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Death domain-associated protein 6 (Daxx) (hDaxx) (ETS1-associated protein 1) (EAP1) (Fas death domain-associated protein)

 DAXX_HUMAN              Reviewed;         740 AA.
Q9UER7; B4E1I3; F5ANJ6; F5ANJ7; F5H082; O14747; O15141; O15208;
Q5STK9; Q9BWI3;
01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
01-NOV-2002, sequence version 2.
25-OCT-2017, entry version 176.
RecName: Full=Death domain-associated protein 6;
AltName: Full=Daxx;
Short=hDaxx;
AltName: Full=ETS1-associated protein 1;
Short=EAP1;
AltName: Full=Fas death domain-associated protein;
Name=DAXX; Synonyms=BING2, DAP6;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9215629; DOI=10.1016/S0092-8674(00)80294-9;
Yang X., Khosravi-Far R., Chang H.Y., Baltimore D.;
"Daxx, a novel Fas-binding protein that activates JNK and apoptosis.";
Cell 89:1067-1076(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBCELLULAR LOCATION.
TISSUE=Placenta;
PubMed=9407001; DOI=10.1089/dna.1997.16.1289;
Kiriakidou M., Driscoll D.A., Lopez-Guisa J.M., Strauss J.F. III;
"Cloning and expression of primate Daxx cDNAs and mapping of the human
gene to chromosome 6p21.3 in the MHC region.";
DNA Cell Biol. 16:1289-1298(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH CENPC, AND
SUBCELLULAR LOCATION.
TISSUE=Cervix carcinoma;
PubMed=9645950;
Pluta A.F., Earnshaw W.C., Goldberg I.G.;
"Interphase-specific association of intrinsic centromere protein CENP-
C with HDaxx, a death domain-binding protein implicated in Fas-
mediated cell death.";
J. Cell Sci. 111:2029-2041(1998).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
PubMed=9545376; DOI=10.1006/jmbi.1998.1637;
Herberg J.A., Beck S., Trowsdale J.;
"TAPASIN, DAXX, RGL2, HKE2 and four new genes (BING 1, 3 to 5) form a
dense cluster at the centromeric end of the MHC.";
J. Mol. Biol. 277:839-857(1998).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=T-cell;
PubMed=10698492; DOI=10.1038/sj.onc.1203385;
Li R., Pei H., Watson D.K., Papas T.S.;
"EAP1/Daxx interacts with ETS1 and represses transcriptional
activation of ETS1 target genes.";
Oncogene 19:745-753(2000).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BETA AND GAMMA), SUBCELLULAR
LOCATION (ISOFORMS BETA AND GAMMA), AND ALTERNATIVE SPLICING.
TISSUE=Renal cell carcinoma;
PubMed=21482821; DOI=10.1074/jbc.M110.196311;
Wethkamp N., Hanenberg H., Funke S., Suschek C.V., Wetzel W.,
Heikaus S., Grinstein E., Ramp U., Engers R., Gabbert H.E.,
Mahotka C.;
"Daxx-beta and Daxx-gamma, two novel splice variants of the
transcriptional co-repressor Daxx.";
J. Biol. Chem. 286:19576-19588(2011).
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Usui T.;
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 334-740 (ISOFORM 2).
TISSUE=Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[13]
INTERACTION WITH PAX3 AND PAX7, AND PHOSPHORYLATION.
PubMed=10393185; DOI=10.1093/emboj/18.13.3702;
Hollenbach A.D., Sublett J.E., McPherson C.J., Grosveld G.;
"The Pax3-FKHR oncoprotein is unresponsive to the Pax3-associated
repressor hDaxx.";
EMBO J. 18:3702-3711(1999).
[14]
INTERACTION WITH PML.
PubMed=10684855; DOI=10.1084/jem.191.4.631;
Zhong S., Salomoni P., Ronchetti S., Guo A., Ruggero D.,
Pandolfi P.P.;
"Promyelocytic leukemia protein (PML) and Daxx participate in a novel
nuclear pathway for apoptosis.";
J. Exp. Med. 191:631-640(2000).
[15]
INTERACTION WITH SUMOYLATED PML; HDAC1; HDAC2 AND HDAC3, AND
SUBCELLULAR LOCATION.
PubMed=10669754; DOI=10.1128/MCB.20.5.1784-1796.2000;
Li H., Leo C., Zhu J., Wu X., O'Neil J., Park E.-J., Chen J.D.;
"Sequestration and inhibition of Daxx-mediated transcriptional
repression by PML.";
Mol. Cell. Biol. 20:1784-1796(2000).
[16]
INTERACTION WITH HSPB1.
PubMed=11003656; DOI=10.1128/MCB.20.20.7602-7612.2000;
Charette S.J., Lavoie J.N., Lambert H., Landry J.;
"Inhibition of Daxx-mediated apoptosis by heat shock protein 27.";
Mol. Cell. Biol. 20:7602-7612(2000).
[17]
INTERACTION WITH MAP3K5, AND SUBCELLULAR LOCATION.
PubMed=11495919; DOI=10.1074/jbc.M105928200;
Ko Y.-G., Kang Y.-S., Park H., Seol W., Kim J., Kim T., Park H.-S.,
Choi E.-J., Kim S.;
"Apoptosis signal-regulating kinase 1 controls the proapoptotic
function of death-associated protein (Daxx) in the cytoplasm.";
J. Biol. Chem. 276:39103-39106(2001).
[18]
INTERACTION WITH TGFBR2.
PubMed=11483955; DOI=10.1038/35087019;
Perlman R., Schiemann W.P., Brooks M.W., Lodish H.F., Weinberg R.A.;
"TGF-beta-induced apoptosis is mediated by the adapter protein Daxx
that facilitates JNK activation.";
Nat. Cell Biol. 3:708-714(2001).
[19]
SUMOYLATION AT LYS-630 AND LYS-631, AND MUTAGENESIS OF LYS-630 AND
LYS-631.
PubMed=12150977; DOI=10.1016/S0006-291X(02)00699-X;
Jang M.-S., Ryu S.-W., Kim E.;
"Modification of Daxx by small ubiquitin-related modifier-1.";
Biochem. Biophys. Res. Commun. 295:495-500(2002).
[20]
INTERACTION WITH SLC2A4 AND UBE2I, SUMOYLATION, AND SUBCELLULAR
LOCATION.
PubMed=11842083; DOI=10.1074/jbc.M110294200;
Lalioti V.S., Vergarajauregui S., Pulido D., Sandoval I.V.;
"The insulin-sensitive glucose transporter, GLUT4, interacts
physically with Daxx. Two proteins with capacity to bind Ubc9 and
conjugated to SUMO1.";
J. Biol. Chem. 277:19783-19791(2002).
[21]
INTERACTION WITH MCRS1.
PubMed=11948183; DOI=10.1074/jbc.M200633200;
Lin D.-Y., Shih H.-M.;
"Essential role of the 58-kDa microspherule protein in the modulation
of Daxx-dependent transcriptional repression as revealed by nucleolar
sequestration.";
J. Biol. Chem. 277:25446-25456(2002).
[22]
FUNCTION, PHOSPHORYLATION, AND INTERACTION WITH HDAC2; HISTONES AND
DEK.
