Q9NVP1 (DDX18_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP-dependent RNA helicase DDX18
EC=3.6.4.13

Alternative name(s):
DEAD box protein 18
Myc-regulated DEAD box protein
Short name=MrDb

Gene names

Name:

DDX18

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	670 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Probable RNA-dependent helicase.
Catalytic activity	ATP + H2O = ADP + phosphate.
Subunit structure	Interacts with NOL8; the interaction is RNA-dependent. Ref.6
Subcellular location	Nucleus › nucleolus Ref.6.
Sequence similarities	Belongs to the DEAD box helicase family. DDX18/HAS1 subfamily. Contains 1 helicase ATP-binding domain. Contains 1 helicase C-terminal domain.
Sequence caution	The sequence CAA67295.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Nucleotide-binding RNA-binding
Molecular function	Helicase Hydrolase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Cellular_component	nucleolus Inferred from direct assay Ref.6. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP-dependent RNA helicase activity Traceable author statement Ref.3. Source: ProtInc RNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 670

670

ATP-dependent RNA helicase DDX18

PRO_0000055001

Regions

Domain

210 – 385

176

Helicase ATP-binding

Domain

399 – 569

171

Helicase C-terminal

Nucleotide binding

223 – 230

8

ATP Probable

Motif

179 – 207

29

Q motif

Motif

333 – 336

4

DEAD box

Compositional bias

108 – 116

9

Poly-Lys

Compositional bias

636 – 642

7

Poly-Gly

Natural variations

Natural variant

41

1

G → R in a breast cancer sample; somatic mutation. Ref.10

VAR_035841

Natural variant

94

1

T → S. Ref.2 Ref.4
Corresponds to variant rs1052637 [ dbSNP | Ensembl ].

VAR_013293

Natural variant

647

1

K → R.
Corresponds to variant rs10179772 [ dbSNP | Ensembl ].

VAR_033857

Experimental info

Sequence conflict

248

1

P → T in BAA91709. Ref.1

Sequence conflict

382

1

E → G in CAG33341. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

670

Helix Strand Turn

Details...

