dbPTM

DDX3X_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DDX3X_MOUSE
UniProt AC	Q62167
Protein Name	ATP-dependent RNA helicase DDX3X
Gene Name	Ddx3x
Organism	Mus musculus (Mouse).
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 (By similarity)..
Protein Sequence	MSHVAVENALGLDQQFAGLDLNSSDNQSGGSTASKGRYIPPHLRNREATKGFYDKDSSGWSSSKDKDAYSSFGSRGDSRGKSSFFGDRGSGSRGRFDDRGRGDYDGIGGRGDRSGFGKFERGGNSRWCDKSDEDDWSKPLPPSERLEQELFSGGNTGINFEKYDDIPVEATGNNCPPHIESFSDVEMGEIIMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYADGPGEALRAMKENGRYGRRKQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGAEIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPKGVRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGSTSENITQKVVWVEEIDKRSFLLDLLNATGKDSLTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNERNINITKDLLDLLVEAKQEVPSWLENMAFEHHYKGSSRGRSKSSRFSGGFGARDYRQSSGASSSSFSSSRASSSRSGGGGHGGSRGFGGGGYGGFYNSDGYGGNYNSQGVDWWGN

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	29514104
23	Phosphorylation	FAGLDLNSSDNQSGG HCCCCCCCCCCCCCC	46.49	26824392
24	Phosphorylation	AGLDLNSSDNQSGGS CCCCCCCCCCCCCCC	39.24	26643407
28	Phosphorylation	LNSSDNQSGGSTASK CCCCCCCCCCCCCCC	51.91	26643407
31	Phosphorylation	SDNQSGGSTASKGRY CCCCCCCCCCCCCCC	25.07	26643407
32	Phosphorylation	DNQSGGSTASKGRYI CCCCCCCCCCCCCCC	37.92	26643407
34	Phosphorylation	QSGGSTASKGRYIPP CCCCCCCCCCCCCCH	35.41	26643407
50	Acetylation	LRNREATKGFYDKDS HCCCHHHCCCCCCCC	54.81	22902405
53	Phosphorylation	REATKGFYDKDSSGW CHHHCCCCCCCCCCC	30.65	22817900
55	Acetylation	ATKGFYDKDSSGWSS HHCCCCCCCCCCCCC	48.40	23806337
57	Phosphorylation	KGFYDKDSSGWSSSK CCCCCCCCCCCCCCC	36.17	29899451
61	Phosphorylation	DKDSSGWSSSKDKDA CCCCCCCCCCCCHHH	28.41	26745281
62	Phosphorylation	KDSSGWSSSKDKDAY CCCCCCCCCCCHHHH	34.59	26745281
63	Phosphorylation	DSSGWSSSKDKDAYS CCCCCCCCCCHHHHH	39.08	29899451
66	Malonylation	GWSSSKDKDAYSSFG CCCCCCCHHHHHHCC	48.25	26320211
69	Phosphorylation	SSKDKDAYSSFGSRG CCCCHHHHHHCCCCC	18.25	20116462
70	Phosphorylation	SKDKDAYSSFGSRGD CCCHHHHHHCCCCCC	22.40	25159016
71	Phosphorylation	KDKDAYSSFGSRGDS CCHHHHHHCCCCCCC	22.43	26824392
74	Phosphorylation	DAYSSFGSRGDSRGK HHHHHCCCCCCCCCC	30.95	23684622
78	Phosphorylation	SFGSRGDSRGKSSFF HCCCCCCCCCCCCCC	45.84	25266776
81	Ubiquitination	SRGDSRGKSSFFGDR CCCCCCCCCCCCCCC	41.64	-
82	Phosphorylation	RGDSRGKSSFFGDRG CCCCCCCCCCCCCCC	34.89	27087446
83	Phosphorylation	GDSRGKSSFFGDRGS CCCCCCCCCCCCCCC	28.25	26824392
88	Methylation	KSSFFGDRGSGSRGR CCCCCCCCCCCCCCC	41.37	-
90	Phosphorylation	SFFGDRGSGSRGRFD CCCCCCCCCCCCCCC	34.19	27087446
92	Phosphorylation	FGDRGSGSRGRFDDR CCCCCCCCCCCCCCC	33.00	27087446
93	Dimethylation	GDRGSGSRGRFDDRG CCCCCCCCCCCCCCC	43.78	-
93	Methylation	GDRGSGSRGRFDDRG CCCCCCCCCCCCCCC	43.78	-
95	Methylation	RGSGSRGRFDDRGRG CCCCCCCCCCCCCCC	30.61	-
