Reviewed, UniProtKB/Swiss-Prot Q13206 (DDX10_HUMAN)

Names and origin

Protein names

Recommended name:
    Probable ATP-dependent RNA helicase DDX10
    EC=3.6.1.-
Alternative name(s):
    DEAD box protein 10

Gene names

Name:

DDX10

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	875 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Putative ATP-dependent RNA helicase.
Tissue specificity	High in testis but widely expressed.
Domain	The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Involvement in disease	Defects in DDX10 may be a cause of breast cancer.
Sequence similarities	Belongs to the DEAD box helicase family. DDX10/DBP4 subfamily. Contains 1 helicase ATP-binding domain. Contains 1 helicase C-terminal domain.

Ontologies

Keywords
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Nucleotide-binding RNA-binding
Molecular function	Helicase Hydrolase
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Cellular component	nucleolus Inferred from direct assay. Source: HPA plasma membrane Inferred from direct assay. Source: HPA
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 RNA helicase activity Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 875

875

Probable ATP-dependent RNA helicase DDX10

PRO_0000055083

Regions

Domain

100 – 274

175

Helicase ATP-binding

Domain

287 – 448

162

Helicase C-terminal

Nucleotide binding

113 – 120

8

ATP By similarity

Motif

69 – 97

29

Q motif

Motif

222 – 225

4

DEAD box

Amino acid modifications

Modified residue

4

1

Phosphothreonine Ref.5

Modified residue

7

1

Phosphoserine Ref.5

Modified residue

539

1

Phosphoserine Ref.7

Modified residue

569

1

Phosphothreonine Ref.6

Modified residue

577

1

Phosphothreonine Ref.7

Modified residue

780

1

Phosphoserine Ref.4

Natural variations

Natural variant

566

1

L → V in a breast cancer sample; somatic mutation. Ref.8

VAR_035840

Experimental info

Sequence conflict

647

1

D → A in AAC50823. Ref.1

Sequence conflict

658

1

E → D in AAC50823. Ref.1

Sequence conflict

661

1

K → N in AAC50823. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

875

Helix Strand Turn

Details...

