DDX42_HUMAN - dbPTM
DDX42_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DDX42_HUMAN
UniProt AC Q86XP3
Protein Name ATP-dependent RNA helicase DDX42
Gene Name DDX42
Organism Homo sapiens (Human).
Sequence Length 938
Subcellular Localization Cytoplasm. Nucleus speckle. Nucleus, Cajal body. Isoform 2 is present in Cajal bodies (CBs) and nuclear speckles.
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..
Protein Sequence MNWNKGGPGTKRGFGFGGFAISAGKKEEPKLPQQSHSAFGATSSSSGFGKSAPPQLPSFYKIGSKRANFDEENAYFEDEEEDSSNVDLPYIPAENSPTRQQFHSKPVDSDSDDDPLEAFMAEVEDQAARDMKRLEEKDKERKNVKGIRDDIEEEDDQEAYFRYMAENPTAGVVQEEEEDNLEYDSDGNPIAPTKKIIDPLPPIDHSEIDYPPFEKNFYNEHEEITNLTPQQLIDLRHKLNLRVSGAAPPRPGSSFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDGPIAVIVCPTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVVQGDIGEANEDVTQIVEILHSGPSKWNWLTRRLVEFTSSGSVLLFVTKKANAEELANNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDIDTHTHRIGRTGRAGEKGVAYTLLTPKDSNFAGDLVRNLEGANQHVSKELLDLAMQNAWFRKSRFKGGKGKKLNIGGGGLGYRERPGLGSENMDRGNNNVMSNYEAYKPSTGAMGDRLTAMKAAFQSQYKSHFVAASLSNQKAGSSAAGASGWTSAGSLNSVPTNSAQQGHNSPDSPVTSAAKGIPGFGNTGNISGAPVTYPSAGAQGVNNTASGNNSREGTGGSNGKRERYTENRGSSRHSHGETGNRHSDSPRHGDGGRHGDGYRHPESSSRHTDGHRHGENRHGGSAGRHGENRGANDGRNGESRKEAFNRESKMEPKMEPKVDSSKMDKVDSKTDKTADGFAVPEPPKRKKSRWDS
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
1Acetylation-------MNWNKGGP
-------CCCCCCCC
13.63-
5Acetylation---MNWNKGGPGTKR
---CCCCCCCCCCCC
57.7819608861
10PhosphorylationWNKGGPGTKRGFGFG
CCCCCCCCCCCCCCC
22.2422817900
12MethylationKGGPGTKRGFGFGGF
CCCCCCCCCCCCCCE
45.5724129315
22PhosphorylationGFGGFAISAGKKEEP
CCCCEEEECCCCCCC
27.7828555341
25AcetylationGFAISAGKKEEPKLP
CEEEECCCCCCCCCC
57.6425953088
26AcetylationFAISAGKKEEPKLPQ
EEEECCCCCCCCCCC
67.4126051181
30AcetylationAGKKEEPKLPQQSHS
CCCCCCCCCCCCCCC
75.8830583609
30UbiquitinationAGKKEEPKLPQQSHS
CCCCCCCCCCCCCCC
75.8829967540
37PhosphorylationKLPQQSHSAFGATSS
CCCCCCCCCCCCCCC
30.4628555341
42PhosphorylationSHSAFGATSSSSGFG
CCCCCCCCCCCCCCC
29.5328555341
43O-linked_GlycosylationHSAFGATSSSSGFGK
CCCCCCCCCCCCCCC
27.9130059200
43PhosphorylationHSAFGATSSSSGFGK
CCCCCCCCCCCCCCC
27.9128555341
44PhosphorylationSAFGATSSSSGFGKS
CCCCCCCCCCCCCCC
24.9425627689
45PhosphorylationAFGATSSSSGFGKSA
CCCCCCCCCCCCCCC
33.9625627689
46PhosphorylationFGATSSSSGFGKSAP
CCCCCCCCCCCCCCC
39.8428555341
50AcetylationSSSSGFGKSAPPQLP
CCCCCCCCCCCCCCC
40.9826051181
50MethylationSSSSGFGKSAPPQLP
CCCCCCCCCCCCCCC
40.98-
51PhosphorylationSSSGFGKSAPPQLPS
CCCCCCCCCCCCCCC
46.5223186163
58PhosphorylationSAPPQLPSFYKIGSK
CCCCCCCCCEEECCC
50.2123917254
60PhosphorylationPPQLPSFYKIGSKRA
CCCCCCCEEECCCCC
13.1627080861
75PhosphorylationNFDEENAYFEDEEED
CCCHHHCCCCCCCCC
