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Q8R418 (DICER_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Endoribonuclease Dicer

EC=3.1.26.3
Alternative name(s):
Double-strand-specific ribonuclease mDCR-1
Gene names
Name:Dicer1
Synonyms:Dicer, Mdcr
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1916 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Double-stranded RNA (dsRNA) endoribonuclease playing a central role in short dsRNA-mediated post-transcriptional gene silencing. Cleaves naturally occurring long dsRNAs and short hairpin pre-microRNAs (miRNA) into fragments of twenty-one to twenty-three nucleotides with 3' overhang of two nucleotides, producing respectively short interfering RNAs (siRNA) and mature microRNAs. SiRNAs and miRNAs serve as guide to direct the RNA-induced silencing complex (RISC) to complementary RNAs to degrade them or prevent their translation. Gene silencing mediated by siRNAs, also called RNA interference, controls the elimination of transcripts from mobile and repetitive DNA elements of the genome but also the degradation of exogenous RNA of viral origin for instance. The miRNA pathway on the other side is a mean to specifically regulate the expression of target genes By similarity. Ref.4

Isoform 2:More active than isoform 1 to process long double-stranded RNA into siRNAs. Responsible for the accumulation of endogenous siRNAs observed in mouse oocytes compared to somatic cells and it regulates meiotic spindle organization in female germline. Ref.4

Catalytic activity

Endonucleolytic cleavage to 5'-phosphomonoester. HAMAP-Rule MF_00104

Cofactor

Binds 2 magnesium or manganese ions per subunit Probable.

Subunit structure

Component of the RISC loading complex (RLC), or micro-RNA (miRNA) loading complex (miRLC), which is composed of DICER1, AGO2 and TARBP2; DICER1 and TARBP2 are required to process precursor miRNAs (pre-miRNAs) to mature miRNAs and then load them onto AGO2. Note that the trimeric RLC/miRLC is also referred to as RISC. Interacts with DHX9, AGO1, PIWIL1 and PRKRA. Associates with the 60S ribosome. Interacts with BCDIN3D By similarity.

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00104.

Tissue specificity

Isoform 1 is expressed in a wide variety of tissues. Isoform 2 is specifically expressed in oocytes during their growth (at protein level). Ref.4

Disruption phenotype

Isoform 2:Mice lacking isoform 2 are viable and males are fertile. However, females are sterile, their oocytes displaying meiotic spindle defects. Ref.4

Sequence similarities

Belongs to the helicase family. Dicer subfamily.

Contains 1 Dicer dsRNA-binding fold domain.

Contains 1 DRBM (double-stranded RNA-binding) domain.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Contains 1 PAZ domain.

Contains 2 RNase III domains.

Caution

It is uncertain whether Met-1 or Met-11 is the initiator.

Sequence caution

The sequence AAM21495.1 differs from that shown. Reason: Frameshift at position 8.

The sequence BAC15765.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processRNA-mediated gene silencing
   Cellular componentCytoplasm
   Coding sequence diversityAlternative promoter usage
   DomainRepeat
   LigandATP-binding
Magnesium
Manganese
Metal-binding
Nucleotide-binding
RNA-binding
   Molecular functionEndonuclease
Helicase
Hydrolase
Nuclease
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA phosphodiester bond hydrolysis

