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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.
02-JUN-2021, entry version 208.
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 (MICROBIAL INFECTION).
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 (MICROBIAL INFECTION).
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 (MICROBIAL INFECTION),
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]
INTERACTION WITH SUMO1P1/SUMO5.
PubMed=27211601; DOI=10.1038/srep26509;
Liang Y.C., Lee C.C., Yao Y.L., Lai C.C., Schmitz M.L., Yang W.M.;
"SUMO5, a novel poly-sumo isoform, regulates pml nuclear bodies.";
Sci. Rep. 6:26509-26509(2016).
[60]
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).
[61]
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).
[62]
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).
[63]
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).
[64]
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
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). Interacts with SUMO1P1/SUMO5 (PubMed:27211601).
{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: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:20444888,
ECO:0000269|PubMed:20504901, ECO:0000269|PubMed:20651253,
ECO:0000269|PubMed:21134643, ECO:0000269|PubMed:23075851,
ECO:0000269|PubMed:23142979, ECO:0000269|PubMed:27211601,
ECO:0000269|PubMed:9645950}.
-!- SUBUNIT: (Microbial infection) Interacts with human
cytomegalovirus/HHV-5 tegument phosphoprotein pp71 and protein UL123.
{ECO:0000269|PubMed:18922870}.
-!- SUBUNIT: (Microbial infection) Interacts with Epstein-Barr virus
protein BNRF1. {ECO:0000269|PubMed:25275136}.
-!- SUBUNIT: (Microbial infection) 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.
{ECO:0000269|PubMed:14557665}.
-!- INTERACTION:
Q9UER7; O43918: AIRE; NbExp=5; IntAct=EBI-77321, EBI-1753081;
Q9UER7; Q9Y2J4: AMOTL2; NbExp=3; IntAct=EBI-77321, EBI-746752;
Q9UER7; Q92870-2: APBB2; NbExp=3; IntAct=EBI-77321, EBI-21535880;
Q9UER7; P10275: AR; NbExp=5; IntAct=EBI-77321, EBI-608057;
Q9UER7; P46100: ATRX; NbExp=8; IntAct=EBI-77321, EBI-396461;
Q9UER7; Q9H257: CARD9; NbExp=3; IntAct=EBI-77321, EBI-751319;
Q9UER7; Q96GN5: CDCA7L; NbExp=3; IntAct=EBI-77321, EBI-5278764;
Q9UER7; Q8N726: CDKN2A; NbExp=8; IntAct=EBI-77321, EBI-625922;
Q9UER7; Q96MT8-3: CEP63; NbExp=3; IntAct=EBI-77321, EBI-11522539;
Q9UER7; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-77321, EBI-739624;
Q9UER7; Q92793: CREBBP; NbExp=2; IntAct=EBI-77321, EBI-81215;
Q9UER7; Q9NPF5: DMAP1; NbExp=3; IntAct=EBI-77321, EBI-399105;
Q9UER7; G5E9A7: DMWD; NbExp=3; IntAct=EBI-77321, EBI-10976677;
Q9UER7; Q8IZU0: FAM9B; NbExp=4; IntAct=EBI-77321, EBI-10175124;
Q9UER7; P25445: FAS; NbExp=3; IntAct=EBI-77321, EBI-494743;
Q9UER7; P02794: FTH1; NbExp=5; IntAct=EBI-77321, EBI-713259;
