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Protein

Probable ATP-dependent RNA helicase DDX20

Gene

Ddx20

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The SMN complex plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus. May also play a role in the metabolism of small nucleolar ribonucleoprotein (snoRNPs) (By similarity).By similarity

Catalytic activityi

ATP + H2O = ADP + phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei85 – 851ATP; via carbonyl oxygenBy similarity
Binding sitei90 – 901ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi107 – 1148ATPPROSITE-ProRule annotation
Nucleotide bindingi110 – 1156ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. DNA binding Source: UniProtKB-KW
  3. helicase activity Source: UniProtKB-KW

GO - Biological processi

  1. negative regulation of transcription from RNA polymerase II promoter Source: MGI
  2. oogenesis Source: MGI
  3. positive regulation of apoptotic process Source: UniProtKB
  4. regulation of steroid biosynthetic process Source: MGI
  5. spliceosomal snRNP assembly Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_333207. snRNP Assembly.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable ATP-dependent RNA helicase DDX20 (EC:3.6.4.13)
Alternative name(s):
Component of gems 3
DEAD box protein 20
DEAD box protein DP 103
Gemin-3
Regulator of steroidogenic factor 1
Short name:
ROSF-1
Gene namesi
Name:Ddx20
Synonyms:Dp103, Gemin3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1858415. Ddx20.

Subcellular locationi

  1. Cytoplasm
  2. Nucleusgem

  3. Note: Localized in subnuclear structures next to coiled bodies, called Gemini of Cajal bodies (Gems).

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. cytosol Source: UniProtKB
  3. Gemini of coiled bodies Source: UniProtKB-SubCell
  4. membrane Source: MGI
  5. nucleus Source: MGI
  6. SMN complex Source: UniProtKB
  7. SMN-Sm protein complex Source: UniProtKB
  8. transcriptional repressor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 825825Probable ATP-dependent RNA helicase DDX20PRO_0000055026Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei188 – 1881PhosphoserineBy similarity
Modified residuei501 – 5011PhosphoserineBy similarity
Modified residuei506 – 5061PhosphoserineBy similarity
Modified residuei552 – 5521PhosphothreonineBy similarity
Modified residuei653 – 6531PhosphoserineBy similarity
Modified residuei655 – 6551PhosphoserineBy similarity
Modified residuei657 – 6571PhosphoserineBy similarity
Modified residuei673 – 6731PhosphoserineBy similarity
Modified residuei678 – 6781PhosphoserineBy similarity
Modified residuei679 – 6791PhosphoserineBy similarity
Modified residuei689 – 6891PhosphothreonineBy similarity
Modified residuei706 – 7061PhosphothreonineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9JJY4.
PaxDbiQ9JJY4.
PRIDEiQ9JJY4.

PTM databases

PhosphoSiteiQ9JJY4.

Expressioni

Gene expression databases

BgeeiQ9JJY4.
CleanExiMM_DDX20.
GenevestigatoriQ9JJY4.

Interactioni

Subunit structurei

Part of the core SMN complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8 and STRAP/UNRIP. Part of the SMN-Sm complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8, STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG. Interacts directly with GEMIN5. Interacts directly with SNUPN. Interacts with PPP4R2. Interacts with FOXL2. Interacts with NANOS1 and PUM2.2 Publications

Protein-protein interaction databases

BioGridi207545. 5 interactions.
IntActiQ9JJY4. 1 interaction.
STRINGi10090.ENSMUSP00000088176.

Structurei

3D structure databases

ProteinModelPortaliQ9JJY4.
SMRiQ9JJY4. Positions 6-445.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini94 – 265172Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini300 – 449150Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi63 – 9129Q motifAdd
BLAST
Motifi212 – 2154DEAD box

