dbPTM

DDX3X_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DDX3X_HUMAN
UniProt AC	O00571
Protein Name	ATP-dependent RNA helicase DDX3X
Gene Name	DDX3X
Organism	Homo sapiens (Human).
Sequence Length	662
Subcellular Localization	Nucleus speckle. Cytoplasm. Mitochondrion outer membrane. Located predominantly in nuclear speckles and, at low levels, throughout the cytoplasm. Located to the outer side of nuclear pore complexes (NPC). Shuttles between the nucleus and the cytoplas
Protein Description	Multifunctional ATP-dependent RNA helicase. The ATPase activity can be stimulated by various ribo- and deoxynucleic acids indicative for a relaxed substrate specificity. In vitro can unwind partially double-stranded DNA with a preference for 5'-single-stranded DNA overhangs. Is involved in several steps of gene expression, such as transcription, mRNA maturation, mRNA export and translation. However, the exact mechanisms are not known and some functions may be specific for a subset of mRNAs. Involved in transcriptional regulation. Can enhance transcription from the CDKN1A/WAF1 promoter in a SP1-dependent manner. Found associated with the E-cadherin promoter and can down-regulate transcription from the promoter. Involved in regulation of translation initiation. Proposed to be involved in positive regulation of translation such as of cyclin E1/CCNE1 mRNA and specifically of mRNAs containing complex secondary structures in their 5'UTRs; these functions seem to require RNA helicase activity. Specifically promotes translation of a subset of viral and cellular mRNAs carrying a 5'proximal stem-loop structure in their 5'UTRs and cooperates with the eIF4F complex. Proposed to act prior to 43S ribosomal scanning and to locally destabilize these RNA structures to allow recognition of the mRNA cap or loading onto the 40S subunit. After association with 40S ribosomal subunits seems to be involved in the functional assembly of 80S ribosomes; the function seems to cover translation of mRNAs with structured and non-structured 5'UTRs and is independent of RNA helicase activity. Also proposed to inhibit cap-dependent translation by competetive interaction with EIF4E which can block the EIF4E:EIF4G complex formation. Proposed to be involved in stress response and stress granule assembly; the function is independent of RNA helicase activity and seems to involve association with EIF4E. May be involved in nuclear export of specific mRNAs but not in bulk mRNA export via interactions with XPO1 and NXF1. Also associates with polyadenylated mRNAs independently of NXF1. Associates with spliced mRNAs in an exon junction complex (EJC)-dependent manner and seems not to be directly involved in splicing. May be involved in nuclear mRNA export by association with DDX5 and regulating its nuclear location. Involved in innate immune signaling promoting the production of type I interferon (IFN-alpha and IFN-beta); proposed to act as viral RNA sensor, signaling intermediate and transcriptional coactivator. Involved in TBK1 and IKBKE-dependent IRF3 activation leading to IFNB induction, plays a role of scaffolding adapter that links IKBKE and IRF3 and coordinates their activation. Also found associated with IFNB promoters; the function is independent of IRF3. Can bind to viral RNAs and via association with MAVS/IPS1 and DDX58/RIG-I is thought to induce signaling in early stages of infection. Involved in regulation of apoptosis. May be required for activation of the intrinsic but inhibit activation of the extrinsic apoptotic pathway. Acts as an antiapoptotic protein through association with GSK3A/B and BIRC2 in an apoptosis antagonizing signaling complex; activation of death receptors promotes caspase-dependent cleavage of BIRC2 and DDX3X and relieves the inhibition. May be involved in mitotic chromosome segregation. Is an allosteric activator of CSNK1E, it stimulates CSNK1E-mediated phosphorylation of DVL2 and is involved in the positive regulation of canonical Wnt signaling. [PubMed: 23413191; (Microbial infection) Appears to be a prime target for viral manipulations. Hepatitis B virus (HBV) polymerase and possibly vaccinia virus (VACV) protein K7 inhibit IFNB induction probably by dissociating DDX3X from TBK1 or IKBKE. Is involved in hepatitis C virus (HCV) replication; the function may involve the association with HCV core protein. HCV core protein inhibits the IPS1-dependent function in viral RNA sensing and may switch the function from a INFB inducing to a HCV replication mode. Involved in HIV-1 replication. Acts as a cofactor for XPO1-mediated nuclear export of incompletely spliced HIV-1 Rev RNAs.]