Q9UER7; O95995: GAS8; NbExp=5; IntAct=EBI-77321, EBI-1052570;
Q9UER7; Q53GS7: GLE1; NbExp=3; IntAct=EBI-77321, EBI-1955541;
Q9UER7; Q96IK5: GMCL1; NbExp=3; IntAct=EBI-77321, EBI-2548508;
Q9UER7; Q08379: GOLGA2; NbExp=8; IntAct=EBI-77321, EBI-618309;
Q9UER7; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-77321, EBI-5916454;
Q9UER7; Q4V328: GRIPAP1; NbExp=3; IntAct=EBI-77321, EBI-717919;
Q9UER7; P84243: H3-3B; NbExp=6; IntAct=EBI-77321, EBI-120658;
Q9UER7; Q6NXT2: H3-5; NbExp=3; IntAct=EBI-77321, EBI-2868501;
Q9UER7; Q13547: HDAC1; NbExp=2; IntAct=EBI-77321, EBI-301834;
Q9UER7; Q92769: HDAC2; NbExp=2; IntAct=EBI-77321, EBI-301821;
Q9UER7; P04792: HSPB1; NbExp=4; IntAct=EBI-77321, EBI-352682;
Q9UER7; P42858: HTT; NbExp=15; IntAct=EBI-77321, EBI-466029;
Q9UER7; Q8WVF5: KCTD4; NbExp=3; IntAct=EBI-77321, EBI-741463;
Q9UER7; Q9P2G9-2: KLHL8; NbExp=3; IntAct=EBI-77321, EBI-11959635;
Q9UER7; Q99683: MAP3K5; NbExp=7; IntAct=EBI-77321, EBI-476263;
Q9UER7; Q96EZ8: MCRS1; NbExp=11; IntAct=EBI-77321, EBI-348259;
Q9UER7; Q00987: MDM2; NbExp=18; IntAct=EBI-77321, EBI-389668;
Q9UER7; Q8TD10: MIPOL1; NbExp=3; IntAct=EBI-77321, EBI-2548751;
Q9UER7; Q9UHC7: MKRN1; NbExp=3; IntAct=EBI-77321, EBI-373524;
Q9UER7; Q8NCY6: MSANTD4; NbExp=3; IntAct=EBI-77321, EBI-7850168;
Q9UER7; Q7Z6G3-2: NECAB2; NbExp=6; IntAct=EBI-77321, EBI-10172876;
Q9UER7; Q9BZ95: NSD3; NbExp=2; IntAct=EBI-77321, EBI-3390132;
Q9UER7; Q99497: PARK7; NbExp=6; IntAct=EBI-77321, EBI-1164361;
Q9UER7; Q96AQ6: PBXIP1; NbExp=3; IntAct=EBI-77321, EBI-740845;
Q9UER7; Q7Z412: PEX26; NbExp=3; IntAct=EBI-77321, EBI-752057;
Q9UER7; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-77321, EBI-14066006;
Q9UER7; P29590: PML; NbExp=6; IntAct=EBI-77321, EBI-295890;
Q9UER7; D3DTS7: PMP22; NbExp=3; IntAct=EBI-77321, EBI-25882629;
Q9UER7; Q8ND90: PNMA1; NbExp=5; IntAct=EBI-77321, EBI-302345;
Q9UER7; Q9NS23: RASSF1; NbExp=6; IntAct=EBI-77321, EBI-367363;
Q9UER7; Q9NS23-4: RASSF1; NbExp=5; IntAct=EBI-77321, EBI-438710;
Q9UER7; Q86WH2: RASSF3; NbExp=3; IntAct=EBI-77321, EBI-2845202;
Q9UER7; Q04206: RELA; NbExp=5; IntAct=EBI-77321, EBI-73886;
Q9UER7; P78317: RNF4; NbExp=3; IntAct=EBI-77321, EBI-2340927;
Q9UER7; Q9UJW9: SERTAD3; NbExp=3; IntAct=EBI-77321, EBI-748621;
Q9UER7; O43791: SPOP; NbExp=5; IntAct=EBI-77321, EBI-743549;
Q9UER7; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-77321, EBI-5235340;
Q9UER7; Q9Y2D8: SSX2IP; NbExp=3; IntAct=EBI-77321, EBI-2212028;
Q9UER7; P40763: STAT3; NbExp=4; IntAct=EBI-77321, EBI-518675;
Q9UER7; P63165: SUMO1; NbExp=7; IntAct=EBI-77321, EBI-80140;
Q9UER7; Q86VP1: TAX1BP1; NbExp=3; IntAct=EBI-77321, EBI-529518;
Q9UER7; Q9NQB0: TCF7L2; NbExp=5; IntAct=EBI-77321, EBI-924724;
Q9UER7; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-77321, EBI-1105213;
