.
CC -!- PTM: Sumoylated with SUMO1 on multiple lysine residues.
CC {ECO:0000269|PubMed:11842083, ECO:0000269|PubMed:12150977,
CC ECO:0000269|PubMed:17081986}.
CC -!- PTM: Phosphorylated by HIPK1 upon glucose deprivation.
CC {ECO:0000269|PubMed:10393185, ECO:0000269|PubMed:12140263,
CC ECO:0000269|PubMed:12968034}.
CC -!- PTM: Polyubiquitinated; which is promoted by CUL3 and SPOP and results
CC in proteasomal degradation. Ubiquitinated by MDM2; inducing its
CC degradation. Deubiquitinated by USP7; leading to stabilize it.
CC {ECO:0000269|PubMed:16524876, ECO:0000269|PubMed:20153724}.
CC -!- MISCELLANEOUS: [Isoform beta]: Markedly decreased affinity for PML and
CC TP53/p53, unable to repress p53-mediated transcription. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform gamma]: Markedly decreased affinity for PML and
CC TP53/p53, unable to repress p53-mediated transcription. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the DAXX family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/DAXXID40265ch6p21.html";
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DR EMBL; AF039136; AAB92671.1; -; mRNA.
DR EMBL; AF006041; AAB63043.1; -; mRNA.
DR EMBL; AF015956; AAB66585.2; -; mRNA.
DR EMBL; AF050179; AAC39853.1; -; mRNA.
DR EMBL; AF097742; AAC72843.1; -; mRNA.
DR EMBL; HQ436528; AEC33235.1; -; mRNA.
DR EMBL; HQ436529; AEC33236.1; -; mRNA.
DR EMBL; AB015051; BAA34295.1; -; mRNA.
DR EMBL; AK303854; BAG64795.1; -; mRNA.
DR EMBL; CR457085; CAG33366.1; -; mRNA.
DR EMBL; AL662820; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL662827; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX248088; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR759793; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR759786; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR759817; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z97183; CAB09986.2; -; Genomic_DNA.
DR EMBL; Z97184; CAB09986.2; JOINED; Genomic_DNA.
DR EMBL; Z97184; CAB09989.2; -; Genomic_DNA.
DR EMBL; Z97183; CAB09989.2; JOINED; Genomic_DNA.
DR EMBL; CH471081; EAX03722.1; -; Genomic_DNA.
DR EMBL; BC000220; AAH00220.1; -; mRNA.
DR EMBL; BC109073; AAI09074.1; -; mRNA.
DR EMBL; BC109074; AAI09075.1; -; mRNA.
DR CCDS; CCDS4776.1; -. [Q9UER7-1]
DR CCDS; CCDS59008.1; -. [Q9UER7-3]
DR PIR; T03847; T03847.
DR RefSeq; NP_001135441.1; NM_001141969.1. [Q9UER7-1]
DR RefSeq; NP_001241646.1; NM_001254717.1. [Q9UER7-3]
DR RefSeq; NP_001341.1; NM_001350.4. [Q9UER7-1]
DR PDB; 2KQS; NMR; -; B=721-740.
DR PDB; 2KZS; NMR; -; A=55-144.
DR PDB; 2KZU; NMR; -; A=55-144.
DR PDB; 4H9N; X-ray; 1.95 A; C=178-389.
DR PDB; 4H9O; X-ray; 2.05 A; C=178-389.
DR PDB; 4H9P; X-ray; 2.20 A; C=178-389.
DR PDB; 4H9Q; X-ray; 1.95 A; C=178-389.
DR PDB; 4H9R; X-ray; 2.20 A; C=178-389.
DR PDB; 4H9S; X-ray; 2.60 A; E/F=183-398.
DR PDB; 4HGA; X-ray; 2.80 A; A=184-390.
DR PDB; 5GRQ; X-ray; 1.58 A; A=55-144, B=55-143.
DR PDB; 5KDM; X-ray; 3.50 A; C=178-389.