Protein Sequence	MSHVAVENALGLDQQFAGLDLNSSDNQSGGSTASKGRYIPPHLRNREATKGFYDKDSSGWSSSKDKDAYSSFGSRSDSRGKSSFFSDRGSGSRGRFDDRGRSDYDGIGSRGDRSGFGKFERGGNSRWCDKSDEDDWSKPLPPSERLEQELFSGGNTGINFEKYDDIPVEATGNNCPPHIESFSDVEMGEIIMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYSDGPGEALRAMKENGRYGRRKQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPKGVRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGSTSENITQKVVWVEESDKRSFLLDLLNATGKDSLTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNERNINITKDLLDLLVEAKQEVPSWLENMAYEHHYKGSSRGRSKSSRFSGGFGARDYRQSSGASSSSFSSSRASSSRSGGGGHGSSRGFGGGGYGGFYNSDGYGGNYNSQGVDWWGN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSHVAVENA ------CCCHHHHCC	27.03	10859333
2	Phosphorylation	------MSHVAVENA ------CCCHHHHCC	27.03	27251275
23	Phosphorylation	FAGLDLNSSDNQSGG HCCCCCCCCCCCCCC	46.49	22199227
24	Phosphorylation	AGLDLNSSDNQSGGS CCCCCCCCCCCCCCC	39.24	22199227
28	Phosphorylation	LNSSDNQSGGSTASK CCCCCCCCCCCCCCC	51.91	22199227
31	Phosphorylation	SDNQSGGSTASKGRY CCCCCCCCCCCCCCC	25.07	20873877
32	Phosphorylation	DNQSGGSTASKGRYI CCCCCCCCCCCCCCC	37.92	20873877
34	Phosphorylation	QSGGSTASKGRYIPP CCCCCCCCCCCCCCH	35.41	20873877
38	Phosphorylation	STASKGRYIPPHLRN CCCCCCCCCCHHHCC	26.84	25367160
50	2-Hydroxyisobutyrylation	LRNREATKGFYDKDS HCCCHHHCCCCCCCC	54.81	-
50	Acetylation	LRNREATKGFYDKDS HCCCHHHCCCCCCCC	54.81	26051181
50	Ubiquitination	LRNREATKGFYDKDS HCCCHHHCCCCCCCC	54.81	-
53	Phosphorylation	REATKGFYDKDSSGW CHHHCCCCCCCCCCC	30.65	20090780
55	Ubiquitination	ATKGFYDKDSSGWSS HHCCCCCCCCCCCCC	48.40	21890473
55	Ubiquitination	ATKGFYDKDSSGWSS HHCCCCCCCCCCCCC	48.40	21890473
55	Acetylation	ATKGFYDKDSSGWSS HHCCCCCCCCCCCCC	48.40	23236377
55	Malonylation	ATKGFYDKDSSGWSS HHCCCCCCCCCCCCC	48.40	26320211
55	Ubiquitination	ATKGFYDKDSSGWSS HHCCCCCCCCCCCCC	48.40	21890473
57	Phosphorylation	KGFYDKDSSGWSSSK CCCCCCCCCCCCCCC	36.17	20873877
58	Phosphorylation	GFYDKDSSGWSSSKD CCCCCCCCCCCCCCC	55.18	20068231
61	Phosphorylation	DKDSSGWSSSKDKDA CCCCCCCCCCCCHHH	28.41	25159151
62	Phosphorylation	KDSSGWSSSKDKDAY CCCCCCCCCCCHHHH	34.59	30576142
63	Phosphorylation	DSSGWSSSKDKDAYS CCCCCCCCCCHHHHH	39.08	20068231
64	Ubiquitination	SSGWSSSKDKDAYSS CCCCCCCCCHHHHHH	71.40	-
66	2-Hydroxyisobutyrylation	GWSSSKDKDAYSSFG CCCCCCCHHHHHHCC	48.25	-
66	Acetylation	GWSSSKDKDAYSSFG CCCCCCCHHHHHHCC	48.25	25953088
66	Malonylation	GWSSSKDKDAYSSFG CCCCCCCHHHHHHCC	48.25	26320211
66	Methylation	GWSSSKDKDAYSSFG CCCCCCCHHHHHHCC	48.25	-
66	Ubiquitination	GWSSSKDKDAYSSFG CCCCCCCHHHHHHCC	48.25	-
69	Phosphorylation	SSKDKDAYSSFGSRS CCCCHHHHHHCCCCC	18.25	27273156