Q9UER7; P37173: TGFBR2; NbExp=2; IntAct=EBI-77321, EBI-296151;
Q9UER7; P04637: TP53; NbExp=12; IntAct=EBI-77321, EBI-366083;
Q9UER7; Q99816: TSG101; NbExp=4; IntAct=EBI-77321, EBI-346882;
Q9UER7; P0CG48: UBC; NbExp=2; IntAct=EBI-77321, EBI-3390054;
Q9UER7; P63279: UBE2I; NbExp=3; IntAct=EBI-77321, EBI-80168;
Q9UER7; Q495M9: USH1G; NbExp=3; IntAct=EBI-77321, EBI-8601749;
Q9UER7; Q93009: USP7; NbExp=14; IntAct=EBI-77321, EBI-302474;
Q9UER7; Q8N680: ZBTB2; NbExp=3; IntAct=EBI-77321, EBI-2515601;
Q9UER7; Q9HCK0: ZBTB26; NbExp=3; IntAct=EBI-77321, EBI-3918996;
Q9UER7; P03179: BNRF1; Xeno; NbExp=5; IntAct=EBI-77321, EBI-9349301;
Q9UER7; P03244: E1B; Xeno; NbExp=4; IntAct=EBI-77321, EBI-1561155;
Q9UER7; P25446: Fas; Xeno; NbExp=4; IntAct=EBI-77321, EBI-296206;
Q9UER7; O88904: Hipk1; Xeno; NbExp=3; IntAct=EBI-77321, EBI-692945;
Q9UER7; P15991: HSPB1; Xeno; NbExp=3; IntAct=EBI-77321, EBI-1559114;
Q9UER7; Q02650: Pax5; Xeno; NbExp=4; IntAct=EBI-77321, EBI-296260;
Q9UER7; Q9QZL0: Ripk3; Xeno; NbExp=2; IntAct=EBI-77321, EBI-2367423;
Q9UER7; P03243; Xeno; NbExp=4; IntAct=EBI-77321, EBI-1561361;
Q9UER7-1; P14921-1: ETS1; NbExp=3; IntAct=EBI-287635, EBI-913224;
Q9UER7-1; P14921-2: ETS1; NbExp=2; IntAct=EBI-287635, EBI-913228;
Q9UER7-1; P84243: H3-3B; NbExp=21; IntAct=EBI-287635, EBI-120658;
Q9UER7-1; P68431: H3C12; NbExp=6; IntAct=EBI-287635, EBI-79722;
Q9UER7-1; Q71DI3: H3C15; NbExp=5; IntAct=EBI-287635, EBI-750650;
-!- 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;
Name=3;
IsoId=Q9UER7-3; Sequence=VSP_045588;
Name=beta;
IsoId=Q9UER7-4; Sequence=VSP_057438, VSP_057440;
Name=gamma;
IsoId=Q9UER7-5; Sequence=VSP_057437, VSP_057439;
-!- 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}.
-!- MISCELLANEOUS: [Isoform beta]: Markedly decreased affinity for PML and
TP53/p53, unable to repress p53-mediated transcription. {ECO:0000305}.
-!- MISCELLANEOUS: [Isoform gamma]: Markedly decreased affinity for PML and
TP53/p53, unable to repress p53-mediated transcription. {ECO:0000305}.
-!- 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; AL662820; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL662827; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BX248088; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CR759793; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CR759786; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CR759817; -; NOT_ANNOTATED_CDS; 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]
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; 5GRQ; X-ray; 1.58 A; A=55-144, B=55-143.
PDB; 5KDM; X-ray; 3.50 A; C=178-389.
PDB; 5Y18; X-ray; 2.20 A; A=55-144.
PDB; 5Y6O; X-ray; 3.10 A; A/B/C/D/E/F/G/H/I=50-144.
PDBsum; 2KQS; -.
PDBsum; 2KZS; -.
PDBsum; 2KZU; -.
PDBsum; 4H9N; -.
PDBsum; 4H9O; -.
PDBsum; 4H9P; -.
PDBsum; 4H9Q; -.
PDBsum; 4H9R; -.
PDBsum; 4H9S; -.
