CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018842
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Probable ATP-dependent RNA helicase DDX17 
Protein Synonyms/Alias
 DEAD box protein 17; DEAD box protein p72; RNA-dependent helicase p72 
Gene Name
 DDX17 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
108GGGGLPPKKFGNPGEacetylation[1]
109GGGLPPKKFGNPGERacetylation[1]
121GERLRKKKWDLSELPacetylation[1]
121GERLRKKKWDLSELPubiquitination[2]
129WDLSELPKFEKNFYVacetylation[3]
129WDLSELPKFEKNFYVsumoylation[4]
129WDLSELPKFEKNFYVubiquitination[2]
132SELPKFEKNFYVEHPubiquitination[2]
274YGKCSRLKSTCIYGGubiquitination[5]
284CIYGGAPKGPQIRDLubiquitination[5]
515RTARSTNKGTAYTFFubiquitination[2]
528FFTPGNLKQARELIKubiquitination[2]
547ANQAINPKLMQLVDHubiquitination[2]
Reference
 [1] Pleiotropic effects of p300-mediated acetylation on p68 and p72 RNA helicase.
 Mooney SM, Goel A, D'Assoro AB, Salisbury JL, Janknecht R.
 J Biol Chem. 2010 Oct 1;285(40):30443-52. [PMID: 20663877]
 [2] 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]
 [3] 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]
 [4] Sumoylation of p68 and p72 RNA helicases affects protein stability and transactivation potential.
 Mooney SM, Grande JP, Salisbury JL, Janknecht R.
 Biochemistry. 2010 Jan 12;49(1):1-10. [PMID: 19995069]
 [5] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572] 
Functional Description
 RNA-dependent ATPase activity. Involved in transcriptional regulation. Transcriptional coactivator for estrogen receptor ESR1. Increases ESR1 AF-1 domain-mediated transactivation. Synergizes with DDX5 and SRA1 RNA to activate MYOD1 transcriptional activity and probably involved in skeletal muscle differentiation. Required for zinc-finger antiviral protein ZC3HAV1-mediated mRNA degradation. 
Sequence Annotation
 DOMAIN 202 377 Helicase ATP-binding.
 DOMAIN 405 552 Helicase C-terminal.
 NP_BIND 215 222 ATP (By similarity).
 REGION 547 729 Transactivation domain.
 MOTIF 171 199 Q motif.
 MOTIF 325 328 DEAD box.
 MOD_RES 64 64 Phosphoserine.
 MOD_RES 523 523 Phosphothreonine.
 CROSSLNK 129 129 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 Alternative initiation; Alternative splicing; ATP-binding; Complete proteome; Helicase; Hydrolase; Isopeptide bond; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; RNA-binding; Transcription; Transcription regulation; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 729 AA 
Protein Sequence
MPTGFVAPIL CVLLPSPTRE AATVASATGD SASERESAAP AAAPTAEAPP PSVVTRPEPQ 60
ALPSPAIRAP LPDLYPFGTM RGGGFGDRDR DRDRGGFGAR GGGGLPPKKF GNPGERLRKK 120
KWDLSELPKF EKNFYVEHPE VARLTPYEVD ELRRKKEITV RGGDVCPKPV FAFHHANFPQ 180
YVMDVLMDQH FTEPTPIQCQ GFPLALSGRD MVGIAQTGSG KTLAYLLPAI VHINHQPYLE 240
RGDGPICLVL APTRELAQQV QQVADDYGKC SRLKSTCIYG GAPKGPQIRD LERGVEICIA 300
TPGRLIDFLE SGKTNLRRCT YLVLDEADRM LDMGFEPQIR KIVDQIRPDR QTLMWSATWP 360
KEVRQLAEDF LRDYTQINVG NLELSANHNI LQIVDVCMES EKDHKLIQLM EEIMAEKENK 420
TIIFVETKRR CDDLTRRMRR DGWPAMCIHG DKSQPERDWV LNEFRSGKAP ILIATDVASR 480
GLDVEDVKFV INYDYPNSSE DYVHRIGRTA RSTNKGTAYT FFTPGNLKQA RELIKVLEEA 540
NQAINPKLMQ LVDHRGGGGG GGGRSRYRTT SSANNPNLMY QDECDRRLRG VKDGGRRDSA 600
SYRDRSETDR AGYANGSGYG SPNSAFGAQA GQYTYGQGTY GAAAYGTSSY TAQEYGAGTY 660
GASSTTSTGR SSQSSSQQFS GIGRSGQQPQ PLMSQQFAQP PGATNMIGYM GQTAYQYPPP 720
PPPPPPSRK 729 
Gene Ontology
 GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
 GO:0030331; F:estrogen receptor binding; IDA:UniProtKB.
 GO:0003723; F:RNA binding; TAS:ProtInc.
 GO:0003724; F:RNA helicase activity; TAS:ProtInc.
 GO:0008186; F:RNA-dependent ATPase activity; TAS:ProtInc.
 GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
 GO:0033148; P:positive regulation of intracellular estrogen receptor signaling pathway; IDA:UniProtKB.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
 GO:2001014; P:regulation of skeletal muscle cell differentiation; IMP:UniProtKB.
 GO:0006396; P:RNA processing; TAS:ProtInc.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
 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
 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