DDX21_HUMAN - dbPTM
DDX21_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DDX21_HUMAN
UniProt AC Q9NR30
Protein Name Nucleolar RNA helicase 2 {ECO:0000305}
Gene Name DDX21
Organism Homo sapiens (Human).
Sequence Length 783
Subcellular Localization Nucleus, nucleolus . Nucleus, nucleoplasm . Present both in nucleolus and nucleoplasm. Interaction with JUN promotes translocation from the nucleolus to the nucleoplasm (PubMed:11823437, PubMed:18180292). Interaction with WDR46 is required for locali
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). [PubMed: 25470060 Binds various RNAs, such as rRNAs, snoRNAs, 7SK and, at lower extent, mRNAs]
Protein Sequence MPGKLRSDAGLESDTAMKKGETLRKQTEEKEKKEKPKSDKTEEIAEEEETVFPKAKQVKKKAEPSEVDMNSPKSKKAKKKEEPSQNDISPKTKSLRKKKEPIEKKVVSSKTKKVTKNEEPSEEEIDAPKPKKMKKEKEMNGETREKSPKLKNGFPHPEPDCNPSEAASEESNSEIEQEIPVEQKEGAFSNFPISEETIKLLKGRGVTFLFPIQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEKLHGELQDRKRGRAPQVLVLAPTRELANQVSKDFSDITKKLSVACFYGGTPYGGQFERMRNGIDILVGTPGRIKDHIQNGKLDLTKLKHVVLDEVDQMLDMGFADQVEEILSVAYKKDSEDNPQTLLFSATCPHWVFNVAKKYMKSTYEQVDLIGKKTQKTAITVEHLAIKCHWTQRAAVIGDVIRVYSGHQGRTIIFCETKKEAQELSQNSAIKQDAQSLHGDIPQKQREITLKGFRNGSFGVLVATNVAARGLDIPEVDLVIQSSPPKDVESYIHRSGRTGRAGRTGVCICFYQHKEEYQLVQVEQKAGIKFKRIGVPSATEIIKASSKDAIRLLDSVPPTAISHFKQSAEKLIEEKGAVEALAAALAHISGATSVDQRSLINSNVGFVTMILQCSIEMPNISYAWKELKEQLGEEIDSKVKGMVFLKGKLGVCFDVPTASVTEIQEKWHDSRRWQLSVATEQPELEGPREGYGGFRGQREGSRGFRGQRDGNRRFRGQREGSRGPRGQRSGGGNKSNRSQNKGQKRSFSKAFGQ
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
1 (in isoform 2)Acetylation-9.9722814378
7Phosphorylation-MPGKLRSDAGLESD
-CCCCCCCCCCCCCH
42.1023927012
13PhosphorylationRSDAGLESDTAMKKG
CCCCCCCCHHHHHHH
45.3522167270
15PhosphorylationDAGLESDTAMKKGET
CCCCCCHHHHHHHHH
37.6230266825
17SulfoxidationGLESDTAMKKGETLR
CCCCHHHHHHHHHHH
5.1021406390
182-HydroxyisobutyrylationLESDTAMKKGETLRK
CCCHHHHHHHHHHHH
55.98-
18AcetylationLESDTAMKKGETLRK
CCCHHHHHHHHHHHH
55.9828790157
18UbiquitinationLESDTAMKKGETLRK
CCCHHHHHHHHHHHH
55.9824816145
19AcetylationESDTAMKKGETLRKQ
CCHHHHHHHHHHHHH
49.2330583679
22PhosphorylationTAMKKGETLRKQTEE
HHHHHHHHHHHHHHH
40.3023927012
23UbiquitinationAMKKGETLRKQTEEK
HHHHHHHHHHHHHHH
5.8429967540
