CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015928
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 ATP-dependent RNA helicase DHX29 
Protein Synonyms/Alias
 DEAH box protein 29; Nucleic acid helicase DDXx 
Gene Name
 DHX29 
Gene Synonyms/Alias
 DDX29 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
93LKVVINNKLEQRIIGubiquitination[1]
230KNMEVNMKEWILRYAubiquitination[1]
275AAKLLDAKEQAATFKubiquitination[1]
380SWTGKSPKQFLIDWVubiquitination[1]
401SPNPSFEKVPVGRYWubiquitination[1]
494PRDLFIAKLLNKLKQubiquitination[1, 2, 3, 4, 5]
500AKLLNKLKQQQQQQQubiquitination[6]
564QSTPKYQKLLKERQQubiquitination[1]
828DLNPFYQKYSSRTQHubiquitination[1]
1084PVNVKIGKMLIFGAIubiquitination[1]
1178LLTLEDVKQELIKLVubiquitination[1]
1235VGKIIYTKSVDVTEKubiquitination[7]
Reference
 [1] 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]
 [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] 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]
 [4] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [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] 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] 
Functional Description
 ATP-binding RNA helicase involved in translation initiation. Part of the 43S pre-initiation complex that is required for efficient initiation on mammalian mRNAs with structured 5'-UTRs by promoting efficient NTPase-dependent 48S complex formation. Specifically binds to the 40S ribosome near the mRNA entrance. Does not possess a processive helicase activity. 
Sequence Annotation
 DOMAIN 582 755 Helicase ATP-binding.
 DOMAIN 849 1026 Helicase C-terminal.
 NP_BIND 595 602 ATP (By similarity).
 MOTIF 702 705 DEAH box.
 MOD_RES 71 71 Phosphoserine.
 MOD_RES 192 192 Phosphoserine.
 MOD_RES 200 200 Phosphoserine.  
Keyword
 ATP-binding; Coiled coil; Complete proteome; Cytoplasm; Helicase; Hydrolase; Initiation factor; Nucleotide-binding; Phosphoprotein; Polymorphism; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1369 AA 
Protein Sequence
MGGKNKKHKA PAAAVVRAAV SASRAKSAEA GIAGEAQSKK PVSRPATAAA AAAGSREPRV 60
KQGPKIYSFN STNDSSGPAN LDKSILKVVI NNKLEQRIIG VINEHKKQNN DKGMISGRLT 120
AKKLQDLYMA LQAFSFKTKD IEDAMTNTLL YGGDLHSALD WLCLNLSDDA LPEGFSQEFE 180
EQQPKSRPKF QSPQIQATIS PPLQPKTKTY EEDPKSKPKK EEKNMEVNMK EWILRYAEQQ 240
NEEEKNENSK SLEEEEKFDP NERYLHLAAK LLDAKEQAAT FKLEKNKQGQ KEAQEKIRKF 300
QREMETLEDH PVFNPAMKIS HQQNERKKPP VATEGESALN FNLFEKSAAA TEEEKDKKKE 360
PHDVRNFDYT ARSWTGKSPK QFLIDWVRKN LPKSPNPSFE KVPVGRYWKC RVRVIKSEDD 420
VLVVCPTILT EDGMQAQHLG ATLALYRLVK GQSVHQLLPP TYRDVWLEWS DAEKKREELN 480
KMETNKPRDL FIAKLLNKLK QQQQQQQQHS ENKRENSEDP EESWENLVSD EDFSALSLES 540
ANVEDLEPVR NLFRKLQSTP KYQKLLKERQ QLPVFKHRDS IVETLKRHRV VVVAGETGSG 600
KSTQVPHFLL EDLLLNEWEA SKCNIVCTQP RRISAVSLAN RVCDELGCEN GPGGRNSLCG 660
YQIRMESRAC ESTRLLYCTT GVLLRKLQED GLLSNVSHVI VDEVHERSVQ SDFLLIILKE 720
ILQKRSDLHL ILMSATVDSE KFSTYFTHCP ILRISGRSYP VEVFHLEDII EETGFVLEKD 780
SEYCQKFLEE EEEVTINVTS KAGGIKKYQE YIPVQTGAHA DLNPFYQKYS SRTQHAILYM 840
NPHKINLDLI LELLAYLDKS PQFRNIEGAV LIFLPGLAHI QQLYDLLSND RRFYSERYKV 900
IALHSILSTQ DQAAAFTLPP PGVRKIVLAT NIAETGITIP DVVFVIDTGR TKENKYHESS 960
QMSSLVETFV SKASALQRQG RAGRVRDGFC FRMYTRERFE GFMDYSVPEI LRVPLEELCL 1020
HIMKCNLGSP EDFLSKALDP PQLQVISNAM NLLRKIGACE LNEPKLTPLG QHLAALPVNV 1080
KIGKMLIFGA IFGCLDPVAT LAAVMTEKSP FTTPIGRKDE ADLAKSALAM ADSDHLTIYN 1140
AYLGWKKARQ EGGYRSEITY CRRNFLNRTS LLTLEDVKQE LIKLVKAAGF SSSTTSTSWE 1200
GNRASQTLSF QEIALLKAVL VAGLYDNVGK IIYTKSVDVT EKLACIVETA QGKAQVHPSS 1260
VNRDLQTHGW LLYQEKIRYA RVYLRETTLI TPFPVLLFGG DIEVQHRERL LSIDGWIYFQ 1320
APVKIAVIFK QLRVLIDSVL RKKLENPKMS LENDKILQII TELIKTENN 1369 
Gene Ontology
 GO:0005739; C:mitochondrion; IEA:Compara.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
 GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW. 
Interpro
 IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
 IPR002464; DNA/RNA_helicase_DEAH_CS.
 IPR011709; DUF1605.
 IPR007502; Helicase-assoc_dom.
 IPR014001; Helicase_ATP-bd.
 IPR001650; Helicase_C.
 IPR027417; P-loop_NTPase. 
Pfam
 PF00270; DEAD
 PF04408; HA2
 PF00271; Helicase_C
 PF07717; OB_NTP_bind 
SMART
 SM00487; DEXDc
 SM00847; HA2
 SM00490; HELICc 
PROSITE
 PS00690; DEAH_ATP_HELICASE
 PS51192; HELICASE_ATP_BIND_1
 PS51194; HELICASE_CTER 
PRINTS