PDBsum; 4HGA; -.
PDBsum; 5GRQ; -.
PDBsum; 5KDM; -.
PDBsum; 5Y18; -.
PDBsum; 5Y6O; -.
BMRB; Q9UER7; -.
SMR; Q9UER7; -.
BioGRID; 107985; 276.
CORUM; Q9UER7; -.
DIP; DIP-27628N; -.
IntAct; Q9UER7; 162.
MINT; Q9UER7; -.
STRING; 9606.ENSP00000363668; -.
iPTMnet; Q9UER7; -.
PhosphoSitePlus; Q9UER7; -.
BioMuta; DAXX; -.
DMDM; 24636785; -.
EPD; Q9UER7; -.
jPOST; Q9UER7; -.
MassIVE; Q9UER7; -.
PaxDb; Q9UER7; -.
PeptideAtlas; Q9UER7; -.
PRIDE; Q9UER7; -.
ProteomicsDB; 25260; -.
ProteomicsDB; 84150; -. [Q9UER7-1]
ProteomicsDB; 84151; -. [Q9UER7-2]
Antibodypedia; 1411; 995 antibodies.
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; -.
GeneCards; DAXX; -.
HGNC; HGNC:2681; DAXX.
HPA; ENSG00000204209; Low tissue specificity.
MalaCards; DAXX; -.
MIM; 603186; gene.
neXtProt; NX_Q9UER7; -.
OpenTargets; ENSG00000204209; -.
Orphanet; 100075; Neuroendocrine tumor of stomach.
PharmGKB; PA27148; -.
VEuPathDB; HostDB:ENSG00000204209.10; -.
eggNOG; ENOG502QRS6; Eukaryota.
GeneTree; ENSGT00390000009448; -.
HOGENOM; CLU_022811_1_0_1; -.
InParanoid; Q9UER7; -.
OMA; AMMQDKS; -.
PhylomeDB; Q9UER7; -.
TreeFam; TF325803; -.
PathwayCommons; Q9UER7; -.
Reactome; R-HSA-3899300; SUMOylation of transcription cofactors.
Reactome; R-HSA-6804757; Regulation of TP53 Degradation.
Reactome; R-HSA-9609690; HCMV Early Events.
Reactome; R-HSA-9670095; Inhibition of DNA recombination at telomere.
Reactome; R-HSA-9670613; Defective Inhibition of DNA Recombination at Telomere Due to DAXX Mutations.
Reactome; R-HSA-9670615; Defective Inhibition of DNA Recombination at Telomere Due to ATRX Mutations.
SignaLink; Q9UER7; -.
SIGNOR; Q9UER7; -.
BioGRID-ORCS; 1616; 110 hits in 995 CRISPR screens.
ChiTaRS; DAXX; human.
EvolutionaryTrace; Q9UER7; -.
GeneWiki; Death-associated_protein_6; -.
GenomeRNAi; 1616; -.
Pharos; Q9UER7; Tbio.
PRO; PR:Q9UER7; -.
Proteomes; UP000005640; Chromosome 6.
RNAct; Q9UER7; protein.
Bgee; ENSG00000204209; Expressed in granulocyte and 234 other tissues.
ExpressionAtlas; Q9UER7; baseline and differential.
Genevisible; Q9UER7; HS.
GO; GO:0000775; C:chromosome, centromeric region; IDA:CACAO.
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; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:GO_Central.
GO; GO:0016605; C:PML body; 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: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:0140037; F:sumo-dependent protein binding; IPI:UniProtKB.
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:0140416; F:transcription regulator inhibitor activity; IDA:GO_Central.
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: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:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; TAS:ProtInc.
GO; GO:0048239; P:negative regulation of DNA recombination at telomere; TAS:Reactome.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0006334; P:nucleosome assembly; IDA:UniProtKB.
GO; GO:1900051; P:positive regulation of histone exchange; TAS:Reactome.
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:0042981; P:regulation of apoptotic process; IBA:GO_Central.
GO; GO:0031396; P:regulation of protein ubiquitination; IDA:UniProtKB.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0019058; P:viral life cycle; TAS:Reactome.
