CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022220
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 ATP-dependent RNA helicase DDX18 
Protein Synonyms/Alias
 DEAD box protein 18; Myc-regulated DEAD box protein; MrDb 
Gene Name
 DDX18 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
7*MSHLPMKLLRKKIEacetylation[1, 2, 3, 4]
195ENTLKAIKEMGFTNMubiquitination[5, 6, 7]
208NMTEIQHKSIRPLLEubiquitination[6]
224RDLLAAAKTGSGKTLubiquitination[4, 6, 8, 9]
297NRSAEAQKLGNGINIubiquitination[4, 6, 8]
370FSATQTRKVEDLARIubiquitination[6]
458PVLAIHGKQKQNKRTacetylation[1]
545LRYLKQSKVPLSEFDacetylation[3]
545LRYLKQSKVPLSEFDubiquitination[6]
557EFDFSWSKISDIQSQubiquitination[8, 10]
571QLEKLIEKNYFLHKSacetylation[1]
571QLEKLIEKNYFLHKSubiquitination[5, 7]
Reference
 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [3] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [4] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [5] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [6] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [7] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [8] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [9] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [10] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094
Functional Description
 Probable RNA-dependent helicase. 
Sequence Annotation
 DOMAIN 210 385 Helicase ATP-binding.
 DOMAIN 399 569 Helicase C-terminal.
 NP_BIND 223 230 ATP (Probable).
 MOTIF 179 207 Q motif.
 MOTIF 333 336 DEAD box.  
Keyword
 3D-structure; ATP-binding; Complete proteome; Direct protein sequencing; Helicase; Hydrolase; Nucleotide-binding; Nucleus; Polymorphism; Reference proteome; RNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 670 AA 
Protein Sequence
MSHLPMKLLR KKIEKRNLKL RQRNLKFQGA SNLTLSETQN GDVSEETMGS RKVKKSKQKP 60
MNVGLSETQN GGMSQEAVGN IKVTKSPQKS TVLTNGEAAM QSSNSESKKK KKKKRKMVND 120
AEPDTKKAKT ENKGKSEEES AETTKETENN VEKPDNDEDE SEVPSLPLGL TGAFEDTSFA 180
SLCNLVNENT LKAIKEMGFT NMTEIQHKSI RPLLEGRDLL AAAKTGSGKT LAFLIPAVEL 240
IVKLRFMPRN GTGVLILSPT RELAMQTFGV LKELMTHHVH TYGLIMGGSN RSAEAQKLGN 300
GINIIVATPG RLLDHMQNTP GFMYKNLQCL VIDEADRILD VGFEEELKQI IKLLPTRRQT 360
MLFSATQTRK VEDLARISLK KEPLYVGVDD DKANATVDGL EQGYVVCPSE KRFLLLFTFL 420
KKNRKKKLMV FFSSCMSVKY HYELLNYIDL PVLAIHGKQK QNKRTTTFFQ FCNADSGTLL 480
CTDVAARGLD IPEVDWIVQY DPPDDPKEYI HRVGRTARGL NGRGHALLIL RPEELGFLRY 540
LKQSKVPLSE FDFSWSKISD IQSQLEKLIE KNYFLHKSAQ EAYKSYIRAY DSHSLKQIFN 600
VNNLNLPQVA LSFGFKVPPF VDLNVNSNEG KQKKRGGGGG FGYQKTKKVE KSKIFKHISK 660
KSSDSRQFSH 670 
Gene Ontology
 GO:0005730; C:nucleolus; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004004; F:ATP-dependent RNA helicase activity; TAS:ProtInc.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW. 
Interpro
 IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
 IPR025313; DUF4217.
 IPR014001; Helicase_ATP-bd.
 IPR001650; Helicase_C.
 IPR027417; P-loop_NTPase.
 IPR000629; RNA-helicase_DEAD-box_CS.
 IPR014014; RNA_helicase_DEAD_Q_motif. 
Pfam
 PF00270; DEAD
 PF13959; DUF4217
 PF00271; Helicase_C 
SMART
 SM00487; DEXDc
 SM00490; HELICc 
PROSITE
 PS00039; DEAD_ATP_HELICASE
 PS51192; HELICASE_ATP_BIND_1
 PS51194; HELICASE_CTER
 PS51195; Q_MOTIF 
PRINTS