PubMed=12140263;
Hollenbach A.D., McPherson C.J., Mientjes E.J., Iyengar R.,
Grosveld G.;
"Daxx and histone deacetylase II associate with chromatin through an
interaction with core histones and the chromatin-associated protein
Dek.";
J. Cell Sci. 115:3319-3330(2002).
[23]
INTERACTION WITH HIPK2.
PubMed=14678985;
Hofmann T.G., Stollberg N., Schmitz M.L., Will H.;
"HIPK2 regulates transforming growth factor-beta-induced c-Jun NH(2)-
terminal kinase activation and apoptosis in human hepatoma cells.";
Cancer Res. 63:8271-8277(2003).
[24]
OLIGOMERIZATION, SUBCELLULAR LOCATION, INTERACTION WITH MAP3K5,
MUTAGENESIS OF SER-668 AND SER-671, AND PHOSPHORYLATION AT SER-668.
PubMed=12968034; DOI=10.1074/jbc.M213201200;
Song J.J., Lee Y.J.;
"Role of the ASK1-SEK1-JNK1-HIPK1 signal in Daxx trafficking and ASK1
oligomerization.";
J. Biol. Chem. 278:47245-47252(2003).
[25]
INTERACTION WITH HIPK1.
PubMed=12529400; DOI=10.1128/MCB.23.3.950-960.2003;
Ecsedy J.A., Michaelson J.S., Leder P.;
"Homeodomain-interacting protein kinase 1 modulates Daxx localization,
phosphorylation, and transcriptional activity.";
Mol. Cell. Biol. 23:950-960(2003).
[26]
INTERACTION WITH ATRX, AND SUBCELLULAR LOCATION.
PubMed=12953102; DOI=10.1073/pnas.1937626100;
Xue Y., Gibbons R., Yan Z., Yang D., McDowell T.L., Sechi S., Qin J.,
Zhou S., Higgs D., Wang W.;
"The ATRX syndrome protein forms a chromatin-remodeling complex with
Daxx and localizes in promyelocytic leukemia nuclear bodies.";
Proc. Natl. Acad. Sci. U.S.A. 100:10635-10640(2003).
[27]
INTERACTION WITH HADV5 E1B-55K.
PubMed=14557665; DOI=10.1128/JVI.77.21.11809-11821.2003;
Zhao L.Y., Colosimo A.L., Liu Y., Wan Y., Liao D.;
"Adenovirus E1B 55-kilodalton oncoprotein binds to Daxx and eliminates
enhancement of p53-dependent transcription by DAXX.";
J. Virol. 77:11809-11821(2003).
[28]
INTERACTION WITH SPOP.
PubMed=15240113; DOI=10.1016/j.bbrc.2004.06.022;
La M., Kim K., Park J., Won J., Lee J.-H., Fu Y.M., Meadows G.G.,
Joe C.O.;
"Daxx-mediated transcriptional repression of MMP1 gene is reversed by
SPOP.";
Biochem. Biophys. Res. Commun. 320:760-765(2004).
[29]
FUNCTION, INTERACTION WITH ATRX, AND SUBCELLULAR LOCATION.
PubMed=14990586; DOI=10.1074/jbc.M401321200;
Tang J., Wu S., Liu H., Stratt R., Barak O.G., Shiekhattar R.,
Picketts D.J., Yang X.;
"A novel transcription regulatory complex containing death domain-
associated protein and the ATR-X syndrome protein.";
J. Biol. Chem. 279:20369-20377(2004).
[30]
FUNCTION, AND INTERACTION WITH MDM2 AND TP53.
PubMed=15364927; DOI=10.1074/jbc.M406743200;
Zhao L.Y., Liu J., Sidhu G.S., Niu Y., Liu Y., Wang R., Liao D.;
"Negative regulation of p53 functions by Daxx and the involvement of
MDM2.";
J. Biol. Chem. 279:50566-50579(2004).
[31]
FUNCTION, AND INTERACTION WITH HSF1.
PubMed=15016915; DOI=10.1073/pnas.0304768101;
Boellmann F., Guettouche T., Guo Y., Fenna M., Mnayer L., Voellmy R.;
"DAXX interacts with heat shock factor 1 during stress activation and
enhances its transcriptional activity.";
Proc. Natl. Acad. Sci. U.S.A. 101:4100-4105(2004).
[32]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[33]
IDENTIFICATION IN A COMPLEX WITH CUL3 AND SPOP, AND UBIQUITINATION.
PubMed=16524876; DOI=10.1074/jbc.M600204200;
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.;
"BTB domain-containing speckle-type POZ protein (SPOP) serves as an
adaptor of Daxx for ubiquitination by Cul3-based ubiquitin ligase.";
J. Biol. Chem. 281:12664-12672(2006).
[34]
FUNCTION, SUBCELLULAR LOCATION, SUMOYLATION, SUMO INTERACTION MOTIF,
AND MUTAGENESIS OF 733-ILE--ASP-740.
PubMed=17081986; DOI=10.1016/j.molcel.2006.10.019;
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.;
"Role of SUMO-interacting motif in Daxx SUMO modification, subnuclear
localization, and repression of sumoylated transcription factors.";
Mol. Cell 24:341-354(2006).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-702, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[36]
FUNCTION, IDENTIFICATION IN A COMPLEX WITH MDM2 AND USP7, INTERACTION
WITH MDM2; TP53 AND USP7, AND SUBCELLULAR LOCATION.
PubMed=16845383; DOI=10.1038/ncb1442;
Tang J., Qu L.K., Zhang J., Wang W., Michaelson J.S., Degenhardt Y.Y.,
El-Deiry W.S., Yang X.;
"Critical role for Daxx in regulating Mdm2.";
Nat. Cell Biol. 8:855-862(2006).
[37]
INTERACTION WITH AXIN1.
PubMed=17210684; DOI=10.1158/0008-5472.CAN-06-1671;
Li Q., Wang X., Wu X., Rui Y., Liu W., Wang J., Wang X., Liou Y.C.,
Ye Z., Lin S.C.;
"Daxx cooperates with the Axin/HIPK2/p53 complex to induce cell
death.";
Cancer Res. 67:66-74(2007).
[38]
IDENTIFICATION IN A COMPLEX WITH MDM2; RASSF1 AND USP7, INTERACTION
WITH RASSF1; USP7 AND MDM2, AND SUBCELLULAR LOCATION.
PubMed=18566590; DOI=10.1038/emboj.2008.115;
Song M.S., Song S.J., Kim S.Y., Oh H.J., Lim D.S.;
"The tumour suppressor RASSF1A promotes MDM2 self-ubiquitination by
disrupting the MDM2-DAXX-HAUSP complex.";
EMBO J. 27:1863-1874(2008).
[39]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-671 AND SER-702, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[40]
FUNCTION IN HCMV RESTRICTION.