Inferred from direct assay PubMed 14528307. Source: GOC

RNA phosphodiester bond hydrolysis, endonucleolytic

Inferred from direct assay PubMed 14528307. Source: GOC

RNA processing

Inferred from direct assay PubMed 14528307. Source: MGI

anatomical structure development

Inferred from mutant phenotype PubMed 22844247. Source: MGI

angiogenesis

Inferred from mutant phenotype PubMed 15613470PubMed 17613256. Source: MGI

branching morphogenesis of an epithelial tube

Inferred from mutant phenotype PubMed 16452165. Source: MGI

cardiac muscle cell development

Inferred from mutant phenotype PubMed 18256189. Source: MGI

cell proliferation

Inferred from mutant phenotype PubMed 20708584. Source: MGI

cerebral cortex development

Inferred from mutant phenotype PubMed 18997113. Source: MGI

defense response to virus

Inferred from mutant phenotype PubMed 17613256. Source: MGI

digestive tract development

Inferred from mutant phenotype PubMed 21307095. Source: MGI

embryonic hindlimb morphogenesis

Inferred from mutant phenotype PubMed 16319892. Source: MGI

embryonic limb morphogenesis

Inferred from mutant phenotype PubMed 16040801. Source: MGI

epidermis morphogenesis

Inferred from mutant phenotype PubMed 16682203. Source: MGI

hair follicle cell proliferation

Inferred from mutant phenotype PubMed 16682203. Source: MGI

hair follicle development

Inferred from mutant phenotype PubMed 16682203. Source: MGI

hair follicle morphogenesis

Inferred from mutant phenotype PubMed 16682203. Source: MGI

inner ear receptor cell development

Inferred from mutant phenotype PubMed 19416898. Source: MGI

intestinal epithelial cell development

Inferred from genetic interaction PubMed 21307095. Source: MGI

lung development

Inferred from mutant phenotype PubMed 16452165. Source: MGI

mRNA stabilization

Inferred from mutant phenotype PubMed 22844247. Source: MGI

meiotic spindle organization

Inferred from mutant phenotype Ref.4. Source: UniProtKB

multicellular organism growth

Inferred from mutant phenotype PubMed 16682203. Source: MGI

negative regulation of Schwann cell proliferation

Inferred from mutant phenotype PubMed 20805985. Source: BHF-UCL

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 20463238PubMed 20805985. Source: BHF-UCL

nerve development

Inferred from mutant phenotype PubMed 20463238. Source: BHF-UCL

neuron projection morphogenesis

Inferred from mutant phenotype PubMed 20463238. Source: BHF-UCL

olfactory bulb interneuron differentiation

Inferred from mutant phenotype PubMed 18184563. Source: MGI

peripheral nervous system myelin formation

Inferred from mutant phenotype PubMed 20463238PubMed 20805985. Source: BHF-UCL

positive regulation of Schwann cell differentiation

Inferred from mutant phenotype PubMed 20463238PubMed 20805985. Source: BHF-UCL

positive regulation of gene expression

Inferred from mutant phenotype PubMed 16682203. Source: MGI

positive regulation of miRNA metabolic process

Inferred from mutant phenotype PubMed 20975942. Source: MGI

positive regulation of myelination

Inferred from mutant phenotype PubMed 20463238PubMed 20805985. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 20805985. Source: BHF-UCL

post-embryonic development

Inferred from mutant phenotype PubMed 16682203PubMed 18997113. Source: MGI

pre-miRNA processing

Inferred from sequence or structural similarity. Source: UniProtKB

production of miRNAs involved in gene silencing by miRNA

Inferred from mutant phenotype PubMed 20463238PubMed 20805985. Source: BHF-UCL

production of siRNA involved in RNA interference

Inferred from mutant phenotype Ref.4. Source: UniProtKB

rRNA catabolic process

Inferred from electronic annotation. Source: InterPro

regulation of Notch signaling pathway

Inferred by curator PubMed 20805985. Source: BHF-UCL

regulation of RNA metabolic process

Inferred from mutant phenotype PubMed 17613256. Source: MGI

regulation of cell cycle

Inferred from mutant phenotype PubMed 20708584. Source: MGI

regulation of cell differentiation

Inferred from mutant phenotype PubMed 20102707. Source: MGI

regulation of enamel mineralization

Inferred from mutant phenotype PubMed 20102707. Source: MGI

regulation of gene expression

Inferred from mutant phenotype PubMed 20708584PubMed 21573140PubMed 21911408. Source: MGI

regulation of miRNA metabolic process

Inferred from mutant phenotype PubMed 17613256PubMed 18184563. Source: MGI

regulation of myelination

Inferred from mutant phenotype PubMed 20223197. Source: MGI

regulation of neurogenesis

Inferred from mutant phenotype PubMed 18184563. Source: MGI

regulation of neuron differentiation

Inferred from mutant phenotype PubMed 17761882PubMed 18997113. Source: MGI

regulation of odontogenesis of dentin-containing tooth

Inferred from mutant phenotype PubMed 20102707. Source: MGI

regulation of oligodendrocyte differentiation

Inferred from mutant phenotype PubMed 20223197. Source: MGI

regulation of protein phosphorylation

Inferred from mutant phenotype PubMed 20805985. Source: BHF-UCL

regulation of viral genome replication

Inferred from mutant phenotype PubMed 17613256. Source: MGI

spinal cord motor neuron differentiation

Inferred from mutant phenotype PubMed 21338882. Source: MGI

spindle assembly

Inferred from mutant phenotype PubMed 17369397. Source: MGI

spleen development

Inferred from mutant phenotype PubMed 21307095. Source: MGI

stem cell maintenance

Inferred from mutant phenotype PubMed 14528307. Source: MGI

targeting of mRNA for destruction involved in RNA interference

Inferred from sequence or structural similarity. Source: UniProtKB

zygote asymmetric cell division

Inferred from mutant phenotype PubMed 17369397. Source: MGI

   Cellular_componentRISC complex

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.4. Source: MGI

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP-dependent helicase activity

