Q9H0S4 (DDX47_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable ATP-dependent RNA helicase DDX47
EC=3.6.4.13

Alternative name(s):
DEAD box protein 47

Gene names

Name:

DDX47

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	455 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in apoptosis. May have a role in rRNA processing and mRNA splicing. Associates with pre-rRNA precursors. Ref.9 Ref.11
Catalytic activity	ATP + H2O = ADP + phosphate.
Subunit structure	Interacts with EIF2C1 and EIF2C2. Interacts with GABARAP. Interacts with NOL8; the interaction is RNA-dependent. Ref.9 Ref.11 Ref.12
Subcellular location	Nucleus › nucleolus. Note: Localizes in the nucleolar-organizing region during ribosome biogenesis. Ref.8 Ref.11
Sequence similarities	Belongs to the DEAD box helicase family. DDX47/RRP3 subfamily. Contains 1 helicase ATP-binding domain. Contains 1 helicase C-terminal domain.

Ontologies

Keywords
Biological process	Apoptosis mRNA processing mRNA splicing rRNA processing
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding RNA-binding
Molecular function	Helicase Hydrolase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	RNA splicing Inferred from mutant phenotype Ref.11. Source: UniProtKB apoptotic process Inferred from direct assay Ref.9. Source: UniProtKB mRNA processing Inferred from electronic annotation. Source: UniProtKB-KW rRNA processing Inferred from mutant phenotype Ref.11. Source: UniProtKB
Cellular_component	nucleolus Inferred from direct assay Ref.11. Source: UniProtKB
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...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GABARAP	O95166	3	EBI-2515241,EBI-712001

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9H0S4-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9H0S4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-132: Missing.
     251-299: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.7

Chain

2 – 455

454

Probable ATP-dependent RNA helicase DDX47

PRO_0000055050

Regions

Domain

55 – 226

172

Helicase ATP-binding

Domain

237 – 397

161

Helicase C-terminal

Nucleotide binding

68 – 75

8

ATP

Motif

24 – 52

29

Q motif

Motif

174 – 177

4

DEAD box

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.7 Ref.14 Ref.16

Modified residue

9

1

Phosphoserine Ref.16

Modified residue

424

1

Phosphoserine Ref.13

Natural variations

Alternative sequence

1 – 132

132

Missing in isoform 2.

VSP_045238

Alternative sequence

251 – 299

49

Missing in isoform 2.

VSP_045239

Experimental info

Sequence conflict

55

1

I → V in BAB70762. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

455

Helix Strand Turn

Details...

Helix

18 – 23

6

Helix

27 – 29

3

Helix

33 – 41

9

Helix

49 – 59

11

Beta strand

64 – 67

4

Helix

74 – 88

15

Beta strand

95 – 98

4

Helix

102 – 116

15

Helix

117 – 119

3

Beta strand

123 – 126

4

Helix

132 – 140

9

Beta strand

144 – 148

5

Helix

150 – 159

10

Beta strand

170 – 173

4

Helix

176 – 181

6

Helix

185 – 193

9

Beta strand

197 – 207

11

Helix

210 – 219

10

Beta strand

224 – 227

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 5F64F26AD2C11286	FASTA	455	50,647
	10 20 30 40 50 60 MAAPEEHDSP TEASQPIVEE EETKTFKDLG VTDVLCEACD QLGWTKPTKI QIEAIPLALQ 70 80 90 100 110 120 GRDIIGLAET GSGKTGAFAL PILNALLETP QRLFALVLTP TRELAFQISE QFEALGSSIG 130 140 150 160 170 180 VQSAVIVGGI DSMSQSLALA KKPHIIIATP GRLIDHLENT KGFNLRALKY LVMDEADRIL 190 200 210 220 230 240 NMDFETEVDK ILKVIPRDRK TFLFSATMTK KVQKLQRAAL KNPVKCAVSS KYQTVEKLQQ 250 260 270 280 290 300 YYIFIPSKFK DTYLVYILNE LAGNSFMIFC STCNNTQRTA LLLRNLGFTA IPLHGQMSQS 310 320 330 340 350 360 KRLGSLNKFK AKARSILLAT DVASRGLDIP HVDVVVNFDI PTHSKDYIHR VGRTARAGRS 370 380 390 400 410 420 GKAITFVTQY DVELFQRIEH LIGKKLPGFP TQDDEVMMLT ERVAEAQRFA RMELREHGEK 430 440 450 KKRSREDAGD NDDTEGAIGV RNKVAGGKMK KRKGR
	Isoform 2 [UniParc]. Checksum: F96092988E6BC44D	FASTA	274	31,181
	10 20 30 40 50 60 MSQSLALAKK PHIIIATPGR LIDHLENTKG FNLRALKYLV MDEADRILNM DFETEVDKIL 70 80 90 100 110 120 KVIPRDRKTF LFSATMTKKV QKLQRAALKN PVKCAVSSKY QTVEKLQQYY IFIPSKFKSK 130 140 150 160 170 180 RLGSLNKFKA KARSILLATD VASRGLDIPH VDVVVNFDIP THSKDYIHRV GRTARAGRSG 190 200 210 220 230 240 KAITFVTQYD VELFQRIEHL IGKKLPGFPT QDDEVMMLTE RVAEAQRFAR MELREHGEKK 250 260 270 KRSREDAGDN DDTEGAIGVR NKVAGGKMKK RKGR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Functional prediction of the coding sequences of 50 new genes deduced by analysis of cDNA clones from human fetal liver." Yu Y., Zhang C., Luo L., Ouyang S., Zhang S., Li W., Wu J., Zhou S., Liu M., He F. Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Liver.
[2]	"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs." Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A. Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain.
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]	"The finished DNA sequence of human chromosome 12." Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A. Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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] (ISOFORM 1). Tissue: Brain and Eye.
[7]	Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-24; 75-102; 142-161; 170-190; 238-248; 285-301; 315-325; 378-384 AND 424-441, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: Ovarian carcinoma.
[8]	"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.
[9]	"GABAA receptor-associated protein (GABARAP) induces apoptosis by interacting with DEAD (Asp-Glu-Ala-Asp/His) box polypeptide 47 (DDX 47)." Lee J.H., Rho S.B., Chun T. Biotechnol. Lett. 27:623-628(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH GABARAP, IDENTIFICATION BY MASS SPECTROMETRY.
[10]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[11]	"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: FUNCTION, INTERACTION WITH NOL8, SUBCELLULAR LOCATION.
[12]	"Proteomic and functional analysis of Argonaute-containing mRNA-protein complexes in human cells." Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M., Urlaub H., Meister G. EMBO Rep. 8:1052-1060(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EIF2C1 AND EIF2C2.
[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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-424, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"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].
[16]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, MASS SPECTROMETRY.
[17]	"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 (1.4 ANGSTROMS) OF 1-230 IN COMPLEX WITH AMP.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF078843 mRNA. Translation: AAF23354.1.
AL136666 mRNA. Translation: CAB66601.1.
AK054574 mRNA. Translation: BAB70762.1.
AK127712 mRNA. Translation: BAG54556.1.
AC007215 Genomic DNA. No translation available.
CH471094 Genomic DNA. Translation: EAW96277.1.
CH471094 Genomic DNA. Translation: EAW96283.1.
BC009379 mRNA. Translation: AAH09379.2.
BC068009 mRNA. Translation: AAH68009.1.

IPI

IPI00023972.
IPI00397372.

RefSeq

NP_057439.2. NM_016355.3.
NP_957518.1. NM_201224.1.

UniGene

Hs.719938.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3BER	X-ray	1.40	A	5-230	[»]

ProteinModelPortal

Q9H0S4.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9H0S4. 9 interactions.

MINT

MINT-3056694.

STRING

9606.ENSP00000350698.

PTM databases

PhosphoSite

Q9H0S4.

Polymorphism databases

DMDM

52782792.

2D gel databases

SWISS-2DPAGE

Q9H0S4.

Proteomic databases

PaxDb

Q9H0S4.

PRIDE

Q9H0S4.

Protocols and materials databases

DNASU

51202.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000352940; ENSP00000319578; ENSG00000213782.
ENST00000358007; ENSP00000350698; ENSG00000213782.

GeneID

51202.

KEGG

hsa:51202.

UCSC

uc001rav.3. human.

Organism-specific databases

CTD

51202.

GeneCards

GC12P012966.

HGNC

HGNC:18682. DDX47.

HPA

HPA014855.

neXtProt

NX_Q9H0S4.

PharmGKB

PA134918403.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0513.

HOGENOM

HOG000268802.

HOVERGEN

HBG100512.

InParanoid

Q9H0S4.

KO

K14777.

OMA

IFIPSKF.

PhylomeDB

Q9H0S4.

Gene expression databases

ArrayExpress

Q9H0S4.

Bgee

Q9H0S4.

CleanEx

HS_DDX47.

Genevestigator

Q9H0S4.

GermOnline

ENSG00000178878. Homo sapiens.

Family and domain databases

InterPro

IPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR000629. RNA-helicase_DEAD-box_CS.
[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

ChiTaRS

DDX47. human.

EvolutionaryTrace

Q9H0S4.

GenomeRNAi

51202.

NextBio

54238.

Entry information

Entry name

DDX47_HUMAN

Accession

Primary (citable) accession number: Q9H0S4
Secondary accession number(s): B3KXP4 , G5E955, Q96GM0, Q96NV8, Q9UI98

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 27, 2004
Last sequence update:	March 1, 2001
Last modified:	May 1, 2013
This is version 111 of the entry and version 1 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.