dbPTM

DAXX_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DAXX_HUMAN
UniProt AC	Q9UER7
Protein Name	Death domain-associated protein 6
Gene Name	DAXX
Organism	Homo sapiens (Human).
Sequence Length	740
Subcellular Localization	Cytoplasm . Nucleus, nucleoplasm . Nucleus, PML body . Nucleus, nucleolus . Chromosome, centromere . Dispersed throughout the nucleoplasm, in PML/POD/ND10 nuclear bodies, and in nucleoli (Probable). Colocalizes with histone H3.3, ATRX, HIRA and ASF1A
Protein Description	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]
Protein Sequence	MATANSIIVLDDDDEDEAAAQPGPSHPLPNAASPGAEAPSSSEPHGARGSSSSGGKKCYKLENEKLFEEFLELCKMQTADHPEVVPFLYNRQQRAHSLFLASAEFCNILSRVLSRARSRPAKLYVYINELCTVLKAHSAKKKLNLAPAATTSNEPSGNNPPTHLSLDPTNAENTASQSPRTRGSRRQIQRLEQLLALYVAEIRRLQEKELDLSELDDPDSAYLQEARLKRKLIRLFGRLCELKDCSSLTGRVIEQRIPYRGTRYPEVNRRIERLINKPGPDTFPDYGDVLRAVEKAAARHSLGLPRQQLQLMAQDAFRDVGIRLQERRHLDLIYNFGCHLTDDYRPGVDPALSDPVLARRLRENRSLAMSRLDEVISKYAMLQDKSEEGERKKRRARLQGTSSHSADTPEASLDSGEGPSGMASQGCPSASRAETDDEDDEESDEEEEEEEEEEEEEATDSEEEEDLEQMQEGQEDDEEEDEEEEAAAGKDGDKSPMSSLQISNEKNLEPGKQISRSSGEQQNKGRIVSPSLLSEEPLAPSSIDAESNGEQPEELTLEEESPVSQLFELEIEALPLDTPSSVETDISSSRKQSEEPFTTVLENGAGMVSSTSFNGGVSPHNWGDSGPPCKKSRKEKKQTGSGPLGNSYVERQRSVHEKNGKKICTLPSPPSPLASLAPVADSSTRVDSPSHGLVTSSLCIPSPARLSQTPHSQPPRPGTCKTSVATQCDPEEIIVLSDSD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MATANSIIVL -----CCCCCEEEEE	25.69	27251275
6	Phosphorylation	--MATANSIIVLDDD --CCCCCEEEEECCC	15.95	27251275
25	Phosphorylation	AAAQPGPSHPLPNAA HHHCCCCCCCCCCCC	43.59	23401153
33	Phosphorylation	HPLPNAASPGAEAPS CCCCCCCCCCCCCCC	22.81	26055452
40	Phosphorylation	SPGAEAPSSSEPHGA CCCCCCCCCCCCCCC	54.25	26552605
41	Phosphorylation	PGAEAPSSSEPHGAR CCCCCCCCCCCCCCC	37.35	26552605
42	Phosphorylation	GAEAPSSSEPHGARG CCCCCCCCCCCCCCC	60.53	26552605
50	Phosphorylation	EPHGARGSSSSGGKK CCCCCCCCCCCCCCC	22.84	26074081
51	Phosphorylation	PHGARGSSSSGGKKC CCCCCCCCCCCCCCC	31.20	26074081
52	Phosphorylation	HGARGSSSSGGKKCY CCCCCCCCCCCCCCE	34.40	26074081
53	Phosphorylation	GARGSSSSGGKKCYK CCCCCCCCCCCCCEE	54.21	26074081
59	Phosphorylation	SSGGKKCYKLENEKL CCCCCCCEECCCHHH	27.73	26074081
60	Sumoylation	SGGKKCYKLENEKLF CCCCCCEECCCHHHH	59.81	-
60	Sumoylation	SGGKKCYKLENEKLF CCCCCCEECCCHHHH	59.81	-
60	Ubiquitination	SGGKKCYKLENEKLF CCCCCCEECCCHHHH	59.81	-
65	Ubiquitination	CYKLENEKLFEEFLE CEECCCHHHHHHHHH	70.79	-
75	Ubiquitination	EEFLELCKMQTADHP HHHHHHHHCCCCCCC	46.82	-
97	Phosphorylation	NRQQRAHSLFLASAE CHHHHHHHHHHHHHH	21.60	20068231