PubMed=17942542; DOI=10.1128/JVI.01685-07;
Tavalai N., Papior P., Rechter S., Stamminger T.;
"Nuclear domain 10 components promyelocytic leukemia protein and hDaxx
independently contribute to an intrinsic antiviral defense against
human cytomegalovirus infection.";
J. Virol. 82:126-137(2008).
[41]
INTERACTION WITH HCMV PP71.
PubMed=18922870; DOI=10.1128/JVI.01215-08;
Lukashchuk V., McFarlane S., Everett R.D., Preston C.M.;
"Human cytomegalovirus protein pp71 displaces the chromatin-associated
factor ATRX from nuclear domain 10 at early stages of infection.";
J. Virol. 82:12543-12554(2008).
[42]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178; SER-213; SER-495;
SER-668; SER-671; SER-688; SER-702; SER-737 AND SER-739, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[43]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[44]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-702; SER-737 AND
SER-739, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[45]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-512, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[46]
UBIQUITINATION, AND DEUBIQUITINATION BY USP7.
PubMed=20153724; DOI=10.1016/j.bbrc.2010.02.051;
Tang J., Qu L., Pang M., Yang X.;
"Daxx is reciprocally regulated by Mdm2 and Hausp.";
Biochem. Biophys. Res. Commun. 393:542-545(2010).
[47]
FUNCTION AS HISTONE CHAPERONE, FUNCTION OF THE ATRX:DAXX COMPLEX, AND
INTERACTION WITH HISTONE H3.3.
PubMed=20504901; DOI=10.1101/gad.566910;
Drane P., Ouararhni K., Depaux A., Shuaib M., Hamiche A.;
"The death-associated protein DAXX is a novel histone chaperone
involved in the replication-independent deposition of H3.3.";
Genes Dev. 24:1253-1265(2010).
[48]
INTERACTION WITH HHV-5 PROTEIN UL123.
PubMed=20444888; DOI=10.1128/JVI.02231-09;
Reeves M., Woodhall D., Compton T., Sinclair J.;
"Human cytomegalovirus IE72 protein interacts with the transcriptional
repressor hDaxx to regulate LUNA gene expression during lytic
infection.";
J. Virol. 84:7185-7194(2010).
[49]
FUNCTION AS HISTONE H3.3 CHAPERONE, AND INTERACTION WITH HISTONE H3.3.
PubMed=20651253; DOI=10.1073/pnas.1008850107;
Lewis P.W., Elsaesser S.J., Noh K.M., Stadler S.C., Allis C.D.;
"Daxx is an H3.3-specific histone chaperone and cooperates with ATRX
in replication-independent chromatin assembly at telomeres.";
Proc. Natl. Acad. Sci. U.S.A. 107:14075-14080(2010).
[50]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495; SER-702; SER-737
AND SER-739, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[51]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[52]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495 AND SER-702, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[53]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=23222847; DOI=10.1101/gr.142703.112;
Delbarre E., Ivanauskiene K., Kuntziger T., Collas P.;
"DAXX-dependent supply of soluble (H3.3-H4) dimers to PML bodies
pending deposition into chromatin.";
Genome Res. 23:440-451(2013).
[54]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178; SER-412; SER-424;
SER-495; SER-671; SER-688 AND SER-702, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[55]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=24200965; DOI=10.4161/cc.26988;
Corpet A., Olbrich T., Gwerder M., Fink D., Stucki M.;
"Dynamics of histone H3.3 deposition in proliferating and senescent
cells reveals a DAXX-dependent targeting to PML-NBs important for
pericentromeric heterochromatin organization.";
Cell Cycle 13:249-267(2014).
[56]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[57]
INTERACTION WITH EPSTEIN-BARR VIRUS PROTEIN BNRF1, AND SUBCELLULAR
LOCATION.
PubMed=25275136; DOI=10.1128/JVI.01895-14;
Tsai K., Chan L., Gibeault R., Conn K., Dheekollu J., Domsic J.,
Marmorstein R., Schang L.M., Lieberman P.M.;
"Viral reprogramming of the Daxx histone H3.3 chaperone during early
Epstein-Barr virus infection.";
J. Virol. 88:14350-14363(2014).
[58]
FUNCTION.
PubMed=24530302; DOI=10.1016/j.molcel.2014.01.018;
Lacoste N., Woolfe A., Tachiwana H., Garea A.V., Barth T.,
Cantaloube S., Kurumizaka H., Imhof A., Almouzni G.;
"Mislocalization of the centromeric histone variant CenH3/CENP-A in
human cells depends on the chaperone DAXX.";
Mol. Cell 53:631-644(2014).
[59]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-142, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[60]
STRUCTURE BY NMR OF 55-144 IN COMPLEX WITH RASSF1, AND INTERACTION
WITH RASSF1.
PubMed=21134643; DOI=10.1016/j.str.2010.09.016;
Escobar-Cabrera E., Lau D.K., Giovinazzi S., Ishov A.M.,
McIntosh L.P.;
"Structural characterization of the DAXX N-terminal helical bundle
domain and its complex with Rassf1C.";
Structure 18:1642-1653(2010).
[61]
STRUCTURE BY NMR OF 721-740.
PubMed=20927612; DOI=10.1007/s12104-010-9271-4;
Naik M.T., Chang C.C., Naik N.M., Kung C.C., Shih H.M., Huang T.H.;
"NMR chemical shift assignments of a complex between SUMO-1 and SIM
peptide derived from the C-terminus of Daxx.";
Biomol. NMR. Assign. 5:75-77(2011).
[62]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 184-390 IN COMPLEX WITH
HISTONE H3.3/H4 DIMER, AND MUTAGENESIS OF TYR-222.
PubMed=23142979; DOI=10.1038/nsmb.2439;
Liu C.P., Xiong C., Wang M., Yu Z., Yang N., Chen P., Zhang Z., Li G.,
Xu R.M.;
"Structure of the variant histone H3.3-H4 heterodimer in complex with
its chaperone DAXX.";
Nat. Struct. Mol. Biol. 19:1287-1292(2012).
[63]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 178-389 IN COMPLEX WITH
HISTONE H3.3/H4 DIMER, AND MUTAGENESIS OF GLN-206; SER-220; TYR-222;
GLU-225; LYS-229; ARG-251; PHE-317; ARG-328 AND ASP-331.
PubMed=23075851; DOI=10.1038/nature11608;
Elsasser S.J., Huang H., Lewis P.W., Chin J.W., Allis C.D.,
Patel D.J.;
"DAXX envelops a histone H3.3-H4 dimer for H3.3-specific
recognition.";
Nature 491:560-565(2012).
-!- FUNCTION: Transcription corepressor known to repress
transcriptional potential of several sumoylated transcription
factors. Down-regulates basal and activated transcription. Its
transcription repressor activity is modulated by recruiting it to
subnuclear compartments like the nucleolus or PML/POD/ND10 nuclear
bodies through interactions with MCSR1 and PML, respectively.
