DDX18_HUMAN - dbPTM
DDX18_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DDX18_HUMAN
UniProt AC Q9NVP1
Protein Name ATP-dependent RNA helicase DDX18
Gene Name DDX18
Organism Homo sapiens (Human).
Sequence Length 670
Subcellular Localization Nucleus, nucleolus . Chromosome .
Protein Description Probable RNA-dependent helicase..
Protein Sequence MSHLPMKLLRKKIEKRNLKLRQRNLKFQGASNLTLSETQNGDVSEETMGSRKVKKSKQKPMNVGLSETQNGGMSQEAVGNIKVTKSPQKSTVLTNGEAAMQSSNSESKKKKKKKRKMVNDAEPDTKKAKTENKGKSEEESAETTKETENNVEKPDNDEDESEVPSLPLGLTGAFEDTSFASLCNLVNENTLKAIKEMGFTNMTEIQHKSIRPLLEGRDLLAAAKTGSGKTLAFLIPAVELIVKLRFMPRNGTGVLILSPTRELAMQTFGVLKELMTHHVHTYGLIMGGSNRSAEAQKLGNGINIIVATPGRLLDHMQNTPGFMYKNLQCLVIDEADRILDVGFEEELKQIIKLLPTRRQTMLFSATQTRKVEDLARISLKKEPLYVGVDDDKANATVDGLEQGYVVCPSEKRFLLLFTFLKKNRKKKLMVFFSSCMSVKYHYELLNYIDLPVLAIHGKQKQNKRTTTFFQFCNADSGTLLCTDVAARGLDIPEVDWIVQYDPPDDPKEYIHRVGRTARGLNGRGHALLILRPEELGFLRYLKQSKVPLSEFDFSWSKISDIQSQLEKLIEKNYFLHKSAQEAYKSYIRAYDSHSLKQIFNVNNLNLPQVALSFGFKVPPFVDLNVNSNEGKQKKRGGGGGFGYQKTKKVEKSKIFKHISKKSSDSRQFSH
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
2Phosphorylation------MSHLPMKLL
------CCCCCHHHH
33.4620068231
7Acetylation-MSHLPMKLLRKKIE
-CCCCCHHHHHHHHH
42.2923749302
26AcetylationKLRQRNLKFQGASNL
HHHHHHCCCCCCCCC
38.9126051181
31PhosphorylationNLKFQGASNLTLSET
HCCCCCCCCCEEEEC
38.9226074081
34PhosphorylationFQGASNLTLSETQNG
CCCCCCCEEEECCCC
32.2726074081
36PhosphorylationGASNLTLSETQNGDV
CCCCCEEEECCCCCC
33.1026074081
38PhosphorylationSNLTLSETQNGDVSE
CCCEEEECCCCCCCH
24.7726074081
44PhosphorylationETQNGDVSEETMGSR
ECCCCCCCHHHHCCH
34.1628985074
47PhosphorylationNGDVSEETMGSRKVK
CCCCCHHHHCCHHHC
23.8425159151
50PhosphorylationVSEETMGSRKVKKSK
CCHHHHCCHHHCCCC
20.3621712546
57AcetylationSRKVKKSKQKPMNVG
CHHHCCCCCCCCCCC
71.827712417
59AcetylationKVKKSKQKPMNVGLS
HHCCCCCCCCCCCCC
50.3926051181
66PhosphorylationKPMNVGLSETQNGGM
CCCCCCCCCCCCCCC
32.4426074081
68PhosphorylationMNVGLSETQNGGMSQ
CCCCCCCCCCCCCCH
24.7726074081
74PhosphorylationETQNGGMSQEAVGNI
CCCCCCCCHHHCCCE
28.3025159151
82AcetylationQEAVGNIKVTKSPQK
HHHCCCEEECCCCCC
48.1019822401
84PhosphorylationAVGNIKVTKSPQKST
HCCCEEECCCCCCCE
22.3226074081
86PhosphorylationGNIKVTKSPQKSTVL
CCEEECCCCCCCEEE
24.1730266825
90PhosphorylationVTKSPQKSTVLTNGE
ECCCCCCCEEEECHH
20.6426074081
91PhosphorylationTKSPQKSTVLTNGEA
CCCCCCCEEEECHHH
26.9428464451
94PhosphorylationPQKSTVLTNGEAAMQ
CCCCEEEECHHHHHH
