Q9Y2R4 (DDX52_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable ATP-dependent RNA helicase DDX52
EC=3.6.4.13

Alternative name(s):
ATP-dependent RNA helicase ROK1-like
DEAD box protein 52

Gene names

Name:	DDX52
Synonyms:	ROK1
ORF Names:	HUSSY-19

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	599 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	ATP + H2O = ADP + phosphate.
Subcellular location	Nucleus › nucleolus Ref.6.
Sequence similarities	Belongs to the DEAD box helicase family. DDX52/ROK1 subfamily. Contains 1 helicase ATP-binding domain. Contains 1 helicase C-terminal domain.
Sequence caution	The sequence AAD27766.1 differs from that shown. Reason: Frameshift at positions 324, 327, 330, 350, 365 and 377. The sequence AK093661 differs from that shown. Reason: Cloning artifact. The sequence BAA91812.1 differs from that shown. Reason: Cloning artifact. The sequence CAA09374.1 differs from that shown. Reason: Frameshift at positions 355 and 377.

Ontologies

Keywords
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Nucleotide-binding RNA-binding
Molecular function	Helicase Hydrolase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP-dependent helicase activity Inferred from electronic annotation. Source: InterPro 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 – 599

599

Probable ATP-dependent RNA helicase DDX52

PRO_0000055060

Regions

Domain

196 – 374

179

Helicase ATP-binding

Domain

385 – 546

162

Helicase C-terminal

Nucleotide binding

209 – 216

8

ATP

Motif

165 – 193

29

Q motif

Motif

318 – 321

4

DEAD box

Compositional bias

543 – 592

50

Lys-rich

Amino acid modifications

Modified residue

15

1

N6-acetyllysine Ref.9

Modified residue

39

1

Phosphoserine Ref.8

Natural variations

Natural variant

403

1

M → V. Ref.1 Ref.2 Ref.4 Ref.5
Corresponds to variant rs7216445 [ dbSNP | Ensembl ].

VAR_060235

Experimental info

Sequence conflict

299

1

L → S in AK093661. Ref.2

Sequence conflict

582

1

K → R in BAA91812. Ref.2

Sequence conflict

584

1

V → F in CAA09374. Ref.4

Secondary structure

1

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599

Helix Strand Turn

Details...