21.0530576142
83PhosphorylationFEDEEEDSSNVDLPY
CCCCCCCCCCCCCCC
27.3930266825
84PhosphorylationEDEEEDSSNVDLPYI
CCCCCCCCCCCCCCC
53.8730266825
90PhosphorylationSSNVDLPYIPAENSP
CCCCCCCCCCCCCCC
27.1730266825
96PhosphorylationPYIPAENSPTRQQFH
CCCCCCCCCCCHHHC
21.1025159151
98PhosphorylationIPAENSPTRQQFHSK
CCCCCCCCCHHHCCC
40.7130266825
104PhosphorylationPTRQQFHSKPVDSDS
CCCHHHCCCCCCCCC
39.6921955146
109PhosphorylationFHSKPVDSDSDDDPL
HCCCCCCCCCCCCHH
38.9725159151
111PhosphorylationSKPVDSDSDDDPLEA
CCCCCCCCCCCHHHH
47.0625159151
145AcetylationDKERKNVKGIRDDIE
HHHHHCCCCCCCCCC
59.0023236377
160PhosphorylationEEDDQEAYFRYMAEN
CCCCHHHHHHHHHHC
6.4522817900
163PhosphorylationDQEAYFRYMAENPTA
CHHHHHHHHHHCCCC
7.2623927012
169PhosphorylationRYMAENPTAGVVQEE
HHHHHCCCCCCCCCH
47.8530266825
183PhosphorylationEEEDNLEYDSDGNPI
HHCCCCCCCCCCCCC
24.7429255136
185PhosphorylationEDNLEYDSDGNPIAP
CCCCCCCCCCCCCCC
46.6629255136
193PhosphorylationDGNPIAPTKKIIDPL
CCCCCCCCCCCCCCC
35.6330266825
195UbiquitinationNPIAPTKKIIDPLPP
CCCCCCCCCCCCCCC
47.5829967540
206PhosphorylationPLPPIDHSEIDYPPF
CCCCCCHHHCCCCCC
32.2824247654
210PhosphorylationIDHSEIDYPPFEKNF
CCHHHCCCCCCCCCC
20.6120873877
215UbiquitinationIDYPPFEKNFYNEHE
CCCCCCCCCCCCCCH
53.3829967540
225PhosphorylationYNEHEEITNLTPQQL
CCCCHHHHCCCHHHH
27.7027732954
228PhosphorylationHEEITNLTPQQLIDL
CHHHHCCCHHHHHHH
22.5625159151
270SumoylationQLMHQIRKSEYTQPT
HHHHHHHHCCCCCCC
49.63-
270AcetylationQLMHQIRKSEYTQPT
HHHHHHHHCCCCCCC
49.6326051181
270MalonylationQLMHQIRKSEYTQPT
HHHHHHHHCCCCCCC
49.6326320211
270SumoylationQLMHQIRKSEYTQPT
HHHHHHHHCCCCCCC
49.63-
270UbiquitinationQLMHQIRKSEYTQPT
HHHHHHHHCCCCCCC
49.6329967540
271PhosphorylationLMHQIRKSEYTQPTP
HHHHHHHCCCCCCCC
26.4528152594
273PhosphorylationHQIRKSEYTQPTPIQ
HHHHHCCCCCCCCCE
20.1228152594
274PhosphorylationQIRKSEYTQPTPIQC
HHHHCCCCCCCCCEE
24.8328152594
277PhosphorylationKSEYTQPTPIQCQGV
HCCCCCCCCCEECCE
24.1728152594
2982-HydroxyisobutyrylationRDMIGIAKTGSGKTA
CCEEEEEECCCCHHH
52.04-
298AcetylationRDMIGIAKTGSGKTA
CCEEEEEECCCCHHH
52.0425953088
298UbiquitinationRDMIGIAKTGSGKTA
CCEEEEEECCCCHHH
52.04-
341UbiquitinationPTRELCQQIHAECKR
CHHHHHHHHHHHHHH
28.5624816145
347AcetylationQQIHAECKRFGKAYN
HHHHHHHHHHCHHCC
42.1225953088
351AcetylationAECKRFGKAYNLRSV
HHHHHHCHHCCCCEE
45.0126051181
383PhosphorylationGAEIVVCTPGRLIDH
CCEEEEECCCHHHHH
19.7127690223
3922-HydroxyisobutyrylationGRLIDHVKKKATNLQ
CHHHHHHHHHCCCCC
45.17-
422UbiquitinationMGFEYQVRSIASHVR
CCCHHHHHHHHHHCC
13.5624816145
442UbiquitinationLLFSATFRKKIEKLA
EEEEHHHHHHHHHHH
34.7024816145
519AcetylationEELANNLKQEGHNLG
HHHHHHHHHHCCCHH
48.7226051181
523UbiquitinationNNLKQEGHNLGLLHG
HHHHHHCCCHHCCCC
26.1124816145
5452-HydroxyisobutyrylationNKVISDFKKKDIPVL