102	Phosphorylation	AHSLFLASAEFCNIL HHHHHHHHHHHHHHH	30.40	20068231
110	Phosphorylation	AEFCNILSRVLSRAR HHHHHHHHHHHHHHH	19.29	20068231
118	Phosphorylation	RVLSRARSRPAKLYV HHHHHHHCCCCEEEE	41.45	29083192
122	Ubiquitination	RARSRPAKLYVYINE HHHCCCCEEEEHHHH	42.93	19789334
124	Phosphorylation	RSRPAKLYVYINELC HCCCCEEEEHHHHHH	7.18	22817900
126	Phosphorylation	RPAKLYVYINELCTV CCCEEEEHHHHHHHH	5.62	22817900
132	Phosphorylation	VYINELCTVLKAHSA EHHHHHHHHHHHCCH	41.31	29083192
141	Ubiquitination	LKAHSAKKKLNLAPA HHHCCHHHHCCCCCC	63.31	-
142	Sumoylation	KAHSAKKKLNLAPAA HHCCHHHHCCCCCCC	41.73	28112733
142	Ubiquitination	KAHSAKKKLNLAPAA HHCCHHHHCCCCCCC	41.73	-
150	Phosphorylation	LNLAPAATTSNEPSG CCCCCCCCCCCCCCC	32.63	22167270
151	Phosphorylation	NLAPAATTSNEPSGN CCCCCCCCCCCCCCC	25.48	22167270
152	Phosphorylation	LAPAATTSNEPSGNN CCCCCCCCCCCCCCC	34.54	22167270
156	Phosphorylation	ATTSNEPSGNNPPTH CCCCCCCCCCCCCCC	48.23	22167270
162	Phosphorylation	PSGNNPPTHLSLDPT CCCCCCCCCCCCCCC	36.38	29255136
165	Phosphorylation	NNPPTHLSLDPTNAE CCCCCCCCCCCCCCC	24.11	29255136
169	Phosphorylation	THLSLDPTNAENTAS CCCCCCCCCCCCCCC	46.88	22167270
174	Phosphorylation	DPTNAENTASQSPRT CCCCCCCCCCCCCCC	21.13	22167270
176	Phosphorylation	TNAENTASQSPRTRG CCCCCCCCCCCCCCC	29.20	23401153
178	Phosphorylation	AENTASQSPRTRGSR CCCCCCCCCCCCCCH	17.54	29255136
181	Phosphorylation	TASQSPRTRGSRRQI CCCCCCCCCCCHHHH	42.65	28111955
184	Phosphorylation	QSPRTRGSRRQIQRL CCCCCCCCHHHHHHH	22.46	19789334
208	Ubiquitination	EIRRLQEKELDLSEL HHHHHHHHCCCHHHC	51.09	21906983
208 (in isoform 1)	Ubiquitination	-	51.09	21890473
208 (in isoform 2)	Ubiquitination	-	51.09	21890473
213	Phosphorylation	QEKELDLSELDDPDS HHHCCCHHHCCCCCH	35.46	25159151
229	Ubiquitination	YLQEARLKRKLIRLF HHHHHHHHHHHHHHH	41.77	-
243	Acetylation	FGRLCELKDCSSLTG HHHHHHCCCHHHCCC	34.10	25953088
243	Ubiquitination	FGRLCELKDCSSLTG HHHHHHCCCHHHCCC	34.10	-
246	Phosphorylation	LCELKDCSSLTGRVI HHHCCCHHHCCCCHH	38.22	21474068
249	Phosphorylation	LKDCSSLTGRVIEQR CCCHHHCCCCHHHHC	25.53	21474068
259	Phosphorylation	VIEQRIPYRGTRYPE HHHHCCCCCCCCCHH	21.21	-
264	Phosphorylation	IPYRGTRYPEVNRRI CCCCCCCCHHHHHHH	12.00	-
277	Sumoylation	RIERLINKPGPDTFP HHHHHHCCCCCCCCC	44.34	-
277	Sumoylation	RIERLINKPGPDTFP HHHHHHCCCCCCCCC	44.34	-
277	Ubiquitination	RIERLINKPGPDTFP HHHHHHCCCCCCCCC	44.34	21906983
277 (in isoform 1)	Ubiquitination	-	44.34	21890473
277 (in isoform 2)	Ubiquitination	-	44.34	21890473