DR PDB; 5Y18; X-ray; 2.20 A; A=55-144.
DR PDB; 5Y6O; X-ray; 3.10 A; A/B/C/D/E/F/G/H/I=50-144.
DR PDBsum; 2KQS; -.
DR PDBsum; 2KZS; -.
DR PDBsum; 2KZU; -.
DR PDBsum; 4H9N; -.
DR PDBsum; 4H9O; -.
DR PDBsum; 4H9P; -.
DR PDBsum; 4H9Q; -.
DR PDBsum; 4H9R; -.
DR PDBsum; 4H9S; -.
DR PDBsum; 4HGA; -.
DR PDBsum; 5GRQ; -.
DR PDBsum; 5KDM; -.
DR PDBsum; 5Y18; -.
DR PDBsum; 5Y6O; -.
DR AlphaFoldDB; Q9UER7; -.
DR BMRB; Q9UER7; -.
DR SMR; Q9UER7; -.
DR BioGRID; 107985; 344.
DR CORUM; Q9UER7; -.
DR DIP; DIP-27628N; -.
DR IntAct; Q9UER7; 164.
DR MINT; Q9UER7; -.
DR STRING; 9606.ENSP00000363668; -.
DR GlyGen; Q9UER7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UER7; -.
DR PhosphoSitePlus; Q9UER7; -.
DR BioMuta; DAXX; -.
DR DMDM; 24636785; -.
DR EPD; Q9UER7; -.
DR jPOST; Q9UER7; -.
DR MassIVE; Q9UER7; -.
DR MaxQB; Q9UER7; -.
DR PaxDb; Q9UER7; -.
DR PeptideAtlas; Q9UER7; -.
DR PRIDE; Q9UER7; -.
DR ProteomicsDB; 25260; -.
DR ProteomicsDB; 84150; -. [Q9UER7-1]
DR ProteomicsDB; 84151; -. [Q9UER7-2]
DR Antibodypedia; 1411; 1027 antibodies from 47 providers.
DR DNASU; 1616; -.
DR Ensembl; ENST00000266000.10; ENSP00000266000.6; ENSG00000204209.13. [Q9UER7-1]
DR Ensembl; ENST00000374542.10; ENSP00000363668.5; ENSG00000204209.13. [Q9UER7-1]
DR Ensembl; ENST00000383062.8; ENSP00000372539.4; ENSG00000206206.11. [Q9UER7-1]
DR Ensembl; ENST00000383194.8; ENSP00000372681.4; ENSG00000206279.10. [Q9UER7-1]
DR Ensembl; ENST00000399060.7; ENSP00000382014.3; ENSG00000206206.11. [Q9UER7-1]
DR Ensembl; ENST00000399344.7; ENSP00000382281.3; ENSG00000206279.10. [Q9UER7-1]
DR Ensembl; ENST00000414083.6; ENSP00000396876.2; ENSG00000204209.13. [Q9UER7-3]
DR Ensembl; ENST00000433482.5; ENSP00000404623.1; ENSG00000231617.8. [Q9UER7-1]
DR Ensembl; ENST00000436311.6; ENSP00000404376.2; ENSG00000227046.8. [Q9UER7-1]
DR Ensembl; ENST00000445009.6; ENSP00000394108.2; ENSG00000231617.8. [Q9UER7-1]
DR Ensembl; ENST00000455860.6; ENSP00000410772.2; ENSG00000227046.8. [Q9UER7-1]
DR Ensembl; ENST00000612868.4; ENSP00000479172.1; ENSG00000227046.8. [Q9UER7-3]
DR Ensembl; ENST00000612888.2; ENSP00000483394.1; ENSG00000206206.11. [Q9UER7-3]
DR Ensembl; ENST00000613912.3; ENSP00000477633.1; ENSG00000206206.11. [Q9UER7-4]
DR Ensembl; ENST00000616312.1; ENSP00000483517.1; ENSG00000227046.8. [Q9UER7-4]
DR Ensembl; ENST00000617660.4; ENSP00000480448.1; ENSG00000206279.10. [Q9UER7-3]
DR Ensembl; ENST00000619421.1; ENSP00000478810.1; ENSG00000206279.10. [Q9UER7-4]
DR Ensembl; ENST00000620164.4; ENSP00000482399.1; ENSG00000204209.13. [Q9UER7-4]
DR Ensembl; ENST00000622655.1; ENSP00000484830.1; ENSG00000231617.8. [Q9UER7-4]
DR GeneID; 1616; -.