25AcetylationKKGETLRKQTEEKEK
HHHHHHHHHHHHHHH
65.7630583669
30AcetylationLRKQTEEKEKKEKPK
HHHHHHHHHHHCCCC
69.4730583673
38PhosphorylationEKKEKPKSDKTEEIA
HHHCCCCCCCHHHHH
53.5225627689
40AcetylationKEKPKSDKTEEIAEE
HCCCCCCCHHHHHHH
66.0025953088
40UbiquitinationKEKPKSDKTEEIAEE
HCCCCCCCHHHHHHH
66.0029967540
48UbiquitinationTEEIAEEEETVFPKA
HHHHHHHHHCCCHHH
50.9333845483
50PhosphorylationEIAEEEETVFPKAKQ
HHHHHHHCCCHHHHH
30.6321601212
54AcetylationEEETVFPKAKQVKKK
HHHCCCHHHHHHHHH
57.6726051181
54UbiquitinationEEETVFPKAKQVKKK
HHHCCCHHHHHHHHH
57.6729967540
60UbiquitinationPKAKQVKKKAEPSEV
HHHHHHHHHCCCCCC
59.36-
61AcetylationKAKQVKKKAEPSEVD
HHHHHHHHCCCCCCC
52.8726051181
61UbiquitinationKAKQVKKKAEPSEVD
HHHHHHHHCCCCCCC
52.8729967540
63UbiquitinationKQVKKKAEPSEVDMN
HHHHHHCCCCCCCCC
59.2329967540
65PhosphorylationVKKKAEPSEVDMNSP
HHHHCCCCCCCCCCC
41.5823927012
69SulfoxidationAEPSEVDMNSPKSKK
CCCCCCCCCCCHHHH
6.9021406390
71PhosphorylationPSEVDMNSPKSKKAK
CCCCCCCCCHHHHCC
27.3719664994
73UbiquitinationEVDMNSPKSKKAKKK
CCCCCCCHHHHCCCC
74.7929967540
74PhosphorylationVDMNSPKSKKAKKKE
CCCCCCHHHHCCCCC
42.6524732914
79UbiquitinationPKSKKAKKKEEPSQN
CHHHHCCCCCCCCCC
70.9929967540
80AcetylationKSKKAKKKEEPSQND
HHHHCCCCCCCCCCC
67.6126051181
80UbiquitinationKSKKAKKKEEPSQND
HHHHCCCCCCCCCCC
67.6129967540
84PhosphorylationAKKKEEPSQNDISPK
CCCCCCCCCCCCCHH
44.9123927012
89PhosphorylationEPSQNDISPKTKSLR
CCCCCCCCHHHHHHH
24.1719664994
91UbiquitinationSQNDISPKTKSLRKK
CCCCCCHHHHHHHHC
62.8929967540
92PhosphorylationQNDISPKTKSLRKKK
CCCCCHHHHHHHHCC
29.2924732914
1042-HydroxyisobutyrylationKKKEPIEKKVVSSKT
HCCCCCHHHHCCCCC
52.14-
105PhosphorylationKKEPIEKKVVSSKTK
CCCCCHHHHCCCCCC
34.7733259812
112AcetylationKVVSSKTKKVTKNEE
HHCCCCCCCCCCCCC
49.3220167786
115PhosphorylationSSKTKKVTKNEEPSE
CCCCCCCCCCCCCCH
36.7123927012
116AcetylationSKTKKVTKNEEPSEE
CCCCCCCCCCCCCHH
66.4120167786
116SumoylationSKTKKVTKNEEPSEE
CCCCCCCCCCCCCHH
66.4125114211
116UbiquitinationSKTKKVTKNEEPSEE
CCCCCCCCCCCCCHH
66.4133845483
121PhosphorylationVTKNEEPSEEEIDAP
CCCCCCCCHHHCCCC
62.0029255136
129AcetylationEEEIDAPKPKKMKKE
HHHCCCCCCCCCCHH
71.7926051181
129UbiquitinationEEEIDAPKPKKMKKE
HHHCCCCCCCCCCHH
71.7929967540
131UbiquitinationEIDAPKPKKMKKEKE
HCCCCCCCCCCHHHH
