CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-038746
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 ATP-dependent RNA helicase A 
Protein Synonyms/Alias
  
Gene Name
 Dhx9 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
5***MGDIKNFLYAWCacetylation[1]
14FLYAWCGKRKMTPAYacetylation[1]
149WDRGANLKDYYSRKEacetylation[2]
149WDRGANLKDYYSRKEubiquitination[3]
194RLNQYFQKEKIQGEYubiquitination[3]
239REHGSNKKLAAQSCAubiquitination[3]
267EAYSGLTKKKEGERVacetylation[1]
267EAYSGLTKKKEGERVubiquitination[3]
700IPREEQRKVFDPVPDubiquitination[3]
860PLGRILAKLPIEPRFubiquitination[3]
1027GRNALIHKSSVNCPFacetylation[2]
1027GRNALIHKSSVNCPFphosphoglycerylation[4]
1027GRNALIHKSSVNCPFubiquitination[3]
1040PFSSQDMKYPSPFFVubiquitination[3]
1051PFFVFGEKIRTRAISubiquitination[3]
Reference
 [1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [2] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [3] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [4] Functional lysine modification by an intrinsically reactive primary glycolytic metabolite.
 Moellering RE, Cravatt BF.
 Science. 2013 Aug 2;341(6145):549-53. [PMID: 23908237
Functional Description
  
Sequence Annotation
  
Keyword
 ATP-binding; Complete proteome; Helicase; Hydrolase; Nucleotide-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1384 AA 
Protein Sequence
MGDIKNFLYA WCGKRKMTPA YEIRAVGNKN RQKFMCEVRV EGFNYAGMGN STNKKDAQSN 60
AARDFVNYLV RINEVKSEEV PAVGIVPPPP ILSDTSDSTA SAAEGLPAPM GGPLPPHLAL 120
KAEAENNSGV ESSGYGSPGP TWDRGANLKD YYSRKEEQEV QATLESEEVD LNAGLHGNWT 180
LENAKARLNQ YFQKEKIQGE YKYTQVGPDH NRSFIAEMTI YIKQLGRRIF AREHGSNKKL 240
AAQSCALSLV RQLYHLGVIE AYSGLTKKKE GERVEPYKVF LSPDLELQLQ NVVQELDLEI 300
VPPPVDPSMP VILNIGKLAH FEPSQRQNAV GVVPWSPPQS NWNPWTSSNI DEGPLAYAST 360
EQISMDLKNE LTYQMEQDHN LQSVLQEREL LPVKKFEAEI LEAISSNSVV IIRGATGCGK 420
TTQVPQYILD DFIQNDRAAE CNIVVTQPRR ISAVAVAERV AYERGEEPGK SCGYSVRFES 480
ILPRPHASIM FCTVGVLLRK LEAGIRGISH VIVDEIHERD INTDFLLVVL RDVVLAYPEV 540
RIVLMSATID TTMFCEYFFN CPIIEVYGRT FPVQEYFLED CIQMTQFIPP PKDKKKKDKE 600
DDGGEDDDAN CNLICGDEYG PETKLSMSQL NEKETPFELI EALLKYIETL NVPGAVLVFL 660
PGWNLIYTMQ KHLENNSHFG SHRYQILPLH SQIPREEQRK VFDPVPDGVT KVILSTNIAE 720
TSITINDVVY VIDSCKQKVK LFTAHNNMTN YATVWASKTN LEQRKGRAGR VRPGFCFHLC 780
SRARFDRLET HMTPEMFRTP LHEIALSIKL LRLGGIGQFL AKAIEPPPLD AVIEAEHTLR 840
ELDALDANDE LTPLGRILAK LPIEPRFGKM MIMGCIFYVG DAVCTISAAT CFPEPFISEG 900
KRLGYIHRNF AGNRFSDHVA LLSVFQAWDD ARMSGEEAEI RFCEQKRLNM ATLRMTWEAK 960
VQLKEILINS GFPEDCLLTQ VFTNTGPDNN LDVVISLLAF GVYPNVCYHK EKRKILTTEG 1020
RNALIHKSSV NCPFSSQDMK YPSPFFVFGE KIRTRAISAK GMTLVTPLQL LLFASKKVQS 1080
DGQIVFIDDW IRLQISHEAA ACITALRAAM EALVVEVSKQ PNIISQLDPV NEHMLNTIRQ 1140
ISRPSAAGIN LMIGSVRYGD GPRPPKMARY DNGSGYRRGY GGGGYGGGGY GGGYGSGGFG 1200
GGFGSGGGFG GGFNSGGGGF GSGGGGFGSG GGGFGGGGGG FSGGGGGGFG GGRGGGGGGF 1260
GGSGGFGSGG GGYGVGGGGY GGGGGGGYGG GSGGYGGGGG GYGGGEGYSI SPNSYRGNYG 1320
GGGGGYRGGS QGGYRNNFGG DYRGSSGDYR GSGGGYRGSG GFQRRGYGGG YFGQGRGGGG 1380
GGGY 1384 
Gene Ontology
 GO:0005813; C:centrosome; IEA:Compara.
 GO:0070937; C:CRD-mediated mRNA stability complex; IEA:Compara.
 GO:0005730; C:nucleolus; IDA:MGI.
 GO:0030529; C:ribonucleoprotein complex; ISO:MGI.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
 GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
 GO:0034605; P:cellular response to heat; IDA:MGI.
 GO:0007623; P:circadian rhythm; IMP:MGI.
 GO:0070934; P:CRD-mediated mRNA stabilization; IEA:Compara. 
Interpro
 IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
 IPR002464; DNA/RNA_helicase_DEAH_CS.
 IPR001159; Ds-RNA-bd.
 IPR014720; dsRNA-bd-like_dom.
 IPR011709; DUF1605.
 IPR007502; Helicase-assoc_dom.
 IPR014001; Helicase_ATP-bd.
 IPR001650; Helicase_C.
 IPR027417; P-loop_NTPase. 
Pfam
 PF00270; DEAD
 PF00035; dsrm
 PF04408; HA2
 PF00271; Helicase_C
 PF07717; OB_NTP_bind 
SMART
 SM00487; DEXDc
 SM00358; DSRM
 SM00847; HA2
 SM00490; HELICc 
PROSITE
 PS00690; DEAH_ATP_HELICASE
 PS50137; DS_RBD
 PS51192; HELICASE_ATP_BIND_1
 PS51194; HELICASE_CTER 
PRINTS