DDX42_MOUSE - dbPTM
DDX42_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DDX42_MOUSE
UniProt AC Q810A7
Protein Name ATP-dependent RNA helicase DDX42
Gene Name Ddx42
Organism Mus musculus (Mouse).
Sequence Length 929
Subcellular Localization Cytoplasm. Nucleus speckle. Nucleus, Cajal body.
Protein Description ATP-dependent RNA helicase. Binds to partially double-stranded RNAs (dsRNAs) in order to unwind RNA secondary structures. Unwinding is promoted in the presence of single-strand binding proteins. Mediates also RNA duplex formation thereby displacing the single-strand RNA binding protein. ATP and ADP modulate its activity: ATP binding and hydrolysis by DDX42 triggers RNA strand separation, whereas the ADP-bound form of the protein triggers annealing of complementary RNA strands. Involved in the survival of cells by interacting with TP53BP2 and thereby counteracting the apoptosis-stimulating activity of TP53BP2. Relocalizes TP53BP2 to the cytoplasm (By similarity)..
Protein Sequence MNWNKGGPGTKRGFGFGGFAISAGKKEEAKLPQQSHSAFGAASSSSGFGKSAPPQLPSFYKIGSKRANFDEENAYFEDEEEDSSNVDLPYIPAENSPTRQQFHSKPADSDSDDDPLEAFMAEVEDQAARDMKRLEEKDKERKNVKGIRDDIEEEDDQEAYFRYMAENPTAGVVQEEEEDNLEYDSDGNPIAPSKKIIDPLPPIDHSEIDYPPFEKNFYNEHEEITNLTPQQLIDLRHKLNLRVSGAAPPRPGSSFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDGPIAVIVCPTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVVQGDIGEANEDVTQIVEILHSGPSKWNWLTRRLVEFTSSGSVLLFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDIDTHTHRIGRTGRAGEKGVAYTLLTPKDSNFAGDLVRNLEGANQHVSKELLDLAMQNAWFRKSRFKGGKGKKLNIGGGGLGYRERPGLGSENSDRGNNNNVMSNYEAYKPSTGAMGDRLTAMKAAFQSQYKSHFVAASLSNQKAGTSSAGASGWTSAGSLNSVPTNSAQQGHNSPDNPMTSSTKNIPGFNNSGNISSAPVTYPSIGAQGVNNTASGNNSREGIGGGNGKRERYTENRGGSRHSHGDGGNRHGDGGRHGDGYRYPESGSRHTDGHRHGETRHGGSAGRHGESRGANDGRNGESRKEGFNRENKMDPKVDSSRMDKVDSKTDKTPDGFAVPEPPKRKKSRWDS
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
5Acetylation---MNWNKGGPGTKR
---CCCCCCCCCCCC		57.78-
12MethylationKGGPGTKRGFGFGGF
CCCCCCCCCCCCCCE		45.5724129315
35PhosphorylationEAKLPQQSHSAFGAA
HHCCCCCCCCCCCCC		17.7328059163
50AcetylationSSSSGFGKSAPPQLP
CCCCCCCCCCCCCCC		40.9822826441
58PhosphorylationSAPPQLPSFYKIGSK
CCCCCCCCCEEECCC		50.21-
83PhosphorylationFEDEEEDSSNVDLPY
CCCCCCCCCCCCCCC		27.3930635358
84PhosphorylationEDEEEDSSNVDLPYI
CCCCCCCCCCCCCCC		53.8730635358
90PhosphorylationSSNVDLPYIPAENSP
CCCCCCCCCCCCCCC		27.1723984901
96PhosphorylationPYIPAENSPTRQQFH
CCCCCCCCCCHHHHC		21.1027087446
98PhosphorylationIPAENSPTRQQFHSK
CCCCCCCCHHHHCCC		40.7125521595
104PhosphorylationPTRQQFHSKPADSDS
CCHHHHCCCCCCCCC		41.4421082442
109PhosphorylationFHSKPADSDSDDDPL
HCCCCCCCCCCCCHH		40.9118388127
111PhosphorylationSKPADSDSDDDPLEA
CCCCCCCCCCCHHHH		47.0618388127
120OxidationDDPLEAFMAEVEDQA
CCHHHHHHHHHHHHH		3.9117242355
145AcetylationDKERKNVKGIRDDIE
HHHHHCCCCCCCCCC		59.0023236377
163PhosphorylationDQEAYFRYMAENPTA
CHHHHHHHHHHCCCC		7.2625619855
169PhosphorylationRYMAENPTAGVVQEE
HHHHHCCCCCCCCCH		47.8525619855
183PhosphorylationEEEDNLEYDSDGNPI
HHCCCCCCCCCCCCC		24.7424925903
185PhosphorylationEDNLEYDSDGNPIAP
CCCCCCCCCCCCCCC		46.6624925903
