CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021757
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Nucleolar RNA helicase 2 
Protein Synonyms/Alias
 DEAD box protein 21; Gu-alpha; Nucleolar RNA helicase Gu; Nucleolar RNA helicase II; RH II/Gu 
Gene Name
 Ddx21 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
10GKLRSGAKLGSDGAEacetylation[1, 2]
39RKEKTKSKTEEATEGacetylation[1, 2]
217ASGDAGEKSPRLKDGacetylation[2]
222GEKSPRLKDGLSQPSubiquitination[3]
358DFSDITKKLSVACFYacetylation[4]
399KDHLQNGKLDLTKLKubiquitination[3]
459HWVFNVAKKYMKSTYubiquitination[3]
474EQVDLIGKKTQKAAIubiquitination[3]
521IIFCETKKDAQELSQubiquitination[3]
546LHGDIPQKQREITLKubiquitination[3]
627QLAQVEQKAGIKFKRubiquitination[3]
645PSATEIIKASSKDAIubiquitination[3]
730SYAWKELKEQLGESIacetylation[1]
Reference
 [1] 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]
 [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] 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
Functional Description
 Can unwind double-stranded RNA (helicase) and can fold or introduce a secondary structure to a single-stranded RNA (foldase). Functions as cofactor for JUN-activated transcription (By similarity). 
Sequence Annotation
 REPEAT 117 153 1-1.
 REPEAT 154 190 1-2.
 REPEAT 191 227 1-3.
 DOMAIN 289 468 Helicase ATP-binding.
 DOMAIN 501 645 Helicase C-terminal.
 REPEAT 807 811 2-1.
 REPEAT 817 823 2-2.
 REPEAT 829 833 2-3.
 NP_BIND 302 309 ATP (By similarity).
 REGION 117 227 3 X 37 AA tandem repeats.
 REGION 807 833 3 X 5 AA repeats.
 MOTIF 258 286 Q motif.
 MOTIF 411 414 DEVD box.
 MOD_RES 13 13 Phosphoserine (By similarity).
 MOD_RES 118 118 Phosphoserine.
 MOD_RES 144 144 Phosphoserine.
 MOD_RES 155 155 Phosphoserine.
 MOD_RES 192 192 Phosphoserine.
 MOD_RES 236 236 Phosphoserine.
 MOD_RES 244 244 Phosphoserine.
 MOD_RES 245 245 Phosphoserine.
 MOD_RES 247 247 Phosphothreonine.
 MOD_RES 261 261 Phosphoserine.
 MOD_RES 368 368 Phosphothreonine (By similarity).
 MOD_RES 639 639 Phosphoserine (By similarity).
 MOD_RES 847 847 N6-acetyllysine (By similarity).  
Keyword
 Acetylation; ATP-binding; Complete proteome; Helicase; Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat; RNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 851 AA 
Protein Sequence
MPGKLRSGAK LGSDGAEESM ETLPKPSEKK TRKEKTKSKT EEATEGMEEA VSSKAKKTNK 60
KGPSEDDVDP PKSRKAKKQE EEPQDDTAST SKTSKKKKEP LEKQADSETK EIITEEPSEE 120
EADMPKPKKM KKGKEANGDA GEKSPKLKNG LSQPSEEEAD IPKPKKMKKG KEANGDAGEK 180
SPKLKNGLSQ PSEEEVDIPK PKKMKKGKEA SGDAGEKSPR LKDGLSQPSE PKSNSSDAPG 240
EESSSETEKE IPVEQKEGAF SNFPISEETV KLLKARGVNF LFPIQAKTFH HVYSGKDLIA 300
QARTGTGKTF SFAIPLIEKL QGGLQERKRG RAPQVLVLAP TRELANQVSK DFSDITKKLS 360
VACFYGGTPY GGQIERMRSG IDILVGTPGR IKDHLQNGKL DLTKLKHVVL DEVDQMLDMG 420
FADQVEEILC VAYKKDSEDN PQTLLFSATC PHWVFNVAKK YMKSTYEQVD LIGKKTQKAA 480
ITVEHLAIKC HWTERAAVIG DVIRVYSGHQ GRTIIFCETK KDAQELSQNT CIKQDAQSLH 540
GDIPQKQREI TLKGFRNGNF GVLVATNVAA RGLDIPEVDL VVQSCPPKDV ESYIHRSGRT 600
GRAGRTGVCI CFYQNKEEYQ LAQVEQKAGI KFKRIGVPSA TEIIKASSKD AIRLLDSVPP 660
TAISHFKQSA EKLIEEKGAV EALAAALAHI SGATSVDQRS LINSQAGFVT MILRCSIEMP 720
NISYAWKELK EQLGESIDAK VKGMVFLKGK LGVCFDVRTE AVTEIQEKWH DSRRWQLTVA 780
TEQPELEGPP DGYRGRMGQR DGSRGAFRGQ RGGSRNFRGQ GQRGGSRNFR GQRPGGGNRG 840
QKRSFSKAFG Q 851 
Gene Ontology
 GO:0005730; C:nucleolus; ISS: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; IDA:MGI.
 GO:0003724; F:RNA helicase activity; ISS:MGI.
 GO:0043330; P:response to exogenous dsRNA; IMP:MGI.
 GO:0009615; P:response to virus; IMP:MGI. 
Interpro
 IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
 IPR012562; GUCT.
 IPR014001; Helicase_ATP-bd.
 IPR001650; Helicase_C.
 IPR027417; P-loop_NTPase.
 IPR014014; RNA_helicase_DEAD_Q_motif. 
Pfam
 PF00270; DEAD
 PF08152; GUCT
 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