Reviewed, UniProtKB/Swiss-Prot Q9UHI6 (DDX20_HUMAN)

Names and origin

Protein names

Recommended name:
    Probable ATP-dependent RNA helicase DDX20
    EC=3.6.1.-
Alternative name(s):
    DEAD box protein 20
    DEAD box protein DP 103
    Component of gems 3
    Gemin-3

Gene names

Name:	DDX20
Synonyms:	DP103, GEMIN3

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	824 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	The SMN complex plays an essential role in spliceosomal snRNP assembly in the cytoplasm and is required for pre-mRNA splicing in the nucleus. It may also play a role in the metabolism of snoRNPs.
Subunit structure	Part of the core SMN complex that contains SMN1, SIP1/GEMIN2, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8 and STRAP/UNRIP. Interacts directly with SMN1 and with several spliceosomal snRNP core Sm proteins, including SNUPN, SNRPB, SNRPD2 and SNRPD3. Interacts with PPP4R2. Interacts with EBV EBNA2 and EBNA3C. Ref.1 Ref.2 Ref.7 Ref.8
Subcellular location	Cytoplasm. Nucleus › gem. Note: Localized in subnuclear structures next to coiled bodies, called Gemini of Cajal bodies (Gems).
Tissue specificity	Ubiquitous.
Sequence similarities	Belongs to the DEAD box helicase family. DDX20 subfamily. Contains 1 helicase ATP-binding domain. Contains 1 helicase C-terminal domain.

Ontologies

Keywords
Biological process	mRNA processing mRNA splicing
Cellular component	Cytoplasm Nucleus Spliceosome
Coding sequence diversity	Polymorphism
Ligand	ATP-binding DNA-binding Nucleotide-binding
Molecular function	Helicase Hydrolase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	assembly of spliceosomal tri-snRNP Ref.1 Traceable author statement. Source: ProtInc
Cellular component	Cajal body Inferred from electronic annotation. Source: UniProtKB-SubCell cytoskeleton Ref.2 Traceable author statement. Source: ProtInc cytosol Inferred from Experiment. Source: Reactome spliceosome Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP-dependent RNA helicase activity Ref.2 Traceable author statement. Source: ProtInc DNA binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BAT2	P48634	1	EBI-347658,EBI-347545
GSK3B	P49841	1	EBI-347658,EBI-373586
PHB2	Q99623	1	EBI-347658,EBI-358348
PNKP	Q96T60	1	EBI-347658,EBI-1045072
POLR1E	Q9GZS1	1	EBI-347658,EBI-359458
RNPS1	Q15287	1	EBI-347658,EBI-395959