CDD; cd13151; DAXX_helical_bundle; 1.
DisProt; DP00707; -.
Gene3D; 1.10.8.810; -; 1.
IDEAL; IID00398; -.
InterPro; IPR005012; Daxx.
InterPro; IPR031333; Daxx_N.
InterPro; IPR038298; Daxx_N_sf.
PANTHER; PTHR12766:SF7; PTHR12766:SF7; 1.
Pfam; PF03344; Daxx; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Apoptosis; Centromere;
Chaperone; Chromatin regulator; Chromosome; Coiled coil; Cytoplasm;
Host-virus interaction; Isopeptide bond; Nucleus; Phosphoprotein;
Reference proteome; Repressor; Transcription; Transcription regulation;
Ubl conjugation.
CHAIN 1..740
/note="Death domain-associated protein 6"
/id="PRO_0000151258"
REGION 1..160
/note="Necessary for interaction with USP7 and ATRX"
REGION 1..55
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 147..185
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 183..417
/note="Interaction with histone H3.3"
REGION 347..570
/note="Necessary for interaction with USP7"
REGION 384..724
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 501..625
/note="Interaction with MAP3K5"
REGION 626..740
/note="Interaction with SPOP"
/evidence="ECO:0000269|PubMed:15240113"
REGION 733..740
/note="Sumo interaction motif (SIM)"
COILED 180..217
/evidence="ECO:0000255"
COILED 358..399
/evidence="ECO:0000255"
COILED 430..489
/evidence="ECO:0000255"
MOTIF 391..395
/note="Nuclear localization signal"
/evidence="ECO:0000255"
MOTIF 628..634
/note="Nuclear localization signal"
/evidence="ECO:0000255"
COMPBIAS 147..184
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 434..487
/note="Acidic residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 496..529
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 580..619
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 677..724
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
MOD_RES 25
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:24275569"
MOD_RES 178
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:23186163"
MOD_RES 213
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18669648"
MOD_RES 412
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:23186163"
MOD_RES 424
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:23186163"
MOD_RES 459
/note="Phosphothreonine"
/evidence="ECO:0000250|UniProtKB:O35613"
MOD_RES 495
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
ECO:0007744|PubMed:23186163"
MOD_RES 498
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q8VIB2"
MOD_RES 512
/note="N6-acetyllysine"
/evidence="ECO:0007744|PubMed:19608861"
MOD_RES 561
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q8VIB2"
MOD_RES 580
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q8VIB2"
MOD_RES 668
/note="Phosphoserine"
/evidence="ECO:0000269|PubMed:12968034,
ECO:0007744|PubMed:18669648"
MOD_RES 671
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18220336,
ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
MOD_RES 688
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:23186163"
MOD_RES 702
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:16964243,
ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
MOD_RES 737
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
MOD_RES 739
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
CROSSLNK 142
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0007744|PubMed:28112733"
CROSSLNK 630
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO1)"
/evidence="ECO:0000269|PubMed:12150977"
CROSSLNK 631
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO1)"
/evidence="ECO:0000269|PubMed:12150977"
VAR_SEQ 1..75
/note="Missing (in isoform 3)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_045588"
VAR_SEQ 648..682
/note="YVERQRSVHEKNGKKICTLPSPPSPLASLAPVADS -> PAVPNPPFTASSA
WYLQDKCGHTMRSRRDHRALRL (in isoform gamma)"
/evidence="ECO:0000303|PubMed:21482821"
/id="VSP_057437"
VAR_SEQ 653..688
/note="RSVHEKNGKKICTLPSPPSPLASLAPVADSSTRVDS -> SPAVPNPPFTAS
SAWYLQDKCGHTMRSRRDHRALRL (in isoform beta)"
/evidence="ECO:0000303|PubMed:21482821"
/id="VSP_057438"
VAR_SEQ 683..740
/note="Missing (in isoform gamma)"
/evidence="ECO:0000303|PubMed:21482821"
/id="VSP_057439"
VAR_SEQ 689..740
/note="Missing (in isoform beta)"
/evidence="ECO:0000303|PubMed:21482821"
/id="VSP_057440"
VAR_SEQ 696..740
/note="SSLCIPSPARLSQTPHSQPPRPGTCKTSVATQCDPEEIIVLSDSD -> PAK
NLGRRRSKQDQG (in isoform 2)"
/evidence="ECO:0000303|PubMed:15489334"
/id="VSP_001270"
MUTAGEN 206
/note="Q->L: Impairs interaction with histones H3 and H4."
