CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021173
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 ATP-dependent RNA helicase DDX24 
Protein Synonyms/Alias
 DEAD box protein 24 
Gene Name
 DDX24 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
17PKQSSCGKFQTKGIKacetylation[1, 2]
21SCGKFQTKGIKVVGKacetylation[2]
71NPSSLFSKEAPKRKAacetylation[1]
195KADVSAWKDLFVPRPubiquitination[3, 4, 5]
290AETRSPGKAEAESDAubiquitination[6]
320IAAEARAKTGGTVSDubiquitination[6]
429VGGMSTQKQQRMLNRubiquitination[4, 7]
453GRLWELIKEKHYHLRubiquitination[4]
541KLDLLMQKIGMRGKPubiquitination[4]
601ANSISCIKRLSGLLKubiquitination[4]
624LHACMHQKQRLRNLEubiquitination[4]
655ARGLDIPKVQHVIHYubiquitination[4]
700PEDVINFKKIYKTLKubiquitination[6, 8]
720PLFPVQTKYMDVVKEubiquitination[6, 8]
726TKYMDVVKERIRLARubiquitination[4]
737RLARQIEKSEYRNFQubiquitination[4]
772EDMYKGGKADQQEERubiquitination[6]
806PLFTESQKTKYPTQSubiquitination[6]
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] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661
Functional Description
 ATP-dependent RNA helicase (Potential). 
Sequence Annotation
 DOMAIN 224 528 Helicase ATP-binding.
 DOMAIN 578 723 Helicase C-terminal.
 NP_BIND 237 244 ATP (By similarity).
 MOTIF 192 220 Q motif.
 MOTIF 471 474 DEAD box.
 MOD_RES 17 17 N6-acetyllysine.
 MOD_RES 71 71 N6-acetyllysine.
 MOD_RES 82 82 Phosphoserine.
 MOD_RES 94 94 Phosphoserine.
 MOD_RES 287 287 Phosphoserine.
 MOD_RES 295 295 Phosphoserine.
 MOD_RES 302 302 Phosphothreonine.  
Keyword
 Acetylation; ATP-binding; Complete proteome; Helicase; Hydrolase; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome; RNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 859 AA 
Protein Sequence
MKLKDTKSRP KQSSCGKFQT KGIKVVGKWK EVKIDPNMFA DGQMDDLVCF EELTDYQLVS 60
PAKNPSSLFS KEAPKRKAQA VSEEEEEEEG KSSSPKKKIK LKKSKNVATE GTSTQKEFEV 120
KDPELEAQGD DMVCDDPEAG EMTSENLVQT APKKKKNKGK KGLEPSQSTA AKVPKKAKTW 180
IPEVHDQKAD VSAWKDLFVP RPVLRALSFL GFSAPTPIQA LTLAPAIRDK LDILGAAETG 240
SGKTLAFAIP MIHAVLQWQK RNAAPPPSNT EAPPGETRTE AGAETRSPGK AEAESDALPD 300
DTVIESEALP SDIAAEARAK TGGTVSDQAL LFGDDDAGEG PSSLIREKPV PKQNENEEEN 360
LDKEQTGNLK QELDDKSATC KAYPKRPLLG LVLTPTRELA VQVKQHIDAV ARFTGIKTAI 420
LVGGMSTQKQ QRMLNRRPEI VVATPGRLWE LIKEKHYHLR NLRQLRCLVV DEADRMVEKG 480
HFAELSQLLE MLNDSQYNPK RQTLVFSATL TLVHQAPARI LHKKHTKKMD KTAKLDLLMQ 540
KIGMRGKPKV IDLTRNEATV ETLTETKIHC ETDEKDFYLY YFLMQYPGRS LVFANSISCI 600
KRLSGLLKVL DIMPLTLHAC MHQKQRLRNL EQFARLEDCV LLATDVAARG LDIPKVQHVI 660
HYQVPRTSEI YVHRSGRTAR ATNEGLSLML IGPEDVINFK KIYKTLKKDE DIPLFPVQTK 720
YMDVVKERIR LARQIEKSEY RNFQACLHNS WIEQAAAALE IELEEDMYKG GKADQQEERR 780
RQKQMKVLKK ELRHLLSQPL FTESQKTKYP TQSGKPPLLV SAPSKSESAL SCLSKQKKKK 840
TKKPKEPQPE QPQPSTSAN 859 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005730; C:nucleolus; IDA:LIFEdb.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004004; F:ATP-dependent RNA helicase activity; NAS:UniProtKB.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0016070; P:RNA metabolic process; NAS:UniProtKB. 
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