193PhosphorylationDGNPIAPSKKIIDPL
CCCCCCCCCCCCCCC		37.2424925903
195AcetylationNPIAPSKKIIDPLPP
CCCCCCCCCCCCCCC		49.5923806337
206PhosphorylationPLPPIDHSEIDYPPF
CCCCCCHHHCCCCCC		32.2825338131
319AcetylationLIHIMDQKELEPGDG
HHHHHCCCCCCCCCC		61.0619855963
442MethylationLLFSATFRKKIEKLA
EEEEHHHHHHHHHHH		34.70-
516PhosphorylationANAEELASNLKQEGH
CCHHHHHHHHHHHCC		56.1529514104
535PhosphorylationLHGDMDQSERNKVIS
CCCCCCHHHHHHHHH		33.9729109428
626AcetylationGANQHVSKELLDLAM
HHHHHHCHHHHHHHH		51.827713433
706PhosphorylationAMKAAFQSQYKSHFV
HHHHHHHHHHHHHHH		29.0829176673
716PhosphorylationKSHFVAASLSNQKAG
HHHHHHHHCCCCCCC		23.6930635358
718PhosphorylationHFVAASLSNQKAGTS
HHHHHHCCCCCCCCC		34.4230635358
724PhosphorylationLSNQKAGTSSAGASG
CCCCCCCCCCCCCCC		25.1123984901
725PhosphorylationSNQKAGTSSAGASGW
CCCCCCCCCCCCCCC		19.7823984901
726PhosphorylationNQKAGTSSAGASGWT
CCCCCCCCCCCCCCC		30.4722942356
733PhosphorylationSAGASGWTSAGSLNS
CCCCCCCCCCCCCCC		16.5426643407
734PhosphorylationAGASGWTSAGSLNSV
CCCCCCCCCCCCCCC		24.9126643407
737PhosphorylationSGWTSAGSLNSVPTN
CCCCCCCCCCCCCCC		24.8823984901
740PhosphorylationTSAGSLNSVPTNSAQ
CCCCCCCCCCCCCCC		34.4623984901
743PhosphorylationGSLNSVPTNSAQQGH
CCCCCCCCCCCCCCC		39.3827087446
745PhosphorylationLNSVPTNSAQQGHNS
CCCCCCCCCCCCCCC		29.9026745281
752PhosphorylationSAQQGHNSPDNPMTS
CCCCCCCCCCCCCCC		28.1427087446
758PhosphorylationNSPDNPMTSSTKNIP
CCCCCCCCCCCCCCC		22.3026745281
759PhosphorylationSPDNPMTSSTKNIPG
CCCCCCCCCCCCCCC		29.7423984901
760PhosphorylationPDNPMTSSTKNIPGF
CCCCCCCCCCCCCCC		33.9523984901
761PhosphorylationDNPMTSSTKNIPGFN
CCCCCCCCCCCCCCC		28.0723984901
779PhosphorylationNISSAPVTYPSIGAQ
CCCCCCCCCCCCCCC		28.7628285833
807AcetylationGIGGGNGKRERYTEN
CCCCCCCCCCCCCCC		55.9015615001
821PhosphorylationNRGGSRHSHGDGGNR
CCCCCCCCCCCCCCC		28.2320139300
897PhosphorylationKMDPKVDSSRMDKVD
CCCCCCCHHHHCCCC		23.88-
898PhosphorylationMDPKVDSSRMDKVDS
CCCCCCHHHHCCCCC		27.45-
929PhosphorylationRKKSRWDS-------
CCCCCCCC-------		34.8524719451
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 DDX42_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DDX42_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 DDX42_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of DDX42_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DDX42_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-104, AND MASSSPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109 AND SER-111, ANDMASS SPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, AND MASSSPECTROMETRY.
"A differential phosphoproteomic analysis of retinoic acid-treated P19cells.";
Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
J. Proteome Res. 6:3174-3186(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104; SER-109 ANDSER-111, AND MASS SPECTROMETRY.
"Phosphoproteomic analysis of the developing mouse brain.";
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
Mol. Cell. Proteomics 3:1093-1101(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185, AND MASSSPECTROMETRY.

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