72.1832015554
135AcetylationPKPKKMKKEKEMNGE
CCCCCCCHHHHCCCC
71.2026051181
137AcetylationPKKMKKEKEMNGETR
CCCCCHHHHCCCCCC
71.7523749302
143PhosphorylationEKEMNGETREKSPKL
HHHCCCCCCCCCCCC
45.5927174698
147PhosphorylationNGETREKSPKLKNGF
CCCCCCCCCCCCCCC
23.6325849741
156UbiquitinationKLKNGFPHPEPDCNP
CCCCCCCCCCCCCCH
36.7729967540
164PhosphorylationPEPDCNPSEAASEES
CCCCCCHHHHHCHHC
26.3523927012
168PhosphorylationCNPSEAASEESNSEI
CCHHHHHCHHCCCHH
49.2823927012
168UbiquitinationCNPSEAASEESNSEI
CCHHHHHCHHCCCHH
49.2829967540
171O-linked_GlycosylationSEAASEESNSEIEQE
HHHHCHHCCCHHCCC
41.4223301498
171PhosphorylationSEAASEESNSEIEQE
HHHHCHHCCCHHCCC
41.4223927012
173PhosphorylationAASEESNSEIEQEIP
HHCHHCCCHHCCCCC
49.5925159151
184UbiquitinationQEIPVEQKEGAFSNF
CCCCCCCCCCCCCCC
44.61-
189PhosphorylationEQKEGAFSNFPISEE
CCCCCCCCCCCCCHH
36.7121082442
199SumoylationPISEETIKLLKGRGV
CCCHHHHHHHCCCCC
56.01-
199UbiquitinationPISEETIKLLKGRGV
CCCHHHHHHHCCCCC
56.0132015554
210UbiquitinationGRGVTFLFPIQAKTF
CCCCEEEEEEEECEE
4.3529967540
215AcetylationFLFPIQAKTFHHVYS
EEEEEEECEEEEEEC
35.0325953088
216PhosphorylationLFPIQAKTFHHVYSG
EEEEEECEEEEEECC
31.0823312004
217UbiquitinationFPIQAKTFHHVYSGK
EEEEECEEEEEECCH
3.5533845483
221PhosphorylationAKTFHHVYSGKDLIA
ECEEEEEECCHHHEE
13.8328152594
222PhosphorylationKTFHHVYSGKDLIAQ
CEEEEEECCHHHEEE
37.9728152594
224AcetylationFHHVYSGKDLIAQAR
EEEEECCHHHEEECC
43.3426051181
224UbiquitinationFHHVYSGKDLIAQAR
EEEEECCHHHEEECC
43.3429967540
236UbiquitinationQARTGTGKTFSFAIP
ECCCCCCCCCHHHHH
46.3529967540
237PhosphorylationARTGTGKTFSFAIPL
CCCCCCCCCHHHHHH
26.3423898821
239PhosphorylationTGTGKTFSFAIPLIE
CCCCCCCHHHHHHHH
20.9923898821
255MethylationLHGELQDRKRGRAPQ
HHHHHHCCCCCCCCC
20.01-
259UbiquitinationLQDRKRGRAPQVLVL
HHCCCCCCCCCEEEE
47.3132015554
264UbiquitinationRGRAPQVLVLAPTRE
CCCCCCEEEECCHHH
1.8929967540
2782-HydroxyisobutyrylationELANQVSKDFSDITK
HHHHHHCCCHHHHHH
65.03-
278AcetylationELANQVSKDFSDITK
HHHHHHCCCHHHHHH
65.0326051181
278SuccinylationELANQVSKDFSDITK
HHHHHHCCCHHHHHH
65.0323954790
278UbiquitinationELANQVSKDFSDITK
HHHHHHCCCHHHHHH
65.0329967540
2852-HydroxyisobutyrylationKDFSDITKKLSVACF
CCHHHHHHHHHHEEE
52.64-
285AcetylationKDFSDITKKLSVACF
CCHHHHHHHHHHEEE
52.6425953088