Sequence similaritiesi

Belongs to the DEAD box helicase family.Curated
Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0513.
GeneTreeiENSGT00780000122030.
HOGENOMiHOG000112184.
HOVERGENiHBG051330.
InParanoidiQ9JJY4.
KOiK13131.
OMAiQYYKIVN.
OrthoDBiEOG7PGDPX.
TreeFamiTF101524.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000629. RNA-helicase_DEAD-box_CS.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9JJY4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAAAFEVPA ALTTSESTMA AERAAAPVQA VEPTPASPWT QRTAHDIGGP
60 70 80 90 100
RTRTGDVVLA EPADFESLLL SRPVLEGLRA AGFERPSPVQ LKAIPLGRCG
110 120 130 140 150
LDLIVQAKSG TGKTCVFSTI ALDSLILENY STQILILAPT REIAVQIHSV
160 170 180 190 200
ITAIGIKMEG LECHVFIGGT PLSQDKTRLK KCHIAVGSPG RIKQLIELDY
210 220 230 240 250
LNPGSIRLFI LDEADKLLEE GSFQEQINWI YSSLPASKQM LAVSATYPEV
260 270 280 290 300
LANALTRYMR DPTFVRLNPS DPSLIGLKQY YQVVNSYPLA HKIFEEKTQH
310 320 330 340 350
LQELFSKVPF NQALVFSNLH SRAQHLADIL SSKGFPTECI SGNMNQNQRL
360 370 380 390 400
DAMAKLKQFH CRVLISTDLT SRGIDAEKVN LVVNLDVPLD WETYMHRIGR
410 420 430 440 450
AGRFGTLGLT VTYCCRGEEE NMMMKIAQKC NINLLPLPDP IPPGLMEECL
460 470 480 490 500
NWDVEVKAAM HTYSSPTVAT QSPKKQVQKL ERAFQSQRTP GNQTPSPRNT
510 520 530 540 550
SASALSARPK HSKPKLPVKS HSECGVLEKA APPQESGCPA QLEEQVKNSV
560 570 580 590 600
QTSVEDSSSN SQHQAKDSSP GSLPKIPCLS SFKVHQPSTL TFAELVDDYE
610 620 630 640 650
HYIKEGLEKP VEIIRHYTGP EAQTGNPQNG FVRNRVSEDR AQMLVSSSQS
660 670 680 690 700
GDSESDSDSC SSRTSSQSKG NKSYLEGSSD TQLKDTECTP VGGPLSLEQV
710 720 730 740 750
QNGNDTPTQV EYQEAPETQV KARHKEGANQ RSKQSRRNPA RRSSYRVQSE
760 770 780 790 800
PQEESWYDCH RETTASFSDT YQDYEEYWRA YYRAWQEYYA AASHSYYWNA
810 820
QRHPSWMAAY HMNTVYLQEM MRGNQ
Length:825
Mass (Da):91,710
Last modified:July 27, 2011 - v2
Checksum:iB5BCD0754D4075C3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51A → T in AAF76301 (PubMed:11145740).Curated
Sequence conflicti9 – 91P → R in AAF76301 (PubMed:11145740).Curated
Sequence conflicti226 – 2261Q → H in CAB86201 (PubMed:10767334).Curated
Sequence conflicti468 – 4681V → I in AAF76301 (PubMed:11145740).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ250027 mRNA. Translation: CAB86201.1.
AF220454 mRNA. Translation: AAF76301.1.
CH466608 Genomic DNA. Translation: EDL07549.1.
BC125471 mRNA. Translation: AAI25472.1.
BC137721 mRNA. Translation: AAI37722.1.
CCDSiCCDS38581.1.
RefSeqiNP_059093.3. NM_017397.3.
XP_006501764.1. XM_006501701.2.
UniGeneiMm.272826.

Genome annotation databases

EnsembliENSMUST00000090680; ENSMUSP00000088176; ENSMUSG00000027905.
GeneIDi53975.
KEGGimmu:53975.
UCSCiuc008qva.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ250027 mRNA. Translation: CAB86201.1.
AF220454 mRNA. Translation: AAF76301.1.
CH466608 Genomic DNA. Translation: EDL07549.1.
BC125471 mRNA. Translation: AAI25472.1.
BC137721 mRNA. Translation: AAI37722.1.
CCDSiCCDS38581.1.
RefSeqiNP_059093.3. NM_017397.3.
XP_006501764.1. XM_006501701.2.
UniGeneiMm.272826.

3D structure databases

ProteinModelPortaliQ9JJY4.
SMRiQ9JJY4. Positions 6-445.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207545. 5 interactions.
IntActiQ9JJY4. 1 interaction.
STRINGi10090.ENSMUSP00000088176.

PTM databases

PhosphoSiteiQ9JJY4.

Proteomic databases

MaxQBiQ9JJY4.
PaxDbiQ9JJY4.
PRIDEiQ9JJY4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000090680; ENSMUSP00000088176; ENSMUSG00000027905.
GeneIDi53975.
KEGGimmu:53975.
UCSCiuc008qva.1. mouse.

Organism-specific databases

CTDi11218.
MGIiMGI:1858415. Ddx20.

Phylogenomic databases

eggNOGiCOG0513.
GeneTreeiENSGT00780000122030.
HOGENOMiHOG000112184.
HOVERGENiHBG051330.
InParanoidiQ9JJY4.
KOiK13131.
OMAiQYYKIVN.
OrthoDBiEOG7PGDPX.
TreeFamiTF101524.

Enzyme and pathway databases

ReactomeiREACT_333207. snRNP Assembly.

Miscellaneous databases

NextBioi310865.
PROiQ9JJY4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JJY4.
CleanExiMM_DDX20.
GenevestigatoriQ9JJY4.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000629. RNA-helicase_DEAD-box_CS.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Direct interaction of Smn with dp103, a putative RNA helicase: a role for Smn in transcription regulation?"
    Campbell L., Hunter K.M., Mohaghegh P., Tinsley J.M., Brasch M.A., Davies K.E.
    Hum. Mol. Genet. 9:1093-1100(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH SMN1.
  2. "The DEAD box protein DP103 is a regulator of steroidogenic factor-1."
    Ou Q., Mouillet J.F., Yan X., Dorn C., Crawford P.A., Sadovsky Y.
    Mol. Endocrinol. 15:69-79(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
    Tissue: Testis.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Thymus.
  5. "Transcriptional factor FOXL2 interacts with DP103 and induces apoptosis."
    Lee K., Pisarska M.D., Ko J.J., Kang Y., Yoon S., Ryou S.M., Cha K.Y., Bae J.
    Biochem. Biophys. Res. Commun. 336:876-881(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FOXL2.

Entry informationi

Entry nameiDDX20_MOUSE
AccessioniPrimary (citable) accession number: Q9JJY4
Secondary accession number(s): Q059Z6, Q9JIK4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: July 27, 2011
Last modified: April 1, 2015
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.