HHHHHHHHHCCCCEE
65.00-
545AcetylationNKVISDFKKKDIPVL
HHHHHHHHHCCCCEE
65.0025953088
555PhosphorylationDIPVLVATDVAARGL
CCCEEEEECHHHCCC
24.4321406692
566PhosphorylationARGLDIPSIKTVINY
HCCCCCCCCCEEEEH
36.7324719451
581PhosphorylationDVARDIDTHTHRIGR
HHHCCCCCCCCCCCC
29.0720068231
583PhosphorylationARDIDTHTHRIGRTG
HCCCCCCCCCCCCCC
18.2320068231
599PhosphorylationAGEKGVAYTLLTPKD
CCCCCEEEEEECCCC
8.7728152594
600PhosphorylationGEKGVAYTLLTPKDS
CCCCEEEEEECCCCC
12.9328152594
603PhosphorylationGVAYTLLTPKDSNFA
CEEEEEECCCCCCCC
31.2528857561
605UbiquitinationAYTLLTPKDSNFAGD
EEEEECCCCCCCCHH
69.4324816145
626AcetylationGANQHVSKELLDLAM
HHHHHHCHHHHHHHH
51.827713437
668PhosphorylationRERPGLGSENMDRGN
CCCCCCCCCCCCCCC
30.7320873877
671SulfoxidationPGLGSENMDRGNNNV
CCCCCCCCCCCCCCC
3.0521406390
673MethylationLGSENMDRGNNNVMS
CCCCCCCCCCCCCCC
38.68-
680PhosphorylationRGNNNVMSNYEAYKP
CCCCCCCCCCEECCC
31.7922210691
682PhosphorylationNNNVMSNYEAYKPST
CCCCCCCCEECCCCC
8.4721945579
685PhosphorylationVMSNYEAYKPSTGAM
CCCCCEECCCCCCCC
16.1122210691
686AcetylationMSNYEAYKPSTGAMG
CCCCEECCCCCCCCH
39.2723954790
686UbiquitinationMSNYEAYKPSTGAMG
CCCCEECCCCCCCCH
39.2724816145
688PhosphorylationNYEAYKPSTGAMGDR
CCEECCCCCCCCHHH
35.0121945579
689PhosphorylationYEAYKPSTGAMGDRL
CEECCCCCCCCHHHH
37.1721945579
700AcetylationGDRLTAMKAAFQSQY
HHHHHHHHHHHHHHH
33.8125953088
700MethylationGDRLTAMKAAFQSQY
HHHHHHHHHHHHHHH
33.81-
700UbiquitinationGDRLTAMKAAFQSQY
HHHHHHHHHHHHHHH
33.8132015554
705PhosphorylationAMKAAFQSQYKSHFV
HHHHHHHHHHHHHHH
29.0825159151
707PhosphorylationKAAFQSQYKSHFVAA
HHHHHHHHHHHHHHH
21.50-
708MethylationAAFQSQYKSHFVAAS
HHHHHHHHHHHHHHH
29.8024129315
715O-linked_GlycosylationKSHFVAASLSNQKAG
HHHHHHHHHCCCCCC
23.6930059200
715PhosphorylationKSHFVAASLSNQKAG
HHHHHHHHHCCCCCC
23.6928450419
717PhosphorylationHFVAASLSNQKAGSS
HHHHHHHCCCCCCCC
34.4228450419
723PhosphorylationLSNQKAGSSAAGASG
HCCCCCCCCCCCCCC
22.9723927012
724PhosphorylationSNQKAGSSAAGASGW
CCCCCCCCCCCCCCC
22.6323927012
729PhosphorylationGSSAAGASGWTSAGS
CCCCCCCCCCCCCCC
33.6723927012
732PhosphorylationAAGASGWTSAGSLNS
CCCCCCCCCCCCCCC
16.5423927012
733PhosphorylationAGASGWTSAGSLNSV
CCCCCCCCCCCCCCC
24.9123927012
736PhosphorylationSGWTSAGSLNSVPTN
CCCCCCCCCCCCCCC
24.8823927012
739PhosphorylationTSAGSLNSVPTNSAQ
CCCCCCCCCCCCCCC
34.4623927012
742PhosphorylationGSLNSVPTNSAQQGH
CCCCCCCCCCCCCCC
39.3823401153
744PhosphorylationLNSVPTNSAQQGHNS
CCCCCCCCCCCCCCC
29.9030278072
751PhosphorylationSAQQGHNSPDSPVTS
CCCCCCCCCCCCCCH
25.1425159151
754PhosphorylationQGHNSPDSPVTSAAK
CCCCCCCCCCCHHHC
25.3425159151
757PhosphorylationNSPDSPVTSAAKGIP
CCCCCCCCHHHCCCC
18.9430278072
758PhosphorylationSPDSPVTSAAKGIPG
CCCCCCCHHHCCCCC
26.8530278072
