ID DDX51_MOUSE Reviewed; 639 AA.
AC Q6P9R1; Q3U7M2;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 24-JAN-2024, entry version 140.
DE RecName: Full=ATP-dependent RNA helicase DDX51;
DE EC=3.6.4.13;
DE AltName: Full=DEAD box protein 51;
GN Name=Ddx51;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79 AND SER-432, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: ATP-binding RNA helicase involved in the biogenesis of 60S
CC ribosomal subunits. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC family of RNA helicases and controls ATP binding and hydrolysis.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX51/DBP6
CC subfamily. {ECO:0000305}.
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DR EMBL; AK152599; BAE31347.1; -; mRNA.
DR EMBL; BC060646; AAH60646.1; -; mRNA.
DR CCDS; CCDS19528.1; -.
DR RefSeq; NP_081432.2; NM_027156.3.
DR AlphaFoldDB; Q6P9R1; -.
DR SMR; Q6P9R1; -.
DR BioGRID; 213598; 3.
DR STRING; 10090.ENSMUSP00000031478; -.
DR iPTMnet; Q6P9R1; -.
DR PhosphoSitePlus; Q6P9R1; -.
DR EPD; Q6P9R1; -.
DR jPOST; Q6P9R1; -.
DR MaxQB; Q6P9R1; -.
DR PaxDb; 10090-ENSMUSP00000031478; -.
DR PeptideAtlas; Q6P9R1; -.
DR ProteomicsDB; 277970; -.
DR Pumba; Q6P9R1; -.
DR Antibodypedia; 32048; 141 antibodies from 24 providers.
DR DNASU; 69663; -.
DR Ensembl; ENSMUST00000031478.6; ENSMUSP00000031478.6; ENSMUSG00000029504.6.
DR GeneID; 69663; -.
DR KEGG; mmu:69663; -.
DR UCSC; uc008yre.2; mouse.
DR AGR; MGI:1916913; -.
DR CTD; 317781; -.
DR MGI; MGI:1916913; Ddx51.
DR VEuPathDB; HostDB:ENSMUSG00000029504; -.
DR eggNOG; KOG0350; Eukaryota.
DR GeneTree; ENSGT00550000075141; -.
DR HOGENOM; CLU_003041_15_3_1; -.
DR InParanoid; Q6P9R1; -.
DR OMA; TEQYCVT; -.
DR OrthoDB; 5476171at2759; -.
DR PhylomeDB; Q6P9R1; -.
DR BioGRID-ORCS; 69663; 28 hits in 81 CRISPR screens.
DR ChiTaRS; Ddx51; mouse.
DR PRO; PR:Q6P9R1; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q6P9R1; Protein.
DR Bgee; ENSMUSG00000029504; Expressed in epiblast (generic) and 255 other cell types or tissues.
DR ExpressionAtlas; Q6P9R1; baseline and differential.
DR Genevisible; Q6P9R1; MM.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR CDD; cd17956; DEADc_DDX51; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR PANTHER; PTHR24031:SF68; ATP-DEPENDENT RNA HELICASE DDX51; 1.
DR PANTHER; PTHR24031; RNA HELICASE; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Ribosome biogenesis; RNA-binding;
KW rRNA processing.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8N8A6"
FT CHAIN 2..639
FT /note="ATP-dependent RNA helicase DDX51"
FT /id="PRO_0000228097"
FT DOMAIN 215..424
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 467..615
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 193..201
FT /note="Q motif"
FT MOTIF 343..346
FT /note="DEAD box"
FT COMPBIAS 33..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 228..235
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q8N8A6"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 639
FT /note="A -> D (in Ref. 1; BAE31347)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 639 AA; 70368 MW; 44127413841C6AAB CRC64;
MALFHIARYA GPEAAGQGDT DAEAGSRARV LLERLQNRAR ERQQREPELE TTGTAGEGEA
AAAGKRRRRP RRRRRVSGSA TPNSEAPRAK RRKADKDVDA GRGEEAPEEL SAGAEDPGAN
PQEDVQRPPA PGRVLGDFAR RKTPKVQPFL PAWLAKPSCV KKSVTEDLTP IEDIPEVHPD
LQKQLRANGI TSYFPVQAAV IPALLESADH GFLIGRGGYQ PSDLCVSAPT GSGKTLAFVI
PVVQALLHRV VCHIRALVVL PTKELAQQVS KVFNIYTDTT PLRVALVTGQ KSLAKEQESL
VQKTADGFRC LADIVVATPG RLVDHIDQTP GFSLQQLRFL IIDEADRMID SMHQSWLPRV
VAAAFYSEGP TGSCALLQRT QPQALTAAST CVPQMPLQKL LFSATLTQDP EKLQRLGLYQ
PRLFSTRLGQ QSPKDTAEVD ENSGKYTFPV GLTHHYVPCR LSSKPLIVLH LVLRMSCSRA
LCFTNSRENS HRLYLLAQAF GGVSVAEFSS RYGPGQRKKI LKQFEQGKIQ LLISTDATAR
GIDVQGVELV INYDAPQYLR TYVHRVGRTA RAGKTGQAFT LLLKVQERKF LQMVSEAGVP
ELTHHEIPRK LLQPLVARYE TALSQLEKTV KEEQKLKAA
//
