DDX3L_MOUSE - dbPTM
DDX3L_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DDX3L_MOUSE
UniProt AC P16381
Protein Name Putative ATP-dependent RNA helicase Pl10
Gene Name D1Pas1
Organism Mus musculus (Mouse).
Sequence Length 660
Subcellular Localization
Protein Description Putative ATP-dependent RNA helicase. Possible role in a key step of the spermatogenic process..
Protein Sequence MSHVAEEDELGLDQQLAGLDLTSRDSQSGGSTASKGRYIPPHLRNREAAKAFYDKDGSRWSKDKDAYSSFGSRSDTRAKSSFFSDRGGSGSRGRFDERGRSDYESVGSRGGRSGFGKFERGGNSRWCDKADEDDWSKPLPPSERLEQELFSGGNTGINFEKYDDIPVEATGNNCPPHIESFSDVEMGEIIMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYTDGPGEALRAMKENGKYGRRKQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPKGVRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGSTSENITQKVVWVEEADKRSFLLDLLNATGKDSLILVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNERNINITKDLLDLLVEAKQEVPSWLENMAFEHHYKGGSRGRSKSRFSGGFGARDYRQSSGASSSSFSSGRASNSRSGGGSHGSSRGFGGGSYGGFYNSDGYGGNYSSQGVDWWGN
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
2Acetylation------MSHVAEEDE
------CCCCCHHHH		27.03-
2Phosphorylation------MSHVAEEDE
------CCCCCHHHH		27.0325293948
26PhosphorylationLDLTSRDSQSGGSTA
CCCCCCCCCCCCCCC		25.74-
28PhosphorylationLTSRDSQSGGSTASK
CCCCCCCCCCCCCCC		49.42-
55AcetylationAAKAFYDKDGSRWSK
HHHHHHCCCCCCCCC		53.24-
64AcetylationGSRWSKDKDAYSSFG
CCCCCCCHHHHHHCC		48.2523806337
64MalonylationGSRWSKDKDAYSSFG
CCCCCCCHHHHHHCC		48.2526320211
67PhosphorylationWSKDKDAYSSFGSRS
CCCCHHHHHHCCCCC		18.2525159016
68PhosphorylationSKDKDAYSSFGSRSD
CCCHHHHHHCCCCCH		22.4025159016
69PhosphorylationKDKDAYSSFGSRSDT
CCHHHHHHCCCCCHH		22.4327180971
72PhosphorylationDAYSSFGSRSDTRAK
HHHHHCCCCCHHCCH		26.9725159016
80PhosphorylationRSDTRAKSSFFSDRG
CCHHCCHHHCCCCCC		31.24-
81PhosphorylationSDTRAKSSFFSDRGG
CHHCCHHHCCCCCCC		29.60-
84PhosphorylationRAKSSFFSDRGGSGS
CCHHHCCCCCCCCCC		25.12-
86MethylationKSSFFSDRGGSGSRG
HHHCCCCCCCCCCCC		50.61-
89PhosphorylationFFSDRGGSGSRGRFD
CCCCCCCCCCCCCCC		36.10-
100MethylationGRFDERGRSDYESVG
CCCCCCCCCCCCCCC		32.35-
101PhosphorylationRFDERGRSDYESVGS
CCCCCCCCCCCCCCC		47.58-
103PhosphorylationDERGRSDYESVGSRG
CCCCCCCCCCCCCCC		16.02-
109MethylationDYESVGSRGGRSGFG
CCCCCCCCCCCCCCC		45.73-
117AcetylationGGRSGFGKFERGGNS
CCCCCCCCCCCCCCC		41.62-
117UbiquitinationGGRSGFGKFERGGNS
CCCCCCCCCCCCCCC		41.62-
151PhosphorylationRLEQELFSGGNTGIN
HHHHHHHCCCCCCCC		59.4229514104
182PhosphorylationPPHIESFSDVEMGEI
CCCCCCCCCCCCCEE		50.45-
199PhosphorylationGNIELTRYTRPTPVQ
EEEEEEEECCCCCCH		11.2329514104
214UbiquitinationKHAIPIIKEKRDLMA
HCCCHHHHCHHCHHH		58.88-
225PhosphorylationDLMACAQTGSGKTAA