DR KEGG; hsa:1616; -.
DR MANE-Select; ENST00000374542.10; ENSP00000363668.5; NM_001141969.2; NP_001135441.1.
DR UCSC; uc003oec.4; human. [Q9UER7-1]
DR UCSC; uc063nwl.1; human.
DR CTD; 1616; -.
DR DisGeNET; 1616; -.
DR GeneCards; DAXX; -.
DR HGNC; HGNC:2681; DAXX.
DR HPA; ENSG00000204209; Low tissue specificity.
DR MalaCards; DAXX; -.
DR MIM; 603186; gene.
DR neXtProt; NX_Q9UER7; -.
DR OpenTargets; ENSG00000204209; -.
DR Orphanet; 100075; Neuroendocrine tumor of stomach.
DR PharmGKB; PA27148; -.
DR VEuPathDB; HostDB:ENSG00000204209; -.
DR eggNOG; ENOG502QRS6; Eukaryota.
DR GeneTree; ENSGT00390000009448; -.
DR HOGENOM; CLU_022811_1_0_1; -.
DR InParanoid; Q9UER7; -.
DR OMA; SKYAVMQ; -.
DR PhylomeDB; Q9UER7; -.
DR TreeFam; TF325803; -.
DR PathwayCommons; Q9UER7; -.
DR Reactome; R-HSA-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-HSA-6804757; Regulation of TP53 Degradation.
DR Reactome; R-HSA-9609690; HCMV Early Events.
DR Reactome; R-HSA-9670095; Inhibition of DNA recombination at telomere.
DR Reactome; R-HSA-9670613; Defective Inhibition of DNA Recombination at Telomere Due to DAXX Mutations.
DR Reactome; R-HSA-9670615; Defective Inhibition of DNA Recombination at Telomere Due to ATRX Mutations.
DR SignaLink; Q9UER7; -.
DR SIGNOR; Q9UER7; -.
DR BioGRID-ORCS; 1616; 115 hits in 1079 CRISPR screens.
DR ChiTaRS; DAXX; human.
DR EvolutionaryTrace; Q9UER7; -.
DR GeneWiki; Death-associated_protein_6; -.
DR GenomeRNAi; 1616; -.
DR Pharos; Q9UER7; Tbio.
DR PRO; PR:Q9UER7; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9UER7; protein.
DR Bgee; ENSG00000204209; Expressed in granulocyte and 94 other tissues.
DR ExpressionAtlas; Q9UER7; baseline and differential.
DR Genevisible; Q9UER7; HS.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:CACAO.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:GO_Central.
DR GO; GO:0016605; C:PML body; IDA:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0031072; F:heat shock protein binding; TAS:UniProtKB.
DR GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR GO; GO:0050681; F:nuclear androgen receptor binding; IPI:UniProtKB.
DR GO; GO:0002039; F:p53 binding; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0030295; F:protein kinase activator activity; IGI:ParkinsonsUK-UCL.
DR GO; GO:0019901; F:protein kinase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IDA:UniProtKB.
DR GO; GO:0140037; F:sumo-dependent protein binding; IPI:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
DR GO; GO:0140416; F:transcription regulator inhibitor activity; IDA:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0030521; P:androgen receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0071276; P:cellular response to cadmium ion; IDA:UniProtKB.
