DDX18_HUMAN
ID DDX18_HUMAN Reviewed; 670 AA.
AC Q9NVP1; Q6GTZ9; Q6IAU4; Q92732; Q9BQB7;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=ATP-dependent RNA helicase DDX18;
DE EC=3.6.4.13;
DE AltName: Full=DEAD box protein 18;
DE AltName: Full=Myc-regulated DEAD box protein;
DE Short=MrDb;
GN Name=DDX18; Synonyms=cPERP-D {ECO:0000303|PubMed:20813266};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-94.
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 56-670.
RX PubMed=8861962; DOI=10.1002/j.1460-2075.1996.tb00808.x;
RA Grandori C., Mac J., Siebelt F., Ayer D.A., Eisenman R.E.;
RT "Myc-Max heterodimers activate a DEAD box gene and interact with multiple E
RT box-related sites in vivo.";
RL EMBO J. 15:4344-4357(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 61-670, AND VARIANT SER-94.
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PROTEIN SEQUENCE OF 370-376.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [6]
RP INTERACTION WITH NOL8, AND SUBCELLULAR LOCATION.
RX PubMed=16963496; DOI=10.1093/nar/gkl603;
RA Sekiguchi T., Hayano T., Yanagida M., Takahashi N., Nishimoto T.;
RT "NOP132 is required for proper nucleolus localization of DEAD-box RNA
RT helicase DDX47.";
RL Nucleic Acids Res. 34:4593-4608(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=20813266; DOI=10.1016/j.cell.2010.07.047;
RA Ohta S., Bukowski-Wills J.C., Sanchez-Pulido L., Alves Fde L., Wood L.,
RA Chen Z.A., Platani M., Fischer L., Hudson D.F., Ponting C.P., Fukagawa T.,
RA Earnshaw W.C., Rappsilber J.;
RT "The protein composition of mitotic chromosomes determined using
RT multiclassifier combinatorial proteomics.";
RL Cell 142:810-821(2010).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 149-387 IN COMPLEX WITH PHOSPHATE.
RX PubMed=20941364; DOI=10.1371/journal.pone.0012791;
RA Schutz P., Karlberg T., van den Berg S., Collins R., Lehtio L., Hogbom M.,
RA Holmberg-Schiavone L., Tempel W., Park H.W., Hammarstrom M., Moche M.,
RA Thorsell A.G., Schuler H.;
RT "Comparative structural analysis of human DEAD-box RNA helicases.";
RL PLoS ONE 5:E12791-E12791(2010).
RN [12]
RP VARIANT [LARGE SCALE ANALYSIS] ARG-41.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Probable RNA-dependent helicase.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC -!- SUBUNIT: Interacts with NOL8; the interaction is RNA-dependent.
CC {ECO:0000269|PubMed:16963496, ECO:0000269|PubMed:20941364}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:16963496}.
CC Chromosome {ECO:0000269|PubMed:20813266}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX18/HAS1
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA67295.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK001467; BAA91709.1; -; mRNA.
DR EMBL; BC001238; AAH01238.1; -; mRNA.
DR EMBL; BC003360; AAH03360.1; -; mRNA.
DR EMBL; BC024739; AAH24739.1; -; mRNA.
DR EMBL; X98743; CAA67295.1; ALT_INIT; mRNA.
DR EMBL; CR457060; CAG33341.1; -; mRNA.
DR CCDS; CCDS2120.1; -.
DR PIR; S71758; S71758.
DR RefSeq; NP_006764.3; NM_006773.3.
DR PDB; 3LY5; X-ray; 2.80 A; A/B=149-387.
DR PDBsum; 3LY5; -.
DR AlphaFoldDB; Q9NVP1; -.
DR SMR; Q9NVP1; -.
DR BioGRID; 114404; 269.
DR IntAct; Q9NVP1; 74.
DR MINT; Q9NVP1; -.
DR STRING; 9606.ENSP00000263239; -.
DR GlyGen; Q9NVP1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NVP1; -.
DR MetOSite; Q9NVP1; -.
DR PhosphoSitePlus; Q9NVP1; -.
DR SwissPalm; Q9NVP1; -.
DR BioMuta; DDX18; -.
DR DMDM; 20532388; -.
DR SWISS-2DPAGE; Q9NVP1; -.
DR EPD; Q9NVP1; -.
DR jPOST; Q9NVP1; -.
DR MassIVE; Q9NVP1; -.
DR MaxQB; Q9NVP1; -.
DR PaxDb; Q9NVP1; -.
DR PeptideAtlas; Q9NVP1; -.
DR PRIDE; Q9NVP1; -.
DR ProteomicsDB; 82837; -.
DR Antibodypedia; 33358; 95 antibodies from 23 providers.
DR DNASU; 8886; -.
DR Ensembl; ENST00000263239.7; ENSP00000263239.2; ENSG00000088205.13.
DR GeneID; 8886; -.
DR KEGG; hsa:8886; -.
DR MANE-Select; ENST00000263239.7; ENSP00000263239.2; NM_006773.4; NP_006764.3.
DR UCSC; uc002tlh.2; human.
DR CTD; 8886; -.
DR DisGeNET; 8886; -.
DR GeneCards; DDX18; -.
DR HGNC; HGNC:2741; DDX18.
DR HPA; ENSG00000088205; Low tissue specificity.
DR MIM; 606355; gene.
DR neXtProt; NX_Q9NVP1; -.
DR OpenTargets; ENSG00000088205; -.
DR PharmGKB; PA27207; -.
DR VEuPathDB; HostDB:ENSG00000088205; -.
DR eggNOG; KOG0342; Eukaryota.