Seems to regulate transcription in PML/POD/ND10 nuclear bodies
together with PML and may influence TNFRSF6-dependent apoptosis
thereby. Inhibits transcriptional activation of PAX3 and ETS1
through direct protein-protein interactions. Modulates PAX5
activity; the function seems to involve CREBBP. Acts as an adapter
protein in a MDM2-DAXX-USP7 complex by regulating the RING-finger
E3 ligase MDM2 ubiquitination activity. Under non-stress
condition, in association with the deubiquitinating USP7, prevents
MDM2 self-ubiquitination and enhances the intrinsic E3 ligase
activity of MDM2 towards TP53, thereby promoting TP53
ubiquitination and subsequent proteasomal degradation. Upon DNA
damage, its association with MDM2 and USP7 is disrupted, resulting
in increased MDM2 autoubiquitination and consequently, MDM2
degradation, which leads to TP53 stabilization. Acts as histone
chaperone that facilitates deposition of histone H3.3. Acts as
targeting component of the chromatin remodeling complex ATRX:DAXX
which has ATP-dependent DNA translocase activity and catalyzes the
replication-independent deposition of histone H3.3 in pericentric
DNA repeats outside S-phase and telomeres, and the in vitro
remodeling of H3.3-containing nucleosomes. Does not affect the
ATPase activity of ATRX but alleviates its transcription
repression activity. Upon neuronal activation associates with
regulatory elements of selected immediate early genes where it
promotes deposition of histone H3.3 which may be linked to
transcriptional induction of these genes. Required for the
recruitment of histone H3.3:H4 dimers to PML-nuclear bodies (PML-
NBs); the process is independent of ATRX and facilitated by ASF1A;
PML-NBs are suggested to function as regulatory sites for the
incorporation of newly synthesized histone H3.3 into chromatin. In
case of overexpression of centromeric histone variant CENPA (as
found in various tumors) is involved in its mislocalization to
chromosomes; the ectopic localization involves a heterotypic
tetramer containing CENPA, and histones H3.3 and H4 and decreases
binding of CTCF to chromatin. Proposed to mediate activation of
the JNK pathway and apoptosis via MAP3K5 in response to signaling
from TNFRSF6 and TGFBR2. Interaction with HSPB1/HSP27 may prevent
interaction with TNFRSF6 and MAP3K5 and block DAXX-mediated
apoptosis. In contrast, in lymphoid cells JNC activation and
TNFRSF6-mediated apoptosis may not involve DAXX. Shows restriction
activity towards human cytomegalovirus (HCMV). Plays a role as a
positive regulator of the heat shock transcription factor HSF1
activity during the stress protein response (PubMed:15016915).
{ECO:0000269|PubMed:12140263, ECO:0000269|PubMed:14990586,
ECO:0000269|PubMed:15016915, ECO:0000269|PubMed:15364927,
ECO:0000269|PubMed:16845383, ECO:0000269|PubMed:17081986,
ECO:0000269|PubMed:17942542, ECO:0000269|PubMed:20504901,
ECO:0000269|PubMed:20651253, ECO:0000269|PubMed:23222847,
ECO:0000269|PubMed:24200965, ECO:0000269|PubMed:24530302}.
-!- SUBUNIT: Homomultimer. Interacts (via C-terminus) with TNFRSF6
(via death domain). Interacts with PAX5, SLC2A4/GLUT4, MAP3K5,
TGFBR2, phosphorylated dimeric HSPB1/HSP27, CENPC, ETS1,
sumoylated PML, UBE2I, MCRS1 and TP53. Interacts (via N-terminus)
with HIPK2 and HIPK3. Interacts with HIPK1, which induces
translocation from PML/POD/ND10 nuclear bodies to chromatin and
enhances association with HDAC1. Interacts (non-phosphorylated)
with PAX3, PAX7, DEK, HDAC1, HDAC2, HDAC3, acetylated histone H4
and histones H2A, H2B, H3, H3.3 and H4. Interacts with SPOP;
mediating CUL3-dependent proteosomal degradation. Interacts with
CBP; the interaction is dependent the sumoylation of CBP and
suppresses CBP transcriptional activity via recruitment of HDAC2
directly in the complex with TP53 and HIPK2. Interacts with AXIN1;
the interaction stimulates the interaction of DAXX with TP53,
stimulates 'Ser-46' phosphorylation of TP53 on and induces cell
death on UV irradiation. Interacts with MDM2; the interaction is
direct. Interacts with USP7; the interaction is direct and
independent of MDM2 and TP53. Part of a complex with DAXX, MDM2
and USP7 under non-stress conditions. Interacts (via N-terminus)
with RASSF1 (via C-terminus); the interaction is independent of
MDM2 and TP53; RASSF1 isoform A disrupts interactions among MDM2,
DAXX and USP7, thus contributing to the efficient activation of
TP53 by promoting MDM2 self-ubiquitination in cell-cycle
checkpoint control in response to DNA damage. Interacts with ATRX
to form the chromatin remodeling complex ATRX:DAXX. Interacts with
human cytomegalovirus/HHV-5 tegument phosphoprotein pp71 and
protein UL123. Interacts with Epstein-Barr virus protein BNRF1.
Interacts with human adenovirus 5 E1B-55K protein; this
interaction might alterate the normal interactions of DAXX, PML,
and TP53, which may contribute to cell transformation
(PubMed:14557665). Interacts with HSF1 (via homotrimeric form
preferentially); this interaction relieves homotrimeric HSF1 from
repression of its transcriptional activity by HSP90-dependent
multichaperone complex upon heat shock (PubMed:15016915).
{ECO:0000269|PubMed:10393185, ECO:0000269|PubMed:10669754,
ECO:0000269|PubMed:10684855, ECO:0000269|PubMed:11003656,
ECO:0000269|PubMed:11483955, ECO:0000269|PubMed:11495919,
ECO:0000269|PubMed:11842083, ECO:0000269|PubMed:11948183,
ECO:0000269|PubMed:12140263, ECO:0000269|PubMed:12529400,
ECO:0000269|PubMed:12953102, ECO:0000269|PubMed:12968034,
ECO:0000269|PubMed:14557665, ECO:0000269|PubMed:14678985,
ECO:0000269|PubMed:14990586, ECO:0000269|PubMed:15016915,
ECO:0000269|PubMed:15240113, ECO:0000269|PubMed:15364927,
ECO:0000269|PubMed:16524876, ECO:0000269|PubMed:16845383,
ECO:0000269|PubMed:17210684, ECO:0000269|PubMed:18566590,
ECO:0000269|PubMed:18922870, ECO:0000269|PubMed:20444888,
ECO:0000269|PubMed:20504901, ECO:0000269|PubMed:20651253,
ECO:0000269|PubMed:21134643, ECO:0000269|PubMed:23075851,
ECO:0000269|PubMed:23142979, ECO:0000269|PubMed:25275136,
ECO:0000269|PubMed:9645950}.