295	Sumoylation	DVLRAVEKAAARHSL HHHHHHHHHHHHHHC	36.41	-
295	Sumoylation	DVLRAVEKAAARHSL HHHHHHHHHHHHHHC	36.41	-
295	Ubiquitination	DVLRAVEKAAARHSL HHHHHHHHHHHHHHC	36.41	-
334	Phosphorylation	RRHLDLIYNFGCHLT HHCHHHHEEECCCCC	16.25	-
344	Phosphorylation	GCHLTDDYRPGVDPA CCCCCCCCCCCCCHH	22.86	22817900
378	Ubiquitination	RLDEVISKYAMLQDK HHHHHHHHHHHHHCC	26.38	21890473
378	Ubiquitination	RLDEVISKYAMLQDK HHHHHHHHHHHHHCC	26.38	21906983
378	Ubiquitination	RLDEVISKYAMLQDK HHHHHHHHHHHHHCC	26.38	21890473
378	Ubiquitination	RLDEVISKYAMLQDK HHHHHHHHHHHHHCC	26.38	21890473
378 (in isoform 1)	Ubiquitination	-	26.38	21890473
378 (in isoform 2)	Ubiquitination	-	26.38	21890473
379	Phosphorylation	LDEVISKYAMLQDKS HHHHHHHHHHHHCCC	7.17	19664994
385	Ubiquitination	KYAMLQDKSEEGERK HHHHHHCCCHHHHHH	46.97	21906983
385 (in isoform 1)	Ubiquitination	-	46.97	21890473
385 (in isoform 2)	Ubiquitination	-	46.97	21890473
386	Phosphorylation	YAMLQDKSEEGERKK HHHHHCCCHHHHHHH	49.52	24719451
401	Phosphorylation	RRARLQGTSSHSADT HHHHHCCCCCCCCCC	17.69	23401153
402	Phosphorylation	RARLQGTSSHSADTP HHHHCCCCCCCCCCC	32.64	23663014
403	Phosphorylation	ARLQGTSSHSADTPE HHHCCCCCCCCCCCC	22.69	23663014
405	Phosphorylation	LQGTSSHSADTPEAS HCCCCCCCCCCCCCC	29.77	23663014
408	Phosphorylation	TSSHSADTPEASLDS CCCCCCCCCCCCCCC	23.81	21712546
412	Phosphorylation	SADTPEASLDSGEGP CCCCCCCCCCCCCCC	30.92	21712546
415	Phosphorylation	TPEASLDSGEGPSGM CCCCCCCCCCCCCCH	44.00	30175587
420	Phosphorylation	LDSGEGPSGMASQGC CCCCCCCCCHHHCCC	52.65	23663014
424	Phosphorylation	EGPSGMASQGCPSAS CCCCCHHHCCCCCCH	20.43	30175587
429	Phosphorylation	MASQGCPSASRAETD HHHCCCCCCHHCCCC	42.84	25850435
431	Phosphorylation	SQGCPSASRAETDDE HCCCCCCHHCCCCCC	36.04	25850435
437	Acetylation	ASRAETDDEDDEESD CHHCCCCCCCCCCCH	69.51	19608861
437	Ubiquitination	ASRAETDDEDDEESD CHHCCCCCCCCCCCH	69.51	19608861
459	Phosphorylation	EEEEEEATDSEEEED HHHHHHCCCCHHHHH	43.25	-
495	Phosphorylation	AGKDGDKSPMSSLQI CCCCCCCCCCHHCCC	30.49	29255136
498	Phosphorylation	DGDKSPMSSLQISNE CCCCCCCHHCCCCCC	31.14	30266825
499	Phosphorylation	GDKSPMSSLQISNEK CCCCCCHHCCCCCCC	20.31	30266825
503	Phosphorylation	PMSSLQISNEKNLEP CCHHCCCCCCCCCCC	26.44	25159151
506	Ubiquitination	SLQISNEKNLEPGKQ HCCCCCCCCCCCCCC	71.70	-
512	Sumoylation	EKNLEPGKQISRSSG CCCCCCCCCCCCCCC	55.99	-
512	Acetylation	EKNLEPGKQISRSSG CCCCCCCCCCCCCCC	55.99	19608861
512	Sumoylation	EKNLEPGKQISRSSG CCCCCCCCCCCCCCC	55.99	-
512	Ubiquitination	EKNLEPGKQISRSSG CCCCCCCCCCCCCCC	55.99	2190698