36.5226074081
102PhosphorylationNGEAAMQSSNSESKK
CHHHHHHCCCCHHHH
20.5729978859
103PhosphorylationGEAAMQSSNSESKKK
HHHHHHCCCCHHHHH
27.7322199227
105PhosphorylationAAMQSSNSESKKKKK
HHHHCCCCHHHHHHH
45.2422199227
107PhosphorylationMQSSNSESKKKKKKK
HHCCCCHHHHHHHHH
49.9822199227
125PhosphorylationVNDAEPDTKKAKTEN
CCCCCCCHHHHHCCC
45.2022210691
126AcetylationNDAEPDTKKAKTENK
CCCCCCHHHHHCCCC
59.1025953088
130PhosphorylationPDTKKAKTENKGKSE
CCHHHHHCCCCCCCH
50.0430576142
135SumoylationAKTENKGKSEEESAE
HHCCCCCCCHHHHHH
57.19-
135SumoylationAKTENKGKSEEESAE
HHCCCCCCCHHHHHH
57.19-
135AcetylationAKTENKGKSEEESAE
HHCCCCCCCHHHHHH
57.1926051181
136PhosphorylationKTENKGKSEEESAET
HCCCCCCCHHHHHHH
59.9325849741
140PhosphorylationKGKSEEESAETTKET
CCCCHHHHHHHHHHH
34.3828985074
195UbiquitinationENTLKAIKEMGFTNM
HHHHHHHHHCCCCCC
46.6521890473
195AcetylationENTLKAIKEMGFTNM
HHHHHHHHHCCCCCC
46.6526051181
1952-HydroxyisobutyrylationENTLKAIKEMGFTNM
HHHHHHHHHCCCCCC
46.65-
208UbiquitinationNMTEIQHKSIRPLLE
CCCCCCCCCHHHHHC
31.07-
224AcetylationRDLLAAAKTGSGKTL
HHHHHHHHCCCCHHH
49.0125953088
224UbiquitinationRDLLAAAKTGSGKTL
HHHHHHHHCCCCHHH
49.0121890473
225PhosphorylationDLLAAAKTGSGKTLA
HHHHHHHCCCCHHHH
31.6718491316
227PhosphorylationLAAAKTGSGKTLAFL
HHHHHCCCCHHHHHH
42.2018491316
230PhosphorylationAKTGSGKTLAFLIPA
HHCCCCHHHHHHHHH
27.18-
258PhosphorylationGTGVLILSPTRELAM
CCEEEEECCCHHHHH
19.7525867546
260PhosphorylationGVLILSPTRELAMQT
EEEEECCCHHHHHHH
33.1425867546
265SulfoxidationSPTRELAMQTFGVLK
CCCHHHHHHHHHHHH
6.3621406390
289PhosphorylationYGLIMGGSNRSAEAQ
HCHHCCCCCHHHHHH
24.2823532336
297AcetylationNRSAEAQKLGNGINI
CHHHHHHHHCCCCEE
66.4625953088
297UbiquitinationNRSAEAQKLGNGINI
CHHHHHHHHCCCCEE
66.4621890473
308PhosphorylationGINIIVATPGRLLDH
CCEEEEECCHHHHHH
18.5130266825
319PhosphorylationLLDHMQNTPGFMYKN
HHHHHCCCCCHHHCC
14.1120860994
324PhosphorylationQNTPGFMYKNLQCLV
CCCCCHHHCCCEEEE
8.41-
325AcetylationNTPGFMYKNLQCLVI
CCCCHHHCCCEEEEE
39.1226051181
348UbiquitinationVGFEEELKQIIKLLP
CCCHHHHHHHHHHCC
42.61-
352AcetylationEELKQIIKLLPTRRQ
HHHHHHHHHCCCCCH
45.6725953088
360PhosphorylationLLPTRRQTMLFSATQ
HCCCCCHHCCEEECC
17.6520068231
361SulfoxidationLPTRRQTMLFSATQT
CCCCCHHCCEEECCC
2.4228183972
364PhosphorylationRRQTMLFSATQTRKV
CCHHCCEEECCCCCH
26.8420068231
366PhosphorylationQTMLFSATQTRKVED
HHCCEEECCCCCHHH
29.3120068231
368PhosphorylationMLFSATQTRKVEDLA
CCEEECCCCCHHHHH
28.2720068231