-!- INTERACTION:
P03243:- (xeno); NbExp=4; IntAct=EBI-77321, EBI-1561361;
O43918:AIRE; NbExp=5; IntAct=EBI-77321, EBI-1753081;
P10275:AR; NbExp=5; IntAct=EBI-77321, EBI-608057;
P46100:ATRX; NbExp=7; IntAct=EBI-77321, EBI-396461;
P03179:BNRF1 (xeno); NbExp=5; IntAct=EBI-77321, EBI-9349301;
Q9H257:CARD9; NbExp=3; IntAct=EBI-77321, EBI-751319;
Q96GN5:CDCA7L; NbExp=3; IntAct=EBI-77321, EBI-5278764;
Q8N726:CDKN2A; NbExp=8; IntAct=EBI-77321, EBI-625922;
Q92793:CREBBP; NbExp=2; IntAct=EBI-77321, EBI-81215;
P03244:E1B (xeno); NbExp=4; IntAct=EBI-77321, EBI-1561155;
P14921-1:ETS1; NbExp=3; IntAct=EBI-287635, EBI-913224;
P14921-2:ETS1; NbExp=2; IntAct=EBI-287635, EBI-913228;
Q8IZU0:FAM9B; NbExp=3; IntAct=EBI-77321, EBI-10175124;
P25445:FAS; NbExp=3; IntAct=EBI-77321, EBI-494743;
P25446:Fas (xeno); NbExp=4; IntAct=EBI-77321, EBI-296206;
P02794:FTH1; NbExp=5; IntAct=EBI-77321, EBI-713259;
Q08379:GOLGA2; NbExp=7; IntAct=EBI-77321, EBI-618309;
P84243:H3F3B; NbExp=21; IntAct=EBI-287635, EBI-120658;
Q13547:HDAC1; NbExp=2; IntAct=EBI-77321, EBI-301834;
Q92769:HDAC2; NbExp=2; IntAct=EBI-77321, EBI-301821;
O88904:Hipk1 (xeno); NbExp=3; IntAct=EBI-77321, EBI-692945;
P68431:HIST1H3D; NbExp=6; IntAct=EBI-287635, EBI-79722;
Q71DI3:HIST2H3A; NbExp=5; IntAct=EBI-287635, EBI-750650;
P04792:HSPB1; NbExp=4; IntAct=EBI-77321, EBI-352682;
P15991:HSPB1 (xeno); NbExp=3; IntAct=EBI-77321, EBI-1559114;
Q99683:MAP3K5; NbExp=7; IntAct=EBI-77321, EBI-476263;
Q96EZ8:MCRS1; NbExp=10; IntAct=EBI-77321, EBI-348259;
Q00987:MDM2; NbExp=18; IntAct=EBI-77321, EBI-389668;
Q9UHC7:MKRN1; NbExp=4; IntAct=EBI-77321, EBI-373524;
Q7Z6G3-2:NECAB2; NbExp=3; IntAct=EBI-77321, EBI-10172876;
Q9BZ95:NSD3; NbExp=2; IntAct=EBI-77321, EBI-3390132;
Q99497:PARK7; NbExp=3; IntAct=EBI-77321, EBI-1164361;
Q02650:Pax5 (xeno); NbExp=4; IntAct=EBI-77321, EBI-296260;
Q96AQ6:PBXIP1; NbExp=3; IntAct=EBI-77321, EBI-740845;
P29590:PML; NbExp=6; IntAct=EBI-77321, EBI-295890;
Q8ND90:PNMA1; NbExp=4; IntAct=EBI-77321, EBI-302345;
Q9NS23:RASSF1; NbExp=6; IntAct=EBI-77321, EBI-367363;
Q9NS23-4:RASSF1; NbExp=5; IntAct=EBI-77321, EBI-438710;
Q04206:RELA; NbExp=5; IntAct=EBI-77321, EBI-73886;
Q9QZL0:Ripk3 (xeno); NbExp=2; IntAct=EBI-77321, EBI-2367423;
O43791:SPOP; NbExp=5; IntAct=EBI-77321, EBI-743549;
Q9Y2D8:SSX2IP; NbExp=3; IntAct=EBI-77321, EBI-2212028;
P40763:STAT3; NbExp=4; IntAct=EBI-77321, EBI-518675;
P63165:SUMO1; NbExp=7; IntAct=EBI-77321, EBI-80140;
Q9NQB0:TCF7L2; NbExp=5; IntAct=EBI-77321, EBI-924724;
P37173:TGFBR2; NbExp=2; IntAct=EBI-77321, EBI-296151;
P04637:TP53; NbExp=12; IntAct=EBI-77321, EBI-366083;
Q99816:TSG101; NbExp=4; IntAct=EBI-77321, EBI-346882;
P0CG48:UBC; NbExp=2; IntAct=EBI-77321, EBI-3390054;
P63279:UBE2I; NbExp=3; IntAct=EBI-77321, EBI-80168;
Q93009:USP7; NbExp=13; IntAct=EBI-77321, EBI-302474;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11495919,
ECO:0000269|PubMed:11842083, ECO:0000269|PubMed:12968034,
ECO:0000269|PubMed:9407001}. Nucleus, nucleoplasm
{ECO:0000269|PubMed:10669754, ECO:0000269|PubMed:16845383,
ECO:0000269|PubMed:18566590, ECO:0000269|PubMed:23222847,
ECO:0000269|PubMed:9407001}. Nucleus, PML body
{ECO:0000269|PubMed:10669754, ECO:0000269|PubMed:11842083,
ECO:0000269|PubMed:14990586, ECO:0000269|PubMed:17081986,
ECO:0000269|PubMed:21482821, ECO:0000269|PubMed:23222847,
ECO:0000269|PubMed:24200965, ECO:0000269|PubMed:25275136}.
Nucleus, nucleolus {ECO:0000269|PubMed:23222847}. Chromosome,
centromere {ECO:0000269|PubMed:24200965,
ECO:0000269|PubMed:9645950}. Note=Dispersed throughout the
nucleoplasm, in PML/POD/ND10 nuclear bodies, and in nucleoli
(Probable). Colocalizes with histone H3.3, ATRX, HIRA and ASF1A at
PML-nuclear bodies (PubMed:12953102, PubMed:14990586,
PubMed:23222847, PubMed:24200965). Colocalizes with a subset of
interphase centromeres, but is absent from mitotic centromeres
(PubMed:9645950). Detected in cytoplasmic punctate structures
(PubMed:11842083). Translocates from the nucleus to the cytoplasm
upon glucose deprivation or oxidative stress (PubMed:12968034).
Colocalizes with RASSF1 in the nucleus (PubMed:18566590).
Colocalizes with USP7 in nucleoplasma with accumulation in
speckled structures (PubMed:16845383).
{ECO:0000269|PubMed:11842083, ECO:0000269|PubMed:12953102,
ECO:0000269|PubMed:12968034, ECO:0000269|PubMed:14990586,
ECO:0000269|PubMed:16845383, ECO:0000269|PubMed:18566590,
ECO:0000269|PubMed:23222847, ECO:0000269|PubMed:24200965,
ECO:0000269|PubMed:9645950, ECO:0000305|PubMed:10669754}.
-!- SUBCELLULAR LOCATION: Isoform beta: Nucleus
{ECO:0000269|PubMed:21482821}. Note=Diffuse nuclear distribution
pattern and no comparable dot-like accumulation of isoform 1.