285UbiquitinationKDFSDITKKLSVACF
CCHHHHHHHHHHEEE
52.6433845483
286AcetylationDFSDITKKLSVACFY
CHHHHHHHHHHEEEC
37.0326051181
288PhosphorylationSDITKKLSVACFYGG
HHHHHHHHHEEECCC
19.2929214152
293PhosphorylationKLSVACFYGGTPYGG
HHHHEEECCCCCCCH
17.9629214152
295UbiquitinationSVACFYGGTPYGGQF
HHEEECCCCCCCHHH
16.4929967540
296PhosphorylationVACFYGGTPYGGQFE
HEEECCCCCCCHHHH
14.6925159151
298PhosphorylationCFYGGTPYGGQFERM
EECCCCCCCHHHHHH
33.4523186163
306MethylationGGQFERMRNGIDILV
CHHHHHHHCCEEEEE
44.43-
315PhosphorylationGIDILVGTPGRIKDH
CEEEEECCCHHHHHH
18.3223401153
319UbiquitinationLVGTPGRIKDHIQNG
EECCCHHHHHHHHCC
8.3429967540
3202-HydroxyisobutyrylationVGTPGRIKDHIQNGK
ECCCHHHHHHHHCCC
41.72-
320AcetylationVGTPGRIKDHIQNGK
ECCCHHHHHHHHCCC
41.7226051181
3272-HydroxyisobutyrylationKDHIQNGKLDLTKLK
HHHHHCCCCCHHHCC
46.51-
327AcetylationKDHIQNGKLDLTKLK
HHHHHCCCCCHHHCC
46.5125953088
327UbiquitinationKDHIQNGKLDLTKLK
HHHHHCCCCCHHHCC
46.5132015554
332AcetylationNGKLDLTKLKHVVLD
CCCCCHHHCCCHHHH
63.9426822725
332UbiquitinationNGKLDLTKLKHVVLD
CCCCCHHHCCCHHHH
63.9429967540
334UbiquitinationKLDLTKLKHVVLDEV
CCCHHHCCCHHHHHH
35.5933845483
335UbiquitinationLDLTKLKHVVLDEVD
CCHHHCCCHHHHHHH
25.9229967540
338UbiquitinationTKLKHVVLDEVDQML
HHCCCHHHHHHHHHH
4.5233845483
358PhosphorylationDQVEEILSVAYKKDS
HHHHHHHHHHHCCCC
15.4618452278
361PhosphorylationEEILSVAYKKDSEDN
HHHHHHHHCCCCCCC
19.2018452278
363UbiquitinationILSVAYKKDSEDNPQ
HHHHHHCCCCCCCCC
54.5329967540
371PhosphorylationDSEDNPQTLLFSATC
CCCCCCCEEEEEECC
27.04-
378GlutathionylationTLLFSATCPHWVFNV
EEEEEECCHHHHHHH
2.0322555962
387AcetylationHWVFNVAKKYMKSTY
HHHHHHHHHHHHHHH
39.9025953088
387UbiquitinationHWVFNVAKKYMKSTY
HHHHHHHHHHHHHHH
39.9029967540
392PhosphorylationVAKKYMKSTYEQVDL
HHHHHHHHHHHHHCC
21.4920860994
393PhosphorylationAKKYMKSTYEQVDLI
HHHHHHHHHHHHCCC
26.0920860994
393UbiquitinationAKKYMKSTYEQVDLI
HHHHHHHHHHHHCCC
26.0929967540
394PhosphorylationKKYMKSTYEQVDLIG
HHHHHHHHHHHCCCC
16.0828152594
4022-HydroxyisobutyrylationEQVDLIGKKTQKTAI
HHHCCCCCCCCCEEE
45.73-
402AcetylationEQVDLIGKKTQKTAI
HHHCCCCCCCCCEEE
45.7323236377
402MalonylationEQVDLIGKKTQKTAI
HHHCCCCCCCCCEEE
45.7326320211
402UbiquitinationEQVDLIGKKTQKTAI
HHHCCCCCCCCCEEE
45.7333845483
