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Probable ATP-dependent RNA helicase DDX47 (EC 3.6.4.13) (DEAD box protein 47)

 DDX47_HUMAN             Reviewed;         455 AA.
Q9H0S4; B3KXP4; G5E955; Q96GM0; Q96NV8; Q9UI98;
27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
13-FEB-2019, entry version 164.
RecName: Full=Probable ATP-dependent RNA helicase DDX47;
EC=3.6.4.13;
AltName: Full=DEAD box protein 47;
Name=DDX47;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=11230166; DOI=10.1101/gr.GR1547R;
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.;
"Towards a catalog of human genes and proteins: sequencing and
analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
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.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain, and Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
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, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Ovarian carcinoma;
Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
Submitted (DEC-2008) to UniProtKB.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-455 (ISOFORM 2).
TISSUE=Liver;
Yu Y., Zhang C., Luo L., Ouyang S., Zhang S., Li W., Wu J., Zhou S.,
Liu M., He F.;
"Functional prediction of the coding sequences of 50 new genes deduced
by analysis of cDNA clones from human fetal liver.";
Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
[8]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=12429849; DOI=10.1091/mbc.E02-05-0271;
Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
Greco A., Hochstrasser D.F., Diaz J.-J.;
"Functional proteomic analysis of human nucleolus.";
Mol. Biol. Cell 13:4100-4109(2002).
[9]
FUNCTION, INTERACTION WITH GABARAP, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=15977068; DOI=10.1007/s10529-005-3628-2;
Lee J.H., Rho S.B., Chun T.;
"GABAA receptor-associated protein (GABARAP) induces apoptosis by
interacting with DEAD (Asp-Glu-Ala-Asp/His) box polypeptide 47 (DDX
47).";
Biotechnol. Lett. 27:623-628(2005).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[11]
FUNCTION, INTERACTION WITH NOL8, AND SUBCELLULAR LOCATION.
PubMed=16963496; DOI=10.1093/nar/gkl603;
Sekiguchi T., Hayano T., Yanagida M., Takahashi N., Nishimoto T.;
"NOP132 is required for proper nucleolus localization of DEAD-box RNA
helicase DDX47.";
Nucleic Acids Res. 34:4593-4608(2006).
[12]
INTERACTION WITH AGO1 AND AGO2.
PubMed=17932509; DOI=10.1038/sj.embor.7401088;
Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M.,
Urlaub H., Meister G.;
"Proteomic and functional analysis of Argonaute-containing mRNA-
protein complexes in human cells.";
EMBO Rep. 8:1052-1060(2007).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-424, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-9, CLEAVAGE OF INITIATOR METHIONINE [LARGE
SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9 AND THR-149, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[19]
X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 1-230 IN COMPLEX WITH AMP.
PubMed=20941364; DOI=10.1371/journal.pone.0012791;
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.;
"Comparative structural analysis of human DEAD-box RNA helicases.";
PLoS ONE 5:E12791-E12791(2010).
-!- FUNCTION: Involved in apoptosis. May have a role in rRNA
processing and mRNA splicing. Associates with pre-rRNA precursors.
{ECO:0000269|PubMed:15977068, ECO:0000269|PubMed:16963496}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
-!- SUBUNIT: Interacts with AGO1 and AGO2. Interacts with GABARAP.
Interacts with NOL8; the interaction is RNA-dependent.
{ECO:0000269|PubMed:15977068, ECO:0000269|PubMed:16963496,
ECO:0000269|PubMed:17932509, ECO:0000269|PubMed:20941364}.
-!- INTERACTION:
O95166:GABARAP; NbExp=3; IntAct=EBI-2515241, EBI-712001;
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus
{ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:16963496}.
Note=Localizes in the nucleolar-organizing region during ribosome
biogenesis.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9H0S4-1; Sequence=Displayed;
Name=2;
IsoId=Q9H0S4-2; Sequence=VSP_045239;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the DEAD box helicase family. DDX47/RRP3
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAF23354.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AL136666; CAB66601.1; -; mRNA.