Helix

47 – 58

12

Turn

59 – 62

4

Helix

65 – 67

3

Helix

71 – 73

3

Helix

78 – 86

9

Helix

94 – 104

11

Beta strand

109 – 112

4

Helix

119 – 133

15

Helix

138 – 140

3

Beta strand

144 – 147

4

Helix

151 – 164

14

Turn

165 – 167

3

Beta strand

172 – 175

4

Helix

182 – 188

7

Beta strand

192 – 196

5

Helix

198 – 207

10

Beta strand

218 – 221

4

Helix

224 – 229

6

Turn

230 – 232

3

Helix

233 – 241

9

Beta strand

247 – 255

9

Helix

258 – 266

9

Beta strand

272 – 275

4

Sequences

	Sequence		Length	Mass (Da)
	Q13206-1 [UniParc]. Last modified September 27, 2005. Version 2. Checksum: B61BF325921C62FD	FASTA	875	100,888
	10 20 30 40 50 60 MGKTANSPGS GARPDPVRSF NRWKKKHSHR QNKKKQLRKQ LKKPEWQVER ESISRLMQNY 70 80 90 100 110 120 EKINVNEITR FSDFPLSKKT LKGLQEAQYR LVTEIQKQTI GLALQGKDVL GAAKTGSGKT 130 140 150 160 170 180 LAFLVPVLEA LYRLQWTSTD GLGVLIISPT RELAYQTFEV LRKVGKNHDF SAGLIIGGKD 190 200 210 220 230 240 LKHEAERINN INILVCTPGR LLQHMDETVS FHATDLQMLV LDEADRILDM GFADTMNAVI 250 260 270 280 290 300 ENLPKKRQTL LFSATQTKSV KDLARLSLKN PEYVWVHEKA KYSTPATLEQ NYIVCELQQK 310 320 330 340 350 360 ISVLYSFLRS HLKKKSIVFF SSCKEVQYLY RVFCRLRPGV SILALHGRQQ QMRRMEVYNE 370 380 390 400 410 420 FVRKRAAVLF ATDIAARGLD FPAVNWVLQF DCPEDANTYI HRAGRTARYK EDGEALLILL 430 440 450 460 470 480 PSEKAMVQQL LQKKVPVKEI KINPEKLIDV QKKLESILAQ DQDLKERAQR CFVSYVRSVY 490 500 510 520 530 540 LMKDKEVFDV SKLPIPEYAL SLGLAVAPRV RFLQKMQKQP TKELVRSQAD KVIEPRAPSL 550 560 570 580 590 600 TNDEVEEFRA YFNEKMSILQ KGGKRLEGTE HRQDNDTGNE EQEEEEDDEE EMEEKLAKAK 610 620 630 640 650 660 GSQAPSLPNT SEAQKIKEVP TQFLDRDEEE EDADFLKVKR HNVFGLDLKD EKTLQKKEPS 670 680 690 700 710 720 KSSIKKKMTK VAEAKKVMKR NFKVNKKITF TDEGELVQQW PQMQKSAIKD AEEDDDTGGI 730 740 750 760 770 780 NLHKAKERLQ EEDKFDKEEY RKKIKAKHRE KRLKEREARR EANKRQAKAK DEEEAFLDWS 790 800 810 820 830 840 DDDDDDDDGF DPSTLPDPDK YRSSEDSDSE DMENKISDTK KKQGMKKRSN SEVEDVGPTS 850 860 870 HNRKKARWDT LEPLDTGLSL AEDEELVLHL LRSQS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A human gene (DDX10) encoding a putative DEAD-box RNA helicase at 11q22-q23." Savitsky K., Ziv Y., Bar-Shira A., Gilad S., Tagle D.A., Smith S., Uziel T., Sfez S., Nahmias J., Sartiel A., Eddy R.L., Shows T.B., Collins F.S., Shiloh Y., Rotman G. Genomics 33:199-206(1996) [PubMed: 8660968] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Molecular analysis of the chromosomal breakpoints and identification of the repetitive sequences near the breakpoints of NUP98 in therapy-related leukemia with inv(11)(p15q22)." Arai Y., Kaneko Y., Kubo T., Arai K., Hosoda F., Ohki M. Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.
[4]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-780, MASS SPECTROMETRY. Tissue: Epithelium.
[5]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-4 AND SER-7, MASS SPECTROMETRY.
[6]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-569, MASS SPECTROMETRY.
[7]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-539 AND THR-577, MASS SPECTROMETRY.
[8]	"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: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-566.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBLGenBankDDBJ

U28042 mRNA. Translation: AAC50823.1.
AB040537 mRNA. Translation: BAB18536.1.
BC091521 mRNA. Translation: AAH91521.1.
BC093654 mRNA. Translation: AAH93654.1.
BC093656 mRNA. Translation: AAH93656.1.

IPI

IPI00297900.

RefSeq

NP_004389.2.

UniGene

Hs.591931

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2PL3	X-ray	2.15	A	47-280	[»]

ModBase

Search...

PTM databases

PhosphoSite

Q13206.

2-D gel databases

SWISS-2DPAGE

Q13206.

Proteomic databases

PeptideAtlas

Q13206.

PRIDE

Q13206.

Genome annotation databases

Ensembl

ENSG00000178105. Homo sapiens. [Contig view]

GeneID

1662.

KEGG

hsa:1662.

Organism-specific databases

GeneCards

GC11P108041.

HGNC

HGNC:2735. DDX10.

HPA

HPA004691.

MIM

601235. gene.

PharmGKB

PA27200.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

Q13206.

HOVERGEN

Q13206.

OMA

Q13206. KVKRHNV.

Gene expression databases

ArrayExpress

Q13206.

Bgee

Q13206.

CleanEx

HS_DDX10.

GermOnline

ENSG00000178105. Homo sapiens.

Family and domain databases

InterPro

IPR014001. DEAD-like_N.
IPR001650. DNA/RNA_helicase_C.
IPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
IPR014021. Helicase_SF1/SF2_ATP-bd.
IPR000629. RNA-helicase_DEAD-box_CS.
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]

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 Resources

NextBio

6838.

SOURCE

Search...

Entry information

Entry name

DDX10_HUMAN

Accession

Primary (citable) accession number: Q13206
Secondary accession number(s): Q5BJD8

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	September 27, 2005
Last modified:	June 16, 2009
This is version 85 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)