DR GeneTree; ENSGT00680000100037; -.
DR HOGENOM; CLU_003041_26_5_1; -.
DR InParanoid; Q9NVP1; -.
DR OMA; EYEFPAN; -.
DR OrthoDB; 973872at2759; -.
DR PhylomeDB; Q9NVP1; -.
DR TreeFam; TF300471; -.
DR PathwayCommons; Q9NVP1; -.
DR SignaLink; Q9NVP1; -.
DR BioGRID-ORCS; 8886; 771 hits in 1050 CRISPR screens.
DR ChiTaRS; DDX18; human.
DR EvolutionaryTrace; Q9NVP1; -.
DR GenomeRNAi; 8886; -.
DR Pharos; Q9NVP1; Tbio.
DR PRO; PR:Q9NVP1; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9NVP1; protein.
DR Bgee; ENSG00000088205; Expressed in oocyte and 205 other tissues.
DR ExpressionAtlas; Q9NVP1; baseline and differential.
DR Genevisible; Q9NVP1; HS.
DR GO; GO:0005694; C:chromosome; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003724; F:RNA helicase activity; TAS:ProtInc.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR CDD; cd17942; DEADc_DDX18; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR044773; DDX18/Has1_DEADc.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR025313; DUF4217.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF13959; DUF4217; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01178; DUF4217; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Chromosome; Direct protein sequencing; Helicase;
KW Hydrolase; Nucleotide-binding; Nucleus; Reference proteome; RNA-binding.
FT CHAIN 1..670
FT /note="ATP-dependent RNA helicase DDX18"
FT /id="PRO_0000055001"
FT DOMAIN 210..385
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 399..569
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 31..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 179..207
FT /note="Q motif"
FT MOTIF 333..336
FT /note="DEAD box"
FT COMPBIAS 31..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 223..230
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT VARIANT 41
FT /note="G -> R (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035841"
FT VARIANT 94
FT /note="T -> S (in dbSNP:rs1052637)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.4"
FT /id="VAR_013293"
FT VARIANT 647
FT /note="K -> R (in dbSNP:rs10179772)"
FT /id="VAR_033857"
FT CONFLICT 248
FT /note="P -> T (in Ref. 1; BAA91709)"
FT /evidence="ECO:0000305"
FT CONFLICT 382
FT /note="E -> G (in Ref. 4; CAG33341)"
FT /evidence="ECO:0000305"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:3LY5"
FT HELIX 188..196
FT /evidence="ECO:0007829|PDB:3LY5"
FT HELIX 204..215
FT /evidence="ECO:0007829|PDB:3LY5"
FT HELIX 229..243
FT /evidence="ECO:0007829|PDB:3LY5"
FT HELIX 248..250
FT /evidence="ECO:0007829|PDB:3LY5"
FT STRAND 254..257
FT /evidence="ECO:0007829|PDB:3LY5"
FT HELIX 261..274
FT /evidence="ECO:0007829|PDB:3LY5"
FT TURN 275..277
FT /evidence="ECO:0007829|PDB:3LY5"
FT STRAND 282..285
FT /evidence="ECO:0007829|PDB:3LY5"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:3LY5"
FT HELIX 291..300
FT /evidence="ECO:0007829|PDB:3LY5"
FT STRAND 303..307
FT /evidence="ECO:0007829|PDB:3LY5"
FT HELIX 309..318
FT /evidence="ECO:0007829|PDB:3LY5"
FT STRAND 329..332
FT /evidence="ECO:0007829|PDB:3LY5"
FT HELIX 335..340
FT /evidence="ECO:0007829|PDB:3LY5"
FT HELIX 344..353
FT /evidence="ECO:0007829|PDB:3LY5"
FT STRAND 356..363
FT /evidence="ECO:0007829|PDB:3LY5"
FT HELIX 369..378
FT /evidence="ECO:0007829|PDB:3LY5"
SQ SEQUENCE 670 AA; 75407 MW; 2FE653A98751F9DC CRC64;
MSHLPMKLLR KKIEKRNLKL RQRNLKFQGA SNLTLSETQN GDVSEETMGS RKVKKSKQKP
MNVGLSETQN GGMSQEAVGN IKVTKSPQKS TVLTNGEAAM QSSNSESKKK KKKKRKMVND
AEPDTKKAKT ENKGKSEEES AETTKETENN VEKPDNDEDE SEVPSLPLGL TGAFEDTSFA
SLCNLVNENT LKAIKEMGFT NMTEIQHKSI RPLLEGRDLL AAAKTGSGKT LAFLIPAVEL
IVKLRFMPRN GTGVLILSPT RELAMQTFGV LKELMTHHVH TYGLIMGGSN RSAEAQKLGN
GINIIVATPG RLLDHMQNTP GFMYKNLQCL VIDEADRILD VGFEEELKQI IKLLPTRRQT
MLFSATQTRK VEDLARISLK KEPLYVGVDD DKANATVDGL EQGYVVCPSE KRFLLLFTFL
KKNRKKKLMV FFSSCMSVKY HYELLNYIDL PVLAIHGKQK QNKRTTTFFQ FCNADSGTLL
CTDVAARGLD IPEVDWIVQY DPPDDPKEYI HRVGRTARGL NGRGHALLIL RPEELGFLRY
LKQSKVPLSE FDFSWSKISD IQSQLEKLIE KNYFLHKSAQ EAYKSYIRAY DSHSLKQIFN
VNNLNLPQVA LSFGFKVPPF VDLNVNSNEG KQKKRGGGGG FGYQKTKKVE KSKIFKHISK
KSSDSRQFSH