CHHHHHHCCCCHHHH		18.1324759943
227PhosphorylationMACAQTGSGKTAAFL
HHHHHCCCCHHHHHH		40.2724759943
263UbiquitinationNGKYGRRKQYPISLV
HCCCCCCCCCCCEEE		53.47-
282PhosphorylationRELAVQIYEEARKFS
HHHHHHHHHHHHHCC		7.2222817900
292PhosphorylationARKFSYRSRVRPCVV
HHHCCHHHCCCCEEE		27.22-
300PhosphorylationRVRPCVVYGGADIGQ
CCCCEEEECCCCHHH		6.88-
316GlutathionylationIRDLERGCHLLVATP
HHHHHCCCEEEEECC		2.2724333276
322PhosphorylationGCHLLVATPGRLVDM
CCEEEEECCCHHHHH		20.8526824392
334MalonylationVDMMERGKIGLDFCK
HHHHHCCCCCHHHHH		39.5626320211
334UbiquitinationVDMMERGKIGLDFCK
HHHHHCCCCCHHHHH		39.56-
340GlutathionylationGKIGLDFCKYLVLDE
CCCCHHHHHHHHCCH		2.5724333276
409PhosphorylationLAVGRVGSTSENITQ
HHCCCCCCCCCCCCE		26.3830635358
410PhosphorylationAVGRVGSTSENITQK
HCCCCCCCCCCCCEE		33.8526745281
411PhosphorylationVGRVGSTSENITQKV
CCCCCCCCCCCCEEE		30.2829176673
428PhosphorylationVEEADKRSFLLDLLN
EEEHHHHHHHHHHHH		26.45-
455PhosphorylationETKKGADSLEDFLYH
EECCCCCCHHHHHHC		32.8822817900
461PhosphorylationDSLEDFLYHEGYACT
CCHHHHHHCCCCCCC		9.6022817900
465PhosphorylationDFLYHEGYACTSIHG
HHHHCCCCCCCCCCC		8.7722817900
507PhosphorylationAARGLDISNVKHVIN
HHCCCCCCCCEEEEE		34.9322006019
510UbiquitinationGLDISNVKHVINFDL
CCCCCCCEEEEECCC		36.08-
519PhosphorylationVINFDLPSDIEEYVH
EEECCCCCCHHHHHH		59.5226745281
524PhosphorylationLPSDIEEYVHRIGRT
CCCCHHHHHHHHCCC		6.7026745281
553UbiquitinationERNINITKDLLDLLV
CCCCCCCHHHHHHHH		42.45-
589PhosphorylationGSRGRSKSRFSGGFG
CCCCCCCCCCCCCCC		39.5426745281
590MethylationSRGRSKSRFSGGFGA
CCCCCCCCCCCCCCC		33.22-
592PhosphorylationGRSKSRFSGGFGARD
CCCCCCCCCCCCCCC		36.5823684622
603PhosphorylationGARDYRQSSGASSSS
CCCCCCCCCCCCCCC		23.0323684622
604PhosphorylationARDYRQSSGASSSSF
CCCCCCCCCCCCCCC		30.00-
610PhosphorylationSSGASSSSFSSGRAS
CCCCCCCCCCCCCCC		30.97-
615MethylationSSSFSSGRASNSRSG
CCCCCCCCCCCCCCC		36.47-
630MethylationGGSHGSSRGFGGGSY
CCCCCCCCCCCCCCC		46.27-
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 DDX3L_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DDX3L_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 DDX3L_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of DDX3L_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DDX3L_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-465, AND MASSSPECTROMETRY.
"Quantitative time-resolved phosphoproteomic analysis of mast cellsignaling.";
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,Kawakami T., Salomon A.R.;
J. Immunol. 179:5864-5876(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-282, AND MASSSPECTROMETRY.

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