70	Phosphorylation	SKDKDAYSSFGSRSD CCCHHHHHHCCCCCC	22.40	27273156
71	Phosphorylation	KDKDAYSSFGSRSDS CCHHHHHHCCCCCCC	22.43	23401153
74	Phosphorylation	DAYSSFGSRSDSRGK HHHHHCCCCCCCCCC	26.97	23401153
75	Methylation	AYSSFGSRSDSRGKS HHHHCCCCCCCCCCC	44.88	-
76	Phosphorylation	YSSFGSRSDSRGKSS HHHCCCCCCCCCCCC	41.45	25159151
78	Phosphorylation	SFGSRSDSRGKSSFF HCCCCCCCCCCCCCC	44.15	17287340
79	Methylation	FGSRSDSRGKSSFFS CCCCCCCCCCCCCCC	62.64	-
81	2-Hydroxyisobutyrylation	SRSDSRGKSSFFSDR CCCCCCCCCCCCCCC	41.64	-
81	Acetylation	SRSDSRGKSSFFSDR CCCCCCCCCCCCCCC	41.64	26051181
81	Malonylation	SRSDSRGKSSFFSDR CCCCCCCCCCCCCCC	41.64	26320211
81	Methylation	SRSDSRGKSSFFSDR CCCCCCCCCCCCCCC	41.64	-
81	Ubiquitination	SRSDSRGKSSFFSDR CCCCCCCCCCCCCCC	41.64	-
82	Phosphorylation	RSDSRGKSSFFSDRG CCCCCCCCCCCCCCC	34.89	25463755
83	Phosphorylation	SDSRGKSSFFSDRGS CCCCCCCCCCCCCCC	33.52	23401153
86	Phosphorylation	RGKSSFFSDRGSGSR CCCCCCCCCCCCCCC	25.12	22167270
88	Methylation	KSSFFSDRGSGSRGR CCCCCCCCCCCCCCC	39.72	-
90	Phosphorylation	SFFSDRGSGSRGRFD CCCCCCCCCCCCCCC	34.19	22167270
92	Phosphorylation	FSDRGSGSRGRFDDR CCCCCCCCCCCCCCC	33.00	22167270
93	Dimethylation	SDRGSGSRGRFDDRG CCCCCCCCCCCCCCC	43.78	-
93	Methylation	SDRGSGSRGRFDDRG CCCCCCCCCCCCCCC	43.78	-
95	Methylation	RGSGSRGRFDDRGRS CCCCCCCCCCCCCCC	30.61	-
99	Methylation	SRGRFDDRGRSDYDG CCCCCCCCCCCCCCC	44.24	-
101	Methylation	GRFDDRGRSDYDGIG CCCCCCCCCCCCCCC	27.52	-
102	Acetylation	RFDDRGRSDYDGIGS CCCCCCCCCCCCCCC	43.26	19608861
102	Phosphorylation	RFDDRGRSDYDGIGS CCCCCCCCCCCCCCC	43.26	21945579
102	Ubiquitination	RFDDRGRSDYDGIGS CCCCCCCCCCCCCCC	43.26	19608861
104	Phosphorylation	DDRGRSDYDGIGSRG CCCCCCCCCCCCCCC	19.81	21945579
109	Phosphorylation	SDYDGIGSRGDRSGF CCCCCCCCCCCCCCC	31.04	21945579
110	Methylation	DYDGIGSRGDRSGFG CCCCCCCCCCCCCCC	45.90	-
114	Phosphorylation	IGSRGDRSGFGKFER CCCCCCCCCCCCCCC	43.12	28985074
118	Sumoylation	GDRSGFGKFERGGNS CCCCCCCCCCCCCCC	41.62	-
118	Acetylation	GDRSGFGKFERGGNS CCCCCCCCCCCCCCC	41.62	19608861
118	Methylation	GDRSGFGKFERGGNS CCCCCCCCCCCCCCC	41.62	19608861
118	Sumoylation	GDRSGFGKFERGGNS CCCCCCCCCCCCCCC	41.62	19608861
118	Ubiquitination	GDRSGFGKFERGGNS CCCCCCCCCCCCCCC	41.62	21906983
121	Methylation	SGFGKFERGGNSRWC CCCCCCCCCCCCCCC	62.54	-
125	Phosphorylation	KFERGGNSRWCDKSD CCCCCCCCCCCCCCC	30.36	22817900
130	Acetylation	GNSRWCDKSDEDDWS CCCCCCCCCCCCCCC	57.58	26051181
130	Ubiquitination	GNSRWCDKSDEDDWS CCCCCCCCCCCCCCC	57.58	-
131	Phosphorylation	NSRWCDKSDEDDWSK CCCCCCCCCCCCCCC	32.74	25159151
137	Phosphorylation	KSDEDDWSKPLPPSE CCCCCCCCCCCCHHH	31.24	20873877
138	Acetylation	SDEDDWSKPLPPSER CCCCCCCCCCCHHHH	46.44	26051181