{ECO:0000269|PubMed:21482821}.
-!- SUBCELLULAR LOCATION: Isoform gamma: Nucleus
{ECO:0000269|PubMed:21482821}. Note=Diffuse nuclear distribution
pattern and no comparable dot-like accumulation of isoform 1.
{ECO:0000269|PubMed:21482821}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=Q9UER7-1; Sequence=Displayed;
Name=2;
IsoId=Q9UER7-2; Sequence=VSP_001270;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q9UER7-3; Sequence=VSP_045588;
Note=No experimental confirmation available.;
Name=beta;
IsoId=Q9UER7-4; Sequence=VSP_057438, VSP_057440;
Note=Markedly decreased affinity for PML and TP53/p53, unable to
repress p53-mediated transcription.
{ECO:0000269|PubMed:21482821};
Name=gamma;
IsoId=Q9UER7-5; Sequence=VSP_057437, VSP_057439;
Note=Markedly decreased affinity for PML and TP53/p53, unable to
repress p53-mediated transcription.
{ECO:0000269|PubMed:21482821};
-!- 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.
-!- PTM: Sumoylated with SUMO1 on multiple lysine residues.
{ECO:0000269|PubMed:11842083, ECO:0000269|PubMed:12150977,
ECO:0000269|PubMed:17081986}.
-!- PTM: Phosphorylated by HIPK1 upon glucose deprivation.
{ECO:0000269|PubMed:10393185, ECO:0000269|PubMed:12140263,
ECO:0000269|PubMed:12968034}.
-!- PTM: Polyubiquitinated; which is promoted by CUL3 and SPOP and
results in proteasomal degradation. Ubiquitinated by MDM2;
inducing its degradation. Deubiquitinated by USP7; leading to
stabilize it. {ECO:0000269|PubMed:16524876,
ECO:0000269|PubMed:20153724}.
-!- SIMILARITY: Belongs to the DAXX family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/DAXXID40265ch6p21.html";
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EMBL; AF039136; AAB92671.1; -; mRNA.
EMBL; AF006041; AAB63043.1; -; mRNA.
EMBL; AF015956; AAB66585.2; -; mRNA.
EMBL; AF050179; AAC39853.1; -; mRNA.
EMBL; AF097742; AAC72843.1; -; mRNA.
EMBL; HQ436528; AEC33235.1; -; mRNA.
EMBL; HQ436529; AEC33236.1; -; mRNA.
EMBL; AB015051; BAA34295.1; -; mRNA.
EMBL; AK303854; BAG64795.1; -; mRNA.
EMBL; CR457085; CAG33366.1; -; mRNA.
EMBL; AL662827; CAI17527.1; -; Genomic_DNA.
EMBL; AL662820; CAI18124.1; -; Genomic_DNA.
EMBL; BX248088; CAI41788.1; -; Genomic_DNA.
EMBL; CR759793; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CR759817; CAQ08035.1; -; Genomic_DNA.
EMBL; CR759786; CAQ08265.1; -; Genomic_DNA.
EMBL; Z97183; CAB09986.2; -; Genomic_DNA.
EMBL; Z97184; CAB09986.2; JOINED; Genomic_DNA.
EMBL; Z97184; CAB09989.2; -; Genomic_DNA.
EMBL; Z97183; CAB09989.2; JOINED; Genomic_DNA.
EMBL; CH471081; EAX03722.1; -; Genomic_DNA.
EMBL; BC000220; AAH00220.1; -; mRNA.
EMBL; BC109073; AAI09074.1; -; mRNA.
EMBL; BC109074; AAI09075.1; -; mRNA.
CCDS; CCDS4776.1; -. [Q9UER7-1]
CCDS; CCDS59008.1; -. [Q9UER7-3]
PIR; T03847; T03847.
RefSeq; NP_001135441.1; NM_001141969.1. [Q9UER7-1]
RefSeq; NP_001241646.1; NM_001254717.1. [Q9UER7-3]
RefSeq; NP_001341.1; NM_001350.4. [Q9UER7-1]
UniGene; Hs.336916; -.
PDB; 2KQS; NMR; -; B=721-740.
PDB; 2KZS; NMR; -; A=55-144.
PDB; 2KZU; NMR; -; A=55-144.
PDB; 4H9N; X-ray; 1.95 A; C=178-389.
PDB; 4H9O; X-ray; 2.05 A; C=178-389.
PDB; 4H9P; X-ray; 2.20 A; C=178-389.
PDB; 4H9Q; X-ray; 1.95 A; C=178-389.
PDB; 4H9R; X-ray; 2.20 A; C=178-389.
PDB; 4H9S; X-ray; 2.60 A; E/F=183-398.
PDB; 4HGA; X-ray; 2.80 A; A=184-390.
PDB; 5KDM; X-ray; 3.50 A; C=178-389.
PDBsum; 2KQS; -.
PDBsum; 2KZS; -.
PDBsum; 2KZU; -.
PDBsum; 4H9N; -.
PDBsum; 4H9O; -.
PDBsum; 4H9P; -.
PDBsum; 4H9Q; -.
PDBsum; 4H9R; -.
PDBsum; 4H9S; -.
PDBsum; 4HGA; -.
PDBsum; 5KDM; -.
DisProt; DP00707; -.
ProteinModelPortal; Q9UER7; -.
SMR; Q9UER7; -.
BioGrid; 107985; 233.
CORUM; Q9UER7; -.
DIP; DIP-27628N; -.
IntAct; Q9UER7; 124.
MINT; MINT-122943; -.
STRING; 9606.ENSP00000266000; -.
iPTMnet; Q9UER7; -.
PhosphoSitePlus; Q9UER7; -.
BioMuta; DAXX; -.
DMDM; 24636785; -.
EPD; Q9UER7; -.
PaxDb; Q9UER7; -.
PeptideAtlas; Q9UER7; -.
PRIDE; Q9UER7; -.
DNASU; 1616; -.
Ensembl; ENST00000266000; ENSP00000266000; ENSG00000204209. [Q9UER7-1]
Ensembl; ENST00000374542; ENSP00000363668; ENSG00000204209. [Q9UER7-1]
Ensembl; ENST00000383062; ENSP00000372539; ENSG00000206206. [Q9UER7-1]
Ensembl; ENST00000383194; ENSP00000372681; ENSG00000206279. [Q9UER7-1]
Ensembl; ENST00000399060; ENSP00000382014; ENSG00000206206. [Q9UER7-1]
Ensembl; ENST00000399344; ENSP00000382281; ENSG00000206279. [Q9UER7-1]
Ensembl; ENST00000414083; ENSP00000396876; ENSG00000204209. [Q9UER7-3]
Ensembl; ENST00000433482; ENSP00000404623; ENSG00000231617. [Q9UER7-1]
Ensembl; ENST00000436311; ENSP00000404376; ENSG00000227046. [Q9UER7-1]
Ensembl; ENST00000445009; ENSP00000394108; ENSG00000231617. [Q9UER7-1]
Ensembl; ENST00000455860; ENSP00000410772; ENSG00000227046. [Q9UER7-1]
Ensembl; ENST00000612868; ENSP00000479172; ENSG00000227046. [Q9UER7-3]
Ensembl; ENST00000612888; ENSP00000483394; ENSG00000206206. [Q9UER7-3]
Ensembl; ENST00000613912; ENSP00000477633; ENSG00000206206. [Q9UER7-4]
Ensembl; ENST00000616312; ENSP00000483517; ENSG00000227046. [Q9UER7-4]
Ensembl; ENST00000617660; ENSP00000480448; ENSG00000206279. [Q9UER7-3]
Ensembl; ENST00000619421; ENSP00000478810; ENSG00000206279. [Q9UER7-4]
Ensembl; ENST00000620164; ENSP00000482399; ENSG00000204209. [Q9UER7-4]
Ensembl; ENST00000622655; ENSP00000484830; ENSG00000231617. [Q9UER7-4]
GeneID; 1616; -.
