Legends: 1, BINDING ATP; via carbonyl oxygen. {ECO:0000250}; 2, BINDING ATP. {ECO:0000250}; 3, Phosphoserine. {ECO:0000250|UniProtKB:Q9UHI6}; 4, Phosphoserine. {ECO:0000244|PubMed:21183079}; 5, Phosphothreonine. {ECO:0000250|UniProtKB:Q9UHI6}; 6, CONFLICT A -> T (in Ref. 2; AAF76301). {ECO:0000305}; 7, CONFLICT P -> R (in Ref. 2; AAF76301). {ECO:0000305}; 8, CONFLICT Q -> H (in Ref. 1; CAB86201). {ECO:0000305}; 9, CONFLICT V -> I (in Ref. 2; AAF76301). {ECO:0000305}; 10, Helicase ATP-binding. {ECO:0000255|PROSITE-ProRule:PRU00541}; 11, Helicase C-terminal. {ECO:0000255|PROSITE-ProRule:PRU00542}; 12, NP_BIND ATP. {ECO:0000255|PROSITE- ProRule:PRU00541}; 13, MOTIF Q motif; 14, MOTIF DEAD box; 15, iprf:HELICASE_CTER [T]; 16, ipat:DEAD_ATP_HELICASE [T]; 17, ismart:HELICc [T]; 18, iprf:HELICASE_ATP_BIND_1 [T]; 19, ipfam:Helicase_C [T]; 20, iprf:Q_MOTIF [T].
|
ID DDX20_MOUSE Reviewed; 825 AA.
AC Q9JJY4; Q059Z6; Q9JIK4;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 10-MAY-2017, entry version 158.
DE RecName: Full=Probable ATP-dependent RNA helicase DDX20;
DE EC=3.6.4.13;
DE AltName: Full=Component of gems 3;
DE AltName: Full=DEAD box protein 20;
DE AltName: Full=DEAD box protein DP 103;
DE AltName: Full=Gemin-3;
DE AltName: Full=Regulator of steroidogenic factor 1;
DE Short=ROSF-1;
GN Name=Ddx20; Synonyms=Dp103, Gemin3;
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 [MRNA], AND INTERACTION WITH SMN1.
RX PubMed=10767334; DOI=10.1093/hmg/9.7.1093;
RA Campbell L., Hunter K.M., Mohaghegh P., Tinsley J.M., Brasch M.A.,
RA Davies K.E.;
RT "Direct interaction of Smn with dp103, a putative RNA helicase: a role
RT for Smn in transcription regulation?";
RL Hum. Mol. Genet. 9:1093-1100(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Testis;
RX PubMed=11145740; DOI=10.1210/mend.15.1.0580;
RA Ou Q., Mouillet J.F., Yan X., Dorn C., Crawford P.A., Sadovsky Y.;
RT "The DEAD box protein DP103 is a regulator of steroidogenic factor-
RT 1.";
RL Mol. Endocrinol. 15:69-79(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
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 [5]
RP INTERACTION WITH FOXL2.
RX PubMed=16153597; DOI=10.1016/j.bbrc.2005.08.184;
RA Lee K., Pisarska M.D., Ko J.J., Kang Y., Yoon S., Ryou S.M., Cha K.Y.,
RA Bae J.;
RT "Transcriptional factor FOXL2 interacts with DP103 and induces
RT apoptosis.";
RL Biochem. Biophys. Res. Commun. 336:876-881(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-472, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas, 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: The SMN complex plays a catalyst role in the assembly of
CC small nuclear ribonucleoproteins (snRNPs), the building blocks of
CC the spliceosome. Thereby, plays an important role in the splicing
CC of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common
CC set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and
CC SNRPG that assemble in a heptameric protein ring on the Sm site of
CC the small nuclear RNA to form the core snRNP. In the cytosol, the
CC Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in
CC an inactive 6S pICln-Sm complex by the chaperone CLNS1A that
CC controls the assembly of the core snRNP. Dissociation by the SMN
CC complex of CLNS1A from the trapped Sm proteins and their transfer
CC to an SMN-Sm complex triggers the assembly of core snRNPs and
CC their transport to the nucleus. May also play a role in the
CC metabolism of small nucleolar ribonucleoprotein (snoRNPs) (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC -!- SUBUNIT: Part of the core SMN complex that contains SMN1,
CC GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8
CC and STRAP/UNRIP. Part of the SMN-Sm complex that contains SMN1,
CC GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8,
CC STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3,
CC SNRPE, SNRPF and SNRPG. Interacts directly with GEMIN5. Interacts
CC directly with SNUPN. Interacts with PPP4R2. Interacts with FOXL2.
