DDX21_MOUSE - dbPTM
DDX21_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DDX21_MOUSE
UniProt AC Q9JIK5
Protein Name Nucleolar RNA helicase 2 {ECO:0000305}
Gene Name Ddx21
Organism Mus musculus (Mouse).
Sequence Length 851
Subcellular Localization Nucleus, nucleolus . Nucleus, nucleoplasm . Present both in nucleolus and nucleoplasm. Interaction with JUN promotes translocation from the nucleolus to the nucleoplasm. Interaction with WDR46 is required for localization to the nucleolus.
Protein Description RNA helicase that acts as a sensor of the transcriptional status of both RNA polymerase (Pol) I and II: promotes ribosomal RNA (rRNA) processing and transcription from polymerase II (Pol II). Binds various RNAs, such as rRNAs, snoRNAs, 7SK and, at lower extent, mRNAs. In the nucleolus, localizes to rDNA locus, where it directly binds rRNAs and snoRNAs, and promotes rRNA transcription, processing and modification. Required for rRNA 2'-O-methylation, possibly by promoting the recruitment of late-acting snoRNAs SNORD56 and SNORD58 with pre-ribosomal complexes. In the nucleoplasm, binds 7SK RNA and is recruited to the promoters of Pol II-transcribed genes: acts by facilitating the release of P-TEFb from inhibitory 7SK snRNP in a manner that is dependent on its helicase activity, thereby promoting transcription of its target genes. Functions as cofactor for JUN-activated transcription: required for phosphorylation of JUN at 'Ser-77'. Can unwind double-stranded RNA (helicase) and can fold or introduce a secondary structure to a single-stranded RNA (foldase). Involved in rRNA processing. May bind to specific miRNA hairpins (By similarity)..
Protein Sequence MPGKLRSGAKLGSDGAEESMETLPKPSEKKTRKEKTKSKTEEATEGMEEAVSSKAKKTNKKGPSEDDVDPPKSRKAKKQEEEPQDDTASTSKTSKKKKEPLEKQADSETKEIITEEPSEEEADMPKPKKMKKGKEANGDAGEKSPKLKNGLSQPSEEEADIPKPKKMKKGKEANGDAGEKSPKLKNGLSQPSEEEVDIPKPKKMKKGKEASGDAGEKSPRLKDGLSQPSEPKSNSSDAPGEESSSETEKEIPVEQKEGAFSNFPISEETVKLLKARGVNFLFPIQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEKLQGGLQERKRGRAPQVLVLAPTRELANQVSKDFSDITKKLSVACFYGGTPYGGQIERMRSGIDILVGTPGRIKDHLQNGKLDLTKLKHVVLDEVDQMLDMGFADQVEEILCVAYKKDSEDNPQTLLFSATCPHWVFNVAKKYMKSTYEQVDLIGKKTQKAAITVEHLAIKCHWTERAAVIGDVIRVYSGHQGRTIIFCETKKDAQELSQNTCIKQDAQSLHGDIPQKQREITLKGFRNGNFGVLVATNVAARGLDIPEVDLVVQSCPPKDVESYIHRSGRTGRAGRTGVCICFYQNKEEYQLAQVEQKAGIKFKRIGVPSATEIIKASSKDAIRLLDSVPPTAISHFKQSAEKLIEEKGAVEALAAALAHISGATSVDQRSLINSQAGFVTMILRCSIEMPNISYAWKELKEQLGESIDAKVKGMVFLKGKLGVCFDVRTEAVTEIQEKWHDSRRWQLTVATEQPELEGPPDGYRGRMGQRDGSRGAFRGQRGGSRNFRGQGQRGGSRNFRGQRPGGGNRGQKRSFSKAFGQ
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
7Phosphorylation-MPGKLRSGAKLGSD
-CCCCCCCCCCCCCC		54.24-
10AcetylationGKLRSGAKLGSDGAE
CCCCCCCCCCCCCHH		57.8323806337
13PhosphorylationRSGAKLGSDGAEESM
CCCCCCCCCCHHHHH		43.2225521595
19PhosphorylationGSDGAEESMETLPKP