403UbiquitinationQVDLIGKKTQKTAIT
HHCCCCCCCCCEEEE
51.4829967540
406AcetylationLIGKKTQKTAITVEH
CCCCCCCCEEEEEEH
45.1925953088
406UbiquitinationLIGKKTQKTAITVEH
CCCCCCCCEEEEEEH
45.1923000965
407PhosphorylationIGKKTQKTAITVEHL
CCCCCCCEEEEEEHH
17.3020860994
410PhosphorylationKTQKTAITVEHLAIK
CCCCEEEEEEHHHHH
19.8520860994
413UbiquitinationKTAITVEHLAIKCHW
CEEEEEEHHHHHCHH
19.0721890473
417AcetylationTVEHLAIKCHWTQRA
EEEHHHHHCHHHHHH
17.9125953088
432MethylationAVIGDVIRVYSGHQG
HHHHHEEEEEECCCC
22.59-
434NitrationIGDVIRVYSGHQGRT
HHHEEEEEECCCCCE
10.09-
445S-palmitoylationQGRTIIFCETKKEAQ
CCCEEEEECCHHHHH
4.5929575903
447PhosphorylationRTIIFCETKKEAQEL
CEEEEECCHHHHHHH
48.9020068231
4482-HydroxyisobutyrylationTIIFCETKKEAQELS
EEEEECCHHHHHHHH
26.73-
448AcetylationTIIFCETKKEAQELS
EEEEECCHHHHHHHH
26.7325953088
4492-HydroxyisobutyrylationIIFCETKKEAQELSQ
EEEECCHHHHHHHHH
66.75-
449AcetylationIIFCETKKEAQELSQ
EEEECCHHHHHHHHH
66.7526051181
451UbiquitinationFCETKKEAQELSQNS
EECCHHHHHHHHHCH
19.6124816145
455PhosphorylationKKEAQELSQNSAIKQ
HHHHHHHHHCHHHHH
26.9421406692
458PhosphorylationAQELSQNSAIKQDAQ
HHHHHHCHHHHHHHH
24.5925159151
461AcetylationLSQNSAIKQDAQSLH
HHHCHHHHHHHHHHC
41.6726051181
461UbiquitinationLSQNSAIKQDAQSLH
HHHCHHHHHHHHHHC
41.6729967540
466PhosphorylationAIKQDAQSLHGDIPQ
HHHHHHHHHCCCCCH
24.8520068231
474AcetylationLHGDIPQKQREITLK
HCCCCCHHHHEEEEE
46.0725953088
474UbiquitinationLHGDIPQKQREITLK
HCCCCCHHHHEEEEE
46.0723000965
4812-HydroxyisobutyrylationKQREITLKGFRNGSF
HHHEEEEECCCCCCC
47.56-
481AcetylationKQREITLKGFRNGSF
HHHEEEEECCCCCCC
47.5626051181
481MalonylationKQREITLKGFRNGSF
HHHEEEEECCCCCCC
47.5630639696
481MethylationKQREITLKGFRNGSF
HHHEEEEECCCCCCC
47.56-
481UbiquitinationKQREITLKGFRNGSF
HHHEEEEECCCCCCC
47.5622817900
487UbiquitinationLKGFRNGSFGVLVAT
EECCCCCCCEEEEEE
23.5229967540
494PhosphorylationSFGVLVATNVAARGL
CCEEEEEECHHHCCC
23.8124114839
505UbiquitinationARGLDIPEVDLVIQS
HCCCCCCCCCEEEEC
49.3433845483
512PhosphorylationEVDLVIQSSPPKDVE
CCCEEEECCCCCCHH
33.4220873877
513PhosphorylationVDLVIQSSPPKDVES
CCEEEECCCCCCHHH
28.9229496963
516AcetylationVIQSSPPKDVESYIH
EEECCCCCCHHHHHH
77.2126051181
519UbiquitinationSSPPKDVESYIHRSG
CCCCCCHHHHHHHCC
48.2124816145
520PhosphorylationSPPKDVESYIHRSGR