138	Methylation	SDEDDWSKPLPPSER CCCCCCCCCCCHHHH	46.44	-
138	Sumoylation	SDEDDWSKPLPPSER CCCCCCCCCCCHHHH	46.44	-
138	Ubiquitination	SDEDDWSKPLPPSER CCCCCCCCCCCHHHH	46.44	-
152	Phosphorylation	RLEQELFSGGNTGIN HHHHHHHCCCCCCCC	59.42	21815630
156	Phosphorylation	ELFSGGNTGINFEKY HHHCCCCCCCCCCCC	42.59	20873877
163	Phosphorylation	TGINFEKYDDIPVEA CCCCCCCCCCCCCCC	16.20	26074081
171	Phosphorylation	DDIPVEATGNNCPPH CCCCCCCCCCCCCCC	27.26	26074081
181	Phosphorylation	NCPPHIESFSDVEMG CCCCCCCCCCCCCCC	29.46	18583960
183	Phosphorylation	PPHIESFSDVEMGEI CCCCCCCCCCCCCEE	50.45	18583960
200	Phosphorylation	GNIELTRYTRPTPVQ EEEEEEEECCCCCCH	11.23	28152594
201	Phosphorylation	NIELTRYTRPTPVQK EEEEEEECCCCCCHH	27.21	21406692
204	Phosphorylation	LTRYTRPTPVQKHAI EEEECCCCCCHHCCC	32.57	16280325
208	Ubiquitination	TRPTPVQKHAIPIIK CCCCCCHHCCCHHHH	34.93	21890473
208	Ubiquitination	TRPTPVQKHAIPIIK CCCCCCHHCCCHHHH	34.93	21890473
208	Ubiquitination	TRPTPVQKHAIPIIK CCCCCCHHCCCHHHH	34.93	21890473
215	Sumoylation	KHAIPIIKEKRDLMA HCCCHHHHCHHCHHH	58.88	-
215	Acetylation	KHAIPIIKEKRDLMA HCCCHHHHCHHCHHH	58.88	26051181
215	Sumoylation	KHAIPIIKEKRDLMA HCCCHHHHCHHCHHH	58.88	28112733
215	Ubiquitination	KHAIPIIKEKRDLMA HCCCHHHHCHHCHHH	58.88	-
217	Ubiquitination	AIPIIKEKRDLMACA CCHHHHCHHCHHHHH	46.33	-
221	Sulfoxidation	IKEKRDLMACAQTGS HHCHHCHHHHHHCCC	3.18	30846556
223	Glutathionylation	EKRDLMACAQTGSGK CHHCHHHHHHCCCCH	1.47	22555962
226	Phosphorylation	DLMACAQTGSGKTAA CHHHHHHCCCCHHHH	18.13	20873877
228	Phosphorylation	MACAQTGSGKTAAFL HHHHHCCCCHHHHHH	40.27	20873877
230	Ubiquitination	CAQTGSGKTAAFLLP HHHCCCCHHHHHHHH	36.37	-
231	Phosphorylation	AQTGSGKTAAFLLPI HHCCCCHHHHHHHHH	27.09	20873877
240	Phosphorylation	AFLLPILSQIYSDGP HHHHHHHHHHHCCCC	18.43	18583960
243	Phosphorylation	LPILSQIYSDGPGEA HHHHHHHHCCCCHHH	7.96	20090780
244	Phosphorylation	PILSQIYSDGPGEAL HHHHHHHCCCCHHHH	37.41	20873877
260	Phosphorylation	AMKENGRYGRRKQYP HHHHHCCCCCCCCCC	19.18	22817900
264	Ubiquitination	NGRYGRRKQYPISLV HCCCCCCCCCCCEEE	53.47	21890473
264	Ubiquitination	NGRYGRRKQYPISLV HCCCCCCCCCCCEEE	53.47	21890473
264	Malonylation	NGRYGRRKQYPISLV HCCCCCCCCCCCEEE	53.47	26320211
264	Ubiquitination	NGRYGRRKQYPISLV HCCCCCCCCCCCEEE	53.47	21890473
266	Phosphorylation	RYGRRKQYPISLVLA CCCCCCCCCCEEEEC	12.93	20090780
269	Phosphorylation	RRKQYPISLVLAPTR CCCCCCCEEEECCCH	14.12	28152594
283	Phosphorylation	RELAVQIYEEARKFS HHHHHHHHHHHHHCC	7.22	28152594
290	Phosphorylation	YEEARKFSYRSRVRP HHHHHHCCHHHCCCC	23.75	24144214
291	Phosphorylation	EEARKFSYRSRVRPC HHHHHCCHHHCCCCE	18.75	24144214
293	Phosphorylation	ARKFSYRSRVRPCVV HHHCCHHHCCCCEEE	27.22	24144214
