CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023692
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Probable ATP-dependent RNA helicase DDX52 
Protein Synonyms/Alias
 ATP-dependent RNA helicase ROK1-like; DEAD box protein 52 
Gene Name
 DDX52 
Gene Synonyms/Alias
 ROK1; HUSSY-19 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
15RRLGAGAKFDTRRFSacetylation[1]
53LDFFGNKKSVPGVCGubiquitination[2]
131ESKLTSGKLENLRKEubiquitination[2]
139LENLRKEKINFLRNKubiquitination[2]
228IPILMQLKQPANKGFubiquitination[2]
409AMRELVKKGFNPPVLubiquitination[2]
511GRAGNKGKAITFFTEubiquitination[2]
521TFFTEDDKPLLRSVAubiquitination[2]
543CPVPEYIKGFQKLLSubiquitination[2]
547EYIKGFQKLLSKQKKubiquitination[2]
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] 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] 
Functional Description
  
Sequence Annotation
 DOMAIN 196 374 Helicase ATP-binding.
 DOMAIN 385 546 Helicase C-terminal.
 NP_BIND 209 216 ATP.
 MOTIF 165 193 Q motif.
 MOTIF 318 321 DEAD box.
 MOD_RES 15 15 N6-acetyllysine.
 MOD_RES 39 39 Phosphoserine.  
Keyword
 3D-structure; Acetylation; ATP-binding; Complete proteome; Helicase; Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; RNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 599 AA 
Protein Sequence
MDVHDLFRRL GAGAKFDTRR FSADAARFQI GKRKYDFDSS EVLQGLDFFG NKKSVPGVCG 60
ASQTHQKPQN GEKKEESLTE RKREQSKKKR KTMTSEIASQ EEGATIQWMS SVEAKIEDKK 120
VQRESKLTSG KLENLRKEKI NFLRNKHKIH VQGTDLPDPI ATFQQLDQEY KINSRLLQNI 180
LDAGFQMPTP IQMQAIPVML HGRELLASAP TGSGKTLAFS IPILMQLKQP ANKGFRALII 240
SPTRELASQI HRELIKISEG TGFRIHMIHK AAVAAKKFGP KSSKKFDILV TTPNRLIYLL 300
KQDPPGIDLA SVEWLVVDES DKLFEDGKTG FRDQLASIFL ACTSHKVRRA MFSATFAYDV 360
EQWCKLNLDN VISVSIGARN SAVETVEQEL LFVGSETGKL LAMRELVKKG FNPPVLVFVQ 420
SIERAKELFH ELIYEGINVD VIHAERTQQQ RDNTVHSFRA GKIWVLICTA LLARGIDFKG 480
VNLVINYDFP TSSVEYIHRI GRTGRAGNKG KAITFFTEDD KPLLRSVANV IQQAGCPVPE 540
YIKGFQKLLS KQKKKMIKKP LERESISTTP KCFLEKAKDK QKKVTGQNSK KKVALEDKS 599 
Gene Ontology
 GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW. 
Interpro
 IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
 IPR014001; Helicase_ATP-bd.
 IPR001650; Helicase_C.
 IPR027417; P-loop_NTPase.
 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