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

miRNA binding

Inferred from direct assay PubMed 18604195. Source: MGI

protein binding

Inferred from physical interaction PubMed 16938833PubMed 17452327. Source: UniProtKB

ribonuclease III activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative promoter usage. [Align] [Select]
Isoform 1 (identifier: Q8R418-1)

Also known as: DicerS;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8R418-2)

Also known as: DicerO;

The sequence of this isoform differs from the canonical sequence as follows:
     1-245: MKSPALQPLS...TATDLVVLDR → MSRDTEV
Note: An MT-C retrotransposon in intron 6 of the mouse DICER gene functions as a promoter producing a transcript lacking exons 1 to 6. A new alternative first exon is directly derived from the retrotransposon.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 19161916Endoribonuclease Dicer HAMAP-Rule MF_00104
PRO_0000180471

Regions

Domain51 – 227177Helicase ATP-binding
Domain433 – 602170Helicase C-terminal
Domain630 – 72293Dicer dsRNA-binding fold
Domain891 – 1042152PAZ
Domain1276 – 1403128RNase III 1
Domain1660 – 1818159RNase III 2
Domain1843 – 190866DRBM
Nucleotide binding64 – 718ATP By similarity
Region256 – 595340Required for interaction with PRKRA and TARBP2 By similarity
Motif175 – 1784DECH box HAMAP-Rule MF_00104

Sites

Metal binding13161Magnesium or manganese 1 By similarity
Metal binding13951Magnesium or manganese 1 By similarity
Metal binding13981Magnesium or manganese 1 By similarity
Metal binding16991Magnesium or manganese 2
Metal binding18041Magnesium or manganese 2
Metal binding18071Magnesium or manganese 2
Site18001Important for activity

Amino acid modifications

Modified residue4131Phosphoserine By similarity
Modified residue4151Phosphoserine By similarity
Modified residue10161Phosphoserine By similarity

Natural variations

Alternative sequence1 – 245245MKSPA…VVLDR → MSRDTEV in isoform 2.
VSP_053586

Experimental info

Mutagenesis18001K → A, R, S or T: Loss of activity. Ref.5
Sequence conflict11M → L in BAC15765. Ref.2
Sequence conflict1071A → C in AAM21495. Ref.3
Sequence conflict1671S → P in BAC15765. Ref.2
Sequence conflict2891H → Y in AAM21495. Ref.3
Sequence conflict6101A → T in BAC15765. Ref.2
Sequence conflict7591E → D in AAM21495. Ref.3
Sequence conflict8371T → I in AAM21495. Ref.3
Sequence conflict8881G → S in AAL84638. Ref.1
Sequence conflict9651Y → C in BAC15765. Ref.2
Sequence conflict9931T → A in BAC15765. Ref.2
Sequence conflict10901R → G in BAC15765. Ref.2
Sequence conflict11101T → S in BAC15765. Ref.2
Sequence conflict13361P → H in AAL84638. Ref.1
Sequence conflict16191A → S in AAL84637. Ref.1
Sequence conflict16191A → S in BAC15765. Ref.2
Sequence conflict18601K → E in BAC15765. Ref.2

Secondary structure

............................... 1916
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (DicerS) [UniParc].

Last modified September 1, 2009. Version 3.
Checksum: D97EA17922D7E79C

FASTA1,916216,821
        10         20         30         40         50         60 
MKSPALQPLS MAGLQLMTPA SSPMGPFFGL PWQQEAIHDN IYTPRKYQVE LLEAALDHNT 

        70         80         90        100        110        120 
IVCLNTGSGK TFIAVLLTKE LAHQIRGDLN PHAKRTVFLV NSANQVAQQV SAVRTHSDLK 

       130        140        150        160        170        180 
VGEYSDLEVN ASWTKERWSQ EFTKHQVLIM TCYVALTVLK NGYLSLSDIN LLVFDECHLA 

       190        200        210        220        230        240 
ILDHPYREIM KLCESCPSCP RILGLTASIL NGKCDPEELE EKIQKLERIL RSDAETATDL 

       250        260        270        280        290        300 
VVLDRYTSQP CEIVVDCGPF TDRSGLYERL LMELEAALDF INDCNVAVHS KERDSTLISK 

       310        320        330        340        350        360 
QILSDCRAVL VVLGPWCADK VAGMMVRELQ KYIKHEQEEL HRKFLLFTDT LLRKIHALCE 

       370        380        390        400        410        420 
EYFSPASLDL KYVTPKVMKL LEILRKYKPY ERQQFESVEW YNNRNQDNYV SWSDSEDDDD 