KEGG; hsa:1616; -.
UCSC; uc003oec.4; human. [Q9UER7-1]
UCSC; uc063nwl.1; human.
CTD; 1616; -.
DisGeNET; 1616; -.
EuPathDB; HostDB:ENSG00000204209.10; -.
GeneCards; DAXX; -.
HGNC; HGNC:2681; DAXX.
HPA; CAB002224; -.
HPA; CAB025546; -.
HPA; HPA008736; -.
HPA; HPA008797; -.
HPA; HPA065779; -.
MIM; 603186; gene.
neXtProt; NX_Q9UER7; -.
OpenTargets; ENSG00000204209; -.
PharmGKB; PA27148; -.
eggNOG; ENOG410IGIP; Eukaryota.
eggNOG; ENOG4111K0B; LUCA.
GeneTree; ENSGT00390000009448; -.
HOGENOM; HOG000112148; -.
HOVERGEN; HBG031495; -.
InParanoid; Q9UER7; -.
KO; K02308; -.
OMA; LCKTQTA; -.
OrthoDB; EOG09370P3D; -.
PhylomeDB; Q9UER7; -.
TreeFam; TF325803; -.
BRENDA; 2.7.7.19; 2681.
Reactome; R-HSA-6804757; Regulation of TP53 Degradation.
SignaLink; Q9UER7; -.
SIGNOR; Q9UER7; -.
ChiTaRS; DAXX; human.
EvolutionaryTrace; Q9UER7; -.
GeneWiki; Death-associated_protein_6; -.
GenomeRNAi; 1616; -.
PRO; PR:Q9UER7; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000204209; -.
CleanEx; HS_DAXX; -.
ExpressionAtlas; Q9UER7; baseline and differential.
Genevisible; Q9UER7; HS.
GO; GO:0000775; C:chromosome, centromeric region; IDA:CACAO.
GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0016605; C:PML body; IDA:UniProtKB.
GO; GO:0070603; C:SWI/SNF superfamily-type complex; IDA:UniProtKB.
GO; GO:0050681; F:androgen receptor binding; IPI:UniProtKB.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0031072; F:heat shock protein binding; TAS:UniProtKB.
GO; GO:0042393; F:histone binding; IDA:UniProtKB.
GO; GO:0002039; F:p53 binding; IPI:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IDA:CAFA.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0030295; F:protein kinase activator activity; IGI:ParkinsonsUK-UCL.
GO; GO:0019901; F:protein kinase binding; IPI:ParkinsonsUK-UCL.
GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
GO; GO:0005057; F:signal transducer activity, downstream of receptor; TAS:ProtInc.
GO; GO:0032183; F:SUMO binding; IPI:CAFA.
GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IDA:UniProtKB.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0007257; P:activation of JUN kinase activity; TAS:ProtInc.
GO; GO:0030521; P:androgen receptor signaling pathway; IDA:UniProtKB.
GO; GO:0006915; P:apoptotic process; TAS:UniProtKB.
GO; GO:0071276; P:cellular response to cadmium ion; IDA:UniProtKB.
GO; GO:0071280; P:cellular response to copper ion; IDA:UniProtKB.
GO; GO:0072738; P:cellular response to diamide; IDA:UniProtKB.
GO; GO:0034605; P:cellular response to heat; IDA:UniProtKB.
GO; GO:1903936; P:cellular response to sodium arsenite; IDA:UniProtKB.
GO; GO:0034620; P:cellular response to unfolded protein; IDA:UniProtKB.
GO; GO:0006338; P:chromatin remodeling; IDA:UniProtKB.
GO; GO:0016569; P:covalent chromatin modification; IEA:UniProtKB-KW.
GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; TAS:ProtInc.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0006334; P:nucleosome assembly; IDA:UniProtKB.
GO; GO:1901216; P:positive regulation of neuron death; IGI:ParkinsonsUK-UCL.
GO; GO:0045860; P:positive regulation of protein kinase activity; IGI:ParkinsonsUK-UCL.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IGI:ParkinsonsUK-UCL.
GO; GO:0031396; P:regulation of protein ubiquitination; IDA:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
CDD; cd13151; DAXX_helical_bundle; 1.
Gene3D; 3.80.10.10; -; 1.
InterPro; IPR005012; Daxx.
InterPro; IPR031333; Daxx_N.
InterPro; IPR032675; L_dom-like.
PANTHER; PTHR12766; PTHR12766; 1.
Pfam; PF03344; Daxx; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Apoptosis;
Centromere; Chaperone; Chromatin regulator; Chromosome; Coiled coil;
Complete proteome; Cytoplasm; Host-virus interaction; Isopeptide bond;
Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 740 Death domain-associated protein 6.
/FTId=PRO_0000151258.
REGION 1 160 Necessary for interaction with USP7 and
ATRX.
REGION 183 417 Interaction with histone H3.3.
REGION 347 570 Necessary for interaction with USP7.
REGION 501 625 Interaction with MAP3K5.
REGION 626 740 Interaction with SPOP.
{ECO:0000269|PubMed:15240113}.
REGION 733 740 Sumo interaction motif (SIM).
COILED 180 217 {ECO:0000255}.
COILED 358 399 {ECO:0000255}.
COILED 430 489 {ECO:0000255}.
MOTIF 391 395 Nuclear localization signal.
{ECO:0000255}.
MOTIF 628 634 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 11 16 Poly-Asp.
COMPBIAS 434 572 Asp/Glu-rich (acidic).
MOD_RES 25 25 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 178 178 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 213 213 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 412 412 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 424 424 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 459 459 Phosphothreonine.
{ECO:0000250|UniProtKB:O35613}.
MOD_RES 495 495 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 498 498 Phosphoserine.
{ECO:0000250|UniProtKB:Q8VIB2}.
MOD_RES 512 512 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 561 561 Phosphoserine.
{ECO:0000250|UniProtKB:Q8VIB2}.
MOD_RES 580 580 Phosphoserine.
{ECO:0000250|UniProtKB:Q8VIB2}.
MOD_RES 668 668 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000269|PubMed:12968034}.