370UbiquitinationFSATQTRKVEDLARI
EEECCCCCHHHHHCC
54.05-
380SumoylationDLARISLKKEPLYVG
HHHCCCCCCCCCEEC
48.58-
381UbiquitinationLARISLKKEPLYVGV
HHCCCCCCCCCEECC
70.61-
3812-HydroxyisobutyrylationLARISLKKEPLYVGV
HHCCCCCCCCCEECC
70.61-
385PhosphorylationSLKKEPLYVGVDDDK
CCCCCCCEECCCCCC
13.0827642862
392AcetylationYVGVDDDKANATVDG
EECCCCCCCCCEECC
51.0026051181
411AcetylationYVVCPSEKRFLLLFT
EEECCCHHHHHHHHH
53.4326051181
4112-HydroxyisobutyrylationYVVCPSEKRFLLLFT
EEECCCHHHHHHHHH
53.43-
434PhosphorylationKLMVFFSSCMSVKYH
EEEEEHHCCCCHHHH
14.53-
437PhosphorylationVFFSSCMSVKYHYEL
EEHHCCCCHHHHHHH
21.5624719451
440PhosphorylationSSCMSVKYHYELLNY
HCCCCHHHHHHHHHH
13.8922817900
442PhosphorylationCMSVKYHYELLNYID
CCCHHHHHHHHHHCC
12.7522817900
447PhosphorylationYHYELLNYIDLPVLA
HHHHHHHHCCCCEEE
8.8622817900
458AcetylationPVLAIHGKQKQNKRT
CEEEEECCCCCCCCC
39.9123954790
458MalonylationPVLAIHGKQKQNKRT
CEEEEECCCCCCCCC
39.9126320211
507AcetylationYDPPDDPKEYIHRVG
CCCCCCHHHHHHHHH
70.8726051181
545UbiquitinationLRYLKQSKVPLSEFD
HHHHHHCCCCHHHCC
45.43-
545AcetylationLRYLKQSKVPLSEFD
HHHHHHCCCCHHHCC
45.4323954790
549PhosphorylationKQSKVPLSEFDFSWS
HHCCCCHHHCCCCHH
30.10-
554PhosphorylationPLSEFDFSWSKISDI
CHHHCCCCHHHHHHH
32.0828348404
557UbiquitinationEFDFSWSKISDIQSQ
HCCCCHHHHHHHHHH
39.7221890473
563PhosphorylationSKISDIQSQLEKLIE
HHHHHHHHHHHHHHH
36.7527050516
567AcetylationDIQSQLEKLIEKNYF
HHHHHHHHHHHHHCC
64.4625953088
567UbiquitinationDIQSQLEKLIEKNYF
HHHHHHHHHHHHHCC
64.46-
5712-HydroxyisobutyrylationQLEKLIEKNYFLHKS
HHHHHHHHHCCCCHH
50.37-
571UbiquitinationQLEKLIEKNYFLHKS
HHHHHHHHHCCCCHH
50.3721906983
571AcetylationQLEKLIEKNYFLHKS
HHHHHHHHHCCCCHH
50.3719608861
577UbiquitinationEKNYFLHKSAQEAYK
HHHCCCCHHHHHHHH
50.03-
577AcetylationEKNYFLHKSAQEAYK
HHHCCCCHHHHHHHH
50.0325825284
584AcetylationKSAQEAYKSYIRAYD
HHHHHHHHHHHHHHH
43.7826051181
584UbiquitinationKSAQEAYKSYIRAYD
HHHHHHHHHHHHHHH
43.78-
588MethylationEAYKSYIRAYDSHSL
HHHHHHHHHHHHCCC
20.89-
627PhosphorylationFVDLNVNSNEGKQKK
EEECCCCCCCCCCCC
31.7930266825
635MethylationNEGKQKKRGGGGGFG
CCCCCCCCCCCCCCC
56.90-
643PhosphorylationGGGGGFGYQKTKKVE
CCCCCCCHHHCCCCH
12.4620860994
645AcetylationGGGFGYQKTKKVEKS
CCCCCHHHCCCCHHH
54.5525953088

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 DDX18_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DDX18_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 DDX18_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