512 (in isoform 1)	Ubiquitination	-	55.99	21890473
512 (in isoform 2)	Ubiquitination	-	55.99	21890473
515	Phosphorylation	LEPGKQISRSSGEQQ CCCCCCCCCCCCCCC	24.50	20068231
561	Phosphorylation	ELTLEEESPVSQLFE CCCCCCCCCHHHHEE	33.60	26074081
564	Phosphorylation	LEEESPVSQLFELEI CCCCCCHHHHEEEEE	25.26	26074081
578	Phosphorylation	IEALPLDTPSSVETD EEECCCCCCCCCCCC	32.52	26074081
580	Phosphorylation	ALPLDTPSSVETDIS ECCCCCCCCCCCCCC	49.46	26074081
581	Phosphorylation	LPLDTPSSVETDISS CCCCCCCCCCCCCCC	25.77	26074081
584	Phosphorylation	DTPSSVETDISSSRK CCCCCCCCCCCCCCC	36.16	26074081
587	Phosphorylation	SSVETDISSSRKQSE CCCCCCCCCCCCCCC	25.68	26074081
588	Phosphorylation	SVETDISSSRKQSEE CCCCCCCCCCCCCCC	34.20	26074081
589	Phosphorylation	VETDISSSRKQSEEP CCCCCCCCCCCCCCC	36.38	26074081
593	Phosphorylation	ISSSRKQSEEPFTTV CCCCCCCCCCCCEEE	47.14	26074081
598	Phosphorylation	KQSEEPFTTVLENGA CCCCCCCEEEECCCC	27.06	26074081
599	Phosphorylation	QSEEPFTTVLENGAG CCCCCCEEEECCCCC	24.39	26074081
609	Phosphorylation	ENGAGMVSSTSFNGG CCCCCCEEECCCCCC	21.00	26074081
610	Phosphorylation	NGAGMVSSTSFNGGV CCCCCEEECCCCCCC	19.36	26074081
611	Phosphorylation	GAGMVSSTSFNGGVS CCCCEEECCCCCCCC	29.81	26074081
612	Phosphorylation	AGMVSSTSFNGGVSP CCCEEECCCCCCCCC	20.75	26074081
618	Phosphorylation	TSFNGGVSPHNWGDS CCCCCCCCCCCCCCC	24.58	22199227
625	Phosphorylation	SPHNWGDSGPPCKKS CCCCCCCCCCCCCCC	49.62	26074081
630	Sumoylation	GDSGPPCKKSRKEKK CCCCCCCCCCHHHHC	60.60	-
630	Sumoylation	GDSGPPCKKSRKEKK CCCCCCCCCCHHHHC	60.60	12150977
631	Sumoylation	DSGPPCKKSRKEKKQ CCCCCCCCCHHHHCC	63.31	-
631	Sumoylation	DSGPPCKKSRKEKKQ CCCCCCCCCHHHHCC	63.31	12150977
632	Phosphorylation	SGPPCKKSRKEKKQT CCCCCCCCHHHHCCC	33.80	26074081
637	Sumoylation	KKSRKEKKQTGSGPL CCCHHHHCCCCCCCC	54.93	-
637	Sumoylation	KKSRKEKKQTGSGPL CCCHHHHCCCCCCCC	54.93	-
637	Ubiquitination	KKSRKEKKQTGSGPL CCCHHHHCCCCCCCC	54.93	-
639	Phosphorylation	SRKEKKQTGSGPLGN CHHHHCCCCCCCCCH	42.04	25159151
641	Phosphorylation	KEKKQTGSGPLGNSY HHHCCCCCCCCCHHH	40.39	25159151
647	Phosphorylation	GSGPLGNSYVERQRS CCCCCCHHHHHHHHH	28.85	25159151
648	Phosphorylation	SGPLGNSYVERQRSV CCCCCHHHHHHHHHH	15.44	28985074
654	Phosphorylation	SYVERQRSVHEKNGK HHHHHHHHHHHHCCC	21.35	28985074
662 (in isoform 4)	Phosphorylation	-	44.40	26471730
664 (in isoform 4)	Phosphorylation	-	4.37	26471730
665	Phosphorylation	KNGKKICTLPSPPSP HCCCEEECCCCCCCC	45.22	29255136
665 (in isoform 4)	Phosphorylation	-	45.22	26471730
668	Phosphorylation	KKICTLPSPPSPLAS CEEECCCCCCCCHHH	53.18	29255136