CCCCHHHHHHCCCCC		17.2725619855
22PhosphorylationGAEESMETLPKPSEK
CHHHHHHCCCCCCCC		39.4525619855
27PhosphorylationMETLPKPSEKKTRKE
HHCCCCCCCCCCHHH		69.0825619855
38PhosphorylationTRKEKTKSKTEEATE
CHHHHHCHHHHHHHH		50.4725338131
39AcetylationRKEKTKSKTEEATEG
HHHHHCHHHHHHHHH		62.6023806337
64PhosphorylationKTNKKGPSEDDVDPP
HCCCCCCCCCCCCCC		63.4326824392
87PhosphorylationEEEPQDDTASTSKTS
CCCCCCCCCCCCCCC		30.6925159016
89PhosphorylationEPQDDTASTSKTSKK
CCCCCCCCCCCCCHH		34.9925521595
90PhosphorylationPQDDTASTSKTSKKK
CCCCCCCCCCCCHHC		31.6025159016
91PhosphorylationQDDTASTSKTSKKKK
CCCCCCCCCCCHHCC		31.2925159016
93PhosphorylationDTASTSKTSKKKKEP
CCCCCCCCCHHCCCC		45.6122345495
94PhosphorylationTASTSKTSKKKKEPL
CCCCCCCCHHCCCCC		46.3326824392
107PhosphorylationPLEKQADSETKEIIT
CCHHHCCHHHHHHHC		50.6225619855
109PhosphorylationEKQADSETKEIITEE
HHHCCHHHHHHHCCC		37.6225619855
114PhosphorylationSETKEIITEEPSEEE
HHHHHHHCCCCCHHH		39.7027742792
118PhosphorylationEIITEEPSEEEADMP
HHHCCCCCHHHCCCC		62.0027087446
124OxidationPSEEEADMPKPKKMK
CCHHHCCCCCCCCCC		6.2317242355
134AcetylationPKKMKKGKEANGDAG
CCCCCCCCCCCCCCC		63.63-
144PhosphorylationNGDAGEKSPKLKNGL
CCCCCCCCHHHCCCC		23.9827087446
152PhosphorylationPKLKNGLSQPSEEEA
HHHCCCCCCCCHHHC		41.2522942356
155PhosphorylationKNGLSQPSEEEADIP
CCCCCCCCHHHCCCC		50.4225521595
181PhosphorylationNGDAGEKSPKLKNGL
CCCCCCCCHHHCCCC		23.9827087446
189PhosphorylationPKLKNGLSQPSEEEV
HHHCCCCCCCCHHHC		41.2522942356
192PhosphorylationKNGLSQPSEEEVDIP
CCCCCCCCHHHCCCC		50.4227087446
211PhosphorylationMKKGKEASGDAGEKS
CCCCCCCCCCCCCCC		37.9924068923
217AcetylationASGDAGEKSPRLKDG
CCCCCCCCCCCCCCC		65.9123806337
218PhosphorylationSGDAGEKSPRLKDGL
CCCCCCCCCCCCCCC		15.7927087446
222UbiquitinationGEKSPRLKDGLSQPS
CCCCCCCCCCCCCCC		51.54-
226PhosphorylationPRLKDGLSQPSEPKS
CCCCCCCCCCCCCCC		45.6422817900
229PhosphorylationKDGLSQPSEPKSNSS
CCCCCCCCCCCCCCC		59.9228066266
233PhosphorylationSQPSEPKSNSSDAPG
CCCCCCCCCCCCCCC		53.3027087446
235PhosphorylationPSEPKSNSSDAPGEE
CCCCCCCCCCCCCCC		36.3623684622
236PhosphorylationSEPKSNSSDAPGEES
CCCCCCCCCCCCCCC		41.8825521595
243PhosphorylationSDAPGEESSSETEKE
CCCCCCCCCCCCCCC		34.5627087446
244PhosphorylationDAPGEESSSETEKEI
CCCCCCCCCCCCCCC		35.1627087446
245PhosphorylationAPGEESSSETEKEIP
CCCCCCCCCCCCCCC		58.7927087446
247PhosphorylationGEESSSETEKEIPVE
CCCCCCCCCCCCCHH		55.0625521595
261PhosphorylationEQKEGAFSNFPISEE
HHCCCCCCCCCCCHH		36.7124453211
293PhosphorylationAKTFHHVYSGKDLIA
ECEEEEEECCHHHEE		13.8325367039
311PhosphorylationTGTGKTFSFAIPLIE
CCCCCEEHHHHHHHH		20.9922006019
319UbiquitinationFAIPLIEKLQGGLQE
HHHHHHHHHHHHHHH		38.83-
349PhosphorylationRELANQVSKDFSDIT
HHHHHHHCCCHHHHH		19.4222871156
358AcetylationDFSDITKKLSVACFY
CHHHHHHHHHHEEEC		37.0322826441
368PhosphorylationVACFYGGTPYGGQIE
HEEECCCCCCCHHHH		14.69-
387PhosphorylationGIDILVGTPGRIKDH