/evidence="ECO:0000269|PubMed:23075851"
MUTAGEN 220
/note="S->A: Abolishes interaction with histones H3 and
H4."
/evidence="ECO:0000269|PubMed:23075851"
MUTAGEN 222
/note="Y->A,S: Abolishes interaction with histones H3 and
H4."
/evidence="ECO:0000269|PubMed:23075851,
ECO:0000269|PubMed:23142979"
MUTAGEN 222
/note="Y->E: Abolishes interaction with histone H3.3."
/evidence="ECO:0000269|PubMed:23075851,
ECO:0000269|PubMed:23142979"
MUTAGEN 225
/note="E->L: Impairs interaction with histones H3 and H4."
/evidence="ECO:0000269|PubMed:23075851"
MUTAGEN 229
/note="K->A,L: Impairs interaction with histones H3 and
H4."
/evidence="ECO:0000269|PubMed:23075851"
MUTAGEN 251
/note="R->A: Abolishes interaction with histones H3 and
H4."
/evidence="ECO:0000269|PubMed:23075851"
MUTAGEN 317
/note="F->A: Abolishes interaction with histones H3 and
H4."
/evidence="ECO:0000269|PubMed:23075851"
MUTAGEN 328
/note="R->A: Abolishes interaction with histones H3 and
H4."
/evidence="ECO:0000269|PubMed:23075851"
MUTAGEN 331
/note="D->A: Abolishes interaction with histones H3 and
H4."
/evidence="ECO:0000269|PubMed:23075851"
MUTAGEN 630
/note="K->A: Abolishes sumoylation; when associated with A-
631."
/evidence="ECO:0000269|PubMed:12150977"
MUTAGEN 631
/note="K->A: Abolishes sumoylation; when associated with A-
630."
/evidence="ECO:0000269|PubMed:12150977"
MUTAGEN 668
/note="S->A: No translocation to the cytosol upon glucose
deprivation."
/evidence="ECO:0000269|PubMed:12968034"
MUTAGEN 671
/note="S->A: No effect on cytosol translocation. upon
glucose deprivation."
/evidence="ECO:0000269|PubMed:12968034"
MUTAGEN 733..740
/note="Missing: Abolishes sumoylation."
/evidence="ECO:0000269|PubMed:17081986"
CONFLICT 177
/note="Q -> R (in Ref. 2; AAB66585)"
/evidence="ECO:0000305"
CONFLICT 263
/note="R -> H (in Ref. 5; AAC72843)"
/evidence="ECO:0000305"
CONFLICT 323
/note="R -> W (in Ref. 2; AAB66585)"
/evidence="ECO:0000305"
CONFLICT 365
/note="R -> Q (in Ref. 2; AAB66585)"
/evidence="ECO:0000305"
CONFLICT 382
/note="L -> S (in Ref. 2; AAB66585)"
/evidence="ECO:0000305"
CONFLICT 505
/note="E -> G (in Ref. 8; BAG64795)"
/evidence="ECO:0000305"
CONFLICT 647
/note="S -> R (in Ref. 10; CAB09986/CAB09989)"
/evidence="ECO:0000305"
CONFLICT 722
/note="T -> A (in Ref. 10; CAB09986/CAB09989)"
/evidence="ECO:0000305"
CONFLICT 731..732
/note="EE -> KK (in Ref. 5; AAC72843)"
/evidence="ECO:0000305"
HELIX 60..77
/evidence="ECO:0007829|PDB:5GRQ"
TURN 78..80
/evidence="ECO:0007829|PDB:2KZU"
HELIX 84..93
/evidence="ECO:0007829|PDB:5GRQ"
HELIX 97..100
/evidence="ECO:0007829|PDB:5GRQ"
HELIX 103..118
/evidence="ECO:0007829|PDB:5GRQ"
HELIX 120..122
/evidence="ECO:0007829|PDB:5GRQ"
HELIX 123..136
/evidence="ECO:0007829|PDB:5GRQ"
STRAND 138..140
/evidence="ECO:0007829|PDB:2KZS"
HELIX 185..206
/evidence="ECO:0007829|PDB:4H9N"
HELIX 214..216
/evidence="ECO:0007829|PDB:4H9N"
HELIX 221..242
/evidence="ECO:0007829|PDB:4H9N"
HELIX 252..254
/evidence="ECO:0007829|PDB:4H9N"
HELIX 265..275
/evidence="ECO:0007829|PDB:4H9N"