668 (in isoform 4)	Phosphorylation	-	53.18	26471730
671	Phosphorylation	CTLPSPPSPLASLAP ECCCCCCCCHHHHCC	35.61	29255136
675	Phosphorylation	SPPSPLASLAPVADS CCCCCHHHHCCCCCC	32.52	30278072
682	Phosphorylation	SLAPVADSSTRVDSP HHCCCCCCCCCCCCC	24.70	23927012
683	Phosphorylation	LAPVADSSTRVDSPS HCCCCCCCCCCCCCC	22.30	23927012
684	Phosphorylation	APVADSSTRVDSPSH CCCCCCCCCCCCCCC	38.37	23927012
688	Phosphorylation	DSSTRVDSPSHGLVT CCCCCCCCCCCCEEC	25.99	29255136
690	Phosphorylation	STRVDSPSHGLVTSS CCCCCCCCCCEECCC	33.85	29255136
695	Phosphorylation	SPSHGLVTSSLCIPS CCCCCEECCCCEECC	20.03	30266825
696	Phosphorylation	PSHGLVTSSLCIPSP CCCCEECCCCEECCC	17.52	30266825
697	O-linked_Glycosylation	SHGLVTSSLCIPSPA CCCEECCCCEECCCC	20.21	30379171
697	Phosphorylation	SHGLVTSSLCIPSPA CCCEECCCCEECCCC	20.21	30266825
702	Phosphorylation	TSSLCIPSPARLSQT CCCCEECCCCHHCCC	15.98	29255136
707	Phosphorylation	IPSPARLSQTPHSQP ECCCCHHCCCCCCCC	26.84	23927012
709	Phosphorylation	SPARLSQTPHSQPPR CCCHHCCCCCCCCCC	21.42	17525332
712	Phosphorylation	RLSQTPHSQPPRPGT HHCCCCCCCCCCCCC	45.65	17525332
719	Phosphorylation	SQPPRPGTCKTSVAT CCCCCCCCCCCEECC	17.32	23403867
722	Phosphorylation	PRPGTCKTSVATQCD CCCCCCCCEECCCCC	30.49	27251275
723	Phosphorylation	RPGTCKTSVATQCDP CCCCCCCEECCCCCH	8.68	27251275
726	Phosphorylation	TCKTSVATQCDPEEI CCCCEECCCCCHHHE	27.81	20873877
737	Phosphorylation	PEEIIVLSDSD---- HHHEEEEECCC----	24.95	26503892
739	Phosphorylation	EIIVLSDSD------ HEEEEECCC------	41.67	25159151

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
176	S	Phosphorylation	Kinase	MAP3K5	Q99683	GPS
184	S	Phosphorylation	Kinase	MAP3K5	Q99683	GPS
424	S	Phosphorylation	Kinase	ATR	Q13535	PSP
564	S	Phosphorylation	Kinase	ATM	Q13315	PSP
668	S	Phosphorylation	Kinase	HIPK3	Q9H422	PSP
668	S	Phosphorylation	Kinase	RIPK3	Q9Y572	PSP
737	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
739	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	SPOP	O43791	PMID:16524876
-	K	Ubiquitination	E3 ubiquitin ligase	MDM2	Q00987	PMID:20153724

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of DAXX_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of DAXX_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MCRS1_HUMAN	MCRS1	physical	11948183
ANDR_HUMAN	AR	physical	15572661
DAPK3_HUMAN	DAPK3	physical	12917339
GCR_HUMAN	NR3C1	physical	12595526
SUMO1_HUMAN	SUMO1	physical	11948183
HDAC1_HUMAN	HDAC1	physical	10669754
PML_HUMAN	PML	physical	10669754
GTR4_HUMAN	SLC2A4	physical	11842083