CC Interacts with NANOS1 and PUM2. {ECO:0000269|PubMed:10767334,
CC ECO:0000269|PubMed:16153597}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus, gem. Note=Localized in
CC subnuclear structures next to coiled bodies, called Gemini of
CC Cajal bodies (Gems).
CC -!- SIMILARITY: Belongs to the DEAD box helicase family.
CC {ECO:0000305}.
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DR EMBL; AJ250027; CAB86201.1; -; mRNA.
DR EMBL; AF220454; AAF76301.1; -; mRNA.
DR EMBL; CH466608; EDL07549.1; -; Genomic_DNA.
DR EMBL; BC125471; AAI25472.1; -; mRNA.
DR EMBL; BC137721; AAI37722.1; -; mRNA.
DR CCDS; CCDS38581.1; -.
DR RefSeq; NP_059093.3; NM_017397.3.
DR RefSeq; XP_006501764.1; XM_006501701.3.
DR UniGene; Mm.272826; -.
DR ProteinModelPortal; Q9JJY4; -.
DR SMR; Q9JJY4; -.
DR BioGrid; 207545; 6.
DR IntAct; Q9JJY4; 1.
DR STRING; 10090.ENSMUSP00000088176; -.
DR iPTMnet; Q9JJY4; -.
DR PhosphoSitePlus; Q9JJY4; -.
DR EPD; Q9JJY4; -.
DR MaxQB; Q9JJY4; -.
DR PaxDb; Q9JJY4; -.
DR PeptideAtlas; Q9JJY4; -.
DR PRIDE; Q9JJY4; -.
DR Ensembl; ENSMUST00000090680; ENSMUSP00000088176; ENSMUSG00000027905.
DR GeneID; 53975; -.
DR KEGG; mmu:53975; -.
DR UCSC; uc008qva.1; mouse.
DR CTD; 11218; -.
DR MGI; MGI:1858415; Ddx20.
DR eggNOG; KOG4284; Eukaryota.
DR eggNOG; COG0513; LUCA.
DR GeneTree; ENSGT00530000062880; -.
DR HOGENOM; HOG000112184; -.
DR HOVERGEN; HBG051330; -.
DR InParanoid; Q9JJY4; -.
DR KO; K13131; -.
DR OMA; KSHSECG; -.
DR OrthoDB; EOG091G0461; -.
DR TreeFam; TF101524; -.
DR Reactome; R-MMU-191859; snRNP Assembly.
DR PRO; PR:Q9JJY4; -.
DR Proteomes; UP000000589; Chromosome 3.
DR Bgee; ENSMUSG00000027905; -.
DR CleanEx; MM_DDX20; -.
DR ExpressionAtlas; Q9JJY4; baseline and differential.
DR Genevisible; Q9JJY4; MM.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0097504; C:Gemini of coiled bodies; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0090571; C:RNA polymerase II transcription repressor complex; IDA:BHF-UCL.
DR GO; GO:0032797; C:SMN complex; ISS:UniProtKB.
DR GO; GO:0034719; C:SMN-Sm protein complex; ISS:UniProtKB.
DR GO; GO:0017053; C:transcriptional repressor complex; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004004; F:ATP-dependent RNA helicase activity; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042826; F:histone deacetylase binding; IPI:BHF-UCL.
DR GO; GO:0030674; F:protein binding, bridging; IDA:BHF-UCL.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0070491; F:repressing transcription factor binding; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR GO; GO:0048477; P:oogenesis; IMP:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0050810; P:regulation of steroid biosynthetic process; IMP:MGI.
DR GO; GO:0010501; P:RNA secondary structure unwinding; IBA:GO_Central.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; ISS:UniProtKB.
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 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; 1.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
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 ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Helicase;
KW Hydrolase; mRNA processing; mRNA splicing; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1 825 Probable ATP-dependent RNA helicase
FT DDX20.
FT /FTId=PRO_0000055026.
FT DOMAIN 94 265 Helicase ATP-binding.
FT {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT DOMAIN 300 449 Helicase C-terminal.
FT {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT NP_BIND 107 114 ATP. {ECO:0000255|PROSITE-
FT ProRule:PRU00541}.
FT NP_BIND 110 115 ATP. {ECO:0000255|PROSITE-
FT ProRule:PRU00541}.
FT MOTIF 63 91 Q motif.