DR GO; GO:0071280; P:cellular response to copper ion; IDA:UniProtKB.
DR GO; GO:0072738; P:cellular response to diamide; IDA:UniProtKB.
DR GO; GO:0034605; P:cellular response to heat; IDA:UniProtKB.
DR GO; GO:1903936; P:cellular response to sodium arsenite; IDA:UniProtKB.
DR GO; GO:0034620; P:cellular response to unfolded protein; IDA:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IDA:UniProtKB.
DR GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IDA:UniProtKB.
DR GO; GO:0007254; P:JNK cascade; IDA:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006334; P:nucleosome assembly; IDA:UniProtKB.
DR GO; GO:1901216; P:positive regulation of neuron death; IGI:ParkinsonsUK-UCL.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; IGI:ParkinsonsUK-UCL.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IGI:ParkinsonsUK-UCL.
DR GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0031396; P:regulation of protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
DR CDD; cd13151; DAXX_helical_bundle; 1.
DR CDD; cd13150; DAXX_histone_binding; 1.
DR DisProt; DP00707; -.
DR Gene3D; 1.10.8.810; -; 1.
DR Gene3D; 1.20.58.2170; -; 1.
DR IDEAL; IID00398; -.
DR InterPro; IPR005012; Daxx.
DR InterPro; IPR046378; DAXX_histone_binding.
DR InterPro; IPR046426; DAXX_histone_binding_sf.
DR InterPro; IPR031333; Daxx_N.
DR InterPro; IPR038298; Daxx_N_sf.
DR PANTHER; PTHR12766:SF7; PTHR12766:SF7; 1.
DR Pfam; PF03344; Daxx; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Apoptosis; Centromere;
KW Chaperone; Chromatin regulator; Chromosome; Coiled coil; Cytoplasm;
KW Host-virus interaction; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..740
FT /note="Death domain-associated protein 6"
FT /id="PRO_0000151258"
FT REGION 1..160
FT /note="Necessary for interaction with USP7 and ATRX"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..417
FT /note="Interaction with histone H3.3"
FT REGION 347..570
FT /note="Necessary for interaction with USP7"
FT REGION 384..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..625
FT /note="Interaction with MAP3K5"
FT REGION 626..740
FT /note="Interaction with SPOP"
FT /evidence="ECO:0000269|PubMed:15240113"
FT REGION 627..634
FT /note="(Microbial infection) Interaction with Puumala
FT hantavirus nucleoprotein"
FT /evidence="ECO:0000269|PubMed:11907324"
FT REGION 658..663
FT /note="(Microbial infection) Interaction with Puumala
FT hantavirus nucleoprotein"
FT /evidence="ECO:0000269|PubMed:11907324"
FT REGION 733..740
FT /note="Sumo interaction motif (SIM)"
FT COILED 180..217
FT /evidence="ECO:0000255"
FT COILED 358..399
FT /evidence="ECO:0000255"
FT COILED 430..489
FT /evidence="ECO:0000255"
FT MOTIF 391..395
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 628..634
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 147..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..487
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..619
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..724
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 412
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 424
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 459
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O35613"
FT MOD_RES 495
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 498
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VIB2"
FT MOD_RES 512
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 561
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VIB2"
FT MOD_RES 580
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VIB2"
FT MOD_RES 668
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12968034,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 671
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 688
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 702
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 737
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT MOD_RES 739
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT CROSSLNK 142
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 630
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000269|PubMed:12150977"
FT CROSSLNK 631
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000269|PubMed:12150977"
FT VAR_SEQ 1..75
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045588"
FT VAR_SEQ 648..682
FT /note="YVERQRSVHEKNGKKICTLPSPPSPLASLAPVADS -> PAVPNPPFTASSA
FT WYLQDKCGHTMRSRRDHRALRL (in isoform gamma)"
FT /evidence="ECO:0000303|PubMed:21482821"
FT /id="VSP_057437"
FT VAR_SEQ 653..688
FT /note="RSVHEKNGKKICTLPSPPSPLASLAPVADSSTRVDS -> SPAVPNPPFTAS
FT SAWYLQDKCGHTMRSRRDHRALRL (in isoform beta)"
FT /evidence="ECO:0000303|PubMed:21482821"
FT /id="VSP_057438"
FT VAR_SEQ 683..740
FT /note="Missing (in isoform gamma)"
FT /evidence="ECO:0000303|PubMed:21482821"
FT /id="VSP_057439"
FT VAR_SEQ 689..740
FT /note="Missing (in isoform beta)"
FT /evidence="ECO:0000303|PubMed:21482821"
FT /id="VSP_057440"
FT VAR_SEQ 696..740
FT /note="SSLCIPSPARLSQTPHSQPPRPGTCKTSVATQCDPEEIIVLSDSD -> PAK
FT NLGRRRSKQDQG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_001270"
FT MUTAGEN 206
FT /note="Q->L: Impairs interaction with histones H3 and H4."