STRAND 278..280
/evidence="ECO:0007829|PDB:4H9S"
HELIX 286..299
/evidence="ECO:0007829|PDB:4H9N"
HELIX 306..333
/evidence="ECO:0007829|PDB:4H9N"
HELIX 339..341
/evidence="ECO:0007829|PDB:4H9N"
HELIX 346..348
/evidence="ECO:0007829|PDB:4H9N"
HELIX 350..353
/evidence="ECO:0007829|PDB:4H9N"
HELIX 355..384
/evidence="ECO:0007829|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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Pathways :
WP1689: Porphyrin and chlorophyll metabolism
WP1659: Glycine, serine and threonine metabolism
WP1713: Two-component system
WP1438: Influenza A virus infection
WP1049: G Protein Signaling Pathways
WP1665: Limonene and pinene degradation
WP232: G Protein Signaling Pathways
WP1675: Nitrogen metabolism
WP1531: Vitamin D synthesis
WP1909: Signal regulatory protein (SIRP) family interactions
WP525: Mitochondrial Unfolded-Protein Response
WP1616: ABC transporters
WP73: G Protein Signaling Pathways
WP1685: Peptidoglycan biosynthesis
WP1692: Protein export
WP1644: DNA replication
WP211: BMP signaling pathway
WP1657: Glycerolipid metabolism
WP2218: sGC
WP1700: Selenoamino acid metabolism
WP1663: Homologous recombination
WP2292: Chemokine signaling pathway
WP1371: G Protein Signaling Pathways
WP1673: Naphthalene and anthracene degradation
WP2371: Parkinsons Disease Pathway

Related Genes :
[DAXX BING2 DAP6] Death domain-associated protein 6 (Daxx) (hDaxx) (ETS1-associated protein 1) (EAP1) (Fas death domain-associated protein)
[Daxx] Death domain-associated protein 6 (Daxx)
[ETS1 EWSR2] Protein C-ets-1 (p54)
[Daxx] Death domain-associated protein 6 (Daxx)
[DAXX] Death domain-associated protein 6 (Daxx)
[DAXX] Death domain-associated protein 6 (Daxx)
[Fadd Mort1] FAS-associated death domain protein (FAS-associating death domain-containing protein) (Mediator of receptor induced toxicity)
[IRF2BPL C14orf4 EAP1 KIAA1865 My039] Probable E3 ubiquitin-protein ligase IRF2BPL (EC 2.3.2.27) (Enhanced at puberty protein 1) (Interferon regulatory factor 2-binding protein-like)
[FADD MORT1 GIG3] FAS-associated death domain protein (FAS-associating death domain-containing protein) (Growth-inhibiting gene 3 protein) (Mediator of receptor induced toxicity)
[TDP2 EAP2 TTRAP AD-022] Tyrosyl-DNA phosphodiesterase 2 (Tyr-DNA phosphodiesterase 2) (hTDP2) (EC 3.1.4.-) (5'-tyrosyl-DNA phosphodiesterase) (5'-Tyr-DNA phosphodiesterase) (ETS1-associated protein 2) (ETS1-associated protein II) (EAPII) (TRAF and TNF receptor-associated protein) (Tyrosyl-RNA phosphodiesterase) (VPg unlinkase)
[FADD] FAS-associated death domain protein (FAS-associating death domain-containing protein)
[CASP10 MCH4] Caspase-10 (CASP-10) (EC 3.4.22.63) (Apoptotic protease Mch-4) (FAS-associated death domain protein interleukin-1B-converting enzyme 2) (FLICE2) (ICE-like apoptotic protease 4) [Cleaved into: Caspase-10 subunit p23/17; Caspase-10 subunit p12]
[Fadd fadd rCG_48606] FAS-associated death domain protein (FAS-associating death domain-containing protein) (Protein FADD)