CCCEEECCCHHHHHH		18.3226824392
399UbiquitinationKDHLQNGKLDLTKLK
HHHHHCCCCCHHHCH		46.51-
450S-nitrosylationTLLFSATCPHWVFNV
EEEEEECCHHHHHHH		2.0320925432
450S-nitrosocysteineTLLFSATCPHWVFNV
EEEEEECCHHHHHHH		2.03-
459UbiquitinationHWVFNVAKKYMKSTY
HHHHHHHHHHHHHHH		39.90-
474UbiquitinationEQVDLIGKKTQKAAI
HHHHHCCHHHHCEEE		45.73-
521UbiquitinationIIFCETKKDAQELSQ
EEEECCHHHHHHHHH		66.76-
538PhosphorylationCIKQDAQSLHGDIPQ
HHHHHHHHHHCCCCH		24.8522817900
546UbiquitinationLHGDIPQKQREITLK
HHCCCCHHHCEEEEE		46.07-
553UbiquitinationKQREITLKGFRNGNF
HHCEEEEEECCCCCC		47.56-
585S-nitrosocysteineVDLVVQSCPPKDVES
CCEEEECCCCCHHHH		3.60-
585S-nitrosylationVDLVVQSCPPKDVES
CCEEEECCCCCHHHH		3.6020925432
592PhosphorylationCPPKDVESYIHRSGR
CCCCHHHHHHHHCCC		29.2722817900
597PhosphorylationVESYIHRSGRTGRAG
HHHHHHHCCCCCCCC		20.6124453211
627UbiquitinationQLAQVEQKAGIKFKR
HHHHHHHHHCCCEEE		34.77-
639PhosphorylationFKRIGVPSATEIIKA
EEECCCCCHHHHHHH		45.47-
641PhosphorylationRIGVPSATEIIKASS
ECCCCCHHHHHHHCC		31.86-
645UbiquitinationPSATEIIKASSKDAI
CCHHHHHHHCCHHHH		48.12-
657PhosphorylationDAIRLLDSVPPTAIS
HHHHHHHCCCHHHHH		36.17-
672AcetylationHFKQSAEKLIEEKGA
HHHHHHHHHHHHHHH		55.25-
730AcetylationSYAWKELKEQLGESI
HHHHHHHHHHHCCCC		44.5023236377
754S-nitrosylationLKGKLGVCFDVRTEA
ECCCEEEEEEECHHH		1.9820925432
754S-nitrosocysteineLKGKLGVCFDVRTEA
ECCCEEEEEEECHHH		1.98-
759PhosphorylationGVCFDVRTEAVTEIQ
EEEEEECHHHHHHHH		28.3024759943
763PhosphorylationDVRTEAVTEIQEKWH
EECHHHHHHHHHHHH		34.1224759943
814PhosphorylationFRGQRGGSRNFRGQG
CCCCCCCCCCCCCCC		27.2029514104
818MethylationRGGSRNFRGQGQRGG
CCCCCCCCCCCCCCC		39.82-
823MethylationNFRGQGQRGGSRNFR
CCCCCCCCCCCCCCC		59.26-
826PhosphorylationGQGQRGGSRNFRGQR
CCCCCCCCCCCCCCC		27.2029514104
844PhosphorylationGNRGQKRSFSKAFGQ
CCCCCCCCHHHHHCC		40.6924759943
846PhosphorylationRGQKRSFSKAFGQ--
CCCCCCHHHHHCC--		25.0724759943
847AcetylationGQKRSFSKAFGQ---
CCCCCHHHHHCC---		45.80-
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 DDX21_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DDX21_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 DDX21_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IMA7_HUMANKPNA6physical
20360068
DDX21_HUMANDDX21physical
20360068
IMA5_HUMANKPNA1physical
20360068
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DDX21_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118; SER-155; THR-247AND SER-261, AND MASS SPECTROMETRY.
"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-118 AND SER-144, ANDMASS SPECTROMETRY.
"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-118; SER-155 ANDSER-192, AND MASS SPECTROMETRY.
"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-236; SER-244; SER-245AND THR-247, AND MASS SPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, AND MASSSPECTROMETRY.

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