Helix

139 – 146

8

Beta strand

149 – 155

7

Helix

163 – 170

8

Helix

174 – 182

9

Helix

190 – 200

11

Beta strand

205 – 208

4

Helix

215 – 227

13

Beta strand

232 – 234

3

Beta strand

237 – 240

4

Helix

244 – 257

14

Turn

258 – 260

3

Helix

270 – 275

6

Turn

276 – 278

3

Beta strand

288 – 291

4

Helix

293 – 301

9

Beta strand

302 – 304

3

Beta strand

314 – 319

6

Helix

320 – 326

7

Helix

331 – 341

11

Beta strand

348 – 355

8

Helix

358 – 367

10

Beta strand

368 – 370

3

Beta strand

372 – 376

5

Sequences

	Sequence		Length	Mass (Da)
	Q9Y2R4 [UniParc]. Last modified May 18, 2010. Version 3. Checksum: F31EA34AC478EE21	FASTA	599	67,498
	10 20 30 40 50 60 MDVHDLFRRL GAGAKFDTRR FSADAARFQI GKRKYDFDSS EVLQGLDFFG NKKSVPGVCG 70 80 90 100 110 120 ASQTHQKPQN GEKKEESLTE RKREQSKKKR KTMTSEIASQ EEGATIQWMS SVEAKIEDKK 130 140 150 160 170 180 VQRESKLTSG KLENLRKEKI NFLRNKHKIH VQGTDLPDPI ATFQQLDQEY KINSRLLQNI 190 200 210 220 230 240 LDAGFQMPTP IQMQAIPVML HGRELLASAP TGSGKTLAFS IPILMQLKQP ANKGFRALII 250 260 270 280 290 300 SPTRELASQI HRELIKISEG TGFRIHMIHK AAVAAKKFGP KSSKKFDILV TTPNRLIYLL 310 320 330 340 350 360 KQDPPGIDLA SVEWLVVDES DKLFEDGKTG FRDQLASIFL ACTSHKVRRA MFSATFAYDV 370 380 390 400 410 420 EQWCKLNLDN VISVSIGARN SAVETVEQEL LFVGSETGKL LAMRELVKKG FNPPVLVFVQ 430 440 450 460 470 480 SIERAKELFH ELIYEGINVD VIHAERTQQQ RDNTVHSFRA GKIWVLICTA LLARGIDFKG 490 500 510 520 530 540 VNLVINYDFP TSSVEYIHRI GRTGRAGNKG KAITFFTEDD KPLLRSVANV IQQAGCPVPE 550 560 570 580 590 YIKGFQKLLS KQKKKMIKKP LERESISTTP KCFLEKAKDK QKKVTGQNSK KKVALEDKS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human putative ATP-dependent RNA helicase rok1 mRNA." Mao M., Liu T., Zhang J., Zhang Q., Fu G., Zhou J., Wu J., Shen Y., Yu M., Ye M., Chen S., Chen Z. Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-403.
[2]	"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], VARIANT VAL-403. Tissue: Teratocarcinoma and Thymus.
[3]	"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage." Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C. Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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 VAL-403. Tissue: Prostate.
[5]	"Characterization of 16 novel human genes showing high similarity to yeast sequences." Stanchi F., Bertocco E., Toppo S., Dioguardi R., Simionati B., Cannata N., Zimbello R., Lanfranchi G., Valle G. Yeast 18:69-80(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 180-599, VARIANT VAL-403. Tissue: Liver and Spleen.
[6]	"Functional proteomic analysis of human nucleolus." Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., Greco A., Hochstrasser D.F., Diaz J.-J. Mol. Biol. Cell 13:4100-4109(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Embryonic kidney.
[8]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-15, MASS SPECTROMETRY.
[10]	"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].
[11]	"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 (2.1 ANGSTROMS) OF 139-381 IN COMPLEX WITH ADP.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF077033 mRNA. Translation: AAD27766.1. Frameshift.
AK001652 mRNA. Translation: BAA91812.1. Sequence problems.
AK093661 mRNA. No translation available.
AC091199 Genomic DNA. No translation available.
BC041785 mRNA. Translation: AAH41785.1.
AJ010840 mRNA. Translation: CAA09374.1. Frameshift.

IPI

IPI00032423.

RefSeq

NP_008941.2. NM_007010.3.

UniGene

Hs.590937.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3DKP	X-ray	2.10	A	139-381	[»]

ProteinModelPortal

Q9Y2R4.

SMR

Q9Y2R4. Positions 139-543.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9Y2R4. 7 interactions.

MINT

MINT-2823243.

STRING

9606.ENSP00000268854.

PTM databases

PhosphoSite

Q9Y2R4.

Polymorphism databases

DMDM

296439375.

2D gel databases

SWISS-2DPAGE

Q9Y2R4.

Proteomic databases

PaxDb

Q9Y2R4.

PRIDE

Q9Y2R4.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000349699; ENSP00000268854; ENSG00000141141.

GeneID

11056.

KEGG

hsa:11056.

UCSC

uc002hoh.2. human.

Organism-specific databases

CTD

11056.

GeneCards

GC17M035969.

HGNC

HGNC:20038. DDX52.

MIM

612500. gene.

neXtProt

NX_Q9Y2R4.

PharmGKB

PA134904836.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0513.

HOGENOM

HOG000242486.

HOVERGEN

HBG051332.

InParanoid

Q9Y2R4.

KO

K14779.

OMA

NVMKQSG.

OrthoDB

EOG4XKV6Q.

PhylomeDB

Q9Y2R4.

Gene expression databases

ArrayExpress

Q9Y2R4.

Bgee

Q9Y2R4.

CleanEx

HS_DDX52.

Genevestigator

Q9Y2R4.

GermOnline

ENSG00000141141. Homo sapiens.

Family and domain databases

InterPro

IPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view]

Pfam

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

SMART

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

SUPFAM

SSF52540. SSF52540. 2 hits.

PROSITE

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

ProtoNet

Search...

Other

ChiTaRS

DDX52. human.

EvolutionaryTrace

Q9Y2R4.

GenomeRNAi

11056.

NextBio

42007.

SOURCE

Search...

Entry information

Entry name

DDX52_HUMAN

Accession

Primary (citable) accession number: Q9Y2R4
Secondary accession number(s): Q86YG1 , Q8N213, Q9NVE0, Q9Y482

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 9, 2003
Last sequence update:	May 18, 2010
Last modified:	May 29, 2013
This is version 114 of the entry and version 3 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.