MOD_RES 671 671 Phosphoserine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 688 688 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 702 702 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 737 737 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231}.
MOD_RES 739 739 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231}.
CROSSLNK 142 142 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 630 630 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000269|PubMed:12150977}.
CROSSLNK 631 631 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000269|PubMed:12150977}.
VAR_SEQ 1 75 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045588.
VAR_SEQ 648 682 YVERQRSVHEKNGKKICTLPSPPSPLASLAPVADS -> PA
VPNPPFTASSAWYLQDKCGHTMRSRRDHRALRL (in
isoform gamma).
{ECO:0000303|PubMed:21482821}.
/FTId=VSP_057437.
VAR_SEQ 653 688 RSVHEKNGKKICTLPSPPSPLASLAPVADSSTRVDS -> S
PAVPNPPFTASSAWYLQDKCGHTMRSRRDHRALRL (in
isoform beta).
{ECO:0000303|PubMed:21482821}.
/FTId=VSP_057438.
VAR_SEQ 683 740 Missing (in isoform gamma).
{ECO:0000303|PubMed:21482821}.
/FTId=VSP_057439.
VAR_SEQ 689 740 Missing (in isoform beta).
{ECO:0000303|PubMed:21482821}.
/FTId=VSP_057440.
VAR_SEQ 696 740 SSLCIPSPARLSQTPHSQPPRPGTCKTSVATQCDPEEIIVL
SDSD -> PAKNLGRRRSKQDQG (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_001270.
MUTAGEN 206 206 Q->L: Impairs interaction with histones
H3 and H4. {ECO:0000269|PubMed:23075851}.
MUTAGEN 220 220 S->A: Abolishes interaction with histones
H3 and H4. {ECO:0000269|PubMed:23075851}.
MUTAGEN 222 222 Y->A,S: Abolishes interaction with
histones H3 and H4.
{ECO:0000269|PubMed:23075851,
ECO:0000269|PubMed:23142979}.
MUTAGEN 222 222 Y->E: Abolishes interaction with histone
H3.3. {ECO:0000269|PubMed:23075851,
ECO:0000269|PubMed:23142979}.
MUTAGEN 225 225 E->L: Impairs interaction with histones
H3 and H4. {ECO:0000269|PubMed:23075851}.
MUTAGEN 229 229 K->A,L: Impairs interaction with histones
H3 and H4. {ECO:0000269|PubMed:23075851}.
MUTAGEN 251 251 R->A: Abolishes interaction with histones
H3 and H4. {ECO:0000269|PubMed:23075851}.
MUTAGEN 317 317 F->A: Abolishes interaction with histones
H3 and H4. {ECO:0000269|PubMed:23075851}.
MUTAGEN 328 328 R->A: Abolishes interaction with histones
H3 and H4. {ECO:0000269|PubMed:23075851}.
MUTAGEN 331 331 D->A: Abolishes interaction with histones
H3 and H4. {ECO:0000269|PubMed:23075851}.
MUTAGEN 630 630 K->A: Abolishes sumoylation; when
associated with A-631.
{ECO:0000269|PubMed:12150977}.
MUTAGEN 631 631 K->A: Abolishes sumoylation; when
associated with A-630.
{ECO:0000269|PubMed:12150977}.
MUTAGEN 668 668 S->A: No translocation to the cytosol
upon glucose deprivation.
{ECO:0000269|PubMed:12968034}.
MUTAGEN 671 671 S->A: No effect on cytosol translocation.
upon glucose deprivation.
{ECO:0000269|PubMed:12968034}.
MUTAGEN 733 740 Missing: Abolishes sumoylation.
{ECO:0000269|PubMed:17081986}.
CONFLICT 177 177 Q -> R (in Ref. 2; AAB66585).
{ECO:0000305}.
CONFLICT 263 263 R -> H (in Ref. 5; AAC72843).
{ECO:0000305}.
CONFLICT 323 323 R -> W (in Ref. 2; AAB66585).
{ECO:0000305}.
CONFLICT 365 365 R -> Q (in Ref. 2; AAB66585).
{ECO:0000305}.
CONFLICT 382 382 L -> S (in Ref. 2; AAB66585).
{ECO:0000305}.
CONFLICT 505 505 E -> G (in Ref. 8; BAG64795).
{ECO:0000305}.
CONFLICT 647 647 S -> R (in Ref. 10; CAB09986/CAB09989).
{ECO:0000305}.
CONFLICT 722 722 T -> A (in Ref. 10; CAB09986/CAB09989).
{ECO:0000305}.
CONFLICT 731 732 EE -> KK (in Ref. 5; AAC72843).
{ECO:0000305}.
HELIX 60 77 {ECO:0000244|PDB:2KZS}.
TURN 78 80 {ECO:0000244|PDB:2KZU}.
HELIX 84 93 {ECO:0000244|PDB:2KZS}.
HELIX 97 100 {ECO:0000244|PDB:2KZS}.
HELIX 103 118 {ECO:0000244|PDB:2KZS}.
HELIX 120 122 {ECO:0000244|PDB:2KZU}.
HELIX 123 136 {ECO:0000244|PDB:2KZS}.
STRAND 138 140 {ECO:0000244|PDB:2KZS}.
HELIX 185 206 {ECO:0000244|PDB:4H9N}.
HELIX 214 216 {ECO:0000244|PDB:4H9N}.
HELIX 221 242 {ECO:0000244|PDB:4H9N}.
HELIX 252 254 {ECO:0000244|PDB:4H9N}.
HELIX 265 275 {ECO:0000244|PDB:4H9N}.
STRAND 278 280 {ECO:0000244|PDB:4H9S}.
HELIX 286 299 {ECO:0000244|PDB:4H9N}.
HELIX 306 333 {ECO:0000244|PDB:4H9N}.
HELIX 339 341 {ECO:0000244|PDB:4H9N}.
HELIX 346 348 {ECO:0000244|PDB:4H9N}.
HELIX 350 353 {ECO:0000244|PDB:4H9N}.
HELIX 355 384 {ECO:0000244|PDB:4H9N}.
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


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CSB-EL006507DO Dog Death domain-associated protein 6(DAXX) ELISA kit 96T
CSB-EL006507MO Mouse Death domain-associated protein 6(DAXX) ELISA kit 96T
CSB-EL006507RA Rat Death domain-associated protein 6(DAXX) ELISA kit SpeciesRat 96T
CSB-EL006507HU Human Death domain-associated protein 6(DAXX) ELISA kit 96T
CSB-EL006507DO Dog Death domain-associated protein 6(DAXX) ELISA kit SpeciesDog 96T
EIAAB14325 Bos taurus,Bovine,FADD,FAS-associated death domain protein,FAS-associating death domain-containing protein,Protein FADD
20-272-190237 FADD - Mouse monoclonal [FD19] to FADD; FAS-associated death domain protein; FAS-associating death domain-containing protein; Mediator of receptor induced toxicity Monoclonal 0.1 ml
CSB-EL006507MO Mouse Death domain-associated protein 6(DAXX) ELISA kit SpeciesMouse 96T


 

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