EMBL; AK054574; BAB70762.1; -; mRNA.
EMBL; AK127712; BAG54556.1; -; mRNA.
EMBL; AC007215; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471094; EAW96277.1; -; Genomic_DNA.
EMBL; CH471094; EAW96283.1; -; Genomic_DNA.
EMBL; BC009379; AAH09379.2; -; mRNA.
EMBL; BC068009; AAH68009.1; -; mRNA.
EMBL; AF078843; AAF23354.1; ALT_INIT; mRNA.
CCDS; CCDS8655.1; -. [Q9H0S4-1]
CCDS; CCDS8656.1; -. [Q9H0S4-2]
RefSeq; NP_057439.2; NM_016355.3. [Q9H0S4-1]
RefSeq; NP_957518.1; NM_201224.1. [Q9H0S4-2]
UniGene; Hs.719938; -.
PDB; 3BER; X-ray; 1.40 A; A=5-230.
PDBsum; 3BER; -.
ProteinModelPortal; Q9H0S4; -.
SMR; Q9H0S4; -.
BioGrid; 119375; 69.
IntAct; Q9H0S4; 36.
MINT; Q9H0S4; -.
STRING; 9606.ENSP00000350698; -.
iPTMnet; Q9H0S4; -.
PhosphoSitePlus; Q9H0S4; -.
SwissPalm; Q9H0S4; -.
BioMuta; DDX47; -.
DMDM; 52782792; -.
SWISS-2DPAGE; Q9H0S4; -.
EPD; Q9H0S4; -.
jPOST; Q9H0S4; -.
MaxQB; Q9H0S4; -.
PaxDb; Q9H0S4; -.
PeptideAtlas; Q9H0S4; -.
PRIDE; Q9H0S4; -.
ProteomicsDB; 80322; -.
DNASU; 51202; -.
Ensembl; ENST00000352940; ENSP00000319578; ENSG00000213782. [Q9H0S4-2]
Ensembl; ENST00000358007; ENSP00000350698; ENSG00000213782. [Q9H0S4-1]
GeneID; 51202; -.
KEGG; hsa:51202; -.
UCSC; uc001rax.4; human. [Q9H0S4-1]
CTD; 51202; -.
EuPathDB; HostDB:ENSG00000213782.7; -.
GeneCards; DDX47; -.
HGNC; HGNC:18682; DDX47.
HPA; HPA014855; -.
MIM; 615428; gene.
neXtProt; NX_Q9H0S4; -.
OpenTargets; ENSG00000213782; -.
PharmGKB; PA134918403; -.
eggNOG; KOG0330; Eukaryota.
eggNOG; ENOG410XQU7; LUCA.
GeneTree; ENSGT00940000155774; -.
HOGENOM; HOG000268802; -.
HOVERGEN; HBG100512; -.
InParanoid; Q9H0S4; -.
KO; K14777; -.
OMA; KAKNRSI; -.
OrthoDB; 744428at2759; -.
PhylomeDB; Q9H0S4; -.
TreeFam; TF105714; -.
Reactome; R-HSA-6790901; rRNA modification in the nucleus and cytosol.
Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
ChiTaRS; DDX47; human.
EvolutionaryTrace; Q9H0S4; -.
GeneWiki; DDX47; -.
GenomeRNAi; 51202; -.
PRO; PR:Q9H0S4; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000213782; Expressed in 94 organ(s), highest expression level in ectocervix.
ExpressionAtlas; Q9H0S4; baseline and differential.
Genevisible; Q9H0S4; HS.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IDA:UniProtKB.
GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO; GO:0008380; P:RNA splicing; IMP:UniProtKB.
GO; GO:0006364; P:rRNA processing; IMP:UniProtKB.
CDD; cd00079; HELICc; 1.
InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
Pfam; PF00270; DEAD; 1.
Pfam; PF00271; Helicase_C; 1.
SMART; SM00487; DEXDc; 1.
SMART; SM00490; HELICc; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
PROSITE; PS51195; Q_MOTIF; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Apoptosis;
ATP-binding; Complete proteome; Direct protein sequencing; Helicase;
Hydrolase; mRNA processing; mRNA splicing; Nucleotide-binding;
Nucleus; Phosphoprotein; Reference proteome; RNA-binding;
rRNA processing.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000269|Ref.6}.
CHAIN 2 455 Probable ATP-dependent RNA helicase
DDX47.
/FTId=PRO_0000055050.
DOMAIN 55 226 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 237 397 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
NP_BIND 68 75 ATP.
MOTIF 24 52 Q motif.
MOTIF 174 177 DEAD box.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000269|Ref.6}.
MOD_RES 9 9 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 149 149 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 424 424 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
VAR_SEQ 251 299 Missing (in isoform 2).
{ECO:0000303|Ref.7}.
/FTId=VSP_045239.
CONFLICT 55 55 I -> V (in Ref. 3; BAB70762).
{ECO:0000305}.
HELIX 18 23 {ECO:0000244|PDB:3BER}.
HELIX 27 29 {ECO:0000244|PDB:3BER}.
HELIX 33 41 {ECO:0000244|PDB:3BER}.
HELIX 49 59 {ECO:0000244|PDB:3BER}.
STRAND 64 67 {ECO:0000244|PDB:3BER}.
HELIX 74 88 {ECO:0000244|PDB:3BER}.
STRAND 95 98 {ECO:0000244|PDB:3BER}.
HELIX 102 116 {ECO:0000244|PDB:3BER}.
HELIX 117 119 {ECO:0000244|PDB:3BER}.
STRAND 123 126 {ECO:0000244|PDB:3BER}.
HELIX 132 140 {ECO:0000244|PDB:3BER}.
STRAND 144 148 {ECO:0000244|PDB:3BER}.
HELIX 150 159 {ECO:0000244|PDB:3BER}.
STRAND 170 173 {ECO:0000244|PDB:3BER}.
HELIX 176 181 {ECO:0000244|PDB:3BER}.
HELIX 185 193 {ECO:0000244|PDB:3BER}.
STRAND 197 207 {ECO:0000244|PDB:3BER}.
HELIX 210 219 {ECO:0000244|PDB:3BER}.
STRAND 224 227 {ECO:0000244|PDB:3BER}.
SEQUENCE 455 AA; 50647 MW; 5F64F26AD2C11286 CRC64;
MAAPEEHDSP TEASQPIVEE EETKTFKDLG VTDVLCEACD QLGWTKPTKI QIEAIPLALQ
GRDIIGLAET GSGKTGAFAL PILNALLETP QRLFALVLTP TRELAFQISE QFEALGSSIG
VQSAVIVGGI DSMSQSLALA KKPHIIIATP GRLIDHLENT KGFNLRALKY LVMDEADRIL
NMDFETEVDK ILKVIPRDRK TFLFSATMTK KVQKLQRAAL KNPVKCAVSS KYQTVEKLQQ
YYIFIPSKFK DTYLVYILNE LAGNSFMIFC STCNNTQRTA LLLRNLGFTA IPLHGQMSQS
KRLGSLNKFK AKARSILLAT DVASRGLDIP HVDVVVNFDI PTHSKDYIHR VGRTARAGRS
GKAITFVTQY DVELFQRIEH LIGKKLPGFP TQDDEVMMLT ERVAEAQRFA RMELREHGEK
KKRSREDAGD NDDTEGAIGV RNKVAGGKMK KRKGR


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Kits Elisa; taq POLYMERASE

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Gentaur; yes we can

Pathways :
WP1672: Mismatch repair
WP1678: Nucleotide excision repair
WP1493: Carbon assimilation C4 pathway
WP1625: Base excision repair
WP1676: Non-homologous end-joining
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1502: Mitochondrial biogenesis
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1616: ABC transporters
WP1619: Amino sugar and nucleotide sugar metabolism
WP1624: Bacterial secretion system
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1663: Homologous recombination
WP1665: Limonene and pinene degradation
WP1673: Naphthalene and anthracene degradation

Related Genes :
[DDX17] Probable ATP-dependent RNA helicase DDX17 (EC 3.6.4.13) (DEAD box protein 17) (DEAD box protein p72) (DEAD box protein p82) (RNA-dependent helicase p72)
[Ddx3x D1Pas1-rs2 Ddx3 Dead3 Erh] ATP-dependent RNA helicase DDX3X (EC 3.6.4.13) (D1Pas1-related sequence 2) (DEAD box RNA helicase DEAD3) (mDEAD3) (DEAD box protein 3, X-chromosomal) (Embryonic RNA helicase)
[Ddx17] Probable ATP-dependent RNA helicase DDX17 (EC 3.6.4.13) (DEAD box protein 17)
[DHX36 DDX36 KIAA1488 MLEL1 RHAU] ATP-dependent DNA/RNA helicase DHX36 (EC 3.6.4.12) (EC 3.6.4.13) (DEAD/H box polypeptide 36) (DEAH-box protein 36) (G4-resolvase-1) (G4R1) (MLE-like protein 1) (RNA helicase associated with AU-rich element protein)
[Eif4a3 Ddx48] Eukaryotic initiation factor 4A-III (eIF-4A-III) (eIF4A-III) (EC 3.6.4.13) (ATP-dependent RNA helicase DDX48) (ATP-dependent RNA helicase eIF4A-3) (DEAD box protein 48) (Eukaryotic translation initiation factor 4A isoform 3) [Cleaved into: Eukaryotic initiation factor 4A-III, N-terminally processed]
[Dhx36 Ddx36 Kiaa1488 Mlel1] ATP-dependent DNA/RNA helicase DHX36 (EC 3.6.4.13) (DEAD/H box polypeptide 36) (DEAH box protein 36) (MLE-like protein 1) (RNA helicase associated with AU-rich element ARE)
[DDX39B BAT1 UAP56] Spliceosome RNA helicase DDX39B (EC 3.6.4.13) (56 kDa U2AF65-associated protein) (ATP-dependent RNA helicase p47) (DEAD box protein UAP56) (HLA-B-associated transcript 1 protein)
[DDX3X DBX DDX3] ATP-dependent RNA helicase DDX3X (EC 3.6.4.13) (DEAD box protein 3, X-chromosomal) (DEAD box, X isoform) (Helicase-like protein 2) (HLP2)
[EIF4A3 DDX48 KIAA0111] Eukaryotic initiation factor 4A-III (eIF-4A-III) (eIF4A-III) (EC 3.6.4.13) (ATP-dependent RNA helicase DDX48) (ATP-dependent RNA helicase eIF4A-3) (DEAD box protein 48) (Eukaryotic initiation factor 4A-like NUK-34) (Eukaryotic translation initiation factor 4A isoform 3) (Nuclear matrix protein 265) (NMP 265) (hNMP 265) [Cleaved into: Eukaryotic initiation factor 4A-III, N-terminally processed]
[DDX19B DBP5 DDX19 TDBP] ATP-dependent RNA helicase DDX19B (EC 3.6.4.13) (DEAD box RNA helicase DEAD5) (DEAD box protein 19B)
[Ddx39b Bat1 Bat1a Uap56] Spliceosome RNA helicase Ddx39b (EC 3.6.4.13) (56 kDa U2AF65-associated protein) (ATP-dependent RNA helicase p47) (DEAD box protein Uap56)
[DDX27 cPERP-F RHLP HSPC259 PP3241] Probable ATP-dependent RNA helicase DDX27 (EC 3.6.4.13) (DEAD box protein 27)
[DDX58] Probable ATP-dependent RNA helicase DDX58 (EC 3.6.4.13) (DEAD box protein 58) (RIG-I-like receptor 1) (RLR-1) (Retinoic acid-inducible gene 1 protein) (RIG-1) (Retinoic acid-inducible gene I protein) (RIG-I)
[Dhx36] ATP-dependent DNA/RNA helicase DHX36 (EC 3.6.4.12) (EC 3.6.4.13) (DEAD/H box polypeptide 36) (DEAH-box protein 36) (G4-resolvase-1) (G4R1) (MLE-like protein 1) (RNA helicase associated with AU-rich element protein)
[Eif4a3 Ddx48] Eukaryotic initiation factor 4A-III (eIF-4A-III) (eIF4A-III) (EC 3.6.4.13) (ATP-dependent RNA helicase DDX48) (ATP-dependent RNA helicase eIF4A-3) (DEAD box protein 48) (Eukaryotic translation initiation factor 4A isoform 3) [Cleaved into: Eukaryotic initiation factor 4A-III, N-terminally processed]
[DHX36] ATP-dependent DNA/RNA helicase DHX36 (EC 3.6.4.12) (EC 3.6.4.13) (DEAD/H box polypeptide 36) (DEAH-box protein 36) (G4-resolvase-1) (G4R1) (MLE-like protein 1) (RNA helicase associated with AU-rich element protein)
[DDX31] Probable ATP-dependent RNA helicase DDX31 (EC 3.6.4.13) (DEAD box protein 31) (Helicain)
[Dhx9 Ddx9] ATP-dependent RNA helicase A (EC 3.6.4.13) (DEAH box protein 9) (mHEL-5) (Nuclear DNA helicase II) (NDH II) (RNA helicase A) (RHA)
[DDX1] ATP-dependent RNA helicase DDX1 (EC 3.6.4.13) (DEAD box protein 1) (DEAD box protein retinoblastoma) (DBP-RB)
[DDX46 KIAA0801] Probable ATP-dependent RNA helicase DDX46 (EC 3.6.4.13) (DEAD box protein 46) (PRP5 homolog)
[RH10 EAST2 At5g60990 MSL3.13 MSL3_110] DEAD-box ATP-dependent RNA helicase 10 (EC 3.6.4.13) (Protein ENHANCER OF ASYMMETRIC LEAVES TWO)
[Ddx1] ATP-dependent RNA helicase DDX1 (EC 3.6.4.13) (DEAD box protein 1)
[DDX28 MDDX28] Probable ATP-dependent RNA helicase DDX28 (EC 3.6.4.13) (Mitochondrial DEAD box protein 28)
[DDX5 QtsA-17658] Probable ATP-dependent RNA helicase DDX5 (EC 3.6.4.13) (DEAD box protein 5)
[EIF4A3 DDX48] Eukaryotic initiation factor 4A-III (EC 3.6.4.13) (ATP-dependent RNA helicase DDX48) (ATP-dependent RNA helicase eIF4A-3) (DEAD box protein 48) (Eukaryotic translation initiation factor 4A isoform 3) [Cleaved into: Eukaryotic initiation factor 4A-III, N-terminally processed]
[EIF4A3 DDX48] Eukaryotic initiation factor 4A-III (eIF-4A-III) (eIF4A-III) (EC 3.6.4.13) (ATP-dependent RNA helicase DDX48) (ATP-dependent RNA helicase eIF4A-3) (DEAD box protein 48) (Eukaryotic translation initiation factor 4A isoform 3) [Cleaved into: Eukaryotic initiation factor 4A-III, N-terminally processed]
[DDX60] Probable ATP-dependent RNA helicase DDX60 (EC 3.6.4.13) (DEAD box protein 60)
[DHX9 DDX9 LKP NDH2] ATP-dependent RNA helicase A (EC 3.6.4.13) (DEAH box protein 9) (DExH-box helicase 9) (Leukophysin) (LKP) (Nuclear DNA helicase II) (NDH II) (RNA helicase A)
[Dhx58 D11lgp2e Lgp2] Probable ATP-dependent RNA helicase DHX58 (EC 3.6.4.13) (Probable ATP-dependent helicase LGP2) (Protein D11Lgp2) (RIG-I-like receptor 3) (RLR-3) (RIG-I-like receptor Lgp2) (RLR)
[rde-12 F58G11.2] DEAD-box ATP-dependent RNA helicase rde-12 (EC 3.6.4.13) (RNA interference defective protein 12)

Bibliography :
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