CCCCCHHHHHHHCCC
29.2728122231
521PhosphorylationPPKDVESYIHRSGRT
CCCCHHHHHHHCCCC
6.2928122231
527UbiquitinationSYIHRSGRTGRAGRT
HHHHHCCCCCCCCCE
34.9429967540
537UbiquitinationRAGRTGVCICFYQHK
CCCCEEEEEEEEECH
2.0733845483
541PhosphorylationTGVCICFYQHKEEYQ
EEEEEEEEECHHHEE
12.8025159151
544AcetylationCICFYQHKEEYQLVQ
EEEEEECHHHEEEEE
36.3926051181
547PhosphorylationFYQHKEEYQLVQVEQ
EEECHHHEEEEEEEH
14.29-
555AcetylationQLVQVEQKAGIKFKR
EEEEEEHHHCCCEEE
34.7726051181
555UbiquitinationQLVQVEQKAGIKFKR
EEEEEEHHHCCCEEE
34.7729967540
559AcetylationVEQKAGIKFKRIGVP
EEHHHCCCEEECCCC
43.8726051181
567PhosphorylationFKRIGVPSATEIIKA
EEECCCCCHHHHHHH
45.4730266825
569PhosphorylationRIGVPSATEIIKASS
ECCCCCHHHHHHHCC
31.8630266825
5732-HydroxyisobutyrylationPSATEIIKASSKDAI
CCHHHHHHHCCHHHH
48.12-
573AcetylationPSATEIIKASSKDAI
CCHHHHHHHCCHHHH
48.1226051181
573UbiquitinationPSATEIIKASSKDAI
CCHHHHHHHCCHHHH
48.1233845483
575PhosphorylationATEIIKASSKDAIRL
HHHHHHHCCHHHHHH
32.6823403867
576PhosphorylationTEIIKASSKDAIRLL
HHHHHHCCHHHHHHH
39.1423403867
577AcetylationEIIKASSKDAIRLLD
HHHHHCCHHHHHHHH
49.007683501
577SuccinylationEIIKASSKDAIRLLD
HHHHHCCHHHHHHHH
49.0023954790
577UbiquitinationEIIKASSKDAIRLLD
HHHHHCCHHHHHHHH
49.00-
585PhosphorylationDAIRLLDSVPPTAIS
HHHHHHHCCCHHHHH
36.1721406692
589PhosphorylationLLDSVPPTAISHFKQ
HHHCCCHHHHHHHHH
30.4721406692
592PhosphorylationSVPPTAISHFKQSAE
CCCHHHHHHHHHHHH
22.0221406692
5952-HydroxyisobutyrylationPTAISHFKQSAEKLI
HHHHHHHHHHHHHHH
37.61-
595AcetylationPTAISHFKQSAEKLI
HHHHHHHHHHHHHHH
37.6127452117
595UbiquitinationPTAISHFKQSAEKLI
HHHHHHHHHHHHHHH
37.6129967540
597PhosphorylationAISHFKQSAEKLIEE
HHHHHHHHHHHHHHH
38.7025159151
600AcetylationHFKQSAEKLIEEKGA
HHHHHHHHHHHHHHH
55.2525953088
600UbiquitinationHFKQSAEKLIEEKGA
HHHHHHHHHHHHHHH
55.2529967540
602UbiquitinationKQSAEKLIEEKGAVE
HHHHHHHHHHHHHHH
10.7329967540
605AcetylationAEKLIEEKGAVEALA
HHHHHHHHHHHHHHH
39.1026051181
605UbiquitinationAEKLIEEKGAVEALA
HHHHHHHHHHHHHHH
39.1033845483
610UbiquitinationEEKGAVEALAAALAH
HHHHHHHHHHHHHHH
8.9029967540
628PhosphorylationATSVDQRSLINSNVG
CCCCCHHHHHCCCCC
28.1526270265
632PhosphorylationDQRSLINSNVGFVTM
CHHHHHCCCCCHHHE
26.3726270265
638PhosphorylationNSNVGFVTMILQCSI
CCCCCHHHEEEHHHC
