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DDX51_MOUSE
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   03-AUG-2022, entry version 133.
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; 2.
DR   STRING; 10090.ENSMUSP00000031478; -.
DR   iPTMnet; Q6P9R1; -.
DR   PhosphoSitePlus; Q6P9R1; -.
DR   EPD; Q6P9R1; -.
DR   jPOST; Q6P9R1; -.
DR   MaxQB; Q6P9R1; -.
DR   PaxDb; Q6P9R1; -.
DR   PeptideAtlas; Q6P9R1; -.
DR   PRIDE; Q6P9R1; -.
DR   ProteomicsDB; 277970; -.
DR   Antibodypedia; 32048; 121 antibodies from 23 providers.
DR   DNASU; 69663; -.
DR   Ensembl; ENSMUST00000031478; ENSMUSP00000031478; ENSMUSG00000029504.
DR   GeneID; 69663; -.
DR   KEGG; mmu:69663; -.
DR   UCSC; uc008yre.2; mouse.
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; 973872at2759; -.
DR   PhylomeDB; Q6P9R1; -.
DR   BioGRID-ORCS; 69663; 28 hits in 75 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 251 other 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   Gene3D; 3.40.50.300; -; 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   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 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
 
 
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