101	Methylation	GRFDDRGRGDYDGIG CCCCCCCCCCCCCCC	35.39	24129315
104	Phosphorylation	DDRGRGDYDGIGGRG CCCCCCCCCCCCCCC	20.92	16873679
110	Methylation	DYDGIGGRGDRSGFG CCCCCCCCCCCCCCC	38.33	24129315
113	Methylation	GIGGRGDRSGFGKFE CCCCCCCCCCCCCCC	41.31	-
114	Phosphorylation	IGGRGDRSGFGKFER CCCCCCCCCCCCCCC	43.12	-
118	Ubiquitination	GDRSGFGKFERGGNS CCCCCCCCCCCCCCC	41.62	-
118	Acetylation	GDRSGFGKFERGGNS CCCCCCCCCCCCCCC	41.62	-
128	Glutathionylation	RGGNSRWCDKSDEDD CCCCCCCCCCCCCCC	4.60	24333276
130	Acetylation	GNSRWCDKSDEDDWS CCCCCCCCCCCCCCC	57.58	23806337
131	Phosphorylation	NSRWCDKSDEDDWSK CCCCCCCCCCCCCCC	32.74	26643407
152	Phosphorylation	RLEQELFSGGNTGIN HHHHHHHCCCCCCCC	59.42	29514104
183	Phosphorylation	PPHIESFSDVEMGEI CCCCCCCCCCCCCEE	50.45	-
200	Phosphorylation	GNIELTRYTRPTPVQ EEEEEEEECCCCCCH	11.23	29514104
215	Ubiquitination	KHAIPIIKEKRDLMA HCCCHHHHCHHCHHH	58.88	-
223	S-nitrosocysteine	EKRDLMACAQTGSGK CHHCHHHHHHCCCCH	1.47	-
223	S-nitrosylation	EKRDLMACAQTGSGK CHHCHHHHHHCCCCH	1.47	20925432
223	S-palmitoylation	EKRDLMACAQTGSGK CHHCHHHHHHCCCCH	1.47	28526873
226	Phosphorylation	DLMACAQTGSGKTAA CHHHHHHCCCCHHHH	18.13	24759943
228	Phosphorylation	MACAQTGSGKTAAFL HHHHHCCCCHHHHHH	40.27	24759943
240	Phosphorylation	AFLLPILSQIYADGP HHHHHHHHHHHCCCC	18.43	28059163
243	Phosphorylation	LPILSQIYADGPGEA HHHHHHHHCCCCHHH	7.33	22817900
264	Ubiquitination	NGRYGRRKQYPISLV HCCCCCCCCCCCEEE	53.47	-
266	Phosphorylation	RYGRRKQYPISLVLA CCCCCCCCCCEEEEC	12.93	29514104
283	Phosphorylation	RELAVQIYEEARKFS HHHHHHHHHHHHHCC	7.22	22817900
293	Phosphorylation	ARKFSYRSRVRPCVV HHHCCHHHCCCCEEE	27.22	-
298	S-nitrosocysteine	YRSRVRPCVVYGGAE HHHCCCCEEEECCHH	1.96	-
298	S-palmitoylation	YRSRVRPCVVYGGAE HHHCCCCEEEECCHH	1.96	28526873
298	S-nitrosylation	YRSRVRPCVVYGGAE HHHCCCCEEEECCHH	1.96	20925432
301	Phosphorylation	RVRPCVVYGGAEIGQ CCCCEEEECCHHHHH	6.88	22817900
317	S-nitrosocysteine	IRDLERGCHLLVATP HHHHHCCCEEEEECC	2.27	-
317	S-palmitoylation	IRDLERGCHLLVATP HHHHHCCCEEEEECC	2.27	28526873
317	S-nitrosylation	IRDLERGCHLLVATP HHHHHCCCEEEEECC	2.27	20925432
323	Phosphorylation	GCHLLVATPGRLVDM CCEEEEECCCHHHHH	20.85	26824392
335	Ubiquitination	VDMMERGKIGLDFCK HHHHHCCCCCHHHHH	39.56	-
335	Malonylation	VDMMERGKIGLDFCK HHHHHCCCCCHHHHH	39.56	26320211
410	Phosphorylation	LAVGRVGSTSENITQ HHCCCCCCCCCCCCE	26.38	30635358
411	Phosphorylation	AVGRVGSTSENITQK HCCCCCCCCCCCCEE	33.85	26745281
412	Phosphorylation	VGRVGSTSENITQKV CCCCCCCCCCCCEEE	30.28	29176673
456	Phosphorylation	ETKKGADSLEDFLYH EECCCCCCHHHHHHC	32.88	22817900
462	Phosphorylation	DSLEDFLYHEGYACT CCHHHHHHCCCCCCC	9.60	22817900
466	Phosphorylation	DFLYHEGYACTSIHG HHHHCCCCCCCCCCC	8.77	18034455
468	S-nitrosocysteine	LYHEGYACTSIHGDR HHCCCCCCCCCCCCC	2.00	-
468	S-nitrosylation	LYHEGYACTSIHGDR HHCCCCCCCCCCCCC	2.00	20925432