FT MOTIF 212 215 DEAD box.
FT BINDING 85 85 ATP; via carbonyl oxygen. {ECO:0000250}.
FT BINDING 90 90 ATP. {ECO:0000250}.
FT MOD_RES 188 188 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q9UHI6}.
FT MOD_RES 270 270 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q9UHI6}.
FT MOD_RES 472 472 Phosphoserine.
FT {ECO:0000244|PubMed:21183079}.
FT MOD_RES 501 501 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q9UHI6}.
FT MOD_RES 506 506 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q9UHI6}.
FT MOD_RES 552 552 Phosphothreonine.
FT {ECO:0000250|UniProtKB:Q9UHI6}.
FT MOD_RES 561 561 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q9UHI6}.
FT MOD_RES 653 653 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q9UHI6}.
FT MOD_RES 655 655 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q9UHI6}.
FT MOD_RES 657 657 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q9UHI6}.
FT MOD_RES 673 673 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q9UHI6}.
FT MOD_RES 678 678 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q9UHI6}.
FT MOD_RES 679 679 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q9UHI6}.
FT MOD_RES 689 689 Phosphothreonine.
FT {ECO:0000250|UniProtKB:Q9UHI6}.
FT MOD_RES 706 706 Phosphothreonine.
FT {ECO:0000250|UniProtKB:Q9UHI6}.
FT CONFLICT 5 5 A -> T (in Ref. 2; AAF76301).
FT {ECO:0000305}.
FT CONFLICT 9 9 P -> R (in Ref. 2; AAF76301).
FT {ECO:0000305}.
FT CONFLICT 226 226 Q -> H (in Ref. 1; CAB86201).
FT {ECO:0000305}.
FT CONFLICT 468 468 V -> I (in Ref. 2; AAF76301).
FT {ECO:0000305}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 300 449 iprf:HELICASE_CTER [T]
FT MYHIT 88 250 ipfam:DEAD [T]
FT MYHIT 210 218 ipat:DEAD_ATP_HELICASE [T]
FT MYHIT 324 405 ismart:HELICc [T]
FT MYHIT 94 265 iprf:HELICASE_ATP_BIND_1 [T]
FT MYHIT 296 405 ipfam:Helicase_C [T]
FT MYHIT 63 91 iprf:Q_MOTIF [T]
FT MYHIT 82 280 ismart:DEXDc [T]
SQ SEQUENCE 825 AA; 91710 MW; B5BCD0754D4075C3 CRC64;
MAAAAFEVPA ALTTSESTMA AERAAAPVQA VEPTPASPWT QRTAHDIGGP RTRTGDVVLA
EPADFESLLL SRPVLEGLRA AGFERPSPVQ LKAIPLGRCG LDLIVQAKSG TGKTCVFSTI
ALDSLILENY STQILILAPT REIAVQIHSV ITAIGIKMEG LECHVFIGGT PLSQDKTRLK
KCHIAVGSPG RIKQLIELDY LNPGSIRLFI LDEADKLLEE GSFQEQINWI YSSLPASKQM
LAVSATYPEV LANALTRYMR DPTFVRLNPS DPSLIGLKQY YQVVNSYPLA HKIFEEKTQH
LQELFSKVPF NQALVFSNLH SRAQHLADIL SSKGFPTECI SGNMNQNQRL DAMAKLKQFH
CRVLISTDLT SRGIDAEKVN LVVNLDVPLD WETYMHRIGR AGRFGTLGLT VTYCCRGEEE
NMMMKIAQKC NINLLPLPDP IPPGLMEECL NWDVEVKAAM HTYSSPTVAT QSPKKQVQKL
ERAFQSQRTP GNQTPSPRNT SASALSARPK HSKPKLPVKS HSECGVLEKA APPQESGCPA
QLEEQVKNSV QTSVEDSSSN SQHQAKDSSP GSLPKIPCLS SFKVHQPSTL TFAELVDDYE
HYIKEGLEKP VEIIRHYTGP EAQTGNPQNG FVRNRVSEDR AQMLVSSSQS GDSESDSDSC
SSRTSSQSKG NKSYLEGSSD TQLKDTECTP VGGPLSLEQV QNGNDTPTQV EYQEAPETQV
KARHKEGANQ RSKQSRRNPA RRSSYRVQSE PQEESWYDCH RETTASFSDT YQDYEEYWRA
YYRAWQEYYA AASHSYYWNA QRHPSWMAAY HMNTVYLQEM MRGNQ
//
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