Helix

175 – 177

3

Helix

188 – 196

9

Helix

204 – 215

12

Helix

229 – 243

15

Helix

248 – 250

3

Beta strand

254 – 257

4

Helix

261 – 274

14

Turn

275 – 277

3

Beta strand

282 – 285

4

Beta strand

287 – 289

3

Helix

291 – 300

10

Beta strand

303 – 307

5

Helix

309 – 318

10

Beta strand

329 – 332

4

Helix

335 – 340

6

Helix

344 – 353

10

Beta strand

356 – 363

8

Helix

369 – 378

10

Sequences

	Sequence		Length	Mass (Da)
	Q9NVP1 [UniParc]. Last modified May 10, 2002. Version 2. Checksum: 2FE653A98751F9DC	FASTA	670	75,407
	10 20 30 40 50 60 MSHLPMKLLR KKIEKRNLKL RQRNLKFQGA SNLTLSETQN GDVSEETMGS RKVKKSKQKP 70 80 90 100 110 120 MNVGLSETQN GGMSQEAVGN IKVTKSPQKS TVLTNGEAAM QSSNSESKKK KKKKRKMVND 130 140 150 160 170 180 AEPDTKKAKT ENKGKSEEES AETTKETENN VEKPDNDEDE SEVPSLPLGL TGAFEDTSFA 190 200 210 220 230 240 SLCNLVNENT LKAIKEMGFT NMTEIQHKSI RPLLEGRDLL AAAKTGSGKT LAFLIPAVEL 250 260 270 280 290 300 IVKLRFMPRN GTGVLILSPT RELAMQTFGV LKELMTHHVH TYGLIMGGSN RSAEAQKLGN 310 320 330 340 350 360 GINIIVATPG RLLDHMQNTP GFMYKNLQCL VIDEADRILD VGFEEELKQI IKLLPTRRQT 370 380 390 400 410 420 MLFSATQTRK VEDLARISLK KEPLYVGVDD DKANATVDGL EQGYVVCPSE KRFLLLFTFL 430 440 450 460 470 480 KKNRKKKLMV FFSSCMSVKY HYELLNYIDL PVLAIHGKQK QNKRTTTFFQ FCNADSGTLL 490 500 510 520 530 540 CTDVAARGLD IPEVDWIVQY DPPDDPKEYI HRVGRTARGL NGRGHALLIL RPEELGFLRY 550 560 570 580 590 600 LKQSKVPLSE FDFSWSKISD IQSQLEKLIE KNYFLHKSAQ EAYKSYIRAY DSHSLKQIFN 610 620 630 640 650 660 VNNLNLPQVA LSFGFKVPPF VDLNVNSNEG KQKKRGGGGG FGYQKTKKVE KSKIFKHISK 670 KSSDSRQFSH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-94. Tissue: Placenta.
[3]	"Myc-Max heterodimers activate a DEAD box gene and interact with multiple E box-related sites in vivo." Grandori C., Mac J., Siebelt F., Ayer D.A., Eisenman R.E. EMBO J. 15:4344-4357(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 56-670.
[4]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 61-670, VARIANT SER-94.
[5]	"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 370-376. Tissue: Platelet.
[6]	"NOP132 is required for proper nucleolus localization of DEAD-box RNA helicase DDX47." Sekiguchi T., Hayano T., Yanagida M., Takahashi N., Nishimoto T. Nucleic Acids Res. 34:4593-4608(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NOL8, SUBCELLULAR LOCATION.
[7]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]	"Comparative structural analysis of human DEAD-box RNA helicases." Schutz P., Karlberg T., van den Berg S., Collins R., Lehtio L., Hogbom M., Holmberg-Schiavone L., Tempel W., Park H.W., Hammarstrom M., Moche M., Thorsell A.G., Schuler H. PLoS ONE 5:E12791-E12791(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 149-387 IN COMPLEX WITH PHOSPHATE.
[10]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-41.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AK001467 mRNA. Translation: BAA91709.1.
BC001238 mRNA. Translation: AAH01238.1.
BC003360 mRNA. Translation: AAH03360.1.
BC024739 mRNA. Translation: AAH24739.1.
X98743 mRNA. Translation: CAA67295.1. Different initiation.
CR457060 mRNA. Translation: CAG33341.1.

IPI

IPI00301323.

PIR

S71758.

RefSeq

NP_006764.3. NM_006773.3.

UniGene

Hs.363492.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3LY5	X-ray	2.80	A/B	149-387	[»]

ProteinModelPortal

Q9NVP1.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9NVP1. 6 interactions.

MINT

MINT-1382348.

STRING

9606.ENSP00000263239.

PTM databases

PhosphoSite

Q9NVP1.

Polymorphism databases

DMDM

20532388.

2D gel databases

SWISS-2DPAGE

Q9NVP1.

Proteomic databases

PaxDb

Q9NVP1.

PeptideAtlas

Q9NVP1.

PRIDE

Q9NVP1.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000263239; ENSP00000263239; ENSG00000088205.

GeneID

8886.

KEGG

hsa:8886.

UCSC

uc002tlh.1. human.

Organism-specific databases

CTD

8886.

GeneCards

GC02P118572.

HGNC

HGNC:2741. DDX18.

HPA

HPA035400.

MIM

606355. gene.

neXtProt

NX_Q9NVP1.

PharmGKB

PA27207.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0513.

HOGENOM

HOG000268799.

HOVERGEN

HBG105702.

InParanoid

Q9NVP1.

KO

K13179.

OMA

KDGYRSY.

OrthoDB

EOG4894MF.

PhylomeDB

Q9NVP1.

Gene expression databases

ArrayExpress

Q9NVP1.

Bgee

Q9NVP1.

CleanEx

HS_DDX18.

Genevestigator

Q9NVP1.

GermOnline

ENSG00000088205. Homo sapiens.

Family and domain databases

InterPro

IPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
IPR025313. DUF4217.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR000629. RNA-helicase_DEAD-box_CS.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view]

Pfam

PF00270. DEAD. 1 hit.
PF13959. DUF4217. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]

SMART

SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]

PROSITE

PS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL5060.

ChiTaRS

DDX18. human.

EvolutionaryTrace

Q9NVP1.

GenomeRNAi

8886.

NextBio

33369.

SOURCE

Search...

Entry information

Entry name

DDX18_HUMAN

Accession

Primary (citable) accession number: Q9NVP1
Secondary accession number(s): Q6GTZ9 , Q6IAU4, Q92732, Q9BQB7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2001
Last sequence update:	May 10, 2002
Last modified:	May 1, 2013
This is version 120 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.