DDX59_MOUSE
ID DDX59_MOUSE Reviewed; 619 AA.
AC Q9DBN9; Q8C667; Q9CSD1;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Probable ATP-dependent RNA helicase DDX59;
DE EC=3.6.4.13;
DE AltName: Full=DEAD box protein 59;
DE AltName: Full=Zinc finger HIT domain-containing protein 5 {ECO:0000250|UniProtKB:Q5T1V6};
GN Name=Ddx59; Synonyms=Znhit5 {ECO:0000250|UniProtKB:Q5T1V6};
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Head, and Lung;
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=FVB/N; TISSUE=Mammary tumor;
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-160, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
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).
RN [4]
RP DEVELOPMENTAL STAGE.
RX PubMed=23972372; DOI=10.1016/j.ajhg.2013.07.012;
RA Shamseldin H.E., Rajab A., Alhashem A., Shaheen R., Al-Shidi T., Alamro R.,
RA Al Harassi S., Alkuraya F.S.;
RT "Mutations in DDX59 implicate RNA helicase in the pathogenesis of
RT orofaciodigital syndrome.";
RL Am. J. Hum. Genet. 93:555-560(2013).
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 -!- SUBUNIT: Interacts (via HIT-type zinc finger) with the RUVBL1/RUVBL2
CC complex in the presence of ADP. {ECO:0000250|UniProtKB:Q5T1V6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q5T1V6}. Nucleus
CC {ECO:0000250|UniProtKB:Q5T1V6}. Note=Exhibits granular localization in
CC the nucleus, as well as in the cytoplasm.
CC {ECO:0000250|UniProtKB:Q5T1V6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9DBN9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9DBN9-2; Sequence=VSP_026429, VSP_026430;
CC -!- DEVELOPMENTAL STAGE: AT 11.5 dpc, expressed in the developing snout
CC region, eye and limb buds. At 13.5 dpc, highly enriched in the lips,
CC palatal shelves (secondary palate), and developing limb buds.
CC {ECO:0000269|PubMed:23972372}.
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. DDX59 subfamily.
CC {ECO:0000305}.
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DR EMBL; AK004833; BAB23601.1; -; mRNA.
DR EMBL; AK013179; BAB28694.1; -; mRNA.
DR EMBL; AK076462; BAC36354.1; -; mRNA.
DR EMBL; BC023840; AAH23840.1; -; mRNA.
DR CCDS; CCDS15326.1; -. [Q9DBN9-1]
DR RefSeq; NP_080776.1; NM_026500.3. [Q9DBN9-1]
DR AlphaFoldDB; Q9DBN9; -.
DR SMR; Q9DBN9; -.
DR STRING; 10090.ENSMUSP00000027655; -.
DR iPTMnet; Q9DBN9; -.
DR PhosphoSitePlus; Q9DBN9; -.
DR EPD; Q9DBN9; -.
DR jPOST; Q9DBN9; -.
DR MaxQB; Q9DBN9; -.
DR PaxDb; Q9DBN9; -.
DR PeptideAtlas; Q9DBN9; -.
DR PRIDE; Q9DBN9; -.
DR ProteomicsDB; 279856; -. [Q9DBN9-1]
DR ProteomicsDB; 279857; -. [Q9DBN9-2]
DR Antibodypedia; 34489; 263 antibodies from 22 providers.
DR DNASU; 67997; -.
DR Ensembl; ENSMUST00000027655; ENSMUSP00000027655; ENSMUSG00000026404. [Q9DBN9-1]
DR GeneID; 67997; -.
DR KEGG; mmu:67997; -.
DR UCSC; uc007cut.1; mouse. [Q9DBN9-2]
DR UCSC; uc007cuu.2; mouse. [Q9DBN9-1]
DR CTD; 83479; -.
DR MGI; MGI:1915247; Ddx59.
DR VEuPathDB; HostDB:ENSMUSG00000026404; -.
DR eggNOG; KOG0331; Eukaryota.
DR GeneTree; ENSGT00940000158639; -.
DR HOGENOM; CLU_003041_1_5_1; -.
DR InParanoid; Q9DBN9; -.
DR OMA; DESFCIR; -.
DR OrthoDB; 400908at2759; -.
DR PhylomeDB; Q9DBN9; -.
DR TreeFam; TF330866; -.
DR BioGRID-ORCS; 67997; 25 hits in 79 CRISPR screens.
DR ChiTaRS; Ddx59; mouse.
DR PRO; PR:Q9DBN9; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9DBN9; protein.
DR Bgee; ENSMUSG00000026404; Expressed in saccule of membranous labyrinth and 249 other tissues.
DR Genevisible; Q9DBN9; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
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; IPR014014; RNA_helicase_DEAD_Q_motif.
DR InterPro; IPR007529; Znf_HIT.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF04438; zf-HIT; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytoplasm; Helicase; Hydrolase;
KW Isopeptide bond; Metal-binding; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..619
FT /note="Probable ATP-dependent RNA helicase DDX59"
FT /id="PRO_0000282714"
FT DOMAIN 234..405
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 416..579
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT ZN_FING 104..133
FT /note="HIT-type"
FT REGION 1..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 583..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 203..231
FT /note="Q motif"
FT MOTIF 353..356
FT /note="DEAD box"
FT COMPBIAS 9..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 247..254
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T1V6"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 26
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5T1V6"
FT VAR_SEQ 269..292
FT /note="DKTPSALILTPTRELAIQIERQAK -> VIYQSDMSSSLKQTRDLPSFIVCN
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_026429"
FT VAR_SEQ 293..619
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_026430"
FT CONFLICT 208
FT /note="C -> S (in Ref. 1; BAB28694)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 619 AA; 68234 MW; E4FE6E723D125697 CRC64;
MFVPRSLKIK RSSNDDLKSG EAKKSKPEAG GLQVEGDRDT PVHTSVTEEA VTADKPGHAS
STNSPSCQLA EVSSTGPDEG VKDSHPSEEP VKSFSKTQRW PEPGEPVCVV CGRYGEYICD
KTDEDVCSLE CKAKHLLQVK EGEGSLRPSS PQRVAAEPES PLDAFYVYKE HPFIVTLKED
QIETLKQQLG ISVQGQDVAR PIIDFEHCGF PETLNQNLKK SGYEVPTPIQ MQMIPVGLLG
RDILASADTG SGKTAAFLLP VIIRAFSEDK TPSALILTPT RELAIQIERQ AKELMSGLPR
MKTVLLVGGL PLPPQLYRLR QHVKVIIATP GRLLDIIKQS SVSLSGIKIV VVDEADTMLK
MGFQQQVLDV LEHTPGDCQT ILVSATIPDS IEQLTDQLLH NPVRIITGDK NLPCASVRQI
ILWVEDPAKK KKLFEILNDQ KLFKPPVLVF VDCKLGADLL SEAVQKITGL NSTSIHSEKS
QVERRDILKG LLEGDYEVVV STGVLGRGLD LVNVKLVVNF DMPSSMDEYV HQVGRVGRLG
QNGTAITFIN NNSKRLFWDV AKRVKPTGSI LPPQLLNSPY LHEQKRKEQQ KDRQTQNSLV
TGANLMDIIR KHEKSSSQK