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 824	824	Probable ATP-dependent RNA helicase DDX20		PRO_0000055025
Regions
	Domain	93 – 264	172	Helicase ATP-binding
	Domain	299 – 448	150	Helicase C-terminal
	Nucleotide binding	106 – 113	8	ATP By similarity
	Region	456 – 548	93	SMN interacting
	Motif	62 – 90	29	Q motif
	Motif	211 – 214	4	DEAD box
Amino acid modifications
	Modified residue	48	1	Phosphoserine Ref.12 Ref.13
	Modified residue	187	1	Phosphoserine Ref.12
	Modified residue	500	1	Phosphoserine Ref.13 Ref.10
	Modified residue	532	1	Phosphoserine Ref.13
	Modified residue	552	1	Phosphothreonine Ref.12 Ref.13
	Modified residue	649	1	Phosphoserine Ref.13
	Modified residue	652	1	Phosphoserine Ref.13
	Modified residue	654	1	Phosphoserine Ref.13
	Modified residue	656	1	Phosphoserine Ref.13
	Modified residue	672	1	Phosphoserine Ref.13
	Modified residue	677	1	Phosphoserine Ref.12 Ref.13
	Modified residue	678	1	Phosphoserine Ref.12 Ref.13 Ref.11
	Modified residue	703	1	Phosphoserine Ref.13
	Modified residue	705	1	Phosphothreonine Ref.12 Ref.13 Ref.9
	Modified residue	714	1	Phosphoserine Ref.12 Ref.13 Ref.9
Natural variations
	Natural variant	636	1	I → T: dbSNP rs197412.		VAR_057231
	Natural variant	693	1	R → S: dbSNP rs197414.		VAR_057232
	Natural variant	762	1	I → T: dbSNP rs85276.		VAR_057233
Experimental info
	Sequence conflict	5	1	F → V in AAD42744. Ref.2
	Sequence conflict	279	1	Y → C in BAA91727. Ref.3
	Sequence conflict	639	1	R → K in AAF14544. Ref.1
	Sequence conflict	659	1	Y → H in AAD42744. Ref.2
	Sequence conflict	676	1	G → S in AAF14544. Ref.1
	Sequence conflict	703	1	S → T in AAF14544. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9UHI6-1 [UniParc]. Last modified December 1, 2000. Version 2. Checksum: 76712F014B2A0CF2	FASTA	824	92,241
	10 20 30 40 50 60 MAAAFEASGA LAAVATAMPA EHVAVQVPAP EPTPGPVRIL RTAQDLSSPR TRTGDVLLAE 70 80 90 100 110 120 PADFESLLLS RPVLEGLRAA GFERPSPVQL KAIPLGRCGL DLIVQAKSGT GKTCVFSTIA 130 140 150 160 170 180 LDSLVLENLS TQILILAPTR EIAVQIHSVI TAIGIKMEGL ECHVFIGGTP LSQDKTRLKK 190 200 210 220 230 240 CHIAVGSPGR IKQLIELDYL NPGSIRLFIL DEADKLLEEG SFQEQINWIY SSLPASKQML 250 260 270 280 290 300 AVSATYPEFL ANALTKYMRD PTFVRLNSSD PSLIGLKQYY KVVNSYPLAH KVFEEKTQHL 310 320 330 340 350 360 QELFSRIPFN QALVFSNLHS RAQHLADILS SKGFPAECIS GNMNQNQRLD AMAKLKHFHC 370 380 390 400 410 420 RVLISTDLTS RGIDAEKVNL VVNLDVPLDW ETYMHRIGRA GRFGTLGLTV TYCCRGEEEN 430 440 450 460 470 480 MMMRIAQKCN INLLPLPDPI PSGLMEECVD WDVEVKAAVH TYGIASVPNQ PLKKQIQKIE 490 500 510 520 530 540 RTLQIQKAHG DHMASSRNNS VSGLSVKSKN NTKQKLPVKS HSECGIIEKA TSPKELGCDR 550 560 570 580 590 600 QSEEQMKNSV QTPVENSTNS QHQVKEALPV SLPQIPCLSS FKIHQPYTLT FAELVEDYEH 610 620 630 640 650 660 YIKEGLEKPV EIIRHYTGPG DQTVNPQNGF VRNKVIEQRV PVLASSSQSG DSESDSDSYS 670 680 690 700 710 720 SRTSSQSKGN KSYLEGSSDN QLKDSESTPV DDRISLEQPP NGSDTPNPEK YQESPGIQMK 730 740 750 760 770 780 TRLKEGASQR AKQSRRNLPR RSSFRLQTEA QEDDWYDCHR EIRLSFSDTY QDYEEYWRAY 790 800 810 820 YRAWQEYYAA ASHSYYWNAQ RHPSWMAAYH MNTIYLQEMM HSNQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Gemin3: a novel DEAD box protein that interacts with SMN, the spinal muscular atrophy gene product, and a component of gems." Charroux B., Pellizzoni L., Perkinson R.A., Shevchenko A., Mann M., Dreyfuss G. J. Cell Biol. 147:1181-1194(1999) [PubMed: 10601333] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION IN THE CORE SMN COMPLEX, INTERACTION WITH SNRPB; SNRPD2 AND SNRPD3, MASS SPECTROMETRY.
[2]	"Characterization of DP103, a novel DEAD box protein that binds to the Epstein-Barr virus nuclear proteins EBNA2 and EBNA3C." Grundhoff A.T., Kremmer E., Tuereci O., Glieden A., Gindorf C., Atz J., Mueller-Lantzsch N., Schubach W.H., Grasser F.A. J. Biol. Chem. 274:19136-19144(1999) [PubMed: 10383418] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH EBV EBNA2 AND EBV EBNA3C.
[3]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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], VARIANT THR-636. Tissue: Placenta.
[6]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 189-275. Tissue: Testis.
[7]	"SMN, the spinal muscular atrophy protein, forms a pre-import snRNP complex with snurportin1 and importin beta." Narayanan U., Ospina J.K., Frey M.R., Hebert M.D., Matera A.G. Hum. Mol. Genet. 11:1785-1795(2002) [PubMed: 12095920] [Abstract] Cited for: INTERACTION WITH SNUPN; SMN1 AND SNRPB.
[8]	"Protein phosphatase 4 interacts with the survival of motor neurons complex and enhances the temporal localisation of snRNPs." Carnegie G.K., Sleeman J.E., Morrice N., Hastie C.J., Peggie M.W., Philp A., Lamond A.I., Cohen P.T.W. J. Cell Sci. 116:1905-1913(2003) [PubMed: 12668731] [Abstract] Cited for: INTERACTION WITH PPP4R2.
[9]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-705 AND SER-714, MASS SPECTROMETRY. Tissue: Epithelium.
[10]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-500, MASS SPECTROMETRY. Tissue: Epithelium.
[11]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-678, MASS SPECTROMETRY.
[12]	"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 SER-48; SER-187; THR-552; SER-677; SER-678; THR-705 AND SER-714, MASS SPECTROMETRY.
[13]	"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-48; SER-500; SER-532; THR-552; SER-649; SER-652; SER-654; SER-656; SER-672; SER-677; SER-678; SER-703; THR-705 AND SER-714, MASS SPECTROMETRY.
[14]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AF171063 mRNA. Translation: AAF14544.1.
AF106019 mRNA. Translation: AAD42744.1.
AK001506 mRNA. Translation: BAA91727.1.
AL049557 Genomic DNA. Translation: CAB55686.2.
BC011556 mRNA. Translation: AAH11556.1.
AL133598 mRNA. Translation: CAB63734.2.

IPI

IPI00005904.

PIR

T43476.

RefSeq

NP_009135.3.

UniGene

Hs.591405

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2OXC	X-ray	1.30	A/B	41-268	[»]
3B7G	X-ray	1.90	A/B	41-268	[»]

SMR

Q9UHI6. Positions 62-266.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9UHI6. 18 interactions.

PTM databases

PhosphoSite

Q9UHI6.

Proteomic databases

PeptideAtlas

Q9UHI6.

PRIDE

Q9UHI6.

Genome annotation databases

Ensembl

ENSG00000064703. Homo sapiens. [Contig view]

GeneID

11218.

KEGG

hsa:11218.

UCSC

uc001ebs.1. human.

Organism-specific databases

GeneCards

GC01P112010.

HGNC

HGNC:2743. DDX20.

HPA

CAB015427.
HPA005516.

MIM

606168. gene.

PharmGKB

PA27209.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

Q9UHI6.

HOVERGEN

Q9UHI6.

OMA

Q9UHI6. KTRLKKC.

Enzyme and pathway databases

Reactome

REACT_11052. Metabolism of non-coding RNA.

Gene expression databases

ArrayExpress

Q9UHI6.

Bgee

Q9UHI6.

CleanEx

HS_DDX20.

GermOnline

ENSG00000064703. 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

42699.

SOURCE

Search...

Entry information

Entry name

DDX20_HUMAN

Accession

Primary (citable) accession number: Q9UHI6
Secondary accession number(s): Q96F72 , Q9NVM3, Q9UF59, Q9UIY0, Q9Y659

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	December 1, 2000
Last modified:	July 7, 2009
This is version 104 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)