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DDX56_MOUSE
ID   DDX56_MOUSE             Reviewed;         546 AA.
AC   Q9D0R4;
DT   23-JAN-2002, 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 DDX56;
DE            EC=3.6.4.13;
DE   AltName: Full=ATP-dependent 61 kDa nucleolar RNA helicase;
DE   AltName: Full=DEAD box protein 56;
GN   Name=Ddx56; Synonyms=D11Ertd619e, Noh61;
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=Embryo;
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=Salivary gland;
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).
CC   -!- FUNCTION: May play a role in later stages of the processing of the pre-
CC       ribosomal particles leading to mature 60S ribosomal subunits. Has
CC       intrinsic ATPase activity (By similarity). {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   -!- SUBUNIT: May form homooligomeric complexes.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX56/DBP9
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AK011136; BAB27426.1; -; mRNA.
DR   EMBL; AK077514; BAC36839.1; -; mRNA.
DR   EMBL; BC018291; AAH18291.1; -; mRNA.
DR   CCDS; CCDS24414.1; -.
DR   RefSeq; NP_080814.1; NM_026538.3.
DR   AlphaFoldDB; Q9D0R4; -.
DR   SMR; Q9D0R4; -.
DR   BioGRID; 206632; 4.
DR   CORUM; Q9D0R4; -.
DR   IntAct; Q9D0R4; 1.
DR   STRING; 10090.ENSMUSP00000004507; -.
DR   iPTMnet; Q9D0R4; -.
DR   PhosphoSitePlus; Q9D0R4; -.
DR   EPD; Q9D0R4; -.
DR   MaxQB; Q9D0R4; -.
DR   PaxDb; Q9D0R4; -.
DR   PRIDE; Q9D0R4; -.
DR   ProteomicsDB; 279182; -.
DR   Antibodypedia; 13419; 357 antibodies from 27 providers.
DR   DNASU; 52513; -.
DR   Ensembl; ENSMUST00000004507; ENSMUSP00000004507; ENSMUSG00000004393.
DR   GeneID; 52513; -.
DR   KEGG; mmu:52513; -.
DR   UCSC; uc007hyc.1; mouse.
DR   CTD; 54606; -.
DR   MGI; MGI:1277172; Ddx56.
DR   VEuPathDB; HostDB:ENSMUSG00000004393; -.
DR   eggNOG; KOG0346; Eukaryota.
DR   GeneTree; ENSGT00550000074946; -.
DR   HOGENOM; CLU_003041_17_1_1; -.
DR   InParanoid; Q9D0R4; -.
DR   OMA; GYEKDFK; -.
DR   OrthoDB; 973872at2759; -.
DR   PhylomeDB; Q9D0R4; -.
DR   TreeFam; TF300620; -.
DR   BioGRID-ORCS; 52513; 24 hits in 75 CRISPR screens.
DR   ChiTaRS; Ddx56; mouse.
DR   PRO; PR:Q9D0R4; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q9D0R4; protein.
DR   Bgee; ENSMUSG00000004393; Expressed in otic placode and 250 other tissues.
DR   ExpressionAtlas; Q9D0R4; baseline and differential.
DR   Genevisible; Q9D0R4; MM.
DR   GO; GO:0005730; C:nucleolus; IDA:MGI.
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:0010976; P:positive regulation of neuron projection development; ISO:MGI.
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; IPR014014; RNA_helicase_DEAD_Q_motif.
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; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Ribosome biogenesis; RNA-binding;
KW   rRNA processing.
FT   CHAIN           1..546
FT                   /note="Probable ATP-dependent RNA helicase DDX56"
FT                   /id="PRO_0000055059"
FT   DOMAIN          38..218
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          230..424
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          324..344
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          508..546
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           7..35
FT                   /note="Q motif"
FT   MOTIF           166..169
FT                   /note="DEAD box"
FT   BINDING         51..58
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOD_RES         126
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NY93"
FT   MOD_RES         141
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NY93"
SQ   SEQUENCE   546 AA;  61212 MW;  3C19F7354C29F9A1 CRC64;
     MEDQEALGFE HMGLDPRLLQ AVTDLGWSRP TLIQEKAIPL ALEGKDLLAR ARTGSGKTAA
     YAIPMLQSLL HKKATGPVME QAVRGLVLVP TKELARQAQA MIQQLAAYCA RDVRVANVSA
     AEDSASQRAV LMEKPDVVVG TPSRVLSHLQ QNTLKLRDSL ELLVVDEADL LFSFGFEDEL
     KSLLCHLPRI YQAFLMSATF NEDVQTLKEL VLHNPVTLKL QESQLPGPDQ LQQFQVVCET
     EEDKFLLLYA LLKLSLIRGK ALLFVNTLER GYRLRLFLEQ FSIPSCVLNG ELPLRSRCHI
     ISQFNQGLYD CVIATDAEIL GPQVKGKRRG RGSKGNKASD PESGVARGID FHHVSAVLNF
     DLPPTAEAYV HRAGRTARAN NPGIVLTFVL PAEQPFLGKI EDLLSGEGEA PILLPYQFQM
     EEIESFRYRC RDAMRSVTKQ AIREARLKEI KEELLHSEKL KTYFEDNPRD LQLLRHDLPL
     HPAVVKPHLG HVPDYLVPAA LRGLVHPRKK RRKVPFSRKA KKVKAQNPLR DFKHRGKKPK
     PAAKPS
 
 
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