773PhosphorylationFGNTGNISGAPVTYP
CCCCCCCCCCCCCCC
32.6628555341
792PhosphorylationQGVNNTASGNNSREG
CCCCCCCCCCCCCCC
39.7628555341
806AcetylationGTGGSNGKRERYTEN
CCCCCCCCHHCCCCC
56.1715615005
810PhosphorylationSNGKRERYTENRGSS
CCCCHHCCCCCCCCC
17.4121888424
814MethylationRERYTENRGSSRHSH
HHCCCCCCCCCCCCC
39.89-
817PhosphorylationYTENRGSSRHSHGET
CCCCCCCCCCCCCCC
36.5221888424
820PhosphorylationNRGSSRHSHGETGNR
CCCCCCCCCCCCCCC
31.88-
829PhosphorylationGETGNRHSDSPRHGD
CCCCCCCCCCCCCCC
36.2226699800
831PhosphorylationTGNRHSDSPRHGDGG
CCCCCCCCCCCCCCC
27.1830576142
844PhosphorylationGGRHGDGYRHPESSS
CCCCCCCCCCCCCCC
15.53-
850PhosphorylationGYRHPESSSRHTDGH
CCCCCCCCCCCCCCC
29.7230576142
851PhosphorylationYRHPESSSRHTDGHR
CCCCCCCCCCCCCCC
37.0430576142
875MethylationAGRHGENRGANDGRN
CCCCCCCCCCCCCCC
41.10-
894PhosphorylationKEAFNRESKMEPKME
HHHHHHHHCCCCCCC
33.7823917254
899SumoylationRESKMEPKMEPKVDS
HHHCCCCCCCCCCCH
42.46-
899SumoylationRESKMEPKMEPKVDS
HHHCCCCCCCCCCCH
42.4628112733
906PhosphorylationKMEPKVDSSKMDKVD
CCCCCCCHHHHCCCC
34.5428258704
907PhosphorylationMEPKVDSSKMDKVDS
CCCCCCHHHHCCCCC
27.7728258704
914PhosphorylationSKMDKVDSKTDKTAD
HHHCCCCCCCCCCCC
40.20-
918AcetylationKVDSKTDKTADGFAV
CCCCCCCCCCCCCCC
51.3426051181
938AcetylationRKKSRWDS-------
CCCCCCCC-------
34.8519608861
938PhosphorylationRKKSRWDS-------
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_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DDX42_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 DDX42_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
TCRG1_HUMANTCERG1physical
22939629
HNRPQ_HUMANSYNCRIPphysical
22939629
KS6A4_HUMANRPS6KA4physical
22939629
RL36_HUMANRPL36physical
22939629
PIN4_HUMANPIN4physical
22939629
PHF20_HUMANPHF20physical
22939629
KALM_HUMANKAL1physical
22939629
NOSIP_HUMANNOSIPphysical
22939629
SYEP_HUMANEPRSphysical
22939629
FOXJ3_HUMANFOXJ3physical
22939629
RU1C_HUMANSNRPCphysical
22365833
SF3A1_HUMANSF3A1physical
22365833
SF3B4_HUMANSF3B4physical
22365833
DHX15_HUMANDHX15physical
22365833
SR140_HUMANU2SURPphysical
22365833
PRP19_HUMANPRPF19physical
22365833

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 DDX42_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 MET-1 AND LYS-5, AND MASSSPECTROMETRY.
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-109 AND SER-111, ANDMASS SPECTROMETRY.
"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-185; SER-751 ANDSER-754, 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-104; SER-109; SER-111;SER-185 AND SER-754, 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 THR-10; SER-96; SER-109 ANDSER-111, AND MASS SPECTROMETRY.

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