9.0226270265
644PhosphorylationVTMILQCSIEMPNIS
HHEEEHHHCCCCCHH
14.5022617229
651PhosphorylationSIEMPNISYAWKELK
HCCCCCHHHHHHHHH
18.5526270265
652PhosphorylationIEMPNISYAWKELKE
CCCCCHHHHHHHHHH
16.8222617229
657UbiquitinationISYAWKELKEQLGEE
HHHHHHHHHHHHCHH
7.0324816145
6582-HydroxyisobutyrylationSYAWKELKEQLGEEI
HHHHHHHHHHHCHHH
44.50-
658AcetylationSYAWKELKEQLGEEI
HHHHHHHHHHHCHHH
44.5026822725
667PhosphorylationQLGEEIDSKVKGMVF
HHCHHHHHHHCEEEE
45.0420860994
6682-HydroxyisobutyrylationLGEEIDSKVKGMVFL
HCHHHHHHHCEEEEE
44.19-
668AcetylationLGEEIDSKVKGMVFL
HCHHHHHHHCEEEEE
44.1926051181
668SumoylationLGEEIDSKVKGMVFL
HCHHHHHHHCEEEEE
44.19-
668UbiquitinationLGEEIDSKVKGMVFL
HCHHHHHHHCEEEEE
44.1929967540
6702-HydroxyisobutyrylationEEIDSKVKGMVFLKG
HHHHHHHCEEEEECC
45.05-
670UbiquitinationEEIDSKVKGMVFLKG
HHHHHHHCEEEEECC
45.0529967540
676AcetylationVKGMVFLKGKLGVCF
HCEEEEECCCEEEEE
42.4025953088
6782-HydroxyisobutyrylationGMVFLKGKLGVCFDV
EEEEECCCEEEEEEC
40.24-
678AcetylationGMVFLKGKLGVCFDV
EEEEECCCEEEEEEC
40.2425953088
678UbiquitinationGMVFLKGKLGVCFDV
EEEEECCCEEEEEEC
40.2429967540
682GlutathionylationLKGKLGVCFDVPTAS
ECCCEEEEEECCCCC
1.9822555962
696AcetylationSVTEIQEKWHDSRRW
CCHHHHHHHHHCCCE
33.1926051181
711AcetylationQLSVATEQPELEGPR
EEEEEECCCCCCCCC
32.2019608861
711UbiquitinationQLSVATEQPELEGPR
EEEEEECCCCCCCCC
32.2033845483
721PhosphorylationLEGPREGYGGFRGQR
CCCCCCCCCCCCCCC
14.8820860994
725MethylationREGYGGFRGQREGSR
CCCCCCCCCCCCCCC
43.54-
725UbiquitinationREGYGGFRGQREGSR
CCCCCCCCCCCCCCC
43.5424816145
728MethylationYGGFRGQREGSRGFR
CCCCCCCCCCCCCCC
53.74-
731PhosphorylationFRGQREGSRGFRGQR
CCCCCCCCCCCCCCC
25.2021406692
751PhosphorylationFRGQREGSRGPRGQR
CCCCCCCCCCCCCCC
29.3428176443
759O-linked_GlycosylationRGPRGQRSGGGNKSN
CCCCCCCCCCCCCCC
33.6223301498
759PhosphorylationRGPRGQRSGGGNKSN
CCCCCCCCCCCCCCC
33.62-
776PhosphorylationQNKGQKRSFSKAFGQ
CCCCCCCCHHHHHCC
40.6927422710
778PhosphorylationKGQKRSFSKAFGQ--
CCCCCCHHHHHCC--
25.0727422710
779AcetylationGQKRSFSKAFGQ---
CCCCCHHHHHCC---
45.8019608861
779UbiquitinationGQKRSFSKAFGQ---
CCCCCHHHHHCC---
45.8033845483

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_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DDX21_HUMAN !!