M3K5_HUMAN	MAP3K5	physical	9743501
CDN2A_HUMAN	CDKN2A	physical	18583933
ARF_HUMAN	CDKN2A	physical	18583933
MDM2_HUMAN	MDM2	physical	18583933
RASF1_HUMAN	RASSF1	physical	18566590
PLAL1_HUMAN	PLAGL1	physical	20097304
RASF1_HUMAN	RASSF1	physical	16810318
AXIN1_HUMAN	AXIN1	physical	17210684
MYH11_HUMAN	MYH11	physical	20936779
UBC_HUMAN	UBC	physical	20936779
ITF2_HUMAN	TCF4	physical	20211142
RELB_HUMAN	RELB	physical	16982744
ETS1_HUMAN	ETS1	physical	16861237
CBP_HUMAN	CREBBP	physical	16287980
ATRX_HUMAN	ATRX	physical	12953102
HDAC2_HUMAN	HDAC2	physical	12140263
SMAD4_HUMAN	SMAD4	physical	15637079
ATRX_HUMAN	ATRX	physical	15252119
ATRX_HUMAN	ATRX	physical	14990586
CHIP_HUMAN	STUB1	physical	19465479
HIPK2_HUMAN	HIPK2	physical	19465479
UBP7_HUMAN	USP7	physical	16845383
MDM2_HUMAN	MDM2	physical	16845383
P53_HUMAN	TP53	physical	16845383
M3K5_HUMAN	MAP3K5	physical	19789334
RL13_HUMAN	RPL13	physical	21900206
CAH12_HUMAN	CA12	physical	21900206
DMAP1_HUMAN	DMAP1	physical	14978102
DNMT1_HUMAN	DNMT1	physical	14978102
PML_HUMAN	PML	physical	21779164
UBP7_HUMAN	USP7	physical	18566590
SUMO1_HUMAN	SUMO1	physical	21383010
SUMO2_HUMAN	SUMO2	physical	21383010
ATRX_HUMAN	ATRX	physical	20147399
TS101_HUMAN	TSG101	physical	15033475
DMAP1_HUMAN	DMAP1	physical	15033475
PML_HUMAN	PML	physical	12150977
SUMO1_HUMAN	SUMO1	physical	21474068
PML_HUMAN	PML	physical	21474068
PIN1_HUMAN	PIN1	physical	17938171
RASF1_HUMAN	RASSF1	physical	21643015
SUMO1_HUMAN	SUMO1	physical	16475184
SUMO2_HUMAN	SUMO2	physical	16475184
SNW1_HUMAN	SNW1	physical	15878163
CYTSB_HUMAN	SPECC1	physical	22170762
CEBPB_HUMAN	CEBPB	physical	19690170
M3K5_HUMAN	MAP3K5	physical	11495919
P53_HUMAN	TP53	physical	12954772
P73_HUMAN	TP73	physical	12954772
P63_HUMAN	TP63	physical	12954772
P53_HUMAN	TP53	physical	12482984
PP71_HCMVM	UL82	physical	15919932
SPOP_HUMAN	SPOP	physical	15240113
FRIH_HUMAN	FTH1	physical	21573799
SPOP_HUMAN	SPOP	physical	21573799
BTBD6_HUMAN	BTBD6	physical	21573799
RASF1_HUMAN	RASSF1	physical	21134643
SL9A1_HUMAN	SLC9A1	physical	18003619
M3K5_HUMAN	MAP3K5	physical	15983381
P53_HUMAN	TP53	physical	15364927
TF7L2_HUMAN	TCF7L2	physical	16569639
DAXX_HUMAN	DAXX	physical	12968034
DBF4A_HUMAN	DBF4	physical	12968034
TNR6_HUMAN	FAS	physical	14637155
CFLAR_HUMAN	CFLAR	physical	14637155
PP71_HCMVM	UL82	physical	12097584
M3K5_HUMAN	MAP3K5	physical	15258908
HSF1_HUMAN	HSF1	physical	15016915
P73_HUMAN	TP73	physical	15339933
P53_HUMAN	TP53	physical	15339933
M3K5_HUMAN	MAP3K5	physical	11003656
