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Database: UniProt
Entry: Q6P9R1
LinkDB: Q6P9R1
Original site: Q6P9R1 
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   16-OCT-2019, entry version 119.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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
RT   project: 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
RT   expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: ATP-binding RNA helicase involved in the biogenesis of
CC       60S 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
CC       box family of RNA helicases and controls ATP binding and
CC       hydrolysis.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX51/DBP6
CC       subfamily. {ECO:0000305}.
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   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   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   eggNOG; KOG0350; Eukaryota.
DR   eggNOG; ENOG410XRWM; LUCA.
DR   GeneTree; ENSGT00550000075141; -.
DR   HOGENOM; HOG000239572; -.
DR   InParanoid; Q6P9R1; -.
DR   KO; K14807; -.
DR   OMA; CHIRALV; -.
DR   OrthoDB; 973872at2759; -.
DR   PhylomeDB; Q6P9R1; -.
DR   ChiTaRS; Ddx51; mouse.
DR   PRO; PR:Q6P9R1; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   Bgee; ENSMUSG00000029504; Expressed in 285 organ(s), highest expression level in primary oocyte.
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:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
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; Complete proteome; Helicase; Hydrolase;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Ribosome biogenesis; RNA-binding; rRNA processing.
FT   INIT_MET      1      1       Removed. {ECO:0000250|UniProtKB:Q8N8A6}.
FT   CHAIN         2    639       ATP-dependent RNA helicase DDX51.
FT                                /FTId=PRO_0000228097.
FT   DOMAIN      215    424       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      467    615       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     228    235       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       193    201       Q motif.
FT   MOTIF       343    346       DEAD box.
FT   COMPBIAS     27     92       Arg-rich.
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {ECO:0000250|UniProtKB:Q8N8A6}.
FT   MOD_RES      79     79       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     432    432       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   CONFLICT    639    639       A -> D (in Ref. 1; BAE31347).
FT                                {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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