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_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RL6_HUMANRPL6physical
22939629
NPM_HUMANNPM1physical
22939629
RL7_HUMANRPL7physical
22939629
RL31_HUMANRPL31physical
22939629
RL37A_HUMANRPL37Aphysical
22939629
RS11_HUMANRPS11physical
22939629
RS24_HUMANRPS24physical
22939629
RL5_HUMANRPL5physical
22939629
RL1D1_HUMANRSL1D1physical
22939629
RL19_HUMANRPL19physical
22939629
RS23_HUMANRPS23physical
22939629
RED_HUMANIKphysical
22939629
RNPS1_HUMANRNPS1physical
22939629
SAP18_HUMANSAP18physical
22939629
SRSF5_HUMANSRSF5physical
22939629
SRSF7_HUMANSRSF7physical
22939629
HNRPR_HUMANHNRNPRphysical
22939629
SFPQ_HUMANSFPQphysical
22939629
U5S1_HUMANEFTUD2physical
22939629
RBM39_HUMANRBM39physical
22939629
PARP1_HUMANPARP1physical
22939629
RRP7A_HUMANRRP7Aphysical
22939629
RRS1_HUMANRRS1physical
22939629
TR150_HUMANTHRAP3physical
22939629
SON_HUMANSONphysical
22939629
MYO1C_HUMANMYO1Cphysical
22939629
SSRG_HUMANSSR3physical
22939629
SPB1_HUMANFTSJ3physical
22939629
NFIA_HUMANNFIAphysical
22939629
NOP2_HUMANNOP2physical
22939629
SMCA1_HUMANSMARCA1physical
22939629
PCDA2_HUMANPCDHA2physical
22939629
SP16H_HUMANSUPT16Hphysical
22939629
PDS5A_HUMANPDS5Aphysical
22939629
LAMP2_HUMANLAMP2physical
22939629
LMNB1_HUMANLMNB1physical
22939629
S10A9_HUMANS100A9physical
22939629
IL7RA_HUMANIL7Rphysical
23151878

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 DDX21_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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-779, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-71; SER-121 ANDTHR-315, AND MASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89 AND SER-121, AND MASSSPECTROMETRY.
"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-13; SER-71; SER-89;SER-121; SER-168; SER-171 AND SER-173, AND MASS SPECTROMETRY.
"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-13; SER-71; SER-89;SER-121; SER-164; SER-168; SER-171; SER-173 AND THR-315, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71; SER-89 AND SER-121,AND MASS SPECTROMETRY.
"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-71; SER-89 AND SER-121,AND MASS SPECTROMETRY.
"Toward a global characterization of the phosphoproteome in prostatecancer cells: identification of phosphoproteins in the LNCaP cellline.";
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
Electrophoresis 28:2027-2034(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121, AND MASSSPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71; SER-89 AND SER-121,AND MASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71; SER-89 AND SER-121,AND MASS SPECTROMETRY.
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
Kim J.-E., Tannenbaum S.R., White F.M.;
J. Proteome Res. 4:1339-1346(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171, AND MASSSPECTROMETRY.

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