[Bid] BH3-interacting domain death agonist (p22 BID) (BID) [Cleaved into: BH3-interacting domain death agonist p15 (p15 BID); BH3-interacting domain death agonist p13 (p13 BID); BH3-interacting domain death agonist p11 (p11 BID)]
[Nlrp1a Card7 Nalp1 Nalp1a Nlrp1] NACHT, LRR and PYD domains-containing protein 1a (EC 3.4.-.-) (Caspase recruitment domain-containing protein 7) (Death effector filament-forming ced-4-like apoptosis protein) (Nucleotide-binding domain and caspase recruitment domain) [Cleaved into: NACHT, LRR and PYD domains-containing protein 1a, C-terminus (Nlrp1a-CT); NACHT, LRR and PYD domains-containing protein 1a, N-terminus (Nlrp1a-NT)]
[Fas Apt1 Tnfrsf6] Tumor necrosis factor receptor superfamily member 6 (Apo-1 antigen) (Apoptosis-mediating surface antigen FAS) (FASLG receptor) (CD antigen CD95)
[FADD TNFRSF6] FAS-associated death domain protein (FAS-associating death domain-containing protein) (Protein FADD)
[Pdcd6 Alg2] Programmed cell death protein 6 (ALG-257) (Apoptosis-linked gene 2 protein) (ALG-2) (PMP41)
[Ripk1 Rinp Rip] Receptor-interacting serine/threonine-protein kinase 1 (EC 2.7.11.1) (Cell death protein RIP) (Receptor-interacting protein 1) (RIP-1)
[TRADD] Tumor necrosis factor receptor type 1-associated DEATH domain protein (TNFR1-associated DEATH domain protein) (TNFRSF1A-associated via death domain)
[NLRP1 CARD7 DEFCAP KIAA0926 NAC NALP1] NACHT, LRR and PYD domains-containing protein 1 (EC 3.4.-.-) (EC 3.6.4.-) (Caspase recruitment domain-containing protein 7) (Death effector filament-forming ced-4-like apoptosis protein) (Nucleotide-binding domain and caspase recruitment domain) [Cleaved into: NACHT, LRR and PYD domains-containing protein 1, C-terminus (NLRP1-CT); NACHT, LRR and PYD domains-containing protein 1, N-terminus (NLRP1-NT)]
[Tradd] Tumor necrosis factor receptor type 1-associated DEATH domain protein (TNFR1-associated DEATH domain protein) (TNFRSF1A-associated via death domain)
[Aifm1 Aif Pdcd8] Apoptosis-inducing factor 1, mitochondrial (EC 1.6.99.-) (Programmed cell death protein 8)
[FADD] FAS-associated death domain protein (FAS-associating death domain-containing protein) (Protein FADD)
[FAS APT1 FAS1 TNFRSF6] Tumor necrosis factor receptor superfamily member 6 (Apo-1 antigen) (Apoptosis-mediating surface antigen FAS) (FASLG receptor) (CD antigen CD95)
[Rybp Dedaf] RING1 and YY1-binding protein (Death effector domain-associated factor) (DED-associated factor)
[FADD] FAS-associated death domain protein (FAS-associating death domain-containing protein) (Protein FADD)
[FADD] FAS-associated death domain protein (FAS-associating death domain-containing protein) (Protein FADD)
[FADD] FAS-associated death domain protein (FAS-associating death domain-containing protein) (Protein FADD)
[PIDD1 LRDD PIDD] p53-induced death domain-containing protein 1 (EC 3.4.21.-) (Leucine-rich repeat and death domain-containing protein) [Cleaved into: PIDD-N; PIDD-C; PIDD-CC]

Bibliography :