       430        440        450        460        470        480 
DEEIEEKEKP ETNFPSPFTN ILCGIIFVER RYTAVVLNRL IKEAGKQDPE LAYISSNFIT 

       490        500        510        520        530        540 
GHGIGKNQPR SKQMEAEFRK QEEVLRKFRA HETNLLIATS VVEEGVDIPK CNLVVRFDLP 

       550        560        570        580        590        600 
TEYRSYVQSK GRARAPISNY VMLADTDKIK SFEEDLKTYK AIEKILRNKC SKSADGAEAD 

       610        620        630        640        650        660 
VHAGVDDEDA FPPYVLRPDD GGPRVTINTA IGHINRYCAR LPSDPFTHLA PKCRTRELPD 

       670        680        690        700        710        720 
GTFYSTLYLP INSPLRASIV GPPMDSVRLA ERVVALICCE KLHKIGELDE HLMPVGKETV 

       730        740        750        760        770        780 
KYEEELDLHD EEETSVPGRP GSTKRRQCYP KAIPECLRES YPKPDQPCYL YVIGMVLTTP 

       790        800        810        820        830        840 
LPDELNFRRR KLYPPEDTTR CFGILTAKPI PQIPHFPVYT RSGEVTISIE LKKSGFTLSQ 

       850        860        870        880        890        900 
QMLELITRLH QYIFSHILRL EKPALEFKPT GAESAYCVLP LNVVNDSGTL DIDFKFMEDI 

       910        920        930        940        950        960 
EKSEARIGIP STKYSKETPF VFKLEDYQDA VIIPRYRNFD QPHRFYVADV YTDLTPLSKF 

       970        980        990       1000       1010       1020 
PSPEYETFAE YYKTKYNLDL TNLNQPLLDV DHTSSRLNLL TPRHLNQKGK ALPLSSAEKR 

      1030       1040       1050       1060       1070       1080 
KAKWESLQNK QILVPELCAI HPIPASLWRK AVCLPSILYR LHCLLTAEEL RAQTASDAGV 

      1090       1100       1110       1120       1130       1140 
GVRSLPVDFR YPNLDFGWKK SIDSKSFIST CNSSLAESDN YCKHSTTVVP EHAAHQGATR 

      1150       1160       1170       1180       1190       1200 
PSLENHDQMS VNCKRLPAES PAKLQSEVST DLTAINGLSY NKNLANGSYD LVNRDFCQGN 

      1210       1220       1230       1240       1250       1260 
QLNYFKQEIP VQPTTSYPIQ NLYNYENQPK PSNECPLLSN TYLDGNANTS TSDGSPAVST 

      1270       1280       1290       1300       1310       1320 
MPAMMNAVKA LKDRMDSEQS PSVGYSSRTL GPNPGLILQA LTLSNASDGF NLERLEMLGD 

      1330       1340       1350       1360       1370       1380 
SFLKHAITTY LFCTYPDAHE GRLSYMRSKK VSNCNLYRLG KKKGLPSRMV VSIFDPPVNW 

      1390       1400       1410       1420       1430       1440 
LPPGYVVNQD KSNSEKWEKD EMTKDCLLAN GKLGEACEEE EDLTWRAPKE EAEDEDDFLE 

      1450       1460       1470       1480       1490       1500 
YDQEHIQFID SMLMGSGAFV RKISLSPFSA SDSAYEWKMP KKASLGSMPF ASGLEDFDYS 

      1510       1520       1530       1540       1550       1560 
SWDAMCYLDP SKAVEEDDFV VGFWNPSEEN CGVDTGKQSI SYDLHTEQCI ADKSIADCVE 

      1570       1580       1590       1600       1610       1620 
ALLGCYLTSC GERAAQLFLC SLGLKVLPVI KRTSREKALD PAQENGSSQQ KSLSGSCAAP 

      1630       1640       1650       1660       1670       1680 
VGPRSSAGKD LEYGCLKIPP RCMFDHPDAE KTLNHLISGF ETFEKKINYR FKNKAYLLQA 

      1690       1700       1710       1720       1730       1740 
FTHASYHYNT ITDCYQRLEF LGDAILDYLI TKHLYEDPRQ HSPGVLTDLR SALVNNTIFA 

      1750       1760       1770       1780       1790       1800 
SLAVKYDYHK YFKAVSPELF HVIDDFVKFQ LEKNEMQGMD SELRRSEEDE EKEEDIEVPK 

      1810       1820       1830       1840       1850       1860 
AMGDIFESLA GAIYMDSGMS LEVVWQVYYP MMQPLIEKFS ANVPRSPVRE LLEMEPETAK 

      1870       1880       1890       1900       1910 
FSPAERTYDG KVRVTVEVVG KGKFKGVGRS YRIAKSAAAR RALRSLKANQ PQVPNS 

« Hide

Isoform 2 (DicerO) [UniParc].