FT /evidence="ECO:0000269|PubMed:23075851"
FT MUTAGEN 220
FT /note="S->A: Abolishes interaction with histones H3 and
FT H4."
FT /evidence="ECO:0000269|PubMed:23075851"
FT MUTAGEN 222
FT /note="Y->A,S: Abolishes interaction with histones H3 and
FT H4."
FT /evidence="ECO:0000269|PubMed:23075851,
FT ECO:0000269|PubMed:23142979"
FT MUTAGEN 222
FT /note="Y->E: Abolishes interaction with histone H3.3."
FT /evidence="ECO:0000269|PubMed:23075851,
FT ECO:0000269|PubMed:23142979"
FT MUTAGEN 225
FT /note="E->L: Impairs interaction with histones H3 and H4."
FT /evidence="ECO:0000269|PubMed:23075851"
FT MUTAGEN 229
FT /note="K->A,L: Impairs interaction with histones H3 and
FT H4."
FT /evidence="ECO:0000269|PubMed:23075851"
FT MUTAGEN 251
FT /note="R->A: Abolishes interaction with histones H3 and
FT H4."
FT /evidence="ECO:0000269|PubMed:23075851"
FT MUTAGEN 317
FT /note="F->A: Abolishes interaction with histones H3 and
FT H4."
FT /evidence="ECO:0000269|PubMed:23075851"
FT MUTAGEN 328
FT /note="R->A: Abolishes interaction with histones H3 and
FT H4."
FT /evidence="ECO:0000269|PubMed:23075851"
FT MUTAGEN 331
FT /note="D->A: Abolishes interaction with histones H3 and
FT H4."
FT /evidence="ECO:0000269|PubMed:23075851"
FT MUTAGEN 630
FT /note="K->A: Abolishes sumoylation; when associated with A-
FT 631."
FT /evidence="ECO:0000269|PubMed:12150977"
FT MUTAGEN 631
FT /note="K->A: Abolishes sumoylation; when associated with A-
FT 630."
FT /evidence="ECO:0000269|PubMed:12150977"
FT MUTAGEN 668
FT /note="S->A: No translocation to the cytosol upon glucose
FT deprivation."
FT /evidence="ECO:0000269|PubMed:12968034"
FT MUTAGEN 671
FT /note="S->A: No effect on cytosol translocation. upon
FT glucose deprivation."
FT /evidence="ECO:0000269|PubMed:12968034"
FT MUTAGEN 733..740
FT /note="Missing: Abolishes sumoylation."