PRP6_HUMANPRPF6physical
22939629
REQU_HUMANDPF2physical
22939629
PR40A_HUMANPRPF40Aphysical
22939629
SRSF3_HUMANSRSF3physical
22939629
ABCF2_HUMANABCF2physical
26344197
BCCIP_HUMANBCCIPphysical
26344197
BRX1_HUMANBRIX1physical
26344197
BYST_HUMANBYSLphysical
26344197
DCA13_HUMANDCAF13physical
26344197
DDX24_HUMANDDX24physical
26344197
DDX47_HUMANDDX47physical
26344197
DDX5_HUMANDDX5physical
26344197
DDX55_HUMANDDX55physical
26344197
DDX56_HUMANDDX56physical
26344197
DHX15_HUMANDHX15physical
26344197
DKC1_HUMANDKC1physical
26344197
EBP2_HUMANEBNA1BP2physical
26344197
ESF1_HUMANESF1physical
26344197
FBRL_HUMANFBLphysical
26344197
GAR1_HUMANGAR1physical
26344197
GLYR1_HUMANGLYR1physical
26344197
GNL1_HUMANGNL1physical
26344197
GRWD1_HUMANGRWD1physical
26344197
NOG1_HUMANGTPBP4physical
26344197
HNRPR_HUMANHNRNPRphysical
26344197
MPP10_HUMANMPHOSPH10physical
26344197
NAT10_HUMANNAT10physical
26344197
NH2L1_HUMANNHP2L1physical
26344197
MK67I_HUMANNIFKphysical
26344197
NIP7_HUMANNIP7physical
26344197
NOC2L_HUMANNOC2Lphysical
26344197
NOL10_HUMANNOL10physical
26344197
NOL6_HUMANNOL6physical
26344197
NOP2_HUMANNOP2physical
26344197
NOP56_HUMANNOP56physical
26344197
NOP58_HUMANNOP58physical
26344197
NSA2_HUMANNSA2physical
26344197
RPA2_HUMANPOLR1Bphysical
26344197
RPAC1_HUMANPOLR1Cphysical
26344197
RPA49_HUMANPOLR1Ephysical
26344197
PWP1_HUMANPWP1physical
26344197
PWP2_HUMANPWP2physical
26344197
RBM28_HUMANRBM28physical
26344197
RPF2_HUMANRPF2physical
26344197
RL11_HUMANRPL11physical
26344197
RL18A_HUMANRPL18Aphysical
26344197
RL23_HUMANRPL23physical
26344197
RL27_HUMANRPL27physical
26344197
RL36_HUMANRPL36physical
26344197
RL5_HUMANRPL5physical
26344197
RL8_HUMANRPL8physical
26344197
RL9_HUMANRPL9physical
26344197
RS15A_HUMANRPS15Aphysical
26344197
RS4X_HUMANRPS4Xphysical
26344197
RS6_HUMANRPS6physical
26344197
RS7_HUMANRPS7physical
26344197
RRP15_HUMANRRP15physical
26344197
RRS1_HUMANRRS1physical
26344197
TBL3_HUMANTBL3physical
26344197
TSR1_HUMANTSR1physical
26344197
UT14A_HUMANUTP14Aphysical
26344197
UTP20_HUMANUTP20physical
26344197
WDR3_HUMANWDR3physical
26344197
WDR36_HUMANWDR36physical
26344197

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 DDX18_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-7 AND LYS-571, AND MASSSPECTROMETRY.

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