298	Glutathionylation	YRSRVRPCVVYGGAD HHHCCCCEEEECCCC	1.96	22555962
301	Phosphorylation	RVRPCVVYGGADIGQ CCCCEEEECCCCHHH	6.88	20090780
315	Methylation	QQIRDLERGCHLLVA HHHHHHHCCCEEEEE	61.41	-
317	Glutathionylation	IRDLERGCHLLVATP HHHHHCCCEEEEECC	2.27	22555962
317	S-nitrosylation	IRDLERGCHLLVATP HHHHHCCCEEEEECC	2.27	2212679
317	S-palmitoylation	IRDLERGCHLLVATP HHHHHCCCEEEEECC	2.27	26865113
323	Phosphorylation	GCHLLVATPGRLVDM CCEEEEECCCHHHHH	20.85	25159151
335	2-Hydroxyisobutyrylation	VDMMERGKIGLDFCK HHHHHCCCCCHHHHH	39.56	-
335	Acetylation	VDMMERGKIGLDFCK HHHHHCCCCCHHHHH	39.56	25953088
335	Ubiquitination	VDMMERGKIGLDFCK HHHHHCCCCCHHHHH	39.56	21906983
341	Glutathionylation	GKIGLDFCKYLVLDE CCCCHHHHHHHHCCH	2.57	22555962
342	2-Hydroxyisobutyrylation	KIGLDFCKYLVLDEA CCCHHHHHHHHCCHH	41.43	-
342	Ubiquitination	KIGLDFCKYLVLDEA CCCHHHHHHHHCCHH	41.43	-
343	Phosphorylation	IGLDFCKYLVLDEAD CCHHHHHHHHCCHHH	11.83	28152594
352	Sulfoxidation	VLDEADRMLDMGFEP HCCHHHHHHHCCCHH	3.71	21406390
355	Sulfoxidation	EADRMLDMGFEPQIR HHHHHHHCCCHHHHH	6.12	28183972
362	Methylation	MGFEPQIRRIVEQDT CCCHHHHHHHHHHCC	19.61	-
370	Sulfoxidation	RIVEQDTMPPKGVRH HHHHHCCCCCCCCCE	7.81	21406390
373	Ubiquitination	EQDTMPPKGVRHTMM HHCCCCCCCCCEEEE	65.25	-
382	Phosphorylation	VRHTMMFSATFPKEI CCEEEEEECCCCHHH	14.43	28450419
384	Phosphorylation	HTMMFSATFPKEIQM EEEEEECCCCHHHHH	38.99	28450419
410	Phosphorylation	LAVGRVGSTSENITQ HHCCCCCCCCCCCEE	26.38	25159151
411	Phosphorylation	AVGRVGSTSENITQK HCCCCCCCCCCCEEE	33.85	28450419
412	Phosphorylation	VGRVGSTSENITQKV CCCCCCCCCCCEEEE	30.28	28450419
416	Phosphorylation	GSTSENITQKVVWVE CCCCCCCEEEEEEEE	33.64	30108239
418	Acetylation	TSENITQKVVWVEES CCCCCEEEEEEEECH	30.06	26051181
418	Ubiquitination	TSENITQKVVWVEES CCCCCEEEEEEEECH	30.06	-
427	2-Hydroxyisobutyrylation	VWVEESDKRSFLLDL EEEECHHHHHHHHHH	60.26	-
427	Acetylation	VWVEESDKRSFLLDL EEEECHHHHHHHHHH	60.26	26051181
427	Ubiquitination	VWVEESDKRSFLLDL EEEECHHHHHHHHHH	60.26	-
429	Phosphorylation	VEESDKRSFLLDLLN EECHHHHHHHHHHHH	26.45	18583960
438	Phosphorylation	LLDLLNATGKDSLTL HHHHHHHCCCCCEEE	43.63	18583960
442	Phosphorylation	LNATGKDSLTLVFVE HHHCCCCCEEEEEEE	27.09	18583960
452	Acetylation	LVFVETKKGADSLED EEEEEECCCCCCHHH	67.75	26051181
452	Ubiquitination	LVFVETKKGADSLED EEEEEECCCCCCHHH	67.75	-
456	Phosphorylation	ETKKGADSLEDFLYH EECCCCCCHHHHHHC	32.88	28450419
462	Phosphorylation	DSLEDFLYHEGYACT CCHHHHHHCCCCCCC	9.60	20090780
466	Phosphorylation	DFLYHEGYACTSIHG HHHHCCCCCCCCCCC	8.77	30108239
469	Phosphorylation	YHEGYACTSIHGDRS HCCCCCCCCCCCCCC	23.65	20873877
470	Phosphorylation	HEGYACTSIHGDRSQ CCCCCCCCCCCCCCH	16.69	20873877