FT /evidence="ECO:0000269|PubMed:17081986"
FT CONFLICT 177
FT /note="Q -> R (in Ref. 2; AAB66585)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="R -> H (in Ref. 5; AAC72843)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="R -> W (in Ref. 2; AAB66585)"
FT /evidence="ECO:0000305"
FT CONFLICT 365
FT /note="R -> Q (in Ref. 2; AAB66585)"
FT /evidence="ECO:0000305"
FT CONFLICT 382
FT /note="L -> S (in Ref. 2; AAB66585)"
FT /evidence="ECO:0000305"
FT CONFLICT 505
FT /note="E -> G (in Ref. 8; BAG64795)"
FT /evidence="ECO:0000305"
FT CONFLICT 647
FT /note="S -> R (in Ref. 10; CAB09986/CAB09989)"
FT /evidence="ECO:0000305"
FT CONFLICT 722
FT /note="T -> A (in Ref. 10; CAB09986/CAB09989)"
FT /evidence="ECO:0000305"
FT CONFLICT 731..732
FT /note="EE -> KK (in Ref. 5; AAC72843)"
FT /evidence="ECO:0000305"
FT HELIX 60..77
FT /evidence="ECO:0007829|PDB:5GRQ"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:2KZU"
FT HELIX 84..93
FT /evidence="ECO:0007829|PDB:5GRQ"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:5GRQ"
FT HELIX 103..118
FT /evidence="ECO:0007829|PDB:5GRQ"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:5GRQ"
FT HELIX 123..136
FT /evidence="ECO:0007829|PDB:5GRQ"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:2KZS"
FT HELIX 185..206
FT /evidence="ECO:0007829|PDB:4H9N"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:4H9N"
FT HELIX 221..242
FT /evidence="ECO:0007829|PDB:4H9N"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:4H9N"
FT HELIX 265..275
FT /evidence="ECO:0007829|PDB:4H9N"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:4H9S"
FT HELIX 286..299
FT /evidence="ECO:0007829|PDB:4H9N"
FT HELIX 306..333
FT /evidence="ECO:0007829|PDB:4H9N"
FT HELIX 339..341
FT /evidence="ECO:0007829|PDB:4H9N"
FT HELIX 346..348
FT /evidence="ECO:0007829|PDB:4H9N"
FT HELIX 350..353
FT /evidence="ECO:0007829|PDB:4H9N"
FT HELIX 355..384
FT /evidence="ECO:0007829|PDB:4H9N"
SQ SEQUENCE 740 AA; 81373 MW; 1B309ADDAA878040 CRC64;
MATANSIIVL DDDDEDEAAA QPGPSHPLPN AASPGAEAPS SSEPHGARGS SSSGGKKCYK
LENEKLFEEF LELCKMQTAD HPEVVPFLYN RQQRAHSLFL ASAEFCNILS RVLSRARSRP
AKLYVYINEL CTVLKAHSAK KKLNLAPAAT TSNEPSGNNP PTHLSLDPTN AENTASQSPR
TRGSRRQIQR LEQLLALYVA EIRRLQEKEL DLSELDDPDS AYLQEARLKR KLIRLFGRLC
ELKDCSSLTG RVIEQRIPYR GTRYPEVNRR IERLINKPGP DTFPDYGDVL RAVEKAAARH
SLGLPRQQLQ LMAQDAFRDV GIRLQERRHL DLIYNFGCHL TDDYRPGVDP ALSDPVLARR
LRENRSLAMS RLDEVISKYA MLQDKSEEGE RKKRRARLQG TSSHSADTPE ASLDSGEGPS
GMASQGCPSA SRAETDDEDD EESDEEEEEE EEEEEEEATD SEEEEDLEQM QEGQEDDEEE
DEEEEAAAGK DGDKSPMSSL QISNEKNLEP GKQISRSSGE QQNKGRIVSP SLLSEEPLAP
SSIDAESNGE QPEELTLEEE SPVSQLFELE IEALPLDTPS SVETDISSSR KQSEEPFTTV
LENGAGMVSS TSFNGGVSPH NWGDSGPPCK KSRKEKKQTG SGPLGNSYVE RQRSVHEKNG
KKICTLPSPP SPLASLAPVA DSSTRVDSPS HGLVTSSLCI PSPARLSQTP HSQPPRPGTC
KTSVATQCDP EEIIVLSDSD