508	Phosphorylation	AARGLDISNVKHVIN HHCCCCCCCCEEEEE	34.93	22006019
511	Ubiquitination	GLDISNVKHVINFDL CCCCCCCEEEEECCC	36.08	-
520	Phosphorylation	VINFDLPSDIEEYVH EEECCCCCCHHHHHH	59.52	26745281
525	Phosphorylation	LPSDIEEYVHRIGRT CCCCHHHHHHHHCCC	6.70	26745281
554	Ubiquitination	ERNINITKDLLDLLV CCCCCCCHHHHHHHH	42.45	-
580	Phosphorylation	NMAFEHHYKGSSRGR HHHHHHCCCCCCCCC	20.96	29514104
583	Phosphorylation	FEHHYKGSSRGRSKS HHHCCCCCCCCCCCC	16.83	27600695
588	Phosphorylation	KGSSRGRSKSSRFSG CCCCCCCCCCCCCCC	39.45	29514104
590	Phosphorylation	SSRGRSKSSRFSGGF CCCCCCCCCCCCCCC	28.17	27087446
591	Phosphorylation	SRGRSKSSRFSGGFG CCCCCCCCCCCCCCC	40.87	27600695
592	Dimethylation	RGRSKSSRFSGGFGA CCCCCCCCCCCCCCC	36.52	-
592	Methylation	RGRSKSSRFSGGFGA CCCCCCCCCCCCCCC	36.52	-
594	Phosphorylation	RSKSSRFSGGFGARD CCCCCCCCCCCCCCC	36.58	27087446
602	Phosphorylation	GGFGARDYRQSSGAS CCCCCCCHHCCCCCC	12.66	29899451
605	Phosphorylation	GARDYRQSSGASSSS CCCCHHCCCCCCCCC	23.03	25521595
606	Phosphorylation	ARDYRQSSGASSSSF CCCHHCCCCCCCCCC	30.00	25521595
609	Phosphorylation	YRQSSGASSSSFSSS HHCCCCCCCCCCCCC	33.99	25521595
610	Phosphorylation	RQSSGASSSSFSSSR HCCCCCCCCCCCCCC	29.48	30635358
611	Phosphorylation	QSSGASSSSFSSSRA CCCCCCCCCCCCCCC	32.67	30635358
612	Phosphorylation	SSGASSSSFSSSRAS CCCCCCCCCCCCCCC	30.97	25521595
614	Phosphorylation	GASSSSFSSSRASSS CCCCCCCCCCCCCCC	29.38	29472430
615	Phosphorylation	ASSSSFSSSRASSSR CCCCCCCCCCCCCCC	23.10	23984901
616	Phosphorylation	SSSSFSSSRASSSRS CCCCCCCCCCCCCCC	30.57	23984901
617	Methylation	SSSFSSSRASSSRSG CCCCCCCCCCCCCCC	40.20	-
619	Phosphorylation	SFSSSRASSSRSGGG CCCCCCCCCCCCCCC	27.95	27149854
621	Phosphorylation	SSSRASSSRSGGGGH CCCCCCCCCCCCCCC	28.15	29899451
632	Methylation	GGGHGGSRGFGGGGY CCCCCCCCCCCCCCC	47.97	24129315

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
Oops, there are no upstream regulatory protein records of DDX3X_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of DDX3X_MOUSE !!

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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of DDX3X_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of DDX3X_MOUSE

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]
Phosphorylation
Reference	PubMed
"The phagosomal proteome in interferon-gamma-activated macrophages."; Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.; Immunity 30:143-154(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-594, AND MASSSPECTROMETRY.	19144319 [Abstract]
"Identification of phosphoproteins and their phosphorylation sites inthe WEHI-231 B lymphoma cell line."; Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.; Mol. Cell. Proteomics 3:279-286(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, AND MASSSPECTROMETRY.	14729942 [Abstract]