HSPB1_HUMAN	HSPB1	physical	11003656
HSPB2_HUMAN	HSPB2	physical	11003656
CDC20_HUMAN	CDC20	physical	23239745
BUB1B_HUMAN	BUB1B	physical	23239745
MD2L1_HUMAN	MAD2L1	physical	23239745
FZR1_HUMAN	FZR1	physical	23239745
ATRX_HUMAN	ATRX	physical	23135716
PP71_HCMVM	UL82	physical	23135716
UBP7_HUMAN	USP7	physical	23348568
MDM2_HUMAN	MDM2	physical	23405218
DAXX_HUMAN	DAXX	physical	21572393
H33_HUMAN	H3F3A	physical	23142979
H33_HUMAN	H3F3A	physical	23075851
CREB1_HUMAN	CREB1	physical	22185778
PDCD4_HUMAN	PDCD4	physical	23536002
HIPK2_HUMAN	HIPK2	physical	23536002
RELB_HUMAN	RELB	physical	23548901
DNMT1_HUMAN	DNMT1	physical	23548901
DNM3A_HUMAN	DNMT3A	physical	23548901
MDM2_HUMAN	MDM2	physical	15364927
NSD3_HUMAN	WHSC1L1	physical	23455924
SPOP_HUMAN	SPOP	physical	16524876
CUL3_HUMAN	CUL3	physical	16524876
SPOP_HUMAN	SPOP	physical	21988832
FRIH_HUMAN	FTH1	physical	21988832
HBA_HUMAN	HBA1	physical	21988832
TRAF3_HUMAN	TRAF3	physical	21988832
CARM1_HUMAN	CARM1	physical	23455924
ANM1_HUMAN	PRMT1	physical	23455924
ATRX_HUMAN	ATRX	physical	23222847
H33_HUMAN	H3F3A	physical	23222847
P53_HUMAN	TP53	physical	23038753
DNMT1_HUMAN	DNMT1	physical	23038753
MDM2_HUMAN	MDM2	physical	23038753
H33_HUMAN	H3F3A	physical	24530302
UBC9_HUMAN	UBE2I	physical	23395904
GOGA2_HUMAN	GOLGA2	physical	25416956
NECA2_HUMAN	NECAB2	physical	25416956
CDA7L_HUMAN	CDCA7L	physical	25416956
PBIP1_HUMAN	PBXIP1	physical	25416956
CARD9_HUMAN	CARD9	physical	25416956
ADIP_HUMAN	SSX2IP	physical	25416956
FAM9B_HUMAN	FAM9B	physical	25416956
SUMO3_HUMAN	SUMO3	physical	21474068
SUMO1_HUMAN	SUMO1	physical	22578841
SUMO1_HUMAN	SUMO1	physical	17081986
SUMO2_HUMAN	SUMO2	physical	22578841
GCR_HUMAN	NR3C1	physical	17081986
SUMO2_HUMAN	SUMO2	physical	17081986
UBC9_HUMAN	UBE2I	physical	17081986
PML_HUMAN	PML	physical	17081986
RIPK3_HUMAN	RIPK3	physical	23260419
TF7L2_HUMAN	TCF7L2	physical	19563778
DAXX_HUMAN	DAXX	physical	11483955
PARP1_HUMAN	PARP1	physical	26496610
ATRX_HUMAN	ATRX	physical	26496610
H2B1B_HUMAN	HIST1H2BB	physical	26496610
KI67_HUMAN	MKI67	physical	26496610
RFC1_HUMAN	RFC1	physical	26496610
RFC2_HUMAN	RFC2	physical	26496610
RFC3_HUMAN	RFC3	physical	26496610
SUV91_HUMAN	SUV39H1	physical	26496610
TOP2A_HUMAN	TOP2A	physical	26496610
TOP2B_HUMAN	TOP2B	physical	26496610
UBF1_HUMAN	UBTF	physical	26496610
SMCA5_HUMAN	SMARCA5	physical	26496610
BAZ1B_HUMAN	BAZ1B	physical	26496610
RL23_HUMAN	RPL23	physical	26496610
PHF14_HUMAN	PHF14	physical	26496610