489	Phosphorylation	EALHQFRSGKSPILV HHHHHHHCCCCCHHH	52.43	30108239
491	Acetylation	LHQFRSGKSPILVAT HHHHHCCCCCHHHHH	55.06	25953088
491	Malonylation	LHQFRSGKSPILVAT HHHHHCCCCCHHHHH	55.06	26320211
491	Ubiquitination	LHQFRSGKSPILVAT HHHHHCCCCCHHHHH	55.06	-
492	Phosphorylation	HQFRSGKSPILVATA HHHHCCCCCHHHHHH	22.24	30108239
498	Phosphorylation	KSPILVATAVAARGL CCCHHHHHHHHHCCC	17.74	28857561
508	Phosphorylation	AARGLDISNVKHVIN HHCCCCCCCCEEEEE	34.93	21815630
511	Acetylation	GLDISNVKHVINFDL CCCCCCCEEEEECCC	36.08	21466224
511	Ubiquitination	GLDISNVKHVINFDL CCCCCCCEEEEECCC	36.08	21906983
520	Phosphorylation	VINFDLPSDIEEYVH EEECCCCCCHHHHHH	59.52	28450419
542	Phosphorylation	VGNLGLATSFFNERN CCCCHHCHHHHCCCC	30.98	20873877
543	Phosphorylation	GNLGLATSFFNERNI CCCHHCHHHHCCCCC	23.41	20873877
554	Ubiquitination	ERNINITKDLLDLLV CCCCCCCHHHHHHHH	42.45	2190698
564	Ubiquitination	LDLLVEAKQEVPSWL HHHHHHHHHHCCHHH	33.22	-
569	Phosphorylation	EAKQEVPSWLENMAY HHHHHCCHHHHHHHH	49.85	20873877
574	Sulfoxidation	VPSWLENMAYEHHYK CCHHHHHHHHHCCCC	2.83	30846556
576	Phosphorylation	SWLENMAYEHHYKGS HHHHHHHHHCCCCCC	12.67	29978859
580	Phosphorylation	NMAYEHHYKGSSRGR HHHHHCCCCCCCCCC	20.96	28796482
581	Methylation	MAYEHHYKGSSRGRS HHHHCCCCCCCCCCC	48.21	-
583	Phosphorylation	YEHHYKGSSRGRSKS HHCCCCCCCCCCCCC	16.83	24719451
584	O-linked_Glycosylation	EHHYKGSSRGRSKSS HCCCCCCCCCCCCCC	47.63	28510447
584	Phosphorylation	EHHYKGSSRGRSKSS HCCCCCCCCCCCCCC	47.63	24719451
585	Methylation	HHYKGSSRGRSKSSR CCCCCCCCCCCCCCC	46.36	-
587	Methylation	YKGSSRGRSKSSRFS CCCCCCCCCCCCCCC	39.54	-
588	O-linked_Glycosylation	KGSSRGRSKSSRFSG CCCCCCCCCCCCCCC	39.45	28510447
588	Phosphorylation	KGSSRGRSKSSRFSG CCCCCCCCCCCCCCC	39.45	24732914
590	Phosphorylation	SSRGRSKSSRFSGGF CCCCCCCCCCCCCCC	28.17	23927012
591	Phosphorylation	SRGRSKSSRFSGGFG CCCCCCCCCCCCCCC	40.87	23927012
592	Methylation	RGRSKSSRFSGGFGA CCCCCCCCCCCCCCC	36.52	24129315
593	Phosphorylation	GRSKSSRFSGGFGAR CCCCCCCCCCCCCCC	9.57	24719451
594	Phosphorylation	RSKSSRFSGGFGARD CCCCCCCCCCCCCCC	36.58	29255136
600	Methylation	FSGGFGARDYRQSSG CCCCCCCCCHHCCCC	41.70	-
602	Phosphorylation	GGFGARDYRQSSGAS CCCCCCCHHCCCCCC	12.66	26434776
603	Methylation	GFGARDYRQSSGASS CCCCCCHHCCCCCCC	33.91	-
605	Phosphorylation	GARDYRQSSGASSSS CCCCHHCCCCCCCCC	23.03	25159151
606	Phosphorylation	ARDYRQSSGASSSSF CCCHHCCCCCCCCCC	30.00	20164059
609	Phosphorylation	YRQSSGASSSSFSSS HHCCCCCCCCCCCCC	33.99	25159151
610	Phosphorylation	RQSSGASSSSFSSSR HCCCCCCCCCCCCCC	29.48	22115753
611	O-linked_Glycosylation	QSSGASSSSFSSSRA CCCCCCCCCCCCCCC	32.67	28510447
611	Phosphorylation	QSSGASSSSFSSSRA CCCCCCCCCCCCCCC	32.67	21955146
612	Phosphorylation	SSGASSSSFSSSRAS CCCCCCCCCCCCCCC	30.97	23401153
614	Phosphorylation	GASSSSFSSSRASSS CCCCCCCCCCCCCCC	29.38	25159151
615	Phosphorylation	ASSSSFSSSRASSSR CCCCCCCCCCCCCCC	23.10	27794612
616	O-linked_Glycosylation	SSSSFSSSRASSSRS CCCCCCCCCCCCCCC	30.57	28510447
616	Phosphorylation	SSSSFSSSRASSSRS CCCCCCCCCCCCCCC	30.57	25159151
617	Methylation	SSSFSSSRASSSRSG CCCCCCCCCCCCCCC	40.20	24129315
619	Phosphorylation	SFSSSRASSSRSGGG CCCCCCCCCCCCCCC	27.95	23403867
620	Phosphorylation	FSSSRASSSRSGGGG CCCCCCCCCCCCCCC	28.87	26074081
621	Phosphorylation	SSSRASSSRSGGGGH CCCCCCCCCCCCCCC	28.15	23403867
622	Methylation	SSRASSSRSGGGGHG CCCCCCCCCCCCCCC	41.07	-
623	Phosphorylation	SRASSSRSGGGGHGS CCCCCCCCCCCCCCC	43.68	26074081
630	Phosphorylation	SGGGGHGSSRGFGGG CCCCCCCCCCCCCCC	15.93	26074081
631	Phosphorylation	GGGGHGSSRGFGGGG CCCCCCCCCCCCCCC	40.80	26074081
632	Methylation	GGGHGSSRGFGGGGY CCCCCCCCCCCCCCC	46.27	24129315
639	Phosphorylation	RGFGGGGYGGFYNSD CCCCCCCCCCCCCCC	19.83	26074081
643	Phosphorylation	GGGYGGFYNSDGYGG CCCCCCCCCCCCCCC	19.61	22210691
645	Phosphorylation	GYGGFYNSDGYGGNY CCCCCCCCCCCCCCC	22.49	26074081
648	Phosphorylation	GFYNSDGYGGNYNSQ CCCCCCCCCCCCCCC	27.18	24719451
652	Phosphorylation	SDGYGGNYNSQGVDW CCCCCCCCCCCCCCC	21.33	27251275
654	Phosphorylation	GYGGNYNSQGVDWWG CCCCCCCCCCCCCCC	20.25	22210691

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
102	S	Phosphorylation	Kinase	IKBKE	Q14164	GPS
181	S	Phosphorylation	Kinase	TBK1	Q9UHD2	Uniprot
183	S	Phosphorylation	Kinase	TBK1	Q9UHD2	Uniprot
204	T	Phosphorylation	Kinase	CDK1	P06493	PSP
204	T	Phosphorylation	Kinase	CDK2	P24941	PSP
240	S	Phosphorylation	Kinase	TBK1	Q9UHD2	Uniprot
269	S	Phosphorylation	Kinase	TBK1	Q9UHD2	Uniprot
323	T	Phosphorylation	Kinase	CDK1	P06493	PSP
429	S	Phosphorylation	Kinase	CSNK1E	P49674	Uniprot
429	S	Phosphorylation	Kinase	TBK1	Q9UHD2	Uniprot
438	T	Phosphorylation	Kinase	TBK1	Q9UHD2	Uniprot
442	S	Phosphorylation	Kinase	TBK1	Q9UHD2	Uniprot
456	S	Phosphorylation	Kinase	TBK1	Q9UHD2	Uniprot
469	T	Phosphorylation	Kinase	CSNK1E	P49674	Uniprot
470	S	Phosphorylation	Kinase	CSNK1E	P49674	Uniprot
520	S	Phosphorylation	Kinase	TBK1	Q9UHD2	Uniprot
542	T	Phosphorylation	Kinase	TBK1	Q9UHD2	Uniprot
543	S	Phosphorylation	Kinase	CSNK1E	P49674	Uniprot
543	S	Phosphorylation	Kinase	TBK1	Q9UHD2	Uniprot
594	S	Phosphorylation	Kinase	AURKB	Q96GD4	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
102	S	Phosphorylation		23478265
Phosphorylated by IKBKE at Ser-102 after ssRNA viral infection; enhances the induction of INFB promoter by IRF3.

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 DDX3X_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PRP8_HUMAN	PRPF8	physical	22939629
RBM39_HUMAN	RBM39	physical	22939629
SRSF5_HUMAN	SRSF5	physical	22939629
SRSF9_HUMAN	SRSF9	physical	22939629
HNRDL_HUMAN	HNRNPDL	physical	22939629
U2AF2_HUMAN	U2AF2	physical	22939629
HNRPR_HUMAN	HNRNPR	physical	22939629
HNRPQ_HUMAN	SYNCRIP	physical	22939629
IMDH1_HUMAN	IMPDH1	physical	22939629
NU133_HUMAN	NUP133	physical	22939629
TPR_HUMAN	TPR	physical	22939629
MBD3_HUMAN	MBD3	physical	22939629
EPIPL_HUMAN	EPPK1	physical	22939629
RS11_HUMAN	RPS11	physical	22939629
TPM2_HUMAN	TPM2	physical	22939629
VATF_HUMAN	ATP6V1F	physical	22939629
IKKE_HUMAN	IKBKE	physical	18636090
EIF3A_HUMAN	EIF3A	physical	18628297
EIF3B_HUMAN	EIF3B	physical	18628297
EIF3C_HUMAN	EIF3C	physical	18628297
EIF3D_HUMAN	EIF3D	physical	18628297
EIF3E_HUMAN	EIF3E	physical	18628297
EIF3F_HUMAN	EIF3F	physical	18628297
EIF3G_HUMAN	EIF3G	physical	18628297
EIF3H_HUMAN	EIF3H	physical	18628297
EIF3I_HUMAN	EIF3I	physical	18628297
EIF3J_HUMAN	EIF3J	physical	18628297
EIF3K_HUMAN	EIF3K	physical	18628297
IL7RA_HUMAN	IL7R	physical	23151878
RS11_HUMAN	RPS11	physical	22863883
RS23_HUMAN	RPS23	physical	22863883
RS2_HUMAN	RPS2	physical	22863883
RS3_HUMAN	RPS3	physical	22863883
RS7_HUMAN	RPS7	physical	22863883
RS9_HUMAN	RPS9	physical	22863883
SND1_HUMAN	SND1	physical	22863883
IKKE_HUMAN	IKBKE	physical	27980081
TRAF3_HUMAN	TRAF3	physical	27980081
MAVS_HUMAN	MAVS	physical	27980081
IRF3_HUMAN	IRF3	physical	27980081

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 DDX3X_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"An N-acetylated natural ligand of human histocompatibility leukocyteantigen (HLA)-B39. Classical major histocompatibility complex class Iproteins bind peptides with a blocked NH(2) terminus in vivo."; Yaguee J., Alvarez I., Rognan D., Ramos M., Vazquez J.,Lopez de Castro J.A.; J. Exp. Med. 191:2083-2092(2000). Cited for: PROTEIN SEQUENCE OF 2-10, AND ACETYLATION AT SER-2.	10859333 [Abstract]
"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-118, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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-594, AND MASSSPECTROMETRY.	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-594 AND SER-612, ANDMASS SPECTROMETRY.	18669648 [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 SER-74; SER-76; SER-78 ANDSER-125, AND MASS SPECTROMETRY.	17287340 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-343; SER-590 ANDSER-594, AND MASS SPECTROMETRY.	17924679 [Abstract]
"Global phosphoproteome analysis on human HepG2 hepatocytes usingreversed-phase diagonal LC."; Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K.,Demol H., Martens L., Goethals M., Vandekerckhove J.; Proteomics 5:3589-3599(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-343, AND MASSSPECTROMETRY.	16097034 [Abstract]
"Quantitative phosphoproteome analysis using a dendrimer conjugationchemistry and tandem mass spectrometry."; Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J.,Bodenmiller B., Watts J.D., Hood L., Aebersold R.; Nat. Methods 2:591-598(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-69, AND MASSSPECTROMETRY.	16094384 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-69 AND TYR-104, AND MASSSPECTROMETRY.	15592455 [Abstract]

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