Checksum: 4F445FDFB774C3EB
Show »

FASTA1,678190,213

References

[1]"Molecular characterization of a mouse cDNA encoding Dicer, a ribonuclease III ortholog involved in RNA interference."
Nicholson R.H., Nicholson A.W.
Mamm. Genome 13:67-73(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 17-1916.
Strain: C57BL/6J.
[2]"Short-interfering-RNA-mediated gene silencing in mammalian cells requires Dicer and eIF2C translation initiation factors."
Doi N., Zenno S., Ueda R., Ohki-Hamazaki H., Ui-Tei K., Saigo K.
Curr. Biol. 13:41-46(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"RNAi and expression of retrotransposons MuERV-L and IAP in preimplantation mouse embryos."
Svoboda P., Stein P., Anger M., Bernstein E., Hannon G.J., Schultz R.M.
Dev. Biol. 269:276-285(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Strain: Czech II.
[4]"A retrotransposon-driven dicer isoform directs endogenous small interfering RNA production in mouse oocytes."
Flemr M., Malik R., Franke V., Nejepinska J., Sedlacek R., Vlahovicek K., Svoboda P.
Cell 155:807-816(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF ISOFORM 2, FUNCTION (ISOFORMS 1 AND 2), DISRUPTION PHENOTYPE (ISOFORM 2), TISSUE SPECIFICITY (ISOFORMS 1 AND 2).
[5]"Structural and biochemical insights into the dicing mechanism of mouse Dicer: a conserved lysine is critical for dsRNA cleavage."
Du Z., Lee J.K., Tjhen R., Stroud R.M., James T.L.
Proc. Natl. Acad. Sci. U.S.A. 105:2391-2396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) OF 1647-1910, MUTAGENESIS OF LYS-1800.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF484523 Genomic DNA. Translation: AAL84637.1.
AF484524 Genomic DNA. Translation: AAL84638.1.
AB081470 mRNA. Translation: BAC15765.1. Different initiation.
AF430845 mRNA. Translation: AAM21495.1. Frameshift.
UniGeneMm.21135.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3C4BX-ray1.68A1648-1910[»]
3C4TX-ray2.80A1648-1910[»]
ProteinModelPortalQ8R418.
SMRQ8R418. Positions 766-1063, 1648-1910.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-29721N.
IntActQ8R418. 2 interactions.

PTM databases

PhosphoSiteQ8R418.

Proteomic databases

MaxQBQ8R418.
PaxDbQ8R418.
PRIDEQ8R418.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

MGIMGI:2177178. Dicer1.

Phylogenomic databases

eggNOGCOG1111.
HOGENOMHOG000001567.
HOVERGENHBG107811.
InParanoidQ8R419.
PhylomeDBQ8R418.

Gene expression databases

CleanExMM_DICER1.
GenevestigatorQ8R418.

Family and domain databases

Gene3D1.10.1520.10. 4 hits.
3.30.160.20. 1 hit.
3.40.50.300. 2 hits.
HAMAPMF_00104. RNase_III.
InterProIPR005034. Dicer_dimerisation_dom.
IPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
IPR014720. dsRNA-bd_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR003100. PAZ_dom.
IPR011907. RNase_III.
IPR000999. RNase_III_dom.
[Graphical view]
PfamPF00270. DEAD. 1 hit.
PF03368. Dicer_dimer. 1 hit.
PF00271. Helicase_C. 1 hit.
PF02170. PAZ. 1 hit.
PF00636. Ribonuclease_3. 2 hits.
[Graphical view]
SMARTSM00487. DEXDc. 1 hit.
SM00358. DSRM. 1 hit.
SM00490. HELICc. 1 hit.
SM00949. PAZ. 1 hit.
SM00535. RIBOc. 2 hits.
[Graphical view]
SUPFAMSSF101690. SSF101690. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF69065. SSF69065. 4 hits.
PROSITEPS51327. DICER_DSRBF. 1 hit.
PS50137. DS_RBD. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS50821. PAZ. 1 hit.
PS00517. RNASE_3_1. 1 hit.
PS50142. RNASE_3_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ8R418.
PROQ8R418.
SOURCESearch...

Entry information

Entry nameDICER_MOUSE
AccessionPrimary (citable) accession number: Q8R418
Secondary accession number(s): Q8R419
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2002
Last sequence update: September 1, 2009
Last modified: July 9, 2014
This is version 119 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot