[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). DOI=10.1016/S0092-8674(00)80294-9; PubMed=9215629 [NCBI, ExPASy, EBI, Israel, Japan] 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; DOI=10.1089/dna.1997.16.1289; PubMed=9407001 [NCBI, ExPASy, EBI, Israel, Japan] 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 CENPC1, AND SUBCELLULAR LOCATION. TISSUE=Cervix carcinoma; PubMed=9645950 [NCBI, ExPASy, EBI, Israel, Japan] 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). DOI=10.1006/jmbi.1998.1637; PubMed=9545376 [NCBI, ExPASy, EBI, Israel, Japan] 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; DOI=10.1038/sj.onc.1203385; PubMed=10698492 [NCBI, ExPASy, EBI, Israel, Japan] 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] (ISOFORM 1). Usui T.; Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
[7]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1038/nature02055; PubMed=14574404 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[8]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 334-740 (ISOFORM 2). TISSUE=Eye; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[9]	INTERACTION WITH PAX3 AND PAX7, AND PHOSPHORYLATION. DOI=10.1093/emboj/18.13.3702; PubMed=10393185 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[10]	INTERACTION WITH PML. DOI=10.1084/jem.191.4.631; PubMed=10684855 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[11]	INTERACTION WITH SUMOYLATED PML; HDAC1; HDAC2 AND HDAC3. DOI=10.1128/MCB.20.5.1784-1796.2000; PubMed=10669754 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[12]	INTERACTION WITH HSPB1. DOI=10.1128/MCB.20.20.7602-7612.2000; PubMed=11003656 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[13]	INTERACTION WITH MAP3K5, AND SUBCELLULAR LOCATION. DOI=10.1074/jbc.M105928200; PubMed=11495919 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[14]	INTERACTION WITH TGFBR2. DOI=10.1038/35087019; PubMed=11483955 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[15]	SUMOYLATION, AND MUTAGENESIS OF LYS-630 AND LYS-631. DOI=10.1016/S0006-291X(02)00699-X; PubMed=12150977 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[16]	INTERACTION WITH SLC2A4 AND UBE2I, SUMOYLATION, AND SUBCELLULAR LOCATION. DOI=10.1074/jbc.M110294200; PubMed=11842083 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[17]	INTERACTION WITH MCRS1. DOI=10.1074/jbc.M200633200; PubMed=11948183 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[18]	FUNCTION, PHOSPHORYLATION, AND INTERACTION WITH HDAC2; HISTONES AND DEK. PubMed=12140263 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[19]	INTERACTION WITH HIPK2. PubMed=14678985 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[20]	OLIGOMERIZATION, SUBCELLULAR LOCATION, INTERACTION WITH MAP3K5, MUTAGENESIS OF SER-668 AND SER-671, AND PHOSPHORYLATION AT SER-668. DOI=10.1074/jbc.M213201200; PubMed=12968034 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[21]	INTERACTION WITH HIPK1. DOI=10.1128/MCB.23.3.950-960.2003; PubMed=12529400 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[22]	INTERACTION WITH SPOP. DOI=10.1016/j.bbrc.2004.06.022; PubMed=15240113 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[23]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-671, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1073/pnas.0404720101; PubMed=15302935 [NCBI, ExPASy, EBI, Israel, Japan] Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.; "Large-scale characterization of HeLa cell nuclear phosphoproteins."; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
[24]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-737 AND SER-739, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[25]	IDENTIFICATION IN A COMPLEX WITH CUL3 AND SPOP, AND UBIQUITINATION. DOI=10.1074/jbc.M600204200; PubMed=16524876 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[26]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-648, AND MASS SPECTROMETRY. DOI=10.1073/pnas.0611217104; PubMed=17287340 [NCBI, ExPASy, EBI, Israel, Japan] Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; "Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry."; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
[27]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-709 AND SER-712, AND MASS SPECTROMETRY. DOI=10.1126/science.1140321; PubMed=17525332 [NCBI, ExPASy, EBI, Israel, Japan] Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; "ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."; Science 316:1160-1166(2007).
[28]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178; SER-671; SER-688; SER-690 AND SER-702, AND MASS SPECTROMETRY. DOI=10.1021/pr0705441; PubMed=18220336 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[29]	INTERACTION WITH HCMV PP71. DOI=10.1128/JVI.01215-08; PubMed=18922870 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[30]	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 MASS SPECTROMETRY. DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[31]	IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. Colinge J., Superti-Furga G., Bennett K.L.; Submitted (OCT-2008) to UniProtKB.

Comments

FUNCTION: Proposed to mediate activation of the JNK pathway and apoptosis via MAP3K5 in response to signaling from TNFRSF6 and TGFBR2. Interaction with HSPB1/HSP27 may prevent interaction with TNFRSF6 and MAP3K5 and block DAXX-mediated apoptosis. In contrast, in lymphoid cells JNC activation and TNFRSF6-mediated apoptosis may not involve DAXX. Seems to regulate transcription in PML/POD/ND10 nuclear bodies together with PML and may influence TNFRSF6-dependent apoptosis thereby. Down-regulates basal and activated transcription. Seems to act as a transcriptional co-repressor and inhibits PAX3 and ETS1 through direct protein-protein interaction. Modulates PAX5 activity. Its transcription repressor activity is modulated by recruiting it to subnuclear compartments like the nucleolus or PML/POD/ND10 nuclear bodies through interactions with MCSR1 and PML, respectively.
SUBUNIT: Homomultimer. Binds to the TNFRSF6 death domain via its C-terminus and to PAX5. Binds to SLC2A4/GLUT4, MAP3K5, TGFBR2, phosphorylated dimeric HSPB1/HSP27, CENPC1, ETS1, sumoylated PML, UBE2I and MCRS1. Is part of a complex containing PAX5 and CREBBP. Interacts with HIPK2 and HIPK3 via its N-terminus. Interacts with HIPK1, which induces translocation from PML/POD/ND10 nuclear bodies to chromatin and enhances association with HDAC1 (By similarity). The non-phosphorylated form binds to PAX3, PAX7, DEK, HDAC1, HDAC2, HDAC3, acetylated histone H4 and histones H2A, H2B, H3 and H4. Interacts with SPOP. Part of a complex consisting of DAXX, CUL3 and SPOP. Interacts with CBP; the interaction is dependent the sumoylation of CBP and suppresses CBP transcriptional activity via recruitment of HDAC2 (By similarity). Interacts with HCMV tegument phosphoprotein pp71.
INTERACTION:
Self; NbExp=1; IntAct=EBI-287635, EBI-287635;
P03243:- (xeno); NbExp=1; IntAct=EBI-77321, EBI-1561361;
P10275:AR; NbExp=2; IntAct=EBI-77321, EBI-608057;
P46100:ATRX; NbExp=1; IntAct=EBI-77321, EBI-396461;
Q8N726:CDKN2A; NbExp=3; IntAct=EBI-77321, EBI-625922;
Q92793:CREBBP; NbExp=1; IntAct=EBI-77321, EBI-81215;
O43293:DAPK3; NbExp=1; IntAct=EBI-77321, EBI-77293;
P03244:E1B (xeno); NbExp=3; IntAct=EBI-77321, EBI-1561155;
P14921:ETS1; NbExp=2; IntAct=EBI-287635, EBI-913209;
P14921-1:ETS1; NbExp=1; IntAct=EBI-287635, EBI-913224;
P14921-2:ETS1; NbExp=1; IntAct=EBI-287635, EBI-913228;
P25445:FAS; NbExp=2; IntAct=EBI-77321, EBI-494743;
P25446:Fas (xeno); NbExp=4; IntAct=EBI-77321, EBI-296206;
Q13547:HDAC1; NbExp=1; IntAct=EBI-77321, EBI-301834;
Q92769:HDAC2; NbExp=1; IntAct=EBI-77321, EBI-301821;
Q86Z02:HIPK1; NbExp=1; IntAct=EBI-77321, EBI-692891;
O88904:Hipk1 (xeno); NbExp=1; IntAct=EBI-77321, EBI-692945;
P04792:HSPB1; NbExp=1; IntAct=EBI-77321, EBI-352682;
P15991:HSPB1 (xeno); NbExp=2; IntAct=EBI-77321, EBI-1559114;
Q99683:MAP3K5; NbExp=4; IntAct=EBI-77321, EBI-476263;
Q96EZ8:MCRS1; NbExp=2; IntAct=EBI-77321, EBI-348259;
Q00987:MDM2; NbExp=4; IntAct=EBI-77321, EBI-389668;
Q99497:PARK7; NbExp=1; IntAct=EBI-77321, EBI-1164361;
Q02650:Pax5 (xeno); NbExp=2; IntAct=EBI-77321, EBI-296260;
P29590:PML; NbExp=1; IntAct=EBI-77321, EBI-295890;
P14672:SLC2A4; NbExp=3; IntAct=EBI-77321, EBI-367146;
P40763:STAT3; NbExp=2; IntAct=EBI-77321, EBI-518675;
P63165:SUMO1; NbExp=4; IntAct=EBI-77321, EBI-80140;
Q9NQB0:TCF7L2; NbExp=3; IntAct=EBI-77321, EBI-924724;
P37173:TGFBR2; NbExp=1; IntAct=EBI-77321, EBI-296151;
P04637:TP53; NbExp=3; IntAct=EBI-77321, EBI-366083;
Q99816:TSG101; NbExp=1; IntAct=EBI-77321, EBI-346882;
Q93009:USP7; NbExp=4; IntAct=EBI-77321, EBI-302474;
SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Dispersed throughout the nucleoplasm, in PML/POD/ND10 nuclear bodies, and in nucleoli. Colocalizes with a subset of interphase centromeres, but is absent from mitotic centromeres. Detected in cytoplasmic punctate structures. Translocates from the nucleus to the cytoplasm upon glucose deprivation or oxidative stress.

ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name	1
Isoform ID	Q9UER7-1
This is the isoform sequence displayed in this entry.

Name	2
Isoform ID	Q9UER7-2
Note: No experimental confirmation available.
Features which should be applied to build the isoform sequence: VSP_001270.

TISSUE SPECIFICITY: Ubiquitous.
INDUCTION: Upon mitogenic stimulation by concanavalin A.
PTM: Sumoylated.
PTM: Phosphorylated upon DNA damage, probably by ATM or ATR. Phosphorylated by HIPK1 upon glucose deprivation.
PTM: Polyubiquitinated; which is promoted by CUL3 and SPOP and results in proteasomal degradation.
SIMILARITY: Belongs to the DAXX family.
WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org//Genes/DAXXID40265ch6p21.html";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF039136; AAB92671.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF006041; AAB63043.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF015956; AAB66585.2; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF050179; AAC39853.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z97183; CAB09986.2; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z97184; CAB09986.2; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z97184; CAB09989.2; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z97183; CAB09989.2; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF097742; AAC72843.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB015051; BAA34295.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC000220; AAH00220.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00170867; -.
IPI00220885; -.

PIR

T03847; T03847.

RefSeq

NP_001135441.1; -.
NP_001341.1; -.

UniGene

Hs.336916

3D structure databases

ModBase

Q9UER7.

Protein-protein interaction databases

DIP

DIP:27628N; -.

IntAct

Q9UER7; 43.

PTM databases

PhosphoSite

Q9UER7; -.

Enzyme and pathway databases

Pathway_Interaction_DB

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

Organism-specific databases

GeneCards

GC06M033394; -.

H-InvDB

HIX0032744; -.
HIX0057980; -.
HIX0058158; -.

HGNC:2681; DAXX.

CAB002224; -.
HPA008736; -.

MIM

603186; gene. [NCBI / EBI]

PharmGKB

PA27148; -.

Gene expression databases

Q9UER7; -.

Q9UER7; -.

HS_DAXX; -.

ENSG00000204209; Homo sapiens.

Ontologies

GO:0005737;	Cellular component: cytoplasm (traceable author statement from UniProtKB).
GO:0016605;	Cellular component: PML body (traceable author statement from UniProtKB).
GO:0050681;	Molecular function: androgen receptor binding (inferred from physical interaction from UniProtKB).
GO:0031072;	Molecular function: heat shock protein binding (traceable author statement from UniProtKB).
GO:0042802;	Molecular function: identical protein binding (inferred from physical interaction from IntAct).
GO:0047485;	Molecular function: protein N-terminus binding (inferred from physical interaction from UniProtKB).
GO:0005057;	Molecular function: receptor signaling protein activity (traceable author statement from ProtInc).
GO:0007257;	Biological process: activation of JUN kinase activity (traceable author statement from ProtInc).
GO:0030521;	Biological process: androgen receptor signaling pathway (inferred from direct assay from UniProtKB).
GO:0006915;	Biological process: apoptosis (traceable author statement from UniProtKB).
GO:0008625;	Biological process: induction of apoptosis via death domain receptors (traceable author statement from ProtInc).
GO:0044419;	Biological process: interspecies interaction between organisms (inferred from electronic annotation from UniProtKB-KW).
GO:0045892;	Biological process: negative regulation of transcription, DNA-dependent (inferred from direct assay from UniProtKB).
GO:0006350;	Biological process: transcription (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR005012; Daxx.
Graphical view of domain structure.

PANTHER

PTHR12766; Daxx; 1.

Pfam

PF03344; Daxx; 1.
Pfam graphical view of domain structure.

Proteomic databases

PeptideAtlas

Q9UER7; -.

PRIDE

Q9UER7; -.

Genome annotation databases

Ensembl

ENSG00000204209; Homo sapiens. [Contig view]
ENSG00000206206; Homo sapiens. [Contig view]
ENSG00000206279; Homo sapiens. [Contig view]

GeneID

1616; -.

KEGG

hsa:1616; -.

Phylogenomic databases

HOGENOM

Q9UER7; -.

HOVERGEN

Q9UER7; -.

OMA

Q9UER7; EPSGNNP.

Other

6638; -.

DAXX; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Alternative splicing; Apoptosis; Coiled coil; Cytoplasm; Host-virus interaction; Nucleus; Phosphoprotein; Transcription; Transcription regulation; Ubl conjugation.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 740`	`740`	`Death domain-associated protein 6.`	`PRO_0000151258`
`REGION`	`501 625`	`125`	`Interaction with MAP3K5.`
`REGION`	`626 740`	`115`	`Interaction with SPOP.`
`COILED`	`180 217`	`38`	`Potential.`
`COILED`	`358 399`	`42`	`Potential.`
`COILED`	`430 489`	`60`	`Potential.`
`MOTIF`	`391 395`	`5`	`Nuclear localization signal (Potential).`
`MOTIF`	`628 634`	`7`	`Nuclear localization signal (Potential).`
`COMPBIAS`	`11 16`	`6`	`Poly-Asp.`
`COMPBIAS`	`434 572`	`139`	`Asp/Glu-rich (acidic).`
`MOD_RES`	`178 178`		`Phosphoserine.`
`MOD_RES`	`213 213`		`Phosphoserine.`
`MOD_RES`	`459 459`		`Phosphothreonine (By similarity).`
`MOD_RES`	`495 495`		`Phosphoserine.`
`MOD_RES`	`648 648`		`Phosphotyrosine.`
`MOD_RES`	`668 668`		`Phosphoserine.`
`MOD_RES`	`671 671`		`Phosphoserine.`
`MOD_RES`	`688 688`		`Phosphoserine.`
`MOD_RES`	`690 690`		`Phosphoserine.`
`MOD_RES`	`702 702`		`Phosphoserine.`
`MOD_RES`	`709 709`		`Phosphothreonine.`
`MOD_RES`	`712 712`		`Phosphoserine.`
`MOD_RES`	`737 737`		`Phosphoserine.`
`MOD_RES`	`739 739`		`Phosphoserine.`
`VAR_SEQ`	`696 740`		`SSLCIPSPARLSQTPHSQPPRPGTCKTSVATQCDPEEIIV` `LSDSD -> PAKNLGRRRSKQDQG (in isoform 2).`	`VSP_001270`
`MUTAGEN`	`630 630`		`K->A: Abolishes sumoylation.`
`MUTAGEN`	`631 631`		`K->A: Abolishes sumoylation.`
`MUTAGEN`	`668 668`		`S->A: No translocation to the cytosol upon glucose deprivation.`
`MUTAGEN`	`671 671`		`S->A: No effect on cytosol translocation. upon glucose deprivation.`
`CONFLICT`	`177 177`		`Q -> R (in Ref. 2; AAB66585).`
`CONFLICT`	`263 263`		`R -> H (in Ref. 5; AAC72843).`
`CONFLICT`	`323 323`		`R -> W (in Ref. 2; AAB66585).`
`CONFLICT`	`365 365`		`R -> Q (in Ref. 2; AAB66585).`
`CONFLICT`	`382 382`		`L -> S (in Ref. 2; AAB66585).`
`CONFLICT`	`647 647`		`S -> R (in Ref. 4 and 7).`
`CONFLICT`	`722 722`		`T -> A (in Ref. 4 and 7).`
`CONFLICT`	`731 732`		`EE -> KK (in Ref. 5; AAC72843).`

Sequence information

Length: 740 AA [This is the length of the unprocessed precursor]

Molecular weight: 81373 Da [This is the MW of the unprocessed precursor]

CRC64: 1B309ADDAA878040 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MATANSIIVL DDDDEDEAAA QPGPSHPLPN AASPGAEAPS SSEPHGARGS SSSGGKKCYK 

        70         80         90        100        110        120 
LENEKLFEEF LELCKMQTAD HPEVVPFLYN RQQRAHSLFL ASAEFCNILS RVLSRARSRP 

       130        140        150        160        170        180 
AKLYVYINEL CTVLKAHSAK KKLNLAPAAT TSNEPSGNNP PTHLSLDPTN AENTASQSPR 

       190        200        210        220        230        240 
TRGSRRQIQR LEQLLALYVA EIRRLQEKEL DLSELDDPDS AYLQEARLKR KLIRLFGRLC 

       250        260        270        280        290        300 
ELKDCSSLTG RVIEQRIPYR GTRYPEVNRR IERLINKPGP DTFPDYGDVL RAVEKAAARH 

       310        320        330        340        350        360 
SLGLPRQQLQ LMAQDAFRDV GIRLQERRHL DLIYNFGCHL TDDYRPGVDP ALSDPVLARR 

       370        380        390        400        410        420 
LRENRSLAMS RLDEVISKYA MLQDKSEEGE RKKRRARLQG TSSHSADTPE ASLDSGEGPS 

       430        440        450        460        470        480 
GMASQGCPSA SRAETDDEDD EESDEEEEEE EEEEEEEATD SEEEEDLEQM QEGQEDDEEE 

       490        500        510        520        530        540 
DEEEEAAAGK DGDKSPMSSL QISNEKNLEP GKQISRSSGE QQNKGRIVSP SLLSEEPLAP 

       550        560        570        580        590        600 
SSIDAESNGE QPEELTLEEE SPVSQLFELE IEALPLDTPS SVETDISSSR KQSEEPFTTV 

       610        620        630        640        650        660 
LENGAGMVSS TSFNGGVSPH NWGDSGPPCK KSRKEKKQTG SGPLGNSYVE RQRSVHEKNG 

       670        680        690        700        710        720 
KKICTLPSPP SPLASLAPVA DSSTRVDSPS HGLVTSSLCI PSPARLSQTP HSQPPRPGTC 

       730        740 
KTSVATQCDP EEIIVLSDSD

Q9UER7 in FASTA format

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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools