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Probable ATP-dependent RNA helicase spindle-E (EC 3.6.4.13) (Homeless)

 SPNE_DROME              Reviewed;        1434 AA.
Q9VF26; A2RVD0; Q26453;
02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
12-SEP-2018, entry version 152.
RecName: Full=Probable ATP-dependent RNA helicase spindle-E;
EC=3.6.4.13;
AltName: Full=Homeless;
Name=spn-E; Synonyms=hls; ORFNames=CG3158;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=Canton-S; TISSUE=Ovary;
PubMed=7590230; DOI=10.1101/gad.9.20.2495;
Gillespie D.E., Berg C.A.;
"Homeless is required for RNA localization in Drosophila oogenesis and
encodes a new member of the DE-H family of RNA-dependent ATPases.";
Genes Dev. 9:2495-2508(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley;
Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
[5]
FUNCTION.
PubMed=11513298; DOI=10.1007/s004120100136;
Stapleton W., Das S., McKee B.D.;
"A role of the Drosophila homeless gene in repression of Stellate in
male meiosis.";
Chromosoma 110:228-240(2001).
[6]
FUNCTION.
PubMed=11470406; DOI=10.1016/S0960-9822(01)00299-8;
Aravin A.A., Naumova N.M., Tulin A.V., Vagin V.V., Rozovsky Y.M.,
Gvozdev V.A.;
"Double-stranded RNA-mediated silencing of genomic tandem repeats and
transposable elements in the D. melanogaster germline.";
Curr. Biol. 11:1017-1027(2001).
[7]
FUNCTION.
PubMed=12154120; DOI=10.1101/gad.990802;
Kennerdell J.R., Yamaguchi S., Carthew R.W.;
"RNAi is activated during Drosophila oocyte maturation in a manner
dependent on aubergine and spindle-E.";
Genes Dev. 16:1884-1889(2002).
[8]
FUNCTION.
PubMed=15254241; DOI=10.1128/MCB.24.15.6742-6750.2004;
Aravin A.A., Klenov M.S., Vagin V.V., Bantignies F., Cavalli G.,
Gvozdev V.A.;
"Dissection of a natural RNA silencing process in the Drosophila
melanogaster germ line.";
Mol. Cell. Biol. 24:6742-6750(2004).
[9]
FUNCTION.
PubMed=17194939;
Vagin V.V., Klenov M.S., Kalmykova A.I., Stolyarenko A.D.,
Kotelnikov R.N., Gvozdev V.A.;
"The RNA interference proteins and vasa locus are involved in the
silencing of retrotransposons in the female germline of Drosophila
melanogaster.";
RNA Biol. 1:54-58(2004).
[10]
FUNCTION.
PubMed=14752161; DOI=10.1126/science.1092653;
Pal-Bhadra M., Leibovitch B.A., Gandhi S.G., Rao M., Bhadra U.,
Birchler J.A., Elgin S.C.R.;
"Heterochromatic silencing and HP1 localization in Drosophila are
dependent on the RNAi machinery.";
Science 303:669-672(2004).
[11]
FUNCTION.
PubMed=16452506; DOI=10.1101/gad.370206;
Savitsky M., Kwon D., Georgiev P., Kalmykova A., Gvozdev V.;
"Telomere elongation is under the control of the RNAi-based mechanism
in the Drosophila germline.";
Genes Dev. 20:345-354(2006).
[12]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=16809489; DOI=10.1126/science.1129333;
Vagin V.V., Sigova A., Li C., Seitz H., Gvozdev V., Zamore P.D.;
"A distinct small RNA pathway silences selfish genetic elements in the
germline.";
Science 313:320-324(2006).
[13]
FUNCTION.
PubMed=17603126; DOI=10.1534/genetics.106.066746;
Simmons M.J., Ryzek D.F., Lamour C., Goodman J.W., Kummer N.E.,
Merriman P.J.;
"Cytotype regulation by telomeric P elements in Drosophila
melanogaster: evidence for involvement of an RNA interference gene.";
Genetics 176:1945-1955(2007).
[14]
FUNCTION.
PubMed=17941712; DOI=10.1371/journal.pgen.0030158;
Josse T., Teysset L., Todeschini A.L., Sidor C.M., Anxolabehere D.,
Ronsseray S.;
"Telomeric trans-silencing: an epigenetic repression combining RNA
silencing and heterochromatin formation.";
PLoS Genet. 3:1633-1643(2007).
[15]
FUNCTION.
PubMed=17428915; DOI=10.1073/pnas.0701920104;
Lim A.K., Kai T.;
"Unique germ-line organelle, nuage, functions to repress selfish
genetic elements in Drosophila melanogaster.";
Proc. Natl. Acad. Sci. U.S.A. 104:6714-6719(2007).
[16]
ERRATUM.
Lim A.K., Kai T.;
Proc. Natl. Acad. Sci. U.S.A. 104:20143-20143(2007).
[17]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=19651888; DOI=10.1083/jcb.200904063;
Lim A.K., Tao L., Kai T.;
"piRNAs mediate posttranscriptional retroelement silencing and
localization to pi-bodies in the Drosophila germline.";
J. Cell Biol. 186:333-342(2009).
-!- FUNCTION: Probable ATP-binding RNA helicase which plays a central
role during spermatogenesis and oogenesis by repressing
transposable elements and preventing their mobilization, which is
essential for the germline integrity. Acts via the piRNA metabolic
process, which mediates the repression of transposable elements
during meiosis by forming complexes composed of piRNAs and Piwi
and govern the methylation and subsequent repression of
transposons. Involved in the repression of LTR retrotransposon
copia. Also involved in telomere regulation by repressing
specialized telomeric retroelements HeT-A, TAHRE, and TART;
Drosophila telomeres being maintained by transposition of
specialized telomeric retroelements. Involved in telomeric trans-
silencing, a repression mechanism by which a transposon or a
transgene inserted in subtelomeric heterochromatin has the
capacity to repress in trans in the female germline, a homologous
transposon, or transgene located in euchromatin. Involved in the
repression of testis-expressed Stellate genes by the homologous
Su(Ste) repeats. Required for anteroposterior and dorsoventral
axis formation during oogenesis. {ECO:0000269|PubMed:11470406,
ECO:0000269|PubMed:11513298, ECO:0000269|PubMed:12154120,
ECO:0000269|PubMed:14752161, ECO:0000269|PubMed:15254241,
ECO:0000269|PubMed:16452506, ECO:0000269|PubMed:16809489,
ECO:0000269|PubMed:17194939, ECO:0000269|PubMed:17428915,
ECO:0000269|PubMed:17603126, ECO:0000269|PubMed:17941712,
ECO:0000269|PubMed:19651888, ECO:0000269|PubMed:7590230}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Component of
the nuage, also named P granule, a germ-cell-specific organelle
required to repress transposon during meiosis. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Egg chambers for females lacking spn-E
display startmispositioned oocytes. At a low frequency, females
generate early egg chambers in which the oocyte is positioned
incorrectly within the cyst. At a high frequency, late-stage egg
chambers exhibit a ventralized chorion. Flies show transposable
elements derepression, an aberrant piRNA profile and a reduction
of H3 'Lys-9' methylation and delocalization of HP1 and HP2.
{ECO:0000269|PubMed:16809489, ECO:0000269|PubMed:19651888,
ECO:0000269|PubMed:7590230}.
-!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB35476.2; Type=Frameshift; Positions=531, 545; Evidence={ECO:0000305};
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EMBL; S79915; AAB35476.2; ALT_FRAME; mRNA.
EMBL; AE014297; AAF55235.1; -; Genomic_DNA.
EMBL; BT029921; ABM92795.1; -; mRNA.
EMBL; BT100306; ACZ52618.1; -; mRNA.
PIR; T13889; T13889.
RefSeq; NP_476741.1; NM_057393.4.
UniGene; Dm.21664; -.
ProteinModelPortal; Q9VF26; -.
SMR; Q9VF26; -.
BioGrid; 66977; 6.
IntAct; Q9VF26; 2.
STRING; 7227.FBpp0082637; -.
PaxDb; Q9VF26; -.
PRIDE; Q9VF26; -.
EnsemblMetazoa; FBtr0083183; FBpp0082637; FBgn0003483.
GeneID; 41919; -.
KEGG; dme:Dmel_CG3158; -.
UCSC; CG3158-RA; d. melanogaster.
CTD; 41919; -.
FlyBase; FBgn0003483; spn-E.
eggNOG; KOG0920; Eukaryota.
eggNOG; COG1643; LUCA.
GeneTree; ENSGT00760000119189; -.
InParanoid; Q9VF26; -.
KO; K18408; -.
OMA; DPCRTVY; -.
OrthoDB; EOG091G17CM; -.
PhylomeDB; Q9VF26; -.
GenomeRNAi; 41919; -.
PRO; PR:Q9VF26; -.
Proteomes; UP000000803; Chromosome 3R.
Bgee; FBgn0003483; Expressed in 17 organ(s), highest expression level in egg cell.
ExpressionAtlas; Q9VF26; baseline and differential.
Genevisible; Q9VF26; DM.
GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IDA:FlyBase.
GO; GO:0043186; C:P granule; IDA:FlyBase.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004004; F:ATP-dependent RNA helicase activity; IBA:GO_Central.
GO; GO:0004386; F:helicase activity; ISS:FlyBase.
GO; GO:0003723; F:RNA binding; IBA:GO_Central.
GO; GO:0003724; F:RNA helicase activity; TAS:FlyBase.
GO; GO:0008186; F:RNA-dependent ATPase activity; TAS:FlyBase.
GO; GO:0006342; P:chromatin silencing; IMP:FlyBase.
GO; GO:0046843; P:dorsal appendage formation; IMP:FlyBase.
GO; GO:0007294; P:germarium-derived oocyte fate determination; IGI:FlyBase.
GO; GO:0008298; P:intracellular mRNA localization; IMP:FlyBase.
GO; GO:0007076; P:mitotic chromosome condensation; IMP:FlyBase.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:FlyBase.
GO; GO:0010529; P:negative regulation of transposition; IMP:FlyBase.
GO; GO:0000335; P:negative regulation of transposition, DNA-mediated; IMP:FlyBase.
GO; GO:0030717; P:oocyte karyosome formation; IMP:FlyBase.
GO; GO:0030720; P:oocyte localization involved in germarium-derived egg chamber formation; IMP:FlyBase.
GO; GO:0001556; P:oocyte maturation; IMP:FlyBase.
GO; GO:0048477; P:oogenesis; IMP:FlyBase.
GO; GO:0009949; P:polarity specification of anterior/posterior axis; IMP:FlyBase.
GO; GO:0009951; P:polarity specification of dorsal/ventral axis; IMP:FlyBase.
GO; GO:0007315; P:pole plasm assembly; NAS:FlyBase.
GO; GO:0045451; P:pole plasm oskar mRNA localization; IMP:FlyBase.
GO; GO:0060213; P:positive regulation of nuclear-transcribed mRNA poly(A) tail shortening; IMP:FlyBase.
GO; GO:0007317; P:regulation of pole plasm oskar mRNA localization; IMP:FlyBase.
GO; GO:0016246; P:RNA interference; TAS:FlyBase.
GO; GO:0006403; P:RNA localization; TAS:FlyBase.
GO; GO:0006396; P:RNA processing; IBA:GO_Central.
GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
GO; GO:0030423; P:targeting of mRNA for destruction involved in RNA interference; IMP:FlyBase.
Gene3D; 2.40.50.90; -; 2.
InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
InterPro; IPR007502; Helicase-assoc_dom.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR035437; SNase_OB-fold_sf.
InterPro; IPR002999; Tudor.
InterPro; IPR013087; Znf_C2H2_type.
Pfam; PF00270; DEAD; 1.
Pfam; PF04408; HA2; 1.
Pfam; PF00271; Helicase_C; 1.
Pfam; PF00567; TUDOR; 1.
SMART; SM00487; DEXDc; 1.
SMART; SM00847; HA2; 1.
SMART; SM00490; HELICc; 1.
SMART; SM00333; TUDOR; 1.
SUPFAM; SSF52540; SSF52540; 2.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
PROSITE; PS50304; TUDOR; 1.
2: Evidence at transcript level;
ATP-binding; Complete proteome; Cytoplasm; Developmental protein;
Differentiation; Helicase; Hydrolase; Meiosis; Nucleotide-binding;
Oogenesis; Reference proteome; RNA-mediated gene silencing;
Spermatogenesis.
CHAIN 1 1434 Probable ATP-dependent RNA helicase
spindle-E.
/FTId=PRO_0000391916.
DOMAIN 125 292 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 354 526 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
DOMAIN 938 1001 Tudor. {ECO:0000255|PROSITE-
ProRule:PRU00211}.
NP_BIND 138 145 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
MOTIF 238 241 DEAH box.
CONFLICT 47 47 L -> M (in Ref. 1; AAB35476).
{ECO:0000305}.
CONFLICT 156 156 A -> G (in Ref. 1; AAB35476).
{ECO:0000305}.
CONFLICT 325 325 Q -> H (in Ref. 1; AAB35476).
{ECO:0000305}.
CONFLICT 326 326 V -> G (in Ref. 4; ABM92795).
{ECO:0000305}.
CONFLICT 401 401 R -> G (in Ref. 1; AAB35476).
{ECO:0000305}.
CONFLICT 542 542 N -> D (in Ref. 1; AAB35476).
{ECO:0000305}.
CONFLICT 668 668 S -> SAIRWAK (in Ref. 1; AAB35476).
{ECO:0000305}.
CONFLICT 1109 1110 QR -> HG (in Ref. 1; AAB35476).
{ECO:0000305}.
CONFLICT 1415 1415 L -> LQ (in Ref. 1; AAB35476).
{ECO:0000305}.
SEQUENCE 1434 AA; 164510 MW; 67E8CD39F1484B13 CRC64;
MDQEVMDFFD FSKELKRVAA APQGYISSDP RLMATKFKSS EVPNRELIGT DYVSKIVAKE
KCLLNGTLLN EQPQGKRIRT LDDLDTDDEG EETEIRRDDE YYKKFRFNLN RDKNLSIYAK
REEILAAINA HPVVIIKGET GCGKTTQVPQ YILDEAYKSG KYCNIVVTQP RRIAAISIAN
RVCQEREWQQ NTVCSFQVGL HRPNSLEDTR LLYCTTGVLL NNLINNKTLT HYTHIVLDEV
HERDQNMDFL LIVVRRLLAT NSRHVKIILM SATIDAKELS DYFTTTNSIP PVITTNHRRK
HSIEKFYRDQ LGSIIWNEED VGHQQVPEIN KHGYRAAVKI IVIIDNMERK AAIQSRQSYD
EALRYGAVLI FLPGIYEIDT MAENLTCMLE NDPNIKVSIV RCFSLMTPEN QRDVFNPPPP
GFRKIILTTN IAESSITVPD VSYVIDFCLA KVKVTDTASS FSSLRLTWAS KANCRQRAGR
VGRLRSGRVY RMVNKHFYQR EMPEFGIPEM LRLPLQNSVL KAKVLNMGSP VEILALALSP
PNLSDIHNTI LLLKEVGALY LTVDGIYDPL DGDLTYWGTI MSRLPLDTRQ SRLIILGYIF
NMLEEAIIIA AGLSTPGLFA HEGGRSQLGD SFWMHYIFSD GSGSDLVAIW RVYLTYLNIV
ENGHDQESAI RWAKRFHVSL RSLKEIHLLV QELRVRCTHL GLIPFPVNPN QMMDDREKAI
MLKVIIAGAF YPNYFTRSKE SCADTDRNIY QTISGHDPCR TVYFTNFKPA YMGELYTRRI
KELFQEVRIP PENMDVTFQE GSQKVFVTFK QDDWIEGSSK YVPVSGRVQS EVYKAVMMRQ
NRVERPIHIM NPSAFMSYVQ QRGIGDVIEG RWIPPTKPLN VELLALPSVF DKTISGSITC
IVNCGKFFFQ PQSFEECIRN MSEIFNAPQQ LRNYVTNASA IAKGMMVLAK RDSYFQRATV
IRPENQSNRQ PMFYVRFIDY GNCTLLPMQL MRLMPRELTE QYGDLPPRVF ECRLAMVQPS
SVVSGNNRWS TAANDMLKTV AQCGLIDIEV YSLFNNVAAV LIHMRDGIIN DKLVELMLCR
RSDEDYMSRK DHDFRLRRQE SARNLSTAQR QQINEEYLRS CQLPQDHDLP PPPLEKCKTV
VMLKGPNSPL ECTMRSITRV GLSKRVNIDH LSVNALLLDA DPQDHHDHLI VAHEIAESRN
GQTLTARGTT LMPNVQGFGA LMVMLFSPTM QLKCNKEGTS YVSVLGGLGC DPDTNEPYFA
EHDVLINLDV NILEDDVILI NQIRYYIDSV FFNFKEENNP AVSVNERVSI YTQLRSLINR
LLCKDRRYIE RNMSNADFEW ETNPELPLPN EPFGKRAIFP MHSLTELQEE DTGRLVQLRE
NCSMLHKWRN FEGTLPHMTC KLCNQLLESV PQLRLHLLTI LHRDREKQID YCNQ


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EIAAB10824 ATP-dependent 61 kDa nucleolar RNA helicase,DDX21,DDX56,DEAD box protein 21,DEAD box protein 56,Homo sapiens,Human,NOH61,Probable ATP-dependent RNA helicase DDX56
EIAAB10797 Ddx46,DEAD box protein 46,Hel117,Helicase of 117.4 kDa,Probable ATP-dependent RNA helicase DDX46,Rat,Rattus norvegicus
EIAAB10805 DDX5,DEAD box protein 5,G17P1,HELR,HLR1,Homo sapiens,Human,Probable ATP-dependent RNA helicase DDX5,RNA helicase p68
EIAAB10759 DDX17,DEAD box protein 17,DEAD box protein p72,Homo sapiens,Human,Probable ATP-dependent RNA helicase DDX17,RNA-dependent helicase p72
EIAAB11227 Ddx36,DEAH box protein 36,Dhx36,Kiaa1488,Mlel1,MLE-like protein 1,Mouse,Mus musculus,Probable ATP-dependent RNA helicase DHX36,RNA helicase associated with AU-rich element ARE
EIAAB11226 DDX36,DEAH box protein 36,DHX36,Homo sapiens,Human,KIAA1488,MLEL1,MLE-like protein 1,Probable ATP-dependent RNA helicase DHX36,RHAU,RNA helicase associated with AU-rich element ARE
E1319m Rat ELISA Kit FOR Probable ATP-dependent RNA helicase DDX59 96T
E0879c Pig ELISA Kit FOR Probable ATP-dependent RNA helicase DDX58 96T
E12958m Pig ELISA Kit FOR Probable ATP-dependent RNA helicase DDX4 96T
E1313h Rat ELISA Kit FOR Probable ATP-dependent RNA helicase DHX40 96T
E1463b Human ELISA Kit FOR Probable ATP-dependent RNA helicase DHX37 96T
DDX17_HUMAN Human ELISA Kit FOR Probable ATP-dependent RNA helicase DDX17 96T


 

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