RAI1_HUMAN	RAI1	physical	26496610
KAT7_HUMAN	KAT7	physical	26496610
SP16H_HUMAN	SUPT16H	physical	26496610
WDFY3_HUMAN	WDFY3	physical	26496610
XPO7_HUMAN	XPO7	physical	26496610
ADNP_HUMAN	ADNP	physical	26496610
CBX5_HUMAN	CBX5	physical	26496610
MACF1_HUMAN	MACF1	physical	26496610
SENP3_HUMAN	SENP3	physical	26496610
CHMP3_HUMAN	CHMP3	physical	26496610
CHM4B_HUMAN	CHMP4B	physical	26496610
ATRX_HUMAN	ATRX	physical	25416818
H31T_HUMAN	HIST3H3	physical	25416818
H12_HUMAN	HIST1H1C	physical	25416818
H2B2E_HUMAN	HIST2H2BE	physical	25416818
H2B1L_HUMAN	HIST1H2BL	physical	25416818
GAR1_HUMAN	GAR1	physical	25416818
NHP2_HUMAN	NHP2	physical	25416818
NAF1_HUMAN	NAF1	physical	25416818
NOLC1_HUMAN	NOLC1	physical	25416818
COIL_HUMAN	COIL	physical	25416818
DKC1_HUMAN	DKC1	physical	25416818
TERT_HUMAN	TERT	physical	25416818
SUV91_HUMAN	SUV39H1	physical	26340527
M3K5_HUMAN	MAP3K5	physical	27488634
NOL3_HUMAN	NOL3	physical	27488634
ANDR_HUMAN	AR	physical	27671201
SUMO1_HUMAN	SUMO1	physical	28851805
SUMO2_HUMAN	SUMO2	physical	28851805

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of DAXX_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-512, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-702; SER-737 ANDSER-739, AND MASS SPECTROMETRY.	19690332 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495; SER-671; SER-688AND SER-702, AND MASS SPECTROMETRY.	19413330 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178; SER-213; SER-495;SER-668; SER-671; SER-688; SER-702; SER-737 AND SER-739, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178; SER-671; SER-688;SER-690 AND SER-702, AND MASS SPECTROMETRY.	18220336 [Abstract]
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; 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.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-709 AND SER-712, ANDMASS SPECTROMETRY.	17525332 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-737 AND SER-739, ANDMASS SPECTROMETRY.	17081983 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-671, AND MASSSPECTROMETRY.	15302935 [Abstract]
"Role of the ASK1-SEK1-JNK1-HIPK1 signal in Daxx trafficking and ASK1oligomerization."; Song J.J., Lee Y.J.; J. Biol. Chem. 278:47245-47252(2003). Cited for: OLIGOMERIZATION, SUBCELLULAR LOCATION, INTERACTION WITH MAP3K5,MUTAGENESIS OF SER-668 AND SER-671, AND PHOSPHORYLATION AT SER-668.	12968034 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-648, AND MASSSPECTROMETRY.	17287340 [Abstract]